PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2482548-11	1989	Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	141-149
2482548-11	1989	Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	200-208
2557089-5	1989	However, heparin fragments decreased the proportion of the freshly synthesized pericellular form of fibronectin with a concomitant increase of neosynthesized intracellular fibronectin, indicating an inhibitory effect of CY222 on fibronectin secretion.	Heparin	9-16	fibronectin 1	Homo sapiens	172-183
2557089-5	1989	However, heparin fragments decreased the proportion of the freshly synthesized pericellular form of fibronectin with a concomitant increase of neosynthesized intracellular fibronectin, indicating an inhibitory effect of CY222 on fibronectin secretion.	Heparin	9-16	fibronectin 1	Homo sapiens	100-111
2557089-5	1989	However, heparin fragments decreased the proportion of the freshly synthesized pericellular form of fibronectin with a concomitant increase of neosynthesized intracellular fibronectin, indicating an inhibitory effect of CY222 on fibronectin secretion.	Heparin	9-16	fibronectin 1	Homo sapiens	172-183
2592856-1	1989	Inhibition of thrombin by heparin is mediated by at least two plasma proteins, antithrombin III, and heparin cofactor II.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	14-22
2597694-1	1989	Nonenzymatic glycation of antithrombin III has been reported to cause the reduction of heparin-catalyzed thrombin-inhibiting activity in diabetes.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	30-38
2560285-1	1989	2 or 3 daily injections of unfractionated heparin reduce the risk of thrombosis in patients undergoing general surgery from about 39 to 4 to 5% (sodium-fibrinogen-test).	Heparin	42-49	fibrinogen beta chain	Homo sapiens	152-162
2611327-6	1989	Although heparin significantly accelerated thrombin inhibition by antithrombin lll, the remaining thrombin levels were still significantly above the minimum threshold required for irreversible platelet aggregation.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	43-51
2611327-6	1989	Although heparin significantly accelerated thrombin inhibition by antithrombin lll, the remaining thrombin levels were still significantly above the minimum threshold required for irreversible platelet aggregation.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	70-78
2516663-0	1989	Plasma levels of t-PA:Ag under standard heparin therapy.	Heparin	40-47	plasminogen activator, tissue type	Homo sapiens	17-21
2512126-11	1989	Heparin, which also binds to both fragments, competed with fibronectin binding to the 27-kDa fragment but not to the 70-kDa domain.	Heparin	0-7	fibronectin 1	Homo sapiens	59-70
2512126-12	1989	The fact that heparin also competitively inhibits fibronectin binding of the intact molecule further supports sequestration of the fibronectin-binding domain on the 70-kDa core fragment.	Heparin	14-21	fibronectin 1	Homo sapiens	50-61
2554975-0	1989	Phosphatidylinositol-specific phospholipase C releases lipoprotein lipase from the heparin releasable pool in rat heart cell cultures.	Heparin	83-90	lipoprotein lipase	Rattus norvegicus	55-73
2512126-12	1989	The fact that heparin also competitively inhibits fibronectin binding of the intact molecule further supports sequestration of the fibronectin-binding domain on the 70-kDa core fragment.	Heparin	14-21	fibronectin 1	Homo sapiens	131-142
2554975-8	1989	As there is a previously described correlation between circulating LPL and the heparin-releasable LPL, we hypothesize that the activity of PI-PLC in the endothelial cell membrane or plasma phosphatidyl-specific phospholipase D regulates the plasma LPL levels.	Heparin	79-86	lipoprotein lipase	Rattus norvegicus	67-70
2676156-8	1989	These included an antibody directed against the Mr 25,000 NH2-terminal region of the molecule which has heparin-binding activity and three antibodies the epitopes of which lie within the Mr 140,000 non-heparin-binding fragment of TSP.	Heparin	202-209	thrombospondin 1	Homo sapiens	230-233
2554975-8	1989	As there is a previously described correlation between circulating LPL and the heparin-releasable LPL, we hypothesize that the activity of PI-PLC in the endothelial cell membrane or plasma phosphatidyl-specific phospholipase D regulates the plasma LPL levels.	Heparin	79-86	lipoprotein lipase	Rattus norvegicus	98-101
2554975-8	1989	As there is a previously described correlation between circulating LPL and the heparin-releasable LPL, we hypothesize that the activity of PI-PLC in the endothelial cell membrane or plasma phosphatidyl-specific phospholipase D regulates the plasma LPL levels.	Heparin	79-86	lipoprotein lipase	Rattus norvegicus	98-101
2513808-5	1989	Heparin, but not the endotoxin antagonist polymyxin B, suppressed the stimulation of adhesion by thrombin without altering basal adhesion.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	97-105
2558424-0	1989	Influence of a low molecular weight heparin on the inhibition of factor Xa and thrombin in hip surgery.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	79-87
2686638-2	1989	This fragment, which corresponds to Val 449-Asn 730 of vWF and includes the GPIb-binding domain and binding sites for collagen and heparin, was subcloned into an expression vector containing an inducible lambda PL promoter.	Heparin	131-138	von Willebrand factor	Homo sapiens	55-58
2509458-3	1989	alpha-Thrombin phosphopyridoxylated in the absence of heparin (unprotected) showed approximately 2 mol of label incorporated/mol of thrombin, but only 1 mol of label incorporated/mol of proteinase when modified in the presence of added heparin (protected).	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	6-14
2509458-3	1989	alpha-Thrombin phosphopyridoxylated in the absence of heparin (unprotected) showed approximately 2 mol of label incorporated/mol of thrombin, but only 1 mol of label incorporated/mol of proteinase when modified in the presence of added heparin (protected).	Heparin	236-243	coagulation factor II, thrombin	Homo sapiens	6-14
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	36-44
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	69-77
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	69-77
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	69-77
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	36-44
2509458-6	1989	In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	27-35
2509458-6	1989	In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	66-74
2509458-6	1989	In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding.	Heparin	178-185	coagulation factor II, thrombin	Homo sapiens	27-35
2509458-6	1989	In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding.	Heparin	178-185	coagulation factor II, thrombin	Homo sapiens	66-74
2509458-9	1989	In heparin-protected modified alpha-thrombin, only lysyl residues B21 and B65 were phosphopyridoxylated.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	36-44
2509263-8	1989	These findings indicate that the amino-terminal heparin-binding domain of fibronectin can, within a tissue microenvironment, interact adhesively with heparin-like components on the surfaces of polystyrene beads, and by implication, on mesenchymal cells themselves.	Heparin	48-55	fibronectin 1	Homo sapiens	74-85
2509262-5	1989	In addition to the putative "cell-binding domain," neural crest cells were able to migrate on a 31-kDa fragment corresponding to the C-terminal heparin-binding (II) region of fibronectin, and were inhibited in their migration by exogenous heparin, but not by RGDS peptides.	Heparin	144-151	fibronectin 1	Homo sapiens	175-186
2509262-5	1989	In addition to the putative "cell-binding domain," neural crest cells were able to migrate on a 31-kDa fragment corresponding to the C-terminal heparin-binding (II) region of fibronectin, and were inhibited in their migration by exogenous heparin, but not by RGDS peptides.	Heparin	239-246	fibronectin 1	Homo sapiens	175-186
2509262-6	1989	Heparin potentiated the inhibitory effect of RGDS peptides on intact fibronectin, but not on the 105-kDa fragment.	Heparin	0-7	fibronectin 1	Homo sapiens	69-80
2509263-3	1989	Beads coated with heparin, chondroitin sulfate, or poly L-lysine, that were mixed with limb bud mesenchymal cells were centripetally conveyed into fibronectin-rich regions of cell condensation over a period of several days.	Heparin	18-25	fibronectin 1	Homo sapiens	147-158
2509263-5	1989	A monoclonal antibody directed against the amino-terminal heparin-binding domain of fibronectin completely inhibited accumulation of heparin-coated beads at condensing foci, but monoclonal antibodies directed against the collagen- or cell-binding domains of fibronectin were not inhibitory.	Heparin	58-65	fibronectin 1	Homo sapiens	84-95
2676156-9	1989	High concentrations of exogenously added TSP as well as the recombinant form of the heparin-binding domain from the TSP molecule also partially inhibited killing while laminin and fibronectin were ineffective.	Heparin	84-91	thrombospondin 1	Homo sapiens	116-119
2818580-1	1989	Epinephrine was used to activate the heparin non-releasable lipoprotein lipase (LPL) in the 3 skeletal muscle fiber types of the perfused rat hindlimb.	Heparin	37-44	lipoprotein lipase	Rattus norvegicus	60-78
2613696-3	1989	It was shown that bFGF stimulated the DNA synthesis and proliferation of C6 glioma cells in serum-free medium, and that the activity was potentiated by heparin, the bFGF concentrations for half-maximal stimulation being 0.2 and 5 ng/ml in the presence and absence of heparin, respectively.	Heparin	152-159	fibroblast growth factor 2	Homo sapiens	165-169
2613696-3	1989	It was shown that bFGF stimulated the DNA synthesis and proliferation of C6 glioma cells in serum-free medium, and that the activity was potentiated by heparin, the bFGF concentrations for half-maximal stimulation being 0.2 and 5 ng/ml in the presence and absence of heparin, respectively.	Heparin	267-274	fibroblast growth factor 2	Homo sapiens	18-22
2613696-7	1989	On the basis of its immunoreactivity, molecular weight, affinity for heparin, and growth-promoting activity, this substance was identified as bFGF.	Heparin	69-76	fibroblast growth factor 2	Homo sapiens	142-146
2614271-2	1989	Heparin-Sepharose chromatography was used to separate large VLDL (Sf 60-400) from fasted subjects, into an apoE-poor, unbound fraction and an apoE-rich, bound fraction.	Heparin	0-7	apolipoprotein E	Homo sapiens	107-111
2614271-2	1989	Heparin-Sepharose chromatography was used to separate large VLDL (Sf 60-400) from fasted subjects, into an apoE-poor, unbound fraction and an apoE-rich, bound fraction.	Heparin	0-7	apolipoprotein E	Homo sapiens	142-146
2614271-9	1989	Separation in the latter likely results from apoB-100 binding to heparin, as opposed to apoE binding of VLDL from Type IV and IIb subjects.	Heparin	65-72	apolipoprotein B	Homo sapiens	45-53
2685921-11	1989	This particular precaution seems to be necessary because low-molecular-weight heparin increases levels of plasminogen activators (t-PA) and therefore has fibrinolytic activity.	Heparin	78-85	plasminogen activator, tissue type	Homo sapiens	130-134
2818580-1	1989	Epinephrine was used to activate the heparin non-releasable lipoprotein lipase (LPL) in the 3 skeletal muscle fiber types of the perfused rat hindlimb.	Heparin	37-44	lipoprotein lipase	Rattus norvegicus	80-83
2690940-1	1989	A 39/34-kilodalton (kDa) monomeric dispase fragment of von Willebrand factor (vWF) has been purified by heparin affinity chromatography.	Heparin	104-111	von Willebrand factor	Homo sapiens	55-76
2690940-1	1989	A 39/34-kilodalton (kDa) monomeric dispase fragment of von Willebrand factor (vWF) has been purified by heparin affinity chromatography.	Heparin	104-111	von Willebrand factor	Homo sapiens	78-81
2688761-2	1989	The anticoagulant heparin greatly accelerates the rate of inactivation of proteinases by antithrombin, predominantly through its well defined, highly specific binding reaction with the inhibitor, but also through a less strictly defined interaction with some of the proteinases (such as thrombin).	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	93-101
2477370-6	1989	Both 116-kDa and 52/48-kDa fragments inhibited vWF binding to heparin with similar potency, while fragment III-T2 had no effect in this regard.	Heparin	62-69	von Willebrand factor	Homo sapiens	47-50
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	8-12
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	63-70	fibroblast growth factor 1	Homo sapiens	17-21
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	38-45	fibroblast growth factor 1	Homo sapiens	17-21
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	8-12
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	63-70	fibroblast growth factor 1	Homo sapiens	17-21
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	8-12
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	63-70	fibroblast growth factor 1	Homo sapiens	17-21
2777898-5	1989	Since the growth of SW-13 cells is stimulated by TGFe and by bFGF, we hypothesized that heparin would inhibit the growth of SW-13 cells by binding to these growth factors and that the effects of heparin could be overcome with the addition of either growth factor.	Heparin	88-95	fibroblast growth factor 2	Homo sapiens	61-65
2777898-9	1989	The effects of heparin in both monolayer and soft agar were at least partially overcome by TGFe and by basic or acidic FGF.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	119-122
2777898-13	1989	We propose that heparin, TGFe, bFGF, and aFGF modulate the growth of SW-13 cells and possibly of other epithelial cells in complex ways and that heparin-like substances present in the extracellular matrix play an important role in the control of epithelial growth.	Heparin	145-152	fibroblast growth factor 2	Homo sapiens	31-35
2777898-3	1989	Whereas bFGF and aFGF bind tightly to heparin and elute from a heparin-Sepharose column with 2 M NaCl and 1.6 M NaCl, respectively, TGFe binds to heparin with lower affinity and can be eluted from heparin-Sepharose column with 0.5 M NaCl.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	8-12
2613105-2	1989	Both FR-860 and UF-heparin dose-dependently prolonged the recalcification time, activated partial thromboplastin time, prothrombin time, factor Xa (F.Xa) clotting time and thrombin time.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	122-130
2630632-0	1989	Enhancement of heparin-binding ability of fibronectin by S-carboxamide-methylation.	Heparin	15-22	fibronectin 1	Homo sapiens	42-53
2630632-3	1989	S-Cam-FN, compared with intact FN, obviously had a more potent ability to bind heparin, while it had little or no binding ability to gelatin, fibrin and thrombin-stimulated platelets.	Heparin	79-86	fibronectin 1	Homo sapiens	6-8
2675842-3	1989	The stimulation of PGI2 production by AT III was observed at physiological concentrations and was inhibited by the addition of anti-AT III antiserum and heparin.	Heparin	153-160	serpin family C member 1	Bos taurus	38-44
2675842-4	1989	These results suggest that AT III may stimulate PGI2 production by binding to heparin-like molecules on the endothelial cell membrane.	Heparin	78-85	serpin family C member 1	Bos taurus	27-33
2534619-1	1989	Electrophoretic purified fibronectin (FN) was isolated with high concentration (0.5 mg/ml plasma) from porcine plasma by affinity chromatography with gelatin-sepharose 4B and heparin-sepharose 4B.	Heparin	175-182	fibronectin 1	Homo sapiens	25-36
2678451-0	1989	[Thrombin-antithrombin III complexes as a measure of effective heparin treatment?].	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	1-9
2479114-2	1989	Conversion of scu-PA to u-PA catalyzed by plasmin was enhanced by chondroitin sulfate C and heparin, maximally by 10-fold and 3-fold, respectively.	Heparin	92-99	plasminogen activator, urokinase	Homo sapiens	16-20
2683190-3	1989	Our results show that heparin plus AT III is able to significantly reduce the generation of endotoxin-induced PAI activity in rabbits" circulation.	Heparin	22-29	plasminogen activator inhibitor 1	Oryctolagus cuniculus	110-113
2482065-3	1989	In the presence of heparin, recognition of vitronectin by 8E6 was increased 64- or 52-fold by interaction with the complex of alpha-thrombin and heparin cofactor II or the Pittsburgh mutant (Met358----Arg) of alpha 1-protease inhibitor, respectively.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	132-140
2482065-3	1989	In the presence of heparin, recognition of vitronectin by 8E6 was increased 64- or 52-fold by interaction with the complex of alpha-thrombin and heparin cofactor II or the Pittsburgh mutant (Met358----Arg) of alpha 1-protease inhibitor, respectively.	Heparin	19-26	serpin family A member 1	Homo sapiens	209-235
2482065-8	1989	gamma-Thrombin caused 7- and 34-fold increases in recognition of vitronectin by MaVN 8E6 in the absence and presence of heparin, respectively.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	6-14
2683190-4	1989	Low dose of heparin and a bolus injection of AT III both cause a decrease in the generation of PAI at 2 but not at 6 hours of endotoxin infusion.	Heparin	12-19	plasminogen activator inhibitor 1	Oryctolagus cuniculus	95-98
2683190-8	1989	We conclude that heparin plus AT III partially prevents the endotoxin-induced generation of PAI activity which seems to correlate with the reduced presence of fibrin deposits in kidneys and with a reduced mortality.	Heparin	17-24	plasminogen activator inhibitor 1	Oryctolagus cuniculus	92-95
2506671-0	1989	Heparin induced increase of t-PA antigen plasma levels in patients with unstable angina: no evidence for clinical benefit of heparinization during the initial phase of treatment.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	28-32
2504719-1	1989	The activity of tissue plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA) is stimulated by heparin.	Heparin	117-124	plasminogen activator, tissue type	Homo sapiens	16-50
2504719-1	1989	The activity of tissue plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA) is stimulated by heparin.	Heparin	117-124	plasminogen activator, urokinase	Homo sapiens	56-92
2504719-1	1989	The activity of tissue plasminogen activator (t-PA) and urokinase-type plasminogen activator (u-PA) is stimulated by heparin.	Heparin	117-124	plasminogen activator, urokinase	Homo sapiens	94-98
2504719-5	1989	However, these preparations of heparin still efficiently accelerate the inhibition of thrombin by antithrombin III.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	86-94
2504721-0	1989	Structural domains of human tissue-type plasminogen activator that confer stimulation by heparin.	Heparin	89-96	plasminogen activator, tissue type	Homo sapiens	28-61
2504721-1	1989	Heparin has been shown recently to stimulate the activity of human tissue-type plasminogen activator (t-PA).	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	67-100
2504721-1	1989	Heparin has been shown recently to stimulate the activity of human tissue-type plasminogen activator (t-PA).	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	102-106
2504721-2	1989	To investigate this effect further, mutant proteins lacking various domains of t-PA were screened for the ability to be stimulated by heparin.	Heparin	134-141	plasminogen activator, tissue type	Homo sapiens	79-83
2552799-8	1989	Since this ATIII is probably associated with heparin-like substances and exists in a high-affinity state, the inhibitor rapidly binds proteinases such as alpha-thrombin.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	160-168
2475499-1	1989	Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces.	Heparin	121-128	proopiomelanocortin	Homo sapiens	84-98
2506671-2	1989	In heparinized patients thrombin time was prolonged more than 3-fold the normal range indicating effective heparin treatment.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	24-32
2806479-7	1989	Fibrinogen was a cofactor in the reaction as gel-filtered platelets were unreactive to heparin but addition of fibrinogen restored their reactivity.	Heparin	87-94	fibrinogen beta chain	Homo sapiens	0-10
2529852-2	1989	The maximum observed second-order rate constant was, for the antithrombin III-thrombin reaction, 1.2 x 10(9) M-1.min-1 compared with 2.4 x 10(9) M-1.min-1 in the presence of high-affinity heparin.	Heparin	188-195	coagulation factor II, thrombin	Homo sapiens	65-73
2529852-10	1989	It was observed that the apparent binding affinity for thrombin was higher for heparan sulphate (180 nM) than for heparin (14 nM).	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	55-63
2806479-8	1989	Antithrombin III and fibronectin inhibited platelet response to heparin, suggesting that these proteins may protect platelets from aggregation by heparin.	Heparin	64-71	fibronectin 1	Homo sapiens	21-32
2764920-8	1989	148:1264, 1987) that heparin increases smooth muscle cell synthesis of both fibronectin and thrombospondin.	Heparin	21-28	fibronectin 1	Homo sapiens	76-87
2550475-1	1989	The minimal structural requirements for the interaction of heparin with acidic fibroblast growth factor (aFGF) were investigated.	Heparin	59-66	fibroblast growth factor 1	Homo sapiens	72-103
2550475-1	1989	The minimal structural requirements for the interaction of heparin with acidic fibroblast growth factor (aFGF) were investigated.	Heparin	59-66	fibroblast growth factor 1	Homo sapiens	105-109
2760054-1	1989	Heparin cofactor II (HCII) is a highly specific serine proteinase inhibitor, which complexes covalently with thrombin in a reaction catalyzed by heparin and other polyanions.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	109-117
2777882-1	1989	The effects of heparin and other glycosaminoglycans (GAGs) on the mitogenicity and stability of acidic fibroblast growth factor (aFGF) were studied.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	96-127
2502207-3	1989	However, as successive fibrin layers are removed, inaccessible molecules of thrombin are exposed at the surface of the residual clot, possibly contributing to the occurrence during thrombolytic therapy of coagulation that is poorly controlled by heparin.	Heparin	246-253	coagulation factor II, thrombin	Homo sapiens	76-84
2757391-5	1989	The generated thrombin was inhibited by antithrombin, and this reaction was accelerated by heparin with high affinity for antithrombin but not by the corresponding oligosaccharides composed of 8-14 monosaccharide units.	Heparin	91-98	coagulation factor II	Mus musculus	14-22
2757391-5	1989	The generated thrombin was inhibited by antithrombin, and this reaction was accelerated by heparin with high affinity for antithrombin but not by the corresponding oligosaccharides composed of 8-14 monosaccharide units.	Heparin	91-98	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	122-134
2764920-10	1989	The heparin induced increase in fibronectin biosynthesis apparently reflects control at the translational or post-translational level.	Heparin	4-11	fibronectin 1	Homo sapiens	32-43
2598315-3	1989	The HA-heparin-catalyzed thrombin/AT III reaction was faster in the presence of 0.1 M NaCl at pH 6.05 than that in the absence of the salt.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	25-33
2473987-9	1989	In addition, hexabrachion bound to DNA as fibronectin does, and this binding could be inhibited by heparin but not by chondroitin sulfate.	Heparin	99-106	fibronectin 1	Homo sapiens	42-53
2752144-4	1989	Using this assay, time, dose, and heparin-dependent complexes were detected when uPA was incubated with normal plasma or purified urinary PCI, whereas no complexes were measurable using PCI-immunodepleted plasma.	Heparin	34-41	plasminogen activator, urokinase	Homo sapiens	81-84
2818566-0	1989	Anti-thrombin activities of heparin.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	5-13
2665815-0	1989	Heparin decreases the degradation rate of hepatic lipase in Fu5AH rat hepatoma cells.	Heparin	0-7	lipase C, hepatic type	Rattus norvegicus	42-56
2665815-10	1989	The half-intracellular residence times of hepatic lipase were 55 and 31 min in control and heparin-treated cultures, respectively.	Heparin	91-98	lipase C, hepatic type	Rattus norvegicus	42-56
2598315-0	1989	Dependence of the rate of thrombin/antithrombin III reaction upon the turnover rate of a catalytic amount of heparin.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	26-34
2598315-6	1989	Thus, it appears that AT III tends to form a ternary complex with the thrombin-DS or thrombin-LA-heparin complex, even in the presence of 0.1 M NaCl, whereas factor Xa reacts with the AT III-DS or AT III-LA-heparin complex.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	85-93
2598315-2	1989	However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin).	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	236-244
2598315-7	1989	These results indicate that HA-heparin is the only substance having the ability to catalyze the thrombin/AT III reaction, and that its turnover rate is markedly elevated in the presence of strongly electropositive and electronegative ions because of the decreased affinity of the enzyme for heparin under such conditions.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	96-104
2598315-7	1989	These results indicate that HA-heparin is the only substance having the ability to catalyze the thrombin/AT III reaction, and that its turnover rate is markedly elevated in the presence of strongly electropositive and electronegative ions because of the decreased affinity of the enzyme for heparin under such conditions.	Heparin	291-298	coagulation factor II, thrombin	Homo sapiens	96-104
2571200-0	1989	Release of lipoprotein lipase and hepatic triglyceride lipase in rats by heparin and other sulphated polysaccharides.	Heparin	73-80	lipoprotein lipase	Rattus norvegicus	11-29
2760115-7	1989	There is some evidence that the heparin-binding domain mediates incorporation of soluble TSP into the insoluble matrix form.	Heparin	32-39	thrombospondin 1	Homo sapiens	89-92
2760115-8	1989	The heparin-binding domain of TSP is a compact globular amino-terminal moiety that contains two clusters of basic amino acids and a single intrachain disulphide bond.	Heparin	4-11	thrombospondin 1	Homo sapiens	30-33
2551064-8	1989	The second order rate constants for inhibition of bovine APC and Gla-domainless bovine APC by human PCI were 0.61 x 10(4) and 0.26 x 10(4) M-1s-1 in the absence of heparin and 0.54 x 10(6) and 0.71 x 10(6) M-1s-1 in the presence of heparin, respectively.	Heparin	164-171	APC regulator of WNT signaling pathway	Bos taurus	57-60
2551064-8	1989	The second order rate constants for inhibition of bovine APC and Gla-domainless bovine APC by human PCI were 0.61 x 10(4) and 0.26 x 10(4) M-1s-1 in the absence of heparin and 0.54 x 10(6) and 0.71 x 10(6) M-1s-1 in the presence of heparin, respectively.	Heparin	232-239	APC regulator of WNT signaling pathway	Bos taurus	57-60
2571200-1	1989	The ability of parenteral heparin to release the capillary-bound enzymes lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) into the circulation is shared by several other sulphated polysaccharides.	Heparin	26-33	lipoprotein lipase	Rattus norvegicus	73-91
2571200-1	1989	The ability of parenteral heparin to release the capillary-bound enzymes lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) into the circulation is shared by several other sulphated polysaccharides.	Heparin	26-33	lipoprotein lipase	Rattus norvegicus	93-96
2742875-7	1989	Whereas the starting hHDL3 ligand was free of apoE, there was a substantial (7-fold) conversion of the HDL3 to apoE-containing HDL3 following in vivo circulation of the ligand, as shown by sodium phosphotungstate-MgCl2 precipitation or heparin-Sepharose column chromatography.	Heparin	236-243	apolipoprotein E	Rattus norvegicus	111-115
2745454-0	1989	Apolipoprotein E mediates binding of normal very low density lipoprotein to heparin but is not required for high affinity receptor binding.	Heparin	76-83	apolipoprotein E	Homo sapiens	0-16
2745454-8	1989	Lipolyzed VLDL with or without apoE were compared for their ability to bind to heparin or the up-regulated fibroblast LDL receptor.	Heparin	79-86	apolipoprotein E	Homo sapiens	31-35
2742875-7	1989	Whereas the starting hHDL3 ligand was free of apoE, there was a substantial (7-fold) conversion of the HDL3 to apoE-containing HDL3 following in vivo circulation of the ligand, as shown by sodium phosphotungstate-MgCl2 precipitation or heparin-Sepharose column chromatography.	Heparin	236-243	HDL3	Homo sapiens	103-107
2473082-0	1989	Transforming growth factor-beta activity is potentiated by heparin via dissociation of the transforming growth factor-beta/alpha 2-macroglobulin inactive complex.	Heparin	59-66	transforming growth factor beta 1	Homo sapiens	0-31
2673431-11	1989	The domains on the vWF molecule involved in the interactions of vWF with GP Ib, GP IIb-IIIa, collagen, F. VIII and heparin have been localized to varying extents.	Heparin	115-122	von Willebrand factor	Homo sapiens	19-22
2673431-11	1989	The domains on the vWF molecule involved in the interactions of vWF with GP Ib, GP IIb-IIIa, collagen, F. VIII and heparin have been localized to varying extents.	Heparin	115-122	von Willebrand factor	Homo sapiens	64-67
2473082-0	1989	Transforming growth factor-beta activity is potentiated by heparin via dissociation of the transforming growth factor-beta/alpha 2-macroglobulin inactive complex.	Heparin	59-66	transforming growth factor beta 1	Homo sapiens	91-122
2500452-2	1989	Binding of bFGF to ECM can be competed by heparin or heparan sulfate, and ECM-bound bFGF can be released by treating the cells with heparinase or heparatinase.	Heparin	42-49	fibroblast growth factor 2	Bos taurus	11-15
2500452-4	1989	The increase is prevented upon removal of ECM-bound bFGF by a neutral 2 M NaCl wash. Soluble heparin and heparan sulfate reduce the amount of ECM-bound bFGF released into the medium, possibly competing with ECM polysaccharides for heparinase-like enzymes produced by endothelial cells, suggesting that these enzymes are involved in the mobilization of ECM-bound bFGF.	Heparin	93-100	fibroblast growth factor 2	Bos taurus	52-56
2473082-2	1989	The present studies identify an interaction between heparin and TGF-beta in which heparin potentiates the biological action of TGF-beta.	Heparin	52-59	transforming growth factor beta 1	Homo sapiens	127-135
2500452-4	1989	The increase is prevented upon removal of ECM-bound bFGF by a neutral 2 M NaCl wash. Soluble heparin and heparan sulfate reduce the amount of ECM-bound bFGF released into the medium, possibly competing with ECM polysaccharides for heparinase-like enzymes produced by endothelial cells, suggesting that these enzymes are involved in the mobilization of ECM-bound bFGF.	Heparin	93-100	fibroblast growth factor 2	Bos taurus	152-156
2500452-4	1989	The increase is prevented upon removal of ECM-bound bFGF by a neutral 2 M NaCl wash. Soluble heparin and heparan sulfate reduce the amount of ECM-bound bFGF released into the medium, possibly competing with ECM polysaccharides for heparinase-like enzymes produced by endothelial cells, suggesting that these enzymes are involved in the mobilization of ECM-bound bFGF.	Heparin	93-100	fibroblast growth factor 2	Bos taurus	152-156
2738111-2	1989	Three methods of removing bFGF from heparin-like binding sites in the extracellular matrix, but not from bFGF receptors, abolished this long-term effect of a brief exposure to bFGF.	Heparin	36-43	fibroblast growth factor 2	Bos taurus	26-30
2738111-4	1989	Second, BCE cells were incubated with bFGF for 10 minutes in the presence of heparin, and cells were washed with PBS and incubated in bFGF-free medium.	Heparin	77-84	fibroblast growth factor 2	Bos taurus	38-42
2473082-2	1989	The present studies identify an interaction between heparin and TGF-beta in which heparin potentiates the biological action of TGF-beta.	Heparin	82-89	transforming growth factor beta 1	Homo sapiens	64-72
2473082-2	1989	The present studies identify an interaction between heparin and TGF-beta in which heparin potentiates the biological action of TGF-beta.	Heparin	82-89	transforming growth factor beta 1	Homo sapiens	127-135
2473082-3	1989	Using a neutralizing antibody to TGF-beta, we observed that the short term antiproliferative effect of heparin depended upon the presence of biologically active TGF-beta.	Heparin	103-110	transforming growth factor beta 1	Homo sapiens	33-41
2473082-3	1989	Using a neutralizing antibody to TGF-beta, we observed that the short term antiproliferative effect of heparin depended upon the presence of biologically active TGF-beta.	Heparin	103-110	transforming growth factor beta 1	Homo sapiens	161-169
2473082-5	1989	Binding studies demonstrated that the addition of heparin (100 micrograms/ml) to medium containing 10% plasma-derived serum resulted in a 45% increase in the specific binding of 125I-TGF-beta to cells.	Heparin	50-57	transforming growth factor beta 1	Homo sapiens	183-191
2473082-6	1989	Likewise, heparin induced a twofold increase in the growth inhibitory action of TGF-beta at concentrations of TGF-beta near its apparent dissociation constant.	Heparin	10-17	transforming growth factor beta 1	Homo sapiens	80-88
2473082-6	1989	Likewise, heparin induced a twofold increase in the growth inhibitory action of TGF-beta at concentrations of TGF-beta near its apparent dissociation constant.	Heparin	10-17	transforming growth factor beta 1	Homo sapiens	110-118
2473082-8	1989	Heparin increases the electrophoretic mobility of TGF-beta apparently by freeing TGF-beta from its complex with alpha 2-macroglobulin.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	50-58
2473082-8	1989	Heparin increases the electrophoretic mobility of TGF-beta apparently by freeing TGF-beta from its complex with alpha 2-macroglobulin.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	81-89
2473082-10	1989	Relatively high, antiproliferative concentrations of heparin (1-100 micrograms/ml) were required to dissociate the TGF-beta/alpha 2-macroglobulin complex.	Heparin	53-60	transforming growth factor beta 1	Homo sapiens	115-123
2473082-11	1989	Thus, it appears that the antiproliferative effect of heparin may be partially attributed to its ability to potentiate the biological activity of TGF-beta by dissociating it from alpha 2-macroglobulin, which normally renders it inactive.	Heparin	54-61	transforming growth factor beta 1	Homo sapiens	146-154
2508260-0	1989	Additive effect of dDAVP and standard heparin in increasing plasma t-PA.	Heparin	38-45	plasminogen activator, tissue type	Homo sapiens	67-71
2659597-4	1989	Many of these processes are heparin-inhibitable and are mediated by a proteolytic fragment of TSP called the heparin binding domain (HBD).	Heparin	28-35	thrombospondin 1	Homo sapiens	94-97
2659597-4	1989	Many of these processes are heparin-inhibitable and are mediated by a proteolytic fragment of TSP called the heparin binding domain (HBD).	Heparin	109-116	thrombospondin 1	Homo sapiens	94-97
2659597-6	1989	A fragment of a TSP cDNA that encodes the heparin binding domain was inserted into the prokaryotic expression vector pJBL6.	Heparin	42-49	thrombospondin 1	Homo sapiens	16-19
2794798-5	1989	The HSL was adsorbed to heparin-Sepharose and the CO- and PNPB-hydrolyzing activities were eluted together in the same peak.	Heparin	24-31	lipase E, hormone sensitive type	Bos taurus	4-7
2508260-12	1989	Our results demonstrated an additive effect of dDAVP and standard heparin on the increase in circulating t-PA, the effect of dDAVP being potentiated and prolonged by heparin.	Heparin	66-73	plasminogen activator, tissue type	Homo sapiens	105-109
2508260-12	1989	Our results demonstrated an additive effect of dDAVP and standard heparin on the increase in circulating t-PA, the effect of dDAVP being potentiated and prolonged by heparin.	Heparin	166-173	plasminogen activator, tissue type	Homo sapiens	105-109
2525126-5	1989	The detergent-solubilized HSPG bound to octyl-Sepharose columns, whereas the hydrophilic form did not; this latter form, however, was released from the membrane by heparin.	Heparin	164-171	syndecan 2	Rattus norvegicus	26-30
2508260-7	1989	The infusion of dDAVP followed by standard heparin resulted in a higher increase in plasma t-PA activity, t-PA antigen, circulating t-PA specific activity and FPLA when compared with dDAVP followed by saline.	Heparin	43-50	plasminogen activator, tissue type	Homo sapiens	91-95
2508260-7	1989	The infusion of dDAVP followed by standard heparin resulted in a higher increase in plasma t-PA activity, t-PA antigen, circulating t-PA specific activity and FPLA when compared with dDAVP followed by saline.	Heparin	43-50	plasminogen activator, tissue type	Homo sapiens	106-110
2508260-7	1989	The infusion of dDAVP followed by standard heparin resulted in a higher increase in plasma t-PA activity, t-PA antigen, circulating t-PA specific activity and FPLA when compared with dDAVP followed by saline.	Heparin	43-50	plasminogen activator, tissue type	Homo sapiens	106-110
2799755-1	1989	We investigated the effect on thrombin generation in plasma of the pentasaccharide that represent the AT III/binding site in heparin.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	30-38
2470763-9	1989	Heparin, a potent inhibitor of SMC growth, increased the level of type III collagen mRNA about 2.5-fold and also increased the level of alpha 2(V) collagen and fibronectin.	Heparin	0-7	fibronectin 1	Homo sapiens	160-171
2799755-7	1989	In contrast to classical heparin it does inhibit the peak of thrombin formation in platelet rich plasma, probably because it is less subject to inactivation by heparin binding proteins from platelets than classical heparin is.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	61-69
2781509-2	1989	The variant antithrombin was isolated from plasma of the propositus by chromatography on heparin-Sepharose, followed by passage through thrombin-Sepharose to remove the normal antithrombin component that is present.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	16-24
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	130-138	coagulation factor II, thrombin	Homo sapiens	269-277
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	206-214	coagulation factor II, thrombin	Homo sapiens	269-277
2498379-7	1989	The binding of T4 to apoA-I was reduced by known inhibitors of T4 binding to serum proteins (diclofenac = mefenamic acid = furosemide = 8-anilinonaphthalene sulfonic acid much greater than dilantin greater than heparin greater than barbital) and by lipids (unsaturated fatty acids greater than cholesterol = cholesterol esters = phospholipids greater than saturated fatty acids = diglycerides = triglycerides).	Heparin	211-218	apolipoprotein A1	Homo sapiens	21-27
2738102-3	1989	The level of bFGF in BAE cell lysates was compared with the level of heparin-releasable bFGF in intact BAE cell monolayers, intact cells with exposed extracellular matrix (nonlytic matrices), and extracellular matrices prepared by cell lysis (lytic matrices).	Heparin	69-76	fibroblast growth factor 2	Bos taurus	88-92
2719757-5	1989	Lipoprotein lipase activity in post-heparin serum, taken 6 h after a meal, was 31% decreased in mackerel oil-fed animals.	Heparin	36-43	lipoprotein lipase	Sus scrofa	0-18
2524607-5	1989	In the presence of ECGF-heparin, the immediate establishment of an EC layer after sodding was observed, whereas seeded grafts required almost 48 hours for cells to reach the surface.	Heparin	24-31	fibroblast growth factor 1	Homo sapiens	19-23
2470746-1	1989	The high heparin affinity subtype C of the secretory enzyme extracellular superoxide dismutase (EC-SOD) exists in the body mainly complexed with extracellular sulfated glycosaminoglycans (SGAGs).	Heparin	9-16	superoxide dismutase 3	Homo sapiens	60-94
2470746-1	1989	The high heparin affinity subtype C of the secretory enzyme extracellular superoxide dismutase (EC-SOD) exists in the body mainly complexed with extracellular sulfated glycosaminoglycans (SGAGs).	Heparin	9-16	superoxide dismutase 3	Homo sapiens	96-102
2470746-3	1989	Complex formation between heparin and EC-SOD C could also be observed as increases in apparent molecular weight of the enzyme.	Heparin	26-33	superoxide dismutase 3	Homo sapiens	38-44
2730645-1	1989	Basic fibroblast growth factor (bFGF) is a heparin-binding angiogenic polypeptide mitogen.	Heparin	43-50	fibroblast growth factor 2	Cavia porcellus	0-30
2730645-1	1989	Basic fibroblast growth factor (bFGF) is a heparin-binding angiogenic polypeptide mitogen.	Heparin	43-50	fibroblast growth factor 2	Cavia porcellus	32-36
2785417-1	1989	Controversy exists in the literature concerning the potentiating effect of heparin on the inactivation rate of factor XIa by antithrombin III (AT III) in both purified systems and in plasma.	Heparin	75-82	serpin family C member 1	Bos taurus	125-141
2785417-1	1989	Controversy exists in the literature concerning the potentiating effect of heparin on the inactivation rate of factor XIa by antithrombin III (AT III) in both purified systems and in plasma.	Heparin	75-82	serpin family C member 1	Bos taurus	143-149
2785417-4	1989	However, when ionic strength was decreased, a progressive increase in the potentiating effect was observed, reaching 6.5-fold at I = 0.15 N. At saturating concentrations of heparin, which results in the formation of 100% AT III-heparin complex, (greater than ten-fold molar excess over AT III) in purified systems, all heparin preparations (porcine, bovine, low molecular weight [LMW], and high affinity) yielded an approximately 30-fold augmentation of the factor XIa inactivation rate.	Heparin	173-180	serpin family C member 1	Bos taurus	221-227
2785417-4	1989	However, when ionic strength was decreased, a progressive increase in the potentiating effect was observed, reaching 6.5-fold at I = 0.15 N. At saturating concentrations of heparin, which results in the formation of 100% AT III-heparin complex, (greater than ten-fold molar excess over AT III) in purified systems, all heparin preparations (porcine, bovine, low molecular weight [LMW], and high affinity) yielded an approximately 30-fold augmentation of the factor XIa inactivation rate.	Heparin	173-180	serpin family C member 1	Bos taurus	286-292
2785417-4	1989	However, when ionic strength was decreased, a progressive increase in the potentiating effect was observed, reaching 6.5-fold at I = 0.15 N. At saturating concentrations of heparin, which results in the formation of 100% AT III-heparin complex, (greater than ten-fold molar excess over AT III) in purified systems, all heparin preparations (porcine, bovine, low molecular weight [LMW], and high affinity) yielded an approximately 30-fold augmentation of the factor XIa inactivation rate.	Heparin	228-235	serpin family C member 1	Bos taurus	221-227
2785417-4	1989	However, when ionic strength was decreased, a progressive increase in the potentiating effect was observed, reaching 6.5-fold at I = 0.15 N. At saturating concentrations of heparin, which results in the formation of 100% AT III-heparin complex, (greater than ten-fold molar excess over AT III) in purified systems, all heparin preparations (porcine, bovine, low molecular weight [LMW], and high affinity) yielded an approximately 30-fold augmentation of the factor XIa inactivation rate.	Heparin	228-235	serpin family C member 1	Bos taurus	221-227
2785417-5	1989	However, when heparin was less than saturating, we observed that various heparin preparations affected the AT III-induced inactivation of factor XIa to different degrees even though they exhibited the same inhibitory activity (1 U/mL) against thrombin.	Heparin	14-21	serpin family C member 1	Bos taurus	107-113
2785417-5	1989	However, when heparin was less than saturating, we observed that various heparin preparations affected the AT III-induced inactivation of factor XIa to different degrees even though they exhibited the same inhibitory activity (1 U/mL) against thrombin.	Heparin	73-80	serpin family C member 1	Bos taurus	107-113
2785417-6	1989	This variation resulted from differences in the number of AT III binding sites in each heparin preparation, despite a similar Kd for each.	Heparin	87-94	serpin family C member 1	Bos taurus	58-64
2785417-8	1989	A high therapeutic dose of heparin only permits the formation of 2.5% to 16.5% of the AT III-heparin complexes that can be achieved at saturation.	Heparin	27-34	serpin family C member 1	Bos taurus	86-92
2785417-8	1989	A high therapeutic dose of heparin only permits the formation of 2.5% to 16.5% of the AT III-heparin complexes that can be achieved at saturation.	Heparin	93-100	serpin family C member 1	Bos taurus	86-92
2468667-7	1989	Heparin, which binds bFGF, has no effect on complex formation.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	21-25
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	20-28
2726739-0	1989	Fibrin monomer protects thrombin from inactivation by heparin-antithrombin III: implications for heparin efficacy.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	24-32
2523801-3	1989	Although GCP/IL-8 and beta-thromboglobulin had a similar affinity for heparin, they could be separated on a cation-exchange column.	Heparin	70-77	golgin B1	Homo sapiens	9-12
2523801-3	1989	Although GCP/IL-8 and beta-thromboglobulin had a similar affinity for heparin, they could be separated on a cation-exchange column.	Heparin	70-77	C-X-C motif chemokine ligand 8	Homo sapiens	13-17
2745517-12	1989	Prothrombin time (PT) and activated partial thromboplastin time (aPTT) showed a positive correlation (r = 0.36 and r = 0.25) with heparin need in CCHD group but no correlation was found in RHD group.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	0-11
2654474-1	1989	The high heparin-affinity subtype C of the secretory enzyme extracellular-superoxide dismutase (EC-SOD) was found to bind to cultured mammalian cells, forming an equilibrium between the cells and the medium.	Heparin	9-16	superoxide dismutase 3	Homo sapiens	60-94
2654474-1	1989	The high heparin-affinity subtype C of the secretory enzyme extracellular-superoxide dismutase (EC-SOD) was found to bind to cultured mammalian cells, forming an equilibrium between the cells and the medium.	Heparin	9-16	superoxide dismutase 3	Homo sapiens	96-102
2726739-1	1989	Fibrin II monomer has a dramatic inhibitory effect on the rate of heparin-catalyzed inactivation of human alpha-thrombin by antithrombin III.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	112-120
2726739-4	1989	Fibrinogen and the product of plasmin degradation of fibrinogen, fragment E, at 6 microM concentrations also decreased the second-order rate constant for heparin-catalyzed thrombin inactivation, but by factors of only 2.7 and 1.9, respectively.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	172-180
2726739-5	1989	On the basis of these observations it is proposed that protection of thrombin from inactivation by heparin-antithrombin III by fibrin II monomer can explain the limited efficacy of heparin in preventing coronary reocclusion in patients treated with tissue plasminogen activator and other fibrinolytic agents.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	69-77
2546282-4	1989	Reduction of thrombin generation to 20% of control values was closely correlated with the prevention of thrombosis after 20 minutes" stasis, but this was only achieved with UFH.	Heparin	173-176	coagulation factor II, thrombin	Homo sapiens	13-21
2713384-6	1989	Subsequent incubation for 18 h at 37 degrees C produced marked increases in the apoE content of HDL from heparin-treated plasma even when LCAT was inhibited.	Heparin	105-112	apolipoprotein E	Rattus norvegicus	80-84
2539370-8	1989	Heparin caused an increase in CE tracer in a d less than 1.063 g/ml fraction of the medium that more than accounted for the heparin blockade of CETP-stimulated CE uptake.	Heparin	0-7	cholesteryl ester transfer protein	Homo sapiens	144-148
2713384-10	1989	It is concluded that changes in HDL particle size are mainly attributable to LCAT, but that lipase activities, which are either free in rat plasma or releasable by heparin, play a role in restructuring the phospholipid moiety and altering the protein composition of the HDL, especially with respect to apoE, a potential ligand to cellular receptors.	Heparin	164-171	apolipoprotein E	Rattus norvegicus	302-306
2539370-8	1989	Heparin caused an increase in CE tracer in a d less than 1.063 g/ml fraction of the medium that more than accounted for the heparin blockade of CETP-stimulated CE uptake.	Heparin	124-131	cholesteryl ester transfer protein	Homo sapiens	144-148
2719640-10	1989	Heparin increased the amount of lipoprotein lipase activity released to the medium.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	32-50
2488545-2	1989	Data are now presented indicating that MSF present in the conditioned medium of fetal and cancer patient fibroblasts is precipitated at 10% saturation ammonium sulfate and binds to heparin and cation-exchange resins.	Heparin	181-188	fibronectin 1	Homo sapiens	39-42
2726317-2	1989	We explored this apparent paradox by comparing how well heparin accelerated inhibition of exogenous thrombin and prevented thrombin generation in defibrinated neonatal and adult plasmas.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	100-108
2726317-2	1989	We explored this apparent paradox by comparing how well heparin accelerated inhibition of exogenous thrombin and prevented thrombin generation in defibrinated neonatal and adult plasmas.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	123-131
2726317-3	1989	Using amidolytic assays, we determined the effects of heparin on 1) the neutralization of exogenous human alpha-thrombin and on 2) the formation of endogenous thrombin activity after contact activation and recalcification.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	112-120
2726317-6	1989	However, de novo generation of thrombin activity was very susceptible to inhibition by heparin, even in neonatal plasmas with physiologically low AT III levels.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	31-39
2726317-7	1989	Peak thrombin activity generated in neonatal plasma in the absence of heparin was 50% or less of peak adult activity, and this already reduced ability of neonatal plasma to generate thrombin activity upon prothrombin activation was further decreased by heparin (0.05-0.2 U/mL).	Heparin	253-260	coagulation factor II, thrombin	Homo sapiens	5-13
2726317-7	1989	Peak thrombin activity generated in neonatal plasma in the absence of heparin was 50% or less of peak adult activity, and this already reduced ability of neonatal plasma to generate thrombin activity upon prothrombin activation was further decreased by heparin (0.05-0.2 U/mL).	Heparin	253-260	coagulation factor II, thrombin	Homo sapiens	182-190
2726317-8	1989	We conclude that due to the neonatal AT III deficiency, added thrombin is inactivated less effectively by heparin in neonatal than in normal adult plasma.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	62-70
2726317-9	1989	Yet, the generation of thrombin activity is impaired in neonatal plasma and easily suppressed by heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	23-31
2709525-7	1989	Thus we show (1) HIPA can proceed independently of TxA2 synthesis; (2) heparin in certain patients can release lysosomal hydrolases, thus mimicking strong platelet agonists such as thrombin; and (3) iloprost but not aspirin prevents HIPA regardless of the biochemical pathways involved.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	181-189
2488545-3	1989	Based on this information, we have devised a scheme for the purification of MSF involving the sequential application of ammonium sulfate precipitation, heparin affinity, gel filtration, and reverse-phase chromatography.	Heparin	152-159	fibronectin 1	Homo sapiens	76-79
2466666-9	1989	Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced.	Heparin	135-142	coagulation factor II, thrombin	Homo sapiens	19-27
2466666-9	1989	Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced.	Heparin	185-192	coagulation factor II, thrombin	Homo sapiens	19-27
2466666-9	1989	Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced.	Heparin	185-192	coagulation factor II, thrombin	Homo sapiens	19-27
2646946-7	1989	Heparin, by preventing the insulin-induced fall in FFA, also blocked the early rise in carbohydrate oxidation.	Heparin	0-7	insulin	Homo sapiens	27-34
2917997-12	1989	Instead, hepatic lipase originating elsewhere, presumably in the liver, is accumulated from the circulation at heparin-sensitive sites in ovarian blood vessels.	Heparin	111-118	lipase C, hepatic type	Rattus norvegicus	9-23
2466852-7	1989	In comparison, heparin slightly inhibited the stimulatory effect of aFGF and had no effect on epidermal growth factor (EGF) stimulation in keratinocyte cultures.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	68-72
2752479-6	1989	Inhibition of thrombin activity by the ATIII-APC-heparin mixture was weak as compared with that by the ATIII-heparin mixture after a 1-min incubation, but after a 2-min incubation the inhibitory activities were equal.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	14-22
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	15-23
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	155-163
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	15-23
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	155-163
2752479-8	1989	When the inhibitory effect of APC alone or the APC-heparin mixture on the platelet prothrombin converting activity (PPCA) was examined, heparin accelerated the PPCA inhibition by APC.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	83-94
2752479-8	1989	When the inhibitory effect of APC alone or the APC-heparin mixture on the platelet prothrombin converting activity (PPCA) was examined, heparin accelerated the PPCA inhibition by APC.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	83-94
2783905-5	1989	Heparin-Sepharose fractionation of cell extracts revealed that bone cells contained a basic FGF (bFGF)-like molecule, that displayed high affinity for heparin.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	86-95
2783905-5	1989	Heparin-Sepharose fractionation of cell extracts revealed that bone cells contained a basic FGF (bFGF)-like molecule, that displayed high affinity for heparin.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	97-101
2783905-5	1989	Heparin-Sepharose fractionation of cell extracts revealed that bone cells contained a basic FGF (bFGF)-like molecule, that displayed high affinity for heparin.	Heparin	151-158	fibroblast growth factor 2	Bos taurus	86-95
2783905-5	1989	Heparin-Sepharose fractionation of cell extracts revealed that bone cells contained a basic FGF (bFGF)-like molecule, that displayed high affinity for heparin.	Heparin	151-158	fibroblast growth factor 2	Bos taurus	97-101
2466852-8	1989	In fibroblast cultures the addition of heparin enhanced the mitogenic effect of aFGF, had a minimal stimulatory effect on the mitogenic activity of bFGF, and had no effect on EGF-stimulated growth.	Heparin	39-46	fibroblast growth factor 1	Homo sapiens	80-84
2466852-8	1989	In fibroblast cultures the addition of heparin enhanced the mitogenic effect of aFGF, had a minimal stimulatory effect on the mitogenic activity of bFGF, and had no effect on EGF-stimulated growth.	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	148-152
2546277-0	1989	The mode of action of low molecular weight heparin preparation (PK10169) and two of its major components on thrombin generation in plasma.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	108-116
2538819-5	1989	Binding to the EDTA-resistant site, however, is readily inhibited by heparin (as is the LDL receptor) and also by antisera prepared against rat or bovine LDL receptor.	Heparin	69-76	low density lipoprotein receptor	Rattus norvegicus	88-100
2914897-1	1989	The genesis of the positive bands in the far-ultraviolet circular dichroic spectra of human plasma fibronectin and its 31-kDa NH2-terminal heparin-binding fragment was studied.	Heparin	139-146	fibronectin 1	Homo sapiens	99-110
2914965-13	1989	The enhancement of thrombin inhibition by fucoidan, like heparin and dermatan sulfate, is eliminated by selective chemical modification of lysyl residues either of heparin cofactor II or of thrombin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	19-27
2749590-7	1989	The patient"s parents and three of her brothers demonstrated qualitative abnormality of AT III; heparin cofactor activity was 30-50% of normal levels in the presence of both thrombin and F.Xa.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	174-182
2713360-2	1989	The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	63-71
2713360-1	1989	The binding of heparin to high molecular weight kininogen (H-kininogen) was analyzed by the effect of kininogen in decreasing the heparin-induced enhancement of the rate of inactivation of thrombin by antithrombin.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	189-197
2499459-0	1989	Improved haemorheology associated with a reduction in plasma fibrinogen and LDL in patients being treated by heparin-induced extracorporeal LDL precipitation (HELP).	Heparin	109-116	fibrinogen beta chain	Homo sapiens	61-71
2713360-1	1989	The binding of heparin to high molecular weight kininogen (H-kininogen) was analyzed by the effect of kininogen in decreasing the heparin-induced enhancement of the rate of inactivation of thrombin by antithrombin.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	189-197
2492737-0	1989	Enhancement of arterial thrombolysis with native tissue type plasminogen activator by pretreatment with heparin or batroxobin: an angioscopic study.	Heparin	104-111	plasminogen activator, tissue type	Homo sapiens	49-82
2492737-1	1989	The enhancement of canine arterial thrombolysis with native tissue type plasminogen activator (nt-PA) obtained from human-derived normal cells by pretreatment with heparin or the defibrinogenating agent, batroxobin, was evaluated with angioscopy.	Heparin	164-171	tissue-type plasminogen activator	Canis lupus familiaris	60-93
2492737-5	1989	Fifteen minutes after drug infusion, plasma fibrinogen levels decreased to 89% of preinfusion value in nt-PA alone, to 84% in nt-PA plus heparin, and to less than 5% in nt-PA plus batroxobin.	Heparin	137-144	fibrinogen beta chain	Homo sapiens	44-54
2466498-0	1989	[Alpha-thrombin stimulation of heparin secretion by the peritoneal mast cells in rats].	Heparin	31-38	coagulation factor II	Rattus norvegicus	7-15
2466498-4	1989	CTMC which were stimulated by very low concentrations of alpha-thrombin (10(-11)-10(-8) M) can release high level of heparin, but not histamine.	Heparin	117-124	coagulation factor II	Rattus norvegicus	63-71
2466498-6	1989	Unlike alpha-thrombin which has both the active centre and the recognition site for HMS, beta/gamma-thrombin with catalytic activity but with disrupted recognition site induced the heparin release from mast cells only at higher concentrations than alpha-thrombin.	Heparin	181-188	coagulation factor II	Rattus norvegicus	100-108
2466498-6	1989	Unlike alpha-thrombin which has both the active centre and the recognition site for HMS, beta/gamma-thrombin with catalytic activity but with disrupted recognition site induced the heparin release from mast cells only at higher concentrations than alpha-thrombin.	Heparin	181-188	coagulation factor II	Rattus norvegicus	100-108
2466498-8	1989	We consider that alpha-thrombin induced release of heparin by CTMC account for proteolytic and hormone-like activity enzyme by means of both the active centre and the additional recognition site for HMS.	Heparin	51-58	coagulation factor II	Rattus norvegicus	23-31
2713360-2	1989	The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	72-80
2713360-2	1989	The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration.	Heparin	280-287	coagulation factor II, thrombin	Homo sapiens	63-71
2713360-2	1989	The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration.	Heparin	280-287	coagulation factor II, thrombin	Homo sapiens	72-80
2499459-1	1989	Heparin-induced Extracorporeal LDL-Precipitation (HELP) is an effective procedure for the elimination of both plasma LDL and fibrinogen.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	125-135
2915979-2	1989	The factor, provisionally termed keratinocyte growth factor (KGF) because of its predominant activity on this cell type, was purified to homogeneity by a combination of ultrafiltration, heparin-Sepharose affinity chromatography, and hydrophobic chromatography on a C4 reversed-phase HPLC column.	Heparin	186-193	fibroblast growth factor 7	Homo sapiens	33-59
2915979-2	1989	The factor, provisionally termed keratinocyte growth factor (KGF) because of its predominant activity on this cell type, was purified to homogeneity by a combination of ultrafiltration, heparin-Sepharose affinity chromatography, and hydrophobic chromatography on a C4 reversed-phase HPLC column.	Heparin	186-193	fibroblast growth factor 7	Homo sapiens	61-64
2909522-2	1989	By using the 3-O-sulfated glucosamine residue as a marker for the anti-thrombin-binding sequence, the location of this sequence within the heparin chain was investigated.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	71-79
2491851-8	1989	When this kinase was inhibited with heparin, cAMP addition to the neurofilament preparation stimulated the phosphorylation of L-2, and addition of the purified catalytic subunit of cAMP-dependent protein kinase induced intense labeling of L-2.	Heparin	36-43	skull development traits QTL 2	Mus musculus	126-129
2920007-7	1989	In contrast, heparin and Phe-Pro-Arg-CH2Cl completely inhibited prothrombin activation for at least 45 s in CAP supplemented with 1 nM-thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	67-75
2660684-0	1989	Thrombin anion-binding exosite interactions with heparin and various polyanions.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	0-8
2463827-2	1989	Twelve known heparin-binding sequences in vitronectin, apolipoproteins E and B-100, and platelet factor 4 were used to formulate two search strings for identifying potential heparin-binding regions in other proteins.	Heparin	13-20	apolipoprotein E	Homo sapiens	55-82
2463827-2	1989	Twelve known heparin-binding sequences in vitronectin, apolipoproteins E and B-100, and platelet factor 4 were used to formulate two search strings for identifying potential heparin-binding regions in other proteins.	Heparin	174-181	apolipoprotein E	Homo sapiens	55-82
2713428-0	1989	Activity toward thrombin-antithrombin of heparin immobilized on two hydrogels.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	16-24
2713428-2	1989	We found that as tresyl chloride activation of PVA increased, the specific activity of the bound heparin toward thrombin and antithrombin decreased by nearly a factor of 10 and that commercial heparin bound to PEO had nearly ten-fold greater activity than when bound to PVA at comparable concentrations.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	112-120
2713428-3	1989	These findings suggest that the long "leash" provided by PEO hydrogels may give the heparin more access to the thrombin-antithrombin pair than the tight bond to PVA, and that crowding of heparin units on a surface limits access of the thrombin-antithrombin pair.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	111-119
2713428-3	1989	These findings suggest that the long "leash" provided by PEO hydrogels may give the heparin more access to the thrombin-antithrombin pair than the tight bond to PVA, and that crowding of heparin units on a surface limits access of the thrombin-antithrombin pair.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	124-132
2920007-0	1989	Unfractionated heparin inhibits thrombin-catalysed amplification reactions of coagulation more efficiently than those catalysed by factor Xa.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	32-40
2920007-1	1989	We have proposed previously that the steps in coagulation most sensitive to inhibition by heparin are the thrombin-dependent amplification reactions, and that prothrombinase is formed in heparinized plasma only after Factor Xa activates Factor VIII and Factor V. These propositions were based on the demonstration that both heparin and Phe-Pro-Arg-CH2Cl completely inhibited 125I-prothrombin activation for up to 60 s when contact-activated plasma (CAP) was replenished with Ca2+.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	106-114
2920007-3	1989	Additional support for the above hypotheses is provided in this study by demonstrating that, when the activity of thrombin is suppressed by heparin (indirectly) or by Phe-Pro-Arg-CH2Cl (directly), exogenous Factor Xa reverses the ability of these two agents to inhibit prothrombin activation.	Heparin	140-147	coagulation factor II, thrombin	Homo sapiens	114-122
2920011-0	1989	Effect of heparin on the glia-derived-nexin-thrombin interaction.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	44-52
2920011-6	1989	At optimal heparin concentrations, the rate of inactivation of alpha-thrombin by GdN was 0.5-1.2 nM-1.s-1, which suggests that, under these conditions, the interaction is diffusion-controlled.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	69-77
2598628-1	1989	Characterization of tri-, di- and monoacylglycerol lipase activities in post-heparin effluents.	Heparin	77-84	monoglyceride lipase	Rattus norvegicus	34-57
2910358-8	1989	Cell surface bound heparin was functionally active and markedly accelerated the inactivation of thrombin by antithrombin III.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	96-104
2766666-1	1989	A new competitive binding assay, which measures the concentration of heparin rather than its activity, was used to confirm the presence of a high concentration of heparin in blood samples from a patient which showed unexpected gross prolongation of thrombin time (TT) and activated partial thromboplastin time (APTT).	Heparin	163-170	coagulation factor II, thrombin	Homo sapiens	249-257
2910581-1	1989	We compared concentrations of antithrombin III (AT-III) in plasma, as determined by an immunological method and by a functional thrombin inhibition method, in the presence of heparin in 160 blood samples from Type I diabetics.	Heparin	175-182	coagulation factor II, thrombin	Homo sapiens	34-42
2483237-6	1989	An alternative way for controlling blood clotting activation and thrombin generation appears to be low-dose heparin treatment.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	65-73
2557219-4	1989	Increased transaminases were frequent with conventional heparin (18% and 32% of patients on high-dose heparin developed abnormal AsT and AlT values, respectively compared with 14% and 17% patients on low dose therapy).	Heparin	102-109	solute carrier family 17 member 5	Homo sapiens	129-132
2920976-9	1989	The low antithrombin III concentration (0.44 +/- 0.13 mg/dl) in protein-poor dialysate seems to be sufficient to inhibit the thrombin activity after acceleration by heparin.	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	12-20
2482435-3	1989	The heparin concentration causing 50% inhibition was 45 micrograms/ml for the basal activity and 33 and 85 micrograms/ml for the parathyroid hormone (PTH) and glucagon-stimulated activities, respectively.	Heparin	4-11	parathyroid hormone	Rattus norvegicus	129-148
2488845-1	1989	Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	132-140
2488845-1	1989	Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes.	Heparin	75-82	coagulation factor II, thrombin	Homo sapiens	132-140
2488845-2	1989	The extent of inactivation, for a constant flow time, was approximately constant over ten cycles of exposure to thrombin and antithrombin III, suggesting that the immobilized heparin was reusable, as expected from the catalytic nature of non-immobilized heparin.	Heparin	175-182	coagulation factor II, thrombin	Homo sapiens	112-120
2488845-3	1989	Assessment of the chromogenic substrate activity of adsorbed thrombin and the extent of displacement were less conclusive with the implication that thrombin is adsorbed to heparin-PVA or PVA without heparin in multiple states.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	148-156
2910884-0	1989	Interaction of heparin with human basic fibroblast growth factor: protection of the angiogenic protein from proteolytic degradation by a glycosaminoglycan.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	34-64
2910884-1	1989	Fibroblast growth factors (FGF) are a family of heparin-binding angiogenic polypeptide mitogens.	Heparin	48-55	fibroblast growth factor 2	Homo sapiens	27-30
2910884-2	1989	In the presence of heparin, recombinant human basic fibroblast growth factor (bFGF) is fully protected from tryptic digestion and partially protected from chymotryptic digestion.	Heparin	19-26	fibroblast growth factor 2	Homo sapiens	46-76
2910884-2	1989	In the presence of heparin, recombinant human basic fibroblast growth factor (bFGF) is fully protected from tryptic digestion and partially protected from chymotryptic digestion.	Heparin	19-26	fibroblast growth factor 2	Homo sapiens	78-82
2910884-3	1989	Complete protection of bFGF by heparin is achieved at ratios of growth factor:heparin of approximately 10 or less (w/w).	Heparin	31-38	fibroblast growth factor 2	Homo sapiens	23-27
2910884-4	1989	The protection requires bioactive bFGF because inactivated bFGF is rapidly degraded by trypsin or chymotrypsin in the presence of heparin.	Heparin	130-137	fibroblast growth factor 2	Homo sapiens	34-38
2910884-4	1989	The protection requires bioactive bFGF because inactivated bFGF is rapidly degraded by trypsin or chymotrypsin in the presence of heparin.	Heparin	130-137	fibroblast growth factor 2	Homo sapiens	59-63
2910884-5	1989	The bFGF-heparin interaction forms hydrophobic complexes which become insoluble in aqueous buffers at bFGF:heparin ratios of 8 to 10 (w/w).	Heparin	9-16	fibroblast growth factor 2	Homo sapiens	4-8
2910884-5	1989	The bFGF-heparin interaction forms hydrophobic complexes which become insoluble in aqueous buffers at bFGF:heparin ratios of 8 to 10 (w/w).	Heparin	9-16	fibroblast growth factor 2	Homo sapiens	102-106
2910884-5	1989	The bFGF-heparin interaction forms hydrophobic complexes which become insoluble in aqueous buffers at bFGF:heparin ratios of 8 to 10 (w/w).	Heparin	107-114	fibroblast growth factor 2	Homo sapiens	4-8
2910884-6	1989	The heparin was found to bind up to a tenfold excess of bFGF on a weight basis.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	56-60
2910884-7	1989	bFGF in the presence of heparin is as active as bFGF alone in inducing 3H-thymidine incorporation into Swiss 3T3 fibroblast DNA.	Heparin	24-31	fibroblast growth factor 2	Homo sapiens	0-4
2562205-2	1989	More recently, assays have been developed which measure the inhibitory action of heparin on isolated coagulation enzymes, notably Factor Xa and thrombin, using specific amidolytic peptide substrates.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	144-152
2718441-2	1989	Inclusion of heparin, miscleron, complamin in the complex treatment was accompanied by a distinct reduction of the concentration of sterol-fibrinogen complexes, normalization of the ratio of polar sterols.	Heparin	13-20	fibrinogen beta chain	Homo sapiens	139-149
2654846-0	1989	[Hypoglycemic activity of the insulin-heparin complex and conditions for its appearance].	Heparin	38-45	insulin	Homo sapiens	30-37
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	72-79	insulin	Homo sapiens	109-116
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	72-79	insulin	Homo sapiens	159-166
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	72-79	insulin	Homo sapiens	159-166
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	117-124	insulin	Homo sapiens	109-116
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	117-124	insulin	Homo sapiens	159-166
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	117-124	insulin	Homo sapiens	159-166
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	117-124	insulin	Homo sapiens	109-116
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	117-124	insulin	Homo sapiens	159-166
2654846-1	1989	In animals with experimentally induced stable hyperglycemia attended by heparin deficiency in the blood, the insulin-heparin complex (the ratio of heparin and insulin in the complex was 1:4.7) produces a stronger hypoglycemic effect than that of an equivalent dose of insulin.	Heparin	117-124	insulin	Homo sapiens	159-166
2654846-4	1989	The results of the study bear evidence that intensification of the hypoglycemic effect in administration of insulin with heparin is due to the existence of hypoheparinemia, and confirm the concept that for adequate manifestation of the hypoglycemic effect of insulin a sufficient concentration of heparin is necessary.	Heparin	121-128	insulin	Homo sapiens	108-115
2654846-4	1989	The results of the study bear evidence that intensification of the hypoglycemic effect in administration of insulin with heparin is due to the existence of hypoheparinemia, and confirm the concept that for adequate manifestation of the hypoglycemic effect of insulin a sufficient concentration of heparin is necessary.	Heparin	121-128	insulin	Homo sapiens	259-266
2654846-4	1989	The results of the study bear evidence that intensification of the hypoglycemic effect in administration of insulin with heparin is due to the existence of hypoheparinemia, and confirm the concept that for adequate manifestation of the hypoglycemic effect of insulin a sufficient concentration of heparin is necessary.	Heparin	160-167	insulin	Homo sapiens	108-115
2506696-2	1989	Addition of heparin to cryoprecipitate extract at acid pH precipitated fibrinogen and fibronectin.	Heparin	12-19	fibrinogen beta chain	Homo sapiens	71-81
2506696-2	1989	Addition of heparin to cryoprecipitate extract at acid pH precipitated fibrinogen and fibronectin.	Heparin	12-19	fibronectin 1	Homo sapiens	86-97
2922698-4	1989	Whole blood anticoagulated by heparin, EDTA or sodium citrate, contained dephosphorylating activity against 32P-labeled fibrinogen, although there were significant differences in activity among the three anticoagulants.	Heparin	30-37	fibrinogen beta chain	Homo sapiens	120-130
2922702-0	1989	Structural features of heparin and their effect on heparin cofactor II mediated inhibition of thrombin.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	94-102
2718441-3	1989	The employment of miscleron and heparin furthered a reduction of the load of sterols on fibrinogen.	Heparin	32-39	fibrinogen beta chain	Homo sapiens	88-98
3191156-0	1988	Heparin modulates the secretion of a major excreted protein-like molecule by vascular smooth muscle cells.	Heparin	0-7	cathepsin L	Homo sapiens	37-59
3238649-1	1988	The influence of heparin on prothrombin conversion in plasma was estimated by measuring prothrombin disappearance with the aid of staphylocoagulase or by calculation from the thrombin generation curve, compensating for simultaneous thrombin inactivation by plasma protease inhibitors.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	31-39
3238649-1	1988	The influence of heparin on prothrombin conversion in plasma was estimated by measuring prothrombin disappearance with the aid of staphylocoagulase or by calculation from the thrombin generation curve, compensating for simultaneous thrombin inactivation by plasma protease inhibitors.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	91-99
3238649-3	1988	In contact-activated plasma prothrombinase generation is inhibited by heparin, because heparin lowers the ambient concentrations of thrombin so that the feedback activation of factor VIII by thrombin is diminished.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	31-39
3238649-3	1988	In contact-activated plasma prothrombinase generation is inhibited by heparin, because heparin lowers the ambient concentrations of thrombin so that the feedback activation of factor VIII by thrombin is diminished.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	132-140
3238649-3	1988	In contact-activated plasma prothrombinase generation is inhibited by heparin, because heparin lowers the ambient concentrations of thrombin so that the feedback activation of factor VIII by thrombin is diminished.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	31-39
3238649-3	1988	In contact-activated plasma prothrombinase generation is inhibited by heparin, because heparin lowers the ambient concentrations of thrombin so that the feedback activation of factor VIII by thrombin is diminished.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	132-140
3238649-5	1988	We conclude that heparin in plasma acts by its thrombin scavenging properties.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	47-55
3146370-19	1988	CONCLUSION: Recombinant tissue type plasminogen activator with heparin and aspirin reduces size of infarct, preserves left ventricular function, and reduces complications and death from cardiac causes but at increased risk of bleeding complications4+	Heparin	63-70	plasminogen activator, tissue type	Homo sapiens	24-57
2461712-1	1988	Pentosan polysulphate (PPS, SP 54, HEMOCLAR), a highly sulphated semi-synthetic polysaccharide of MW 4700 Daltons is as efficient as heparin in potentiating the mitogenic activity of acidic FGF (aFGF) on human umbilical vein endothelial cells (HUVEC).	Heparin	133-140	fibroblast growth factor 1	Homo sapiens	183-193
2461712-7	1988	PPS and heparin, which were chemotactic alone on BAEC, potentiated acidic FGF-induced migration but inhibited the chemotactic response of basic FGF.	Heparin	8-15	fibroblast growth factor 1	Homo sapiens	67-77
2461712-7	1988	PPS and heparin, which were chemotactic alone on BAEC, potentiated acidic FGF-induced migration but inhibited the chemotactic response of basic FGF.	Heparin	8-15	fibroblast growth factor 2	Homo sapiens	138-147
3209587-5	1988	The factor from NT2/D1 EC cells, bovine FGFb and FGFb produced by the human hepatoma cell line SK-HEP-1 elute from heparin at similar salt concentrations.	Heparin	115-122	fibroblast growth factor 2	Homo sapiens	40-44
3209587-5	1988	The factor from NT2/D1 EC cells, bovine FGFb and FGFb produced by the human hepatoma cell line SK-HEP-1 elute from heparin at similar salt concentrations.	Heparin	115-122	fibroblast growth factor 2	Homo sapiens	49-53
3196724-8	1988	This change in affinity for heparin suggests that the originally dimeric lipoprotein lipase had dissociated into monomers, in analogy to the findings in model experiments.	Heparin	28-35	lipoprotein lipase	Rattus norvegicus	73-91
3191156-7	1988	The release of MEP-like protein from SMC is decreased by heparin, while the remaining two heparin-modulated proteins are increased in the presence of heparin.	Heparin	57-64	cathepsin L	Homo sapiens	15-18
2849981-7	1988	Analysis of the results indicate that plasma fibrinopeptide A (FPA) levels correlate with anti-factor Xa (r = -0.45) and anti-thrombin (substrate) (r = -0.63) levels of UFH, but only with the anti-factor Xa levels (r = -0.41) of CY222.	Heparin	169-172	coagulation factor II, thrombin	Homo sapiens	126-134
3188809-0	1988	Effects of heparin treatments in vivo and in vitro on adrenal angiotensin II receptors and angiotensin II-induced aldosterone production in rats.	Heparin	11-18	angiotensinogen	Rattus norvegicus	62-76
3188809-0	1988	Effects of heparin treatments in vivo and in vitro on adrenal angiotensin II receptors and angiotensin II-induced aldosterone production in rats.	Heparin	11-18	angiotensinogen	Rattus norvegicus	91-105
3188809-1	1988	To evaluate the heparin effects in vivo and in vitro on adrenal angiotensin II receptors and angiotensin II-induced aldosterone production, we examined the angiotensin II binding and the maximum angiotensin II-induced aldosterone production using adrenal glomerulosa cells from rats treated with a heparin preparation containing benzyl alcohol (1500 IU/kg, twice daily for 6 weeks) or cells to which heparin (300 IU/l) was directly added.	Heparin	16-23	angiotensinogen	Rattus norvegicus	64-78
3188809-3	1988	Specific binding of [125I]iodo-angiotensin II was decreased in the cells from heparin-treated rats or in the heparin-treated cells.	Heparin	78-85	angiotensinogen	Rattus norvegicus	31-45
3188809-3	1988	Specific binding of [125I]iodo-angiotensin II was decreased in the cells from heparin-treated rats or in the heparin-treated cells.	Heparin	109-116	angiotensinogen	Rattus norvegicus	31-45
3188809-4	1988	Scatchard analysis showed that the decrease in binding was due to a decrease in both the number and the affinity of angiotensin II receptors in the cells from heparin-treated rats and a decrease in the number, but not the affinity, of the receptors in the heparin-treated cells.	Heparin	159-166	angiotensinogen	Rattus norvegicus	116-130
3188809-5	1988	Heparin also caused a decrease in the maximum angiotensin II-induced production, but not the basal production, of aldosterone in the cells from heparin-treated rats and in the heparin-treated cells.	Heparin	0-7	angiotensinogen	Rattus norvegicus	46-60
3188809-5	1988	Heparin also caused a decrease in the maximum angiotensin II-induced production, but not the basal production, of aldosterone in the cells from heparin-treated rats and in the heparin-treated cells.	Heparin	144-151	angiotensinogen	Rattus norvegicus	46-60
3188809-5	1988	Heparin also caused a decrease in the maximum angiotensin II-induced production, but not the basal production, of aldosterone in the cells from heparin-treated rats and in the heparin-treated cells.	Heparin	176-183	angiotensinogen	Rattus norvegicus	46-60
3188809-6	1988	These data suggest that heparin interacts with adrenal angiotensin II receptors to inhibit the angiotensin II-induced aldosterone production.	Heparin	24-31	angiotensinogen	Rattus norvegicus	55-69
3188809-6	1988	These data suggest that heparin interacts with adrenal angiotensin II receptors to inhibit the angiotensin II-induced aldosterone production.	Heparin	24-31	angiotensinogen	Rattus norvegicus	95-109
3179329-6	1988	In the presence of heparin, they also showed an enhanced release of lipoprotein lipase activity to the medium.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	68-86
3194891-0	1988	Effect of synthetic thrombin inhibitor (MD805) as an alternative drug on heparin induced thrombocytopenia during hemodialysis.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	20-28
2973466-6	1988	Binding of bFGF to frozen sections and to purified proteoglycan could be strongly inhibited by heparin and was displaced by an excess of unlabeled factor and completely suppressed after heparitinase and heparinase treatments.	Heparin	95-102	fibroblast growth factor 2	Homo sapiens	11-15
2851191-0	1988	An approach to assigning in vitro potency to unfractionated and low molecular weight heparins based on the inhibition of prothrombin activation and catalysis of thrombin inhibition.	Heparin	85-93	coagulation factor II, thrombin	Homo sapiens	124-132
2851191-1	1988	Unfractionated and low molecular weight (LMW) heparins with good antithrombotic activity invariably catalyze thrombin inhibition and inhibit the appearance of thrombin activity in contact-activated plasma.	Heparin	46-54	coagulation factor II, thrombin	Homo sapiens	109-117
2851191-1	1988	Unfractionated and low molecular weight (LMW) heparins with good antithrombotic activity invariably catalyze thrombin inhibition and inhibit the appearance of thrombin activity in contact-activated plasma.	Heparin	46-54	coagulation factor II, thrombin	Homo sapiens	159-167
2851195-7	1988	Standard heparin and Kabi 2165, 10,000 anti-Xa U, produced a statistically significant increase in t-PA level at 1 hour after the infusion.	Heparin	9-16	plasminogen activator, tissue type	Homo sapiens	99-103
2458767-1	1988	Intravenous heparin has previously been shown to release the high-heparin-affinity fraction C of extracellular-superoxide dismutase (EC-SOD, EC 1.15.1.1) to plasma in man and other mammals.	Heparin	12-19	superoxide dismutase 3	Homo sapiens	97-131
2458767-1	1988	Intravenous heparin has previously been shown to release the high-heparin-affinity fraction C of extracellular-superoxide dismutase (EC-SOD, EC 1.15.1.1) to plasma in man and other mammals.	Heparin	12-19	superoxide dismutase 3	Homo sapiens	133-139
2458767-1	1988	Intravenous heparin has previously been shown to release the high-heparin-affinity fraction C of extracellular-superoxide dismutase (EC-SOD, EC 1.15.1.1) to plasma in man and other mammals.	Heparin	66-73	superoxide dismutase 3	Homo sapiens	97-131
2458767-1	1988	Intravenous heparin has previously been shown to release the high-heparin-affinity fraction C of extracellular-superoxide dismutase (EC-SOD, EC 1.15.1.1) to plasma in man and other mammals.	Heparin	66-73	superoxide dismutase 3	Homo sapiens	133-139
3070935-0	1988	[The effect of insulin on the initial stages of heparin clearance].	Heparin	48-55	insulin	Homo sapiens	15-22
3070935-1	1988	Use of 35S-heparin enabled to found that both exogenous and endogenous insulin decreased the intensity of initial steps of heparin metabolic clearance maintaining high content of heparin in blood.	Heparin	11-18	insulin	Homo sapiens	71-78
3070935-1	1988	Use of 35S-heparin enabled to found that both exogenous and endogenous insulin decreased the intensity of initial steps of heparin metabolic clearance maintaining high content of heparin in blood.	Heparin	123-130	insulin	Homo sapiens	71-78
3170576-2	1988	In the presence of heparin and endothelial cell growth factor, subcultured human umbilical vein endothelial cells produced u-PA proteins consisting of about 85-90% Mr 54,000 scu-PA and 10-15% two-chain Mr 54,000.	Heparin	19-26	plasminogen activator, urokinase	Homo sapiens	123-127
3170576-4	1988	Typically, about 8-10 micrograms of purified scu-PA protein (antigen/protein ratio = 1) was isolated from 3-liter batches of heparin-containing serum-free conditioned media with a yield of about 41% of the total starting u-PA antigen.	Heparin	125-132	plasminogen activator, urokinase	Homo sapiens	47-51
3218731-0	1988	Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin.	Heparin	33-41	coagulation factor II, thrombin	Homo sapiens	119-127
3047113-4	1988	In the presence of heparin, there was a large increase in secretion of newly synthesized LPL from the cells, although heparin did not stimulate cellular LPL synthetic rate.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	89-92
3178220-6	1988	We interpret these results as evidence that the stronger binding of fibronectin to gelatin-agarose in the presence of heparin is due to heparin itself binding to gelatin, thus allowing fibronectin to bind simultaneously to both immobilized ligands through appropriate domains of the glycoprotein.	Heparin	118-125	fibronectin 1	Homo sapiens	68-79
3178220-6	1988	We interpret these results as evidence that the stronger binding of fibronectin to gelatin-agarose in the presence of heparin is due to heparin itself binding to gelatin, thus allowing fibronectin to bind simultaneously to both immobilized ligands through appropriate domains of the glycoprotein.	Heparin	118-125	fibronectin 1	Homo sapiens	185-196
3178220-6	1988	We interpret these results as evidence that the stronger binding of fibronectin to gelatin-agarose in the presence of heparin is due to heparin itself binding to gelatin, thus allowing fibronectin to bind simultaneously to both immobilized ligands through appropriate domains of the glycoprotein.	Heparin	136-143	fibronectin 1	Homo sapiens	68-79
3178220-6	1988	We interpret these results as evidence that the stronger binding of fibronectin to gelatin-agarose in the presence of heparin is due to heparin itself binding to gelatin, thus allowing fibronectin to bind simultaneously to both immobilized ligands through appropriate domains of the glycoprotein.	Heparin	136-143	fibronectin 1	Homo sapiens	185-196
3196292-6	1988	Porcine, bovine, low-Mr, and high and low antithrombin III (ATIII)-affinity heparins, however, each had distinctly different proportions of these major oligosaccharide components.	Heparin	76-84	serpin family C member 1	Bos taurus	42-58
3178220-1	1988	The enhancement of the binding of plasma fibronectin to collagen or gelatin by heparin was previously thought to be due primarily to interaction of heparin with fibronectin.	Heparin	79-86	fibronectin 1	Homo sapiens	41-52
3178220-1	1988	The enhancement of the binding of plasma fibronectin to collagen or gelatin by heparin was previously thought to be due primarily to interaction of heparin with fibronectin.	Heparin	79-86	fibronectin 1	Homo sapiens	161-172
3178220-1	1988	The enhancement of the binding of plasma fibronectin to collagen or gelatin by heparin was previously thought to be due primarily to interaction of heparin with fibronectin.	Heparin	148-155	fibronectin 1	Homo sapiens	41-52
3178220-1	1988	The enhancement of the binding of plasma fibronectin to collagen or gelatin by heparin was previously thought to be due primarily to interaction of heparin with fibronectin.	Heparin	148-155	fibronectin 1	Homo sapiens	161-172
3178220-2	1988	We observed, however, that the elution of purified human plasma fibronectin from heparin-treated gelatin-agarose required the same high urea concentrations regardless of whether heparin treatment preceded or followed fibronectin adsorption.	Heparin	81-88	fibronectin 1	Homo sapiens	64-75
3196292-6	1988	Porcine, bovine, low-Mr, and high and low antithrombin III (ATIII)-affinity heparins, however, each had distinctly different proportions of these major oligosaccharide components.	Heparin	76-84	serpin family C member 1	Bos taurus	60-65
3196705-0	1988	A calorimetric analysis of human plasma fibronectin: effects of heparin binding on domain structure.	Heparin	64-71	fibronectin 1	Homo sapiens	40-51
3196705-1	1988	Fibronectin domain structure, as influenced by interaction with heparin, calcium, or chondroitin sulfate C, was analyzed by differential scanning calorimetry.	Heparin	64-71	fibronectin 1	Homo sapiens	0-11
3196705-6	1988	Addition of heparin to fibronectin in varying molar ratios, i.e., 10:1 to 30:1, resulted in a larger calorimetric enthalpy for the first type of structural domain (Tm = 59.1 degrees C) of fibronectin.	Heparin	12-19	fibronectin 1	Homo sapiens	23-34
3196705-6	1988	Addition of heparin to fibronectin in varying molar ratios, i.e., 10:1 to 30:1, resulted in a larger calorimetric enthalpy for the first type of structural domain (Tm = 59.1 degrees C) of fibronectin.	Heparin	12-19	fibronectin 1	Homo sapiens	188-199
3196705-7	1988	At higher heparin to fibronectin ratios (40:1 or 75:1), the enthalpy of this domain decreased, while the others remained unchanged.	Heparin	10-17	fibronectin 1	Homo sapiens	21-32
2902851-4	1988	In contrast there was a greater potentiation of the inhibition of thrombin by heparin cofactor II with DPS showing an activity comparable to heparin in this interaction at a concentration two orders of magnitude lower than dermatan sulphate.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	66-74
2852498-7	1988	The inhibition rate of APC by PCI (k: 7.5 x 10(5) M-1 min-1) is significantly increased in the presence of 5 i.u./ml heparin (kH: 2.2 x 10(7) M-1 min-1).	Heparin	117-124	CD59 molecule (CD59 blood group)	Homo sapiens	54-59
2852498-7	1988	The inhibition rate of APC by PCI (k: 7.5 x 10(5) M-1 min-1) is significantly increased in the presence of 5 i.u./ml heparin (kH: 2.2 x 10(7) M-1 min-1).	Heparin	117-124	CD59 molecule (CD59 blood group)	Homo sapiens	146-151
2852498-8	1988	PCI also blocks the amidolytic activities of urokinase plasminogen activator (u-PA), thrombin and factor Xa on their chromogenic substrates in a heparin-dependent manner.	Heparin	145-152	plasminogen activator, urokinase	Homo sapiens	45-76
2852498-8	1988	PCI also blocks the amidolytic activities of urokinase plasminogen activator (u-PA), thrombin and factor Xa on their chromogenic substrates in a heparin-dependent manner.	Heparin	145-152	plasminogen activator, urokinase	Homo sapiens	78-82
2852498-8	1988	PCI also blocks the amidolytic activities of urokinase plasminogen activator (u-PA), thrombin and factor Xa on their chromogenic substrates in a heparin-dependent manner.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	85-93
2462549-5	1988	Such growth factors were extracted from subendothelial ECM synthesized in vitro and from basement membranes of the cornea in vivo, and are structurally and functionally related to bFGF;bFGF binds to ECM and is readily released by incubation with either HS, heparin or low MW heparin fragments as well as by various normal and malignant cells and by heparanase-mediated degradation of ECM HS.	Heparin	257-264	fibroblast growth factor 2	Homo sapiens	180-184
3409328-2	1988	The present studies show that PF4 prepared from normal mouse or human serum by absorption to heparin-agarose and elution between 0.5 and 1.5 M NaCl is also active in this respect.	Heparin	93-100	platelet factor 4	Mus musculus	30-33
2462549-5	1988	Such growth factors were extracted from subendothelial ECM synthesized in vitro and from basement membranes of the cornea in vivo, and are structurally and functionally related to bFGF;bFGF binds to ECM and is readily released by incubation with either HS, heparin or low MW heparin fragments as well as by various normal and malignant cells and by heparanase-mediated degradation of ECM HS.	Heparin	257-264	fibroblast growth factor 2	Homo sapiens	185-189
2462549-5	1988	Such growth factors were extracted from subendothelial ECM synthesized in vitro and from basement membranes of the cornea in vivo, and are structurally and functionally related to bFGF;bFGF binds to ECM and is readily released by incubation with either HS, heparin or low MW heparin fragments as well as by various normal and malignant cells and by heparanase-mediated degradation of ECM HS.	Heparin	275-282	fibroblast growth factor 2	Homo sapiens	180-184
2462549-5	1988	Such growth factors were extracted from subendothelial ECM synthesized in vitro and from basement membranes of the cornea in vivo, and are structurally and functionally related to bFGF;bFGF binds to ECM and is readily released by incubation with either HS, heparin or low MW heparin fragments as well as by various normal and malignant cells and by heparanase-mediated degradation of ECM HS.	Heparin	275-282	fibroblast growth factor 2	Homo sapiens	185-189
3261294-8	1988	Given the association rate constant of alpha 1-antitrypsin for APC of 10 M-1 s-1 and its plasma concentration of approximately 40 microM, it accounts for approximately half of the heparin-independent APC inhibitory activity of plasma.	Heparin	180-187	serpin family A member 1	Homo sapiens	39-58
3417782-3	1988	One of these, peptide F-9 (RYVVLPRPVCFEKGMNYTVR), which is derived from the inner globular domain of the lateral short arm, demonstrated specific binding to heparin.	Heparin	157-164	coagulation factor IX	Homo sapiens	22-25
3417782-5	1988	The binding of [3H]heparin to peptide F-9 was dramatically reduced when heparin but not other glycosaminoglycans other than heparin (dextran sulfate, dermatan sulfate) were used in competition assays.	Heparin	19-26	coagulation factor IX	Homo sapiens	38-41
3417782-5	1988	The binding of [3H]heparin to peptide F-9 was dramatically reduced when heparin but not other glycosaminoglycans other than heparin (dextran sulfate, dermatan sulfate) were used in competition assays.	Heparin	72-79	coagulation factor IX	Homo sapiens	38-41
3417782-5	1988	The binding of [3H]heparin to peptide F-9 was dramatically reduced when heparin but not other glycosaminoglycans other than heparin (dextran sulfate, dermatan sulfate) were used in competition assays.	Heparin	72-79	coagulation factor IX	Homo sapiens	38-41
3417870-1	1988	Extracellular-superoxide dismutase (EC-SOD) is heterogenous in the vasculature with regard to heparin affinity and can be separated into three fractions: A, without affinity; B, with weak affinity; and C, with relatively strong heparin affinity.	Heparin	94-101	superoxide dismutase 3	Homo sapiens	0-34
3417870-1	1988	Extracellular-superoxide dismutase (EC-SOD) is heterogenous in the vasculature with regard to heparin affinity and can be separated into three fractions: A, without affinity; B, with weak affinity; and C, with relatively strong heparin affinity.	Heparin	94-101	superoxide dismutase 3	Homo sapiens	36-42
3417870-1	1988	Extracellular-superoxide dismutase (EC-SOD) is heterogenous in the vasculature with regard to heparin affinity and can be separated into three fractions: A, without affinity; B, with weak affinity; and C, with relatively strong heparin affinity.	Heparin	228-235	superoxide dismutase 3	Homo sapiens	0-34
3417870-1	1988	Extracellular-superoxide dismutase (EC-SOD) is heterogenous in the vasculature with regard to heparin affinity and can be separated into three fractions: A, without affinity; B, with weak affinity; and C, with relatively strong heparin affinity.	Heparin	228-235	superoxide dismutase 3	Homo sapiens	36-42
3211161-10	1988	A synthetic pentasaccharide representing the minimal critical sequence responsible for the binding of heparin to anti-thrombin III exhibited a similar inhibitory capacity on formation of the C3 convertases as another synthetic pentasaccharide that was devoid of anti-Xa activity.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	118-126
3401503-0	1988	Studies on the structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	71-79
2457021-0	1988	Structural changes in the NH2-terminal domain of fibronectin upon interaction with heparin.	Heparin	83-90	fibronectin 1	Homo sapiens	49-60
2457021-2	1988	The effects of heparin and various related polysaccharides on the circular dichroic spectra of fibronectin and its 31-kDa NH2-terminal tryptic fragment were studied.	Heparin	15-22	fibronectin 1	Homo sapiens	95-106
3401503-1	1988	The structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II (HC II) were investigated.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	60-68
3401503-2	1988	A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III).	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	112-120
3391345-7	1988	On the basis of these data, it is concluded that glycosylated antithrombin III with 50% depressed heparin cofactor activity is three times weaker than normal antithrombin III as an inhibitor of thrombin.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	66-74
3191114-10	1988	Patient antithrombin III, isolated by affinity chromatography on heparin-Sepharose, was reacted with purified thrombin.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	12-20
3417768-3	1988	Protein blots using laminin and laminin fragments provided evidence that this LBP interacts with the major heparin-binding domain, E3, of laminin.	Heparin	107-114	calsequestrin 1	Rattus norvegicus	78-81
3215905-1	1988	The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	21-29
3215905-1	1988	The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels.	Heparin	189-196	coagulation factor II, thrombin	Homo sapiens	21-29
3215905-5	1988	While indicating that diffusion of thrombin limited the full utilization of the immobilized heparin, these values for the effectiveness factor could not completely account for the low apparent heparin activity (0.2%) in a thrombin time test of heparin-PVA "beads" (J. Biomed.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	35-43
3215905-0	1988	Permeability of a heparin-polyvinyl alcohol hydrogel to thrombin and antithrombin III.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	56-64
3134521-3	1988	Vascular permeability factor activity falls into a molecular weight range of 41,000 to 56,000 D. Activity is bound to hydroxylapatite, carboxymethyl-Sepharose, phenyl-Sepharose, and heparin-Sepharose, whereas little or no activity was bound to diethylaminoethyl-Sephacel.	Heparin	182-189	vascular endothelial growth factor A	Homo sapiens	0-28
3134521-5	1988	This suggests that VPF is a hydrophobic, positively charged (cationic) polypeptide with a potentially biologically significant affinity for heparin.	Heparin	140-147	vascular endothelial growth factor A	Homo sapiens	19-22
3260474-11	1988	Addition of heparin to 20 U/mL decreased ng/mL C3a generated from 10,872 to 913 and C5a from 200 to 8.	Heparin	12-19	complement C5a receptor 1	Homo sapiens	84-87
3260902-4	1988	The heparin concentrations (10-100 micrograms/ml) and pretreatment times (48-72 h) necessary for suppression of EGF binding correlated with the concentrations and temporal requirements necessary for growth inhibition.	Heparin	4-11	LOC521832	Bos taurus	112-115
2838349-2	1988	Further evidence of the similarity of this growth factor to FGF is provided by the finding that biological activity is lost when the material is bound to a heparin-Sepharose column and restored upon elution with 2.5 M NaCl; the 2.5 M NaCl fraction from Day 12 embryos contains several polypeptides of apparent molecular weights 12,500-17,500.	Heparin	156-163	fibroblast growth factor 10	Gallus gallus	60-63
3260902-1	1988	The effect of heparin on the binding of epidermal growth factor (EGF) to vascular smooth muscle cells (SMC) was examined.	Heparin	14-21	LOC521832	Bos taurus	40-63
3260902-1	1988	The effect of heparin on the binding of epidermal growth factor (EGF) to vascular smooth muscle cells (SMC) was examined.	Heparin	14-21	LOC521832	Bos taurus	65-68
2455567-1	1988	Vitronectin, also known as serum-spreading factor or S-protein, mediates cell adhesion and inhibits formation of the membrane-lytic complex of complement and the rapid inactivation of thrombin by antithrombin III in the presence of heparin.	Heparin	232-239	coagulation factor II, thrombin	Homo sapiens	184-192
3260902-2	1988	Heparin pretreatment of SMC obtained from bovine aortic explant tissue resulted in significant reductions in the amount of EGF bound.	Heparin	0-7	LOC521832	Bos taurus	123-126
3260902-8	1988	Scatchard analysis revealed that heparin induced 50 to 60% reductions in the numbers of high and low affinity EGF receptors without detectable changes in the binding affinity or ratio of high to low receptors.	Heparin	33-40	LOC521832	Bos taurus	110-113
3260902-10	1988	These cultures were inhibited by heparin in a time dependent manner which was partially reversible in the presence of EGF.	Heparin	33-40	LOC521832	Bos taurus	118-121
3260902-11	1988	Subsequent studies revealed that heparin suppressed EGF binding in these cultures by 20 to 40%.	Heparin	33-40	LOC521832	Bos taurus	52-55
3260902-12	1988	In summary, heparin reduces the number of EGF receptors on both explant and enzyme dispersed SMC by a mechanism which closely parallels the antiproliferative effects of this glycosaminoglycan.	Heparin	12-19	LOC521832	Bos taurus	42-45
3370022-3	1988	HepFn appeared more charged than unfractionated heparin, as evidenced by enhanced electrophoretic mobility and ability to effect a cathodic shift in the electrophoretic migration of fibronectin.	Heparin	48-55	fibronectin 1	Homo sapiens	182-193
3412326-1	1988	A human astrocytoma cell line, U87-MG, synthesizes a growth factor which is structurally related to basic fibroblast growth factor (bFGF) by several criteria: 1) it binds to heparin-Sepharose and elutes at 2 M NaCl; 2) it cross-reacts with N-terminal specific anti-bFGF antibodies; 3) it is a potent mitogen for rabbit fetal chondrocytes.	Heparin	174-181	fibroblast growth factor 2	Homo sapiens	100-130
3412326-1	1988	A human astrocytoma cell line, U87-MG, synthesizes a growth factor which is structurally related to basic fibroblast growth factor (bFGF) by several criteria: 1) it binds to heparin-Sepharose and elutes at 2 M NaCl; 2) it cross-reacts with N-terminal specific anti-bFGF antibodies; 3) it is a potent mitogen for rabbit fetal chondrocytes.	Heparin	174-181	fibroblast growth factor 2	Homo sapiens	132-136
3289966-3	1988	Furthermore, on heparin HPLC the activity was eluted at exactly the same retention time as that for authentic pituitary bFGF.	Heparin	16-23	fibroblast growth factor 2	Bos taurus	120-124
3259402-7	1988	Serial determinations of complement components C3a and C5a showed significant increases in parallel with leukopenia during heparin anticoagulation, but the anaphylatoxin concentration changes were dissociated during dialysis with citrate anticoagulation.	Heparin	123-130	complement C5a receptor 1	Homo sapiens	55-58
3043199-4	1988	Inhibition of glycosylation impaired secretion, and the stability of the secreted K-FGF was greatly enhanced by the presence of heparin in the cultured medium.	Heparin	128-135	fibroblast growth factor 4	Mus musculus	82-87
2460964-0	1988	Heparin potentiates endothelial cell growth factor stimulation of plasminogen activator synthesis by diploid human lung fibroblasts.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	20-50
2460964-1	1988	Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin.	Heparin	175-182	fibroblast growth factor 1	Homo sapiens	0-30
2460964-1	1988	Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin.	Heparin	175-182	fibroblast growth factor 1	Homo sapiens	32-36
2460964-1	1988	Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin.	Heparin	175-182	plasminogen activator, tissue type	Homo sapiens	66-70
2460964-1	1988	Endothelial cell growth factor (ECGF) stimulates the synthesis of t-PA and u-PA by confluent, diploid human lung fibroblasts, and this activity is potentiated considerably by heparin.	Heparin	175-182	plasminogen activator, urokinase	Homo sapiens	75-79
2460964-4	1988	The mechanism by which heparin potentiates this effect is thought to reside in its ability to prolong or strengthen the interaction of ECGF with cell surface receptors.	Heparin	23-30	fibroblast growth factor 1	Homo sapiens	135-139
3382684-2	1988	Lipoprotein lipase activity was present in an intracellular and heparin-releasable pool and was also secreted into the culture medium.	Heparin	64-71	lipoprotein lipase	Rattus norvegicus	0-18
3382684-7	1988	Thus, glycosylation of lipoprotein lipase in heart cell cultures is mandatory for enzyme activity and translocation from an intracellular to the heparin-releasable pool and for secretion into the medium.	Heparin	145-152	lipoprotein lipase	Rattus norvegicus	23-41
3181520-2	1988	administration of 1.5 ml of the heparin complexes with plasma proteins prior to the injection of tissue thromboplastin induced a stronger neutralization of formed thrombin in the blood and higher anticoagulating and fibrinolytic activities in albino rats as compared to the injection of tissue thromboplastin alone.	Heparin	32-39	coagulation factor II	Rattus norvegicus	163-171
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	86-94
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	102-110
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	86-94
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	102-110
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	86-94
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	102-110
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	86-94
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	102-110
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	86-94
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	102-110
3129047-2	1988	However, results of studies in vitro suggest that heparin competes with fibrin for binding of tissue-type plasminogen activator (t-PA), augments activation of free plasminogen, decreases fibrin specificity, and impairs thrombolysis.	Heparin	50-57	plasminogen activator, tissue type	Homo sapiens	94-127
3129047-2	1988	However, results of studies in vitro suggest that heparin competes with fibrin for binding of tissue-type plasminogen activator (t-PA), augments activation of free plasminogen, decreases fibrin specificity, and impairs thrombolysis.	Heparin	50-57	plasminogen activator, tissue type	Homo sapiens	129-133
3129047-3	1988	To define the biological implications of these observations, we characterized effects of therapeutic concentrations of heparin on the binding of t-PA to thrombi formed in whole blood, effects of heparin on activation of plasminogen by t-PA in plasma, and effects of heparin on thrombolysis induced by t-PA in a clot lysis system designed to simulate conditions in vivo.	Heparin	119-126	plasminogen activator, tissue type	Homo sapiens	145-149
3382640-1	1988	Incubation of bovine brain derived acidic fibroblast growth factor (aFGF) with bovine or human thrombin, 0.5 NIH unit/mL, for 24 h at 37 degrees C results in cleavage of the mitogen, generating a 14-kilodalton fragment which has significantly reduced affinity for immobilized heparin as compared to aFGF, and is at least 50-fold less potent at stimulating mitogenesis.	Heparin	276-283	coagulation factor II, thrombin	Homo sapiens	95-103
3294068-0	1988	Artificial induction of intravascular lipolysis by lipid-heparin infusion leads to insulin resistance in man.	Heparin	57-64	insulin	Homo sapiens	83-90
3294068-6	1988	These data suggest that the artificial induction of intravascular lipolysis by lipid-heparin infusion leads to a state of insulin resistance in man.	Heparin	85-92	insulin	Homo sapiens	122-129
2835773-7	1988	This was supported by the finding that heparin addition reduced the thrombin concentration in serum-containing medium and stimulated neurite outgrowth from neuroblastoma cells in serum-containing medium.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	68-76
3397495-3	1988	The cells were obtained in the presence of heparin, in order to free the lipoprotein lipase attached to the cell surface.	Heparin	43-50	lipoprotein lipase	Rattus norvegicus	73-91
3360140-0	1988	Antithrombin Glasgow, 393 Arg to His: a P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	4-12
3355842-5	1988	When heparin or gelatin was added in the solution of PRM-fibronectin complex, the fluorescence polarization tended to increase principally by combining heparin or gelatin to fibronectin.	Heparin	5-12	fibronectin 1	Homo sapiens	57-68
3355842-5	1988	When heparin or gelatin was added in the solution of PRM-fibronectin complex, the fluorescence polarization tended to increase principally by combining heparin or gelatin to fibronectin.	Heparin	5-12	fibronectin 1	Homo sapiens	174-185
3355842-5	1988	When heparin or gelatin was added in the solution of PRM-fibronectin complex, the fluorescence polarization tended to increase principally by combining heparin or gelatin to fibronectin.	Heparin	152-159	fibronectin 1	Homo sapiens	57-68
3355842-6	1988	It was found that the rotation of whole or partial fibronectin containing the cell-binding domain through fluorescent lifetime of 100 ns was suppressed by combining of heparin or gelatin to fibronectin.	Heparin	168-175	fibronectin 1	Homo sapiens	51-62
3355842-6	1988	It was found that the rotation of whole or partial fibronectin containing the cell-binding domain through fluorescent lifetime of 100 ns was suppressed by combining of heparin or gelatin to fibronectin.	Heparin	168-175	fibronectin 1	Homo sapiens	190-201
3355842-7	1988	When heparin or gelatin was added in the solution of ANM- or FAM-fibronectin complex, on the contrary, the fluorescence polarization tended to decrease, that is, slightly depolarize through the fluorescent lifetime of 5 or 20 ns, respectively.	Heparin	5-12	fibronectin 1	Homo sapiens	65-76
3355842-8	1988	It was found that the rotation of the cell-binding domain, or of part of the fibronectin molecule containing the domain, was slightly promoted by combining heparin or gelatin to its domain.	Heparin	156-163	fibronectin 1	Homo sapiens	77-88
3350814-5	1988	Tritiated heparin bound to thrombin-resistant (600 kDa) and chymotrypsin-resistant (440 kDa) laminin fragments, both known to lack the terminal globular domain of the long arm.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	27-35
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	136-144
3258907-3	1988	Peak IL-2 concentrations in the supernatant of heparin-containing cultures were two- to fourfold higher than in heparin-free cultures.	Heparin	47-54	interleukin 2	Homo sapiens	5-9
3258907-3	1988	Peak IL-2 concentrations in the supernatant of heparin-containing cultures were two- to fourfold higher than in heparin-free cultures.	Heparin	112-119	interleukin 2	Homo sapiens	5-9
2455066-11	1988	Adding increasing concentrations of heparin progressively inhibited the neurite extension on laminin, whereas similar addition of soluble chondroitin sulfate proteoglycan had no effect.	Heparin	36-43	laminin, beta 2 (laminin S)	Gallus gallus	93-100
3353388-4	1988	The action of aFGF on process outgrowth was markedly potentiated by the addition of heparin (10 micrograms/ml) to the medium, but heparin alone had no effect.	Heparin	84-91	fibroblast growth factor 1	Homo sapiens	14-18
3353388-4	1988	The action of aFGF on process outgrowth was markedly potentiated by the addition of heparin (10 micrograms/ml) to the medium, but heparin alone had no effect.	Heparin	130-137	fibroblast growth factor 1	Homo sapiens	14-18
3353388-5	1988	In the presence of heparin, half-maximal process outgrowth occurred at an aFGF concentration of less than 20 pg/ml (1 pM).	Heparin	19-26	fibroblast growth factor 1	Homo sapiens	74-78
3353388-7	1988	Statistical analysis of the increase in process growth revealed that aFGF with heparin contributed to both neurite initiation and elongation.	Heparin	79-86	fibroblast growth factor 1	Homo sapiens	69-73
3353388-11	1988	The potentiation of this effect by heparin leads us to speculate that the interaction of aFGF with a heparin-like molecule located in the extracellular matrix (such as heparan sulfate proteoglycan) may produce physiological effects in vivo.	Heparin	35-42	fibroblast growth factor 1	Homo sapiens	89-93
3353388-11	1988	The potentiation of this effect by heparin leads us to speculate that the interaction of aFGF with a heparin-like molecule located in the extracellular matrix (such as heparan sulfate proteoglycan) may produce physiological effects in vivo.	Heparin	101-108	fibroblast growth factor 1	Homo sapiens	89-93
3349091-4	1988	When isolated livers from Intralipid-treated rats were perfused with heparin, substantial amounts of lipoprotein lipase were released into the perfusate.	Heparin	69-76	lipoprotein lipase	Rattus norvegicus	101-119
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	161-169
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	161-169
2831901-2	1988	The biological activity and heparin binding ability was retained when the serine was substituted for the cysteine residue at either 70 or 88 of the bFGF protein.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	148-152
2831901-4	1988	The substitution of the residues at these positions, especially at position 88, reduced the heterogeneity recognized as several peaks of bFGF eluted from a heparin affinity column, even after oxidation with hydrogen peroxide, suggesting that the cysteines at these positions are exposed to the surface of the molecule to form disulfide bonds that induce heterologous conformations.	Heparin	156-163	fibroblast growth factor 2	Homo sapiens	137-141
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	136-144
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	161-169
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	136-144
3342932-3	1988	Heparin-induced inhibition of skeletal muscle growth is a consequence of its interaction with a growth factor(s) present in the media used to support myogenesis; heparin-Sepharose column absorbed horse serum can support muscle growth only in the presence of added heparin-binding growth factors like fibroblast growth factor (FGF) or chicken muscle growth factor (CMGF).	Heparin	0-7	fibroblast growth factor 10	Gallus gallus	300-324
3345342-2	1988	FPA was observed in the first samples (30 to 60 seconds) obtained, increased progressively until cessation of bleeding, and was markedly diminished after heparin administration, thus indicating that thrombin formation occurs early in incisional blood.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	199-207
2460305-11	1988	The identification of acidic fibroblast growth factor (FGF)in heparin-sepharose-purified material was accomplished by immunoblot experiments involving antibodies against acidic and basic FGF.	Heparin	62-69	fibroblast growth factor 1	Mus musculus	22-53
2460305-11	1988	The identification of acidic fibroblast growth factor (FGF)in heparin-sepharose-purified material was accomplished by immunoblot experiments involving antibodies against acidic and basic FGF.	Heparin	62-69	fibroblast growth factor 1	Mus musculus	55-58
3350007-1	1988	Four distinct tyrosine protein kinases active on poly(Glu4,Tyr1) and angiotensin II, and operationally termed TPK-I, TPK-IIA, TPK-IIB and TPK-III have been resolved and partially purified from rat spleen particulate fraction by combining DEAE-Sepharose, heparin-Sepharose, phosphocellulose and polylysine-agarose chromatographies.	Heparin	254-261	angiotensinogen	Rattus norvegicus	69-83
3342932-3	1988	Heparin-induced inhibition of skeletal muscle growth is a consequence of its interaction with a growth factor(s) present in the media used to support myogenesis; heparin-Sepharose column absorbed horse serum can support muscle growth only in the presence of added heparin-binding growth factors like fibroblast growth factor (FGF) or chicken muscle growth factor (CMGF).	Heparin	0-7	fibroblast growth factor 10	Gallus gallus	326-329
3342932-3	1988	Heparin-induced inhibition of skeletal muscle growth is a consequence of its interaction with a growth factor(s) present in the media used to support myogenesis; heparin-Sepharose column absorbed horse serum can support muscle growth only in the presence of added heparin-binding growth factors like fibroblast growth factor (FGF) or chicken muscle growth factor (CMGF).	Heparin	162-169	fibroblast growth factor 10	Gallus gallus	300-324
3342932-3	1988	Heparin-induced inhibition of skeletal muscle growth is a consequence of its interaction with a growth factor(s) present in the media used to support myogenesis; heparin-Sepharose column absorbed horse serum can support muscle growth only in the presence of added heparin-binding growth factors like fibroblast growth factor (FGF) or chicken muscle growth factor (CMGF).	Heparin	162-169	fibroblast growth factor 10	Gallus gallus	326-329
3342932-4	1988	Furthermore, heparin prevents the binding of iodinated FGF to the myoblast surface.	Heparin	13-20	fibroblast growth factor 10	Gallus gallus	55-58
3342932-6	1988	Finally, we provide evidence indicating that FGF can combine with endogenously occurring heparin-like components: immobilized FGF binds sodium-[35S]sulfate labeled components secreted in muscle culture conditioned medium, an interaction inhibited by anti-HeSPG antibodies or heparin, but not by other sulfated glycosaminoglycans.	Heparin	89-96	fibroblast growth factor 10	Gallus gallus	126-129
3342932-6	1988	Finally, we provide evidence indicating that FGF can combine with endogenously occurring heparin-like components: immobilized FGF binds sodium-[35S]sulfate labeled components secreted in muscle culture conditioned medium, an interaction inhibited by anti-HeSPG antibodies or heparin, but not by other sulfated glycosaminoglycans.	Heparin	275-282	fibroblast growth factor 10	Gallus gallus	45-48
3342932-6	1988	Finally, we provide evidence indicating that FGF can combine with endogenously occurring heparin-like components: immobilized FGF binds sodium-[35S]sulfate labeled components secreted in muscle culture conditioned medium, an interaction inhibited by anti-HeSPG antibodies or heparin, but not by other sulfated glycosaminoglycans.	Heparin	275-282	fibroblast growth factor 10	Gallus gallus	126-129
2894469-3	1988	Portions of the same blood specimens collected in lithium-heparin anticoagulant yielded higher mean plasma-insulin values of 15.5 and 11.4 microU/ml respectively, with no significant difference between them (p less than 0.05).	Heparin	58-65	insulin	Homo sapiens	107-114
3391999-1	1988	Lysophospholipase released from rat platelets upon activation with thrombin has been purified to near homogeneity by sequential column chromatography on heparin-Sepharose, CM-Sephadex C-50, and TSK gel G2000SW.	Heparin	153-160	asparaginase	Rattus norvegicus	0-17
2829978-7	1988	In particular, protein phosphatase T is endowed with phosphorylase phosphatase activity that is stimulated by protamine, histone H1 and heparin, it is inhibited by spermine, it does not bind to heparin-Sepharose and it readily dephosphorylates the phosphopeptide Arg-Arg-Leu-Ser(P)-Ile-Ser-Thr-Glu-Ser reproducing the phosphorylation site of the alpha-subunit of phosphorylase kinase.	Heparin	136-143	protein phosphatase 5, catalytic subunit	Rattus norvegicus	15-36
2969081-5	1988	In the presence of antithrombin III, thrombin action on adenylate cyclase was blocked by unfractionated and high molecular weight heparin at 0.1 microgram/ml.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	23-31
2969081-8	1988	The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III.	Heparin	23-31	coagulation factor II, thrombin	Homo sapiens	157-165
2969081-8	1988	The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III.	Heparin	237-245	coagulation factor II, thrombin	Homo sapiens	157-165
2828369-0	1988	Characterization and identification of heparin-induced nonopioid-binding sites for beta-endorphin in human plasma.	Heparin	39-46	proopiomelanocortin	Homo sapiens	83-97
2449429-5	1988	A structural protein (apolipoprotein B) epitope characteristic of VLDL+E was expressed during lipolysis prior to ApoE or heparin binding.	Heparin	121-128	apolipoprotein B	Homo sapiens	22-38
2449429-7	1988	The appearance of apoB is modified during lipolysis, with expression of a major heparin-binding site.	Heparin	80-87	apolipoprotein B	Homo sapiens	18-22
2966638-8	1988	The amino-terminal sequence was determined for this fragment, as well as a tryptic 31K fragment which is located to the carboxyl-terminal side of the 33K heparin binding fragment in A chains of fibronectin.	Heparin	154-161	fibronectin 1	Homo sapiens	194-205
2966638-10	1988	Two monoclonal antibodies, termed AHB-1 and AHB-2, recognized epitopes common to heparin binding fragments derived from the carboxyl terminus of both the A and B chains of fibronectin.	Heparin	81-88	fibronectin 1	Homo sapiens	172-183
2966638-11	1988	Monoclonal antibody AHB-2 inhibited melanoma adhesion to the 33K heparin binding fragment of fibronectin in a concentration-dependent manner, whereas monoclonal antibody AHB-1 had no effect on adhesion to this fragment.	Heparin	65-72	fibronectin 1	Homo sapiens	93-104
2966638-14	1988	AHB-2 recognized an epitope common to both the A- and B-chain carboxyl-terminal heparin binding region of fibronectin.	Heparin	80-87	fibronectin 1	Homo sapiens	106-117
2828369-1	1988	We have characterized the specific binding of human beta-endorphin (1-31) to novel binding sites which are formed in human plasma or serum in the presence of heparin.	Heparin	158-165	proopiomelanocortin	Homo sapiens	52-66
3276727-9	1988	IGF-I and a high insulin concentration (70 nM) stimulated only the heparin-releasable (HR) component of LPL activity and immunoreactive mass, and neither IGF-I nor insulin affected LPL specific activity.	Heparin	67-74	insulin like growth factor 1	Homo sapiens	0-5
3276727-9	1988	IGF-I and a high insulin concentration (70 nM) stimulated only the heparin-releasable (HR) component of LPL activity and immunoreactive mass, and neither IGF-I nor insulin affected LPL specific activity.	Heparin	67-74	insulin	Homo sapiens	17-24
2839055-3	1988	A hydrophobic moment analysis of the apolipoprotein E sequence yielded interesting data concerning its receptor-binding and heparin binding characteristics.	Heparin	124-131	apolipoprotein E	Homo sapiens	37-53
3398837-8	1988	These date indicate the presence of a considerable pool of inactive LPL protein in addition to active LPL, that can be released in the presence of heparin.	Heparin	147-154	lipoprotein lipase	Rattus norvegicus	68-71
3398837-8	1988	These date indicate the presence of a considerable pool of inactive LPL protein in addition to active LPL, that can be released in the presence of heparin.	Heparin	147-154	lipoprotein lipase	Rattus norvegicus	102-105
3126814-0	1988	Reductive methylation of lysine residues in acidic fibroblast growth factor: effect on mitogenic activity and heparin affinity.	Heparin	110-117	fibroblast growth factor 1	Mus musculus	44-75
3126814-2	1988	Fractionation of methylated aFGF on immobilized heparin shows that the affinity of the modified mitogen for heparin is also decreased substantially.	Heparin	48-55	fibroblast growth factor 1	Mus musculus	28-32
3126814-2	1988	Fractionation of methylated aFGF on immobilized heparin shows that the affinity of the modified mitogen for heparin is also decreased substantially.	Heparin	108-115	fibroblast growth factor 1	Mus musculus	28-32
3126814-3	1988	The capacity of methylated mitogen of low heparin affinity (LA-aFGF) to stimulate mitogenesis is also reduced, and this correlates with a reduced affinity for its cell surface receptor.	Heparin	42-49	fibroblast growth factor 1	Mus musculus	63-67
3276312-1	1988	This report describes the purification of placental protein 5, PP5, from the human placenta by two affinity chromatography steps, the first with Heparin-Sepharose and the second with Sepharose-linked monoclonal anti-PP5 antibody.	Heparin	145-152	tissue factor pathway inhibitor 2	Homo sapiens	42-61
2461016-3	1988	In general surgery low-dose heparin (LDH) is more effective in preventing isotopic deep-vein thrombosis diagnosed by the radioactive fibrinogen test, but in orthopaedic surgery dextran is superior to heparin.	Heparin	28-35	fibrinogen beta chain	Homo sapiens	133-143
3276111-0	1988	Decrease in frequency of anginal episodes by control of thrombin generation with low-dose heparin: a controlled cross-over randomized study.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	56-64
3276111-7	1988	Present results indicate that the control of thrombin generation obtained by low-dose heparin treatment favorably affects the degree of anginal activity in patients with spontaneous angina.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	45-53
3356754-2	1988	In this report, we describe the purification of MGSA from acid ethanol extracts of Hs294T tumors grown in nude mice using a series of Bio-Gel P30, reverse phase-high performance liquid chromatography and heparin-sepharose steps.	Heparin	204-211	chemokine (C-X-C motif) ligand 1	Mus musculus	48-52
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	46-54
2894851-11	1988	The recombinant HCII formed a complex with 125I-thrombin in a reaction that required the presence of heparin or dermatan sulfate.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	48-56
2840370-0	1988	Significance of thrombin-receptors of thrombocytes for the interaction of heparins and low-molecular-weight heparin in human whole blood clotting.	Heparin	74-82	coagulation factor II, thrombin	Homo sapiens	16-24
2449177-4	1988	Both t-PA and urokinase activities were promoted by heparin and by pentosan polysulphate, but not by chondroitin sulphate or hyaluronic acid.	Heparin	52-59	plasminogen activator, tissue type	Homo sapiens	5-9
2449177-7	1988	In the presence of soluble fibrin (and its mimic, CNBr-digested fibrinogen) the effect of heparin on t-PA was attenuated, although not abolished.	Heparin	90-97	plasminogen activator, tissue type	Homo sapiens	101-105
2449177-15	1988	If these influences of heparin and fibrin also occur in vivo, then, in the presence of heparin, the relative fibrin enhancement of t-PA will be diminished and the likelihood of systemic activation by t-PA is increased.	Heparin	23-30	plasminogen activator, tissue type	Homo sapiens	131-135
2449177-15	1988	If these influences of heparin and fibrin also occur in vivo, then, in the presence of heparin, the relative fibrin enhancement of t-PA will be diminished and the likelihood of systemic activation by t-PA is increased.	Heparin	23-30	plasminogen activator, tissue type	Homo sapiens	200-204
3349123-1	1988	Heparin-like materials, characterized by a defined superficial density of functional groups which activate antithrombin III (AT III), when in contact with blood specifically inhibit thrombin as soon as it appears.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	111-119
3408808-6	1988	Furthermore, the combined ZAS and heparin-induced PMNAGG was partially inhibited by specific antibodies to C5a but not to C3a.	Heparin	34-41	complement C5a receptor 1	Homo sapiens	107-110
2459037-1	1988	The effect of hirudin and heparin on thrombin-induced consumption of antithrombin III, fibrinogen and platelets was studied in a rat model.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	37-45
2465225-8	1988	Although preventive application of subcutaneous heparin did not affect the whole blood coagulability it showed a suppressive impact on the thrombin activity level in examined surgical patients.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	139-147
2840370-0	1988	Significance of thrombin-receptors of thrombocytes for the interaction of heparins and low-molecular-weight heparin in human whole blood clotting.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	16-24
2840370-1	1988	We describe in the present paper the results of the influence of normal and low-molecular-weight heparin on the interaction of human fibrinogen and thrombocytes in human whole blood cotting ex vivo.	Heparin	97-104	fibrinogen beta chain	Homo sapiens	133-143
2840370-3	1988	The data show that low-molecular-weight heparin inhibits plasma thrombin generation in vivo for longer than normal heparin and it affects the fibrinogen platelet binding less.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	64-72
2840370-3	1988	The data show that low-molecular-weight heparin inhibits plasma thrombin generation in vivo for longer than normal heparin and it affects the fibrinogen platelet binding less.	Heparin	40-47	fibrinogen beta chain	Homo sapiens	142-152
2840370-3	1988	The data show that low-molecular-weight heparin inhibits plasma thrombin generation in vivo for longer than normal heparin and it affects the fibrinogen platelet binding less.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	64-72
3680267-6	1987	Fluorescence spectroscopy was used to study the interaction between recombinant ECGF and heparin.	Heparin	89-96	fibroblast growth factor 1	Homo sapiens	80-84
3374475-2	1988	The secretion of LPL occurred in two phases: a rapid release (5-10 min of incubation with heparin) that was independent of protein synthesis followed by a slower rate of release that was inhibited by cycloheximide.	Heparin	90-97	lipoprotein lipase	Rattus norvegicus	17-20
3374475-3	1988	The rapid release of LPL induced by heparin likely occurs from sites that are at or near the cell surface.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	21-24
3374475-5	1988	Heparin-releasable LPL activity measured in short-term incubations represented a large fraction (40-50%) of the initial LPL activity associated with myocytes, but the fall in cellular LPL activity following heparin was less than the amount of LPL activity secreted into the incubation medium.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-22
3374475-5	1988	Heparin-releasable LPL activity measured in short-term incubations represented a large fraction (40-50%) of the initial LPL activity associated with myocytes, but the fall in cellular LPL activity following heparin was less than the amount of LPL activity secreted into the incubation medium.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	120-123
3374475-5	1988	Heparin-releasable LPL activity measured in short-term incubations represented a large fraction (40-50%) of the initial LPL activity associated with myocytes, but the fall in cellular LPL activity following heparin was less than the amount of LPL activity secreted into the incubation medium.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	120-123
3374475-5	1988	Heparin-releasable LPL activity measured in short-term incubations represented a large fraction (40-50%) of the initial LPL activity associated with myocytes, but the fall in cellular LPL activity following heparin was less than the amount of LPL activity secreted into the incubation medium.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	120-123
3238583-3	1988	Fibronectin biological activity was assessed by cold heparin precipitation.	Heparin	53-60	fibronectin 1	Homo sapiens	0-11
3480242-0	1987	The phosphorylation of nucleoplasmin by casein kinase-2 is resistant to heparin inhibition.	Heparin	72-79	nucleophosmin/nucleoplasmin 2 S homeolog	Xenopus laevis	23-36
3480242-5	1987	These findings indicate that the phosphorylation of nucleoplasmin by purified casein kinase-2, while showing typical response to DRB and spermine, exhibits anomalous behavior in its resistance to heparin inhibition.	Heparin	196-203	nucleophosmin/nucleoplasmin 2 S homeolog	Xenopus laevis	52-65
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	80-88
3339946-5	1988	Infusion of heparin to the whole animal before liver exposure decreased by 80% the TEL content of parenchymal cells (a property typical of hepatic lipase) whilst MEL was unchanged.	Heparin	12-19	lipase C, hepatic type	Rattus norvegicus	139-153
3339946-6	1988	These results question the concept that heparin-releasable hepatic lipase acts at the surface of endothelial liver cells and further suggest that TEL and MEL refer to distinct catalytic entities.	Heparin	40-47	lipase C, hepatic type	Rattus norvegicus	59-73
3375141-3	1988	ARn was estimated by a microassay which involves extraction of nuclear pellets with a heparin-containing buffer, exchange labeling of the nuclear extract with 3H-R1881, and quantitation of the receptor with protamine sulphate precipitation.	Heparin	86-93	androgen receptor	Homo sapiens	0-3
3120775-0	1987	Localization of the binding sites of porcine tissue-type plasminogen activator and plasminogen to heparin.	Heparin	98-105	plasminogen activator, tissue type	Homo sapiens	45-78
3120775-1	1987	To localize the binding region of porcine tissue-type plasminogen activator (EC 3.4.21.31) (t-plasminogen activator) to heparin, functionally active A and B chains (molecular mass of each 33 kDa) were separated from the two-chain t-plasminogen activator after mild reduction and alkylation.	Heparin	120-127	plasminogen activator, tissue type	Homo sapiens	42-75
3120775-1	1987	To localize the binding region of porcine tissue-type plasminogen activator (EC 3.4.21.31) (t-plasminogen activator) to heparin, functionally active A and B chains (molecular mass of each 33 kDa) were separated from the two-chain t-plasminogen activator after mild reduction and alkylation.	Heparin	120-127	plasminogen activator, tissue type	Homo sapiens	92-115
3120775-6	1987	The stimulatory effect of fibrin on two-chain t-plasminogen activator-catalyzed Val442-plasminogen activation was clearly diminished by heparin.	Heparin	136-143	plasminogen activator, tissue type	Homo sapiens	46-69
3120775-7	1987	These results suggest that heparin can form a complex with both t-plasminogen activator and plasminogen molecules through their catalytic regions located in each B chain, and that the heparin connection between t-plasminogen activator and plasminogen may improve the plasminogen activation kinetics by making a situation in which t-plasminogen activator is easily approachable to plasminogen.	Heparin	27-34	plasminogen activator, tissue type	Homo sapiens	64-87
3120775-7	1987	These results suggest that heparin can form a complex with both t-plasminogen activator and plasminogen molecules through their catalytic regions located in each B chain, and that the heparin connection between t-plasminogen activator and plasminogen may improve the plasminogen activation kinetics by making a situation in which t-plasminogen activator is easily approachable to plasminogen.	Heparin	27-34	plasminogen activator, tissue type	Homo sapiens	211-234
3120775-7	1987	These results suggest that heparin can form a complex with both t-plasminogen activator and plasminogen molecules through their catalytic regions located in each B chain, and that the heparin connection between t-plasminogen activator and plasminogen may improve the plasminogen activation kinetics by making a situation in which t-plasminogen activator is easily approachable to plasminogen.	Heparin	27-34	plasminogen activator, tissue type	Homo sapiens	211-234
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	42-50
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	122-130
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Heparin	171-178	coagulation factor II, thrombin	Homo sapiens	32-40
3691797-2	1987	The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	18-26
3691797-3	1987	However, this enhancement by heparin dwindled to 110- and 9.6-fold when the modified HC II and the modified thrombin, respectively, were substituted for native proteins.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	108-116
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	79-87
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	172-180
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	172-180
3680267-7	1987	Heparin-binding resulted in a 40% reduction in the intrinsic fluorescence of ECGF, consistent with a heparin-induced conformational change.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	77-81
3680267-7	1987	Heparin-binding resulted in a 40% reduction in the intrinsic fluorescence of ECGF, consistent with a heparin-induced conformational change.	Heparin	101-108	fibroblast growth factor 1	Homo sapiens	77-81
3481660-1	1987	Time response curves of the anti-thrombotic effects, bleeding enhancing effects, effects on APTT, anti-Xa activities, anti-thrombin activities and thrombin generation inhibitory activities of the low molecular weight heparinoid Org 10172 and heparin have been compared in rats.	Heparin	217-224	coagulation factor II	Rattus norvegicus	147-155
3691497-0	1987	Effect of heparin on the interaction between thrombin and hirudin.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	45-53
3691497-1	1987	The effect of heparin on the interaction between thrombin and hirudin has been examined by kinetic methods.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	49-57
3691497-2	1987	Three forms of heparin fractionated on the basis of their affinity for antithrombin III and unfractionated heparin were found to act as noncompetitive inhibitors of the formation of the thrombin-hirudin complex.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	75-83
3681425-4	1987	This VPF is an acid-stable heat-labile macromolecule that is inactivated by trypsin and pepsin and binds immobilized heparin.	Heparin	117-124	vascular endothelial growth factor A	Homo sapiens	5-8
3321056-3	1987	The insulin-stimulated activity was inhibited by low concentrations of heparin and was stimulated by spermine.	Heparin	71-78	insulin	Homo sapiens	4-11
3693392-6	1987	A 31-kD heparin-binding fragment also stimulated NC cell migration, whereas NC cells dispersed to a markedly lower extent on the isolated collagen-binding domain (40 kD), or the latter domain linked to the NH2-terminal part of the FN molecule.	Heparin	8-15	fibronectin 1	Homo sapiens	231-233
3481660-4	1987	The half-life of the anti-thrombin effect after Org 10172 seemed somewhat longer than after heparin administration.	Heparin	92-99	coagulation factor II	Rattus norvegicus	26-34
3481660-5	1987	Thrombin generation inhibition by Org 10172 showed a slightly longer duration than by heparin.	Heparin	86-93	coagulation factor II	Rattus norvegicus	0-8
3427089-0	1987	Further characterization of the interaction of histidine-rich glycoprotein with heparin: evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in heparin binding.	Heparin	80-87	histidine-rich glycoprotein	Oryctolagus cuniculus	47-74
3427089-0	1987	Further characterization of the interaction of histidine-rich glycoprotein with heparin: evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in heparin binding.	Heparin	80-87	histidine-rich glycoprotein	Oryctolagus cuniculus	134-161
3427089-1	1987	Rabbit histidine-rich glycoprotein (HRG, 94 kDa) binds heparin with high affinity (apparent Kd 60-110 nM).	Heparin	55-62	histidine-rich glycoprotein	Oryctolagus cuniculus	7-34
3427089-1	1987	Rabbit histidine-rich glycoprotein (HRG, 94 kDa) binds heparin with high affinity (apparent Kd 60-110 nM).	Heparin	55-62	histidine-rich glycoprotein	Oryctolagus cuniculus	36-39
3427089-2	1987	Eosin Y (1 equiv) bound to HRG was used as a reporter group to monitor associations of HRG with heparins of molecular mass 10, 17.5, and 30 kDa.	Heparin	96-104	histidine-rich glycoprotein	Oryctolagus cuniculus	87-90
3427089-4	1987	Two types of complex form: complexes of 1 heparin:1 HRG and of 1 heparin:2 HRG.	Heparin	42-49	histidine-rich glycoprotein	Oryctolagus cuniculus	52-55
3427089-4	1987	Two types of complex form: complexes of 1 heparin:1 HRG and of 1 heparin:2 HRG.	Heparin	65-72	histidine-rich glycoprotein	Oryctolagus cuniculus	75-78
3427089-5	1987	The 1:2 complex formation requires a minimum heparin chain length since 17.5-kDa but not 10-kDa heparin binds two HRG molecules.	Heparin	45-52	histidine-rich glycoprotein	Oryctolagus cuniculus	114-117
3427089-6	1987	The formation of the 1:2 complexes of the larger heparin fractions is enhanced by divalent copper or zinc (1-10 equiv) bound to HRG.	Heparin	49-56	histidine-rich glycoprotein	Oryctolagus cuniculus	128-131
3427089-7	1987	However, metal is not required for complex formation since all sizes of heparin examined interact tightly with HRG in the presence of ethylenediaminetetraacetic acid.	Heparin	72-79	histidine-rich glycoprotein	Oryctolagus cuniculus	111-114
3427089-8	1987	Between 0.1 and 0.3 M ionic strength, both 1:1 and 1:2 complexes of heparin with HRG are progressively destabilized.	Heparin	68-75	histidine-rich glycoprotein	Oryctolagus cuniculus	81-84
2823050-4	1987	Heparin-sepharose affinity chromatography was used to isolate subfractions of HDL devoid of apolipoprotein E (apo E-free HDL).	Heparin	0-7	apolipoprotein E	Rattus norvegicus	92-108
3689394-0	1987	The effect of heparin on fibronectin and thrombospondin synthesis by human smooth muscle cells.	Heparin	14-21	fibronectin 1	Homo sapiens	25-36
3689394-1	1987	Heparin causes increased synthesis of fibronectin and thrombospondin by human vascular smooth muscle cells as assessed by immunoprecipitation and ELISA techniques.	Heparin	0-7	fibronectin 1	Homo sapiens	38-49
3689394-2	1987	More fibronectin and thrombospondin were immunoprecipitated from the medium of cells treated with 180 micrograms/ml heparin than from that of control cells.	Heparin	116-123	fibronectin 1	Homo sapiens	5-16
3689394-4	1987	By ELISA, heparin was found to cause a 1.7 fold increase in medium fibronectin levels/cell and a 10 fold increase in medium thrombospondin levels/cell.	Heparin	10-17	fibronectin 1	Homo sapiens	67-78
3679862-3	1987	Thrombin time assay was chosen because it is a component of the coagulation screening panel and because it is useful in assessing heparin contamination of specimens.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	0-8
3433256-3	1987	When heparin or gelatin were added to fragments or to fibronectin, the affinities for the alternate ligand increased.	Heparin	5-12	fibronectin 1	Homo sapiens	54-65
3500532-1	1987	A plasma fibronectin-rich component was prepared by heparin-induced 4 degrees C precipitation of fresh or stored (21 days at 4 degrees C), single-donor plasma.	Heparin	52-59	fibronectin 1	Homo sapiens	9-20
2829381-0	1987	Potentiation by heparin fragments of thrombolysis induced with human tissue-type plasminogen activator or human single-chain urokinase-type plasminogen activator.	Heparin	16-23	plasminogen activator, tissue type	Homo sapiens	69-102
3433248-6	1987	In contrast, 1 microgram/ml of UFH completely suppressed thrombin generation in vitro, and 150 micrograms/kg prevented thrombogenesis over a period of 20 minutes" stasis.	Heparin	31-34	coagulation factor II, thrombin	Homo sapiens	57-65
3500532-2	1987	The recovery of plasma fibronectin was 45 percent at a concentration of 0.05 mg heparin per ml (7.5 units/ml) and 75 percent at 0.1 mg per ml (15 units/ml).	Heparin	80-87	fibronectin 1	Homo sapiens	23-34
3433248-8	1987	While DS has antithrombotic activity, it is less effective than UFH in inhibiting thrombin generation, and as an antithrombotic agent.	Heparin	64-67	coagulation factor II, thrombin	Homo sapiens	82-90
3500532-4	1987	Only 20 to 30 percent of the factor VIII activity in fresh plasma was recovered in cryoprecipitate produced after the heparin-induced precipitate containing fibronectin was removed.	Heparin	118-125	fibronectin 1	Homo sapiens	157-168
3500532-7	1987	However, heparin-induced cold precipitation provides an efficient method for preparing plasma fibronectin concentrates from small plasma pools or single units of stored or fresh plasma.	Heparin	9-16	fibronectin 1	Homo sapiens	94-105
3321438-8	1987	Heparin and chemically modified heparins that lack anticoagulant activity inhibited degradation of the ECM-HS by heparanase.	Heparin	0-7	heparanase	Homo sapiens	113-123
3321438-8	1987	Heparin and chemically modified heparins that lack anticoagulant activity inhibited degradation of the ECM-HS by heparanase.	Heparin	32-40	heparanase	Homo sapiens	113-123
3321438-12	1987	Our observation that nonanticoagulant heparins may interfere with heparanase-mediated degradation of ECM-HS suggests a potential therapeutic use for such heparins in neoplastic disorders.	Heparin	38-46	heparanase	Homo sapiens	66-76
3321438-12	1987	Our observation that nonanticoagulant heparins may interfere with heparanase-mediated degradation of ECM-HS suggests a potential therapeutic use for such heparins in neoplastic disorders.	Heparin	154-162	heparanase	Homo sapiens	66-76
2957118-0	1987	Coagulation responses to heparin in the ischemic limb: assessment of thrombin and platelet activation during vascular surgery.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	69-77
3620505-0	1987	Isolation of dermatan sulfate with high heparin cofactor II-mediated thrombin-inhibitory activity from porcine spleen.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	69-77
2445254-3	1987	Heparin manganese isolates had the highest HDL cholesterol concentrations and the lowest HLD2:HDL3 cholesterol ratios, which differed further from the other isolates at higher HDL concentrations.	Heparin	0-7	HDL3	Homo sapiens	94-98
2956994-2	1987	At fixed concentrations of the other molecular components of the complex, the maximal rate of complex formation, measured turbidimetrically, was reached at a concentration of 4 microM heparin and 0.9 microM collagen, while the rate of complex formation was linearly related to concentrations of fibronectin as high as 3 microM.	Heparin	184-191	fibronectin 1	Homo sapiens	295-306
2956994-5	1987	It is suggested that fibronectin binds both heparin and collagen cooperatively to form an insoluble ternary complex of the extracellular matrix.	Heparin	44-51	fibronectin 1	Homo sapiens	21-32
3675305-4	1987	SMC demonstrated a sixfold difference in sensitivity to heparin when grown on different substrates, with the following rank order: EGTA matrix greater than collagens = plastic = fibronectin greater than deoxycholic acid (DOC) matrix.	Heparin	56-63	fibronectin 1	Homo sapiens	178-189
3476950-9	1987	This sequence probably confers the affinity of EC-SOD for heparin and heparan sulfate.	Heparin	58-65	superoxide dismutase 3	Homo sapiens	47-53
2958303-2	1987	The promotion of normal cell growth by aFGF was suppressed by heparan sulfate but enhanced by heparin, while growth promotion by bFGF was suppressed by both GAGs.	Heparin	94-101	fibroblast growth factor 1	Homo sapiens	39-43
2958303-4	1987	The growth of spontaneously transformed cells was enhanced by heparan sulfate or heparin in the presence of 10% FBS or aFGF, while growth promotion in the presence of bFGF was suppressed by both GAGs.	Heparin	81-88	fibroblast growth factor 1	Homo sapiens	119-123
3676266-5	1987	Heparin binds to the LDL surface by interacting with positively charged amino acid residues of apoB-100, forming soluble complexes in the absence of divalent metals and insoluble complexes in their presence.	Heparin	0-7	apolipoprotein B	Homo sapiens	95-103
3676266-6	1987	The purpose of this study was to isolate and characterize the heparin-binding domain(s) of apoB-100.	Heparin	62-69	apolipoprotein B	Homo sapiens	91-99
2442830-3	1987	The sulfated xylans were more effective than heparin or SP-54 in potentiating the AT-III inhibition of amidolysis of H-D-Phe-Pip-Arg-pNa (S-2238) by thrombin (IIa) or amidolysis of Bz-Ile-Glu-Gly-Arg-pNa (S-2222) by Xa.	Heparin	45-52	prolactin induced protein	Homo sapiens	125-128
3611110-3	1987	In the absence of heparin the second-order rate constants of the inactivation of both thrombin and meizothrombin(des F1) formed in the reaction mixture appeared to be identical, k = 3.7 X 10(5) M-1 min-1.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	86-94
3611110-5	1987	In the presence of heparin the decay of the amidolytic activity was biexponential and could be modeled by a four-parameter equation to determine the pseudo first-order rate constants of inhibition as well as the composition of the reaction with respect to the levels of thrombin and meizothrombin(des F1).	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	270-278
3611110-7	1987	Heparin catalyzed the AT III inhibition of thrombin but not meizothrombin(des F1) formed during the prothrombin activation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	43-51
3611110-8	1987	Thrombin, generated by (Xa-Va-phospholipid-Ca2+) was inhibited by AT III/heparin more slowly than purified thrombin, and the saturation kinetics of the inhibition with respect to AT III differed from those found with purified thrombin.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	0-8
3663509-0	1987	Antithrombin III Glasgow: a variant with increased heparin affinity and reduced ability to inactivate thrombin, associated with familial thrombosis.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	4-12
3320422-0	1987	[Inhibition of acid-activation of inactive renin by heparin].	Heparin	52-59	renin	Homo sapiens	43-48
3301850-1	1987	Seven distinct heparin-binding sites have been demonstrated on human apolipoprotein (apo) B-100 by using a combination of digestion with cyanogen bromide or Staphylococcus aureus V-8 protease and heparin-Sepharose affinity chromatography.	Heparin	15-22	apolipoprotein B	Homo sapiens	69-95
3301850-1	1987	Seven distinct heparin-binding sites have been demonstrated on human apolipoprotein (apo) B-100 by using a combination of digestion with cyanogen bromide or Staphylococcus aureus V-8 protease and heparin-Sepharose affinity chromatography.	Heparin	196-203	apolipoprotein B	Homo sapiens	69-95
3301850-6	1987	Second, apoB-100 fragments generated by cyanogen bromide or S. aureus V-8 protease were separated into low- and high-affinity fractions by gradient salt elution of a heparin-Sepharose column.	Heparin	166-173	apolipoprotein B	Homo sapiens	8-16
3301850-9	1987	Based on the analogy with apoE, in which the high-affinity heparin-binding site coincides with the domain of the protein that interacts with apoB,E (low density lipoprotein) receptors, the results of this study indicate that site E and site F, either singly or in combination, might constitute the receptor binding domain of apoB-100.	Heparin	59-66	apolipoprotein E	Homo sapiens	26-30
3301850-9	1987	Based on the analogy with apoE, in which the high-affinity heparin-binding site coincides with the domain of the protein that interacts with apoB,E (low density lipoprotein) receptors, the results of this study indicate that site E and site F, either singly or in combination, might constitute the receptor binding domain of apoB-100.	Heparin	59-66	apolipoprotein B	Homo sapiens	325-333
3311146-7	1987	On the other hand, CKI-3 accepts both ATP and GTP with equal efficiency, and it is heparin sensitive (50% inhibition at 0.3 microgram/mL) like type II casein kinases.	Heparin	83-90	casein kinase YCK3	Saccharomyces cerevisiae S288C	19-24
3619892-4	1987	In brain c-aFGF represented 66% of the total mitogenic activity retained on the heparin-sepharose column and c-bFGF 34% while retina contained 16% of c-aFGF and 84% of c-bFGF; vitreous 78% of c-aFGF and 22% of c-bFGF.	Heparin	80-87	fibroblast growth factor 1	Homo sapiens	11-15
3619892-5	1987	Like human aFGF, Heparin stimulated purified c-aFGF mitogenic activity in the absence of serum but inhibited the activity of the retina acid soluble extract, in the presence of foetal calf serum (FCS).	Heparin	17-24	fibroblast growth factor 1	Homo sapiens	11-15
3619892-5	1987	Like human aFGF, Heparin stimulated purified c-aFGF mitogenic activity in the absence of serum but inhibited the activity of the retina acid soluble extract, in the presence of foetal calf serum (FCS).	Heparin	17-24	fibroblast growth factor 1	Homo sapiens	47-51
2442016-7	1987	In order to get a better understanding of the nature of this binding, we performed the incubation of the frozen sections with iodinated FGFs preincubated with various compounds: (i) heparin which is known to have a strong affinity for aFGF and bFGF partially decreases the labeling, and (ii) chondroitin sulfate B and dextran sulfate at high concentrations were also partially effective.	Heparin	182-189	fibroblast growth factor 1	Mus musculus	235-239
3475277-10	1987	SMC treated with TGF-beta for 4 or 8 h secreted markedly enhanced amounts of an Mr 38,000-D protein doublet whose synthesis is known to be increased by heparin (another inhibitor of SMC growth), suggesting metabolic similarities between heparin- and TGF-beta-mediated SMC growth inhibition.	Heparin	152-159	transforming growth factor beta 1	Homo sapiens	17-25
3678711-8	1987	Therefore we believe to be prudent to delay the infusion of heparin for 12-18 hours after SK administration, when fibrinogen levels are beginning to increase.	Heparin	60-67	fibrinogen beta chain	Homo sapiens	114-124
3475277-10	1987	SMC treated with TGF-beta for 4 or 8 h secreted markedly enhanced amounts of an Mr 38,000-D protein doublet whose synthesis is known to be increased by heparin (another inhibitor of SMC growth), suggesting metabolic similarities between heparin- and TGF-beta-mediated SMC growth inhibition.	Heparin	152-159	transforming growth factor beta 1	Homo sapiens	250-258
3475277-10	1987	SMC treated with TGF-beta for 4 or 8 h secreted markedly enhanced amounts of an Mr 38,000-D protein doublet whose synthesis is known to be increased by heparin (another inhibitor of SMC growth), suggesting metabolic similarities between heparin- and TGF-beta-mediated SMC growth inhibition.	Heparin	237-244	transforming growth factor beta 1	Homo sapiens	17-25
3499516-8	1987	Heparin also inhibited the IL-2 dependent growth of long-time cultured T cell lines.	Heparin	0-7	interleukin 2	Homo sapiens	27-31
2440029-0	1987	Matrix-driven translocation: dependence on interaction of amino-terminal domain of fibronectin with heparin-like surface components of cells or particles.	Heparin	100-107	fibronectin 1	Homo sapiens	83-94
3625037-5	1987	Heparin inhibited the apoE stimulation in both hepatocytes and hepatoma monolayers.	Heparin	0-7	apolipoprotein E	Rattus norvegicus	22-26
3625037-6	1987	Heparin wash of hepatocytes or hepatoma cells incubated with apoE-[14C]triolein emulsions at 4 degrees C resulted in a considerable loss in radiolabeled cell lipid.	Heparin	0-7	apolipoprotein E	Rattus norvegicus	61-65
2440029-5	1987	Competition experiments using heparin, heparan sulfate, and other sulfated polysaccharides show that this fibronectin site interacts with heparin-like cell or particle surface components in promoting matrix-driven translocation.	Heparin	30-37	fibronectin 1	Homo sapiens	106-117
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	40-48
3584126-14	1987	The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	4-12
3584126-2	1987	Does cleavage by thrombin induce structural changes in the heparin-binding region of antithrombin?	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	17-25
3584126-3	1987	Heparin has been shown to exhibit lower affinity for the antithrombin-thrombin complex than for antithrombin alone (Carlstrom, A.-S., Lieden, K., and Bjork, I.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	61-69
3584126-14	1987	The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	186-194
3584245-7	1987	Fibronectin peptides containing either the heparin-binding domain near the COOH-terminal end or the heparin-binding NH2 terminus were the only fragments interacting with DS-PG and core protein.	Heparin	43-50	fibronectin 1	Homo sapiens	0-11
3584126-14	1987	The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	4-12
3584126-14	1987	The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	186-194
3584127-2	1987	Is the heparin-induced conformational change in antithrombin required for rapid inactivation of thrombin?	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	52-60
3584127-3	1987	The role of antithrombin conformation in heparin-catalyzed inhibition of thrombin was investigated using antithrombins modified with the tryptophan reagent dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNB).	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	16-24
3584127-9	1987	The kinetic analysis indicated that each of these HNB-antithrombin derivatives, which undergo the heparin-induced changes to varying extents, can react with thrombin at the same maximal rate.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	58-66
3584127-10	1987	Thus, this series of chemically modified antithrombin species demonstrated that the conformational change which is induced in antithrombin by heparin does not render the protein intrinsically more reactive toward thrombin.	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	45-53
3584128-0	1987	Histidine-rich glycoprotein modulation of the anticoagulant activity of heparin.	Heparin	72-79	histidine-rich glycoprotein	Oryctolagus cuniculus	0-27
3584128-3	1987	The strong interaction between heparin and HRG was demonstrated to be competitive with the binding of both antithrombin and thrombin to the heparin chain.	Heparin	31-38	histidine-rich glycoprotein	Oryctolagus cuniculus	43-46
3584128-3	1987	The strong interaction between heparin and HRG was demonstrated to be competitive with the binding of both antithrombin and thrombin to the heparin chain.	Heparin	140-147	histidine-rich glycoprotein	Oryctolagus cuniculus	43-46
3584128-4	1987	HRG was further tested as a modulator of the anticoagulant activity of heparin by comparing rates of the heparin-catalyzed reaction between antithrombin and thrombin in the presence and absence of added HRG.	Heparin	71-78	histidine-rich glycoprotein	Oryctolagus cuniculus	0-3
3584128-4	1987	HRG was further tested as a modulator of the anticoagulant activity of heparin by comparing rates of the heparin-catalyzed reaction between antithrombin and thrombin in the presence and absence of added HRG.	Heparin	71-78	histidine-rich glycoprotein	Oryctolagus cuniculus	203-206
3584128-4	1987	HRG was further tested as a modulator of the anticoagulant activity of heparin by comparing rates of the heparin-catalyzed reaction between antithrombin and thrombin in the presence and absence of added HRG.	Heparin	105-112	histidine-rich glycoprotein	Oryctolagus cuniculus	0-3
3584128-5	1987	The heparin-antithrombin-thrombin reaction was modeled using the formalism of a two-substrate enzyme-catalyzed reaction with heparin as the enzyme and HRG analyzed as an enzyme inhibitor.	Heparin	4-11	histidine-rich glycoprotein	Oryctolagus cuniculus	151-154
3584128-7	1987	Thus, both the kinetic and heparin-binding data indicate that the mechanism by which HRG modulates heparin anticoagulant activity involves competition for heparin with both the inhibitor and the protease.	Heparin	27-34	histidine-rich glycoprotein	Oryctolagus cuniculus	85-88
3584128-7	1987	Thus, both the kinetic and heparin-binding data indicate that the mechanism by which HRG modulates heparin anticoagulant activity involves competition for heparin with both the inhibitor and the protease.	Heparin	99-106	histidine-rich glycoprotein	Oryctolagus cuniculus	85-88
3584128-8	1987	Inhibition by HRG of the heparin-catalyzed reaction was found to be highly dependent on pH, with a sharp increase in inhibition from about 15% to greater than 90% observed as pH was lowered from 7.4 to 7.0.	Heparin	25-32	histidine-rich glycoprotein	Oryctolagus cuniculus	14-17
3584128-9	1987	Since little change in the rate of the heparin-catalyzed inhibition of thrombin by antithrombin occurs in this pH region, the dramatic change in HRG inhibition seen upon pH titration may reflect increasing ionic interaction between heparin and HRG due to the protonation of histidine residues which occurs in this pH region.	Heparin	232-239	histidine-rich glycoprotein	Oryctolagus cuniculus	145-148
2822055-6	1987	Also, heparin was found to inhibit thrombin induced platelet aggregation.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	35-43
2822055-7	1987	In washed platelets, the inhibitory effect of thrombin on PGE1 induced cAMP accumulation was counteracted by heparin.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	46-54
2953683-0	1987	Heparin interferes with the biological effectiveness of atriopeptin.	Heparin	0-7	natriuretic peptide A	Homo sapiens	56-67
2953683-1	1987	The chromatographic mobility of atriopeptin-28 or of the prohormone is markedly altered by preincubation of the peptides with heparin before separation on reverse-phase high performance liquid chromatography.	Heparin	126-133	natriuretic peptide A	Homo sapiens	32-43
2953683-4	1987	The influence of heparin on the biological activity of the atriopeptin-28 in anesthetized rats was also investigated.	Heparin	17-24	natriuretic peptide A	Homo sapiens	59-70
2953683-5	1987	Infusion of heparin (30 U/min) significantly reduced the dose-dependent fall of blood pressure produced by atriopeptin-28, but did not interfere with the hypotensive effect of nitroglycerin.	Heparin	12-19	natriuretic peptide A	Homo sapiens	107-118
2953683-6	1987	Similarly, infusion of heparin in volume-expanded rats markedly decreased the diuresis produced by atriopeptin-28 without altering the urine volume excreted in response to furosemide.	Heparin	23-30	natriuretic peptide A	Homo sapiens	99-110
2953683-7	1987	These data suggest that the highly charged molecule heparin can modify the physical and biological properties of atriopeptins, perhaps by binding to the numerous arginine residues (i.e., 5 arginine residues in atriopeptin-28) in the atriopeptin molecules.	Heparin	52-59	natriuretic peptide A	Homo sapiens	113-124
2953683-7	1987	These data suggest that the highly charged molecule heparin can modify the physical and biological properties of atriopeptins, perhaps by binding to the numerous arginine residues (i.e., 5 arginine residues in atriopeptin-28) in the atriopeptin molecules.	Heparin	52-59	natriuretic peptide A	Homo sapiens	210-221
3584245-7	1987	Fibronectin peptides containing either the heparin-binding domain near the COOH-terminal end or the heparin-binding NH2 terminus were the only fragments interacting with DS-PG and core protein.	Heparin	100-107	fibronectin 1	Homo sapiens	0-11
3032981-12	1987	Heparin, which is known to block lipocortin I inhibition of phospholipase A2, also blocked binding of lipocortin I to E. coli membranes.	Heparin	0-7	phospholipase A2 group IB	Homo sapiens	60-76
3627099-4	1987	Heparin therapy was instituted for the prevention of thromboembolism, when prothrombin activity recovered to 50% normal by thrombotest, in 5 of 7 cases.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	75-86
3627099-7	1987	Heparin therapy was stopped when prothrombin activity reached a therapeutic level with sodium warfarin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	33-44
3035321-5	1987	However, the heparin-elutable LPL activity did not change during this treatment in fasted nor fed animals.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	30-33
3035321-6	1987	Pharmacologic levels of insulin in the perfusion medium caused an increase in heparin-releasable LPL activity as a percentage of total fat pad LPL activity (15% v 48%).	Heparin	78-85	lipoprotein lipase	Rattus norvegicus	97-100
3035321-6	1987	Pharmacologic levels of insulin in the perfusion medium caused an increase in heparin-releasable LPL activity as a percentage of total fat pad LPL activity (15% v 48%).	Heparin	78-85	lipoprotein lipase	Rattus norvegicus	143-146
3035321-12	1987	The discrepancy between the LPL activity extractable from an acetone ether powder and the heparin releasable LPL activity suggests impairment of the transport of LPL from the adipocyte to the heparin releasable pool at the endothelium.	Heparin	90-97	lipoprotein lipase	Rattus norvegicus	109-112
3035321-12	1987	The discrepancy between the LPL activity extractable from an acetone ether powder and the heparin releasable LPL activity suggests impairment of the transport of LPL from the adipocyte to the heparin releasable pool at the endothelium.	Heparin	90-97	lipoprotein lipase	Rattus norvegicus	109-112
3035321-12	1987	The discrepancy between the LPL activity extractable from an acetone ether powder and the heparin releasable LPL activity suggests impairment of the transport of LPL from the adipocyte to the heparin releasable pool at the endothelium.	Heparin	192-199	lipoprotein lipase	Rattus norvegicus	109-112
3035321-12	1987	The discrepancy between the LPL activity extractable from an acetone ether powder and the heparin releasable LPL activity suggests impairment of the transport of LPL from the adipocyte to the heparin releasable pool at the endothelium.	Heparin	192-199	lipoprotein lipase	Rattus norvegicus	109-112
3038185-3	1987	Heparin-like structures of the vessel wall have been proposed as another regulatory mechanism catalyzing the inhibition of thrombin by antithrombin III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	123-131
3032267-5	1987	Using heparin Sepharose chromatography and stepwise elution, a lipoprotein lipase enriched fraction was recovered with 2 M NaCl.	Heparin	6-13	lipoprotein lipase	Rattus norvegicus	63-81
3032267-9	1987	The effect of Hepes-conditioned medium on lipoprotein lipase resembled to some extent that of the addition of heparin.	Heparin	110-117	lipoprotein lipase	Rattus norvegicus	42-60
3038185-6	1987	The addition of heparin (0.5 unit/mL) to the reaction mixture interfered neither with the binding of thrombin to TM nor with the activation of protein C. However, the polycations protamine (1 unit/mL) as well as polybrene (0.1 mg/mL) affected the thrombin-TM interaction.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	247-255
2443128-0	1987	The inhibition of thrombin-dependent positive-feedback reactions is critical to the expression of the anticoagulant effect of heparin.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	18-26
3032574-5	1987	Exposure to PTH and, to a lesser extent, 1,25-dihydroxyvitamin D3, prostaglandin E2, retinoic acid, and epidermal growth factor stimulated the release of collagenase, an effect not seen with interleukin-1 or heparin.	Heparin	208-215	parathyroid hormone	Rattus norvegicus	12-15
2443128-13	1987	These results suggest that the anticoagulant effects of heparin and pentosan polysulphate are mediated primarily by their ability to inhibit the thrombin-dependent activation of Factor V, thereby inhibiting the formation of prothrombinase complex, the physiological activator of prothrombin.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	145-153
3495208-0	1987	C5a and thromboxane generation associated with pulmonary vaso- and broncho-constriction during protamine reversal of heparin.	Heparin	117-124	complement C5a receptor 1	Homo sapiens	0-3
3495208-8	1987	The authors" data indicate that the generation of high plasma levels of C5a anaphylatoxins and thromboxane is associated with pulmonary vaso- and broncho-constriction induced by protamine reversal of heparin in humans.	Heparin	200-207	complement C5a receptor 1	Homo sapiens	72-75
3571333-5	1987	The binding of TSP to type V collagen was inhibited by heparin and fucoidin, both high-affinity ligands of TSP"s heparin-binding domain.	Heparin	55-62	thrombospondin 1	Homo sapiens	15-18
3571333-5	1987	The binding of TSP to type V collagen was inhibited by heparin and fucoidin, both high-affinity ligands of TSP"s heparin-binding domain.	Heparin	55-62	thrombospondin 1	Homo sapiens	107-110
3571333-5	1987	The binding of TSP to type V collagen was inhibited by heparin and fucoidin, both high-affinity ligands of TSP"s heparin-binding domain.	Heparin	113-120	thrombospondin 1	Homo sapiens	15-18
3571333-5	1987	The binding of TSP to type V collagen was inhibited by heparin and fucoidin, both high-affinity ligands of TSP"s heparin-binding domain.	Heparin	113-120	thrombospondin 1	Homo sapiens	107-110
3603437-0	1987	Comparison of the molecular mass dependency of heparin stimulation of heparin cofactor II:thrombin interaction to antithrombin III:thrombin interaction.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	90-98
3603437-1	1987	The influence of increasing concentrations of heparin of different molecular mass (Mr) has been compared in potentiation of the rate of heparin cofactor II:thrombin interaction and of antithrombin III:thrombin interaction.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	156-164
3603437-3	1987	Unfractionated heparin and fractions of 16.5 KDa or less showed a peak acceleration of the rate of interaction of thrombin with both inhibitors at 0.3 X 10(-6) M heparin although the observed maximum rate at this peak decreased with fall in Mr. For both inhibitors two high Mr fractions showed peak stimulation at a lower heparin concentration (0.3 X 10(-7) M) and approximately two-fold greater increase in rate than that observed with unfractionated heparin.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	114-122
3603437-3	1987	Unfractionated heparin and fractions of 16.5 KDa or less showed a peak acceleration of the rate of interaction of thrombin with both inhibitors at 0.3 X 10(-6) M heparin although the observed maximum rate at this peak decreased with fall in Mr. For both inhibitors two high Mr fractions showed peak stimulation at a lower heparin concentration (0.3 X 10(-7) M) and approximately two-fold greater increase in rate than that observed with unfractionated heparin.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	114-122
3603437-3	1987	Unfractionated heparin and fractions of 16.5 KDa or less showed a peak acceleration of the rate of interaction of thrombin with both inhibitors at 0.3 X 10(-6) M heparin although the observed maximum rate at this peak decreased with fall in Mr. For both inhibitors two high Mr fractions showed peak stimulation at a lower heparin concentration (0.3 X 10(-7) M) and approximately two-fold greater increase in rate than that observed with unfractionated heparin.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	114-122
3603437-3	1987	Unfractionated heparin and fractions of 16.5 KDa or less showed a peak acceleration of the rate of interaction of thrombin with both inhibitors at 0.3 X 10(-6) M heparin although the observed maximum rate at this peak decreased with fall in Mr. For both inhibitors two high Mr fractions showed peak stimulation at a lower heparin concentration (0.3 X 10(-7) M) and approximately two-fold greater increase in rate than that observed with unfractionated heparin.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	114-122
3603437-5	1987	It is proposed that differences in the profiles of stimulation by high Mr fractions to those of lower Mr are related to higher binding affinities for the inhibitor permitting maximal binding of heparin before the descending part of the slope due to saturation of thrombin (according to the template hypothesis).	Heparin	194-201	coagulation factor II, thrombin	Homo sapiens	263-271
2443128-1	1987	Heparin catalyses the inhibition of two key enzymes of blood coagulation, namely Factor Xa and thrombin, by enhancing the antiproteinase activities of plasma antithrombin III and heparin cofactor II.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	95-103
2443128-6	1987	D-Phe-Pro-Arg-CH2Cl is rapid enough an inhibitor of thrombin so that when added to plasma no complexes of thrombin with its inhibitors are formed, whether or not the plasma also contains heparin.	Heparin	187-194	coagulation factor II, thrombin	Homo sapiens	52-60
2443128-7	1987	Heparin (0.66 microgram/ml) and pentosan polysulphate (6.6 micrograms/ml) completely inhibited the intrinsic-pathway activation of 125I-prothrombin to 125I-prothrombin fragment 1 + 2 and 125I-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	139-147
2443128-12	1987	Reversal of the inhibitory effects of heparin and pentosan polysulphate was associated with the accelerated formation of 125I-thrombin-antithrombin III and 125I-thrombin-heparin cofactor complexes respectively.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	126-134
2443128-12	1987	Reversal of the inhibitory effects of heparin and pentosan polysulphate was associated with the accelerated formation of 125I-thrombin-antithrombin III and 125I-thrombin-heparin cofactor complexes respectively.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	139-147
3818643-7	1987	However, TFIIB and TFIIE were implicated, along with the other factors and RNA polymerase II, in the subsequent formation of a highly stable preinitiation complex, which was inferred from its ability to initiate (with added nucleotides) in the presence of heparin concentrations which blocked unbound factors.	Heparin	256-263	general transcription factor IIB	Homo sapiens	9-14
3603409-5	1987	Kinetics experiments showed a normal inhibition of thrombin and Xa in absence of heparin, but abnormal in presence of heparin.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	51-59
3606566-1	1987	S protein, a plasma glycoprotein with Mr 78,000, has been shown to interfere with the heparin-catalysed inhibition of thrombin by antithrombin III.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	118-126
2441082-0	1987	Heparin requirement in tissue-type plasminogen activator-induced experimental coronary thrombolysis: comparison with urokinase-induced coronary thrombolysis.	Heparin	0-7	tissue-type plasminogen activator	Canis lupus familiaris	23-56
2441082-1	1987	The requirement of heparin in experimental coronary thrombolysis induced by tissue-type plasminogen activator (t-PA) was studied in closed-chest dogs with one hour old coronary thrombi and compared with that in urokinase (UK)-induced coronary thrombolysis.	Heparin	19-26	tissue-type plasminogen activator	Canis lupus familiaris	76-109
2441082-1	1987	The requirement of heparin in experimental coronary thrombolysis induced by tissue-type plasminogen activator (t-PA) was studied in closed-chest dogs with one hour old coronary thrombi and compared with that in urokinase (UK)-induced coronary thrombolysis.	Heparin	19-26	tissue-type plasminogen activator	Canis lupus familiaris	111-115
3590108-7	1987	Furthermore, insoluble sulfonated polystyrenes grafted with different amino acid were shown to possess an heparin-like behaviour and catalyse the generation of thrombin-AT III complex.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	160-168
3567176-0	1987	Antithrombin III and its interaction with heparin.	Heparin	42-49	serpin family C member 1	Bos taurus	0-16
3567176-12	1987	For human antithrombin III, it was shown that heparin fragments 8, 10, and 16 sugar residues in length result in almost identical perturbations to the protein.	Heparin	46-53	serpin family C member 1	Bos taurus	10-26
2436647-6	1987	Heparin alone did not significantly alter the responses to ADP but consistently reduced those to thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	97-105
3549363-7	1987	Thus, interleukin 3-dependent mouse BMMC can be induced to undergo phenotypic changes in staining characteristics, histamine content, glycosaminoglycan structure, and metabolism of arachidonic acid to resemble heparin-containing CTMC.	Heparin	210-217	interleukin 3	Mus musculus	6-19
3032990-7	1987	To test whether the low affinity binding might play a role in the basic FGF stimulation of plasminogen activator (PA) production by BCE cells, heparin was added to BCE cultures at concentrations which totally blocked binding of 125I-basic FGF to the low affinity sites.	Heparin	143-150	fibroblast growth factor 2	Bos taurus	239-242
3029109-3	1987	TFIIB and TFIIE were also required, in addition to TFIIA, TFIID, RNA polymerase II, and the adenovirus 2 major late promoter, for the formation of a (preinitiation) complex that could initiate transcription (upon addition of nucleoside triphosphates) in the presence of heparin concentrations which inhibited the action of unbound factors.	Heparin	270-277	general transcription factor IIB	Homo sapiens	0-5
3825856-11	1987	Bolus heparin administration (100 IU/kg) during the active phase of angina sharply but incompletely lowered FPA plasma levels, indicating thrombin formation both intravascularly and extravascularly.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	138-146
3827418-1	1987	The effect of heparin on prothrombin times.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	25-36
3827418-2	1987	Sharp decreases in the prothrombin time after discontinuing heparin have been reported in patients undergoing oral anticoagulant therapy.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	23-34
3827418-5	1987	Prothrombin times on the heparin infusion and four to six hours after it was discontinued were compared.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	0-11
3827418-7	1987	Since the change in prothrombin time is unpredictable, a repeated prothrombin time is recommended after stopping heparin therapy prior to discharging a patient.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	66-77
2437972-2	1987	Sephadex derivatives bearing carboxymethyl, sulphonated benzylamine and amino acid groups exhibit heparin-like behaviour as demonstrated by the kinetic study of the thrombin inactivation in the presence of antithrombin III.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	165-173
2437972-4	1987	Hence, in the heparin-like mechanism, the diffusion rate of thrombin inside the beads of hydrogels was not the limiting step.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	60-68
3590093-1	1987	The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III).	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	58-66
3597343-1	1987	It was found that phospholipase A2 and lysophospholipase, both of which were released from thrombin-stimulated rat platelets, had high affinity to insolubilized heparin.	Heparin	161-168	coagulation factor II	Rattus norvegicus	91-99
3597343-6	1987	Lysophospholipase, which was also released from rat platelets, was separated from phospholipase A2 by chromatography on heparin-Sepharose.	Heparin	120-127	asparaginase	Rattus norvegicus	0-17
3101765-6	1987	Heparin accelerated proteolysis of alpha-thrombin by elastase.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	41-49
3590093-4	1987	However, after isolation of the reaction products, both thrombin and prothrombin fragment 1.2 exhibited heparin neutralizing properties in the factor Xa inactivation reaction.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	56-64
3109060-3	1987	Compared to the control group heparin was found to give a significant rise in t-PA antigen before (24.0 vs. 11.2 ng/ml, p = 0.02), and especially after venous stasis (104.8 vs. 47.3 ng/ml, P = 0.007).	Heparin	30-37	plasminogen activator, tissue type	Homo sapiens	78-82
3109060-4	1987	t-PA activity was also significantly more increased after venous stasis in the heparin group than among the controls (4.2 vs. 1.4 U/ml, p = 0.04).	Heparin	79-86	plasminogen activator, tissue type	Homo sapiens	0-4
3590084-3	1987	Rapid inactivation of cell-bound thrombin by antithrombin III (ATIII) accelerated by heparin-like structures represents another anticoagulant mechanism.	Heparin	85-92	serpin family C member 1	Bos taurus	45-61
3109060-7	1987	The present results point to a heparin-induced increase of t-PA synthesis in the endothelium, also giving rise to an increased level of circulating t-PA as measured immunologically.	Heparin	31-38	plasminogen activator, tissue type	Homo sapiens	59-63
3109060-7	1987	The present results point to a heparin-induced increase of t-PA synthesis in the endothelium, also giving rise to an increased level of circulating t-PA as measured immunologically.	Heparin	31-38	plasminogen activator, tissue type	Homo sapiens	148-152
3567152-9	1987	The molecular association of control fibronectin or its glycated counterpart with [3H]heparin was also determined.	Heparin	86-93	fibronectin 1	Homo sapiens	37-48
3593230-2	1987	The primary structure of a 38 kDa heparin-binding domain from human plasma fibronectin has been determined.	Heparin	34-41	fibronectin 1	Homo sapiens	75-86
3593249-3	1987	Intravenous injection of heparin leads to a prompt increase in plasma extracellular-superoxide-dismutase (EC-SOD) activity.	Heparin	25-32	superoxide dismutase 3	Homo sapiens	70-104
3593249-3	1987	Intravenous injection of heparin leads to a prompt increase in plasma extracellular-superoxide-dismutase (EC-SOD) activity.	Heparin	25-32	superoxide dismutase 3	Homo sapiens	106-112
3593249-6	1987	of heparin per kg body weight, showing that the releasing potency of heparin is lower for EC-SOD than for previously investigated heparin-released factors.	Heparin	69-76	superoxide dismutase 3	Homo sapiens	90-96
3593249-7	1987	Chromatography of human plasma on heparin-Sepharose shows nearly equal amounts of EC-SOD fractions A, B and C. Heparin induces specifically the release of fraction C. The findings point to the existence of an equilibrium of EC-SOD fraction C between the plasma phase and endothelial-cell surfaces.	Heparin	111-118	superoxide dismutase 3	Homo sapiens	224-230
3100536-3	1987	We have now established that the fragment extends to residue Lys-728 and demonstrate here that a high affinity heparin-binding domain of vWF also lies within this region and in close proximity to that for GPIb.	Heparin	111-118	von Willebrand factor	Homo sapiens	137-140
3100536-4	1987	We have used an assay employing heparin coupled to Sepharose CL-6B to show that 125I-vWF binds to heparin in a time-dependent, saturable, and reversible manner.	Heparin	32-39	von Willebrand factor	Homo sapiens	85-88
3100536-4	1987	We have used an assay employing heparin coupled to Sepharose CL-6B to show that 125I-vWF binds to heparin in a time-dependent, saturable, and reversible manner.	Heparin	98-105	von Willebrand factor	Homo sapiens	85-88
3100536-9	1987	Twelve monoclonal antibodies to the 52/48-kDa fragment were evaluated for their ability to block binding of 125I-vWF to heparin.	Heparin	120-127	von Willebrand factor	Homo sapiens	113-116
3542643-0	1987	Effects of heparin on insulin binding and biological activity.	Heparin	11-18	insulin	Homo sapiens	22-29
3542643-1	1987	The effect of heparin, a polyanionic glycosaminoglycan known to alter the function of many proteins, on insulin binding and bioactivity was studied.	Heparin	14-21	insulin	Homo sapiens	104-111
3542643-8	1987	Heparin also inhibited insulin binding in Epstein-Barr (EB) virus-transformed lymphocytes but had no effect on insulin binding to isolated adipocytes, human erythrocytes, or intact hepatoma cells.	Heparin	0-7	insulin	Homo sapiens	23-30
3542643-9	1987	When isolated adipocytes were incubated with heparin, there was a dose-dependent inhibition of insulin-stimulated glucose oxidation and, to a lesser extent, of basal glucose oxidation.	Heparin	45-52	insulin	Homo sapiens	95-102
3542643-10	1987	Although heparin has no effect on insulin binding to intact hepatoma cells, heparin inhibited both insulin binding and insulin-stimulated autophosphorylation in receptors solubilized from these cells.	Heparin	76-83	insulin	Homo sapiens	99-106
3542643-10	1987	Although heparin has no effect on insulin binding to intact hepatoma cells, heparin inhibited both insulin binding and insulin-stimulated autophosphorylation in receptors solubilized from these cells.	Heparin	76-83	insulin	Homo sapiens	99-106
2434508-1	1987	The inhibitory effect of heparin and antithrombin III (AT) on the interaction of fibrinogen and thrombin was investigated in preference to studies on heparinizing devices.	Heparin	25-32	fibrinogen beta chain	Homo sapiens	81-91
2434508-3	1987	It was found that AT did not act on fibrinogen but, rather, on thrombin, and the main role of heparin is to accelerate the AT-thrombin reaction.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	126-134
2434508-5	1987	When heparin and AT were incubated with thrombin, inhibition did not depend on the mixing order but on the incubation time.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	40-48
2434508-6	1987	Thus, a ternary complex of heparin, AT, and thrombin was supposed to form for the inhibition.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	44-52
2434508-7	1987	The reaction of heparin with fibrinogen and thrombin in the presence of AT was well-explained by assuming a Freundlich-type adsorption of heparin analogous with the reaction of heparin with fibrinogen.	Heparin	16-23	fibrinogen beta chain	Homo sapiens	29-39
2434508-7	1987	The reaction of heparin with fibrinogen and thrombin in the presence of AT was well-explained by assuming a Freundlich-type adsorption of heparin analogous with the reaction of heparin with fibrinogen.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	44-52
2434508-7	1987	The reaction of heparin with fibrinogen and thrombin in the presence of AT was well-explained by assuming a Freundlich-type adsorption of heparin analogous with the reaction of heparin with fibrinogen.	Heparin	16-23	fibrinogen beta chain	Homo sapiens	190-200
2434508-7	1987	The reaction of heparin with fibrinogen and thrombin in the presence of AT was well-explained by assuming a Freundlich-type adsorption of heparin analogous with the reaction of heparin with fibrinogen.	Heparin	138-145	fibrinogen beta chain	Homo sapiens	29-39
2434508-7	1987	The reaction of heparin with fibrinogen and thrombin in the presence of AT was well-explained by assuming a Freundlich-type adsorption of heparin analogous with the reaction of heparin with fibrinogen.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	44-52
2434508-7	1987	The reaction of heparin with fibrinogen and thrombin in the presence of AT was well-explained by assuming a Freundlich-type adsorption of heparin analogous with the reaction of heparin with fibrinogen.	Heparin	138-145	fibrinogen beta chain	Homo sapiens	190-200
2950245-5	1987	Porcine sodium heparin (20 micrograms/cm2) was added by means of fibronectin"s heparin affinity.	Heparin	8-22	fibronectin 1	Homo sapiens	65-76
2950245-5	1987	Porcine sodium heparin (20 micrograms/cm2) was added by means of fibronectin"s heparin affinity.	Heparin	15-22	fibronectin 1	Homo sapiens	65-76
3807788-3	1987	The constant infusion of heparin stimulated lipolytic activity and accelerated the disappearance of apo B100 radioactivity (VLDL and their remnants) from the Svedberg flotation unit (Sf) greater than 60 fraction by 27%, 33%, 51%, and 55% in the four subjects.	Heparin	25-32	apolipoprotein B	Homo sapiens	100-108
3590084-3	1987	Rapid inactivation of cell-bound thrombin by antithrombin III (ATIII) accelerated by heparin-like structures represents another anticoagulant mechanism.	Heparin	85-92	serpin family C member 1	Bos taurus	63-68
3803394-1	1987	Structural differences between the two subunits of human plasma fibronectin were studied by analyzing the carboxy-terminal heparin-binding domain (Hep-2).	Heparin	123-130	fibronectin 1	Homo sapiens	64-75
3619144-1	1987	Heparin cofactor II is a plasma protein that inhibits thrombin rapidity in the presence of heparin.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	54-62
3790599-0	1987	Comparison of the kinetic behavior of human and bovine proteins in the heparin-catalyzed antithrombin III/thrombin reaction.	Heparin	71-78	serpin family C member 1	Bos taurus	89-105
3790599-1	1987	Significant differences between saturation kinetic properties of heparin-stimulated reactions between thrombin and antithrombin III from human and bovine species were observed.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	102-110
3790599-6	1987	The major differences between the two species appeared to be related to interaction of thrombin or thrombin derivatives with heparin or heparin-antithrombin III complexes.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	87-95
3790599-6	1987	The major differences between the two species appeared to be related to interaction of thrombin or thrombin derivatives with heparin or heparin-antithrombin III complexes.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	99-107
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	14-22
3303833-0	1987	Role of heparin in realization of the hypoglycaemic action of insulin.	Heparin	8-15	insulin	Homo sapiens	62-69
3303833-1	1987	A temporary resistance to the hypoglycaemic action of insulin has been found after preliminary binding of heparin in the blood of animals by 1 mg/200 of protamine sulphate (PS).	Heparin	106-113	insulin	Homo sapiens	54-61
3303833-4	1987	2,5-ionene, a synthetic antagonist of heparin, induced temporary resistance to the hypoglycaemic action of insulin.	Heparin	38-45	insulin	Homo sapiens	107-114
3303833-5	1987	Intravenous injection of heparin in corresponding doses after PS administration restored the hypoglycaemic effect of insulin.	Heparin	25-32	insulin	Homo sapiens	117-124
3303833-6	1987	The results suggest that the presence in the circulation of reactive heparin may be necessary for insulin reception by the target tissue.	Heparin	69-76	insulin	Homo sapiens	98-105
3481165-2	1987	The heparin surface was highly thromboresistant in contact with blood, as manifested by minimal cell adhesion and a pronounced capacity to inactivate coagulation enzymes such as thrombin and factor Xa.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	178-186
3428717-4	1987	At high thrombin doses, tolerated only during additional administration of thrombin inhibitors, heparin leads to increased consumption of antithrombin III, whereas hirudin and the synthetic inhibitor do not.	Heparin	96-103	coagulation factor II	Rattus norvegicus	8-16
3621887-2	1987	Fibronectin purified from humans plasma by affinity chromatography on gelatin-agarose and heparin-agarose was cleaved by thrombin into a 29,000 Dalton and a 210,000 Dalton fragments.	Heparin	90-97	fibronectin 1	Homo sapiens	0-11
3621887-2	1987	Fibronectin purified from humans plasma by affinity chromatography on gelatin-agarose and heparin-agarose was cleaved by thrombin into a 29,000 Dalton and a 210,000 Dalton fragments.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	121-129
3428717-4	1987	At high thrombin doses, tolerated only during additional administration of thrombin inhibitors, heparin leads to increased consumption of antithrombin III, whereas hirudin and the synthetic inhibitor do not.	Heparin	96-103	coagulation factor II	Rattus norvegicus	75-83
3624944-2	1987	There was a significant increase in heparin releasable lipoprotein lipase activity which represents the functional pool without increase in total enzyme activity.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	55-73
2828272-1	1987	In order to obtain a radioiodinated antithrombin III (AT III) with a good labelling yield and optimal biological properties towards heparin, thrombin and its anti-AT III monoclonal antibodies, we compared the classical labelling methods and found them wanting.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	40-48
2947903-1	1987	Fibronectin binding sites on cultured human fibroblasts were localized by high voltage electron microscopy using either 5- or 18-nm colloidal gold beads (Au5 or Au18) bound to intact fibronectin, the 70-kD amino-terminal fragment of fibronectin that blocks incorporation of exogenous fibronectin into extracellular matrix, or 160-180-kD fragments of fibronectin with cell adhesion and heparin-binding activities.	Heparin	385-392	fibronectin 1	Homo sapiens	0-11
3805107-7	1987	The results indicate that the ACT and PTT after giving heparin depended on HNA rather than the patients" weight, and are related to the fibrinogen concentration.	Heparin	55-62	fibrinogen beta chain	Homo sapiens	136-146
3118260-4	1987	In patients with chronic glomerulonephritis and a compromised renin-angiotensin-aldosterone system, heparin may cause drug-induced selective hypoaldosteronism.	Heparin	100-107	renin	Homo sapiens	62-67
3118260-5	1987	The suppressive effect of heparin on aldosterone production was partially compensated for by increasing plasma renin activity.	Heparin	26-33	renin	Homo sapiens	111-116
3798418-0	1986	Thrombin inactivation on surfaces with covalently bonded heparin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	0-8
3629490-0	1987	[Plasma heparin precipitate as a source of fibronectin in the treatment of patients with trophic skin lesions].	Heparin	8-15	fibronectin 1	Homo sapiens	43-54
3629490-1	1987	A study with the help of the hard phase enzyme immunoassay has shown that during incubation in the cold of fresh and fresh-frozen donor plasma in the presence of 10 I. U./ml-30 I.U./ml of heparin over 80% of fibronectin with relation to its basal level in the same plasma sample passes to the residue (heparin precipitate).	Heparin	188-195	fibronectin 1	Homo sapiens	208-219
3629490-2	1987	The effectiveness of local use of the preparation of plasmic heparin precipitate (fibronectin concentration of 1 to 1.5 mg/ml) for therapy of patients with heavy trophic skin lesions was substantiated.	Heparin	61-68	fibronectin 1	Homo sapiens	82-93
3798418-5	1986	It was concluded that the heparin surface has a large capacity to bind thrombin and that the thrombin inhibitory capacity of high affinity heparin fragments is limited.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	71-79
3798418-5	1986	It was concluded that the heparin surface has a large capacity to bind thrombin and that the thrombin inhibitory capacity of high affinity heparin fragments is limited.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	93-101
3798418-8	1986	It is concluded that inhibition of thrombin adsorbed on the heparin surface occurs as follows: Added AT adheres to high affinity heparin fragments on the surface whereupon adsorbed thrombin migrates in the hydrophilic heparin coating towards the reaction site of AT and becomes inhibited.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	35-43
3798418-8	1986	It is concluded that inhibition of thrombin adsorbed on the heparin surface occurs as follows: Added AT adheres to high affinity heparin fragments on the surface whereupon adsorbed thrombin migrates in the hydrophilic heparin coating towards the reaction site of AT and becomes inhibited.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	181-189
3798418-8	1986	It is concluded that inhibition of thrombin adsorbed on the heparin surface occurs as follows: Added AT adheres to high affinity heparin fragments on the surface whereupon adsorbed thrombin migrates in the hydrophilic heparin coating towards the reaction site of AT and becomes inhibited.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	35-43
3798418-8	1986	It is concluded that inhibition of thrombin adsorbed on the heparin surface occurs as follows: Added AT adheres to high affinity heparin fragments on the surface whereupon adsorbed thrombin migrates in the hydrophilic heparin coating towards the reaction site of AT and becomes inhibited.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	35-43
3596677-5	1986	The binding of SAP to Fn was selectively inhibited by a monoclonal antibody specific for the mid-molecule region of Fn, by soluble gelatin, and by heparin in the presence of 3mM Ca++.	Heparin	147-154	fibronectin 1	Homo sapiens	22-24
3782093-7	1986	Glu56-Asp-Asp-Asp-Tyr(SO4)-Leu-Asp62 Glu69-Asp-Asp-Asp-Tyr(SO4)-Ile-Asp75 Sulfate-labeled heparin cofactor II formed a covalent complex with thrombin in a heparin-dependent manner.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	141-149
3782093-7	1986	Glu56-Asp-Asp-Asp-Tyr(SO4)-Leu-Asp62 Glu69-Asp-Asp-Asp-Tyr(SO4)-Ile-Asp75 Sulfate-labeled heparin cofactor II formed a covalent complex with thrombin in a heparin-dependent manner.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	141-149
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	118-126
3798412-6	1986	This suggests that Factor Xa and antithrombin III have similar affinities for this immobilized heparin, unlike the situation for thrombin (Thromb-Res., 20, 543-554, 1980).	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	37-45
2948501-4	1986	The Apo E induced uptake of triglyceride emulsions by hepatocytes was inhibited by highly sulfated polysaccharides (i.e. heparin, dextran sulfate) but other glycosaminoglycans which did not bind the emulsion were ineffective in this inhibition.	Heparin	121-128	apolipoprotein E	Homo sapiens	4-9
3094583-8	1986	30 and 90 min following heparin-enhanced lipolysis "free" apolipoprotein A-I accounted for 23 and 20%, respectively, of the total apolipoprotein A-I of serum.	Heparin	24-31	apolipoprotein A1	Homo sapiens	58-76
3094583-8	1986	30 and 90 min following heparin-enhanced lipolysis "free" apolipoprotein A-I accounted for 23 and 20%, respectively, of the total apolipoprotein A-I of serum.	Heparin	24-31	apolipoprotein A1	Homo sapiens	130-148
2431020-4	1986	If thrombin and fibrin formation are dominant, oral anticoagulant agents or heparin should be beneficial; thus, experimental evidence indicates that with repeated vessel wall injury, the formation of platelet fibrin thrombi on the vessel wall is probably influenced more by inhibitors of thrombin generation than by the subendothelial constituents such as collagen.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	288-296
3782075-0	1986	Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.	Heparin	36-43	endogenous retrovirus group K member 25	Homo sapiens	72-82
3782075-0	1986	Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	59-67
3782075-3	1986	In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	152-160
3782075-5	1986	In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin.	Heparin	109-117	coagulation factor II, thrombin	Homo sapiens	52-60
3782075-5	1986	In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	52-60
3782075-7	1986	These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	56-64
3782075-7	1986	These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	69-77
3768377-1	1986	Heparin-binding fragments derived from the amino- and carboxyl-terminal regions of human plasma fibronectin appear to be at least relatively specific potent inhibitors of the growth of bovine aortic endothelial cells in culture by as yet unknown mechanisms.	Heparin	0-7	fibronectin 1	Homo sapiens	96-107
2946699-6	1986	In contrast, the binding of fibronectin to heparin was not influenced by glycosylation.	Heparin	43-50	fibronectin 1	Homo sapiens	28-39
3778045-3	1986	Heparin solutions (100 U/mL, US Pharmacopoela) used to prevent the formation of clots within the HC appeared to cause, to a significant degree, spuriously elevated levels of fibrin degradation products (FDP), decreased levels of fibrinogen (FBG), and prolongations of the prothrombin time (PT) and activated partial thromboplastin time (PTT) in the first 10 mL of HC blood.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	229-239
2430978-0	1986	Topographic localization of the heparin-binding domain of the neural cell adhesion molecule N-CAM.	Heparin	32-39	neural cell adhesion molecule 1	Mus musculus	62-91
2430978-0	1986	Topographic localization of the heparin-binding domain of the neural cell adhesion molecule N-CAM.	Heparin	32-39	neural cell adhesion molecule 1	Mus musculus	92-97
2430978-10	1986	In the present study we have determined the topographic localization of the heparin-binding fragment from N-CAM, which has been identified by our laboratory.	Heparin	76-83	neural cell adhesion molecule 1	Mus musculus	106-111
3825816-3	1986	AR was purified from 1,700 g of benign prostatic hypertrophic tissue by combining affinity chromatography of heparin Sepharose CL-6B and of 17 alpha-carboxy-hexamethyl-17-hydroxy-4-androstane-3-one Sepharose 4B.	Heparin	109-116	androgen receptor	Homo sapiens	0-2
3825818-3	1986	With 855 g of benign prostatic hypertrophic tissue as starting material, the androgen receptor (AR) was purified by combining the affinity chromatography of heparin Sepharose CL-6B and of R1881-carboxymethyloxime-albumin Sepharose 4B.	Heparin	157-164	androgen receptor	Homo sapiens	77-94
3825818-3	1986	With 855 g of benign prostatic hypertrophic tissue as starting material, the androgen receptor (AR) was purified by combining the affinity chromatography of heparin Sepharose CL-6B and of R1881-carboxymethyloxime-albumin Sepharose 4B.	Heparin	157-164	androgen receptor	Homo sapiens	96-98
2430978-15	1986	We have also shown that the B1A3 mAb recognizes not only chicken N-CAM but also rat and mouse N-CAM, indicating that the heparin-binding domain of N-CAM is evolutionarily conserved among different N-CAM forms.	Heparin	121-128	neural cell adhesion molecule 1	Mus musculus	94-99
2430978-15	1986	We have also shown that the B1A3 mAb recognizes not only chicken N-CAM but also rat and mouse N-CAM, indicating that the heparin-binding domain of N-CAM is evolutionarily conserved among different N-CAM forms.	Heparin	121-128	neural cell adhesion molecule 1	Mus musculus	94-99
2432674-4	1986	At a low salt concentration, about two-thirds of the chymotrypsin was instantaneously inactivated by the AT III preparation in the presence of heparin.	Heparin	143-150	serpin family C member 1	Bos taurus	105-111
2430978-15	1986	We have also shown that the B1A3 mAb recognizes not only chicken N-CAM but also rat and mouse N-CAM, indicating that the heparin-binding domain of N-CAM is evolutionarily conserved among different N-CAM forms.	Heparin	121-128	neural cell adhesion molecule 1	Mus musculus	94-99
2432675-0	1986	Thrombin inhibitory activity of heparin cofactor II depends on the molecular weight and sulfate amount of dextran sulfate.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	0-8
2432675-3	1986	The maximum second order rate constant of heparin cofactor II-thrombin reaction in the presence of the fractions of over-10 kDa and 18% sulfur was 2.7 X 10(8) M-1 min-1 that was almost same as in the presence of heparin or dermatan sulfate.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	62-70
2432675-3	1986	The maximum second order rate constant of heparin cofactor II-thrombin reaction in the presence of the fractions of over-10 kDa and 18% sulfur was 2.7 X 10(8) M-1 min-1 that was almost same as in the presence of heparin or dermatan sulfate.	Heparin	42-49	CD59 molecule (CD59 blood group)	Homo sapiens	163-168
2432675-3	1986	The maximum second order rate constant of heparin cofactor II-thrombin reaction in the presence of the fractions of over-10 kDa and 18% sulfur was 2.7 X 10(8) M-1 min-1 that was almost same as in the presence of heparin or dermatan sulfate.	Heparin	212-219	coagulation factor II, thrombin	Homo sapiens	62-70
2432675-3	1986	The maximum second order rate constant of heparin cofactor II-thrombin reaction in the presence of the fractions of over-10 kDa and 18% sulfur was 2.7 X 10(8) M-1 min-1 that was almost same as in the presence of heparin or dermatan sulfate.	Heparin	212-219	CD59 molecule (CD59 blood group)	Homo sapiens	163-168
3093793-0	1986	Rapid and high-yield purification of porcine heart tissue-type plasminogen activator by heparin-sepharose choromatography.	Heparin	88-95	plasminogen activator, tissue type	Homo sapiens	51-84
3771529-3	1986	PN-I preferentially binds thrombin, urokinase, trypsin, and plasmin, and its binding to thrombin is accelerated by heparin.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	88-96
3463998-2	1986	This protein was found to be similar to basic fibroblast growth factor (bFGF) in size, cationic nature, and affinity for heparin.	Heparin	121-128	fibroblast growth factor 2	Homo sapiens	40-70
3790498-6	1986	The first-order rate constants of these reactions at 200 nM antithrombin III and normalized to heparin at 1 microgram/mL were 0.33 and 9.5 min-1 in the presence and absence of factor Va and phospholipid, respectively.	Heparin	95-102	CD59 molecule (CD59 blood group)	Homo sapiens	139-144
3790498-8	1986	It is our conclusion that factor Xa when acting in prothrombinase on prothrombin is profoundly protected from inhibition by antithrombin III in the absence as well as in the presence of heparin.	Heparin	186-193	coagulation factor II, thrombin	Homo sapiens	51-62
3756204-4	1986	Activities of both lipoprotein lipase and hepatic triacylglycerol lipase in the plasma after heparin injection were markedly lower in the W/WV mice than in the congenic normal mice, although activities of both lipoprotein lipase in the heart and adipose tissue and hepatic triacylglycerol lipase in the liver were not decreased.	Heparin	93-100	lipase, hepatic	Mus musculus	42-72
2877688-4	1986	Proteolytic digestion of [14C]putrescine-labeled TSP with trypsin or thrombin yielded a labeled disulfide-bonded core of 90 or 120-130 kilodalton (kDa) subunits, labeled fragments of less than 10 kDa, and an unlabeled 30-kDa heparin-binding fragment, indicating the presence of multiple factor XIIIa reactive glutaminyl residues located in several domains of the molecule.	Heparin	225-232	coagulation factor II, thrombin	Homo sapiens	69-77
2428602-6	1986	In contrast, chorioallantoic membranes treated with combinations of angiostatic steroid and heparin exhibited capillary BM fragmentation and eventually complete loss of fibronectin and laminin from regions of capillary involution.	Heparin	92-99	laminin, beta 2 (laminin S)	Gallus gallus	185-192
2880412-2	1986	For this purpose, plasma SLI responses were determined in previously gastrectomized subjects during lipid-heparin induced elevation of plasma free fatty acids (FFA), which gave a consistent rise of plasma SLI in normal controls.	Heparin	106-113	SHC adaptor protein 2	Homo sapiens	25-28
2877688-4	1986	Proteolytic digestion of [14C]putrescine-labeled TSP with trypsin or thrombin yielded a labeled disulfide-bonded core of 90 or 120-130 kilodalton (kDa) subunits, labeled fragments of less than 10 kDa, and an unlabeled 30-kDa heparin-binding fragment, indicating the presence of multiple factor XIIIa reactive glutaminyl residues located in several domains of the molecule.	Heparin	225-232	thrombospondin 1	Homo sapiens	49-52
3463998-2	1986	This protein was found to be similar to basic fibroblast growth factor (bFGF) in size, cationic nature, and affinity for heparin.	Heparin	121-128	fibroblast growth factor 2	Homo sapiens	72-76
3509863-3	1986	The most potent inhibitor of neutrophil elastase was alpha 1AT (Leu358), which also proved to be effective against cathepsin G. The alpha 1AT (Arg358) variant inactivated thrombin with kinetics similar to antithrombin III in the presence of heparin.	Heparin	241-248	serpin family A member 1	Homo sapiens	53-62
3509863-3	1986	The most potent inhibitor of neutrophil elastase was alpha 1AT (Leu358), which also proved to be effective against cathepsin G. The alpha 1AT (Arg358) variant inactivated thrombin with kinetics similar to antithrombin III in the presence of heparin.	Heparin	241-248	serpin family A member 1	Homo sapiens	132-141
3509863-3	1986	The most potent inhibitor of neutrophil elastase was alpha 1AT (Leu358), which also proved to be effective against cathepsin G. The alpha 1AT (Arg358) variant inactivated thrombin with kinetics similar to antithrombin III in the presence of heparin.	Heparin	241-248	coagulation factor II, thrombin	Homo sapiens	171-179
3756195-3	1986	Both human and rat lipoprotein lipase from post-heparin plasma are inhibited by HDL.	Heparin	48-55	lipoprotein lipase	Rattus norvegicus	19-37
2945283-0	1986	Stimulation by heparin of the plasmin-mediated conversion of single-chain to two-chain urokinase-type plasminogen activator.	Heparin	15-22	plasminogen activator, urokinase	Homo sapiens	87-123
3751995-5	1986	Treatment of the false positive samples with reptilase, an enzyme unaffected by heparin, resulted in complete removal of the residual FFMP, and in vitro experiments demonstrated that heparin-containing plasma samples could be completely clotted with either reptilase or protamine sulfate plus thrombin.	Heparin	183-190	coagulation factor II, thrombin	Homo sapiens	293-301
3755846-5	1986	In contrast to the reactions in the absence of heparin, in the presence of high affinity heparin, the differences between various forms of thrombin are more pronounced and the shape of the progress curves, as well as rates, are highly dependent on the ionic strength.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	139-147
3091287-0	1986	Enhancement of thrombolysis with tissue-type plasminogen activator by pretreatment with heparin.	Heparin	88-95	tissue-type plasminogen activator	Canis lupus familiaris	33-66
3091287-1	1986	The effect of pretreatment with heparin on lysis of arterial thrombi by tissue-type plasminogen activator (rt-PA) was studied in 19 dogs.	Heparin	32-39	tissue-type plasminogen activator	Canis lupus familiaris	72-105
3022074-4	1986	However, heparin at 0.1 and 0.3 IU/ml doses selectively blocked aldosterone production maximally stimulated by AII but not by ACTH or potassium, while the compound at 1 and 10 IU/ml doses inhibited aldosterone production maximally stimulated by these three stimuli.	Heparin	9-16	angiotensinogen	Rattus norvegicus	111-114
3022074-6	1986	These data suggest that heparin at 0.1 and 0.3 IU/ml doses acts directly on adrenal zona glomerulosa to selectively block the stimulatory action of AII, while the compound at 1 and 10 IU/ml doses inhibits all the stimulatory actions of AII, ACTH and potassium.	Heparin	24-31	angiotensinogen	Rattus norvegicus	148-151
3022074-6	1986	These data suggest that heparin at 0.1 and 0.3 IU/ml doses acts directly on adrenal zona glomerulosa to selectively block the stimulatory action of AII, while the compound at 1 and 10 IU/ml doses inhibits all the stimulatory actions of AII, ACTH and potassium.	Heparin	24-31	angiotensinogen	Rattus norvegicus	236-239
3462733-7	1986	The ability of cells to accelerate the reaction between PN and thrombin was inhibited by protamine, suggesting that the activity was similar to that of heparin.	Heparin	152-159	coagulation factor II, thrombin	Homo sapiens	63-71
3755846-5	1986	In contrast to the reactions in the absence of heparin, in the presence of high affinity heparin, the differences between various forms of thrombin are more pronounced and the shape of the progress curves, as well as rates, are highly dependent on the ionic strength.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	139-147
3730415-0	1986	Mouse preheparin plasma contains high levels of hepatic lipase with low affinity for heparin.	Heparin	9-16	lipase, hepatic	Mus musculus	48-62
3730415-9	1986	Mouse hepatic lipase eluted from heparin-Sepharose at lower salt concentration than rat or human hepatic lipase, demonstrating that it has a relatively low affinity for heparin-like polysaccharides.	Heparin	169-176	lipase, hepatic	Mus musculus	6-20
3527705-7	1986	Although many properties of YCK-2 and LCK-2, including substrate specificity, inhibition by heparin, polyglutamic acid and quercetin and stimulation by polyamines, are similar; their stability under denaturing and dissociating conditions and their response to polybasic peptides are quite different.	Heparin	92-99	serine/threonine protein kinase YCK2	Saccharomyces cerevisiae S288C	28-33
2426262-6	1986	The total rate of thrombin inhibition in plasma containing 4 mM free Ca2+ was of the order of 1.9 min-1, of which 0.4 min-1 was due to alpha 2M and 0.9 min-1 was due to inhibitors that were removed when plasma was passed through heparin-agarose.	Heparin	229-236	coagulation factor II, thrombin	Homo sapiens	18-26
3730415-9	1986	Mouse hepatic lipase eluted from heparin-Sepharose at lower salt concentration than rat or human hepatic lipase, demonstrating that it has a relatively low affinity for heparin-like polysaccharides.	Heparin	33-40	lipase, hepatic	Mus musculus	6-20
3800906-0	1986	A fragment of antithrombin that binds both heparin and thrombin.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	18-26
3778563-0	1986	Peri- and postnatal, teratology and reproductive studies of a low molecular weight heparin in rats.	Heparin	83-90	perilipin 1	Rattus norvegicus	0-4
3800906-2	1986	These fragments did not exhibit direct thrombin-neutralizing activity; however, one unique fragment was found to bind to heparin-Sepharose and also to interfere with the inhibition of thrombin by intact antithrombin.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	184-192
3800906-4	1986	At a concentration of 46 nM, this product decreased the heparin-enhanced thrombin-inhibitory activity of antithrombin by half, and completely abolished this inhibition when above 300 nM.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	73-81
3800906-9	1986	It is concluded that this peptide possesses portions of the antithrombin molecule that bind to heparin as well as to a site on thrombin.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	64-72
3526328-5	1986	This peptide corresponds to the already described fragment that originates from the central part of FN; it contains a low-affinity heparin-binding site, one free SH group, and a cell-binding site.	Heparin	131-138	fibronectin 1	Homo sapiens	100-102
3760786-7	1986	Furthermore we demonstrate interferences, in particular between heparin and collagen in their mutual binding to fibronectin.	Heparin	64-71	fibronectin 1	Homo sapiens	112-123
3729956-0	1986	Effect of heparin on the stimulation of non-vascular cells by human acidic and basic FGF.	Heparin	10-17	fibroblast growth factor 1	Homo sapiens	85-88
3461443-3	1986	The largest clone identified contains an open reading frame that encodes the amino-terminal heparin binding domain of TSP and part of the immediately adjacent collagen binding domain, a region of TSP that includes the site of disulfide crosslinking responsible for trimer formation.	Heparin	92-99	thrombospondin 1	Homo sapiens	118-121
3461443-4	1986	In addition to the known amino-terminal sequence of mature TSP (which is identical to that of the heparin binding domain) and that of the collagen binding domain, the open reading frame predicts the amino acid sequences of four tryptic peptides including the one from which the probe sequences were derived.	Heparin	98-105	thrombospondin 1	Homo sapiens	59-62
2943315-2	1986	Heparin also increases the activity in mixtures of urokinase-type plasminogen activator (uPA) and plasminogen but has no effect on streptokinase or plasmin.	Heparin	0-7	plasminogen activator, urokinase	Homo sapiens	51-87
2943315-2	1986	Heparin also increases the activity in mixtures of urokinase-type plasminogen activator (uPA) and plasminogen but has no effect on streptokinase or plasmin.	Heparin	0-7	plasminogen activator, urokinase	Homo sapiens	89-92
2943315-3	1986	Direct analyses of plasminogen activation by polyacrylamide gel electrophoresis demonstrate that heparin increases the activation of plasminogen by both tPA and uPA.	Heparin	97-104	plasminogen activator, urokinase	Homo sapiens	161-164
2943315-4	1986	Binding studies show that heparin binds to various components of the fibrinolytic system, with tight binding demonstrable with tPA, uPA, and Lys-plasminogen.	Heparin	26-33	plasminogen activator, urokinase	Homo sapiens	132-135
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	36-44
3750270-1	1986	Serum amyloid P component (SAP), and its acute phase homologue C-reactive protein (CRP), prolonged activated partial thromboplastin times (APTT) in cell free plasma when assayed at physiological concentrations in the presence of heparin.	Heparin	229-236	C-reactive protein	Homo sapiens	63-81
3750270-1	1986	Serum amyloid P component (SAP), and its acute phase homologue C-reactive protein (CRP), prolonged activated partial thromboplastin times (APTT) in cell free plasma when assayed at physiological concentrations in the presence of heparin.	Heparin	229-236	C-reactive protein	Homo sapiens	83-86
3729956-2	1986	In both the presence and the absence of foetal calf serum (FCS) heparin cooperates with h-aFGF in a dose dependent manner to stimulate both types of cells.	Heparin	64-71	fibroblast growth factor 1	Homo sapiens	90-94
3518813-4	1986	f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation.	Heparin	30-37	fibroblast growth factor 1	Homo sapiens	2-6
3729956-5	1986	These results indicate that heparin cooperates strongly with h-aFGF to stimulate non-vascular cell proliferation while in a partially purified extract and in the presence of serum it can induce the opposite effect.	Heparin	28-35	fibroblast growth factor 1	Homo sapiens	63-67
3518813-4	1986	f-ECGF had a high affinity to heparin-Sepharose CL-6B, and was isolated by the methods of heparin affinity, of ion-exchange and gel filtration chromatography from the serum-free culture-conditioned medium preparation.	Heparin	90-97	fibroblast growth factor 1	Homo sapiens	2-6
3754869-4	1986	Functionally, S-protein in the presence of low concentrations of heparin, protects thrombin from inactivation by ATIII.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	83-91
3790076-2	1986	This LPL-like activity is eluted by 1.5 M-NaCl from heparin-Sepharose columns.	Heparin	52-59	lipoprotein lipase	Rattus norvegicus	5-8
3754869-9	1986	The protective effect of S-protein on inactivation of thrombin by ATIII was demonstrated in functional assays with purified proteins and in plasma only in the presence of low concentrations of heparin.	Heparin	193-200	coagulation factor II, thrombin	Homo sapiens	54-62
3528366-4	1986	Residual apoE and albumin, amounting up to 0.5% of the apoB mass, were resistant to removal by TGRP treatment as well as by heparin-Sepharose column chromatography.	Heparin	124-131	apolipoprotein E	Homo sapiens	9-13
3707976-2	1986	Lipoprotein lipase was purified by heparin-Sepharose affinity chromatography followed by preparative isoelectric focusing.	Heparin	35-42	lipoprotein lipase	Rattus norvegicus	0-18
3486185-3	1986	Heparin strongly inhibits binding of thrombospondin but only weakly inhibits binding of laminin and von Willebrand factor.	Heparin	0-7	von Willebrand factor	Homo sapiens	100-121
3697371-9	1986	In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	25-33
3699029-9	1986	The heparin-counteracting activity of S protein was found to be mainly expressed in the range of 0.01-0.1 U/ml heparin, thereby shifting the point of 50% inhibition of thrombin from 0.003 U/ml to 0.1 U/ml heparin with a second-order rate constant of k2 = 1.4 X 10(6) M-1.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	168-176
3697371-9	1986	In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	38-46
3697371-9	1986	In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	25-33
3697371-9	1986	In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	38-46
3697371-10	1986	A possible explanation is that thrombin, after initial binding to the heparin, moves rapidly to the site where it combines with antithrombin.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	31-39
3715810-1	1986	An unfractionated heparin (UFH) and a depolymerised derivative of low molecular weight heparin (LMWH) have been compared for their ability to activate platelets suspended in citrated plasma (PRP) or after washing and suspension in hepes buffered tyrode containing fibrinogen.	Heparin	87-94	prion protein	Homo sapiens	191-194
3715810-2	1986	Neither heparin alone induced aggregation of washed platelets, but UFH and to a much lesser extent LMWH, induced aggregation of platelets in PRP.	Heparin	67-70	prion protein	Homo sapiens	141-144
3715810-3	1986	Both heparins caused significant enhancement of a low concentration of ADP-induced activation of PRP and, again, the effect of LMWH was somewhat less than that of UFH.	Heparin	5-13	prion protein	Homo sapiens	97-100
3715810-5	1986	In addition, UFH induced a potentiation of PAF-induced aggregation and dense-granule release in PRP, a property not shared by LMWH.	Heparin	13-16	prion protein	Homo sapiens	96-99
3715810-6	1986	In PRP, UFH was three times more potent at inhibiting thrombin-induced aggregation and dense-granule release, as might be expected from their specific activities in the KCCT and thrombin time assay.	Heparin	8-11	prion protein	Homo sapiens	3-6
3715810-6	1986	In PRP, UFH was three times more potent at inhibiting thrombin-induced aggregation and dense-granule release, as might be expected from their specific activities in the KCCT and thrombin time assay.	Heparin	8-11	coagulation factor II, thrombin	Homo sapiens	54-62
3715810-6	1986	In PRP, UFH was three times more potent at inhibiting thrombin-induced aggregation and dense-granule release, as might be expected from their specific activities in the KCCT and thrombin time assay.	Heparin	8-11	coagulation factor II, thrombin	Homo sapiens	178-186
3715810-7	1986	However, with washed platelets, both heparins were equivalent at inhibiting thrombin-induced aggregation, dense-granule release and elevation of cytosolic free calcium ([Ca++]i) as monitored by quin 2 fluorescence.	Heparin	37-45	coagulation factor II, thrombin	Homo sapiens	76-84
3697371-1	1986	Fluorescence polarization has been used to study the interaction of thrombin and heparin, and the catalysis by heparin of the combination of thrombin and antithrombin.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	68-76
3697371-1	1986	Fluorescence polarization has been used to study the interaction of thrombin and heparin, and the catalysis by heparin of the combination of thrombin and antithrombin.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	141-149
3697371-2	1986	At low ionic strength (20 mM Tris, pH 7.4), the addition of heparins of known molecular weights to thrombin led to the formation of large complexes (defined as "complex 1").	Heparin	60-68	coagulation factor II, thrombin	Homo sapiens	99-107
3697371-4	1986	The molar ratio of thrombin to heparin in complex 1 increased with increasing heparin molecular weight, and corresponded to one thrombin molecule for every heparin segment of Mr 3000.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	128-136
3697371-4	1986	The molar ratio of thrombin to heparin in complex 1 increased with increasing heparin molecular weight, and corresponded to one thrombin molecule for every heparin segment of Mr 3000.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	19-27
3697371-4	1986	The molar ratio of thrombin to heparin in complex 1 increased with increasing heparin molecular weight, and corresponded to one thrombin molecule for every heparin segment of Mr 3000.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	19-27
3697371-5	1986	The stoichiometry of complex 2 was 1 heparin to 1 thrombin, irrespective of the heparin molecular weight.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	50-58
3697371-7	1986	However, by reversing the titration and adding thrombin to fluorescein-heparin the dissociation constant for complex 2 was estimated to be 1-3 microM and independent of the heparin molecular weight.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	47-55
3697371-8	1986	The complex formed between thrombin and heparin, to which antithrombin was attached, has a dissociation constant of 1-2 microM, again irrespective of the heparin molecular weight.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	27-35
3697371-8	1986	The complex formed between thrombin and heparin, to which antithrombin was attached, has a dissociation constant of 1-2 microM, again irrespective of the heparin molecular weight.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	27-35
3699029-0	1986	S protein modulates the heparin-catalyzed inhibition of thrombin by antithrombin III.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	56-64
3699029-2	1986	The interference of S protein with the heparin-catalyzed inhibition of thrombin by antithrombin III was studied in a purified system and in plasma.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	71-79
3699029-6	1986	While the association constant of thrombin--antithrombin III in the presence of 0.05 U/ml heparin amounted to 2.5 X 10(8) M-1, an approximately 200-fold decrease of this value was observed in the presence of S protein.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	34-42
3699029-7	1986	The fast formation of the covalent complex between thrombin and antithrombin III in the presence of heparin was impaired as a result of the presence of S protein, as was shown by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	51-59
3699029-9	1986	The heparin-counteracting activity of S protein was found to be mainly expressed in the range of 0.01-0.1 U/ml heparin, thereby shifting the point of 50% inhibition of thrombin from 0.003 U/ml to 0.1 U/ml heparin with a second-order rate constant of k2 = 1.4 X 10(6) M-1.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	168-176
3699029-9	1986	The heparin-counteracting activity of S protein was found to be mainly expressed in the range of 0.01-0.1 U/ml heparin, thereby shifting the point of 50% inhibition of thrombin from 0.003 U/ml to 0.1 U/ml heparin with a second-order rate constant of k2 = 1.4 X 10(6) M-1.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	168-176
3699029-12	1986	These findings not only indicate a direct interaction of S protein with heparin in the onset of the inhibition of thrombin by antithrombin-III--heparin, but also a contribution of S protein during enzyme-inhibitor complex formation.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	114-122
3700371-8	1986	HDL was depleted of phospholipid (PL) by treatment with either phospholipase A2 or heparin-releasable rat hepatic lipase, followed by incubation with bovine serum albumin.	Heparin	83-90	lipase C, hepatic type	Rattus norvegicus	106-120
3014736-0	1986	[Heparin-induced impairment of thrombin interaction with fibrinogen and receptors of the anti-coagulation system].	Heparin	1-8	coagulation factor II	Rattus norvegicus	31-39
3715809-0	1986	Effects of different ions on the interactions of heparin with bovine antithrombin III and thrombin.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	73-81
3014736-1	1986	Administration of heparin (2 un) into rats with depression of the anticoagulation system before treatment of the animals with alpha-thrombin (8 NIH un) inhibited the enzyme interaction with blood fibrinogen, which was manifested as a distinct decrease in content of soluble fibrin in blood as compared with its concentration evaluated after the treatment with thrombin.	Heparin	18-25	coagulation factor II	Rattus norvegicus	132-140
3715809-5	1986	These findings indicate that the affinity of heparin to AT III was influenced only by strongly electronegative ions, whereas its affinity to thrombin was affected by both strongly electropositive and strongly electronegative ions.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	141-149
3014736-1	1986	Administration of heparin (2 un) into rats with depression of the anticoagulation system before treatment of the animals with alpha-thrombin (8 NIH un) inhibited the enzyme interaction with blood fibrinogen, which was manifested as a distinct decrease in content of soluble fibrin in blood as compared with its concentration evaluated after the treatment with thrombin.	Heparin	18-25	coagulation factor II	Rattus norvegicus	360-368
3014736-2	1986	Heparin inhibited the reaction of thrombin with specific receptors in vascular walls.	Heparin	0-7	coagulation factor II	Rattus norvegicus	34-42
3014736-5	1986	The data obtained suggest that heparin, which inhibits partially the recognition site in thrombin molecule, impaired also the enzyme ability to bind to the specific receptors of vascular walls and therefore it impaired the distinct response of the anticoagulation system.	Heparin	31-38	coagulation factor II	Rattus norvegicus	89-97
3947650-0	1986	The catalysis by heparin of the reaction between thrombin and antithrombin.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	49-57
3754413-1	1986	Heparin cofactor II and antithrombin III are plasma proteins functionally similar in their ability to inhibit thrombin at accelerated rates in the presence of heparin.	Heparin	159-166	coagulation factor II, thrombin	Homo sapiens	28-36
3720040-0	1986	Heparin effect on plasma fibrinogen in the thrombophilic syndrome.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	25-35
3013157-1	1986	Casein kinase 2 from rat liver cytosol phosphorylated human fibrinogen in a reaction that was not stimulated by Ca2+ or cyclic AMP, but was markedly inhibited by heparin, and proceeded at a similar rate when either ATP or GTP was used as phosphate donor.	Heparin	162-169	fibrinogen beta chain	Homo sapiens	60-70
3007451-5	1986	The gelatinase co-purified with fibronectin in chromatography on Sepharoses conjugated with gelatin, arginine, and heparin but could be separated from fibronectin by gel filtration in a physiological buffer.	Heparin	115-122	fibronectin 1	Homo sapiens	32-43
3963947-6	1986	We conclude that bleeding is related to the anticoagulant effects of fibrinogen degradation products interacting with heparin, and may be largely independent of hypofibrinogenemia.	Heparin	118-125	fibrinogen beta chain	Homo sapiens	69-79
3708104-0	1986	Effect of NaCl on the association of thrombin with heparin.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	37-45
3949807-1	1986	The molecular interactions between components of the heparin-catalyzed antithrombin III/thrombin reaction were investigated by light scattering.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	75-83
3949807-5	1986	This behavior was observed for bovine and human antithrombin III in the presence of both unfractionated heparin and high molecular weight-high affinity heparin.	Heparin	104-111	serpin family C member 1	Bos taurus	48-64
3949807-5	1986	This behavior was observed for bovine and human antithrombin III in the presence of both unfractionated heparin and high molecular weight-high affinity heparin.	Heparin	152-159	serpin family C member 1	Bos taurus	48-64
3949807-8	1986	In the presence of stoichiometric amounts of heparin, the bovine proteins formed an initial complex of Mr = 230,000 (corresponding to a dimer of heparin-antithrombin III-thrombin) which underwent further aggregation.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	157-165
3949807-9	1986	The human proteins, however, formed a 1:1 (antithrombin III X thrombin) initial complex in the presence of heparin, followed by aggregation.	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	47-55
3949807-10	1986	These interactions of thrombin and antithrombin with heparin suggest complex interactions that could relate to heparin function.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	22-30
3949807-10	1986	These interactions of thrombin and antithrombin with heparin suggest complex interactions that could relate to heparin function.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	22-30
3955055-8	1986	When heparin was used in these assays, the rate of inhibition of thrombin by antithrombin was much more rapid and 62% of thrombin activity remained after 1 min.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	65-73
3955055-8	1986	When heparin was used in these assays, the rate of inhibition of thrombin by antithrombin was much more rapid and 62% of thrombin activity remained after 1 min.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	81-89
3949769-0	1986	Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity-purified heparin.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	18-26
3949769-3	1986	The binding stoichiometries of antithrombin III and thrombin interactions with the heparin of these fractions were measured, using changes in intrinsic and extrinsic fluorescence.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	35-43
3949769-5	1986	As the molecular weight of heparin varied from about 10,000 to 30,000, the average number of antithrombin and thrombin sites/heparin molecule varied from 1.0 to 2.1 and 2.4 to 6.8.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	97-105
3949769-8	1986	This can be explained by assuming that heparin functions as a template for both proteins, that all bound thrombin and antithrombin III molecules are accessible to each other, and that the rate at which a bound molecule reacts is proportional to the number of molecules of its interacting counterpart bound.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	105-113
3949769-12	1986	259, 5670-5677), who demonstrated that the rate at which single molecules of antithrombin III, covalently attached to heparin, react increases as the thrombin binding capacity (chain length) of heparin increases.	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	81-89
3947650-2	1986	The heparin-catalysed combination of thrombin and antithrombin is saturable with respect to both thrombin and antithrombin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	37-45
3949769-12	1986	259, 5670-5677), who demonstrated that the rate at which single molecules of antithrombin III, covalently attached to heparin, react increases as the thrombin binding capacity (chain length) of heparin increases.	Heparin	194-201	coagulation factor II, thrombin	Homo sapiens	81-89
3947650-2	1986	The heparin-catalysed combination of thrombin and antithrombin is saturable with respect to both thrombin and antithrombin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	54-62
2936763-9	1986	A 285,000-D fragment of vWF multimer was separated from heterogeneous 210,000-225,000-D fragments by its ability to bind to heparin.	Heparin	124-131	von Willebrand factor	Homo sapiens	24-27
2418019-1	1986	Determination of the heparin binding sites of apolipoprotein E3.	Heparin	21-28	apolipoprotein E	Homo sapiens	46-63
3954770-0	1986	Protein kinase activation of heparin-releasable lipoprotein lipase in rat heart.	Heparin	29-36	lipoprotein lipase	Rattus norvegicus	48-66
2418019-2	1986	The interaction of human apolipoprotein (apo-) E3 with heparin was examined using heparin-Sepharose as a model system.	Heparin	55-62	apolipoprotein E	Homo sapiens	25-48
2421433-1	1986	The relative potency of pentosan polysulphate in activation of heparin cofactor II/thrombin interaction has been compared to heparin and dermatan sulphate and found to be within the same order.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	83-91
2418019-3	1986	The approach taken to determine the region of apo-E that is responsible for binding to heparin was to identify apo-E monoclonal antibodies that inhibited heparin binding, to determine the epitopes of the inhibiting antibodies, and finally to examine the heparin binding of fragments containing the inhibiting antibody epitopes.	Heparin	154-161	apolipoprotein E	Homo sapiens	111-116
2418019-3	1986	The approach taken to determine the region of apo-E that is responsible for binding to heparin was to identify apo-E monoclonal antibodies that inhibited heparin binding, to determine the epitopes of the inhibiting antibodies, and finally to examine the heparin binding of fragments containing the inhibiting antibody epitopes.	Heparin	154-161	apolipoprotein E	Homo sapiens	46-51
2418019-3	1986	The approach taken to determine the region of apo-E that is responsible for binding to heparin was to identify apo-E monoclonal antibodies that inhibited heparin binding, to determine the epitopes of the inhibiting antibodies, and finally to examine the heparin binding of fragments containing the inhibiting antibody epitopes.	Heparin	154-161	apolipoprotein E	Homo sapiens	111-116
2418019-4	1986	Three antibodies, designated 1D7, 6C5, and 3H1, were found to inhibit binding, suggesting that multiple heparin binding sites were present on apo-E.	Heparin	104-111	apolipoprotein E	Homo sapiens	142-147
2418019-6	1986	Measurement of the heparin binding activity of fragments containing epitopes of the inhibiting antibodies demonstrated that apo-E3 contains two heparin binding sites.	Heparin	19-26	apolipoprotein E	Homo sapiens	124-130
2418019-6	1986	Measurement of the heparin binding activity of fragments containing epitopes of the inhibiting antibodies demonstrated that apo-E3 contains two heparin binding sites.	Heparin	144-151	apolipoprotein E	Homo sapiens	124-130
2418019-10	1986	A head-to-tail association of apo-E, in which the 6C5 epitope and the second heparin binding site would be in close proximity, is proposed to account for this observation.	Heparin	77-84	apolipoprotein E	Homo sapiens	30-35
2418019-11	1986	In the lipid-free state both heparin binding sites on apo-E are expressed; however, when apo-E is complexed to phospholipid or on the surface of a lipoprotein particle, only the first binding site (residues 142-147) is expressed.	Heparin	29-36	apolipoprotein E	Homo sapiens	54-59
2418019-11	1986	In the lipid-free state both heparin binding sites on apo-E are expressed; however, when apo-E is complexed to phospholipid or on the surface of a lipoprotein particle, only the first binding site (residues 142-147) is expressed.	Heparin	29-36	apolipoprotein E	Homo sapiens	89-94
2418019-2	1986	The interaction of human apolipoprotein (apo-) E3 with heparin was examined using heparin-Sepharose as a model system.	Heparin	82-89	apolipoprotein E	Homo sapiens	25-48
2418019-3	1986	The approach taken to determine the region of apo-E that is responsible for binding to heparin was to identify apo-E monoclonal antibodies that inhibited heparin binding, to determine the epitopes of the inhibiting antibodies, and finally to examine the heparin binding of fragments containing the inhibiting antibody epitopes.	Heparin	87-94	apolipoprotein E	Homo sapiens	46-51
2418019-3	1986	The approach taken to determine the region of apo-E that is responsible for binding to heparin was to identify apo-E monoclonal antibodies that inhibited heparin binding, to determine the epitopes of the inhibiting antibodies, and finally to examine the heparin binding of fragments containing the inhibiting antibody epitopes.	Heparin	87-94	apolipoprotein E	Homo sapiens	111-116
2418019-3	1986	The approach taken to determine the region of apo-E that is responsible for binding to heparin was to identify apo-E monoclonal antibodies that inhibited heparin binding, to determine the epitopes of the inhibiting antibodies, and finally to examine the heparin binding of fragments containing the inhibiting antibody epitopes.	Heparin	154-161	apolipoprotein E	Homo sapiens	46-51
3510669-1	1986	Rat hearts were perfused with heparin for 2 min at 4 degrees C. The lipoprotein lipase activity in the perfusate was inhibited by antiserum to rat adipose tissue lipoprotein lipase.	Heparin	30-37	lipoprotein lipase	Rattus norvegicus	68-86
3004341-0	1986	Heparin modulates conformational states of plasma fibronectin: an electron spin resonance spin label approach.	Heparin	0-7	fibronectin 1	Homo sapiens	50-61
3006413-0	1986	Effect of angiotensin II on aldosterone and its precursor steroid production in adrenal zona glomerulosa cells from heparin-treated rats.	Heparin	116-123	angiotensinogen	Rattus norvegicus	10-24
3006413-2	1986	Heparin-treated rats had low plasma aldosterone levels, high plasma renin activity and plasma AII levels, and normal plasma corticosterone level 6 weeks after the treatment (1500 IU/kg, twice daily).	Heparin	0-7	angiotensinogen	Rattus norvegicus	94-97
3006413-4	1986	The cells from heparin-treated rats had a less sensitive and lower response of aldosterone production to AII; an increase by 4 orders of magnitude in the threshold dose for AII and a decrease in the maximum AII-stimulated level.	Heparin	15-22	angiotensinogen	Rattus norvegicus	105-108
3006413-4	1986	The cells from heparin-treated rats had a less sensitive and lower response of aldosterone production to AII; an increase by 4 orders of magnitude in the threshold dose for AII and a decrease in the maximum AII-stimulated level.	Heparin	15-22	angiotensinogen	Rattus norvegicus	173-176
3006413-4	1986	The cells from heparin-treated rats had a less sensitive and lower response of aldosterone production to AII; an increase by 4 orders of magnitude in the threshold dose for AII and a decrease in the maximum AII-stimulated level.	Heparin	15-22	angiotensinogen	Rattus norvegicus	173-176
3006413-5	1986	The maximum AII-stimulated levels, but not the basal levels, of pregnenolone, corticosterone and 18-OHB production were low in the cells from heparin-treated rats.	Heparin	142-149	angiotensinogen	Rattus norvegicus	12-15
3006413-7	1986	The cells from heparin-treated rats had a less sensitive and lower response of aldosterone production to potassium; an increase by one order of magnitude in the threshold dose for potassium and a decrease in the maximum potassium-stimulated level, presumably because of the glomerulosa hyporesponsiveness to AII.	Heparin	15-22	angiotensinogen	Rattus norvegicus	308-311
3006413-8	1986	These results suggest that our heparin-treated rats have selective impairment of adrenal zona glomerulosa cells, involving the specific receptors and the aldosterone biosynthesis, to AII.	Heparin	31-38	angiotensinogen	Rattus norvegicus	183-186
3957961-0	1986	Thrombin uptake and inhibition on endothelium and surfaces with a stable heparin coating: a comparative in vitro study.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	0-8
3957961-6	1986	The disappearance rate of thrombin from the solution was the same on exposure to the endothelium and the covalently bonded heparin surface, but less following exposure to the ionically bonded heparin surface.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	26-34
3957961-6	1986	The disappearance rate of thrombin from the solution was the same on exposure to the endothelium and the covalently bonded heparin surface, but less following exposure to the ionically bonded heparin surface.	Heparin	192-199	coagulation factor II, thrombin	Homo sapiens	26-34
3957961-9	1986	Thrombin bound to the covalently bonded heparin surface was inhibited at a slower rate than on the ionically bonded surface, but still faster than the rate at which free thrombin was inhibited in nonheparinized plasma.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	0-8
3957961-9	1986	Thrombin bound to the covalently bonded heparin surface was inhibited at a slower rate than on the ionically bonded surface, but still faster than the rate at which free thrombin was inhibited in nonheparinized plasma.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	170-178
3957961-10	1986	It is concluded that the endothelium and stabilized heparin coatings bind thrombin and accelerate its inhibition by plasma.	Heparin	52-59	coagulation factor II, thrombin	Homo sapiens	74-82
2422780-0	1986	Effect of NaC1 on inactivation of bovine thrombin by antithrombin III in the presence of low affinity-heparin or dextran sulfate.	Heparin	102-109	serpin family C member 1	Bos taurus	53-69
2422780-1	1986	Heparin with low affinity (LA-heparin) to antithrombin III (AT III) enhanced the rate of inactivation of thrombin by AT III.	Heparin	0-7	serpin family C member 1	Bos taurus	42-58
2422780-1	1986	Heparin with low affinity (LA-heparin) to antithrombin III (AT III) enhanced the rate of inactivation of thrombin by AT III.	Heparin	0-7	serpin family C member 1	Bos taurus	60-66
2422780-1	1986	Heparin with low affinity (LA-heparin) to antithrombin III (AT III) enhanced the rate of inactivation of thrombin by AT III.	Heparin	0-7	serpin family C member 1	Bos taurus	117-123
3947350-0	1986	Binding of a high reactive heparin to human apolipoprotein E: identification of two heparin-binding domains.	Heparin	27-34	apolipoprotein E	Homo sapiens	44-60
3947350-0	1986	Binding of a high reactive heparin to human apolipoprotein E: identification of two heparin-binding domains.	Heparin	84-91	apolipoprotein E	Homo sapiens	44-60
3947350-1	1986	Ligand-blotting and dot-blotting procedures were used to investigate the binding of [125I]-heparin to apolipoprotein E, its thrombin fragments E22 (residues 1-191) and E12 (residues 192-299), and to nine apolipoprotein E synthetic fragments.	Heparin	91-98	apolipoprotein E	Homo sapiens	102-118
3947350-1	1986	Ligand-blotting and dot-blotting procedures were used to investigate the binding of [125I]-heparin to apolipoprotein E, its thrombin fragments E22 (residues 1-191) and E12 (residues 192-299), and to nine apolipoprotein E synthetic fragments.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	124-132
3947350-3	1986	Synthetic peptides of apoE corresponding to residues 129-169, 139-169, and 144-169, but not 148-169, bound [125I] heparin suggesting that residues 144-147 (Leu-Arg-Lys-Arg) in E22 are important for binding.	Heparin	114-121	apolipoprotein E	Homo sapiens	22-26
2436525-14	1986	This inhibition was only partially abolished when thrombin was added to the plasma before heparin, indicating that heparin inhibits prothrombin activation both by catalyzing the inhibition of thrombin activity and by a heparin cofactor-independent mechanism.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	50-58
2436525-14	1986	This inhibition was only partially abolished when thrombin was added to the plasma before heparin, indicating that heparin inhibits prothrombin activation both by catalyzing the inhibition of thrombin activity and by a heparin cofactor-independent mechanism.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	135-143
3814109-1	1986	Heparin and synthetic inhibitors of thrombin are able to decrease the rate of division of porcine vascular smooth muscle cells in primary culture and to increase their myosin content.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	36-44
3948864-7	1986	Furthermore, we have studied the interaction of thermolysin-digested fibronectin both with DNA-cellulose and heparin-Sepharose using the above procedure.	Heparin	109-116	fibronectin 1	Homo sapiens	69-80
2422102-1	1986	We have investigated the effects of triiodothyronine (T3) and thyroxine (T4) on the heparin-stimulated release of hepatic lipase (HL) activity from cultured rat hepatocytes.	Heparin	84-91	lipase C, hepatic type	Rattus norvegicus	114-128
2422102-1	1986	We have investigated the effects of triiodothyronine (T3) and thyroxine (T4) on the heparin-stimulated release of hepatic lipase (HL) activity from cultured rat hepatocytes.	Heparin	84-91	lipase C, hepatic type	Rattus norvegicus	130-132
3030185-0	1986	[Influence of heparin on the radioimmunological assay of ACTH].	Heparin	14-21	proopiomelanocortin	Homo sapiens	57-61
3030185-1	1986	Heparin traps plasma ACTH, promoting the formation of aggregates with apparent high molecular weight as shown by chromatography on Sephadex G 50 fine columns.	Heparin	0-7	proopiomelanocortin	Homo sapiens	21-25
3030185-5	1986	Heparin interferes with direct RIA-ACTH in the plasma by decreasing 125I-ACTH binding to the antibodies and modifying the slope of the standard curve.	Heparin	0-7	proopiomelanocortin	Homo sapiens	35-39
3030185-5	1986	Heparin interferes with direct RIA-ACTH in the plasma by decreasing 125I-ACTH binding to the antibodies and modifying the slope of the standard curve.	Heparin	0-7	proopiomelanocortin	Homo sapiens	73-77
3030185-6	1986	Unsuitable artefacts induced by heparin, as overestimation or underestimation of plasma ACTH levels by RIA, can be avoid by previous hormone extraction from heparinized plasmas.	Heparin	32-39	proopiomelanocortin	Homo sapiens	88-92
3004341-1	1986	We have examined the interaction between heparin and human plasma fibronectin using electron spin resonance (ESR) spin label methods.	Heparin	41-48	fibronectin 1	Homo sapiens	66-77
3004341-6	1986	Addition of heparin resulted in a decrease in the maximum splitting value of the ESR spectrum of spin-labeled fibronectin from 66.8 to 64.3 G, suggesting that heparin induces a conformational alteration of plasma fibronectin.	Heparin	12-19	fibronectin 1	Homo sapiens	110-121
3004341-6	1986	Addition of heparin resulted in a decrease in the maximum splitting value of the ESR spectrum of spin-labeled fibronectin from 66.8 to 64.3 G, suggesting that heparin induces a conformational alteration of plasma fibronectin.	Heparin	12-19	fibronectin 1	Homo sapiens	213-224
3004341-6	1986	Addition of heparin resulted in a decrease in the maximum splitting value of the ESR spectrum of spin-labeled fibronectin from 66.8 to 64.3 G, suggesting that heparin induces a conformational alteration of plasma fibronectin.	Heparin	159-166	fibronectin 1	Homo sapiens	110-121
3004341-6	1986	Addition of heparin resulted in a decrease in the maximum splitting value of the ESR spectrum of spin-labeled fibronectin from 66.8 to 64.3 G, suggesting that heparin induces a conformational alteration of plasma fibronectin.	Heparin	159-166	fibronectin 1	Homo sapiens	213-224
3004341-7	1986	This heparin effect was noticeable at a heparin-to-fibronectin ratio of 20 to 1 and reached a plateau at about 100 to 1.	Heparin	5-12	fibronectin 1	Homo sapiens	51-62
3004341-9	1986	The results presented suggest that the binding of heparin changes the molecular conformation of plasma fibronectin to a more relaxed or flexible state.	Heparin	50-57	fibronectin 1	Homo sapiens	103-114
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Heparin	217-224	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	55-67
3955564-6	1986	Whereas the anticoagulant activity of heparins, as measured by USP, anti-Xa, and thrombin-time assays, was invariably reduced by the chemical transformations effected, the ability of heparin to bind calcium ions was found to be dependent on retention of the 2-sulfamino group, whether or not O-sulfate groups were present.	Heparin	38-46	coagulation factor II, thrombin	Homo sapiens	81-89
3955564-6	1986	Whereas the anticoagulant activity of heparins, as measured by USP, anti-Xa, and thrombin-time assays, was invariably reduced by the chemical transformations effected, the ability of heparin to bind calcium ions was found to be dependent on retention of the 2-sulfamino group, whether or not O-sulfate groups were present.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	81-89
3096631-3	1986	Heparin reduced or abolished the inhibition of lipoprotein lipase by plasma, serum and purified vitellogenin.	Heparin	0-7	vitellogenin 2	Gallus gallus	96-108
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Heparin	217-224	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	186-198
3096631-4	1986	The results suggest that inhibition of lipoprotein lipase by vitellogenin requires the presence of charged phosphate groups on vitellogenin and an unoccupied heparin-binding site on the enzyme.	Heparin	158-165	vitellogenin 2	Gallus gallus	61-73
2937928-1	1986	We have previously communicated that heparan sulfate and heparin released 16S acetylcholinesterase (AChE) from cholinergic synapses.	Heparin	57-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	100-104
3086193-0	1986	Inhibition of thrombin-catalyzed reactions in blood coagulation and platelet activation by heparin fractions in the absence of antithrombin III.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	14-22
3086193-4	1986	The inhibitory action of heparin (fractions) appeared to be the result of the formation of a complex between heparin and thrombin that alters the specificity of thrombin towards high molecular weight substrates.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	121-129
3086193-4	1986	The inhibitory action of heparin (fractions) appeared to be the result of the formation of a complex between heparin and thrombin that alters the specificity of thrombin towards high molecular weight substrates.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	161-169
3086193-4	1986	The inhibitory action of heparin (fractions) appeared to be the result of the formation of a complex between heparin and thrombin that alters the specificity of thrombin towards high molecular weight substrates.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	121-129
3086193-4	1986	The inhibitory action of heparin (fractions) appeared to be the result of the formation of a complex between heparin and thrombin that alters the specificity of thrombin towards high molecular weight substrates.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	161-169
3086193-5	1986	The inhibition of these thrombin-dependent feedback reactions in blood coagulation might be of importance in the mechanisms for the dissociation between the antithrombotic and hemorrhagic properties of low molecular weight heparins.	Heparin	223-231	coagulation factor II, thrombin	Homo sapiens	24-32
3093294-5	1986	Treatment of rats with heparin resulted in a depletion of intestinal DAO and the concomitant appearance of DAO in blood.	Heparin	23-30	D-amino-acid oxidase	Rattus norvegicus	69-72
3093294-5	1986	Treatment of rats with heparin resulted in a depletion of intestinal DAO and the concomitant appearance of DAO in blood.	Heparin	23-30	D-amino-acid oxidase	Rattus norvegicus	107-110
3782314-7	1986	Pretreatment of platelets with heparin markedly increases the number of PNp-[125I]-thrombin complexes that form on platelets.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	83-91
3941152-9	1986	The second fragment that stimulated melanoma adhesion was a 33-kD tryptic/catheptic carboxyl-terminal heparin-binding fragment, which is localized to the A chain of fibronectin.	Heparin	102-109	fibronectin 1	Homo sapiens	165-176
2431979-2	1986	With regard to a long-term stabilization of blood or blood plasma, satisfactory results can only be achieved with the competitive synthetic thrombin inhibitor 4-amidinophenylpyruvic acid by adding slight amounts of heparin and by storing it in a cool room.	Heparin	215-222	coagulation factor II, thrombin	Homo sapiens	140-148
3710297-2	1986	Heparin inhibits blood coagulation by 3 independent mechanisms by augmenting the effect of antithrombin III (the major effect), by augmenting the inhibitory effect of thrombin or heparin cofactor II, and by disrupting the activation of blood coagulation on the platelet surface; it has an additional effect on hemostasis through its interaction with blood platelets.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	95-103
2937928-5	1986	Fifty percent of the binding of the 16S AChE was blocked by heparan sulfate, heparin, or previous treatment of the cell with heparitinase.	Heparin	77-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	40-44
4063380-11	1985	Hyperlipemia, or injection of heparin, led to increased lipoprotein lipase activity in the liver.	Heparin	30-37	lipoprotein lipase	Rattus norvegicus	56-74
3798336-0	1986	[Decreased effectiveness of cold-induced heparin precipitation of plasma fibronectin in infection].	Heparin	41-48	fibronectin 1	Homo sapiens	73-84
3798336-4	1986	The formation of the heparin precipitate following plasma incubation in the cold in the presence of heparin is determined by FN involvement.	Heparin	21-28	fibronectin 1	Homo sapiens	125-127
3798336-4	1986	The formation of the heparin precipitate following plasma incubation in the cold in the presence of heparin is determined by FN involvement.	Heparin	100-107	fibronectin 1	Homo sapiens	125-127
3798336-5	1986	Fibrinogen (FG) is another main component of the heparin precipitate.	Heparin	49-56	fibrinogen beta chain	Homo sapiens	0-10
3798336-5	1986	Fibrinogen (FG) is another main component of the heparin precipitate.	Heparin	49-56	fibrinogen beta chain	Homo sapiens	12-14
3798336-6	1986	To determine the functional activity of plasma FN in sepsis and other pathological conditions, a study was made of the ability of FN and FG to go into the precipitate formed in blood plasma in the cold after its incubation with heparin.	Heparin	228-235	fibronectin 1	Homo sapiens	130-132
3798336-6	1986	To determine the functional activity of plasma FN in sepsis and other pathological conditions, a study was made of the ability of FN and FG to go into the precipitate formed in blood plasma in the cold after its incubation with heparin.	Heparin	228-235	fibrinogen beta chain	Homo sapiens	137-139
3798336-7	1986	Unlike normal subjects in whom over 80% of FN on the average and about 20% of FG went into the heparin precipitate, in patients with hemoblastoses and aplastic anemia complicated by sepsis, less than 40% of FN on the average and about 7% of FG went into the precipitate.	Heparin	95-102	fibrinogen beta chain	Homo sapiens	78-80
3798336-9	1986	The reduction of FN ability to go into the heparin precipitate correlated with the gravity of the patients" condition.	Heparin	43-50	fibronectin 1	Homo sapiens	17-19
3798336-10	1986	In uncomplicated hemoblastoses, cryoglobulinemia and cryofibrinogenemia and in immunocomplex pathology, the consumption of FN and FG during heparin precipitate formation did not significantly differ from the control.	Heparin	140-147	fibrinogen beta chain	Homo sapiens	130-132
4063381-10	1985	The increase in heart lipoprotein lipase was due to an increase in heparin-releasable fraction.	Heparin	67-74	lipoprotein lipase	Rattus norvegicus	22-40
3161948-3	1985	Fibrinogen treated with tryptase together with heparin lost all detectable clotting activity by 4 hr at 37 degrees C, whereas fibrinogen treated with tryptase alone resulted in destruction of only 80% of fibrinogen clotting equivalents after 16 hr.	Heparin	47-54	fibrinogen beta chain	Homo sapiens	0-10
3905460-3	1985	Comparative studies were performed on the relative effects of diabetes and insulin on heparin-releasable adipose lipoprotein lipase (LPL) in the intact and hypothyroid rat.	Heparin	86-93	lipoprotein lipase	Rattus norvegicus	133-136
3905460-15	1985	These studies demonstrate that hypothyroidism counteracts the suppressant effect of diabetes on heparin-releasable rat adipose LPL activity and magnifies the enzyme response to insulin.	Heparin	96-103	lipoprotein lipase	Rattus norvegicus	127-130
3905825-3	1985	Heparin (10(-8) to 10(-10) M) was also chemotactic and was shown to potentiate the chemotactic activity of ECGF.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	107-111
2417623-2	1985	The domain structure of human plasma fibronectin was investigated by using heparin-binding and antibody reactivity of fibronectin and its proteolytically derived fragments.	Heparin	75-82	fibronectin 1	Homo sapiens	37-48
2417623-10	1985	A monoclonal antibody to fibronectin that recognized the 61K heparin-binding fragment was used to isolate a sixth fragment (Mr 34 000) that did not bind to heparin or gelatin and that represents a difference between the 61K and 36K heparin-binding fragments.	Heparin	61-68	fibronectin 1	Homo sapiens	25-36
2417623-11	1985	Cathepsin D digestion produced an 83K heparin-binding, monoclonal antibody reactive fragment that contains the interchain disulfide bond(s) linking the two fibronectin chains at their C-termini.	Heparin	38-45	fibronectin 1	Homo sapiens	156-167
2417623-13	1985	In contrast, enzymatic digestion of cellular fibronectin produced a 50K heparin-binding fragment lacking monoclonal antibody reactivity which suggests that the cellular fibronectin subunit is similar to the plasma A chain in enzyme susceptibility but contains a larger heparin-binding domain.	Heparin	72-79	fibronectin 1	Homo sapiens	45-56
2417623-13	1985	In contrast, enzymatic digestion of cellular fibronectin produced a 50K heparin-binding fragment lacking monoclonal antibody reactivity which suggests that the cellular fibronectin subunit is similar to the plasma A chain in enzyme susceptibility but contains a larger heparin-binding domain.	Heparin	72-79	fibronectin 1	Homo sapiens	169-180
2417623-13	1985	In contrast, enzymatic digestion of cellular fibronectin produced a 50K heparin-binding fragment lacking monoclonal antibody reactivity which suggests that the cellular fibronectin subunit is similar to the plasma A chain in enzyme susceptibility but contains a larger heparin-binding domain.	Heparin	269-276	fibronectin 1	Homo sapiens	45-56
2417623-13	1985	In contrast, enzymatic digestion of cellular fibronectin produced a 50K heparin-binding fragment lacking monoclonal antibody reactivity which suggests that the cellular fibronectin subunit is similar to the plasma A chain in enzyme susceptibility but contains a larger heparin-binding domain.	Heparin	269-276	fibronectin 1	Homo sapiens	169-180
2997575-4	1985	In contrast, the heparin-elutable part of LPL activity in the tissue was not influenced by the Synacthen treatment.	Heparin	17-24	lipoprotein lipase	Rattus norvegicus	42-45
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	49-57
3900070-1	1985	The complete amino acid sequence of a DNA- and heparin-binding domain isolated by limited thermolysin digestion of human plasma fibronectin has been obtained.	Heparin	47-54	fibronectin 1	Homo sapiens	128-139
3902901-3	1985	Human fibrinogen induced platelet aggregation in 65% of platelet rich plasma samples and enhanced submaximal platelet aggregation induced by heparin or by several conventional agonists in all samples.	Heparin	141-148	fibrinogen beta chain	Homo sapiens	6-16
3909150-3	1985	The bacterially produced apoE was purified by heparin-Sepharose affinity chromatography, Sephacryl S-300 gel filtration, and preparative Immobiline isoelectric focusing.	Heparin	46-53	apolipoprotein E	Homo sapiens	25-29
4052441-1	1985	Lipoprotein lipase synthesized by cultured rat preadipocytes is present in three compartments: an intracellular, a surface-related 3-min heparin-releasable, and that secreted into the culture medium.	Heparin	137-144	lipoprotein lipase	Rattus norvegicus	0-18
4052441-8	1985	The intracellular lipoprotein lipase in monensin-treated cells had the same affinity for both the native and synthetic substrate as the lipoprotein lipase in control cells, yet its spontaneous secretion into the culture medium and its release by 3 min heparin treatment was markedly decreased.	Heparin	252-259	lipoprotein lipase	Rattus norvegicus	18-36
3936965-13	1985	LMW-heparin, therefore, appears to be a good alternative to UF-heparin for dialysis patients and may present less risk of bleeding because of its reduced effect on PTT, thrombin time, and thrombocytes.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	169-177
3001968-1	1985	Heparin has been reported to antagonize the platelet antiaggregating activity of prostacyclin (PGI2) and prostaglandin D2 (PGD2).	Heparin	0-7	prostaglandin D2 synthase	Homo sapiens	105-121
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	79-87
2413043-2	1985	One Mab, designated A2.5, inhibits the hemagglutinating activity of TSP and immunoprecipitates the NH2 terminal 25 kD heparin binding domain of TSP (Dixit, V.M., D. M. Haverstick, K. M. O"Rourke, S. W. Hennessy, G. A.	Heparin	118-125	thrombospondin 1	Homo sapiens	144-147
3161948-2	1985	Tryptase (5 micrograms/ml) inactivated the thrombin-induced clotting activity of fibrinogen (100 micrograms/ml) with essentially similar t 1/2 values of 4.6 min in the absence of heparin and 5.8 min in the presence of heparin (20 micrograms/ml) that were not appreciably different than with lysine-Sepharose-purified plasmin (5 micrograms/ml).	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	43-51
3161948-5	1985	Tryptase together with heparin cleaved first the alpha-chain and then the beta-chain, the latter cleavage corresponding to complete loss of fibrinogen clotting activity by 4 hr.	Heparin	23-30	Fc gamma receptor and transporter	Homo sapiens	49-60
3161948-5	1985	Tryptase together with heparin cleaved first the alpha-chain and then the beta-chain, the latter cleavage corresponding to complete loss of fibrinogen clotting activity by 4 hr.	Heparin	23-30	fibrinogen beta chain	Homo sapiens	140-150
4064078-0	1985	Interaction of heparin with multimolecular aggregates of acetylcholinesterase.	Heparin	15-22	acetylcholinesterase (Cartwright blood group)	Homo sapiens	57-77
3863104-2	1985	The rate of thrombin inhibition by heparin cofactor II is accelerated (greater than or equal to 1000-fold) in the presence of the glycosaminoglycans, heparin and dermatan sulfate.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	12-20
3863104-2	1985	The rate of thrombin inhibition by heparin cofactor II is accelerated (greater than or equal to 1000-fold) in the presence of the glycosaminoglycans, heparin and dermatan sulfate.	Heparin	150-157	coagulation factor II, thrombin	Homo sapiens	12-20
3928376-18	1985	(c) Heparin inhibits thrombin cleavage of Arg/Lys-Xaa bonds located near the center of the antibody light chain, but slightly activates thrombin cleavage of those located near the amino or carboxyl-terminal ends of the protein.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	21-29
3928376-18	1985	(c) Heparin inhibits thrombin cleavage of Arg/Lys-Xaa bonds located near the center of the antibody light chain, but slightly activates thrombin cleavage of those located near the amino or carboxyl-terminal ends of the protein.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	136-144
4064078-1	1985	It has been reported previously that heparin, a sulfated glycosaminoglycan, releases the asymmetric 16 S form of acetylcholinesterase (AChE) from cholinergic synapses.	Heparin	37-44	acetylcholinesterase (Cartwright blood group)	Homo sapiens	113-133
4064078-1	1985	It has been reported previously that heparin, a sulfated glycosaminoglycan, releases the asymmetric 16 S form of acetylcholinesterase (AChE) from cholinergic synapses.	Heparin	37-44	acetylcholinesterase (Cartwright blood group)	Homo sapiens	135-139
4064078-2	1985	Here it is shown that heparin releases the synaptic AChE not as individual 16 S species but as multimolecular aggregates (30 S) of such molecules.	Heparin	22-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	52-56
4064078-3	1985	Heparin is able to convert low-ionic strength AChE aggregates into a heparin type of AChE aggregates.	Heparin	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	46-50
4064078-3	1985	Heparin is able to convert low-ionic strength AChE aggregates into a heparin type of AChE aggregates.	Heparin	0-7	acetylcholinesterase (Cartwright blood group)	Homo sapiens	85-89
4064078-4	1985	Our results suggest that the AChE aggregates detached by heparin are likely to be the physiologically important state of aggregation of the 16 S AChE form in the synaptic basal lamina.	Heparin	57-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	29-33
4064078-4	1985	Our results suggest that the AChE aggregates detached by heparin are likely to be the physiologically important state of aggregation of the 16 S AChE form in the synaptic basal lamina.	Heparin	57-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	145-149
4082100-3	1985	From kinetic analysis on the initial stage of the fibrinogen-fibrin conversion catalyzed by thrombin, inhibition constants, Kip, of heparin and heparin analogues were obtained by the turbidimetrical method.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	92-100
2412230-3	1985	Heparin interacts structurally with ECGF [Maciag, T., Mehlman, T., Friesel, R. & Schreiber, A.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	36-40
2412230-6	1985	These data suggest that the association between heparin and ECGF induces a conformational change in the polypeptide that increases or stabilizes the biological activity of the mitogen.	Heparin	48-55	fibroblast growth factor 1	Homo sapiens	60-64
4082103-5	1985	The concentrations of PAP and t-PA-inhibitor were not influenced, while that of t-PA antigen showed a significant increase during heparin infusion.	Heparin	130-137	plasminogen activator, tissue type	Homo sapiens	80-84
4082100-3	1985	From kinetic analysis on the initial stage of the fibrinogen-fibrin conversion catalyzed by thrombin, inhibition constants, Kip, of heparin and heparin analogues were obtained by the turbidimetrical method.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	92-100
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	22-30
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	319-327
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	22-30
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	319-327
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	22-30
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	319-327
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	22-30
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	319-327
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	22-30
4082100-5	1985	In the fibrinogen and thrombin system, heparin and its analogues were observed to act as noncompetitive inhibitors at high concentrations, where the inhibition constant of heparin was 3.91 X 10(-6) M. At low concentrations below 10(-5) M, both heparin and dextran sulphate acted as hyperbolic competitive inhibitors of thrombin, and Kip of heparin was 1.07 X 10(-8) M, which was measured at heparin concentrations below ca.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	319-327
4082100-6	1985	10(-8) M. It was presumed that heparin has electrostatic interaction with the active site of thrombin or the binding site located near the active site of thrombin.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	93-101
4082100-6	1985	10(-8) M. It was presumed that heparin has electrostatic interaction with the active site of thrombin or the binding site located near the active site of thrombin.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	154-162
2861857-8	1985	A competitive dissociation experiment indicated that heparin and other polysulfated polysaccharides share a common binding site on the fibronectin molecule.	Heparin	53-60	fibronectin 1	Homo sapiens	135-146
4019466-4	1985	Disaccharides prepared by cleavage of heparin and N-deacetylated chondroitin 6-sulfate with nitrous acid were used to demonstrate a new sulfatase that catalyzed the removal of the 2-O-sulfate substituents from GlcA but not IdoA residues.	Heparin	38-45	arylsulfatase family member H	Homo sapiens	136-145
2411283-0	1985	The importance of thrombin inhibition for the expression of the anticoagulant activities of heparin, dermatan sulphate, low molecular weight heparin and pentosan polysulphate.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	18-26
2411283-0	1985	The importance of thrombin inhibition for the expression of the anticoagulant activities of heparin, dermatan sulphate, low molecular weight heparin and pentosan polysulphate.	Heparin	141-148	coagulation factor II, thrombin	Homo sapiens	18-26
2411283-4	1985	Standard heparin was the only sulphated polysaccharide that could equally inhibit thrombin generation and enhance the inactivation of factor Xa and thrombin by plasma.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	82-90
2411283-4	1985	Standard heparin was the only sulphated polysaccharide that could equally inhibit thrombin generation and enhance the inactivation of factor Xa and thrombin by plasma.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	148-156
3894594-4	1985	It binds to gelatin- and heparin-coupled Sepharose and it is recognized by specific anti-fibronectin sera.	Heparin	25-32	fibronectin 1	Homo sapiens	89-100
2861857-4	1985	The result showed that the affinity of heparin for fibronectin was dependent exclusively on its molecular size, and that an appropriate level of sulfate content in heparin (1.9-2.4 mol/disaccharide) was essential for the affinity.	Heparin	39-46	fibronectin 1	Homo sapiens	51-62
4049325-0	1985	Evidence that changes in fibrinogen quality during acute phase reactions are of major importance for the amount of heparin precipitable fraction (HPF).	Heparin	115-122	fibrinogen beta chain	Homo sapiens	25-35
4052397-4	1985	This fragment represents the previously characterized heparin binding domain of TSP [Dixit, V.M., Grant, G.A., Santoro, S.A., & Frazier, W.A.	Heparin	54-61	thrombospondin 1	Homo sapiens	80-83
4052397-8	1985	In agreement with this assignment, heparin inhibits the binding of Mab A2.5 to TSP.	Heparin	35-42	immunoglobulin kappa variable 1-22 (pseudogene)	Homo sapiens	71-75
4052397-8	1985	In agreement with this assignment, heparin inhibits the binding of Mab A2.5 to TSP.	Heparin	35-42	thrombospondin 1	Homo sapiens	79-82
4008652-8	1985	The TSP-HRGP-Plg complex bound a similar amount of heparin as the TSP-HRGP complex, demonstrating that the HRGP within the trimolecular complex maintained functional capability.	Heparin	51-58	thrombospondin 1	Homo sapiens	4-7
3161213-7	1985	Heparin stimulated ADP-induced platelet aggregation (0.2 uM; p less than 0.05) and inhibited thrombin induced aggregation (0.3 U/ml; p less than 0.05), while the heparinoid lacked these effects.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	93-101
3901387-4	1985	Under all tested conditions the low molecular weight fractions induced higher heparin levels, both in terms of anti-Xa and of anti-thrombin activity.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	131-139
3997865-0	1985	Heparin binding is necessary, but not sufficient, for fibronectin aggregation.	Heparin	0-7	fibronectin 1	Homo sapiens	54-65
3997865-2	1985	Analysis of parameters governing heparin binding to fibronectin indicates that heparin binding is a necessary, but insufficient, condition for fibronectin cryoprecipitation.	Heparin	33-40	fibronectin 1	Homo sapiens	52-63
3997865-2	1985	Analysis of parameters governing heparin binding to fibronectin indicates that heparin binding is a necessary, but insufficient, condition for fibronectin cryoprecipitation.	Heparin	79-86	fibronectin 1	Homo sapiens	52-63
3997865-4	1985	While cryoprecipitation of fibronectin is abolished at temperatures in excess of 10 degrees C, appreciable heparin binding to fibronectin does occur even at 40 degrees C. While increasing ionic strength and pH inhibit both heparin binding and cryoprecipitation of fibronectin, heparin binding can still occur at high ionic strengths and pH values which completely abolish cryoprecipitation.	Heparin	107-114	fibronectin 1	Homo sapiens	126-137
3997865-4	1985	While cryoprecipitation of fibronectin is abolished at temperatures in excess of 10 degrees C, appreciable heparin binding to fibronectin does occur even at 40 degrees C. While increasing ionic strength and pH inhibit both heparin binding and cryoprecipitation of fibronectin, heparin binding can still occur at high ionic strengths and pH values which completely abolish cryoprecipitation.	Heparin	107-114	fibronectin 1	Homo sapiens	126-137
3997865-4	1985	While cryoprecipitation of fibronectin is abolished at temperatures in excess of 10 degrees C, appreciable heparin binding to fibronectin does occur even at 40 degrees C. While increasing ionic strength and pH inhibit both heparin binding and cryoprecipitation of fibronectin, heparin binding can still occur at high ionic strengths and pH values which completely abolish cryoprecipitation.	Heparin	223-230	fibronectin 1	Homo sapiens	126-137
3997865-4	1985	While cryoprecipitation of fibronectin is abolished at temperatures in excess of 10 degrees C, appreciable heparin binding to fibronectin does occur even at 40 degrees C. While increasing ionic strength and pH inhibit both heparin binding and cryoprecipitation of fibronectin, heparin binding can still occur at high ionic strengths and pH values which completely abolish cryoprecipitation.	Heparin	223-230	fibronectin 1	Homo sapiens	126-137
3997865-4	1985	While cryoprecipitation of fibronectin is abolished at temperatures in excess of 10 degrees C, appreciable heparin binding to fibronectin does occur even at 40 degrees C. While increasing ionic strength and pH inhibit both heparin binding and cryoprecipitation of fibronectin, heparin binding can still occur at high ionic strengths and pH values which completely abolish cryoprecipitation.	Heparin	223-230	fibronectin 1	Homo sapiens	126-137
3997865-4	1985	While cryoprecipitation of fibronectin is abolished at temperatures in excess of 10 degrees C, appreciable heparin binding to fibronectin does occur even at 40 degrees C. While increasing ionic strength and pH inhibit both heparin binding and cryoprecipitation of fibronectin, heparin binding can still occur at high ionic strengths and pH values which completely abolish cryoprecipitation.	Heparin	223-230	fibronectin 1	Homo sapiens	126-137
3997865-9	1985	The role of heparin in the mechanism of fibronectin cryoprecipitation is discussed.	Heparin	12-19	fibronectin 1	Homo sapiens	40-51
3997857-9	1985	In the presence of heparin, protease nexin inhibits thrombin at a nearly diffusion-controlled rate.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	52-60
3875899-4	1985	The profibrinolytic actions of low molecular weight heparin fractions may be related to the release of t-PA, which is easily measured in plasma.	Heparin	52-59	plasminogen activator, tissue type	Homo sapiens	103-107
3160132-0	1985	Effect of heparin and low molecular weight heparins on thrombin-induced blood platelet activation in the absence of antithrombin III.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	55-63
3160132-0	1985	Effect of heparin and low molecular weight heparins on thrombin-induced blood platelet activation in the absence of antithrombin III.	Heparin	43-51	coagulation factor II, thrombin	Homo sapiens	55-63
3160132-4	1985	The inhibitory action of the heparins was found to be the result of a direct effect on thrombin and not of an effect either on platelet activation functions or on the assembly or functioning of the prothrombinase complex.	Heparin	29-37	coagulation factor II, thrombin	Homo sapiens	87-95
3160132-5	1985	Probably this heparin inhibition is due to the masking of secondary macromolecular substrate binding sites on the thrombin molecule.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	114-122
3926940-4	1985	It was found that plasmas from all of the anticoagulants, except sodium heparin, resulted in apparently significant decreases of both trypsin inhibitory capacity and concentration of alpha 1-antitrypsin measured by radial immunodiffusion, relative to serum.	Heparin	65-79	serpin family A member 1	Homo sapiens	183-202
4024529-1	1985	Heparin affected the content of antithrombin III and the thrombin time of blood plasma coagulation depending on the dose of the anticoagulant administered (eight intravenous administrations at single doses of 225, 150, 75, 37 or 18 IU/kg of body mass of healthy rats).	Heparin	0-7	coagulation factor II	Rattus norvegicus	36-44
3981266-4	1985	A heparin-Sepharose affinity column chromatographic method was used to subfractionate HDL into apolipoprotein E (apoE) -rich and apoE-poor subfractions.	Heparin	2-9	apolipoprotein E	Rattus norvegicus	95-111
2579080-4	1985	Thrombin digestion in the presence of calcium results in the release of a 30,000-dalton fragment, designated segment I, which contains the epitope for MA-II and the heparin-binding site.	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	0-8
3919773-2	1985	The first stage of the purification of the lipoprotein lipase was carried out with heparin-Sepharose affinity chromatography.	Heparin	83-90	lipoprotein lipase	Rattus norvegicus	43-61
2987207-4	1985	Myocardial lipoprotein lipase in the 40,000 X g supernatant fraction was then removed by heparin-Sepharose affinity chromatography.	Heparin	89-96	lipoprotein lipase	Rattus norvegicus	11-29
4005050-1	1985	The precipitation of plasma fibronectin by heparin in dependence on various parameters was investigated.	Heparin	43-50	fibronectin 1	Homo sapiens	28-39
4005050-8	1985	The results are discussed on the basis of a model assuming that heparin induces a conformational rearrangement of plasma fibronectin so that masked binding sites responsible for self-association become exposed.	Heparin	64-71	fibronectin 1	Homo sapiens	121-132
3988727-0	1985	The role of surface charge on the accelerating action of heparin on the antithrombin III-inhibited activity of alpha-thrombin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	76-84
3988727-2	1985	Polyelectrolyte titration of thrombin with KPVS or heparin at pH 7.4 clearly indicates an electrostatic interaction.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	29-37
3988727-8	1985	Heparin acts on the antithrombin III-thrombin reaction through cooperative electrostatic binding to thrombin and nonelectrostatic interaction with antithrombin III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	24-32
3988727-8	1985	Heparin acts on the antithrombin III-thrombin reaction through cooperative electrostatic binding to thrombin and nonelectrostatic interaction with antithrombin III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	37-45
3988735-0	1985	Apolipoprotein effects on the lipolysis of perfused triglyceride by heparin-immobilized milk lipase.	Heparin	68-75	apolipoprotein E	Homo sapiens	0-14
3988735-3	1985	Both apo-C-II and apo-E produced enhanced lipolysis in comparison to unsupplemented emulsions, at appropriate enzyme densities on the heparin-Sepharose.	Heparin	134-141	apolipoprotein E	Homo sapiens	18-23
3988735-6	1985	The enhancement of lipolysis produced by apo-E was correlated with the increased binding of triglyceride to the heparin-Sepharose enzyme complex.	Heparin	112-119	apolipoprotein E	Homo sapiens	41-46
4002203-5	1985	RCM potentiated the anti-thrombin action of heparin but the inhibition or delay of fibrinoformation is not related to an antithrombinic effect of contrast media.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	25-33
4016098-6	1985	The two inhibitors benzamidine and p-chlorobenzylamine as well as heparin caused decreases in bis-ANS-thrombin fluorescence: valerylamidine had no effect on the fluorescence of the bis-ANS-thrombin complex.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	102-110
4016098-6	1985	The two inhibitors benzamidine and p-chlorobenzylamine as well as heparin caused decreases in bis-ANS-thrombin fluorescence: valerylamidine had no effect on the fluorescence of the bis-ANS-thrombin complex.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	189-197
3838315-5	1985	The thrombin-HCII complex was undetectable when 5 units/ml of heparin was present or when prothrombin-deficient plasma was used.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	4-12
3898369-0	1985	Validity of serine protease inhibition tests in the evaluation and monitoring of the effect of heparin and its fractions.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	12-27
3919755-0	1985	Dramatic increase of placental protein 5 levels following injection of small doses of heparin.	Heparin	86-93	tissue factor pathway inhibitor 2	Homo sapiens	21-40
3919755-4	1985	Furthermore, the phenomenon appeared to be systemic rather than local, and may well be due to a direct effect of heparin on PP5 secretion by the placenta.	Heparin	113-120	tissue factor pathway inhibitor 2	Homo sapiens	124-127
3838304-2	1985	Heparin cofactor II and antithrombin III are functionally similar in that both proteins have been shown to inhibit thrombin at accelerated rates in the presence of heparin.	Heparin	164-171	coagulation factor II, thrombin	Homo sapiens	28-36
2986309-7	1985	When a higher concentration of thrombin was used (5 U/ml) these combinations caused platelets to deaggregate only when heparin was added before thrombin induced the release reaction.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	31-39
3838304-8	1985	While the similarities in primary structure suggest that heparin cofactor II may be an additional member of the superfamily of proteins consisting of antithrombin III, alpha 1-antitrypsin, alpha 1-antichymotrypsin and ovalbumin, the differences in structure could account for differences in protease specificity and reactivity toward thrombin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	154-162
3838304-10	1985	This observation provides an initial indication that while the reported kinetic mechanisms of action of heparin in accelerating the heparin cofactor II/thrombin and antithrombin III/thrombin reactions are similar, the mechanisms and effects of heparin binding to the two inhibitors may be different.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	152-160
3838304-10	1985	This observation provides an initial indication that while the reported kinetic mechanisms of action of heparin in accelerating the heparin cofactor II/thrombin and antithrombin III/thrombin reactions are similar, the mechanisms and effects of heparin binding to the two inhibitors may be different.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	169-177
3838304-10	1985	This observation provides an initial indication that while the reported kinetic mechanisms of action of heparin in accelerating the heparin cofactor II/thrombin and antithrombin III/thrombin reactions are similar, the mechanisms and effects of heparin binding to the two inhibitors may be different.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	152-160
3838317-1	1985	Heparin cofactor II is a plasma protein that inhibits thrombin rapidly in the presence of either heparin or dermatan sulfate.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	54-62
3882151-3	1985	Lipoprotein lipase in newborns liver was characterized by its inhibition in the presence of 1.0 M NaCl, its specific elution at 1.5 M NaCl on heparin-Sepharose 4B column and its requirement for serum in the assay mixture to manifest its activity.	Heparin	142-149	lipoprotein lipase	Rattus norvegicus	0-18
3970857-0	1985	Purification of antithrombin "Vicenza": a molecule with normal heparin affinity and impaired reactivity to thrombin.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	20-28
2982601-2	1985	Human plasma fibronectin is composed of at least five distinct domains which we refer to as Hep-1/Fib-1, Gel, Cell, Hep-2 and Fib-2 depending on their affinity for heparin (Hep), gelatin (Gel), the cell surface (Cell) or fibrin (Fib).	Heparin	164-171	fibronectin 1	Homo sapiens	13-24
2982601-2	1985	Human plasma fibronectin is composed of at least five distinct domains which we refer to as Hep-1/Fib-1, Gel, Cell, Hep-2 and Fib-2 depending on their affinity for heparin (Hep), gelatin (Gel), the cell surface (Cell) or fibrin (Fib).	Heparin	164-171	protocadherin gamma subfamily B, 4	Homo sapiens	126-131
2982601-2	1985	Human plasma fibronectin is composed of at least five distinct domains which we refer to as Hep-1/Fib-1, Gel, Cell, Hep-2 and Fib-2 depending on their affinity for heparin (Hep), gelatin (Gel), the cell surface (Cell) or fibrin (Fib).	Heparin	92-95	fibronectin 1	Homo sapiens	13-24
3886542-6	1985	A certain amount of the opsonin, fibronectin, is heparin-precipitable in normal serum and has thus retained its native character, while the fibronectin in the commercial serum preserve examined is not heparin-precipitable.	Heparin	49-56	fibronectin 1	Homo sapiens	33-44
3972103-2	1985	The exact role of the heparin-releasable hepatic endothelial lipase has remained controversial.	Heparin	22-29	lipase G, endothelial type	Homo sapiens	49-67
3838317-3	1985	Inhibition of thrombin by heparin cofactor II and heparin was completely prevented by purified histidine-rich glycoprotein at the ratio of 13 micrograms histidine-rich glycoprotein/microgram heparin.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	14-22
3917457-8	1985	These data suggest that plasma FFA elevations induced by lipid-heparin infusion inhibit GH secretion induced by GHRH.	Heparin	63-70	growth hormone releasing hormone	Homo sapiens	112-116
3838317-5	1985	Removal of 85-90% of the histidine-rich glycoprotein from plasma resulted in a fourfold reduction in the amount of heparin required to prolong the thrombin clotting time from 14 s to greater than 180 s but had no effect on the amount of dermatan sulfate required for similar anti-coagulant activity.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	147-155
3838317-6	1985	In contrast to histidine-rich glycoprotein, purified platelet factor 4 prevented inhibition of thrombin by heparin cofactor II in the presence of either heparin or dermatan sulfate at the ratio of 2 micrograms platelet factor 4/micrograms glycosaminoglycan.	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	95-103
3838317-7	1985	Furthermore, the supernatant medium from platelets treated with arachidonic acid to cause secretion of platelet factor 4 prevented inhibition of thrombin by heparin cofactor II in the presence of heparin or dermatan sulfate.	Heparin	157-164	coagulation factor II, thrombin	Homo sapiens	145-153
2578296-0	1985	Kinetic analysis of various heparin fractions and heparin substitutes in the thrombin inhibition reaction.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	77-85
3973025-0	1985	Effect of heparin-induced lipolysis on the distribution of apolipoprotein e among lipoprotein subclasses.	Heparin	10-17	apolipoprotein E	Homo sapiens	59-75
3973025-6	1985	When lipolysis of VLDL was enhanced in these subjects upon release of lipoprotein lipase by intravenous heparin, a shift of the apo E from VLDL into fractions II and III was observed.	Heparin	104-111	apolipoprotein E	Homo sapiens	128-133
3973025-9	1985	Release of hepatic triglyceride lipase by heparin injection in these subjects produced a shift of apo E from fraction I to III with no significant increase in fraction II.	Heparin	42-49	apolipoprotein E	Homo sapiens	98-103
3973461-5	1985	Heparin-like catalytic activity of these materials (assayed by measuring the generation of thrombin-antithrombin complex in plasma) correlated well with the amount of heparin bound, but not as well with AT binding capacity.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	91-99
2578296-0	1985	Kinetic analysis of various heparin fractions and heparin substitutes in the thrombin inhibition reaction.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	77-85
2578296-7	1985	Substitute heparins and depolymerized heparin were poor catalysts for thrombin inhibition, due at least partially to their affinity for thrombin.	Heparin	11-19	coagulation factor II, thrombin	Homo sapiens	70-78
2578296-7	1985	Substitute heparins and depolymerized heparin were poor catalysts for thrombin inhibition, due at least partially to their affinity for thrombin.	Heparin	11-19	coagulation factor II, thrombin	Homo sapiens	136-144
2578296-7	1985	Substitute heparins and depolymerized heparin were poor catalysts for thrombin inhibition, due at least partially to their affinity for thrombin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	70-78
2578296-7	1985	Substitute heparins and depolymerized heparin were poor catalysts for thrombin inhibition, due at least partially to their affinity for thrombin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	136-144
2578296-8	1985	This latter binary interaction inhibits thrombin reaction in the heparin-catalyzed reaction.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	40-48
3913282-13	1985	The concentration of t-PA antigen showed a significant increase during heparin infusion, whereas that of PAP and t-PA inhibitor was not influenced.	Heparin	71-78	plasminogen activator, tissue type	Homo sapiens	21-25
2579452-6	1985	Heparin injection has the same effect, more prolonged, as pentosan polysulphate on thrombin generation but is not so effective on impairing factor Xa generation (27% of inhibition).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	83-91
3981950-4	1985	Highly significant differences were found between UF and LMW heparin in their effects on PTT and thrombin time.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	97-105
3965464-6	1985	Kinetic studies of thrombin inactivation by both antithrombins, in the presence of nonsaturating amounts of heparin, indicated that AT-III beta inhibited thrombin more rapidly.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	19-27
2944348-2	1985	Heparin, at a catalytic amount, increases primarily the inactivation rate of thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	77-85
2944348-3	1985	The two proteinases compete for heparin, i.e. heparin is preferably attached by thrombin.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	80-88
2944348-5	1985	However, at high concentration of heparin, plasmin inactivation by antithrombin III is accelerated even in the presence of fibrinogen or fibrin.	Heparin	34-41	fibrinogen beta chain	Homo sapiens	123-133
2409857-8	1985	Follicular PP5, like antithrombin III, interacted reversibly with heparin and thrombin affinity matrices, suggesting a potential biological role as a follicular anticoagulant, whereas PAPP-A, a specific and potent inhibitor of leukocyte elastase, contributes to the maintenance of proteolytic homeostasis and the protection of spermatozoa and embryo against proteolytic attack originating from the maternal leukocytes.	Heparin	66-73	tissue factor pathway inhibitor 2	Homo sapiens	11-14
3965218-5	1985	Oleate decreased the values, indicating that intravenous heparin, which releases endothelial lipase, causing in vitro lipolysis, should be avoided if indwelling catheters are used for sampling, e.g., during provocation tests for gastrin release.	Heparin	57-64	lipase G, endothelial type	Homo sapiens	81-99
4026390-4	1985	Although PP5 binds to heparin, it does not show any heparin-cofactor activity.	Heparin	22-29	tissue factor pathway inhibitor 2	Homo sapiens	9-12
3966907-5	1985	Pretreatment of HSF with 50 microM verapamil for 24 hours and incubation with 2 to 50 micrograms 125I-LDL protein/ml for 1 hour resulted in a 50% to 200% increase in heparin releasable and in a 40% to 130% increase in cellular 125I-LDL.	Heparin	166-173	interleukin 6	Homo sapiens	16-19
2416032-4	1985	Affinity interactions between PP5 and matrices such as heparin or thrombin-Sepharose were similar and independent of the origin of PP5.	Heparin	55-62	tissue factor pathway inhibitor 2	Homo sapiens	30-33
2931844-2	1985	The method is based on precipitation at 4 degrees C of plasma fibronectin and associated macromolecular complexes by means of heparin.	Heparin	126-133	fibronectin 1	Homo sapiens	62-73
6508799-2	1984	Macrophages prepared from rat lungs released a considerable amount of lipoprotein lipase, with characteristics similar to those of the lipoprotein lipase released from heparin-perfused rat lungs.	Heparin	168-175	lipoprotein lipase	Rattus norvegicus	135-153
6522147-9	1984	The parallel increases in LPL content of peripheral tissues and PHLA suggest that in all age groups heparin-induced release of LPL into the circulation is proportional to tissue lipolytic activity.	Heparin	100-107	lipoprotein lipase	Rattus norvegicus	26-29
6522147-9	1984	The parallel increases in LPL content of peripheral tissues and PHLA suggest that in all age groups heparin-induced release of LPL into the circulation is proportional to tissue lipolytic activity.	Heparin	100-107	lipoprotein lipase	Rattus norvegicus	127-130
6441307-0	1984	Specific fibrinogen quantitation by electroimmunodiffusion in agarose gel containing heparin.	Heparin	85-92	fibrinogen beta chain	Homo sapiens	9-19
6441307-1	1984	In the determination of plasma fibrinogen by electroimmunodiffusion, commercial sodium heparin, previously included in the agarose gel, by interacting with fibrinogen molecules, enhances their anodic mobility more strongly than after carbamylation with potassium cyanate.	Heparin	80-94	fibrinogen beta chain	Homo sapiens	31-41
6441307-1	1984	In the determination of plasma fibrinogen by electroimmunodiffusion, commercial sodium heparin, previously included in the agarose gel, by interacting with fibrinogen molecules, enhances their anodic mobility more strongly than after carbamylation with potassium cyanate.	Heparin	80-94	fibrinogen beta chain	Homo sapiens	156-166
6393995-1	1984	Fibronectin was extracted from normal and atherosclerotic areas of human aorta by urea and heparin and sonication of the tissue.	Heparin	91-98	fibronectin 1	Homo sapiens	0-11
6512326-5	1984	While placing her on replacement and adjunctive therapies the laboratory tests were performed serially, which permitted a close follow-up observation of the subsequent progress of DIC with the detection of lowered platelet counts and fibrinogen levels as administration of Heparin resulted in an increase in the amount of bleeding, FOY, 800mg/day, was instituted and following this treatment the DIC disappeared.	Heparin	273-280	fibrinogen beta chain	Homo sapiens	234-244
6512326-5	1984	While placing her on replacement and adjunctive therapies the laboratory tests were performed serially, which permitted a close follow-up observation of the subsequent progress of DIC with the detection of lowered platelet counts and fibrinogen levels as administration of Heparin resulted in an increase in the amount of bleeding, FOY, 800mg/day, was instituted and following this treatment the DIC disappeared.	Heparin	273-280	solute carrier family 25 member 10	Homo sapiens	396-399
6498225-3	1984	Heparin inhibits aggregation induced by thrombin in the presence of plasma, but it is uneffective, or sometimes stimulates aggregation, in the absence of plasma.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	40-48
6523441-3	1984	Linear relationships were observed between the molecular weight of the heparin fractions and the anti-coagulant activities as determined by thrombin time- and APTT-assay and the classical complement pathway inhibitory activity.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	140-148
6523442-8	1984	In contrast, in the presence of heparin the rate of inactivation of modified and unmodified thrombins by antithrombin III are not significantly different.	Heparin	32-39	serpin family C member 1	Bos taurus	105-121
6523442-9	1984	Thus, the heparin-sensitized inactivation of thrombin by antithrombin III is affected by the modification of one tryptophan residue.	Heparin	10-17	serpin family C member 1	Bos taurus	57-73
6487647-3	1984	Rat HDL was isolated at d 1.085-1.21 g/ml and apolipoprotein E-free HDL was prepared by heparin Sepharose chromatography.	Heparin	88-95	apolipoprotein E	Rattus norvegicus	46-62
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	65-73
6084320-4	1984	Heparin inhibited both the random migration and directed locomotion of human neutrophils toward zymosan-activated serum (ZAS) and F-met-leu-phe (FMLP).	Heparin	0-7	formyl peptide receptor 1	Homo sapiens	145-149
6084320-7	1984	When added directly to the chamber containing chemotactic factor, heparin inhibited the chemotactic activity of ZAS but not that of FMLP, suggesting a direct inhibitory effect against C5a, the principal chemotactic factor in ZAS.	Heparin	66-73	complement C5a receptor 1	Homo sapiens	184-187
6475940-2	1984	Results indicate that, although heparin causes a mild potentiation of platelet aggregation in the PRP systems, a significant inhibitory activity is observed when heparin is added to isolated platelets.	Heparin	32-39	prion protein	Homo sapiens	98-101
6497883-1	1984	Antiserum against a 23Kd heparin binding fragment of thrombospondin inhibits the aggregation of platelets in response to ADP, collagen or thrombin.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	138-146
6475940-4	1984	Although heparin-mediated inhibitory activity can be demonstrated in the presence of a number of different agonists (ADP, arachidonic acid, thrombin, Ionophore A23187, epinephrine, and ristocetin), the most pronounced inhibition is seen in the presence of ristocetin.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	140-148
6509363-0	1984	Effects of heparin fractions of different affinities to antithrombin III and thrombin on the inactivation of thrombin and factor Xa by antithrombin III.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	60-68
6509363-1	1984	To investigate the relative contribution of heparin-binding thrombin and antithrombin III to the enhancement of the rate of inactivation of thrombin by antithrombin III, standard heparin was fractionated on matrix-linked thrombin and (or) antithrombin III.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	60-68
6509363-2	1984	There was a good correlation between heparin affinity for antithrombin III and its ability to enhance the inactivation of thrombin and factor Xa.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	62-70
6509363-3	1984	In addition, there was a good correlation between affinity of heparin for thrombin and its catalytic activity on the inactivation of thrombin by antithrombin III.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	74-82
6509363-3	1984	In addition, there was a good correlation between affinity of heparin for thrombin and its catalytic activity on the inactivation of thrombin by antithrombin III.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	133-141
6509363-7	1984	A heparin fraction with very low affinity to thrombin and high affinity to antithrombin III was prepared by repeated fractionation of a low molecular weight heparin on the two affinity columns.	Heparin	2-9	coagulation factor II, thrombin	Homo sapiens	45-53
6479461-3	1984	Effect on binding was assessed with affinity chromatography on heparin-Sepharose and gelatin-Sepharose, and with an in vitro assay that detects complexation of fibronectin with [3H]-heparin.	Heparin	182-189	fibronectin 1	Homo sapiens	160-171
6479461-5	1984	Inhibition of heparin binding in the in vitro assay was observed even with levels of glycosylation about threefold those of control, which is comparable to the degree of glycosylation determined in fibronectin isolated from plasma of two patients with uncontrolled diabetes.	Heparin	14-21	fibronectin 1	Homo sapiens	198-209
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	146-154
6237929-4	1984	Lysis mediated by an IgG monoclonal antibody (J5) to the common acute lymphoblastic leukemia antigen (CALLA) was more sensitive to heparin inhibition than that due to an IgM antibody (VIL A1).	Heparin	131-138	membrane metalloendopeptidase	Homo sapiens	57-100
6237929-4	1984	Lysis mediated by an IgG monoclonal antibody (J5) to the common acute lymphoblastic leukemia antigen (CALLA) was more sensitive to heparin inhibition than that due to an IgM antibody (VIL A1).	Heparin	131-138	membrane metalloendopeptidase	Homo sapiens	102-107
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	162-170
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	207-214	coagulation factor II, thrombin	Homo sapiens	146-154
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	207-214	coagulation factor II, thrombin	Homo sapiens	162-170
6520110-0	1984	A method to determine the affinity of heparin to thrombin and antithrombin III on equilibrium gel permeation chromatography.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	49-57
6520110-1	1984	Equilibrium gel permeation chromatography was employed to determine the ability of heparin to form complexes with thrombin and antithrombin III.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	114-122
6520110-2	1984	In the eluate from a Sephacryl S-200 column, heparin caused a peak and then a trough in the fluorescence of 48 nM antithrombin III or 63 nM thrombin.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	118-126
6480826-5	1984	The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody.	Heparin	117-124	apolipoprotein E	Homo sapiens	42-47
6520110-5	1984	The ability to form a complex of heparin preparations with different anticoagulant activities for thrombin and antithrombin III could be determined satisfactorily.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	98-106
6520110-7	1984	Of 4 preparations with one low-affinity and three high-affinity subfractions of heparin for antithrombin III, the species with the lowest affinity for antithrombin III had the highest affinity for thrombin.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	96-104
6480826-5	1984	The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody.	Heparin	117-124	apolipoprotein E	Homo sapiens	42-47
6480826-5	1984	The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody.	Heparin	117-124	apolipoprotein E	Homo sapiens	18-23
6480830-5	1984	Heparin-releasable plasma lipoprotein lipase and hepatic lipase activities were decreased by 50% in nephrotic rats compared with pair-fed controls.	Heparin	0-7	lipase C, hepatic type	Rattus norvegicus	49-63
6480826-5	1984	The new series of apo E components, named apo E-Suita, was identical with the ordinary apo E in its interaction with heparin-Sepharose gel and with anti-apo E antibody.	Heparin	117-124	apolipoprotein E	Homo sapiens	42-47
6480830-9	1984	Heparin treatment did not restore to normal the decreased apo BL clearance in nephrotic rats but it produced an increased amount of apo A-IV and apo E in the plasma HDL.	Heparin	0-7	apolipoprotein A4	Rattus norvegicus	132-140
6383479-1	1984	A polypeptide proteinase inhibitor from human articular cartilage has been purified to homogeneity by stepwise Sephadex G-75, heparin-Sepharose and octyl-Sepharose affinity chromatography.	Heparin	126-133	endogenous retrovirus group K member 25	Homo sapiens	14-24
6482738-14	1984	Heparin-releasable LPL activity in exercised ER rats (65.3 +/- 5.7 units) was 43% higher than in exercised M rats (45.5 +/- 5.6 units) and 53% higher than in OI female rats (42.6 +/- 8.1 units).	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-22
6484489-5	1984	The assay was also applied to determine the structure-function relationship of heparin and heparansulphate in activation of fibronectin.	Heparin	79-86	fibronectin 1	Homo sapiens	124-135
6484489-7	1984	Only a small fraction of the heparin was actually capable of activating fibronectin.	Heparin	29-36	fibronectin 1	Homo sapiens	72-83
6484489-8	1984	It is concluded that the assay is very convenient to detect biological active fibronectin and to elucidate the structure-function relationship of heparin and heparansulphate in activating fibronectin.	Heparin	146-153	fibronectin 1	Homo sapiens	78-89
6484489-8	1984	It is concluded that the assay is very convenient to detect biological active fibronectin and to elucidate the structure-function relationship of heparin and heparansulphate in activating fibronectin.	Heparin	146-153	fibronectin 1	Homo sapiens	188-199
6235872-2	1984	In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	70-78
6209818-0	1984	Abolition by dextran sulfate of the heparin-accelerated antithrombin III/thrombin reaction.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	60-68
6209818-4	1984	These findings indicate that binding of dextran sulfate to a site other than the active site of thrombin to prevent the approach of AT III in the presence of heparin.	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	96-104
6468662-0	1984	Binding of fibronectin to gelatin and heparin: effect of surface denaturation and detergents.	Heparin	38-45	fibronectin 1	Homo sapiens	11-22
6506022-5	1984	Native HUV and heparin treated graft surfaces adsorbed and inactivated thrombin, whereas non-heparinized and saline-alcohol treated grafts inactivated surface-bound thrombin to only a small degree.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	71-79
6506022-6	1984	Surface-bound LMW heparin exhibited a significantly lower ability to inactivate thrombin as compared with conventional heparin, but LMW heparin-alcohol surfaces were better than non-heparinized ones.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	80-88
6506022-7	1984	Protamine treatment of "heparinized" surfaces impaired the thrombin inhibiting ability of the heparin-alcohol surface, whereas this property was totally abolished for the LMW heparin-alcohol surface.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	59-67
6506022-7	1984	Protamine treatment of "heparinized" surfaces impaired the thrombin inhibiting ability of the heparin-alcohol surface, whereas this property was totally abolished for the LMW heparin-alcohol surface.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	59-67
6506022-8	1984	The findings indicate that LMW heparin, despite its weaker thrombin inhibiting capacity, may be an alternative to conventional heparin, for "heparinizing" the human umbilical vein graft.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	59-67
6486808-2	1984	This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease inhibitor for mucopolysaccharide.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	85-93
6235872-2	1984	In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	70-78
6091291-4	1984	Heparin (25-500 micrograms/ml) was able to inhibit in a dose-dependent way cellular aggregation and degranulation induced either by FMLP or by zymosan-activated serum.	Heparin	0-7	formyl peptide receptor 1	Homo sapiens	132-136
6500033-2	1984	Heparin exerts an inhibitory action on the thrombin-induced aggregation, which seems likely to be associated with its inhibitory effect on thrombin, an inducer of aggregation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	43-51
6500033-2	1984	Heparin exerts an inhibitory action on the thrombin-induced aggregation, which seems likely to be associated with its inhibitory effect on thrombin, an inducer of aggregation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	139-147
6091291-5	1984	FMLP-dependent superoxide anion generation and chemiluminescence were specifically inhibited by heparin at the concentration of 25 micrograms/ml.	Heparin	96-103	formyl peptide receptor 1	Homo sapiens	0-4
6203552-3	1984	After interruption of enzyme synthesis by cycloheximide, plateauing of enzyme activity in the medium occurred, indicating that addition of heparin may not only stabilize but also enhance hepatic triacylglycerol lipase secretion.	Heparin	139-146	lipase C, hepatic type	Rattus norvegicus	187-217
6236212-1	1984	Calcium-replete thrombospondin has been purified from outdated platelets using heparin-Sepharose affinity chromatography, gelatin-Sepharose to remove fibronectin, and gel filtration to eliminate low-molecular-weight heparin-binding proteins.	Heparin	79-86	thrombospondin 1	Homo sapiens	16-30
6236212-9	1984	Automated Edman degradation in a vapor-phase sequenator of the thermolytic heparin-binding domain electroeluted from sodium dodecyl sulfate-gels indicates that the heparin-binding domain resides at the amino terminus of the Mr 180,000 TSP peptide chain.	Heparin	75-82	thrombospondin 1	Homo sapiens	235-238
6236212-9	1984	Automated Edman degradation in a vapor-phase sequenator of the thermolytic heparin-binding domain electroeluted from sodium dodecyl sulfate-gels indicates that the heparin-binding domain resides at the amino terminus of the Mr 180,000 TSP peptide chain.	Heparin	164-171	thrombospondin 1	Homo sapiens	235-238
6747440-8	1984	Kinetic studies in the absence and in the presence of heparin indicated that the fraction of antithrombin III that could inactivate thrombin was functionally normal.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	97-105
6743573-6	1984	This effect was seen when assaying heparin by the aPTT and thrombin time.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	59-67
6743573-13	1984	There was a significant difference between heparin activities measured in the CIT+ (secreted PF4 58 ng/ml) and CIT60 (secreted PF4 1074 ng/ml) plasma samples by both thrombin time and Xa inactivation.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	166-174
6379981-0	1984	A survey of surface hemorheological experiments on the inhibition of fibrinogenin formation employing surface layers of fibrinogen systems with heparins and other substances.	Heparin	144-152	fibrinogen beta chain	Homo sapiens	69-79
6379981-4	1984	In subsequent studies of the viscoelasticity of surface layers of highly purified fibrinogen (97-100% clottability) of human and bovine origin, we found, with some heparins, marked lowering of surface viscous moduli (eta"s) and of surface elastic moduli (Gs).	Heparin	164-172	fibrinogen beta chain	Homo sapiens	82-92
6379981-10	1984	Preparations of fibrinogen in dog plasma, to which sodium heparin was added, resulted in a decrease of tau values.	Heparin	51-65	fibrinogen beta chain	Homo sapiens	16-26
6206589-0	1984	Inhibition of thrombin-induced platelet aggregation and serotonin release by antithrombin III and heparin cofactor II in the presence of standard heparin, dermatan sulfate and pentosan polysulfate.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	14-22
6732819-6	1984	There was a definite enhancement of lipoprotein lipase activity in the combined P17 /100 fraction after the lipase activity has been washed out from the capillary bed with heparin.	Heparin	172-179	lipoprotein lipase	Rattus norvegicus	36-54
6734448-2	1984	Global clotting activity, measured as activated partial thromboplastin time as well as thrombin activity were inhibited almost equally by commercial and low-molecular heparin.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	87-95
6375731-0	1984	Effects of hormones, amino acids and specific inhibitors on rat heart heparin-releasable lipoprotein lipase and tissue neutral lipase activities during long-term perfusion.	Heparin	70-77	lipoprotein lipase	Rattus norvegicus	89-107
6474452-5	1984	Heparin-releasable lipoprotein lipase activity in epididymal adipose tissue, lipoprotein lipase activity in post-heparin plasma, and VLDL-triolein hydrolyzing activity in adipose tissue stromal vessels were all higher in niceritrol-treated atherosclerotic rats.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-37
6740570-0	1984	Reactivity of heparin with the human plasma heparin-binding proteins thrombin, antithrombin III, and apolipoproteins E and B-100.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	69-77
6740570-0	1984	Reactivity of heparin with the human plasma heparin-binding proteins thrombin, antithrombin III, and apolipoproteins E and B-100.	Heparin	14-21	apolipoprotein E	Homo sapiens	101-128
6740570-1	1984	The heparin-binding properties of human plasma apolipoproteins B-100 and E (apoB-100 and E) of low density lipoproteins (LDL), thrombin, and antithrombin-III (AT-III) were investigated.	Heparin	4-11	apolipoprotein B	Homo sapiens	76-90
6740570-2	1984	A highly reactive heparin (HRH) to apoB-100 was isolated by chromatography of crude heparin on a column of LDL immobilized to Affi-Gel 10.	Heparin	18-25	apolipoprotein B	Homo sapiens	35-43
6202716-4	1984	In the presence of heparin, virtually 100% of the 125I-Factor IXa was bound to ATIII by 1 min.	Heparin	19-26	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	79-84
6748637-0	1984	Heparin-mediated inactivation and transformation of mammary cytoplasmic glucocorticoid receptor.	Heparin	0-7	nuclear receptor subfamily 3, group C, member 1	Mus musculus	72-95
6748637-1	1984	Glucocorticoid receptor of lactating mouse mammary gland cytosol was exposed to heparin when the receptor was either steroid-free or steroid-bound.	Heparin	80-87	nuclear receptor subfamily 3, group C, member 1	Mus musculus	0-23
6725246-9	1984	Incubation of radiolabeled normal proapo -A-I in normal plasma anticoagulated with heparin was associated with progressive conversion to mature apo-A-I over 24 h (initially 85% of the radioactivity was in the proapo -A-I isoform; at 24 h 33% radioactivity remained in the pro-isoform).	Heparin	83-90	apolipoprotein A1	Homo sapiens	144-151
6204398-7	1984	It was concluded that molecular alteration of the antithrombin molecule seemed to affect only the heparin binding site thus preventing from any rate enhancement of thrombin inactivation.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	54-62
6430120-1	1984	Human milk lysozyme was purified by heparin-Sepharose affinity chromatography and Sepharose 4B gel-permeation chromatography.	Heparin	36-43	lysozyme	Homo sapiens	11-19
6370664-3	1984	Lipoprotein lipase was measured in three functional compartments: 1) enzyme activity secreted into the culture medium, 2) activity releasable from cell suspensions by heparin, and 3) activity extractable from cells (after maximal heparin release) in deoxycholate and detergent.	Heparin	167-174	lipoprotein lipase	Rattus norvegicus	0-18
6372894-0	1984	[Role of heparin in the realization of the hypoglycemic action of insulin].	Heparin	9-16	insulin	Homo sapiens	66-73
6372894-1	1984	The presence of reactive heparin in blood circulation is necessary for realization of the hypoglycemic action of insulin.	Heparin	25-32	insulin	Homo sapiens	113-120
6372894-3	1984	In animals with different basal concentration of heparin in the blood, the blockade of insulin action is attained by application of different doses of protamin sulfate, respectively.	Heparin	49-56	insulin	Homo sapiens	87-94
6372894-4	1984	Based on the data obtained one can determine an approximate blood heparin concentration necessary for realization of the hypoglycemic action of insulin.	Heparin	66-73	insulin	Homo sapiens	144-151
6715365-0	1984	Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	75-83
6715365-0	1984	Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	75-83
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	50-58
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	50-58
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	50-58
6715365-5	1984	The bimolecular rate constants for the complexes with heparin of Mr = 4,300 and 3,200 are, respectively, 2 X 10(7) M-1 S-1 and 3 X 10(5) M-1 S-1.	Heparin	54-61	tumor associated calcium signal transducer 2	Homo sapiens	115-144
6715365-6	1984	Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic.	Heparin	75-82	coagulation factor II, thrombin	Homo sapiens	20-28
6715365-6	1984	Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic.	Heparin	190-197	coagulation factor II, thrombin	Homo sapiens	20-28
6715365-6	1984	Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic.	Heparin	190-197	coagulation factor II, thrombin	Homo sapiens	20-28
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	119-127
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	136-144
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	coagulation factor II, thrombin	Homo sapiens	136-144
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	coagulation factor II, thrombin	Homo sapiens	136-144
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	coagulation factor II, thrombin	Homo sapiens	136-144
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	coagulation factor II, thrombin	Homo sapiens	136-144
6715365-8	1984	Increasing the chain length of heparin results in an increased reaction rate because of a higher probability of interaction between thrombin and heparin in solution.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	132-140
6735346-4	1984	Furthermore, the soluble lipoprotein lipase of fat-pads was fractionated by heparin-Sepharose affinity chromatography.	Heparin	76-83	lipoprotein lipase	Rattus norvegicus	25-43
6735346-7	1984	The heterogeneity of lipoprotein lipase of rat adipose tissues was ensured using affinity chromatography on heparin-Sepharose.	Heparin	108-115	lipoprotein lipase	Rattus norvegicus	21-39
6370664-5	1984	Insulin, added the day after preparation, produced a dose-dependent (1-400 ng/ml) increase in lipoprotein lipase releasable from cells by heparin at 2, 4, and 24 h. Insulin also increased intracellular enzyme measured as deoxycholate-detergent-solubilized activity extracted from previously heparin-released cells.	Heparin	138-145	lipoprotein lipase	Rattus norvegicus	94-112
6370664-5	1984	Insulin, added the day after preparation, produced a dose-dependent (1-400 ng/ml) increase in lipoprotein lipase releasable from cells by heparin at 2, 4, and 24 h. Insulin also increased intracellular enzyme measured as deoxycholate-detergent-solubilized activity extracted from previously heparin-released cells.	Heparin	291-298	lipoprotein lipase	Rattus norvegicus	94-112
6729779-1	1984	injection of a thrombin-heparin mixture.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	15-23
6729779-4	1984	It was found that huge amounts of thrombin could be perfused, under the protection of heparin, without untoward effects.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	34-42
6729779-5	1984	But the high amount of thrombin needed to obtain a 50% reduction of the circulating AT III required a corresponding high amount of protective heparin.	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	23-31
6740558-1	1984	Addition of 0.05 IU of heparin per ml normal plasma prolongs its thrombin time from 20 to 27s , but that of plasma specifically depleted in histidine-rich glycoprotein (by immunoadsorption) from 20 to 180s .	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	65-73
6427377-2	1984	Plasma apoE and the primary translation product migrated similarly on SDS-polyacrylamide gels, had similar partial proteolytic peptide maps, and bound to and coeluted from heparin-Sepharose columns.	Heparin	172-179	apolipoprotein E	Rattus norvegicus	7-11
6740558-3	1984	In 54 plasma samples from hospitalized patients a significant negative correlation was found between the anticoagulant activity of heparin measured by thrombin inhibition and the plasma level of histidine-rich glycoprotein (r = 0.69).	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	151-159
6712330-4	1984	The first instrument separates plasma from whole blood using a pneumatic filtration principle, while the heparin assay system measures the effect of heparin on thrombin conversion of a synthetic fluorogenic substrate.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	160-168
6712330-4	1984	The first instrument separates plasma from whole blood using a pneumatic filtration principle, while the heparin assay system measures the effect of heparin on thrombin conversion of a synthetic fluorogenic substrate.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	160-168
6697455-1	1984	The plasma level of fibrinopeptide A (fpA) was used as an index of thrombin action on fibrinogen in order to investigate the rates of fibrin formation and the effect of heparin on thrombin in patients with acute myocardial infarction.	Heparin	169-176	coagulation factor II, thrombin	Homo sapiens	180-188
6697455-8	1984	These data demonstrate increased fibrin formation in patients with acute myocardial infarction and neutralization of thrombin in vivo by heparin.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	117-125
6546700-12	1984	However, thrombin Metz binds less tightly to a heparin-Sepharose column, and the direct inhibition of heparin on its activity on S2238 is weaker.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	9-17
6546700-12	1984	However, thrombin Metz binds less tightly to a heparin-Sepharose column, and the direct inhibition of heparin on its activity on S2238 is weaker.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	9-17
6721831-7	1984	An octadecasaccharide is therefore the smallest heparin fragment (prepared by nitrous acid depolymerization) that can accelerate thrombin inhibition by antithrombin III.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	129-137
6704414-8	1984	The labelled apolipoprotein B, retained by the heart, could be partially released by perfusion of the heart with buffer containing heparin (14 +/- 2%) or trypsin (50 +/- 2%).	Heparin	131-138	apolipoprotein B	Homo sapiens	13-29
6704414-12	1984	The data are consistent with the concept that the retention of apolipoprotein B requires membrane-bound lipoprotein lipase or an interaction with the cell surfaces that is modified by heparin.	Heparin	184-191	apolipoprotein B	Homo sapiens	63-79
6202294-6	1984	The rate of thrombin inhibition at 0.33 microM-heparin was reduced from 7.1 X 10(8) M-1 X min-1 in the absence of pentosan polysulphate to 2.3 X 10(8) M-1 X min-1 at 2 microM-pentosan polysulphate and to 0.3 X 10(8)M-1 X min-1 at 20 microM.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	12-20
6704408-4	1984	In the latter system the uptake of [32P]phosphatidylethanolamine was reduced by preperfusion with heparin to remove heparin-releasable hepatic lipase.	Heparin	98-105	lipase C, hepatic type	Rattus norvegicus	135-149
6704408-4	1984	In the latter system the uptake of [32P]phosphatidylethanolamine was reduced by preperfusion with heparin to remove heparin-releasable hepatic lipase.	Heparin	116-123	lipase C, hepatic type	Rattus norvegicus	135-149
6722255-1	1984	The inhibition of thrombin by antithrombin III is known to be accelerated by heparin through the formation of complexes between the muccopolysaccharide and both proteins.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	18-26
6742497-0	1984	[Relation of the formation of the fibrin network of a blood clot to the amount of thrombin in complexes with endogenous heparin].	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	82-90
6719397-2	1984	This variant is unlike those formerly described, as the plasma concentration is high, the thrombin inhibition with heparin is slow, and factor Xa inhibition is decreased.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	90-98
6725227-0	1984	Anticoagulant properties of heparin preparations from different animal sources with equivalent high affinity for antithrombin III.	Heparin	28-35	serpin family C member 1	Bos taurus	113-129
6719385-7	1984	However, Sepharose-coupled thrombin mixed with plasma in the presence of heparin produced outstanding quantities of residual immunoreactive AT III devoid of inhibitory activity.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	27-35
6719385-8	1984	These data suggest that presence of high affinity heparin in the environment of thrombin attached to a solid support may dramatically decrease the efficiency of enzyme inhibition.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	80-88
6706289-3	1984	The effects of NaCl, serum and heparin on TGL activities in heart muscle homogenates indicated the characteristics of lipoprotein lipase (LPL).	Heparin	31-38	lipoprotein lipase	Rattus norvegicus	118-136
6712769-4	1984	The new apolipoprotein component, named apo E-5, was identical with ordinary apo E in apparent molecular weight by SDS-polyacrylamide gel electrophoresis and in its interactions with heparin-Sepharose gel and with anti-apo E antibody.	Heparin	183-190	apolipoprotein E	Homo sapiens	40-45
6422851-6	1984	In the presence of heparin the inhibition of thrombin as well as factor Xa was enhanced.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	45-53
6230117-6	1984	These data along with a significant increase in the level of complex heparin compounds and plasma thrombin time indicate heparin release as a result of the effector action of the anticoagulation system.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	98-106
6706289-3	1984	The effects of NaCl, serum and heparin on TGL activities in heart muscle homogenates indicated the characteristics of lipoprotein lipase (LPL).	Heparin	31-38	lipoprotein lipase	Rattus norvegicus	138-141
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	60-68
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	60-68
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	191-199
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	60-68
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	191-199
6200322-3	1984	The 90 amino acid extra domain belongs to the so-called type III homology and it is located in the carboxy-terminal half of FN, in between the cell attachment and the heparin binding sites of the protein.	Heparin	167-174	fibronectin 1	Homo sapiens	124-126
6201043-0	1984	Heparin and plasma proteinase inhibitors: influence of heparin on the inhibition of thrombin by alpha 2 macroglobulin.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	84-92
6467514-1	1984	When cardiac muscle cells from mature rats were incubated in vitro in the presence of heparin (8.7 nmole ml-1) lipoprotein lipase activity appeared in the incubation medium.	Heparin	86-93	lipoprotein lipase	Rattus norvegicus	111-129
6701834-3	1984	New correlation equations were proposed firstly between metachromatic and thrombin time assays with heparin units, secondly between metachromatic and thrombin time assays.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	74-82
6541009-7	1984	Thrombin time seems to be the best coagulation test for adapting heparin doses.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	0-8
6083949-3	1984	Heparin potentiates the first aggregation step induced by ADP and epinephrine but inhibits aggregation induced by thrombin and ristocetin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	114-122
6083950-6	1984	The effective substances were related to heparin not only by the anticoagulant activity but also by the inhibitory action on the thrombin- and collagen-induced platelet aggregation.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	129-137
6530023-2	1984	The stimulatory effect of heparin on the activity of nonactivated phosphorylase kinase is also expressed in the presence of calmodulin and glycogen.	Heparin	26-33	calmodulin 1	Homo sapiens	124-134
6198531-8	1984	The therapeutic effects of heparin were assessed by prolonged APTT (45-250 sec) and elevated Anti-FXa activity (0.2-1.2 u/ml of plasma heparin concentration) as an indicator for the evaluation of anticoagulation activity and by normalized FPA, Fbg, FDP, Plg and AT III as an indicator for evaluation of antithrombolic activity.	Heparin	27-34	otoraplin	Homo sapiens	249-252
6735277-5	1984	The automated heparin assays that employ thrombin and Chromozym-Th or S-2238 were found to be most suitable for routine heparin determination.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	41-49
6382161-8	1984	The two most probable sites of action of heparin are: inhibition of thrombin and frustration of the feedback loops and/or inhibition of factor Xa.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	68-76
6607549-0	1984	Does qualitatively altered fibrinogen contribute to the increased heparin precipitable fraction (HPF) in acute myocardial infarction (AMI)?	Heparin	66-73	fibrinogen beta chain	Homo sapiens	27-37
6735276-1	1984	Spectrophotometric heparin assays which are based on the catalytic effect of heparin on either the inactivation of thrombin or that of factor Xa by antithrombin III, were adapted for use in a laboratory batch analyzer.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	115-123
6735276-1	1984	Spectrophotometric heparin assays which are based on the catalytic effect of heparin on either the inactivation of thrombin or that of factor Xa by antithrombin III, were adapted for use in a laboratory batch analyzer.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	115-123
6198746-11	1983	We conclude that plasma contains a component(s) which displaces (thrombin-antithrombin-III) complex from immobilised heparin: presumably this leaves the heparin sites free for further use in enzyme inactivation.	Heparin	117-124	coagulation factor II, thrombin	Homo sapiens	65-73
6198746-11	1983	We conclude that plasma contains a component(s) which displaces (thrombin-antithrombin-III) complex from immobilised heparin: presumably this leaves the heparin sites free for further use in enzyme inactivation.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	65-73
6689383-3	1983	Thrombin is then inhibited by antithrombin III and heparin, heparin neutralized by protamine sulfate, and protein C activity measured in the partial thromboplastin time.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	0-8
6363061-1	1983	Heparin is shown to produce modulatory effects on the amidolytic activity of trypsin, thrombin and plasmin with various synthetic peptide substrates.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	86-94
6643486-3	1983	In low ionic strength buffer, intact fibronectin bound to heparin and high sulfated heparan sulfate, but not to low sulfated heparan sulfate, dermatan sulfate, chondroitin sulfates A and C, or hyaluronic acid.	Heparin	58-65	fibronectin 1	Homo sapiens	37-48
6643486-5	1983	The 150K-140K fragments exhibited the same specificities as intact fibronectin, binding only to heparin and high sulfated heparan sulfate.	Heparin	96-103	fibronectin 1	Homo sapiens	67-78
6643486-10	1983	At physiologic ionic strength, only heparin-Sepharose could bind intact fibronectin.	Heparin	36-43	fibronectin 1	Homo sapiens	72-83
6229271-2	1983	The binding of gelatinized latex beads to liver slices as well as the internalization of these particles by macrophages, in the presence of heparin, is greatly enhanced by fibronectin.	Heparin	140-147	fibronectin 1	Homo sapiens	172-183
6643505-0	1983	A simple rate law that describes the kinetics of the heparin-catalyzed reaction between antithrombin III and thrombin.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	92-100
6643505-1	1983	The kinetics of the reaction between human thrombin and antithrombin III were studied in the presence of heparin fractionated according to its molecular size and affinity for antithrombin III.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	43-51
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	273-281
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	290-298
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	273-281
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	290-298
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	273-281
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	290-298
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	273-281
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	290-298
6689383-3	1983	Thrombin is then inhibited by antithrombin III and heparin, heparin neutralized by protamine sulfate, and protein C activity measured in the partial thromboplastin time.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	0-8
6317700-4	1983	In addition, whereas the ability of PN-I to link to thrombin is strongly modulated by heparin, PN-II and PN-III are essentially unaffected by heparin.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	52-60
6640109-8	1983	The functionally defective antithrombin molecules exhibit a reduced ability to neutralize thrombin in the presence or absence of heparin (approximately 10%-20% of normal).	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	31-39
6618271-4	1983	The increased fibrinogen deposition is abolished by treatment with low dose heparin.	Heparin	76-83	fibrinogen beta chain	Homo sapiens	14-24
6317205-0	1983	Heparin interaction with cultured cells: possible role of fibronectin in uncoupling surface binding and endocytosis.	Heparin	0-7	fibronectin 1	Homo sapiens	58-69
6138099-8	1983	We report here on investigations of plasma fibronectin that had been purified from the "heparin-precipitable fraction" of plasma by DEAE-cellulose chromatography using buffers containing a chaotropic salt (KSCN).	Heparin	88-95	fibronectin 1	Homo sapiens	43-54
6617646-3	1983	The structure of the 70-kDa gelatin-binding, 60-kDa central and 60-65-kDa heparin-binding fragments in solution appeared to be very close to that in the intact fibronectin.	Heparin	74-81	fibronectin 1	Homo sapiens	160-171
6195265-7	1983	Additionally, heparin was able to reduce the myeloperoxidase release from zymosan-stimulated neutrophils by nearly 50%.	Heparin	14-21	myeloperoxidase	Homo sapiens	45-60
6313674-1	1983	We have previously shown that a DNA topoisomerase I from mouse mammary carcinoma cells is inhibited by heparin.	Heparin	103-110	topoisomerase (DNA) I	Mus musculus	32-51
6624878-4	1983	Similarly, heparin also increased PMN degranulation and lactoferrin release following stimulation with FMLP with or without cytochalasin B, compared with controls.	Heparin	11-18	formyl peptide receptor 1	Homo sapiens	103-107
6640057-3	1983	In order to ascertain the heparin-like mechanism of this activity we have studied the interactions of thrombin and antithrombin III with two polymers of this series: sulphonated polystyrene and sulphonate-glutamic acid sulphonamide polystyrene.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	102-110
6641987-0	1983	[Neutralization of thrombin by antithrombin III in the presence of heparin in cobra venom poisoning].	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	19-27
6604220-7	1983	The independence of the new thrombin inhibitor from heparin control explains the bleeding disorder; it also indicates that heparin normally acts directly on antithrombin III, revealing its inherent inhibitory activity.	Heparin	52-59	coagulation factor II, thrombin	Homo sapiens	28-36
6605159-0	1983	Action of heparin on the inhibition of thrombin by alpha 1-proteinase inhibition.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	39-47
6605159-4	1983	The second-order rate constant under the conditions studied was 6.64 X 10(3) M-1 min-1, and heparin was found to cause a decrease in the rate constant.	Heparin	92-99	myoregulin	Homo sapiens	77-86
6605159-5	1983	On the basis of the concentrations used, the kinetics of thrombin inhibition, both in the absence and in the presence of heparin, can be described by a one-step reaction.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	57-65
6605159-6	1983	The effect of heparin is due to its binding to thrombin.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	47-55
6605159-7	1983	The degree to which heparin interferes with the rate of thrombin inhibition depends on its molecular weight but not on its anticoagulant activity.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	56-64
6605159-8	1983	Thus, in the presence of 11.7K and 22K heparins the respective rate constants are 3.5 X 10 and 1.0 X 10(3) M-1 min-1.	Heparin	39-47	myoregulin	Homo sapiens	107-116
6604220-7	1983	The independence of the new thrombin inhibitor from heparin control explains the bleeding disorder; it also indicates that heparin normally acts directly on antithrombin III, revealing its inherent inhibitory activity.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	28-36
6309278-5	1983	The effect of thrombin was inhibited by preincubation of thrombin with hirudin or antithrombin III plus heparin or by preincubation of the monolayers with dibutyryl cyclic adenosine monophosphate (dbcAMP).	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	14-22
6885787-17	1983	These include: 1) formation of sodium dodecyl sulfate-stable complexes with thrombin, urokinase, and plasmin; 2) inhibition of protease activity; 3) heparin-enhanced inhibition of thrombin; and 4) cellular binding of protease-PN complexes in a heparin-sensitive reaction.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	76-84
6885787-17	1983	These include: 1) formation of sodium dodecyl sulfate-stable complexes with thrombin, urokinase, and plasmin; 2) inhibition of protease activity; 3) heparin-enhanced inhibition of thrombin; and 4) cellular binding of protease-PN complexes in a heparin-sensitive reaction.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	180-195
6885787-17	1983	These include: 1) formation of sodium dodecyl sulfate-stable complexes with thrombin, urokinase, and plasmin; 2) inhibition of protease activity; 3) heparin-enhanced inhibition of thrombin; and 4) cellular binding of protease-PN complexes in a heparin-sensitive reaction.	Heparin	244-251	coagulation factor II, thrombin	Homo sapiens	76-84
6885787-17	1983	These include: 1) formation of sodium dodecyl sulfate-stable complexes with thrombin, urokinase, and plasmin; 2) inhibition of protease activity; 3) heparin-enhanced inhibition of thrombin; and 4) cellular binding of protease-PN complexes in a heparin-sensitive reaction.	Heparin	244-251	coagulation factor II, thrombin	Homo sapiens	180-195
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	43-51
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	56-64
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	43-51
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	56-64
6625618-1	1983	The present study has shown that calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	76-84
6625618-2	1983	The initial rate of thrombin (4.0 nM) inhibition by antithrombin III (200 nM) in the presence of heparin (2.5 ng/ml) decreased from 3.6 nM/min (in the absence of calcium) to 0.12 nM/min in the presence of 10 mM calcium.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	20-28
6625618-4	1983	The heparin-catalyzed antithrombin III/thrombin reaction is described by the general rate equation for a random-order, bireactant, enzyme-catalyzed reaction (M. J. Griffith (1982) J. Biol.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	26-34
6427596-7	1983	The immediate needs for treatment of DIC are (1) a cure of underlying infection by surgical drainage and chemotherapy, and (2) inhibition of intravascular coagulation by use of heparin and/or FOY etc.	Heparin	177-184	solute carrier family 25 member 10	Homo sapiens	37-40
6625618-8	1983	The apparent kinetic parameters for the heparin-catalyzed antithrombin III/thrombin reaction were determined in the presence and absence of calcium.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	62-70
6688430-2	1983	To better understand how heparin structure affects its activity the relationships between the functional domains for inhibitor binding and charge density were investigated to determine how these domains affect heparin-mediated thrombin inhibition by two different heparin-dependent protease inhibitors, antithrombin (AT) and heparin cofactor II (HC II).	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	227-235
6882786-0	1983	Heparin-independent release of lipoprotein lipase activity from perfused rat hearts.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	31-49
6577437-6	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and heparin cofactor II/thrombin reactions differed in terms of apparent Vmax and apparent heparin-inhibitor dissociation constant values.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	53-61
6577437-6	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and heparin cofactor II/thrombin reactions differed in terms of apparent Vmax and apparent heparin-inhibitor dissociation constant values.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	66-74
6648899-2	1983	Ten patients participated in this study which evaluated the effect of two heparin dose regimes, a high dose regime (mean dose 6750 IU) and a low dose regime (mean dose 3750 IU), on the thrombin activity, achieved during a 4-hour-dialysis.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	185-193
6577437-4	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and antithrombin III/factor Xa reactions differed in terms of apparent maximum velocity (Vmax) and apparent heparin-protease dissociation constant values.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	53-61
6882786-1	1983	Heparin-independent release of lipoprotein lipase activity from isolated perfused rat hearts was measured and related to the rapid turnover of the enzyme.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	31-49
6615820-0	1983	Biochemical and immunological characterization of three binding sites on human plasma fibronectin with different affinities for heparin.	Heparin	128-135	fibronectin 1	Homo sapiens	86-97
6882786-6	1983	Lipoprotein lipase activity in the 1-min heparin-releasable (extracellular) and residual (intracellular) compartment remained stable during the last 40 min of nonheparin perfusion.	Heparin	41-48	lipoprotein lipase	Rattus norvegicus	0-18
6615439-0	1983	Properties of antithrombin-thrombin complex formed in the presence and in the absence of heparin.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	18-26
6347123-3	1983	We found no significant difference in the incidence of thromboembolism between the two groups but a higher incidence of abnormal fibrinogen uptake test results in patients given heparin alone.	Heparin	178-185	fibrinogen beta chain	Homo sapiens	129-139
6615439-2	1983	Monomeric antithrombin-thrombin complexes formed in the presence and in the absence of heparin had similar conformations and heparin affinities.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	14-22
6615439-2	1983	Monomeric antithrombin-thrombin complexes formed in the presence and in the absence of heparin had similar conformations and heparin affinities.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	14-22
6347476-3	1983	The binding of myeloma IgG to solid phase fibronectin could be inhibited by soluble fibronectin and gelatin, but not by heparin or bovine serum albumin.	Heparin	120-127	fibronectin 1	Homo sapiens	42-53
6883717-1	1983	When protamine sulfate was added to heparinized plasma in vitro for neutralization of heparin, the activities on both thrombin and Xa known as heparin cofactor in antithrombin action were completely abolished.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	118-126
6883717-1	1983	When protamine sulfate was added to heparinized plasma in vitro for neutralization of heparin, the activities on both thrombin and Xa known as heparin cofactor in antithrombin action were completely abolished.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	118-126
6883723-2	1983	The method is based on the observation that PP5 will bind to heparin and employs a heparin-Sepharose column as a key step in the procedure.	Heparin	61-68	tissue factor pathway inhibitor 2	Homo sapiens	44-47
6883723-2	1983	The method is based on the observation that PP5 will bind to heparin and employs a heparin-Sepharose column as a key step in the procedure.	Heparin	83-90	tissue factor pathway inhibitor 2	Homo sapiens	44-47
6412615-2	1983	Plasma renin activity was measured in samples collected in lithium heparin, sodium heparin, and ethylenediaminetetraacetate.	Heparin	76-90	renin	Homo sapiens	7-12
6412615-5	1983	This was obviated by using an alternative incubation medium and was not, therefore, due to direct inhibition of renin by heparin.	Heparin	121-128	renin	Homo sapiens	112-117
6412615-9	1983	These results show that, provided the incubation conditions are suitably modified, samples collected into lithium or sodium heparin can be used for measurement of plasma renin activity.	Heparin	117-131	renin	Homo sapiens	170-175
6348997-1	1983	A study was performed to evaluate the hypothesis that heparin opposes uncontrolled PGI2 production by vessels due to thrombin generation.	Heparin	54-61	coagulation factor II	Rattus norvegicus	117-125
6353731-0	1983	[Effect of heparin on the renin-aldosterone system of patients with different clinical variants of chronic glomerulonephritis].	Heparin	11-18	renin	Homo sapiens	26-31
6193602-6	1983	When PPS was added to heparin containing plasma it was observed to completely inhibit heparin at low concentrations (2:1 on a weight to weight basis) when measured in the thrombin and prothrombin time but not in the KCCT.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	171-179
6884995-1	1983	The steroid-binding core of estradiol receptor was purified from pig uterus cytosol by a protocol consisting of (1) adsorption to heparin-sepharose, (2) enzymatic release of the receptor core, (3) DEAE-chromatography, (4) Sephadex G-150 filtration and (5) chromatography on heparin-sepharose.	Heparin	130-137	estrogen receptor 1	Sus scrofa	28-46
6612698-1	1983	The neutralization of heparin by histone and its subfractions has been systematically studied by measuring the effect of heparin on the esterolytic and proteolytic activity of thrombin.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	176-184
6612698-1	1983	The neutralization of heparin by histone and its subfractions has been systematically studied by measuring the effect of heparin on the esterolytic and proteolytic activity of thrombin.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	176-184
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Heparin	248-255	coagulation factor II, thrombin	Homo sapiens	39-47
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Heparin	248-255	CD59 molecule (CD59 blood group)	Homo sapiens	105-110
6687888-3	1983	In contrast, only heparin and bovine liver heparan sulfate activated ATIII, whereas dermatan sulfate was inactive at concentrations less than or equal to 1 mg/ml.	Heparin	18-25	serpin family C member 1	Bos taurus	69-74
6884995-1	1983	The steroid-binding core of estradiol receptor was purified from pig uterus cytosol by a protocol consisting of (1) adsorption to heparin-sepharose, (2) enzymatic release of the receptor core, (3) DEAE-chromatography, (4) Sephadex G-150 filtration and (5) chromatography on heparin-sepharose.	Heparin	274-281	estrogen receptor 1	Sus scrofa	28-46
6415800-1	1983	Fibronectin (FN) is a glycoprotein (disulfite-bonded dimer of 200 to 220 Kd submits) found in a soluble form in blood (concentration 250--500 microg/ml), it can be removed from it by cryoprecipitation and affinity chromatography on gelatin or heparin-agarose.	Heparin	243-250	fibronectin 1	Homo sapiens	0-11
6862345-8	1983	Thus the improved effectiveness of heparin/dihydroergotamine in prevention of deep vein thrombosis which has been shown in the fibrinogen test cannot be explained by an effect onto the coagulation parameters studied.	Heparin	35-42	fibrinogen beta chain	Homo sapiens	127-137
6602610-2	1983	Inhibition by alpha 1-proteinase inhibitor of thrombin-, but not of 7S-NGF- or kallikrein-catalysed amidolysis was alleviated by incubation of enzyme and heparin before addition of inhibitor.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	46-54
6846326-2	1983	To date, much work has been done to elucidate the interaction of heparin with thrombin and its physiologic inhibitor, Antithrombin III (ATIII).	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	78-86
6851182-0	1983	Interference of heparin in carcinoembryonic antigen radioimmunoassays.	Heparin	16-23	CEA cell adhesion molecule 3	Homo sapiens	27-51
6851182-1	1983	A false Roche carcinoembryonic antigen (CEA) activity could be detected in all commercial and noncommercial heparin preparations we examined.	Heparin	108-115	CEA cell adhesion molecule 3	Homo sapiens	14-38
6851182-1	1983	A false Roche carcinoembryonic antigen (CEA) activity could be detected in all commercial and noncommercial heparin preparations we examined.	Heparin	108-115	CEA cell adhesion molecule 3	Homo sapiens	40-43
6851182-3	1983	Using the Roche procedure, heparin solutions, in the absence of CEA, gave positive CEA activity; on the other hand, no CEA activity was detected in solutions containing only heparin when the Abbott Kit was used.	Heparin	27-34	CEA cell adhesion molecule 3	Homo sapiens	83-86
6851182-3	1983	Using the Roche procedure, heparin solutions, in the absence of CEA, gave positive CEA activity; on the other hand, no CEA activity was detected in solutions containing only heparin when the Abbott Kit was used.	Heparin	27-34	CEA cell adhesion molecule 3	Homo sapiens	83-86
6851182-4	1983	When heparin was present in specimens containing CEA, the Abbott Kit underestimated the CEA activity, whereas the Roche Kit gave false elevated values.	Heparin	5-12	CEA cell adhesion molecule 3	Homo sapiens	49-52
6851182-4	1983	When heparin was present in specimens containing CEA, the Abbott Kit underestimated the CEA activity, whereas the Roche Kit gave false elevated values.	Heparin	5-12	CEA cell adhesion molecule 3	Homo sapiens	88-91
6877243-0	1983	Influence of heparin on interactions between C-reactive protein and polycations.	Heparin	13-20	C-reactive protein	Homo sapiens	45-63
6851280-0	1983	Heparin effect on plasma fibrinogen in the thrombophilic syndrome.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	25-35
6851280-3	1983	Statistically significant results proved that heparin reduces the plasma fibrinogen progressively over a treatment period of 6 weeks.	Heparin	46-53	fibrinogen beta chain	Homo sapiens	73-83
6222069-7	1983	On this basis, we suggest that high in vivo rates of thrombin generation may lead to the sequestration of Factor Xa on the platelet surface and hence allow this serine protease to resist the action of heparin until the complex is cleared from the circulation.	Heparin	201-208	coagulation factor II, thrombin	Homo sapiens	53-61
6348194-1	1983	The functional (heparin-releasable) fraction of myocardial lipoprotein lipase (LPL) has been located at the lumen surface of capillary endothelium by means of an indirect immunocytochemical perfusion method for electron microscopy.	Heparin	16-23	lipoprotein lipase	Rattus norvegicus	59-77
6348194-1	1983	The functional (heparin-releasable) fraction of myocardial lipoprotein lipase (LPL) has been located at the lumen surface of capillary endothelium by means of an indirect immunocytochemical perfusion method for electron microscopy.	Heparin	16-23	lipoprotein lipase	Rattus norvegicus	79-82
6348194-5	1983	The highest coverage by such product occurred when the highest heparin-releasable heart LPL activity was attained after fat-feeding of rats.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	88-91
6348194-6	1983	Coverage was low when a low level of heparin-releasable heart LPL activity was induced by carbohydrate-feeding.	Heparin	37-44	lipoprotein lipase	Rattus norvegicus	62-65
6348194-7	1983	Coverage was very low in the perfused hearts after heparin-release of functional LPL activity.	Heparin	51-58	lipoprotein lipase	Rattus norvegicus	81-84
6877243-7	1983	However, heparin did induce a rapid and efficient dissociation of CRP-polycation precipitates preformed at equivalence, with total release of CRP.	Heparin	9-16	C-reactive protein	Homo sapiens	66-69
6877243-7	1983	However, heparin did induce a rapid and efficient dissociation of CRP-polycation precipitates preformed at equivalence, with total release of CRP.	Heparin	9-16	C-reactive protein	Homo sapiens	142-145
6877243-8	1983	Small amounts of heparin augmented precipitation under conditions of polycation excess of CRP, but as heparin levels were increased to amounts needed to reach equivalence with polycation, CRP was resolubilized in favor of the preferred heparin-polycation complexes.	Heparin	17-24	C-reactive protein	Homo sapiens	90-93
6877243-10	1983	These data indicate that CRP-polycation interactions are significantly and selectively influenced in the presence of small amounts of heparin and certain other polyanions.	Heparin	134-141	C-reactive protein	Homo sapiens	25-28
6870832-0	1983	Electrostatic interactions in the heparin-enhanced reaction between human thrombin and antithrombin.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	74-82
6223404-0	1983	Interaction of heparin with lipoproteins - role of the complex in the inactivation of thrombin and plasmin.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	86-94
6223404-4	1983	Heparin, complexed with LDL, retains its enhancing effect on the rate of thrombin and plasmin inactivation by antithrombin III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	73-81
6687802-3	1983	Heparin and dermatan sulfate which were eluted from the affinity column catalyzed the inhibition of thrombin by heparin cofactor II to a greater degree than did the respective unfractionated mucopolysaccharides.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	100-108
6870832-1	1983	Binding of heparin to thrombin is monitored by means of an aqueous two-phase partition system, and binding of heparin to antithrombin is monitored by means of heparin induced enhancement of the intrinsic fluorescence of the protein.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	22-30
6870832-3	1983	Heparin is displaced from thrombin at lower concentrations of electrolyte than those necessary for its displacement from antithrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	26-34
6870832-5	1983	The kinetics of the reaction between thrombin and antithrombin in the presence of heparin were studied by using an assay where synthetic peptide substrate is present in the reaction mixture during the reaction between proteinase and inhibitor.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	37-45
6870832-7	1983	The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	72-80
6870832-7	1983	The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin.	Heparin	195-202	coagulation factor II, thrombin	Homo sapiens	72-80
6870832-7	1983	The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin.	Heparin	195-202	coagulation factor II, thrombin	Homo sapiens	72-80
6824725-4	1983	There were no differences between control and hypothyroid rats in the disappearance of intravenously injected 125I-labeled lipoprotein lipase, but when a low dose of heparin was injected before the labeled enzyme, the disappearance of 125I-labeled lipoprotein lipase was more retarded in thyroidectomized rats.	Heparin	166-173	lipoprotein lipase	Rattus norvegicus	248-266
6831687-3	1983	In the AT III assay the sample is incubated with excess thrombin and heparin to form the functionally inactive AT III-thrombin complex.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	118-126
6825981-3	1983	The protein can be further characterized as an estrogen receptor by its binding to heparin-Sepharose.	Heparin	83-90	estrogen receptor 1	Homo sapiens	47-64
6833231-8	1983	Both the thrombin times and the activated factor X inhibition following addition of heparin are markedly prolonged in the absence of histidine-rich glycoprotein and shortened by addition of purified histidine-rich glycoprotein.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	9-17
6870799-1	1983	Lipoprotein lipase activity was higher in fat-pad pieces than in isolated adipocytes from the same fed rats, whereas hydrolysis of triacylglycerols from triacylglycerol-rich lipoproteins was similar in the two preparations when incubated either in basal conditions or in the presence of heparin.	Heparin	287-294	lipoprotein lipase	Rattus norvegicus	0-18
6870799-3	1983	In fat-pad pieces, but not in isolated adipocytes, incubation with heparin produced a decrease in the lipoprotein lipase activity measured in the tissue preparation.	Heparin	67-74	lipoprotein lipase	Rattus norvegicus	102-120
6833400-7	1983	The adhesive glycoproteins laminin and fibronectin therefore differ markedly in biological activities in several specific adhesion assays; however, they resemble one another in binding to heparin, collagen, and cell surfaces and in their agglutinin activity.	Heparin	188-195	fibronectin 1	Homo sapiens	39-50
6602754-0	1983	Heparin-stimulated modification of C1-inhibitor by subcomponent C1s of human complement.	Heparin	0-7	complement C1s	Homo sapiens	64-67
6874668-6	1983	These enzymes are very similar to RNase A in that they are inhibited by heparin, show preferential hydrolysis of C5"-O-P linkages adjacent to a cytosine nucleotide rather than a uracil nucleotide, and in their antigenic properties.	Heparin	72-79	ribonuclease pancreatic	Bos taurus	34-41
6824734-1	1983	Heparin dramatically enhanced the rate of unbound glucocorticoid receptor inactivation in vitro in a concentration, time and temperature-dependent manner.	Heparin	0-7	nuclear receptor subfamily 3 group C member 1	Homo sapiens	50-73
6842082-8	1983	ApoE-deficient rat HDL, separated by heparin-Sepharose affinity chromatography also showed highly specific saturable binding to intestinal cells.	Heparin	37-44	apolipoprotein E	Rattus norvegicus	0-4
6855652-2	1983	The system indirectly measures heparin by its inhibition of thrombin protease action on a synthetic substrate.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	60-68
6824734-4	1983	However, in the presence of heparin (40 micrograms per ml cytosol) the glucocorticoid receptor had a half-life of only 15 min at 25 degrees C. Interestingly, 10 mM molybdate (with or without 5 mM dithiothreitol) greatly inhibited heparin-dependent receptor inactivation at 4 degrees C. Dithiothreitol (alone) significantly stabilized receptor binding in control samples at 4 degrees C, but provided no protection from heparin-dependent receptor inactivation.	Heparin	28-35	nuclear receptor subfamily 3 group C member 1	Homo sapiens	71-94
6859531-3	1983	The methodologies were extended to investigations on the effects of heparin in the interaction between thrombin and antithrombin III.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	103-111
6830263-0	1983	Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	48-56
6830263-1	1983	Heparin accelerates the rate of inhibition of thrombin by antithrombin III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	46-54
6847629-1	1983	Heparin fractions of differing Mr (7800-18 800) prepared from commercial heparin by gel filtration and affinity chromatography on immobilized anti-thrombin III had specific activities when determined by anti-Factor Xa and anti-thrombin assays that ranged from 228 to 448 units/mg.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	147-155
6401433-4	1983	When the lysine residue of thrombin involved in heparin binding was protected with heparin against chemical modification (PLP-thrombin), the modified enzyme remained similar to the native one with respect to cellular binding, with some loss of low-affinity binding only.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	27-35
6401433-4	1983	When the lysine residue of thrombin involved in heparin binding was protected with heparin against chemical modification (PLP-thrombin), the modified enzyme remained similar to the native one with respect to cellular binding, with some loss of low-affinity binding only.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	126-134
6401433-4	1983	When the lysine residue of thrombin involved in heparin binding was protected with heparin against chemical modification (PLP-thrombin), the modified enzyme remained similar to the native one with respect to cellular binding, with some loss of low-affinity binding only.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	27-35
6401433-4	1983	When the lysine residue of thrombin involved in heparin binding was protected with heparin against chemical modification (PLP-thrombin), the modified enzyme remained similar to the native one with respect to cellular binding, with some loss of low-affinity binding only.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	126-134
6401433-5	1983	Heparin, in a tenfold molar excess to enzyme, inhibited the binding of the native as well as the PLP-thrombin, whereas it did not influence the interaction between PLP2-thrombin and the cell.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	101-109
6847629-1	1983	Heparin fractions of differing Mr (7800-18 800) prepared from commercial heparin by gel filtration and affinity chromatography on immobilized anti-thrombin III had specific activities when determined by anti-Factor Xa and anti-thrombin assays that ranged from 228 to 448 units/mg.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	227-235
6337177-1	1983	The proportion of immunoreactive somatomedin-C (IR-Sm-C) in blood that is available for measurement in the RIA is influenced by whether the sample is processed as serum or plasma, by how promptly the sample is chilled and frozen, by whether the reaction is carried out in glass or polystyrene tubes and by whether the incubation mixture contains protamine or heparin.	Heparin	359-366	insulin like growth factor 1	Homo sapiens	33-46
6847629-4	1983	An anti-thrombin III-binding oligosaccharide preparation (containing predominantly eight to ten saccharide units), prepared by degradation of heparin with HNO2 had high (800 units/mg) anti-Factor Xa, but negligible anti-thrombin, specific activity.	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	8-16
6822493-5	1983	Differences between thrombin and Factor Xa at low (nanomolar) concentrations of heparin were evident in this rate constant and the relative affinities for the heparin-antithrombin complex (Km for Factor Xa = 100 nM; Km for thrombin less than or equal to 2 nM).	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	20-28
6218163-3	1983	The binding of C1q to heparin was quantitatively examined by utilizing an assay that employs a 125I-labeled low molecular weight heparin glycosaminoglycan (LMW-Hep) (Mr = 8500).	Heparin	22-29	complement C1q C chain	Homo sapiens	15-18
6189236-2	1983	Unfractionated heparin increased the binding of fibrinogen on ADP-treated platelets.	Heparin	15-22	fibrinogen beta chain	Homo sapiens	48-58
6822493-5	1983	Differences between thrombin and Factor Xa at low (nanomolar) concentrations of heparin were evident in this rate constant and the relative affinities for the heparin-antithrombin complex (Km for Factor Xa = 100 nM; Km for thrombin less than or equal to 2 nM).	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	171-179
6822493-7	1983	At high heparin concentrations (micromolar), the kinetic parameters for Factor Xa were unchanged but the Km for thrombin increased dramatically to 100 nM.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	112-120
6838953-6	1983	It was found that immobilized heparin forms complexes with fibrinogen, thrombin and plasmin that produce lytic action on unstabilized fibrin.	Heparin	30-37	fibrinogen beta chain	Homo sapiens	59-69
6680996-5	1983	Heparin-releasable lipoprotein lipase activity in epididymal adipose tissue, lipoprotein lipase activity in post heparin plasma, and VLDL-triolein hydrolizing activity in adipose tissue stromal vessels were higher in clinofibrate-treated rats than in atherosclerotic rats.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-37
6651812-1	1983	The antithrombotic effects of the synthetic thrombin inhibitor 4-amidinophenylpyruvic acid and the naturally occurring thrombin inhibitor heparin were studied in a stasis-induced venous thrombosis model and an extracorporeal shunt model in rats.	Heparin	138-145	coagulation factor II	Rattus norvegicus	119-127
6651812-4	1983	The antithrombotic effect of the synthetic inhibitor was accompanied by considerable prolongation of the plasma thrombin time, whereas the effect of heparin on the thrombin time was less pronounced.	Heparin	149-156	coagulation factor II	Rattus norvegicus	164-172
6651812-7	1983	Synthetic thrombin inhibitors are potential antithrombotic agents whose effectivity corresponds to that of heparin.	Heparin	107-114	coagulation factor II	Rattus norvegicus	10-18
6824792-7	1983	Partial relaxation of the thrombin-treated blood vessel was achieved by the addition of heparin.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	26-34
6838953-6	1983	It was found that immobilized heparin forms complexes with fibrinogen, thrombin and plasmin that produce lytic action on unstabilized fibrin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	71-79
6219115-5	1983	PF4-mediated responses were blocked by treating the PF4-adsorbed substratum with heparin (but not chondroitin sulfate), or alternatively the cells with Flavobacter heparinum heparinase (but not chondroitinase ABC).	Heparin	81-88	platelet factor 4	Mus musculus	0-3
6872546-1	1983	Changes in heart lipoprotein lipase (LPL) activity provoked by colchicine (0.5 mg/100 g body weight) and heparin (10 IU/100 g body weight) were studied in heart homogenates and serum from rats treated with both drugs or with heparin alone.	Heparin	105-112	lipoprotein lipase	Rattus norvegicus	37-40
6654191-6	1983	A significant decrease in the AT-III level (p less than 0.01) and a significant increase (p less than 0.01) in the fibrinogen level were observed after heparin-dipyridamole treatment of patients suspected of IUGR.	Heparin	152-159	fibrinogen beta chain	Homo sapiens	115-125
6667903-3	1983	In the presence of heparin, a lower thrombin-inactivating capacity of plasma was confirmed using crude thrombin, but this phenomenon was less pronounced with the purified thrombin preparation.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	36-44
6667903-3	1983	In the presence of heparin, a lower thrombin-inactivating capacity of plasma was confirmed using crude thrombin, but this phenomenon was less pronounced with the purified thrombin preparation.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	103-111
6667903-3	1983	In the presence of heparin, a lower thrombin-inactivating capacity of plasma was confirmed using crude thrombin, but this phenomenon was less pronounced with the purified thrombin preparation.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	103-111
6873753-0	1983	Effects of heparin and alpha 1-acid glycoprotein on thrombin or Activated Thrombofax Reagent-induced platelet aggregation and clot formation.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	52-60
6873753-2	1983	An anti-heparin effect for AAG was also demonstrable in platelet-rich plasma (PRP) challenged with thrombin, but only over a limited range of heparin concentrations; at elevated heparin concentrations, and only in the presence of AAG, both platelet aggregation and clot formation were substantially inhibited.	Heparin	8-15	complement component 4 binding protein alpha	Homo sapiens	78-81
6873753-2	1983	An anti-heparin effect for AAG was also demonstrable in platelet-rich plasma (PRP) challenged with thrombin, but only over a limited range of heparin concentrations; at elevated heparin concentrations, and only in the presence of AAG, both platelet aggregation and clot formation were substantially inhibited.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	99-107
6219115-5	1983	PF4-mediated responses were blocked by treating the PF4-adsorbed substratum with heparin (but not chondroitin sulfate), or alternatively the cells with Flavobacter heparinum heparinase (but not chondroitinase ABC).	Heparin	81-88	platelet factor 4	Mus musculus	52-55
6336617-10	1983	However, where limitations in the renin-angiotensin-aldosterone axis exist, e.g. in diabetes mellitus, mineralocorticoid insufficiency may be precipitated by heparin.	Heparin	158-165	renin	Homo sapiens	34-39
6412199-3	1983	The glycoprotein fibronectin is a constituent of connective tissue with a high affinity to polyanions such as heparan sulfate or heparin.	Heparin	129-136	fibronectin 1	Homo sapiens	17-28
7150660-3	1982	Heparin and galactose prevented gel formation of fibrinogen with substance 1.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	49-59
6311768-0	1983	Heparin inhibits FMLP and Con-A dependent activation of human polymorphonuclear leucocytes in vitro.	Heparin	0-7	formyl peptide receptor 1	Homo sapiens	17-21
6311768-3	1983	Heparin was able to inhibit, in a dose-dependent way, FMLP-mediated and ConA-mediated granulocyte activation.	Heparin	0-7	formyl peptide receptor 1	Homo sapiens	54-58
6311768-6	1983	The inhibiting effect of heparin on FMLP-induced granulocyte activation proved to be time-dependent.	Heparin	25-32	formyl peptide receptor 1	Homo sapiens	36-40
6839017-1	1983	Two heparin-neutralizing proteins secreted by thrombin-stimulated platelets were purified to homogeneity by means of heparin-agarose affinity chromatography.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	46-54
6839017-1	1983	Two heparin-neutralizing proteins secreted by thrombin-stimulated platelets were purified to homogeneity by means of heparin-agarose affinity chromatography.	Heparin	117-124	coagulation factor II, thrombin	Homo sapiens	46-54
6836542-8	1983	High ATIII and low ATIII affinity conjugate fractions showed the same behavior as ATIII fractionated heparin with respect to thrombin times and Factor Xa inhibition.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	125-133
7142182-2	1982	The results have shown that the reaction is saturable with respect to both thrombin (KT = 3.6 x 10(-8) M) and antithrombin III (KAT = 1.0 x 10(-7) M) when the heparin concentration is low relative to the initial protein concentrations.	Heparin	159-166	coagulation factor II, thrombin	Homo sapiens	75-83
7151803-3	1982	Two fragments of fibronectin, Mr = 205000 and 190000, which lack the NH2-terminal domain of fibronectin and retain the collagen-binding, cell-attachment and heparin-binding functions, and a Mr = 170000 fragment, which retains the collagen-binding and cell-attachment functions, were seen as rods with varying degrees of nodularity while a Mr = 100000 fragment, which only binds to collagen, had two clear-cut domains.	Heparin	157-164	fibronectin 1	Homo sapiens	17-28
7142182-2	1982	The results have shown that the reaction is saturable with respect to both thrombin (KT = 3.6 x 10(-8) M) and antithrombin III (KAT = 1.0 x 10(-7) M) when the heparin concentration is low relative to the initial protein concentrations.	Heparin	159-166	kynurenine aminotransferase 1	Homo sapiens	128-135
7142182-6	1982	When the heparin-enhanced antithrombin III/thrombin reaction was studied under conditions where the heparin concentration was high relative to the initial protein concentrations the overall reaction was second order.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	30-38
7165705-1	1982	Lipoprotein lipase (EC 3.1.1.34) extracted from adipose tissue of glucose-fed rats with 5 mM-sodium barbital, pH 7.5, containing 20% (v/v) glycerol and 0.1% (v/v) Triton X-100, was partially purified by affinity chromatography on heparin linked to Sepharose 4B.	Heparin	230-237	lipoprotein lipase	Rattus norvegicus	0-18
7165705-11	1982	Purification of lipoprotein lipase from adipose tissue of glucose-fed rats was also carried out using affinity chromatography on Sepharose 4B linked to heparin with low affinity for antithrombin-III.	Heparin	152-159	lipoprotein lipase	Rattus norvegicus	16-34
7164033-5	1982	The low affinity heparin fraction and the unfractionated heparin had equivalent inhibitory effects on prothrombin activation in antithrombin III depleted plasma.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	102-113
7150611-7	1982	In order to investigate the role of lipoprotein lipase in this process, we administered heparin, which leads to immediate release of lipoprotein lipase from the endothelium to the circulation in vivo, 10 min and 4 h before isolation and perfusion of the lungs.	Heparin	88-95	lipoprotein lipase	Rattus norvegicus	36-54
7150611-7	1982	In order to investigate the role of lipoprotein lipase in this process, we administered heparin, which leads to immediate release of lipoprotein lipase from the endothelium to the circulation in vivo, 10 min and 4 h before isolation and perfusion of the lungs.	Heparin	88-95	lipoprotein lipase	Rattus norvegicus	133-151
7150611-8	1982	Heparin administration 10 min prior to perfusion led to marked release of lipoprotein lipase from the lungs and completely abolished the subsequent hydrolysis of circulating triacylglycerols.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	74-92
7150611-9	1982	Perfusions carried out 4 h after heparin administration show that in the lung, endothelial lipoprotein lipase levels did not return to normal within 4 h after heparin administration.	Heparin	33-40	lipoprotein lipase	Rattus norvegicus	91-109
7164033-0	1982	Heparin with low affinity to antithrombin III inhibits the activation of prothrombin in normal plasma.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	73-84
7164033-5	1982	The low affinity heparin fraction and the unfractionated heparin had equivalent inhibitory effects on prothrombin activation in antithrombin III depleted plasma.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	102-113
7164033-2	1982	Unfractionated heparin enhances the rates at which antithrombin III inactivates activated clotting factors, and inhibits the activation of both Factor X and prothrombin by disrupting the calcium and phospholipid dependent assembly of the Factor X and prothrombin activator complexes.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	157-168
7158775-0	1982	Preparation of three types of heparin-sepharose and their binding activities to thrombin and antithrombin III.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	80-88
7164033-2	1982	Unfractionated heparin enhances the rates at which antithrombin III inactivates activated clotting factors, and inhibits the activation of both Factor X and prothrombin by disrupting the calcium and phospholipid dependent assembly of the Factor X and prothrombin activator complexes.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	251-262
7157229-6	1982	The inactivation of thrombin or factor Xa by antithrombin is catalysed by the presence in the mixture of these insoluble materials as it is with soluble heparin.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	20-28
7115961-5	1982	Furthermore, despite the ability of heparin (1 U/ml) to increase the inactivation rate of thrombin by plasma, no acceleration of the rate of inhibition of factor XIa by plasma was observed.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	90-98
7126483-6	1982	The greater values of FPA and their responses to heparin indicate that there is increased thrombin formation in a number of patients with liver cirrhosis, with no apparent relation to the severity of the disease.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	90-98
6292573-11	1982	The fibronectin fibrils precipitated with heparin, compared to soluble fibronectin, show a considerably improved affinity to native collagen, especially to type III.	Heparin	42-49	fibronectin 1	Homo sapiens	4-15
7126036-1	1982	Acetone powder extracts prepared from cultured pig aortic smooth muscle cells and the culture medium from these cells (particularly when incubated with heparin) were shown to contain a lipolytic enzyme which was identified as lipoprotein lipase by the following criteria: 1) stimulation by apolipoprotein C-II; 2) an optimal activity at approximately pH 8.0; 3) inhibition by NaCl, and 4) binding to a heparin-Sepharose affinity column.	Heparin	152-159	lipoprotein lipase	Sus scrofa	226-244
7126036-1	1982	Acetone powder extracts prepared from cultured pig aortic smooth muscle cells and the culture medium from these cells (particularly when incubated with heparin) were shown to contain a lipolytic enzyme which was identified as lipoprotein lipase by the following criteria: 1) stimulation by apolipoprotein C-II; 2) an optimal activity at approximately pH 8.0; 3) inhibition by NaCl, and 4) binding to a heparin-Sepharose affinity column.	Heparin	402-409	lipoprotein lipase	Sus scrofa	226-244
6294899-3	1982	The interaction between GP Ib and thrombin was abolished when thrombin was blocked either at the active serine site with tosyl-lysine-chloromethyl-ketone (TLCK) or phenylmethylsulfonylfluoride (PMSF) or at the fibrinogen binding site (macromolecular binding site) with N-bromosuccinimide (NBS) or heparin, indicating that both sites have to be freely accessible for the retention of the glycocalicin-related protein by thrombin.	Heparin	297-304	coagulation factor II, thrombin	Homo sapiens	34-42
6217639-1	1982	Reactions of heparin, covalently immobilized in hydrogel, with fibrinolysin, blood serum albumin, thrombin and fibrinogen were studied.	Heparin	13-20	albumin	Homo sapiens	83-96
6217639-4	1982	Complexes of the immobilized heparin with fibrinogen, thrombin and fibrinolysin hydrolyzed the unstabilized fibrin.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	54-62
6294899-3	1982	The interaction between GP Ib and thrombin was abolished when thrombin was blocked either at the active serine site with tosyl-lysine-chloromethyl-ketone (TLCK) or phenylmethylsulfonylfluoride (PMSF) or at the fibrinogen binding site (macromolecular binding site) with N-bromosuccinimide (NBS) or heparin, indicating that both sites have to be freely accessible for the retention of the glycocalicin-related protein by thrombin.	Heparin	297-304	coagulation factor II, thrombin	Homo sapiens	62-70
6294899-3	1982	The interaction between GP Ib and thrombin was abolished when thrombin was blocked either at the active serine site with tosyl-lysine-chloromethyl-ketone (TLCK) or phenylmethylsulfonylfluoride (PMSF) or at the fibrinogen binding site (macromolecular binding site) with N-bromosuccinimide (NBS) or heparin, indicating that both sites have to be freely accessible for the retention of the glycocalicin-related protein by thrombin.	Heparin	297-304	coagulation factor II, thrombin	Homo sapiens	62-70
7135347-0	1982	On the reliability of the use of heparin immobilized on agarose for the study of the interactions among heparin, thrombin and antithrombin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	113-121
7135347-1	1982	The extent of inhibition of thrombin was re-examined as a consequence of the sequence of addition of thrombin and antithrombin III to a column of heparin immobilized on agarose.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	101-109
6185106-3	1982	After initial contradictory results, the extrafraction was determined to be fibrinogen, present because of the slow release of heparin contained in the catheter, so that electrophoresis was performed on plasma instead of on serum.	Heparin	127-134	fibrinogen beta chain	Homo sapiens	76-86
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	69-76	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	69-76	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-153
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	110-117	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	110-117	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-153
7093524-5	1982	This finding is thought to reflect heparin suppression of thrombin activity on fibrinogen.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	58-66
7093524-5	1982	This finding is thought to reflect heparin suppression of thrombin activity on fibrinogen.	Heparin	35-42	fibrinogen beta chain	Homo sapiens	79-89
7088192-5	1982	Recently, we showed that heparin virtually blocked the binding of thrombin-protease nexin complexes to both mouse and human cells without affecting the ability of these cells to respond to thrombin.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	66-74
7123544-3	1982	The result, in conjunction with the HDL-cholesterol concentration simultaneously determined by the heparin-Ca2+ method, enabled us to calculate the HDL2- and HDL3-cholesterol concentrations.	Heparin	99-106	HDL3	Homo sapiens	158-162
7135350-6	1982	Binding strength for immobilized heparin is decreased in the array fibrinogen congruent to thrombin much greater than plasmin greater than serum albumin.	Heparin	33-40	fibrinogen beta chain	Homo sapiens	67-77
7115744-9	1982	Release of surface-bound endogenous or exogenous lipoprotein lipase by heparin was accompanied by almost complete elimination of uptake of cholesteryl linoleyl ether in presence of complete hydrolysis of [14C]triacylglycerol.	Heparin	71-78	lipoprotein lipase	Rattus norvegicus	49-67
7115750-0	1982	Changes in the plasma lipoprotein distribution of apolipoproteins C-II, C-III1, C-III2 and apolipoprotein B after heparin-induced lipolysis.	Heparin	114-121	apolipoprotein B	Homo sapiens	91-107
7135350-6	1982	Binding strength for immobilized heparin is decreased in the array fibrinogen congruent to thrombin much greater than plasmin greater than serum albumin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	91-99
6923655-4	1982	A significant reduction of kallikrein and antiplasmin in per- and post-operative periods was observed in the control patients compared with the heparin-treated patients, while there was a significant reduction of anti-thrombin III in the control patients compared with the treated patients only in the per-operative period.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	218-226
7135350-7	1982	Complexes of immobilized heparin with fibrinogen, thrombin and plasmin display lytic action towards unstabilized fibrin.	Heparin	25-32	fibrinogen beta chain	Homo sapiens	38-48
7135350-7	1982	Complexes of immobilized heparin with fibrinogen, thrombin and plasmin display lytic action towards unstabilized fibrin.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	50-58
7078434-4	1982	Heparin-releasable LPL activity was significantly greater in lean- than in obese-derived cultures grown in media supplemented with penicillin and streptomycin (pen-strep).	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-22
6214866-5	1982	Heparin protected thrombin from inactivation by alpha-1-antitrypsin.	Heparin	0-7	coagulation factor II	Mus musculus	18-26
6214866-5	1982	Heparin protected thrombin from inactivation by alpha-1-antitrypsin.	Heparin	0-7	serpin family A member 1	Bos taurus	48-67
7106672-2	1982	The antitoxic and antiphlogistic components of heparin could be proved by long-term pre-treatment with heparin ointment, based on clinical experimental trials of inhibition of the pyrexal reaction and reduction of erythema, weal and heat radiation produced by histamin and bradykinin i.c.	Heparin	47-54	kininogen 1	Homo sapiens	273-283
7106672-2	1982	The antitoxic and antiphlogistic components of heparin could be proved by long-term pre-treatment with heparin ointment, based on clinical experimental trials of inhibition of the pyrexal reaction and reduction of erythema, weal and heat radiation produced by histamin and bradykinin i.c.	Heparin	103-110	kininogen 1	Homo sapiens	273-283
7085627-3	1982	Both clotting and amidolytic chromogenic assays were used to measure heparin-potentiated inhibition of both thrombin and Factor Xa.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	108-116
7085631-0	1982	Arrangement of attachment-promoting, self-association, and heparin-binding sites in horse serum fibronectin.	Heparin	59-66	fibronectin 1	Homo sapiens	96-107
7083567-4	1982	The alpha-thrombin is inactivated by the heparin-antithrombin complex while substrate is being hydrolyzed, so that total product formation decreases with heparin concentration.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	10-18
7105411-3	1982	The thrombin time and the whole blood recalcification time give pointless and ambiguous information respectively, concerning the heparin level.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	4-12
6176583-5	1982	Using this approach, we have established the positions of two unique heparin-, a gelatin-, and two monoclonal antibody-binding sites on the fibronectin subunit.	Heparin	69-76	fibronectin 1	Homo sapiens	140-151
7115921-1	1982	Stimulation of the anticoagulation system with the structural analogs of alpha-thrombin, DPP-alpha-thrombin and prothrombin I having no proteolytic activity leads, as is the case with alpha-thrombin, to a decrease in the heparin content in mast cells and to a concurrent rise in the blood level of the complex compounds of heparin and blood proteins.	Heparin	221-228	coagulation factor II, thrombin	Homo sapiens	79-87
7115921-1	1982	Stimulation of the anticoagulation system with the structural analogs of alpha-thrombin, DPP-alpha-thrombin and prothrombin I having no proteolytic activity leads, as is the case with alpha-thrombin, to a decrease in the heparin content in mast cells and to a concurrent rise in the blood level of the complex compounds of heparin and blood proteins.	Heparin	221-228	coagulation factor II, thrombin	Homo sapiens	99-107
7115921-1	1982	Stimulation of the anticoagulation system with the structural analogs of alpha-thrombin, DPP-alpha-thrombin and prothrombin I having no proteolytic activity leads, as is the case with alpha-thrombin, to a decrease in the heparin content in mast cells and to a concurrent rise in the blood level of the complex compounds of heparin and blood proteins.	Heparin	221-228	coagulation factor II, thrombin	Homo sapiens	99-107
6284125-8	1982	The presence of heparin in the binding-protein-fibronectin mixture resulted in an even faster mobility of the complex, whereas the mobility of native fibronectin was unaffected.	Heparin	16-23	fibronectin 1	Homo sapiens	47-58
6213827-1	1982	Previous studies have shown that placental protein 5 (PP5) forms complexes with heparin.	Heparin	80-87	tissue factor pathway inhibitor 2	Homo sapiens	33-52
6213827-1	1982	Previous studies have shown that placental protein 5 (PP5) forms complexes with heparin.	Heparin	80-87	tissue factor pathway inhibitor 2	Homo sapiens	54-57
7079880-5	1982	The fibronectin molecule itself has abnormal properties in pathological cases and is poorly precipitable by heparin.	Heparin	108-115	fibronectin 1	Homo sapiens	4-15
6896131-3	1982	These findings include the following: (1) On the vascular endothelium, a cofactor for antithrombin III (with an activity comparable to stationary phase heparin) catalyzes thrombin inhibition in vivo.	Heparin	152-159	coagulation factor II, thrombin	Homo sapiens	90-98
6920385-2	1982	Chicken antithrombin was purified from fresh chicken plasma by affinity chromatography using heparin-agarose, and its amino acid and carbohydrate compositions, amino-terminal sequence, inhibition of human thrombin, and immunological properties were studied and compared with previously studied mammalian antithrombins (human, pig, rabbit, and rat), and also with chick ovalbumin.	Heparin	93-100	serpin family C member 1	Gallus gallus	8-20
6800421-10	1982	The ability of heparin to induce precipitation of CIg while leaving most VIII:C activity in the supernatant plasma may be useful in the preparation of procoagulant-rich plasma subfractions, since VIII:C can subsequently be recovered in good yield by cryoprecipitation.	Heparin	15-22	fibronectin 1	Homo sapiens	50-53
6187083-3	1982	Fluorescamin labelled heparin of Mr 7 000 interacts with thrombin to form a 2:1 molar complex.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	57-65
7068594-0	1982	The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	55-63
7068594-0	1982	The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	64-72
7068594-1	1982	The heparin-catalyzed inactivation of thrombin by antithrombin was examined using saturation kinetics and fractional reaction lifetimes.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	38-46
7068594-2	1982	Based solely on kinetic analysis, the reaction binding sequence was determined to be heparin binding to antithrombin followed by binding of thrombin.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	108-116
6461438-6	1982	Antithrombin III activity could be determined with 2 microliter of human plasma using human thrombin and heparin as cofactor.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	4-12
6895893-2	1982	We have isolated a previously unrecognized heparin-dependent inhibitor of thrombin from human plasma.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	74-82
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	49-57
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	174-181	coagulation factor II, thrombin	Homo sapiens	49-57
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	174-181	CD59 molecule (CD59 blood group)	Homo sapiens	157-162
7037067-6	1982	These observations support the concept that the conformational change, induced by binding of heparin, exposes specific polypeptide bonds susceptible to thrombin, except that nonproductive proteolysis may then occur even more rapidly than the formation of a stable enzyme-inhibitor complex.	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	152-160
7037067-7	1982	This, in turn, suggests that the presence of highly active heparin may contribute to reduction of the protective inhibitor in blood, if induction of proteolysis by thrombin is in effect.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	164-172
7083646-8	1982	We found that heparin also decreased fibrinogen, hematocrit, serum alpha 2 globulin, and number of platelets.	Heparin	14-21	fibrinogen beta chain	Homo sapiens	37-47
7064134-0	1982	Measurement of the heparin enhanced-antithrombin III/thrombin reaction rate in the presence of synthetic substrate.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	40-48
7061710-5	1982	Platelet factor 4, protamine sulfate and diisopropylphosphoryl thrombin, all antagonists of the antithrombin III cofactor activity of heparin, significantly reduced the capacity of the preparation to inhibit thrombin.	Heparin	134-141	coagulation factor II	Rattus norvegicus	63-71
7061710-5	1982	Platelet factor 4, protamine sulfate and diisopropylphosphoryl thrombin, all antagonists of the antithrombin III cofactor activity of heparin, significantly reduced the capacity of the preparation to inhibit thrombin.	Heparin	134-141	coagulation factor II	Rattus norvegicus	100-108
7060273-0	1982	Placental protein 5 (PP5) in pregnancy and malignant disease: the influence of heparin binding.	Heparin	79-86	tissue factor pathway inhibitor 2	Homo sapiens	0-19
7060273-3	1982	The effect of heparin on PP5 measurements appeared to be enhanced by a serum component related to pregnancy, since addition of heparin decreased the measured level of PP5 to a greater extent in pregnancy serum than in male serum to which purified PP5 had been added.	Heparin	14-21	tissue factor pathway inhibitor 2	Homo sapiens	25-28
7060273-3	1982	The effect of heparin on PP5 measurements appeared to be enhanced by a serum component related to pregnancy, since addition of heparin decreased the measured level of PP5 to a greater extent in pregnancy serum than in male serum to which purified PP5 had been added.	Heparin	14-21	tissue factor pathway inhibitor 2	Homo sapiens	167-170
7060273-3	1982	The effect of heparin on PP5 measurements appeared to be enhanced by a serum component related to pregnancy, since addition of heparin decreased the measured level of PP5 to a greater extent in pregnancy serum than in male serum to which purified PP5 had been added.	Heparin	14-21	tissue factor pathway inhibitor 2	Homo sapiens	167-170
7060273-3	1982	The effect of heparin on PP5 measurements appeared to be enhanced by a serum component related to pregnancy, since addition of heparin decreased the measured level of PP5 to a greater extent in pregnancy serum than in male serum to which purified PP5 had been added.	Heparin	127-134	tissue factor pathway inhibitor 2	Homo sapiens	167-170
7060273-3	1982	The effect of heparin on PP5 measurements appeared to be enhanced by a serum component related to pregnancy, since addition of heparin decreased the measured level of PP5 to a greater extent in pregnancy serum than in male serum to which purified PP5 had been added.	Heparin	127-134	tissue factor pathway inhibitor 2	Homo sapiens	167-170
7057400-0	1982	Pharmacological activities of heparins obtained from different tissues: enrichment of heparin fractions with high lipoprotein lipase, antihemolytic and anticoagulant activities by molecular sieving and antithrombin III affinity chromatography.	Heparin	30-38	serpin family C member 1	Bos taurus	202-218
7057400-1	1982	The pharmacological activities of 14 heparins prepared from bovine and hog tissues and heparin fractions obtained by molecular sieving on sephacryl S-200 and antithrombin III affinity chromatography are reported.	Heparin	37-45	serpin family C member 1	Bos taurus	158-174
7057400-1	1982	The pharmacological activities of 14 heparins prepared from bovine and hog tissues and heparin fractions obtained by molecular sieving on sephacryl S-200 and antithrombin III affinity chromatography are reported.	Heparin	37-44	serpin family C member 1	Bos taurus	158-174
7061918-9	1982	The administration of heparin to cirrhotic patients improved the survival of fibrinogen but not of platelets.	Heparin	22-29	fibrinogen beta chain	Homo sapiens	77-87
7064134-1	1982	An assay approach, designed to allow accurate measurement of the rate of thrombin inhibition by antithrombin III in the presence of heparin, is described.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	73-81
7059179-0	1982	NH2-terminal sequences of DNA-, heparin-, and gelatin-binding tryptic fragments from human plasma fibronectin.	Heparin	32-39	fibronectin 1	Homo sapiens	98-109
7158402-2	1982	Renografin-60 produced a strong anticoagulant effect and the clotting times were significantly prolonged; the addition of heparin resulted in greatly elevated thrombin time.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	159-167
7064128-0	1982	Evaluation of a heparin assay method using a fluorogenic synthetic peptide substrate for thrombin.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	89-97
6752880-5	1982	Local generation of thrombin increases the thrombogenicity of the subendothelium and the accumulation of platelets, an effect inhibited by heparin.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	20-28
7099342-2	1982	Uremic rats had a 6-fold increase in BUN and 75% rise in TG levels associated with a 50% reduction in adipose tissue heparin-releasable LPL activity.	Heparin	117-124	lipoprotein lipase	Rattus norvegicus	136-139
6820841-0	1982	[Effect of heparin and hydrocortisone on the activity of kidney erythropoietin inhibitor in experimental renal lesions].	Heparin	11-18	erythropoietin	Homo sapiens	64-78
6178655-8	1981	Finally, a tentative hypothesis is put forward to explain how the endogenous modulators like heparin determine the biological functions of thrombin.	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	139-147
7164279-0	1982	Invalidation of concerns with long-term use of heparin: thrombin/antithrombin III interactions.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	56-64
7064387-0	1982	[Lipoprotein lipase and liver triglyceride lipase in blood plasma of rabbits and rats subjected to heparin administration].	Heparin	99-106	pancreatic triacylglycerol lipase	Oryctolagus cuniculus	30-49
7287722-1	1981	Lipoprotein lipase released from the rat heart during a 30-s perfusion with heparin was compared to the lipase remaining in the heart tissue.	Heparin	76-83	lipoprotein lipase	Rattus norvegicus	0-18
6271234-2	1981	In rats, previously fasted, lipoprotein lipase activity released into the perfusate by heparin increased approximately 50% 4 h after fat feeding.	Heparin	87-94	lipoprotein lipase	Rattus norvegicus	28-46
7292011-0	1981	Heparin facilitates the extraction of tissue fibronectin.	Heparin	0-7	fibronectin 1	Homo sapiens	45-56
7292011-1	1981	Extraction of fibronectin from two human tissues, lung parenchyma and placental villi, was facilitated by the incorporation of heparin into extraction media.	Heparin	127-134	fibronectin 1	Homo sapiens	14-25
7292011-2	1981	The effect of heparin was additive to the effect of urea which is known to extract fibronectin.	Heparin	14-21	fibronectin 1	Homo sapiens	83-94
7292011-3	1981	These experiments provide further evidence that fibronectin and glycosaminoglycans are associated in connective tissues and the use of heparin forms the basis for a simple method for extraction and quantitation of tissue fibronectin.	Heparin	135-142	fibronectin 1	Homo sapiens	221-232
7296000-1	1981	Two fractions of human prothrombin can be isolated from single donor plasma by the technique of heparin-agarose chromatography in (sodium) citrate buffer, pH 7.5, as previously reported for pooled plasma.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	23-34
6977940-7	1981	Elevation of the antithrombin III inhibitory activity in presence of heparin was apparently responsible for an increase in the antitryptic activity under conditions of severe forms of SH when content of alpha 1-antitrypsin decreased.	Heparin	69-76	serpin family A member 1	Homo sapiens	203-222
6274149-1	1981	Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient.	Heparin	122-129	complement C1r	Homo sapiens	51-54
6274149-1	1981	Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient.	Heparin	122-129	complement C1s	Homo sapiens	59-62
6274149-1	1981	Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient.	Heparin	122-129	complement C1r	Homo sapiens	67-70
6274149-1	1981	Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient.	Heparin	122-129	complement C1s	Homo sapiens	71-74
6274149-4	1981	In the presence of C1t (serum amyloid P component), C1s was firmly retained on heparin-Sepharose, which was probably due to formation of a C1s-C1t complex.	Heparin	79-86	complement C1s	Homo sapiens	52-55
6274149-4	1981	In the presence of C1t (serum amyloid P component), C1s was firmly retained on heparin-Sepharose, which was probably due to formation of a C1s-C1t complex.	Heparin	79-86	complement C1s	Homo sapiens	139-142
7031982-8	1981	Unfractionated heparin and the high molecular weight fraction enhanced ADP-induced platelet aggregation and collagen-mediated MDA production, while the low molecular weight fraction hardly affected these assays, but potently inhibited thrombin-induced MDA production.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	235-243
6168653-1	1981	We have demonstrated that human plasma contains a heparin-dependent inhibitor of thrombin that is distinguishable from antithrombin III (AT III).	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	81-89
7325396-0	1981	[Continuous heparin therapy in deep venous thrombosis and its monitoring with the Howel and thrombin times.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	92-100
6168653-2	1981	When a 1:50 dilution of plasma was incubated with greater than or equal to 0.01 U/ml heparin and 1 U/ml 125I-thrombin, the labeled thrombin B-chains became incorporated into two complexes of Mr-96,000 and Mr-85,000 that were separated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and beta-mercaptoethanol.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	131-139
6168653-4	1981	When a limiting amount of 125I-thrombin was present, the proportion of radioactivity incorporated into each of the two complexes varied with the heparin concentration.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	31-39
6168653-8	1981	The protein that combines with thrombin to form the Mr-96,000 complex was estimated to be present at a minimum concentration of 90 +/- 26 micrograms/ml (mean +/- SD) in identical to any of the known plasma protease inhibitors and that at relatively high heparin concentrations in vitro it reacts with thrombin more rapidly than does AT III.	Heparin	254-261	coagulation factor II, thrombin	Homo sapiens	31-39
7283155-0	1981	Phospholipase A2 activity of post-heparin plasma: a rapid and sensitive assay and partial characterization.	Heparin	34-41	phospholipase A2 group IB	Homo sapiens	0-16
7285133-1	1981	The fibroblast chemoattractant property of fibronectin is retained in the proteolytically produced 160 kilodalton peptide that contains the heparin binding and cell binding domains of the molecule, while the 40 kilodalton collagen binding peptide is inactive.	Heparin	140-147	fibronectin 1	Homo sapiens	43-54
7026867-1	1981	The paper contains new data on the pharmacodynamics of heparin and its interaction with the Xa factor, antithrombin III and thrombin.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	107-115
7236529-0	1981	Thrombin-induced proteolysis of human antithrombin III: an outstanding contribution of heparin.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	0-8
7236529-1	1981	Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	44-52
7236529-3	1981	Thrombin-induced release of this fragment was promoted by polydispersed heparin preparation and, to a variable degree, by all heparin fractions obtained in gel filtration.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	0-8
7236529-3	1981	Thrombin-induced release of this fragment was promoted by polydispersed heparin preparation and, to a variable degree, by all heparin fractions obtained in gel filtration.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	0-8
7236529-7	1981	On the one hand, heparin interacting with AT III and thrombin contributes to a rapid binding and neutralization of the enzyme; on the other, heparin facilitates proteolytic degradation of unbound inhibitor even in the presence of small quantities of thrombin accounting for excessive reduction of the overall inhibitory potential of AT III.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	53-61
7236529-7	1981	On the one hand, heparin interacting with AT III and thrombin contributes to a rapid binding and neutralization of the enzyme; on the other, heparin facilitates proteolytic degradation of unbound inhibitor even in the presence of small quantities of thrombin accounting for excessive reduction of the overall inhibitory potential of AT III.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	250-258
6788765-8	1981	Since the NH2-terminal ends of the 205K, 190K, 100K, and 80K fragments are the same, the results define the order of the active sites in the fibronectin molecule as gelatin-binding site, cell attachment site, and heparin-binding site.	Heparin	213-220	fibronectin 1	Homo sapiens	141-152
6457032-6	1981	One fragment (Mr = 50,000) was bound to gelatin but not to heparin, while the remaining four were bound to heparin but not to gelatin, suggesting that plasma fibronectin takes a discrete domain structure with respect to interaction with these two macromolecules.	Heparin	107-114	fibronectin 1	Homo sapiens	158-169
6457032-11	1981	These results suggest that porcine plasma fibronectin has non-identical subunit chains composed of domains which differ in interaction with heparin and in susceptibility to cathepsin B.	Heparin	140-147	fibronectin 1	Homo sapiens	42-53
7248331-6	1981	The membrane-associated lipoprotein lipase activities described here were found to be resistant to release, by heparin, from their membrane sites.	Heparin	111-118	lipoprotein lipase	Rattus norvegicus	24-42
6910459-0	1981	[Monitoring of post-operative prevention of thrombosis by low dosage heparin with the radioactive iodine fibrinogen test (author"s transl)].	Heparin	69-76	fibrinogen beta chain	Homo sapiens	105-115
6910459-5	1981	Because of the early occurrence of silent signs of deep vein thrombosis in the radioactive iodine fibrinogen test the onset of the subcutaneous heparin prophylaxis of thrombosis was shifted from the post-operative period to the pre-operative administration.	Heparin	144-151	fibrinogen beta chain	Homo sapiens	98-108
7262838-8	1981	On the other hand Intralipid plus heparin induced FFA elevation, completely block GH secretion elicited by exercise (p less than 0.05 at 20 and 40 min).	Heparin	34-41	growth hormone 1	Homo sapiens	82-84
7302907-0	1981	Biophysical characteristics of anionic density-fractionated mucosal heparins in relation to potencies in anticoagulant and thrombin-inhibition assays.	Heparin	68-76	coagulation factor II, thrombin	Homo sapiens	123-131
7295815-0	1981	[Activation by heparin-Sepharose of prothrombin conversion to prethrombin 1].	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	36-47
7295815-1	1981	Using affinity chromatography on heparin-Sepharose, homogeneous prothrombin containing no factor Xa or thrombin was separated into three components differing in their affinities for the bioadsorbent.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	64-75
7295815-4	1981	Rechromatography of component 2 provided further evidence for prothrombin modification to prethrombin 1 by heparin-Sepharose.	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	62-73
7295815-6	1981	Heparin-Sepharose probably induced changes in prothrombin conformation and the formation of a catalytic center responsible for prothrombin splitting to prethrombin 1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	46-57
7295815-6	1981	Heparin-Sepharose probably induced changes in prothrombin conformation and the formation of a catalytic center responsible for prothrombin splitting to prethrombin 1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	127-138
7238175-1	1981	The low-dose heparin prophylaxis depends upon a low-level activation of antithrombin III to prevent thrombin generation.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	76-84
7295815-7	1981	Heparin-Sepharose can be used for separation of prothrombin proteolytic products by thrombin and for isolation of prethrombin 1 and prothrombin fragment 1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	48-59
7295815-7	1981	Heparin-Sepharose can be used for separation of prothrombin proteolytic products by thrombin and for isolation of prethrombin 1 and prothrombin fragment 1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	51-59
7295815-7	1981	Heparin-Sepharose can be used for separation of prothrombin proteolytic products by thrombin and for isolation of prethrombin 1 and prothrombin fragment 1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	132-143
7471418-1	1981	This assay for heparin is based on the heparin-accelerated rate of alpha-thrombin III.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	73-81
6789496-7	1981	The variable responses observed in heparin-PRP may reflect direct interactions of heparin with platelets, and this variability may account for the conflicting results of previous studies.	Heparin	35-42	prion protein	Homo sapiens	43-46
7471418-1	1981	This assay for heparin is based on the heparin-accelerated rate of alpha-thrombin III.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	73-81
7471418-2	1981	The rate or product formation from the residual active thrombin is inversely proportional to plasma heparin content.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	55-63
7218236-0	1981	Cold insoluble globulin and heparin interactions in phagocytosis by macrophage monolayers: mechanism of heparin enhancement.	Heparin	104-111	fibronectin 1	Homo sapiens	0-23
6457413-2	1981	Heparin complexes with thrombin, plasmin, and trypsin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	23-31
6457414-2	1981	The role of heparin in the ATIII inactivation of thrombin, plasmin, and trypsin.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	49-57
7214716-3	1981	The addition of heparin to late pregnancy serum resulted in a dose-dependent decrease in the apparent PP5 concentrations, the maximal effect occurring at heparin concentrations greater than 4 U/ml.	Heparin	16-23	tissue factor pathway inhibitor 2	Homo sapiens	102-105
6791299-0	1981	Uptake and inactivation of thrombin by the fresh, glutardialdehyde or heparin treated human umbilical cord vein endothelium.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	27-35
7214716-0	1981	Specific interaction between placental protein 5 and heparin.	Heparin	53-60	tissue factor pathway inhibitor 2	Homo sapiens	29-48
7225400-6	1981	Very little lipoprotein lipase activity is released from the cell surface by heparin.	Heparin	77-84	lipoprotein lipase	Rattus norvegicus	12-30
6780552-9	1981	In contrast, thrombin modified with pyridoxal-P in the presence of heparin incorporated up to 1 mol of pyridoxal-P per mol of thrombin.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	13-21
6780552-9	1981	In contrast, thrombin modified with pyridoxal-P in the presence of heparin incorporated up to 1 mol of pyridoxal-P per mol of thrombin.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	126-134
6780552-10	1981	The heparin-protected pyridoxal-P-thrombin was only slightly inhibited in its interaction with platelets, and binding studies with the heparin-protected pyridoxal-P-125I-thrombin showed selective loss of low affinity binding but preservation of high affinity binding.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	34-42
6780552-10	1981	The heparin-protected pyridoxal-P-thrombin was only slightly inhibited in its interaction with platelets, and binding studies with the heparin-protected pyridoxal-P-125I-thrombin showed selective loss of low affinity binding but preservation of high affinity binding.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	170-178
6780552-10	1981	The heparin-protected pyridoxal-P-thrombin was only slightly inhibited in its interaction with platelets, and binding studies with the heparin-protected pyridoxal-P-125I-thrombin showed selective loss of low affinity binding but preservation of high affinity binding.	Heparin	135-142	coagulation factor II, thrombin	Homo sapiens	34-42
6780552-10	1981	The heparin-protected pyridoxal-P-thrombin was only slightly inhibited in its interaction with platelets, and binding studies with the heparin-protected pyridoxal-P-125I-thrombin showed selective loss of low affinity binding but preservation of high affinity binding.	Heparin	135-142	coagulation factor II, thrombin	Homo sapiens	170-178
6780552-11	1981	These results provide further support for the hypothesis that residues at the macromolecular binding site of thrombin are involved in the binding of thrombin to platelets and further separate this functional region of thrombin into two lysine-containing subregions, one which is protected from modification by heparin which is involved in high affinity binding, and another which is not protected by heparin which is involved in low affinity binding.	Heparin	310-317	coagulation factor II, thrombin	Homo sapiens	109-117
6780552-11	1981	These results provide further support for the hypothesis that residues at the macromolecular binding site of thrombin are involved in the binding of thrombin to platelets and further separate this functional region of thrombin into two lysine-containing subregions, one which is protected from modification by heparin which is involved in high affinity binding, and another which is not protected by heparin which is involved in low affinity binding.	Heparin	310-317	coagulation factor II, thrombin	Homo sapiens	149-157
6780552-11	1981	These results provide further support for the hypothesis that residues at the macromolecular binding site of thrombin are involved in the binding of thrombin to platelets and further separate this functional region of thrombin into two lysine-containing subregions, one which is protected from modification by heparin which is involved in high affinity binding, and another which is not protected by heparin which is involved in low affinity binding.	Heparin	310-317	coagulation factor II, thrombin	Homo sapiens	149-157
6780552-11	1981	These results provide further support for the hypothesis that residues at the macromolecular binding site of thrombin are involved in the binding of thrombin to platelets and further separate this functional region of thrombin into two lysine-containing subregions, one which is protected from modification by heparin which is involved in high affinity binding, and another which is not protected by heparin which is involved in low affinity binding.	Heparin	400-407	coagulation factor II, thrombin	Homo sapiens	109-117
6780552-11	1981	These results provide further support for the hypothesis that residues at the macromolecular binding site of thrombin are involved in the binding of thrombin to platelets and further separate this functional region of thrombin into two lysine-containing subregions, one which is protected from modification by heparin which is involved in high affinity binding, and another which is not protected by heparin which is involved in low affinity binding.	Heparin	400-407	coagulation factor II, thrombin	Homo sapiens	149-157
6780552-11	1981	These results provide further support for the hypothesis that residues at the macromolecular binding site of thrombin are involved in the binding of thrombin to platelets and further separate this functional region of thrombin into two lysine-containing subregions, one which is protected from modification by heparin which is involved in high affinity binding, and another which is not protected by heparin which is involved in low affinity binding.	Heparin	400-407	coagulation factor II, thrombin	Homo sapiens	149-157
6914196-0	1981	The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	93-164
7214716-3	1981	The addition of heparin to late pregnancy serum resulted in a dose-dependent decrease in the apparent PP5 concentrations, the maximal effect occurring at heparin concentrations greater than 4 U/ml.	Heparin	154-161	tissue factor pathway inhibitor 2	Homo sapiens	102-105
6914196-2	1981	Inhibition of thrombin, Factor IXa and Factor XIa showed similarities in the dependence on the molecular weight of heparin and was found to decrease with decreasing molecular weight.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	14-22
7214716-6	1981	The specificity of the interaction between heparin and PP5 was demonstrated by affinity chromatography with heparin as the ligand.	Heparin	43-50	tissue factor pathway inhibitor 2	Homo sapiens	55-58
7214716-6	1981	The specificity of the interaction between heparin and PP5 was demonstrated by affinity chromatography with heparin as the ligand.	Heparin	108-115	tissue factor pathway inhibitor 2	Homo sapiens	55-58
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	102-110
7240130-6	1981	The sedimentation coefficient of androgen receptor in freshly prepared cytosol was 6S, and became 7S after storage for 2 months at -80 degrees C. The 7S conversion of the receptor was reversed by treatment with heparin.	Heparin	211-218	androgen receptor	Homo sapiens	33-50
6781433-4	1981	Low dose heparin (0,15 to 0,20 ml x 2/day by subcutaneous injection) led to normalisation of the fibrinogen levels, increased the platelet count and reversed the consumptive coagulopathy.	Heparin	9-16	fibrinogen beta chain	Homo sapiens	97-107
6168228-1	1981	When commercially prepared porcine mucosal heparin is added to human plasma, some of the heparin fractions form a complex with antithrombin III activating it to an immediate inhibitor of thrombin as well as of other serine proteases.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	131-139
6168228-1	1981	When commercially prepared porcine mucosal heparin is added to human plasma, some of the heparin fractions form a complex with antithrombin III activating it to an immediate inhibitor of thrombin as well as of other serine proteases.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	131-139
6168228-2	1981	Certain fractions of heparin may complex with other proteins such as alpha 2-macroglobulin, another progressive inhibitor of thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	125-133
7297771-3	1981	The most striking abnormality of coagulation described in diabetes mellitus is a decrement in fibrinogen survival that is rapidly reversible with correction of hyperglycemia or the administration of heparin but not with aspirin and dipyridamole administration, suggesting a hypercoagulable state.	Heparin	199-206	fibrinogen beta chain	Homo sapiens	94-104
7261663-0	1981	The use of topical thrombin to reduce wound haematoma in patients receiving low-dose heparin.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	19-27
7261663-1	1981	The efficacy of topical thrombin in prevention of wound haematoma in patients receiving subcutaneous low-dose heparin was studied in a randomized, controlled trial.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	24-32
7290274-2	1981	The present study of 300 dialyses in 51 patients with prospectively assessed increased risk for bleeding describes a method for limiting heparin administration by using the thrombin clotting time to assess heparin sensitivity before dialysis and to monitor heparin levels during dialysis.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	173-181
6800936-2	1981	The binding of the alkaline phosphatase conjugated fibronectin to C1q was dose dependent and inhibited by fibronectin and by the sulfated polymers heparin and chondroitin sulfate.	Heparin	147-154	fibronectin 1	Homo sapiens	51-62
7027617-0	1981	[Insulin-heparin complex, its physiological properties].	Heparin	9-16	insulin	Homo sapiens	1-8
7440713-2	1980	ApoE was purified from the very low density lipoproteins of hypertriglyceridemic patients by heparin-agarose affinity chromatography, DEAE-cellulose chromatography, and preparative polyacrylamide gel electrophoresis.	Heparin	93-100	apolipoprotein E	Homo sapiens	0-4
6936572-4	1980	The laboratory findings in this case are commented upon, and particular emphasis is made on the measurement of coagulation factors II, V, VII-X, and VIII, the study of fibrin formation and fibrinolysis, and the changes in these parameters brought about by therapy with heparin, coagulation factors (fibrinogen, platelets), and cytostatic drugs.	Heparin	269-276	fibrinogen beta chain	Homo sapiens	299-309
7438456-2	1980	Using molecular sieve chromatography we have shown that PP5 exists in a number of different forms, and that in the presence of heparin or endogenous heparin-like substances PP5 forms complexes and polymers.	Heparin	149-156	tissue factor pathway inhibitor 2	Homo sapiens	173-176
6163408-7	1980	These findings are in agreement with the recognized influence of heparin on the release of lipoprotein lipase and show the direct relationship between heparin action and tissue ability to take up products of lipoprotein triglyceride breakdown.	Heparin	65-72	lipoprotein lipase	Rattus norvegicus	91-109
6157501-7	1980	After removing antithrombin from our media, we carried out experiments which show that heparin is effective even though thrombin, a potent mitogenic agent, is still present and active.	Heparin	87-94	coagulation factor II	Rattus norvegicus	19-27
7417517-0	1980	The heparin-accelerated neutralisation of bovine alpha and beta thrombins by antithrombin III.	Heparin	4-11	serpin family C member 1	Bos taurus	77-93
7417517-3	1980	Low and high molecular weight heparin and heparins fractionated by their affinity for antithrombin III were all able to accelerate the neutralisation of alpha and beta thrombin.	Heparin	30-37	serpin family C member 1	Bos taurus	86-102
7417517-3	1980	Low and high molecular weight heparin and heparins fractionated by their affinity for antithrombin III were all able to accelerate the neutralisation of alpha and beta thrombin.	Heparin	42-50	serpin family C member 1	Bos taurus	86-102
6452123-12	1980	Partial depolymerization of heparin led to a decrease in ability to displace lipoprotein lipase from heparin-Sepharose; however, even fragments of less than decasaccharide size showed definite enzyme-releasing activity.	Heparin	28-35	lipoprotein lipase	Rattus norvegicus	77-95
6452123-12	1980	Partial depolymerization of heparin led to a decrease in ability to displace lipoprotein lipase from heparin-Sepharose; however, even fragments of less than decasaccharide size showed definite enzyme-releasing activity.	Heparin	101-108	lipoprotein lipase	Rattus norvegicus	77-95
6773589-5	1980	On the other hand, the major components of the glycosaminoglycan fractions of the AB-CXBG-MCT-1 and AB-CXBI-MCT-1 and Furth tumors were observed to behave like heparin or heparan sulfate.	Heparin	160-167	modifier of curly tail 1	Mus musculus	108-113
7349668-1	1980	The reactions of covalently immobilized heparin, abbreviated as I-Hep, with thrombin or Factor Xa were investigated both in the presence and absence of antithrombin III, AT III.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	76-84
6448845-4	1980	Subsequently, we demonstrated that labeled heparin could be utilized in conjunction with fluorescence polarization spectroscopy to monitor the binding of mucopolysaccharide to thrombin, factor IXa, factor Xa, and plasmin.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	176-207
6448846-12	1980	The second-order rate constants for the neutralization of factor IXa or thrombin by the heparin .	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	72-80
6448846-14	1980	The second-order rate constants for the inhibition of mucopolysaccharide-factor IXa or mucopolysaccharide-thrombin interaction products by the heparin .	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	106-114
6448846-17	1980	Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	162-193
7004910-3	1980	When given in a dose inhibiting angiotensin II formation and renin-secreting effect of catecholamines, heparin also diminishes their activating effect on tubular sodium transport.	Heparin	103-110	angiotensinogen	Rattus norvegicus	32-46
6109005-4	1980	The interaction of heparin with tyrosine hydroxylase was studied in ways relating to the known interaction with antithrombin.	Heparin	19-26	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	112-124
7455997-4	1980	However, at low heparin concentration the thrombin inhibition proceeds more slowly with A-AT than with N-AT.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	42-50
7437065-0	1980	The interaction of heparin with thrombin and antithrombin.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	32-40
7418200-5	1980	Heparin affinity chromatography of HDL2 in the presence of Ca2+ and Mn2+ showed an interaction of apolipoprotein E-containing HDL2 subfraction only in conditions involving Mn2+.	Heparin	0-7	apolipoprotein E	Homo sapiens	98-114
6452123-0	1980	Interaction of lipoprotein lipase with native and modified heparin-like polysaccharides.	Heparin	59-66	lipoprotein lipase	Rattus norvegicus	15-33
6452123-2	1980	Lipoprotein lipase (EC 3.1.1.34), which was previously shown to bind to immobilized heparin, was now found to bind also to heparan sulphate and dermatan sulphate and to some extent to chondroitin sulphate.	Heparin	84-91	lipoprotein lipase	Rattus norvegicus	0-18
7349668-5	1980	Thrombin and Factor Xa were instantaneously inhibited by AT III in the presence of soluble heparin.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	0-8
7441709-7	1980	Heparin appeared to have a beneficial effect by preventing the endocapillary cellular proliferation induced by injections of DNA-mBSA and LPS.	Heparin	0-7	toll-like receptor 4	Mus musculus	138-141
6160565-0	1980	[Studies on the effect of heparin and hydrocortisone on the activity of renal erythropoietin inhibitor in experimental kidney damage].	Heparin	26-33	erythropoietin	Homo sapiens	78-92
7444870-0	1980	Fractionation of heparin by chromatography on immobilized thrombin.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	58-66
7407251-1	1980	Collagen-fibronectin complexes, formed by binding of fibronectin to gelatin or collagen insolubilized on Sepharose, were found to bind 20-40% of radioactivity in [35S]heparin.	Heparin	167-174	fibronectin 1	Homo sapiens	9-20
7407251-1	1980	Collagen-fibronectin complexes, formed by binding of fibronectin to gelatin or collagen insolubilized on Sepharose, were found to bind 20-40% of radioactivity in [35S]heparin.	Heparin	167-174	fibronectin 1	Homo sapiens	53-64
7407251-2	1980	Fibronectin attached directly to Sepharose also bound [35S]heparin, while gelatin-Sepharose without fibronectin did not.	Heparin	59-66	fibronectin 1	Homo sapiens	0-11
7407251-5	1980	Heparin as well as highly sulfate heparan sulfate and hyaluronic acid brought about agglutination of plastic beads coated with gelatin when fibronectin was present.	Heparin	0-7	fibronectin 1	Homo sapiens	140-151
7027617-1	1981	An insulin-heparin complex was obtained in vitro.	Heparin	11-18	insulin	Homo sapiens	3-10
7027617-3	1981	Contrary to insulin, administration of the insulin-heparin complex increased the anticoagulation properties of blood and exhibited the non-enzymatic fibrinolytic activity towards the unstabilized fibrin both in presence or in absence of inhibitors of fibrinolysis, caused by plasmin.	Heparin	51-58	insulin	Homo sapiens	12-19
7027617-3	1981	Contrary to insulin, administration of the insulin-heparin complex increased the anticoagulation properties of blood and exhibited the non-enzymatic fibrinolytic activity towards the unstabilized fibrin both in presence or in absence of inhibitors of fibrinolysis, caused by plasmin.	Heparin	51-58	insulin	Homo sapiens	43-50
7444858-0	1980	Inhibition of thrombin on surfaces coated with immobilized heparin and heparin-like polysaccharides: a crucial non-thrombogenic principle.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	14-22
7395817-6	1980	The thrombin time was found to be more closely related to the plasma heparin concentration than was the activated partial thromboplastin time.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	4-12
7395817-8	1980	It is suggested that the thrombin time is a good and safe method for monitoring heparin treatment.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	25-33
6105392-1	1980	When prostacyclin (5 ng kg-1 min-1) was given during dialysis it enhanced the biological activity of heparin and prevented the activation and consumption of platelets.	Heparin	101-108	CD59 molecule (CD59 blood group)	Homo sapiens	29-34
7378429-1	1980	Cultured cells derived from the stromal-vascular fraction of rat epididymal adipose tissue have been used to study the release of lipoprotein lipase in response to heparin.	Heparin	164-171	lipoprotein lipase	Rattus norvegicus	130-148
7397357-4	1980	A previously suggested method for isolation of heparin fractions H-3 and H-4 makes it possible to obtain preparations that do not contain the admixtures of other proteoglycans.	Heparin	47-54	H3 clustered histone 14	Homo sapiens	65-76
6158117-0	1980	Interaction of C1s and C1 inactivator in the presence of heparin, dextran sulfate and protamine sulfate.	Heparin	57-64	complement C1s	Homo sapiens	15-25
6156674-0	1980	Heparin enhances the rate of binding of fibronectin to collagen.	Heparin	0-7	fibronectin 1	Homo sapiens	40-51
6158112-0	1980	Heparin prevents thrombin inhibition by alpha 2 macroglobulin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	17-25
7378498-0	1980	[Regulation of alpha and beta/gamma-thrombin activity by heparin and indole].	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	36-44
7378498-5	1980	The fact that alpha- and beta/gamma-thrombin partially retain their catalytic properties even at a 5-fold molar excess of the inhibitor indicates that heparin binds to the thrombin molecule at a site other than the active center.	Heparin	151-158	coagulation factor II, thrombin	Homo sapiens	172-180
7436418-0	1980	Studies on the interaction of heparin with thrombin, antithrombin, and other plasma proteins.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	43-51
7378498-4	1980	Heparin was shown to form an equimolar stoicheometric complex with both alpha- and beta/gamma-thrombin, which results in 40% inhibition of the TAME-esterase, clotting and prothrombinolytic activities of alpha-thrombin and 25% and 40% inhibition of the TAME-esterase and prothrombinolytic activity of beta/gamma-thrombin, respectively.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	94-102
7378498-4	1980	Heparin was shown to form an equimolar stoicheometric complex with both alpha- and beta/gamma-thrombin, which results in 40% inhibition of the TAME-esterase, clotting and prothrombinolytic activities of alpha-thrombin and 25% and 40% inhibition of the TAME-esterase and prothrombinolytic activity of beta/gamma-thrombin, respectively.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	174-182
7378498-4	1980	Heparin was shown to form an equimolar stoicheometric complex with both alpha- and beta/gamma-thrombin, which results in 40% inhibition of the TAME-esterase, clotting and prothrombinolytic activities of alpha-thrombin and 25% and 40% inhibition of the TAME-esterase and prothrombinolytic activity of beta/gamma-thrombin, respectively.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	174-182
7378498-5	1980	The fact that alpha- and beta/gamma-thrombin partially retain their catalytic properties even at a 5-fold molar excess of the inhibitor indicates that heparin binds to the thrombin molecule at a site other than the active center.	Heparin	151-158	coagulation factor II, thrombin	Homo sapiens	36-44
7378498-7	1980	This finding suggests that the localization of binding sites of heparin and the added TAME molecule (and, therefore, indole) in the thrombin molecule is different.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	132-140
6986741-4	1980	At the endothelium heparin acts to prevent endothelial injury, prevent thrombin generation, prevent platelet adhesion to endothelium, and to decrease uptake of serum lipoproteins.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	71-79
7374009-3	1980	Preliminary intravenous injection of small doses of heparin into animals with depressed function of the anticoagulation system and low level of heparin in blood stimulates and promotes the binding of thrombin by antithrombin III under conditions of increased thrombinogenesis following intravenous injection of tissue thromboplastin.	Heparin	52-59	coagulation factor II	Rattus norvegicus	200-208
7374009-3	1980	Preliminary intravenous injection of small doses of heparin into animals with depressed function of the anticoagulation system and low level of heparin in blood stimulates and promotes the binding of thrombin by antithrombin III under conditions of increased thrombinogenesis following intravenous injection of tissue thromboplastin.	Heparin	144-151	coagulation factor II	Rattus norvegicus	200-208
6444419-8	1980	The isolated proteoglycan was indistinguishable from commercial heparin when analyzed in terms of its ability to act as a cofactor in the antithrombin III inhibition of thrombin.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	142-150
7359219-5	1980	From 35 to 80 minutes after feeding the LPL activity released by heparin from hearts of the glucose fed animals decreased 85% compared to the LPL activity released from hearts of the control group fed water.	Heparin	65-72	lipoprotein lipase	Rattus norvegicus	40-43
7359219-8	1980	The LPL activity remaining in the heart tissue after perfusion with heparin was not significantly different in the experimental and control groups.	Heparin	68-75	lipoprotein lipase	Rattus norvegicus	4-7
7359219-1	1980	The effect of feeding various carbohydrates on the activity of lipoprotein lipase (LPL) released by heparin from perfused rat heart was investigated.	Heparin	100-107	lipoprotein lipase	Rattus norvegicus	63-81
7359219-1	1980	The effect of feeding various carbohydrates on the activity of lipoprotein lipase (LPL) released by heparin from perfused rat heart was investigated.	Heparin	100-107	lipoprotein lipase	Rattus norvegicus	83-86
7385105-0	1980	On the binding of thrombin by heparin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	18-26
6768161-0	1980	Altered inactivation of trinitrophenylated thrombin by antithrombin III in the presence of heparin.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	43-51
7368151-1	1980	We describe a new method for determining the biological activity of heparin in plasma with use of thrombin and the substrate Tos-Gly-Pro-Arg-pNA.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	98-106
7368180-0	1980	A differential effect of low-affinity heparin on the inhibition of thrombin and factor Xa by antithrombin.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	67-75
7356660-7	1980	When the modification reaction was performed with added heparin, the extent of modification was decreased and the heparin-promoted enhancement of thrombin inactivation was preserved.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	146-154
7356660-7	1980	When the modification reaction was performed with added heparin, the extent of modification was decreased and the heparin-promoted enhancement of thrombin inactivation was preserved.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	146-154
7191289-1	1980	2nd communication: Chemical analysis of the carbohydrate content and determination of the biological activity of a new potent heparin preparation in vitro, using protamine neutralization and amidolytic methods for factor Xa and thrombin.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	228-236
7191289-2	1980	A new potent heparin preparation was further characterized for carbohydrate content and for biological activities in vitro using the protamine neutralization test and amidolytic methods for factor Xa and thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	204-212
7191289-5	1980	The amidolytic method using chromogenic substrates S-2222 for factor Xa and S-2238 for thrombin demonstrated that the new heparin was also at least two times more effective than commercial heparin in increasing the rate of inactivation of these serin proteases through antithrombin III.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	87-95
7417594-3	1980	Heparin stimulates the inactivation of Factor Xa and thrombin by AT III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	53-61
6155267-5	1980	In patients with the lowest fibrinogen T/2 and platelet count, heparin infusion therapy returned the fibrinogen half-life to normal range.	Heparin	63-70	fibrinogen beta chain	Homo sapiens	28-38
7417594-10	1980	Hep, like soluble AT III and heparin, instantaneously neutralized both thrombin and Factor Xa.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	71-79
6155267-5	1980	In patients with the lowest fibrinogen T/2 and platelet count, heparin infusion therapy returned the fibrinogen half-life to normal range.	Heparin	63-70	fibrinogen beta chain	Homo sapiens	101-111
7376137-0	1980	Effect of monovalent cations on the heparin-enhanced antithrombin III/thrombin reaction.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	57-65
7376139-0	1980	Hydrolysis of N-alpha-benzoyl-L-phenylalanyl-L-valyl-L-arginine-p-nitroanilide by human alpha thrombin in the presence of heparin.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	94-102
316700-0	1979	Effect of heparin on the inhibition of thrombin by alpha 1-proteinase inhibitor.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	39-47
315885-1	1979	So far the Cl inactivator, alpha 2-macroglobulin, antithrombin III (in the presence of heparin), and alpha 1-antitrypsin have been identified as inhibitors of plasma kallikrein; alpha 1-antitrypsin reacts slowly also with tissue kallikreins.	Heparin	87-94	serpin family C member 1	Bos taurus	50-66
542933-0	1979	Thrombin time dilution test: a simple method for the control of heparin therapy.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	0-8
476156-1	1979	The ability of heparin fractions of different molecular weight to potentiate the action of antithrombin III against the coagulation factors thrombin and Xa has been examined in purified reaction mixtures and in plasma.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	95-103
508775-2	1979	In rat, lipoprotein lipase and hepatic triacylglycerol lipase were separated on a heparin-Sepharose affinity chromatography.	Heparin	82-89	lipoprotein lipase	Rattus norvegicus	8-26
508775-2	1979	In rat, lipoprotein lipase and hepatic triacylglycerol lipase were separated on a heparin-Sepharose affinity chromatography.	Heparin	82-89	lipase C, hepatic type	Rattus norvegicus	31-61
120212-0	1979	Chromatography of heparin on sepharose-lysine: molecular size fractionation and its relevance to thrombin and antithrombin III binding.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	97-105
92343-7	1979	Lipoprotein lipase is known to bind to heparin and some related polysacchrides.	Heparin	39-46	lipoprotein lipase	Rattus norvegicus	0-18
476156-3	1979	High molecular weight heparin fractions were found to have higher anticoagulant activities than low molecular weight heparin when studied with both thrombin and Xa incubation mixtures in purified mixtures and in plasma.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	148-156
486540-0	1979	Inhibition of factor VIII-associated platelet aggregation by heparin and dextran sulfate, and its mechanism.	Heparin	61-68	coagulation factor VIII	Bos taurus	14-25
111639-7	1979	Pretreatment with heparin prevents the consumption of fibrinogen and antithrombin III but does not prevent the increase in fibrin split products which was observed.	Heparin	18-25	fibrinogen beta chain	Homo sapiens	54-64
316747-0	1979	Clearance of alpha 1-antitrypsin isoelectric focusing patterns in blood samples treated with heparin.	Heparin	93-100	serpin family A member 1	Homo sapiens	13-32
316747-1	1979	Plasma samples, whose typing for alpha 1-AT is made difficult or impossible because of an excess of heparin used as anticoagulant, can be treated very effectively with protamine sulphate.	Heparin	100-107	serpin family A member 1	Homo sapiens	33-43
486540-4	1979	Both human and bovine factor VIII have a strong affinity for dextran sulfate with high sulfur content and a weak affinity for heparin, but no affinity for dextran sulfate with low sulfur content.	Heparin	126-133	coagulation factor VIII	Bos taurus	22-33
468513-3	1979	The formation product ratio (FPR, limit of metastability or the minimum supersaturation required for spontaneous nucleation) of calcium oxalate was increased 29 per cent by 0.05 mg of heparin per liter, and by 70 per cent with 1 mg of heparin per liter.	Heparin	184-191	formyl peptide receptor 1	Homo sapiens	29-32
505364-1	1979	Modification of 12 arginine residues of bovine Factor Xa with 1,2-cyclohexanedione has resulted in a decrease in heparin sensitivity of the reaction between enzyme and antithrombin-III, whereas the antithrombin-III sensitivity of modified Factor Xa was only slightly affected.	Heparin	113-120	serpin family C member 1	Bos taurus	168-184
505364-2	1979	It is suggested that heparin accelerates the Factor Xa-antithrombin-III reaction by interacting with Factor Xa.	Heparin	21-28	serpin family C member 1	Bos taurus	55-71
462354-6	1979	The fall in fibrinogen was so low in some patients that the routine administration of a conventional dosage of heparin could be dangerous.	Heparin	111-118	fibrinogen beta chain	Homo sapiens	12-22
486155-1	1979	The inactivation of thrombin and factor Xa by antithrombin was determined in the presence of heparin fractions of different molecular weights and with high affinity for antithrombin.	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	20-28
486540-5	1979	From these results, it is suggested that dextran sulfate or heparin binds directly the human and bovine factor VIII, which is an essential factor for the maintenance of the weak interplatelet bonds, and either inhibits or reverses the platelet aggregation.	Heparin	60-67	coagulation factor VIII	Bos taurus	104-115
486540-1	1979	Both ristocetin-induced aggregation in the presence of human factor VIII and bovine factor VIII-induced aggregation of washed normal human platelets were inhibited or reversed by the addition of heparin or dextran sulfate.	Heparin	195-202	coagulation factor VIII	Bos taurus	61-72
486540-1	1979	Both ristocetin-induced aggregation in the presence of human factor VIII and bovine factor VIII-induced aggregation of washed normal human platelets were inhibited or reversed by the addition of heparin or dextran sulfate.	Heparin	195-202	coagulation factor VIII	Bos taurus	84-95
486540-3	1979	In order to study the mechanism of actions of dextran sulfate and heparin, the affinity chromatographic experiment of factor VIII in human and bovine plasma, respectively, was carried out by using a dextran sulfate- and a heparin-Agarose column.	Heparin	66-73	coagulation factor VIII	Bos taurus	118-129
486540-3	1979	In order to study the mechanism of actions of dextran sulfate and heparin, the affinity chromatographic experiment of factor VIII in human and bovine plasma, respectively, was carried out by using a dextran sulfate- and a heparin-Agarose column.	Heparin	222-229	coagulation factor VIII	Bos taurus	118-129
155067-1	1979	Effect of phosphopyridoxylation on the interaction of thrombin with heparin.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	54-62
453082-0	1979	Prothrombin time after heparin removal.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	0-11
453082-4	1979	The mean prothrombin time for Group II, 18.2 +/- 4.9 sec, lengthened with 5 u/ml heparin to 35.5 +/- 16.2 sec, and returned to 19.2 +/- 5.0 (r = 0.9763) after chromatography.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	9-20
453082-6	1979	This means that virtually all prothrombin time reagent systems can be employed to monitor concurrent heparin and coumarin anticoagulation.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	30-41
447077-1	1979	Heparin is a naturally occurring anticoagulant drug that combines with anti-thrombin III to inhibit many steps of the coagulation pathway.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	76-84
316999-4	1979	Affinity chromatography on heparin-Sepharose separated the proteins since alpha 1-AT did not bind to the matrix.	Heparin	27-34	serpin family A member 1	Homo sapiens	74-84
470560-0	1979	Plasma heparin estimation based upon a thrombin clotting time technique.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	39-47
437704-3	1979	In the presence of heparin, however, solutions of native collagen type III, and fibronectin produced precipitates at an ionic strength of 0.2.	Heparin	19-26	fibronectin 1	Homo sapiens	80-91
437704-5	1979	Heparin also enhanced the formation of insoluble complexes from fibronectin and denatured collagen type I and type III.	Heparin	0-7	fibronectin 1	Homo sapiens	64-75
437704-6	1979	In the absence of collagen 125I-fibronectin was partially precipitated by heparin.	Heparin	74-81	fibronectin 1	Homo sapiens	32-43
437704-9	1979	It is suggested that heparin induced the transition of fibronectin from a globular to an elongated form, capable of forming filamentous precipitates which adsorb native collagen.	Heparin	21-28	fibronectin 1	Homo sapiens	55-66
420817-4	1979	These spectral results indicate that the thrombin-antithrombin III complex formed in the presence of heparin differs in its conformation from that produced in its absence.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	41-49
89015-3	1979	In the presence of heparin the rate of inhibition of thrombin clotting activity by alpha-2-macroglobulin is strongly decreased.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	53-61
89015-4	1979	Heparin binds to thrombin, impairing the formation of thrombin-alpha-2-macroglobulin complex.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	17-25
89015-4	1979	Heparin binds to thrombin, impairing the formation of thrombin-alpha-2-macroglobulin complex.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	54-62
429567-11	1979	Heparin infusion during hyperglycemia normalized the fibrinogen kinetics of hyperglycemic diabetic patients, suggesting that reduced fibrinogen survival during hyperglycemia is secondary to an effect on thrombin or one of its antagonists.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	53-63
89015-5	1979	These data show that heparin paradoxically protects thrombin from inhibition by alpha-2-macroglobulin whereas it increases the enzyme inhibition by antithrombin III.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	52-60
429567-11	1979	Heparin infusion during hyperglycemia normalized the fibrinogen kinetics of hyperglycemic diabetic patients, suggesting that reduced fibrinogen survival during hyperglycemia is secondary to an effect on thrombin or one of its antagonists.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	133-143
532498-6	1979	Due to their antithrombin action heparin, hirudin, and APPA prevent the thrombin-induced fibrin formation and thus the induction of secondary fibrinolysis.	Heparin	33-40	coagulation factor II	Rattus norvegicus	17-25
436823-0	1979	Studies on the mechanism of the rate-enhancing effect of heparin on the thrombin-antithrombin III reaction.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	72-80
504072-5	1979	Heparin cofactor activity was demonstrated by immediate inactivation of thrombin by antithrombin III in the presence of minute quantities of heparin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	72-80
436823-1	1979	The rate of the reaction between thrombin and antithrombin III is greatly increased in the presence of heparin.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	33-41
436823-4	1979	The strength of the binding of the two heparin fractions to antithrombin III and thrombin, respectively, was determined by a crossed immunoelectrophoresis technique.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	64-72
436823-6	1979	In contrast, thrombin showed equal binding affinity for both heparin fractions.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	13-21
436823-7	1979	The ability of the two heparin fractions to catalyse the inhibition of thrombin by antithrombin III was determined and was found to be much greater for the high activity heparin fraction.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	71-79
436823-7	1979	The ability of the two heparin fractions to catalyse the inhibition of thrombin by antithrombin III was determined and was found to be much greater for the high activity heparin fraction.	Heparin	170-177	coagulation factor II, thrombin	Homo sapiens	71-79
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	37-45
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	54-62
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	37-45
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	54-62
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	37-45
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	54-62
553509-7	1979	In the treatment of DIC priority is given to intravenous application of AT-III complex human, concentrated and purified, activated in vitro with heparin.	Heparin	145-152	solute carrier family 25 member 10	Homo sapiens	20-23
759824-7	1979	The contributions of H-TGL and LPL to the total plasma triacylglycerol hydrolase (TGH) activity depend on the amount of heparin injected and the time of blood withdrawal after heparin injection.	Heparin	120-127	lipoprotein lipase	Rattus norvegicus	31-34
759824-8	1979	H-TGL was maximally released at higher heparin (50 U/250 g body weight) concentrations, compared to LPL which was maximally released at lower heparin (5 U/250 g body weight) concentrations.	Heparin	142-149	lipoprotein lipase	Rattus norvegicus	100-103
531528-6	1979	A negative correlation was found between the heparin requirement and serum albumin.	Heparin	45-52	albumin	Homo sapiens	69-82
531528-7	1979	It is suggested, that serum albumin might facilitate the action of AT-III and heparin.	Heparin	78-85	albumin	Homo sapiens	22-35
494159-0	1979	Molecular weight dependency of the heparin potentiated inhibition of thrombin and activated factor X.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	69-77
494182-0	1979	The antiheparin effect of alpha1-acid glycoprotein probably due to steric hindrance of the heparin-thrombin interaction.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	99-107
516007-0	1979	The anti-inflammatory action of heparin: heparin as an antagonist to histamine, bradykinin and prostaglandin E1.	Heparin	32-39	kininogen 1	Homo sapiens	80-90
516007-0	1979	The anti-inflammatory action of heparin: heparin as an antagonist to histamine, bradykinin and prostaglandin E1.	Heparin	41-48	kininogen 1	Homo sapiens	80-90
504072-6	1979	It also could be demonstrated that thrombin inactivation by antithrombin III occurs by formation of a bimolecular complex whose rate of formation is markedly enhanced by minute quantities of heparin.	Heparin	191-198	coagulation factor II, thrombin	Homo sapiens	35-43
749267-0	1978	Effect of heparin-binding to thrombin on thrombin activity measured with a chromogenic substrate.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	41-49
743219-10	1978	The activity of high-affinity heparin (i.e. molecules containing high-affinity binding sites for antithrombin), determined either by a whole-blood clotting procedure or by thrombin inactivation in the presence of antithrombin, thus remained dependent on molecular weight.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	101-109
743219-12	1978	One explanation could be a requirement for binding of thrombin to the heparin chain adjacent to antithrombin.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	54-62
708377-0	1978	Effect of heparin on thrombin inactivation by antithrombin-III.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	21-29
81362-10	1978	Both binding activity and heparin precipitability appeared to correlate with an increase in arginine-rich apoprotein (apo-E) in the active H.D.L.	Heparin	26-33	apolipoprotein E	Homo sapiens	106-116
81362-10	1978	Both binding activity and heparin precipitability appeared to correlate with an increase in arginine-rich apoprotein (apo-E) in the active H.D.L.	Heparin	26-33	apolipoprotein E	Homo sapiens	118-123
707979-4	1978	The initial dilution step in the thrombin clotting time method bypasses interference by small amounts of heparin or other inhibitors in jaundiced samples which may present a problem in the measurement of the rate of density development in the clot density method.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	33-41
708377-1	1978	The inactivation of thrombin by heat and by its physiological inhibitor, antithrombin-III, shows quite different dependence on heparin concentration.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	20-28
708377-2	1978	Heparin at 250 microgram/ml protects thrombin against heat inactivation, and thrombin behaves heterogeneously in this reaction.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	37-45
708377-4	1978	When heparin is present, heat inactivation of the protected thrombin species proceeds with deltaH+ = 88 kJ/mol and is independent of temperature in the same range.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	60-68
708377-5	1978	On the other hand, heparin at 0.125-2.5 microgram/ml accelerates the thrombin-antithrombin-III reaction.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	69-77
708377-9	1978	On the basis of these data we suggest a mechanism of action of heparin in the thrombin-antithrombin-III reaction which accounts for all the important features of the latter and seems to unify the different hypotheses that have been advanced.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	78-86
711985-0	1978	[Complex formation reaction between heparin and fibrinogen in normal subjects and in disease].	Heparin	36-43	fibrinogen beta chain	Homo sapiens	48-58
78728-1	1978	Evidence for a ternary complex of heparin cofactor thrombin and heparin.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	51-59
701764-5	1978	Presently it would appear desirable to employ agents to (1) increase blood flow and decrease blood viscosity, such as dextran 70; (2) decrease platelet functions, such as aspirin-type drugs; (3) mitigate against the actions of thrombin on platelets and fibrinogen using low-dose heparin; (4) reduce anxiety and vasospasm using chlorpromazine or Thorazine.	Heparin	279-286	coagulation factor II, thrombin	Homo sapiens	227-235
567858-0	1978	Assay of plasma heparin using thrombin and the chromogenic substrate H-D-Phe-Pip-Arg-pNA (S-2238).	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	30-38
567858-0	1978	Assay of plasma heparin using thrombin and the chromogenic substrate H-D-Phe-Pip-Arg-pNA (S-2238).	Heparin	16-23	prolactin induced protein	Homo sapiens	77-80
78728-2	1978	The interaction of heparin with chemically modified thrombin and heparin cofactor is studied.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	52-60
78728-3	1978	Amidinated heparin cofactor does not bind to heparin-agarose and the reaction rate of the amidinated inhibitor with unmodified thrombin is not affected by heparin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	127-135
78728-6	1978	Affinity chromatography of diisopropylphosphoryl thrombin on heparin cofactor coupled to Sephadex G--50 is used to study the binding of heparin cofactor and thrombin to heparin.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	49-57
78728-6	1978	Affinity chromatography of diisopropylphosphoryl thrombin on heparin cofactor coupled to Sephadex G--50 is used to study the binding of heparin cofactor and thrombin to heparin.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	157-165
78728-9	1978	However, after treatment of the columns with a heparin solution, thrombin binds tightly, and is eluted at high ionic strength.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	65-73
78728-10	1978	Bound thrombin can also be eluted with either excess non-radioactive thrombin or excess free heparin.	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	6-14
78728-12	1978	The ability of heparin to couple solution-phase thrombin to solid-phase heparin cofactor indicates that a ternary complex is formed.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	48-56
78728-13	1978	Analysis of the binding of the proteins to heparin by a dye displacement method suggests that at least one site on heparin binds to thrombin but not to heparin cofactor.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	132-140
78728-13	1978	Analysis of the binding of the proteins to heparin by a dye displacement method suggests that at least one site on heparin binds to thrombin but not to heparin cofactor.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	132-140
78728-13	1978	Analysis of the binding of the proteins to heparin by a dye displacement method suggests that at least one site on heparin binds to thrombin but not to heparin cofactor.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	132-140
78728-14	1978	Further support for a catalytic role for heparin derives from the ability of catalytic concentrations of heparin to enhance the rate of hydrolysis of prothrombin by thrombin, another protein pair which bind mutually to heparin.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	153-161
78728-14	1978	Further support for a catalytic role for heparin derives from the ability of catalytic concentrations of heparin to enhance the rate of hydrolysis of prothrombin by thrombin, another protein pair which bind mutually to heparin.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	153-161
78728-14	1978	Further support for a catalytic role for heparin derives from the ability of catalytic concentrations of heparin to enhance the rate of hydrolysis of prothrombin by thrombin, another protein pair which bind mutually to heparin.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	153-161
667338-2	1978	Under these conditions the half-life of heparin-35S increased from 1.6 h in control animals to 2.35 h in the animals after intravenous injection of a threshold dose of thrombin causing activation of the anticoagulation system.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	168-176
705692-0	1978	Thrombin generation and neutralization test (TGNT) - a simple, practical, and sensitive assay for plasma heparin quantitation.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	0-8
694832-0	1978	Assay for plasma heparin using a synthetic peptide substrate for thrombin: introduction of the fluorophore aminoisophthalic acid, dimethyl ester.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	65-73
99316-5	1978	These results indicate that the abnormal turnover of labelled plasminogen and prothrombin in cirrhosis of the liver is due to two mechanisms; increased breakdown, reversible by heparin administration, and impaired synthesis.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	78-89
207461-1	1978	Plasma high-density lipoprotein is commonly estimated by measuring the cholesterol remaining in plasma supernatant solutions after other lipoproteins, which contain apolipoprotein B, are precipitated with heparin and Mn2+.	Heparin	205-212	apolipoprotein B	Homo sapiens	165-181
673830-7	1978	Thus, in the polysulphate group, heparin has the highest affinity for antithrombin III, liquoid for fibrinogen and dextran sulphate for beta 2-glycoprotein I.	Heparin	33-40	fibrinogen beta chain	Homo sapiens	100-110
675585-0	1978	Studies on the binding of heparin to prothrombin and thrombin and the effect of heparin-binding on thrombin activity.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	40-48
675585-0	1978	Studies on the binding of heparin to prothrombin and thrombin and the effect of heparin-binding on thrombin activity.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	53-61
26436-4	1978	Activation of the DNA and RNA synthesis in the eucaryotic cells, their nuclei and chromatin under the effect of low heparin doses should be associated not with the H1 histone dissociation, but with the dissociation of histones moderately rich in lysine--H2a, and, probably, H2b.	Heparin	116-123	tubulin alpha 4a	Homo sapiens	254-257
347919-7	1978	Heparin retards the thrombin-fibrinogen reaction, but otherwise the effectiveness of heparin as an anticoagulant depends on antithrombin III in laboratory experiments, as well as in therapeutics.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	20-28
646831-4	1978	The mean fibrinogen half-life of 8 patients given intravenous heparin increased to within one standard deviation of normal, a finding that suggested that the fibrinogen molecule in these patients was capable of normal survival.	Heparin	62-69	fibrinogen beta chain	Homo sapiens	9-19
646831-4	1978	The mean fibrinogen half-life of 8 patients given intravenous heparin increased to within one standard deviation of normal, a finding that suggested that the fibrinogen molecule in these patients was capable of normal survival.	Heparin	62-69	fibrinogen beta chain	Homo sapiens	158-168
149422-0	1978	[Importance of the fibrinogen-heparin complex in the fibrinolytic activity of the blood euglobulin fraction after the intravenous administration of thrombin or plasmin].	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	148-156
621432-1	1978	A radioimmunoassay has been developed for the measurement of PF-4--a chemically well-defined heparin-neutralizing molecule.	Heparin	93-100	platelet factor 4 variant 1	Homo sapiens	61-68
631129-0	1978	Decreased heparin sensitivity of cycholhexanedione-modified thrombin.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	60-68
631129-1	1978	Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	42-50
631129-1	1978	Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	178-186
631129-2	1978	It is suggested that heparin accelerates the thrombin antithrombin-III reaction by interacting with thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	45-53
631129-2	1978	It is suggested that heparin accelerates the thrombin antithrombin-III reaction by interacting with thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	58-66
755671-2	1978	Eight dogs (four males and four females) received subcutaneous injections of heparin at 250 units/kg bid, seven days a week.	Heparin	77-84	BH3 interacting domain death agonist	Canis lupus familiaris	101-104
753192-5	1978	This conversion is thrombin-dependent might be blocked by heparin.	Heparin	58-65	coagulation factor II	Rattus norvegicus	19-27
202660-9	1978	Additional observations suggested that, for convenience, the heparin and Mn(2+) can be added simultaneously as a combined reagent, that samples can be incubated for 10 minutes at room temperature before centrifugation, and that turbid supernates from hypertriglyceridemic samples can usually be made free of apoB-associated lipoproteins by centrifugation at 12,000 g for 10 minutes.	Heparin	61-68	apolipoprotein B	Homo sapiens	308-312
33082-2	1978	When serial fibrinogen levels fell below 100 mg% and the prothrombin time was significantly prolonged, intravenously injected heparin corrected hypofibrinogenemia.	Heparin	126-133	fibrinogen beta chain	Homo sapiens	12-22
33082-2	1978	When serial fibrinogen levels fell below 100 mg% and the prothrombin time was significantly prolonged, intravenously injected heparin corrected hypofibrinogenemia.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	57-68
658774-1	1978	Methodological problems encountered using chromogenic substrates on thrombin and Xa are discussed: (1) influence of substrate on inhibitor; (2) influence of heparin; (3) optimal concentrations; (4) specificity; (5) denatured enzymes, and (6) natural versus chromogenic substrates.	Heparin	157-164	coagulation factor II, thrombin	Homo sapiens	68-76
413828-6	1977	These enzymes are very similar to RNase A in that they are inhibited by heparin, show preferential hydrolysis of C5"-O-P linkages adjacent to a cytosine nucleotide rather than a uracil nucleotide, and in their antigenic properties.	Heparin	72-79	ribonuclease pancreatic	Bos taurus	34-41
588723-1	1977	The accelerating effect of intact human erythrocytes upon the thrombin time of plasma (deprothrombinized, thrombocyte depleted) was independent of the presence of calcium ions, preincubation, erythrocytes and plasma, and was not accompanied by a decrease of the free heparin level in the plasma.	Heparin	267-274	coagulation factor II, thrombin	Homo sapiens	62-70
72575-6	1977	A considerably different sensitivity to heparin could be observed in the single PRP"s.	Heparin	40-47	prion protein	Homo sapiens	80-83
72575-7	1977	A special method was found out to exclude the influence of the heparin-sensitivity of the PRP"s to compare the special effects of the heparins.	Heparin	63-70	prion protein	Homo sapiens	90-93
74248-3	1977	Heparin facilitated complex-formation between alpha-thrombin and antithrombin-III, whereas inactivation of beta-thrombin by antithrombin was only slightly influenced, even at a heparin concentration two orders of magnitude higher.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	52-60
74248-3	1977	Heparin facilitated complex-formation between alpha-thrombin and antithrombin-III, whereas inactivation of beta-thrombin by antithrombin was only slightly influenced, even at a heparin concentration two orders of magnitude higher.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	69-77
146278-0	1977	Role of heparin in the inactivation of thrombin, factor Xa, and plasmin by antithrombin III.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	39-47
601748-0	1977	Heparin-like effect of polymethacrylic acid on the reaction between thrombin and antithrombin-III.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	68-76
601749-0	1977	Decreased binding of heparin to antithrombin following the interaction between antithrombin and thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	36-44
601750-0	1977	Purification of thrombin by affinity chromatography on immobilized heparin.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	16-24
19499-0	1977	Interactions among heparin, cold-insoluble globulin, and fibrinogen in formation of the heparin-precipitable fraction of plasma.	Heparin	88-95	fibronectin 1	Homo sapiens	28-51
579513-0	1977	Effect of calcium ion on the interaction between thrombin and heparin.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	49-57
579513-5	1977	Namely, at 4.5 x 10(-6)M, 9 x 10(-6)M, 1.8 x 10(-5)M and 3.6 x 10(-5)M heparin concentrations, the rate constants were 0.27 min -1, 0.17 min-1, 0.11 min-1 and 0.06 min-1, respectively.	Heparin	71-78	CD59 molecule (CD59 blood group)	Homo sapiens	137-142
579513-5	1977	Namely, at 4.5 x 10(-6)M, 9 x 10(-6)M, 1.8 x 10(-5)M and 3.6 x 10(-5)M heparin concentrations, the rate constants were 0.27 min -1, 0.17 min-1, 0.11 min-1 and 0.06 min-1, respectively.	Heparin	71-78	CD59 molecule (CD59 blood group)	Homo sapiens	149-154
579513-5	1977	Namely, at 4.5 x 10(-6)M, 9 x 10(-6)M, 1.8 x 10(-5)M and 3.6 x 10(-5)M heparin concentrations, the rate constants were 0.27 min -1, 0.17 min-1, 0.11 min-1 and 0.06 min-1, respectively.	Heparin	71-78	CD59 molecule (CD59 blood group)	Homo sapiens	149-154
579513-7	1977	The kinetics of enzyme denaturation was not affected by calcium ions, whereas in the presence of heparin the inactivation rate of thrombin changed, i.e.  calcium ions abolished the biphasic character of time course of thermal denaturation.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	130-138
579513-8	1977	Thus, the data suggest that calcium ions contribute to the effect of heparin on thrombin.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	80-88
589020-0	1977	Fan-shaped shadows due to pulmonary artery catheters: heparin prophylaxis.	Heparin	54-61	neutral sphingomyelinase activation associated factor	Homo sapiens	0-3
19499-0	1977	Interactions among heparin, cold-insoluble globulin, and fibrinogen in formation of the heparin-precipitable fraction of plasma.	Heparin	88-95	fibrinogen beta chain	Homo sapiens	57-67
19499-1	1977	Fibrinogen and the cold-insoluble globulin of plasma (CIg) are the main protein components of the heparin-precipitable fraction of normal plasma.	Heparin	98-105	fibrinogen beta chain	Homo sapiens	0-10
19499-1	1977	Fibrinogen and the cold-insoluble globulin of plasma (CIg) are the main protein components of the heparin-precipitable fraction of normal plasma.	Heparin	98-105	fibronectin 1	Homo sapiens	19-42
19499-1	1977	Fibrinogen and the cold-insoluble globulin of plasma (CIg) are the main protein components of the heparin-precipitable fraction of normal plasma.	Heparin	98-105	fibronectin 1	Homo sapiens	54-57
603758-6	1977	However, it was found that PRP containing heparin and A73025 with comparable anti-Factor Xa acitvity responded differently to the addition of thrombin, as A73025 barely inhibited thrombin induced aggregation.	Heparin	42-49	complement component 4 binding protein alpha	Homo sapiens	27-30
603758-6	1977	However, it was found that PRP containing heparin and A73025 with comparable anti-Factor Xa acitvity responded differently to the addition of thrombin, as A73025 barely inhibited thrombin induced aggregation.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	142-150
19499-3	1977	Heparin formed a cold-precipitable complex with purified CIg or with mixtures of CIg and fibrinogen but not with purified fibrinogen alone.	Heparin	0-7	fibronectin 1	Homo sapiens	57-60
71165-0	1977	Effect of heparin on the extent of inhibition of thrombin by heparin cofactor.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	49-57
19499-3	1977	Heparin formed a cold-precipitable complex with purified CIg or with mixtures of CIg and fibrinogen but not with purified fibrinogen alone.	Heparin	0-7	fibronectin 1	Homo sapiens	81-84
19499-3	1977	Heparin formed a cold-precipitable complex with purified CIg or with mixtures of CIg and fibrinogen but not with purified fibrinogen alone.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	89-99
19499-5	1977	Fibrinogen reduced the threshold for heparin-induced CIg cryoprecipitation and, by coprecipitating with heparin and CIg, increased the amount of precipitate that formed.	Heparin	37-44	fibrinogen beta chain	Homo sapiens	0-10
19499-5	1977	Fibrinogen reduced the threshold for heparin-induced CIg cryoprecipitation and, by coprecipitating with heparin and CIg, increased the amount of precipitate that formed.	Heparin	37-44	fibronectin 1	Homo sapiens	53-56
19499-5	1977	Fibrinogen reduced the threshold for heparin-induced CIg cryoprecipitation and, by coprecipitating with heparin and CIg, increased the amount of precipitate that formed.	Heparin	104-111	fibrinogen beta chain	Homo sapiens	0-10
19499-6	1977	In contrast to the heparin-precipitable fraction of normal plasma which contained both fibrinogen and CIg, that from a patient with congenital afibrinogenemia contained CIg but lacked fibrinogen.	Heparin	19-26	fibrinogen beta chain	Homo sapiens	87-97
19499-6	1977	In contrast to the heparin-precipitable fraction of normal plasma which contained both fibrinogen and CIg, that from a patient with congenital afibrinogenemia contained CIg but lacked fibrinogen.	Heparin	19-26	fibronectin 1	Homo sapiens	102-105
19499-8	1977	Thus, CIg is essential for heparin-induced cryoprecipitation to occur.	Heparin	27-34	fibronectin 1	Homo sapiens	6-9
19499-9	1977	Fibrinogen, as assessed by chromatographic experiments with heparin-Sepharose columns, had a considerably lower binding affinity for heparin than did CIg, suggesting that it participates in precipitate formation mainly, if not entirely, by virtue of its affinity for CIg.	Heparin	60-67	fibrinogen beta chain	Homo sapiens	0-10
19499-9	1977	Fibrinogen, as assessed by chromatographic experiments with heparin-Sepharose columns, had a considerably lower binding affinity for heparin than did CIg, suggesting that it participates in precipitate formation mainly, if not entirely, by virtue of its affinity for CIg.	Heparin	133-140	fibrinogen beta chain	Homo sapiens	0-10
19499-10	1977	The region of the fibrinogen molecule accounting for its precipitation with CIg appears to be localized in the carboxy-terminal segment of the Aalpha-chain; fibrinogen subfractions lacking this region failed to augment cryoprecipitation of heparin-CIg mixtures and, even though such species were present in normal plasma, they failed to coprecipitate in the heparin-induced complex.	Heparin	240-247	fibrinogen beta chain	Homo sapiens	18-28
19499-10	1977	The region of the fibrinogen molecule accounting for its precipitation with CIg appears to be localized in the carboxy-terminal segment of the Aalpha-chain; fibrinogen subfractions lacking this region failed to augment cryoprecipitation of heparin-CIg mixtures and, even though such species were present in normal plasma, they failed to coprecipitate in the heparin-induced complex.	Heparin	358-365	fibrinogen beta chain	Homo sapiens	18-28
19499-10	1977	The region of the fibrinogen molecule accounting for its precipitation with CIg appears to be localized in the carboxy-terminal segment of the Aalpha-chain; fibrinogen subfractions lacking this region failed to augment cryoprecipitation of heparin-CIg mixtures and, even though such species were present in normal plasma, they failed to coprecipitate in the heparin-induced complex.	Heparin	358-365	fibronectin 1	Homo sapiens	76-79
71165-1	1977	A heparin preparation obtained by gel chromatography is compared to unfractionated heparin with respect to the effects of heparin on the reaction between thrombin and heparin cofactor.	Heparin	2-9	coagulation factor II, thrombin	Homo sapiens	154-162
917513-0	1977	[Study of the heparin-neutralizing effect of plasma in disorders of hemostasis (clinical use of the "heparin-thrombin coagulation time")].	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	109-117
71165-2	1977	Whereas both preparations enhance the rate of inhibition of thrombin by heparin cofactor, the extent of inhibition is decreased by the unfractionated, but not by the fractionated heparin.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	60-68
71165-4	1977	However both heparin preparations enhance the rate of degradation by thrombin of the thrombin-heparin cofactor complex.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	69-77
71165-4	1977	However both heparin preparations enhance the rate of degradation by thrombin of the thrombin-heparin cofactor complex.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	85-93
579490-6	1977	This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	192-200
579490-7	1977	These results suggest that acceleration of binding and increased utilization of binding capacity are the two regular effects of heparin on thrombin-involving reactions of AT III.	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	139-147
579490-3	1977	Heparin present in reaction together with thrombin invariably induced a more extensive utilization of inhibitor than thrombin alone.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	117-125
579490-5	1977	Heparin itself was neutralized in thrombin-AT III reaction losing its anticoagulant property in proportion to the amount of thrombin bound by inhibitor.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	34-42
579490-8	1977	Both of these effects may be abolished by quantitative binding of heparin to thrombin-AT III complex.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	77-85
579490-5	1977	Heparin itself was neutralized in thrombin-AT III reaction losing its anticoagulant property in proportion to the amount of thrombin bound by inhibitor.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	124-132
579490-6	1977	This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	101-109
889853-1	1977	Monoacylglycerol lipase was separated from triacylglycerol lipase and two kinds of esterase in the microsomes by heparin treatment and DEAE-cellulose column chromatography.	Heparin	113-120	monoglyceride lipase	Rattus norvegicus	0-23
579490-6	1977	This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	192-200
560145-1	1977	Plasma heparin activity in 11 patients undergoing open-heart surgery was measured by comparing thrombin time of patient plasma to thrombin time of plasma containing known heparin concentrations.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	95-103
883969-0	1977	The heparin-thrombin complex in the mechanism of thrombin inactivation by heparin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	12-20
883969-0	1977	The heparin-thrombin complex in the mechanism of thrombin inactivation by heparin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	49-57
560145-1	1977	Plasma heparin activity in 11 patients undergoing open-heart surgery was measured by comparing thrombin time of patient plasma to thrombin time of plasma containing known heparin concentrations.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	130-138
330064-5	1977	The basis for this phenomenon is most probably the binding of the heparin-antithrombin cofactor (AT III) to a complex with heparin and thrombin.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	78-86
33120-9	1977	Lysis of cell walls in the presence of intact staphylococci used as a source of autolysin was strongly inhibited by a variety of anionic polyelectrolytes such as heparine and liquoid.	Heparin	162-170	AT695_RS05875	Staphylococcus aureus	80-89
924340-0	1977	[The interaction of Ca2+ and heparin in the activation of lipoprotein lipase from adipose tissue (author"s transl)].	Heparin	29-36	lipoprotein lipase	Rattus norvegicus	58-76
868792-2	1977	In the proposed procedure (I) a heparin thrombin time curve is constructed by adding gradually increasing amounts of heparin to a commercial plasma substrate and determining thrombin times, (2) a suitable concentration of heparin that gives highest reproducible thrombin time is selected and added to the substrate, (3) thrombin times are determined for the heparinized substrate before and after addition of a test material containing platelet factor 4.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	40-48
868792-2	1977	In the proposed procedure (I) a heparin thrombin time curve is constructed by adding gradually increasing amounts of heparin to a commercial plasma substrate and determining thrombin times, (2) a suitable concentration of heparin that gives highest reproducible thrombin time is selected and added to the substrate, (3) thrombin times are determined for the heparinized substrate before and after addition of a test material containing platelet factor 4.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	174-182
868792-2	1977	In the proposed procedure (I) a heparin thrombin time curve is constructed by adding gradually increasing amounts of heparin to a commercial plasma substrate and determining thrombin times, (2) a suitable concentration of heparin that gives highest reproducible thrombin time is selected and added to the substrate, (3) thrombin times are determined for the heparinized substrate before and after addition of a test material containing platelet factor 4.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	174-182
868792-2	1977	In the proposed procedure (I) a heparin thrombin time curve is constructed by adding gradually increasing amounts of heparin to a commercial plasma substrate and determining thrombin times, (2) a suitable concentration of heparin that gives highest reproducible thrombin time is selected and added to the substrate, (3) thrombin times are determined for the heparinized substrate before and after addition of a test material containing platelet factor 4.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	174-182
868792-2	1977	In the proposed procedure (I) a heparin thrombin time curve is constructed by adding gradually increasing amounts of heparin to a commercial plasma substrate and determining thrombin times, (2) a suitable concentration of heparin that gives highest reproducible thrombin time is selected and added to the substrate, (3) thrombin times are determined for the heparinized substrate before and after addition of a test material containing platelet factor 4.	Heparin	117-124	coagulation factor II, thrombin	Homo sapiens	40-48
868792-3	1977	The two thrombin times are converted to heparin concentration by reference to the heparin thrombin time curve.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	8-16
868792-3	1977	The two thrombin times are converted to heparin concentration by reference to the heparin thrombin time curve.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	90-98
560216-0	1977	Effect of heparin modification on its activity in enhancing the inhibition of thrombin by antithrombin III.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	78-86
875875-2	1977	A dosage of heparin was chosen, which allowed an increase in thrombin time to 20-40 seconds.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	61-69
855665-4	1977	Tests on isolated C1q, C1r and C1s disclosed in addition to the well known interaction between heparin and C1q an equally strong or even stronger interaction between heparin and C1s.	Heparin	166-173	complement C1s	Homo sapiens	178-181
326134-2	1977	This is probably due to an interaction of heparin and serum proteins, together with either fibrinogen or polyethylene glycol.	Heparin	42-49	fibrinogen beta chain	Homo sapiens	91-101
142314-0	1977	The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	20-28
855665-5	1977	Even C1r was adsorbed to heparin although by somewhat weaker ionic bonds.	Heparin	25-32	complement C1r	Homo sapiens	5-8
857810-2	1977	The enzyme activity measured in extrahepatic tissues fulfilled the criteria of lipoprotein lipase from the onset of measurable activity, i.e. it was inhibited by protamine and 1 M NaCl and showed requirement for serum and heparin for optimal activity.	Heparin	222-229	lipoprotein lipase	Rattus norvegicus	79-97
861306-1	1977	It is found by means of different methods (the administration of 35S-heparin, the determination of fibrinolytic activity of blood plasma fractions containing fibrinogen degradation products and fibrinogen--heparin complex, spectral analysis of fibrinogen--heparin complex etc.	Heparin	206-213	fibrinogen beta chain	Homo sapiens	194-204
839844-5	1977	Suppression of insulin secretion during perfusion may be the result of increased catecholamine secretion, induced hypothermia, or heparin administration.	Heparin	130-137	insulin	Homo sapiens	15-22
840146-5	1977	In patients with an increased "tolerance" for heparin, however, the determination of the thrombin time with a thrombin-solution of low concentration (1 N.I.H.-unit/ml) might be useful to indicate whether the dosage of heparin has to be increased or not.	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	89-97
840146-5	1977	In patients with an increased "tolerance" for heparin, however, the determination of the thrombin time with a thrombin-solution of low concentration (1 N.I.H.-unit/ml) might be useful to indicate whether the dosage of heparin has to be increased or not.	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	110-118
407761-0	1977	[The studies on the influence of heparin on the reaction of antithrombin with thrombin, and the optimal dosis of heparin in the reaction (author"s transl)].	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	64-72
861306-0	1977	[Presence of an active fibrinogen--heparin complex in the total blood plasma fraction of plasma fibrinogen degradation products].	Heparin	35-42	fibrinogen beta chain	Homo sapiens	23-33
861306-0	1977	[Presence of an active fibrinogen--heparin complex in the total blood plasma fraction of plasma fibrinogen degradation products].	Heparin	35-42	fibrinogen beta chain	Homo sapiens	96-106
861306-1	1977	It is found by means of different methods (the administration of 35S-heparin, the determination of fibrinolytic activity of blood plasma fractions containing fibrinogen degradation products and fibrinogen--heparin complex, spectral analysis of fibrinogen--heparin complex etc.	Heparin	206-213	fibrinogen beta chain	Homo sapiens	194-204
830556-0	1977	Interaction of heparin with thrombin and antithrombin III.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	28-36
754468-4	1977	Thrombin inactivation by antithrombin was also accelerated at calcium or magnesium chloride concentrations above 0.04 M. Antithrombin was inactivated at pH 7.3 at 65 degrees C in some minutes and heparin failed to protect it against heat denaturation.	Heparin	196-203	coagulation factor II, thrombin	Homo sapiens	0-8
754468-5	1977	Thrombin inactivation by antithrombin did not proceed at 0 degrees C in 60 min, but the interaction between thrombin and antithrombin was facilitated in the presence of heparin.	Heparin	169-176	coagulation factor II, thrombin	Homo sapiens	0-8
754468-5	1977	Thrombin inactivation by antithrombin did not proceed at 0 degrees C in 60 min, but the interaction between thrombin and antithrombin was facilitated in the presence of heparin.	Heparin	169-176	coagulation factor II, thrombin	Homo sapiens	29-37
148961-2	1977	In order to elucidate the mechanism of fibrinogen kinetic abnormalities different drugs, including heparin, prednisone, ticlopidin, aspirin and indomethacin were administered in 68 patients and their effects evaluated by change in the 311I fibrinogen disappearance rate.	Heparin	99-106	fibrinogen beta chain	Homo sapiens	39-49
75141-0	1977	[The role of heparin in thrombin inhibition by antithrombin].	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	24-32
885379-0	1977	The effect of heparin on the interaction of factor VIII and human platelets in vitro.	Heparin	14-21	coagulation factor VIII	Bos taurus	44-55
885379-1	1977	Heparin was found to inhibit the interaction between human factor VIII and platelets.	Heparin	0-7	coagulation factor VIII	Bos taurus	59-70
870737-0	1977	[Importance of heparin in thrombin-131I clearance and in the complex formation processes in animals under experimental restoration of the function of the anticoagulating system].	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	26-34
71827-3	1977	Cold insoluble globulin (CIG) is the main non-clottable protein of heparin precipitable fraction from dermatological patients.	Heparin	67-74	fibronectin 1	Homo sapiens	0-23
71827-3	1977	Cold insoluble globulin (CIG) is the main non-clottable protein of heparin precipitable fraction from dermatological patients.	Heparin	67-74	fibronectin 1	Homo sapiens	25-28
611046-2	1977	As expected, the sensitivity to heparin depended on the concentrations of AT-III and thrombin, whereas the fibrinogen level was less decisive.	Heparin	32-39	serpin family C member 1	Bos taurus	74-80
611046-6	1977	Finally, during storage of purified AT-III at +4 degrees C for more than 4 weeks, the sensitivity to heparin decreased more rapidly than expected from the amidolytic AT-III assays.	Heparin	101-108	serpin family C member 1	Bos taurus	36-42
615088-4	1977	The shortened fibrinogen half-life together with the correcting effect of anticoagulation with heparin indicated that fibrinogen was consumed by chronic disseminated intravascular coagulation.	Heparin	95-102	fibrinogen beta chain	Homo sapiens	118-128
830761-5	1977	CRP also enhanced C consumption during heparin-protamine interactions in whole serum, and in the presence of CRP depletion of C components C1-3 was observed.	Heparin	39-46	C-reactive protein	Homo sapiens	0-3
65798-1	1976	Inactivation of alpha- and beta-thrombin by antithrombin-III and heparin was studied, since it had been suggested that two forms of thrombin exist with respect to heparin sensitivity (Machovich 1975b).	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	32-40
65798-3	1976	Heparin facilitated the complex formation between alpha-thrombin and antithrombin-III, whereas beta-thrombin inactivation was only slightly affected.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	56-64
65798-3	1976	Heparin facilitated the complex formation between alpha-thrombin and antithrombin-III, whereas beta-thrombin inactivation was only slightly affected.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	73-81
65798-4	1976	Furthermore, heparin protected alpha-thrombin against the inactivating effect of heat, while beta-thrombin lost its activity during the heat treatment.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	37-45
1009699-0	1976	Whole-blood thrombin time: a bedside method for determination of heparin activity.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	12-20
187590-7	1976	The enzyme release by thrombin was completely inhibited by heparin but the release by A-23187 was not.	Heparin	59-66	coagulation factor II	Rattus norvegicus	22-30
1009699-4	1976	An increase of the thrombin time of 50-100 per cent above the starting value (3.7-6.6 sec) was aimed at during the heparin infusion.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	19-27
976635-3	1976	The glucagon and growth hormone responses to nicotinic acid were significantly reduced when plasma FFA were raised by intravenous administration of heparin and triglycerides.	Heparin	148-155	growth hormone 1	Homo sapiens	17-31
827443-2	1976	Human coagulation factor IX was purified by two ion-exchange chromatographies on DEAE-Sephadex A-50, heparin-Sepharose chromatography, hydroxyapatite chromatography and immunoadsorbent technique.	Heparin	101-108	coagulation factor IX	Homo sapiens	6-27
12748-7	1976	However, in the particular case of lysozyme and phospholipase A2 the heparin-induced inhibition was maintained in the pH range 4.0-7.0.	Heparin	69-76	lysozyme	Homo sapiens	35-43
12748-7	1976	However, in the particular case of lysozyme and phospholipase A2 the heparin-induced inhibition was maintained in the pH range 4.0-7.0.	Heparin	69-76	phospholipase A2 group IB	Homo sapiens	48-64
12748-9	1976	For certain enzymes, such as acid beta-glycerophosphatase, alpha-galactosidase, acid lipase, lysozyme and phospholipase A2, the pH-dependent behaviour obtained in the presence of heparin was quite different to that obtained with chondroitin sulphate, suggesting the existence of physicochemical characteristic factors playing a role in the intermolecular interaction for each of the sulphated glycosaminoglycans studied.	Heparin	179-186	lysozyme	Homo sapiens	93-101
12748-9	1976	For certain enzymes, such as acid beta-glycerophosphatase, alpha-galactosidase, acid lipase, lysozyme and phospholipase A2, the pH-dependent behaviour obtained in the presence of heparin was quite different to that obtained with chondroitin sulphate, suggesting the existence of physicochemical characteristic factors playing a role in the intermolecular interaction for each of the sulphated glycosaminoglycans studied.	Heparin	179-186	phospholipase A2 group IB	Homo sapiens	106-122
993343-7	1976	This material is thrombin, not intermediates of prothrombin activation, since it disappears after addition of heparin, which promotes thrombin antithrombin III complex formation.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	17-25
791610-0	1976	[Influence of heparin on the radioimmunologic assay of insulin].	Heparin	14-21	insulin	Homo sapiens	55-62
976270-0	1976	Acceleration of the reaction between thrombin and antithrombin III by non-stoichiometric amounts of heparin.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	37-45
1006146-3	1976	A marked shortening of the thrombin-clotting time was observed, indicating fall in heparin anticoagulant effect.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	27-35
976270-1	1976	The accelerating effect of heparin on the reaction between purified human antithrombin and thrombin has been investigated by measuring the amount of thrombin inactivated during a short incubation of the enzyme with the inhibitor in the presence and absence of non-stoichiometric amounts of heparin.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	78-86
976270-1	1976	The accelerating effect of heparin on the reaction between purified human antithrombin and thrombin has been investigated by measuring the amount of thrombin inactivated during a short incubation of the enzyme with the inhibitor in the presence and absence of non-stoichiometric amounts of heparin.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	91-99
976270-1	1976	The accelerating effect of heparin on the reaction between purified human antithrombin and thrombin has been investigated by measuring the amount of thrombin inactivated during a short incubation of the enzyme with the inhibitor in the presence and absence of non-stoichiometric amounts of heparin.	Heparin	290-297	coagulation factor II, thrombin	Homo sapiens	91-99
976270-2	1976	It was demonstrated that one molecule of heparin was able to promote the binding of a large number of antithrombin molecules to thrombin.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	106-114
976270-3	1976	Thus heparin may affect the rate of the inactivation of thrombin by antithrombin in a catalytic manner.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	56-64
949335-6	1976	Maximum inhibition occurred 30 min after the injection and corresponded to about 60% of the lipoprotein lipase activity that could be released from the heart during 30 s perfusion with heparin.	Heparin	185-192	lipoprotein lipase	Rattus norvegicus	92-110
962952-0	1976	Heparin reacts stoichiometrically with thrombin during thrombin inhibition in human plasma.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	39-47
962952-0	1976	Heparin reacts stoichiometrically with thrombin during thrombin inhibition in human plasma.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	55-63
1260029-1	1976	Lipoprotein lipase (EC 3.1.1.3) from rat adipose tissue was purified by affinity chromatography with heparin-Sepharose.	Heparin	101-108	lipoprotein lipase	Rattus norvegicus	0-18
818862-12	1976	It is concluded from these experiments that in Gal-N "hepatitis" of rats plasmatic DAO level changes are mediated by endogenous heparin, released from disrupted mast cells.	Heparin	128-135	D-amino-acid oxidase	Rattus norvegicus	83-86
1278533-4	1976	(The inhibitory effect of plasma after N-acetyl-thrombin administration tells also on the nonfermentative fibrinolytic activity of the Fibrinogen-Heparin complex, activity of the latter dropping practically to the zero level.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	48-56
935809-3	1976	Heparin inhibited the reptilase clot retraction induced either by thrombin or calcium, but did not influence the clot retraction induced by ADP.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	66-74
60792-0	1976	Evidence for an ester bond between thrombin and heparin cofactor.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	35-43
60792-1	1976	Heparin cofactor, a thrombin inhibitor, is purified from human plasma by affinity chromatography on heparin-agarose.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	20-28
1257034-7	1976	Heparine (15000 U/24h) restores the 1/2 T of fibrinogen to normal in 95 p. cent of cases.	Heparin	0-8	fibrinogen beta chain	Homo sapiens	45-55
943139-2	1976	A correlation between TT and the heparin concentration was obtained only when the thrombin was of human origin and when it was reconstituted in divalent cation solutions.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	82-90
1061997-3	1976	Heparin infusion was twice accompanied by normalization of the fibrinogen level, but had to be stopped because of severe bleeding.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	63-73
943139-5	1976	Divalent cation solution, in which thrombin was reconstituted, had a profound influence on TT of heparin plasma.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	35-43
943139-8	1976	The reliability of the thrombin time test as a means of monitoring heparin anticoagulation must be established by individual laboratories via extensive testing of clinical samples.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	23-31
1195668-5	1975	A specific role of the virus in this toxic syndrome can be demonstrated when heparin is employed to circumvent intravascular coagulation and fibrinogen loss.	Heparin	77-84	fibrinogen beta chain	Homo sapiens	141-151
1215973-4	1975	125I-fibrinogen half-life was 2.1 days under aspirin and 1.9 days under combined aspirin/heparin therapy.	Heparin	89-96	fibrinogen beta chain	Homo sapiens	5-15
1191673-0	1975	Mechanism of action of heparin through thrombin on blood coagulation.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	39-47
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	72-80
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	113-121
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	113-121
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	72-80
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	113-121
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	113-121
56053-0	1976	Synthesis of heparin-sepharoses and their binding with thrombin and antithrombin-heparin cofactor.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	55-63
1251351-0	1976	[Role of complex thrombin-heparin formation in the clearance of thrombin in the blood stream and the role of liver and lungs in the absorption of heparin-complexes (author"s transl)].	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	17-25
1251351-0	1976	[Role of complex thrombin-heparin formation in the clearance of thrombin in the blood stream and the role of liver and lungs in the absorption of heparin-complexes (author"s transl)].	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	64-72
1209544-0	1975	Adverse effect of heparin in thrombin-antithrombin III interaction.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	29-37
1209544-4	1975	With a lower enzyme/inhibitor ratio inactivation of thrombin in the presence of hepatin was fast and complete, however, a significant decrease of inhibitory capacity below that found in reaction without heparin, has been established by measuring the residual antithrombin III activity.	Heparin	203-210	coagulation factor II, thrombin	Homo sapiens	52-60
1209544-8	1975	These results may have some bearings on the approach to heparin therapy in the event when thrombin continuously generates or when a marked deficiency of antithrombin III exists.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	90-98
1184738-8	1975	The changes in heparin-releasable (r=0.66, P less than 0.01) and acetone-ether powder (r=0.69, P less than 0.01) activity during feeding were related to the percent increase in plasma insulin.	Heparin	15-22	insulin	Homo sapiens	184-191
1184755-3	1975	In the five insulin-dependent subjects studied, when plasma glucagon concentration remained at the normal basal level of 72+/-14 pg/ml during control saline infusion, the heparin-induced increase in free fatty acid availability resulted in approximately a 20% increase in plasma ketone body concentration.	Heparin	171-178	insulin	Homo sapiens	12-19
1180962-0	1975	Evidence for the formation of an ester between thrombin and heparin cofactor.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	47-55
1180962-1	1975	Heparin cofactor, a thrombin inhibitor, is purified from human plasma by affinity chromatography on heparin-agarose.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	20-28
1188708-4	1975	In normal rat, heparin (2.5 mg/kg), acetylsalicylic acid (30 mg/kg) and tranexamic acid (100 mg/kg) suppressed specifically coagulation, platelet aggregation induced by collagen or thrombin and fibrinolysis respectively.	Heparin	15-22	coagulation factor II	Rattus norvegicus	181-189
1183792-5	1975	The number of cases of deep thrombophlebitis diagnosed by the I-125-Fibrinogen test was significantly less in the group receiving Heparin than in the group receiving Sintrom.	Heparin	130-137	fibrinogen beta chain	Homo sapiens	68-78
1188832-0	1975	Proceedings: Adverse effect of heparin on thrombin inactivation.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	42-50
180515-0	1975	[The role of adrenaline and ACTH in the process of complex heparin compound formation in the blood during imobilization stress].	Heparin	59-66	proopiomelanocortin	Homo sapiens	28-32
1222284-0	1975	[Activation of parathyroid hormone by heparin in vitro].	Heparin	38-45	parathyroid hormone	Homo sapiens	15-34
1222284-2	1975	In vitro heparin activated the effects of parathyroid hormone in respect to bone resorption, but heparin alone was incapable of causing the resorption.	Heparin	9-16	parathyroid hormone	Homo sapiens	42-61
1239278-2	1975	Lipoprotein lipase was purified from pig myocardium by a two-step purification procedure involving (a) the formation of an enzyme-substrate complex and (b) affinity chromatography on Sepharose which contained covalently linked heparin.	Heparin	227-234	lipoprotein lipase	Sus scrofa	0-18
1174522-1	1975	In response to food deprivation, total myocardial lipoprotein lipase activity increased gradually over a period of 9 h. Although lipoprotein lipase exists in a functional and non-functional form in the myocardium, most of the increas in activity occurred in the functional (heparin-releasable) lipoprotein lipase fraction.	Heparin	274-281	lipoprotein lipase	Rattus norvegicus	50-68
1174522-4	1975	These results suggest that the functional lipoprotein lipase is constantly being formed in sites not readily accessible to heparin (presumably the myocardial cells) and transported to its site of action, the surface of the endothelial cells of the capillaries.	Heparin	123-130	lipoprotein lipase	Rattus norvegicus	42-60
1213204-1	1975	On depression of the anticoagulating system"s function due to a prolonged keeping of animals on aterogenic diet, a decrease in the speed of clearance of thrombin-J131 was observed in the blood flow, the absorption of non-fermentative dissolvents of unstabilized fibrin (the heparin complex compounds) is sharply reduced in the liver and lungs tissues, and the fatty dystrophy of the liver cells followed by appearance of vacuoles in cytoplasm and decrease of the RNA and total protein contents in the cells, was observed.	Heparin	274-281	coagulation factor II, thrombin	Homo sapiens	153-161
1082678-2	1975	The heparin complexes were observed in circulation when the anticoagulation system was stimulated due to appearance of thrombin in the blood stream.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	119-127
180515-4	1975	Administration of both adrenaline and ACTH considerably intensified in stress the process of formation of heparin complexes; no summation of the action of the exogenous ACTH and adrenaline occurred.	Heparin	106-113	proopiomelanocortin	Homo sapiens	38-42
1170899-1	1975	Two forms of thrombin (Ts-thrombin and Tp-thrombin) were found with respect to heparin sensitivity.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	13-21
169603-0	1975	[The role of ACTH in the formation of heparin complexes in blood under immobilization stress conditions].	Heparin	38-45	proopiomelanocortin	Homo sapiens	13-17
1170899-1	1975	Two forms of thrombin (Ts-thrombin and Tp-thrombin) were found with respect to heparin sensitivity.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	26-34
1170899-1	1975	Two forms of thrombin (Ts-thrombin and Tp-thrombin) were found with respect to heparin sensitivity.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	26-34
1170899-2	1975	Inactivation of Ts-thrombin by antithrombin-III was facilitated with heparin, whereas inactivation of Tp-thrombin was not.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	19-27
1170899-2	1975	Inactivation of Ts-thrombin by antithrombin-III was facilitated with heparin, whereas inactivation of Tp-thrombin was not.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	35-43
1162646-0	1975	The interaction of thrombin and heparin.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	19-27
1170899-4	1975	Ts-thrombin proved to be more stable and was better protected by heparin against heat inactivation of 54 degrees C than Tp-thrombin.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	3-11
1217689-5	1975	From the results we obtained in our tests, the bleeding which occurs after the neutralization of heparin with protamine-chloride can be explained by increased DIC.	Heparin	97-104	solute carrier family 25 member 10	Homo sapiens	159-162
1149268-1	1975	Methods for plasma fibrinogen based on thrombin time are technically simple, rapid, and sensitive, although "false low" results may occur due to heparin interference.	Heparin	145-152	fibrinogen beta chain	Homo sapiens	19-29
1217689-7	1975	When there is DIC at the end of the by-pass time, one should avoid neutralizing the heparin and continue the heparin treatment for the same reason.	Heparin	84-91	solute carrier family 25 member 10	Homo sapiens	14-17
1217689-7	1975	When there is DIC at the end of the by-pass time, one should avoid neutralizing the heparin and continue the heparin treatment for the same reason.	Heparin	109-116	solute carrier family 25 member 10	Homo sapiens	14-17
1147442-5	1975	In every instance fibrinogen survival was improved by heparin administration.	Heparin	54-61	fibrinogen beta chain	Homo sapiens	18-28
1147442-6	1975	These data indicate that "low dose" heparin improves fibrinogen survival in cirrhosis and suggest that disseminated intravascular coagulation is a primary process in the defibrination syndrome associated with cirrhosis.	Heparin	36-43	fibrinogen beta chain	Homo sapiens	53-63
1147442-0	1975	Fibrinogen survival in cirrhosis: improvement by "low dose" heparin.	Heparin	60-67	fibrinogen beta chain	Homo sapiens	0-10
1147442-1	1975	The effect of "low dose" heparin therapy on fibrinogen survival in patients with cirrhosis was studied in six patients.	Heparin	25-32	fibrinogen beta chain	Homo sapiens	44-54
1147442-3	1975	Average fibrinogen half-life before heparin therapy was 52 hours and after 3000 units of intravenous heparin every 6 hours was 101.8 hours.	Heparin	36-43	fibrinogen beta chain	Homo sapiens	8-18
50744-5	1975	Heparin or hirudin inhibited ADP-INDUCED SECONDARY AGGREGATION AND RELEASE PROMOTED BY TRACES OF THROMBIN.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	97-105
1215178-1	1975	In emergency traumatology, the iodine 125 labelled fibrinogen test is useful in the early detection of phlebitis in patients in whom the routine use of heparin is not possible--fractures of the cervical spine, severe cranial trauma, elderly subjects.	Heparin	152-159	fibrinogen beta chain	Homo sapiens	51-61
1078885-4	1975	Heparin was delivered by constant infusion and dosage regulated by maintaining the thrombin time at 2 to/ times normal.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	83-91
47195-0	1975	Effect of heparin on the neutralization of factor Xa and thrombin by the plasma alpha-2-globulin inhibitor.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	57-65
1138898-0	1975	Interference with the transport of heparin-releasable lipoprotein lipase in the perfused rat heart by colchicine and vinblastine.	Heparin	35-42	lipoprotein lipase	Rattus norvegicus	54-72
1138898-2	1975	Administration of colchicine or vinblastine 4 h prior to perfusion of the heart caused a very marked reduction in lipoprotein lipase activity released into the perfusate within 1 min of heparin perfusion.	Heparin	186-193	lipoprotein lipase	Rattus norvegicus	114-132
1122308-1	1975	The release of plasma lipoprotein lipase by heparin was studied in fed and food-deprived rats pretreated with colchicine and vinblastine.	Heparin	44-51	lipoprotein lipase	Rattus norvegicus	22-40
235320-4	1975	Lungs from fed rats hydrolyzed chylomicron triglyceride at a rate of 13.00 mumoles/g per h; the activity rate was unchanged by fasting 8-72 h. Heparin infusion into isolated lungs caused immediate release of lipoprotein lipase to the venous effluent.	Heparin	143-150	lipoprotein lipase	Rattus norvegicus	208-226
1115795-0	1975	Action of heparin on thrombin-antithrombin reaction.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	21-29
1115795-2	1975	When thrombin and heparin are mixed and incubated for 5 min at 0 degrees C before gel filtration on Sephadex G-200, thrombin with heparin is eluted prior to either thrombin or heparin laone.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	116-124
1115795-2	1975	When thrombin and heparin are mixed and incubated for 5 min at 0 degrees C before gel filtration on Sephadex G-200, thrombin with heparin is eluted prior to either thrombin or heparin laone.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	116-124
1115795-2	1975	When thrombin and heparin are mixed and incubated for 5 min at 0 degrees C before gel filtration on Sephadex G-200, thrombin with heparin is eluted prior to either thrombin or heparin laone.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	5-13
1115795-2	1975	When thrombin and heparin are mixed and incubated for 5 min at 0 degrees C before gel filtration on Sephadex G-200, thrombin with heparin is eluted prior to either thrombin or heparin laone.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	116-124
1122308-2	1975	Four hours after the administration of either drug the lipoprotein lipase activity released by heparin was only half of that found in controls.	Heparin	95-102	lipoprotein lipase	Rattus norvegicus	55-73
1115795-2	1975	When thrombin and heparin are mixed and incubated for 5 min at 0 degrees C before gel filtration on Sephadex G-200, thrombin with heparin is eluted prior to either thrombin or heparin laone.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	116-124
1115795-4	1975	Immobilized heparin binds thrombin.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	26-34
1225326-6	1975	Heparin treatment was successful: haemorrhages stopped already 24 hours later, while an increase of fibrinogen concentration and number of platelets in blood proceeded at slower rate.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	100-110
1202527-6	1975	Laboratory determination of the different constituents of the prothrombin complex makes it possible to regulate perfectly the treatment with antivitamins K of a patient who is also receiving heparin.	Heparin	191-198	coagulation factor II, thrombin	Homo sapiens	62-73
4373048-0	1974	The interaction of thrombin and heparin.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	19-27
1119113-1	1975	An effect of increase in fibrinolytic activity of adrenaline-heparin (ADH) complex was studied under its incubation in a mixture with pure fibrinogen on unstablized plates of fibrin in presence of xi-aminocapronic acid, By means of spectrophotometry in UV-light an increase in lytic activity of the incubated mixture of adrenaline-heparin complex with fibrinogen was shown to be due to formation of a secondary complex, which included adrenaline, heparin and fibrinogen.	Heparin	61-68	fibrinogen beta chain	Homo sapiens	139-149
1119113-1	1975	An effect of increase in fibrinolytic activity of adrenaline-heparin (ADH) complex was studied under its incubation in a mixture with pure fibrinogen on unstablized plates of fibrin in presence of xi-aminocapronic acid, By means of spectrophotometry in UV-light an increase in lytic activity of the incubated mixture of adrenaline-heparin complex with fibrinogen was shown to be due to formation of a secondary complex, which included adrenaline, heparin and fibrinogen.	Heparin	61-68	fibrinogen beta chain	Homo sapiens	352-362
1119113-1	1975	An effect of increase in fibrinolytic activity of adrenaline-heparin (ADH) complex was studied under its incubation in a mixture with pure fibrinogen on unstablized plates of fibrin in presence of xi-aminocapronic acid, By means of spectrophotometry in UV-light an increase in lytic activity of the incubated mixture of adrenaline-heparin complex with fibrinogen was shown to be due to formation of a secondary complex, which included adrenaline, heparin and fibrinogen.	Heparin	61-68	fibrinogen beta chain	Homo sapiens	352-362
4452381-0	1974	[Significance of the formation of a thrombin-heparin complex in the initial stages of thrombin clearance in the blood flow and the role of the liver and lungs in this process].	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	36-44
4452381-0	1974	[Significance of the formation of a thrombin-heparin complex in the initial stages of thrombin clearance in the blood flow and the role of the liver and lungs in this process].	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	86-94
4218658-0	1974	Simultaneous insulin immunoassay in sera, heparin-, and EDTA-plasma.	Heparin	42-49	insulin	Homo sapiens	13-20
4543085-0	1973	In vitro comparison of the thrombin time and activated partial thromboplastin time in the laboratory control of heparin therapy.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	27-35
4525167-3	1973	Factor VIII was prepared from normal canine plasma collected in sodium oxalate and heparin and adsorbed with BaSO(4).	Heparin	83-90	coagulation factor VIII	Canis lupus familiaris	0-11
4592783-0	1973	Influence of heparin on insulin secretion in vitro.	Heparin	13-20	insulin	Homo sapiens	24-31
4377385-0	1973	The interaction of angiotensin II with heparin.	Heparin	39-46	angiotensinogen	Homo sapiens	19-33
4206120-0	1973	Effect of heparin on the concentration of insulin in serum and plasma.	Heparin	10-17	insulin	Homo sapiens	42-49
4780710-0	1973	[Formation of a fibrinogen-heparin complex in the presence of interaction of an adrenaline-heparin complex with fibrinogen in vitro and in vivo].	Heparin	27-34	fibrinogen beta chain	Homo sapiens	16-26
4683798-0	1973	Effects of amino acids, epinephrine and heparin upon the radioimmunoassay of insulin in plasma.	Heparin	40-47	insulin	Homo sapiens	77-84
4780710-0	1973	[Formation of a fibrinogen-heparin complex in the presence of interaction of an adrenaline-heparin complex with fibrinogen in vitro and in vivo].	Heparin	27-34	fibrinogen beta chain	Homo sapiens	112-122
4780710-0	1973	[Formation of a fibrinogen-heparin complex in the presence of interaction of an adrenaline-heparin complex with fibrinogen in vitro and in vivo].	Heparin	91-98	fibrinogen beta chain	Homo sapiens	16-26
4508335-0	1972	Enzymic depolymerization of macromolecular heparin as a factor in control of lipoprotein lipase activity.	Heparin	43-50	lipoprotein lipase	Rattus norvegicus	77-95
4508335-1	1972	Macromolecular heparin from rat skin shows poor lipoprotein lipase-releasing activity in vivo and is a potent inhibitor of rat-heart lipoprotein lipase in vitro.	Heparin	15-22	lipoprotein lipase	Rattus norvegicus	48-66
4780710-0	1973	[Formation of a fibrinogen-heparin complex in the presence of interaction of an adrenaline-heparin complex with fibrinogen in vitro and in vivo].	Heparin	91-98	fibrinogen beta chain	Homo sapiens	112-122
4508335-1	1972	Macromolecular heparin from rat skin shows poor lipoprotein lipase-releasing activity in vivo and is a potent inhibitor of rat-heart lipoprotein lipase in vitro.	Heparin	15-22	lipoprotein lipase	Rattus norvegicus	133-151
4114736-0	1972	Detection of small amounts of heparin by the thrombin clotting-time.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	45-53
5118165-0	1971	Fibrinogen assay during heparin therapy of disseminated intravascular coagulation.	Heparin	24-31	fibrinogen beta chain	Homo sapiens	0-10
5040753-0	1972	Effect of heparin on radio fibrinogen catabolism in renal disease.	Heparin	10-17	fibrinogen beta chain	Homo sapiens	27-37
4335798-2	1972	It was found that after intraperitoneal injection of heparin, deficient rats had a higher level of lipoprotein lipase activity in their plasma than did normal rats.	Heparin	53-60	lipoprotein lipase	Rattus norvegicus	99-117
5020338-0	1972	[Direct inhibitory effect of heparin on the secretion of insulin].	Heparin	29-36	insulin	Homo sapiens	57-64
4121334-0	1972	Thrombin inhibiting action of heparin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	0-8
5093999-0	1971	Inhibition of thrombin induced aggregation of human platelets by heparin.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	14-22
5094686-5	1971	The results suggest that control of heparin therapy can be based on the thrombin clotting time.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	72-80
5090059-3	1971	Lipomul plus heparin administration inhibited both insulin- and arginine-induced plasma HGH elevations with almost complete suppression of the response to arginine.	Heparin	13-20	insulin	Homo sapiens	51-58
5090059-8	1971	These latter observations suggest that the elevation in plasma FFA was responsible for suppression of growth hormone secretion by Lipomul plus heparin.	Heparin	143-150	growth hormone 1	Homo sapiens	102-116
5549989-2	1971	The patients in the streptokinase group also received a loading dose of heparin and were treated with heparin by continuous infusion when their thrombin time returned to normal levels.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	144-152
4907928-0	1970	Effect of heparin administration on plasma growth hormone concentrations.	Heparin	10-17	growth hormone 1	Homo sapiens	43-57
5524716-0	1970	[Control of heparin and oral anticoagulants, with micromethods: thrombin time, quick determination with addition of protamine].	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	64-72
5418473-0	1970	The effect of fasting on the utilization of chylomicron triglyceride fatty acids in relation to clearing factor lipase (lipoprotein lipase) releasable by heparin in the perfused rat heart.	Heparin	154-161	lipoprotein lipase	Rattus norvegicus	120-138
5816627-2	1969	Plasma heparin resistance in relation to plasma fibrinogen and serum proteins].	Heparin	7-14	fibrinogen beta chain	Homo sapiens	48-58
5784902-0	1969	Purification of lipoprotein lipase from rat post-heparin plasma.	Heparin	49-56	lipoprotein lipase	Rattus norvegicus	16-34
5411984-0	1970	Influence of heparin on the removal of serum lipoprotein lipase by the perfused liver of the rat.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	45-63
5411984-4	1970	The addition of heparin to the perfusate in suitable concentration (4 units/ml) almost completely blocked the disappearance of LPL activity from the perfusate.	Heparin	16-23	lipoprotein lipase	Rattus norvegicus	127-130
5411984-5	1970	In addition to the perfusion experiments, we studied the effect of heparin on LPL activity when added to the LPL assay system.	Heparin	67-74	lipoprotein lipase	Rattus norvegicus	78-81
5411984-6	1970	When heparin was added to the assay system containing fresh postheparin serum from rats, it stimulated LPL activity by about 70%.	Heparin	5-12	lipoprotein lipase	Rattus norvegicus	103-106
5411984-7	1970	When heparin was added to postheparin serum which had been perfused through the liver, it stimulated LPL activity over 200%, but it did not restore LPL to its preperfusion value.	Heparin	5-12	lipoprotein lipase	Rattus norvegicus	101-104
5309527-0	1969	[Determination of rheumatic and infectious arthritis activity by studying the heparin sedimented fraction of the blood psma].	Heparin	78-85	folate hydrolase 1	Homo sapiens	119-123
5717813-0	1968	[The protraction of the thrombin time under the effect of elastase (does elastase cause heparin liberation?	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	24-32
4241141-0	1969	Effect of a single neonatal dose of ACTH, TSH, STH, thyroxine and aldosterone on serum heparin and tissue mucopolysaccharides.	Heparin	87-94	proopiomelanocortin	Homo sapiens	36-40
5667258-8	1968	Lipoprotein lipase was also detected in liver alone when large quantities of heparin were added to the assay system.	Heparin	77-84	lipoprotein lipase	Rattus norvegicus	0-18
6021455-2	1967	Changes in fibrinogen concentration during and after cardiopulmonary bypass with particular reference to the effect of heparin neutralization on fibrinogen.	Heparin	119-126	fibrinogen beta chain	Homo sapiens	145-155
5646184-4	1968	From measurements of the lipolytic activity in the presence of 1 M NaCl or 0.2 M NaF and in the absence and presence of heparin and serum, the conclusion is drawn that more lipoprotein lipase was present in adipose tissue of rats on unsaturated fat diets.	Heparin	120-127	lipoprotein lipase	Rattus norvegicus	173-191
5589354-0	1967	[On the effects of prostaglandin El and insulin on the heparin-induced triglyceride hydrolysis].	Heparin	55-62	insulin	Homo sapiens	40-47
6035543-0	1967	Heparin cofactor and plasma antithrombin in relation to the mechanism of inactivation of thrombin by heparin.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	32-40
5731931-0	1968	Inhibition of the thrombin-fibrinogen reaction by heparin in the absence of cofactor.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	18-26
5731932-0	1968	Inhibition of the thrombin-fibrinogen reaction by heparin and purified cofactor.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	18-26
4290582-0	1967	Inhibition of renin by heparin.	Heparin	23-30	renin	Homo sapiens	14-19
16955974-4	1965	The inhibition of thrombin with heparin allows a more complete activation of the thrombin.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	18-26
6008827-2	1966	Inactivation of thrombin by whale heparin].	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	16-24
16955974-4	1965	The inhibition of thrombin with heparin allows a more complete activation of the thrombin.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	81-89
14081260-0	1963	STUDIES ON THROMBIN INACTIVATION IN NORMAL PLASMA, SERUM AND PLASMA FRACTIONS, AND ITS RELATION TO HEPARIN.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	11-19
13908340-0	1961	On the effect of heparin at various concentrations with particular reference to increased heparin resistance measured by the plasma heparin thrombin time.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	140-148
13980541-0	1963	The precipitation of fibrinogen by heparin at pH 4.8.	Heparin	35-42	fibrinogen beta chain	Homo sapiens	21-31
13983862-0	1962	[The effect of vitamin B12 on the blood clearing factor and heparin in atherosclerotic patients].	Heparin	60-67	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	23-26
13912250-0	1962	Hydrolysis of glycerides of C-16 and C-18 fatty acids by post-heparin plasma.	Heparin	62-69	Bardet-Biedl syndrome 9	Homo sapiens	37-41
13908339-0	1962	Heparin resistance (measured by the heparin thrombin time) and plasma fibrinogen in various diseases.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	44-52
13953139-1	1963	Use of heparin for prevention and treatment in patients receiving ACTH or gluco-steroids.	Heparin	7-14	proopiomelanocortin	Homo sapiens	66-70
13919689-0	1961	[Effect of heparin and protamine on fibrinogen precipitation].	Heparin	11-18	fibrinogen beta chain	Homo sapiens	36-46
13715261-0	1961	Studies on increased heparin resistance measured by the plasma heparin thrombin time.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	71-79
13908340-0	1961	On the effect of heparin at various concentrations with particular reference to increased heparin resistance measured by the plasma heparin thrombin time.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	140-148
14402593-0	1960	Heparin resistance in acute coronary occlusion measured by the plasma heparin thrombin time.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	78-86
13706165-0	1961	The assay of heparin in thrombin systems.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	24-32
13709087-0	1961	In vitro effects heparin and chondroitin sulfuric acid B on the generation of thrombin.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	78-86
13850331-0	1960	Precipitation of human fibrinogen with heparin.	Heparin	39-46	fibrinogen beta chain	Homo sapiens	23-33
13848447-0	1960	Heparin resistance, measured by the plasma heparin thrombin time, in patients on long-term anticoagulatn therapy with phenylindanedione following coronary occlusion.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	51-59
14402592-0	1960	Increased heparin resistance after operation measured by teh plasma heparin thrombin time.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	76-84
14428016-13	1960	The disappearance of available heparin would also account for the normal thrombin generation and prothrombin consumption observed when heparinized blood clots.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	73-81
14428016-17	1960	Some plasma and serum fractions can be arranged in order of their increasing affinity for heparin thus: beta Lipoproteins<thrombin clotting system<C.F.<platelet protein<protamine sulphate.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	125-133
13412928-0	1956	[Formation of complexes between heparin and several proteins (insulin, vasopressin, oxytocin,  ACTH)].	Heparin	32-39	insulin	Homo sapiens	62-69
13488575-0	1957	[Study of fibrinogen precipitation by heparin at low temperatures].	Heparin	38-45	fibrinogen beta chain	Homo sapiens	10-20
13412928-0	1956	[Formation of complexes between heparin and several proteins (insulin, vasopressin, oxytocin,  ACTH)].	Heparin	32-39	arginine vasopressin	Homo sapiens	71-82
13412928-0	1956	[Formation of complexes between heparin and several proteins (insulin, vasopressin, oxytocin,  ACTH)].	Heparin	32-39	proopiomelanocortin	Homo sapiens	95-99
13245209-0	1955	[Problem of ACTH-heparin antagonisms].	Heparin	17-24	proopiomelanocortin	Homo sapiens	12-16
14387888-0	1955	[The thrombin inhibitor as expression of the endogenous heparin tolerance; determination and clinical significance].	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	5-13
13319488-0	1956	The action of heparin in the prevention of prothrombin conversion.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	43-54
13349502-0	1956	[Effect of heparin on percentage content of prothrombin; range of variations and their significance in relation to heparin with dicumarol therapy].	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	44-55
13349502-0	1956	[Effect of heparin on percentage content of prothrombin; range of variations and their significance in relation to heparin with dicumarol therapy].	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	44-55
13237261-0	1954	Fibrinogen preservation in serum after heparin.	Heparin	39-46	fibrinogen beta chain	Homo sapiens	0-10
13243272-0	1955	[Thrombin time and antithrombin power of human plasma in the presence of heparin and some synthetic heparinoids].	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	1-9
13305640-0	1955	[A simple method of determining thrombin inhibitor (heparin) activity].	Heparin	52-59	coagulation factor II, thrombin	Homo sapiens	32-40
13171198-0	1954	[Effect of ACTH-heparin regulation system on coagulation processes].	Heparin	16-23	proopiomelanocortin	Homo sapiens	11-15
13202410-0	1954	[Specificity of heparin activation by ACTH preparations].	Heparin	16-23	proopiomelanocortin	Homo sapiens	38-42
13097861-0	1953	[ACTH inhibition of heparin on blood coagulation; bases for ACTH testing].	Heparin	20-27	proopiomelanocortin	Homo sapiens	1-5
13118701-0	1953	[Heparin in ACTH excretion after stress].	Heparin	1-8	proopiomelanocortin	Homo sapiens	12-16
13137856-0	1954	[Studies on the response of ACTH, cortisone and epinephrine to heparin].	Heparin	63-70	proopiomelanocortin	Homo sapiens	28-32
14916345-0	1952	The influence of heparin on the activation energy of thrombin inactivation.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	53-61
13109152-11	1953	Heparin increases the rate considerably with low thrombin concentrations, but does not affect the rate with high thrombin concentrations.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	49-57
14829590-0	1951	Relation between heparin and thrombin inactivation.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	29-37
14926745-0	1952	[Plasma heparin action and prothrombin time during endarterial insulin therapy of peripheral arteritis].	Heparin	8-15	insulin	Homo sapiens	63-70
33289929-6	2021	During one study day, free fatty acids were elevated (to induce insulin resistance) by infusion of Intralipid with heparin.	Heparin	115-122	insulin	Homo sapiens	64-71
14955218-0	1951	[Correlations between heparin and the thrombin inactivation reaction of Gerendas].	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	38-46
18136511-0	1949	Protecting effect of heparin on the inactivation of thrombin by heat.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	52-60
18228878-0	1949	Protecting effect of heparin on the oxidation of thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	49-57
33910609-1	2021	BACKGROUND: During venovenous extracorporeal membrane oxygenation (vvECMO), direct thrombin inhibitors are considered by some potentially advantageous over unfractionated heparin (UFH).	Heparin	171-178	coagulation factor II, thrombin	Homo sapiens	83-91
33725411-9	2021	On heparin, both absolute and proportional changes of thrombin generation were comparable between all four cohorts (-62 to -85%).	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	54-62
33744761-2	2021	Basic fibroblast growth factor (bFGF1) similarly interacts with heparin-like molecules, notably heparan sulfate proteoglycans (HSPG), in the extracellular matrix and on cell surfaces.	Heparin	64-71	syndecan 2	Mus musculus	127-131
33929278-8	2021	Heparin potentiates antithrombin and hirudin binds to active thrombin, inactivating the thrombin irreversibly.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	24-32
33929278-8	2021	Heparin potentiates antithrombin and hirudin binds to active thrombin, inactivating the thrombin irreversibly.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	61-69
33607500-11	2021	The discovery of the binding of A1M to heparin and HS provides new insights into the biological role of A1M and represents the basis for a novel method for purification of A1M from plasma.	Heparin	39-46	PZP, alpha-2-macroglobulin like	Mus musculus	32-35
33607500-11	2021	The discovery of the binding of A1M to heparin and HS provides new insights into the biological role of A1M and represents the basis for a novel method for purification of A1M from plasma.	Heparin	39-46	PZP, alpha-2-macroglobulin like	Mus musculus	104-107
33607500-11	2021	The discovery of the binding of A1M to heparin and HS provides new insights into the biological role of A1M and represents the basis for a novel method for purification of A1M from plasma.	Heparin	39-46	PZP, alpha-2-macroglobulin like	Mus musculus	104-107
33745974-4	2021	We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin.	Heparin	119-126	fibroblast growth factor 1	Homo sapiens	45-49
33745974-4	2021	We have demonstrated that oligomerization of FGF1 with coiled-coil motifs largely improves FGF1 affinity for FGFRs and heparin.	Heparin	119-126	fibroblast growth factor 1	Homo sapiens	91-95
32876926-0	2021	Prediction of heparin binding of mutated short sequences of rat thyroglobulin.	Heparin	14-21	thyroglobulin	Rattus norvegicus	64-77
32876926-1	2021	BACKGROUND: Binding of thyroglobulin (Tg) to heparin is involved in Tg transcytosis via megalin.	Heparin	45-52	thyroglobulin	Rattus norvegicus	23-36
32876926-1	2021	BACKGROUND: Binding of thyroglobulin (Tg) to heparin is involved in Tg transcytosis via megalin.	Heparin	45-52	thyroglobulin	Rattus norvegicus	38-40
32876926-1	2021	BACKGROUND: Binding of thyroglobulin (Tg) to heparin is involved in Tg transcytosis via megalin.	Heparin	45-52	thyroglobulin	Rattus norvegicus	68-70
32876926-2	2021	Rat Tg (rTg) binds to heparin through an exposed carboxyl terminal region (RELPSRRLKRPLPVK, Arg2489-Lys2503) rich in positively charged residues.	Heparin	22-29	thyroglobulin	Rattus norvegicus	4-6
32876926-2	2021	Rat Tg (rTg) binds to heparin through an exposed carboxyl terminal region (RELPSRRLKRPLPVK, Arg2489-Lys2503) rich in positively charged residues.	Heparin	22-29	thyroglobulin	Rattus norvegicus	8-11
32876926-4	2021	Here, we developed a score to predict to what extent secondary structure modifications affect the heparin-binding ability of rTg.	Heparin	98-105	thyroglobulin	Rattus norvegicus	125-128
32876926-10	2021	CONCLUSIONS: The PSSC score allows predicting to what extent point mutations are likely to affect the heparin-binding ability of short sequences of proteins: in this case rTg, regardless of whether mutations affect charge of the sequence.	Heparin	102-109	thyroglobulin	Rattus norvegicus	171-174
32876926-11	2021	The secondary structure of Tg is likely to play a role in heparin binding.	Heparin	58-65	thyroglobulin	Rattus norvegicus	27-29
34006633-0	2021	Heparin-binding VEGFR1 variants as long-acting VEGF inhibitors for treatment of intraocular neovascular disorders.	Heparin	0-7	fms related receptor tyrosine kinase 1	Homo sapiens	16-22
34006633-0	2021	Heparin-binding VEGFR1 variants as long-acting VEGF inhibitors for treatment of intraocular neovascular disorders.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	16-20
34041343-4	2021	Methods: S100B concentrations were determined in 136 matching pairs of serum and lithium heparin blood samples.	Heparin	89-96	S100 calcium binding protein B	Homo sapiens	9-14
33910609-1	2021	BACKGROUND: During venovenous extracorporeal membrane oxygenation (vvECMO), direct thrombin inhibitors are considered by some potentially advantageous over unfractionated heparin (UFH).	Heparin	180-183	coagulation factor II, thrombin	Homo sapiens	83-91
33986810-0	2021	Surface Modification with NGF-Loaded Chitosan/Heparin Nanoparticles for Improving Biocompatibility of Cardiovascular Stent.	Heparin	46-53	nerve growth factor	Homo sapiens	26-29
33986810-4	2021	Based on the specific binding properties between heparin and nerve growth factor (NGF), a new type of NGF-loaded heparin/chitosan nanoparticles was constructed for surface modification.	Heparin	49-56	nerve growth factor	Homo sapiens	82-85
33986810-4	2021	Based on the specific binding properties between heparin and nerve growth factor (NGF), a new type of NGF-loaded heparin/chitosan nanoparticles was constructed for surface modification.	Heparin	49-56	nerve growth factor	Homo sapiens	102-105
33986810-4	2021	Based on the specific binding properties between heparin and nerve growth factor (NGF), a new type of NGF-loaded heparin/chitosan nanoparticles was constructed for surface modification.	Heparin	113-120	nerve growth factor	Homo sapiens	61-80
33986810-4	2021	Based on the specific binding properties between heparin and nerve growth factor (NGF), a new type of NGF-loaded heparin/chitosan nanoparticles was constructed for surface modification.	Heparin	113-120	nerve growth factor	Homo sapiens	82-85
33986810-4	2021	Based on the specific binding properties between heparin and nerve growth factor (NGF), a new type of NGF-loaded heparin/chitosan nanoparticles was constructed for surface modification.	Heparin	113-120	nerve growth factor	Homo sapiens	102-105
33846433-8	2021	Thrombin generation was higher in VA than VV patients, and the heparin dose required to suppress thrombin generation was lower in VA patients.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	97-105
33891270-12	2021	The Wnt/beta-catenin pathway, judged by TCF-driven luciferase activity, seems to be involved to enhance heparanase profile during treatment with exogenous heparin.	Heparin	155-162	catenin (cadherin-associated protein), beta 1	Danio rerio	8-20
33891270-14	2021	Taken together the results suggest that heparin modulates heparanase expression by Wnt/beta-catenin.	Heparin	40-47	catenin (cadherin-associated protein), beta 1	Danio rerio	87-99
33915354-4	2021	We have previously shown that MPO, a highly cationic protein, regulates coagulation through heteromolecular interactions with various negatively charged structures, including membrane phospholipids and low-molecular-weight heparin.	Heparin	223-230	myeloperoxidase	Homo sapiens	30-33
33610598-7	2021	The results indicated that heparin-iron has significantly reduced anticoagulant activity in vitro and in vivo, strongly decreases hepcidin mRNA and IL-6 induced high level of secreted hepcidin in HepG2 cell.	Heparin	27-34	interleukin 6	Homo sapiens	148-152
33610598-8	2021	Heparin-iron was also found to cause a reduction on hepcidin expression through BMP/SMAD and JAK/STAT3 pathways in LPS induced acute inflammation model in mice.	Heparin	0-7	signal transducer and activator of transcription 3	Mus musculus	97-102
33968948-6	2021	Heparin enhances the anticoagulant property of anti-thrombin (AT) and may be useful in conjunction with fibrinolytic drugs for severe COVID-19 patients.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	52-60
33968948-7	2021	Besides, heparin can also modulate immune responses, alleviating TNF-alpha-mediated inflammation, impairing IL-6 production and secretion, and binding to complement proteins and leukotriene B4 (LTB4).	Heparin	9-16	tumor necrosis factor	Homo sapiens	65-74
33968948-7	2021	Besides, heparin can also modulate immune responses, alleviating TNF-alpha-mediated inflammation, impairing IL-6 production and secretion, and binding to complement proteins and leukotriene B4 (LTB4).	Heparin	9-16	interleukin 6	Homo sapiens	108-112
34056268-3	2021	In the present study, we analyzed the effect of amyloid-beta-derived peptidomimetics for inhibiting heparin-induced tau aggregation in vitro.	Heparin	100-107	amyloid beta precursor protein	Homo sapiens	48-60
33595038-0	2021	Heparin-mediated electrostatic immobilization of bFGF via functional polymer films for enhanced self-renewal of human neural stem cells.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	49-53
33860518-4	2021	Thus, by activating antithrombin, heparin mainly inhibits factor Xa and thrombin, whereas VKAs lower the levels of the vitamin K-dependent clotting factors.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	24-32
33065736-5	2021	While LMWH-induced hyperalgesia was attenuated in both male and female rats pretreated with ODN antisense for CD44 and TLR4 mRNA, RHAMM antisense pretreatment only attenuated LMWH-induced hyperalgesia in males.	Heparin	6-10	toll-like receptor 4	Rattus norvegicus	119-123
33733622-0	2021	Heparin-modified alginate microspheres enhance neovessel formation in hiPSC-derived endothelial cells and heterocellular in vitro models by controlled release of vascular endothelial growth factor.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	162-196
33733622-3	2021	Sulfate and heparin moieties are covalently coupled to alginate, and alginate microspheres are produced and used as local delivery depots for vascular endothelial growth factor (VEGF).	Heparin	12-19	vascular endothelial growth factor A	Homo sapiens	142-176
33733622-3	2021	Sulfate and heparin moieties are covalently coupled to alginate, and alginate microspheres are produced and used as local delivery depots for vascular endothelial growth factor (VEGF).	Heparin	12-19	vascular endothelial growth factor A	Homo sapiens	178-182
33790886-6	2021	Alternatively, combining CFP-10-induced TNF-alpha and IP-10 with heparin-binding haemagglutinin (HBHA)-induced-IFN-gamma was more effective in testing recently BCG-vaccinated children or those suspected to be infected with non-tuberculous mycobacteria, providing a correct classification of 97% of the M. tuberculosis-infected children.	Heparin	65-72	interferon gamma	Homo sapiens	111-120
33690235-8	2020	Global transcriptional analysis revealed that the expression of Amphiregulin (Areg), a gene encoding a heparin-binding epidermal growth factor receptor ligand, was decreased drastically in Sox17+/- uterine epithelia.	Heparin	103-110	amphiregulin	Mus musculus	64-76
33690235-8	2020	Global transcriptional analysis revealed that the expression of Amphiregulin (Areg), a gene encoding a heparin-binding epidermal growth factor receptor ligand, was decreased drastically in Sox17+/- uterine epithelia.	Heparin	103-110	amphiregulin	Mus musculus	78-82
33869214-4	2021	Herein, we designed a silver (Ag) step-by-step cross-linking with the basic fibroblast growth factor (bFGF) by polydopamine (PDA) and heparin on titanium nanotube (TNT) as its cargo (TNT/PDA/Ag/bFGF) to improve the implant surface.	Heparin	134-141	fibroblast growth factor 2	Homo sapiens	70-100
33869214-4	2021	Herein, we designed a silver (Ag) step-by-step cross-linking with the basic fibroblast growth factor (bFGF) by polydopamine (PDA) and heparin on titanium nanotube (TNT) as its cargo (TNT/PDA/Ag/bFGF) to improve the implant surface.	Heparin	134-141	fibroblast growth factor 2	Homo sapiens	102-106
33749661-6	2021	However, the beta2 variants lost pH dependency for heparin binding, resulting in aberrant binding under physiologic conditions.	Heparin	51-58	glycoprotein hormone subunit alpha 2	Homo sapiens	13-18
33691128-3	2021	propose that heparin provides protection during gram-negative sepsis by dampening harmful CASP11-dependent signaling through inhibition of HMGB1- and heparanase-mediated cytosolic delivery of LPS.	Heparin	13-20	SR-related CTD associated factor 11	Homo sapiens	90-96
33595038-8	2021	Our results indicate that the coGD surface allowed in situ heparin-mediated bFGF immobilization, which served as a robust platform to generate hNSC neurospheres with enhanced self-renewal and differentiation capabilities and thereby will prompt an advance in the field of therapeutics of neurodegenerative diseases.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	76-80
33278841-7	2021	We detected a non-significant trend to loss of VWF:RCo after heparinisation and a significant recovery after protamine reversal which could reflect a direct heparin effect.	Heparin	61-68	von Willebrand factor	Homo sapiens	47-50
33746978-5	2021	In this study, we clarified the actions of DcR3 and its non-decoy action motif heparin sulfate proteoglycan (HSPG) binding domain (HBD) in the MSU crystal-induced NLRP3 inflammasome activation in the macrophages and in mice.	Heparin	79-86	exocyst complex component 6	Mus musculus	131-134
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	210-213
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	210-213
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	210-213
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	210-213
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	210-213
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-1	2021	To deliver photosensitizers with PEGylated heparin (HP) into tumor cells for photodynamic therapy, we prepared two polyethylene glycol (PEG)-functionalized HP-based polymers conjugated with pyropheophorbide-a (Ppa): a non-GSH-responsive nanoagent (HP-Ppa-mPEG) with the mPEG moiety chemically attached to HP directly; and a GSH-responsive nanoagent (HP-Ppa-SS-mPEG) with the mPEG moiety conjugated to HP via a disulfide linkage.	Heparin	156-158	preproenkephalin	Mus musculus	251-254
33436250-2	2021	The Ppa-functionalized HP without PEGylation (HP-Ppa) was designed as another control.	Heparin	23-25	preproenkephalin	Mus musculus	4-7
33436250-2	2021	The Ppa-functionalized HP without PEGylation (HP-Ppa) was designed as another control.	Heparin	46-48	preproenkephalin	Mus musculus	4-7
33436250-5	2021	HP-Ppa-SS-mPEG was found to achieve the highest tumor accumulation, the longest retention time and the best penetration into tumor tissues, resulting in the highest in vivo anticancer efficacy with 94.3 % tumor growth inhibition rate, suggesting that tumor microenvironment-responsive PEGylated HP-based nanomedicines may act as efficient anticancer agents.	Heparin	0-2	preproenkephalin	Mus musculus	3-6
33436250-5	2021	HP-Ppa-SS-mPEG was found to achieve the highest tumor accumulation, the longest retention time and the best penetration into tumor tissues, resulting in the highest in vivo anticancer efficacy with 94.3 % tumor growth inhibition rate, suggesting that tumor microenvironment-responsive PEGylated HP-based nanomedicines may act as efficient anticancer agents.	Heparin	295-297	preproenkephalin	Mus musculus	3-6
32515102-4	2021	Poly(2-hydroxyethyl methacrylate)-heparin hydrogels were capable of retaining FGF-2 by specific binding to heparin and subsequently showed sustained presentation of the growth factor to mesenchymal stromal cells (MSC).	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	78-83
32515102-4	2021	Poly(2-hydroxyethyl methacrylate)-heparin hydrogels were capable of retaining FGF-2 by specific binding to heparin and subsequently showed sustained presentation of the growth factor to mesenchymal stromal cells (MSC).	Heparin	107-114	fibroblast growth factor 2	Homo sapiens	78-83
32515102-5	2021	Heparin acted as stable anchoring molecules for FGF-2 on the substrate and the synergistic effect of the ensuing heparin-FGF-2 complex was evident in supporting long term cell growth.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	48-53
32515102-5	2021	Heparin acted as stable anchoring molecules for FGF-2 on the substrate and the synergistic effect of the ensuing heparin-FGF-2 complex was evident in supporting long term cell growth.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	121-126
32515102-5	2021	Heparin acted as stable anchoring molecules for FGF-2 on the substrate and the synergistic effect of the ensuing heparin-FGF-2 complex was evident in supporting long term cell growth.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	121-126
33586962-2	2021	The reduced content of N-sulfo, 3-O-sulfo glucosamine, the central and critical residue in heparin"s antithrombin III binding site, is responsible for bovine intestinal heparin"s reduced activity.	Heparin	91-98	serpin family C member 1	Bos taurus	101-117
33837899-9	2021	Fibrinogen is an independent predictor of resistance to heparin and should be considered before thromboprophylaxis.	Heparin	56-63	fibrinogen beta chain	Homo sapiens	0-10
33264641-1	2021	The endocrine FGF21 was discovered as a novel metabolic regulator in 2005 with new functions bifurcating from the canonic heparin-binding FGFs that directly promote cell proliferation and growth independent of a co-receptor.	Heparin	122-129	fibroblast growth factor 21	Homo sapiens	14-19
33508081-0	2021	Heparin Fragments Induce Cervical Inflammation by Recruiting Immune Cells through Toll-like Receptor 4 in nonpregnant mice.	Heparin	0-7	toll-like receptor 4	Mus musculus	82-102
33586962-2	2021	The reduced content of N-sulfo, 3-O-sulfo glucosamine, the central and critical residue in heparin"s antithrombin III binding site, is responsible for bovine intestinal heparin"s reduced activity.	Heparin	169-176	serpin family C member 1	Bos taurus	101-117
33197333-1	2021	Heparin and heparan sulfate (HS) are highly sulfated polysaccharides covalently bound to cell surface proteins, which directly interact with many extracellular proteins, including the transforming growth factor-beta (TGFbeta) family ligand antagonist, follistatin 288 (FS288).	Heparin	0-7	tumor necrosis factor	Homo sapiens	184-215
33430704-0	2021	Assessing the angiogenic efficacy of pleiotrophin released from injectable heparin-alginate gels.	Heparin	75-82	pleiotrophin	Homo sapiens	37-49
33302150-5	2021	To immobilise well-controlled soluble gradients of interleukin-8 (CXCL8), an inflammatory chemokine, we developed a simple procedure using a heparin-coated PDMS-microfluidic device.	Heparin	141-148	C-X-C motif chemokine ligand 8	Homo sapiens	51-64
33302150-5	2021	To immobilise well-controlled soluble gradients of interleukin-8 (CXCL8), an inflammatory chemokine, we developed a simple procedure using a heparin-coated PDMS-microfluidic device.	Heparin	141-148	C-X-C motif chemokine ligand 8	Homo sapiens	66-71
33176060-1	2021	BACKGROUND: Heparin enhances the ability of the plasma protease inhibitor, antithrombin, to neutralize coagulation factor Xa and thrombin.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	79-87
32812381-3	2021	We aimed to evaluate CRP effect on aPTT and anti-Xa assays in the presence of heparin and to determine whether elevated CRP affects laboratory monitoring in pediatric ECMO patients.	Heparin	78-85	C-reactive protein	Homo sapiens	21-24
32812381-6	2021	RESULTS: Elevated CRP prolonged aPTT in normal specimens with or without heparin, but did not affect anti-Xa assay.	Heparin	73-80	C-reactive protein	Homo sapiens	18-21
32812381-11	2021	Discordant changes of CRP and FVIII in plasma could contribute to aPTT/anti-Xa discrepancies observed during heparin therapy in the pediatric population.	Heparin	109-116	C-reactive protein	Homo sapiens	22-25
33263557-9	2021	Moreover, heparin suppresses the ERK response to UAG.	Heparin	10-17	mitogen-activated protein kinase 1	Homo sapiens	33-36
33176060-4	2021	METHODS: Inhibition of factor Xa and thrombin by antithrombin in the presence of different heparins and skeletal muscle myosin or cardiac myosin was studied by measuring inhibition of each enzyme"s chromogenic substrate hydrolysis.	Heparin	91-99	coagulation factor II, thrombin	Homo sapiens	37-45
33176060-5	2021	RESULTS AND CONCLUSIONS: Skeletal muscle myosin and cardiac myosin neutralized unfractionated heparin"s enhancement of antithrombin"s inhibition of purified factor Xa and thrombin.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	123-131
33482195-9	2021	Heparin has previously been reported to interfere with ANGPTL3 binding to LPL, so we questioned if the negatively charged heparin was acting in a similar fashion to the DNA contaminant.	Heparin	0-7	angiopoietin like 3	Homo sapiens	55-62
33618796-1	2021	On page 36, in the fifth sentence of right-side column, where it reads: "Direct thrombin inhibitors (DTI) (argatroban, bivalirrubin) are used in COVID-19 infected patients with significantly lower antithrombin levels,24 or if heparin induced thrombocytopenia (HIT) occurs.	Heparin	226-233	coagulation factor II, thrombin	Homo sapiens	80-88
33202269-0	2021	A Heparin based dual ratiometric sensor for Thrombin.	Heparin	2-9	coagulation factor II, thrombin	Homo sapiens	44-52
33202269-4	2021	Herein, we report a simple, selective, sensitive and label-free fluorescence detection scheme for Thrombin which is based on the interaction between Thrombin and a fluorescent complex of Heparin with a molecular rotor dye, Thioflavin-T.	Heparin	187-194	coagulation factor II, thrombin	Homo sapiens	98-106
33202269-4	2021	Herein, we report a simple, selective, sensitive and label-free fluorescence detection scheme for Thrombin which is based on the interaction between Thrombin and a fluorescent complex of Heparin with a molecular rotor dye, Thioflavin-T.	Heparin	187-194	coagulation factor II, thrombin	Homo sapiens	149-157
33202269-5	2021	The detection scheme exploits selective interaction between cationic Thrombin and anionic Heparin to modulate the monomer-aggregate equilibrium of the Thioflavin-T-Heparin system.	Heparin	164-171	coagulation factor II, thrombin	Homo sapiens	69-77
33618796-2	2021	"It should read: "Direct thrombin inhibitors (DTI) (argatroban, bivalirudin) are used in COVID-19 infected patients with significantly lower antithrombin levels,24 or if heparin induced thrombocytopenia (HIT) occurs.	Heparin	170-177	coagulation factor II, thrombin	Homo sapiens	25-33
33716209-4	2021	Midkine (MK) is a plasma-secreted multifunctional peptide which is a heparin-binding growth factor.	Heparin	69-76	midkine	Homo sapiens	0-7
33035717-2	2021	Herein, we proposed a kind of heparanase (HPSE)-driven sequential released nanoparticles, which modified with beta-cyclodextrin (beta-CD) grafted heparin (NLC/H(D + F + S) NPs) co-loading with doxorubicin (DOX), ferrocene (Fc), and TGF-beta receptor inhibitor (SB431542).	Heparin	146-153	heparanase	Homo sapiens	30-40
33035717-2	2021	Herein, we proposed a kind of heparanase (HPSE)-driven sequential released nanoparticles, which modified with beta-cyclodextrin (beta-CD) grafted heparin (NLC/H(D + F + S) NPs) co-loading with doxorubicin (DOX), ferrocene (Fc), and TGF-beta receptor inhibitor (SB431542).	Heparin	146-153	heparanase	Homo sapiens	42-46
33035717-2	2021	Herein, we proposed a kind of heparanase (HPSE)-driven sequential released nanoparticles, which modified with beta-cyclodextrin (beta-CD) grafted heparin (NLC/H(D + F + S) NPs) co-loading with doxorubicin (DOX), ferrocene (Fc), and TGF-beta receptor inhibitor (SB431542).	Heparin	146-153	ACD shelterin complex subunit and telomerase recruitment factor	Homo sapiens	129-136
32894831-8	2021	Furthermore, heparin-coated PMX-F acquired the capability to adsorb IL-6, IL-12, and tumor necrosis factor alpha.	Heparin	13-20	interleukin 6	Homo sapiens	68-72
32894831-8	2021	Furthermore, heparin-coated PMX-F acquired the capability to adsorb IL-6, IL-12, and tumor necrosis factor alpha.	Heparin	13-20	tumor necrosis factor	Homo sapiens	85-112
33401230-3	2021	In this study, a heparin oligosaccharide library, including dp2, dp4 and dp6, were prepared from the chemical modification of the fully sulfated dp2, dp4 and dp6.	Heparin	17-24	transcription factor Dp family member 3	Homo sapiens	65-68
33401230-3	2021	In this study, a heparin oligosaccharide library, including dp2, dp4 and dp6, were prepared from the chemical modification of the fully sulfated dp2, dp4 and dp6.	Heparin	17-24	transcription factor Dp family member 3	Homo sapiens	150-153
33716209-4	2021	Midkine (MK) is a plasma-secreted multifunctional peptide which is a heparin-binding growth factor.	Heparin	69-76	midkine	Homo sapiens	9-11
33396366-0	2020	Molecular Targeting of VEGF with a Suramin Fragment-DOCA Conjugate by Mimicking the Action of Low Molecular Weight Heparins.	Heparin	115-123	vascular endothelial growth factor A	Homo sapiens	23-27
33396366-2	2020	In the present study, we developed a novel suramin fragment and deoxycholic acid conjugate (SFD) that exhibited the potential to bind to the heparin-binding site (HBD) of vascular endothelial growth factor (VEGF) and to inhibit its pathogenic action for the first time.	Heparin	141-148	vascular endothelial growth factor A	Homo sapiens	171-205
33396366-2	2020	In the present study, we developed a novel suramin fragment and deoxycholic acid conjugate (SFD) that exhibited the potential to bind to the heparin-binding site (HBD) of vascular endothelial growth factor (VEGF) and to inhibit its pathogenic action for the first time.	Heparin	141-148	vascular endothelial growth factor A	Homo sapiens	207-211
33396366-4	2020	In the tubular formation assay, it was observed that SFD could bind to HBD and exhibit antiangiogenic efficacy by inhibiting VEGF, such as heparins.	Heparin	139-147	vascular endothelial growth factor A	Homo sapiens	125-129
32865287-0	2020	Effect of myeloperoxidase on the anticoagulant activity of low-molecular-weight heparin and rivaroxaban in an in-vitro tumor model.	Heparin	80-87	myeloperoxidase	Homo sapiens	10-25
33336117-10	2021	The downstream signaling of the FGF10 was also investigated, with the western blot results showing that FGF10 coacervate activated the p-FGFR, PI3K/Akt and ERK1/2 pathways to a more proper level than free FGF10 or heparin+FGF10.	Heparin	214-221	thymoma viral proto-oncogene 1	Mus musculus	148-151
33301474-5	2020	We identified for the first time that molecular pathways for heparin-binding, RAGE, miRNA, and PLA2 inhibitors were associated with SARS-CoV-2 infection.	Heparin	61-68	phospholipase A2 group IB	Homo sapiens	95-99
33159882-7	2020	As heparan sulfate modulates FGF-mediated signaling, we found a significantly decreased activation of the MAP kinases ERK1/2 in FGF-2-stimulated cell lines of affected individuals that could be restored by addition of heparin, a GAG similar to heparan sulfate.	Heparin	218-225	fibroblast growth factor 2	Homo sapiens	29-32
33159882-7	2020	As heparan sulfate modulates FGF-mediated signaling, we found a significantly decreased activation of the MAP kinases ERK1/2 in FGF-2-stimulated cell lines of affected individuals that could be restored by addition of heparin, a GAG similar to heparan sulfate.	Heparin	218-225	mitogen-activated protein kinase 3	Homo sapiens	118-124
33159882-7	2020	As heparan sulfate modulates FGF-mediated signaling, we found a significantly decreased activation of the MAP kinases ERK1/2 in FGF-2-stimulated cell lines of affected individuals that could be restored by addition of heparin, a GAG similar to heparan sulfate.	Heparin	218-225	fibroblast growth factor 2	Homo sapiens	128-133
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	hepatitis A virus cellular receptor 1	Mus musculus	122-146
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	hepatitis A virus cellular receptor 1	Mus musculus	148-153
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	tumor necrosis factor	Mus musculus	156-183
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	tumor necrosis factor	Mus musculus	185-194
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	interleukin 6	Mus musculus	201-219
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	B cell leukemia/lymphoma 2	Mus musculus	487-492
32976972-7	2020	Enzymic digestion by cell surface heparin/heparan sulfate using heparinase I, II, and III could significantly prevent TFV attachment, suggesting that heparan sulfate plays an important role in TFV attachment.	Heparin	34-41	heparinase i, ii, and iii	None	64-89
32853623-8	2020	Indeed, structural and sequence analysis evidenced for specificity of molecular interactions with cognate receptor (CXCR1) and glycosaminoglycan (heparin), thus providing evidence for a noticeable functional specificity and divergence between the two IL8 orthologs.	Heparin	146-153	C-X-C motif chemokine ligand 8	Homo sapiens	251-254
33356751-6	2021	We highlight one article in which phosphorylation of a 150 kDa platelet protein by heparin-containing ligands has been reported and propose that PEAR1 is a receptor for one or more glycosaminoglycan-conjugated proteins (proteoglycans).	Heparin	83-90	platelet endothelial aggregation receptor 1	Homo sapiens	145-150
33414726-5	2020	In this mini review, we address the physiology of Midkine, a growth factor able to bind heparin, and its pathophysiological potential role in COVID-19 determinism.	Heparin	88-95	midkine	Homo sapiens	50-57
33343739-6	2021	Experience with low serum albumin levels and antithrombin III activity in nephrotic patients helps to point out the decreasing effects of loop diuretics and heparin to other specialist disciplines.	Heparin	157-164	albumin	Homo sapiens	26-33
33362545-5	2020	For example, single-nucleotide polymorphisms (SNPs) in FGG, FGA, and F5 mediate increases in D-dimer and SNPs in ABO, CBS, CPS1 and MTHFR mediate differences in homocysteine levels, and SNPs in TDAG8 associate with Heparin-induced Thrombocytopenia.	Heparin	215-222	fibrinogen gamma chain	Homo sapiens	55-58
33362545-5	2020	For example, single-nucleotide polymorphisms (SNPs) in FGG, FGA, and F5 mediate increases in D-dimer and SNPs in ABO, CBS, CPS1 and MTHFR mediate differences in homocysteine levels, and SNPs in TDAG8 associate with Heparin-induced Thrombocytopenia.	Heparin	215-222	fibrinogen alpha chain	Homo sapiens	60-63
32885899-3	2020	Here, we complemented human embryonic stem cells-derived cardiac progenitor cells (hESC-CPC) therapy by heparin-conjugated, VEGF-loaded fibrin hydrogel as VEGF delivery system.	Heparin	104-111	vascular endothelial growth factor A	Homo sapiens	155-159
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	fibroblast growth factor 1	Homo sapiens	124-150
32682018-0	2020	A Collagen Valpha1-derived fragment inhibits FGF-2 induced-angiogenesis by modulating endothelial cells plasticity through its heparin-binding site.	Heparin	127-134	fibroblast growth factor 2	Homo sapiens	45-50
32682018-5	2020	Here we show that HEPV binds to FGF2 through its heparin-binding site.	Heparin	49-56	fibroblast growth factor 2	Homo sapiens	32-36
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	fibroblast growth factor 1	Homo sapiens	152-156
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	195-199
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	fibroblast growth factor 1	Homo sapiens	317-321
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	fibroblast growth factor 1	Homo sapiens	124-150
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	fibroblast growth factor 1	Homo sapiens	152-156
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	fibroblast growth factor 2	Homo sapiens	195-199
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	fibroblast growth factor 1	Homo sapiens	317-321
32662630-0	2020	Thermodynamic Analysis of the Interaction of Heparin with Lysozyme.	Heparin	45-52	lysozyme	Homo sapiens	58-66
33204588-8	2020	Inhibitor 1 has been proposed to bind to or near the heparin/polyphosphate-binding site in the catalytic domain of FXIa.	Heparin	53-60	protein phosphatase 1 regulatory inhibitor subunit 1A	Homo sapiens	0-11
32662630-2	2020	Aiming at a quantitative analysis of the involved processes, we herein present a thermodynamic study of the interaction of the model GAG heparin and lysozyme in aqueous solution.	Heparin	137-144	lysozyme	Homo sapiens	149-157
32662630-11	2020	The entire analysis shows that heparin-lysozyme interactions are mainly caused by counterion release, that is, ca.	Heparin	31-38	lysozyme	Homo sapiens	39-47
32763614-4	2020	The immunomodulatory extracellular matrix hydrogels (iECM) consist of an interpenetrating network of click functionalized-alginate and fibrillar collagen, in which interferon gamma (IFN-gamma) loaded heparin-coated beads are incorporated.	Heparin	200-207	interferon gamma	Homo sapiens	164-191
33193008-1	2020	Midkine (MK) is a small secreted heparin-binding protein highly expressed during embryonic/fetal development which, through interactions with multiple cell surface receptors promotes growth through effects on cell proliferation, migration, and differentiation.	Heparin	33-40	midkine	Homo sapiens	0-7
33193008-1	2020	Midkine (MK) is a small secreted heparin-binding protein highly expressed during embryonic/fetal development which, through interactions with multiple cell surface receptors promotes growth through effects on cell proliferation, migration, and differentiation.	Heparin	33-40	midkine	Homo sapiens	9-11
33426224-6	2020	Methods: In this paper, we focused on the biological stability of bFGF immobilized on the heparin-conjugated collagen (hep-col) scaffold.	Heparin	90-97	fibroblast growth factor 2	Homo sapiens	66-70
32772348-5	2020	Addition of fibrinogen restored in vitro thrombus formation in the presence of antiplatelet drugs and heparin.	Heparin	102-109	fibrinogen beta chain	Homo sapiens	12-22
32763614-6	2020	Moreover, the inclusion of IFN-gamma loaded heparin-coated beads prolonged the expression of key regulatory genes upregulated upon licensing, including indoleamine 2,3-dioxygenase 1 (IDO1) and galectin-9 (GAL9).	Heparin	44-51	interferon gamma	Homo sapiens	27-36
32763614-6	2020	Moreover, the inclusion of IFN-gamma loaded heparin-coated beads prolonged the expression of key regulatory genes upregulated upon licensing, including indoleamine 2,3-dioxygenase 1 (IDO1) and galectin-9 (GAL9).	Heparin	44-51	galectin 9	Homo sapiens	193-203
32763614-6	2020	Moreover, the inclusion of IFN-gamma loaded heparin-coated beads prolonged the expression of key regulatory genes upregulated upon licensing, including indoleamine 2,3-dioxygenase 1 (IDO1) and galectin-9 (GAL9).	Heparin	44-51	galectin 9	Homo sapiens	205-209
32568405-6	2020	NGF and BDNF were bound by electrostatic interaction to heparin, and the release profile evaluated by ELISA assay, which showed that ca.	Heparin	56-63	nerve growth factor	Homo sapiens	0-3
32562271-1	2020	Heparin is a widely used anti-coagulant that enhances anti-thrombin (AT) activity.	Heparin	0-7	coagulation factor II	Mus musculus	59-67
32002805-0	2020	Heparin Administration, but Not Myocardial Ischemia or Necrosis, Leads to Midkine Elevation.	Heparin	0-7	midkine	Homo sapiens	74-81
31686597-1	2020	The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	20-28
32563919-3	2020	In this paper, two types of materials, P-BMP-2 and PH-BMP-2, were prepared by covalent immobilization and heparin binding of rhBMP-2 respectively to enhance the osteogenic activity of PPENK.	Heparin	106-113	bone morphogenetic protein 2	Mus musculus	41-46
32002805-1	2020	Midkine (MK) is a heparin-binding growth factor, whose role as a biomarker of coronary artery disease, myocardial ischaemia and necrosis has not been well measured.	Heparin	18-25	midkine	Homo sapiens	0-7
32002805-1	2020	Midkine (MK) is a heparin-binding growth factor, whose role as a biomarker of coronary artery disease, myocardial ischaemia and necrosis has not been well measured.	Heparin	18-25	midkine	Homo sapiens	9-11
31686597-1	2020	The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	20-28
32002805-8	2020	Heparin administration had an immediate effect on median MK at 10 min, showing an average 500-fold increase that is dose-dependent (R2 = 0.35, p = 0.001).	Heparin	0-7	midkine	Homo sapiens	57-59
32002805-9	2020	Median MK levels remained elevated at 20 min following heparin administration.	Heparin	55-62	midkine	Homo sapiens	7-9
32002805-13	2020	MK increased significantly in all patients following heparin administration in a dose-dependent manner.	Heparin	53-60	midkine	Homo sapiens	0-2
32931543-0	2020	Heparin-based, injectable microcarriers for controlled delivery of interleukin-13 to the brain.	Heparin	0-7	interleukin 13	Homo sapiens	67-81
32856665-5	2020	In this study, we generated three PEGylated FGF2 variants based on the structure of the FGF2-FGFR-heparin ternary complex via gene mutation and PEGylation, and investigated the effects of these PEGylated sites on protein stability and bioactivity.	Heparin	98-105	fibroblast growth factor 2	Homo sapiens	44-48
32856665-5	2020	In this study, we generated three PEGylated FGF2 variants based on the structure of the FGF2-FGFR-heparin ternary complex via gene mutation and PEGylation, and investigated the effects of these PEGylated sites on protein stability and bioactivity.	Heparin	98-105	fibroblast growth factor 2	Homo sapiens	88-92
32688092-3	2020	The loading efficiency of growth factors into these biomaterials was found to be >90%, revealing a strong affinity of VEGF and BMP-2 to heparin and alginate.	Heparin	136-143	vascular endothelial growth factor A	Homo sapiens	118-122
32717572-2	2020	The inhibitor"s action is enhanced in the presence of polyanionic cofactors, such as heparin and polyphosphate, by increasing the rate of association with key enzymes such as C1s of the classical pathway of complement.	Heparin	85-92	complement C1s	Homo sapiens	175-178
33005203-5	2020	We, furthermore, investigated the influence of heparin on the expressions of TNF-alpha, IL-1beta, CD40, NF-kappaB, and HIF-1alpha after asphyxial CA.	Heparin	47-54	tumor necrosis factor	Rattus norvegicus	77-86
33005203-5	2020	We, furthermore, investigated the influence of heparin on the expressions of TNF-alpha, IL-1beta, CD40, NF-kappaB, and HIF-1alpha after asphyxial CA.	Heparin	47-54	interleukin 1 alpha	Rattus norvegicus	88-96
32931543-2	2020	Herein, we show that heparin-based cryogel microcarriers load high amounts of IL-13, releasing it slowly.	Heparin	21-28	interleukin 13	Homo sapiens	78-83
32905282-6	2020	Careful attention to his daily platelet count suggested the possibility of immune mediated heparin-induced thrombocytopenia (HIT) which was confirmed by laboratory testing and resolved when anticoagulation was switched to a direct thrombin inhibitor.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	231-239
32879333-1	2020	Midkine (MDK), a heparin-binding growth factor cytokine, is involved in the pathogenesis of kidney diseases by augmenting leukocyte trafficking and activation.	Heparin	17-24	midkine	Homo sapiens	0-7
32879333-1	2020	Midkine (MDK), a heparin-binding growth factor cytokine, is involved in the pathogenesis of kidney diseases by augmenting leukocyte trafficking and activation.	Heparin	17-24	midkine	Homo sapiens	9-12
32127275-1	2020	OBJECTIVE: High heparin doses during cardiopulmonary bypass (CPB) have been suggested to reduce thrombin activation and consumption coagulopathy and consequently bleeding complications.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	96-104
32502943-8	2020	Heparin (Hep, a competitive IP3 receptor blocker) and chelerythrine (Che, a protein kinase C inhibitor) also caused plFM.	Heparin	0-7	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	28-40
32127275-3	2020	The authors hypothesized that during CPB a high heparin dose compared with a lower heparin dose would reduce thrombin generation and platelet activation and tested whether this would be reflected in the results of rotational thromboelastometry (TEM) and platelet aggregation, measured with multiple electrode aggregometry (MEA).	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	109-117
32127275-3	2020	The authors hypothesized that during CPB a high heparin dose compared with a lower heparin dose would reduce thrombin generation and platelet activation and tested whether this would be reflected in the results of rotational thromboelastometry (TEM) and platelet aggregation, measured with multiple electrode aggregometry (MEA).	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	109-117
32267995-0	2020	Insulin and heparin challenge tests are useful for choosing an optimal insulin regimen in a case of subcutaneous insulin resistance.	Heparin	12-19	insulin	Homo sapiens	71-78
32267995-0	2020	Insulin and heparin challenge tests are useful for choosing an optimal insulin regimen in a case of subcutaneous insulin resistance.	Heparin	12-19	insulin	Homo sapiens	113-120
32267995-3	2020	To choose an optimal insulin regimen, we performed subcutaneous insulin challenge tests without or with heparin mixture and found a cocktail of insulin lispro and heparin could reduce blood glucose levels markedly.	Heparin	163-170	insulin	Homo sapiens	21-28
32267995-3	2020	To choose an optimal insulin regimen, we performed subcutaneous insulin challenge tests without or with heparin mixture and found a cocktail of insulin lispro and heparin could reduce blood glucose levels markedly.	Heparin	163-170	insulin	Homo sapiens	64-71
32267995-3	2020	To choose an optimal insulin regimen, we performed subcutaneous insulin challenge tests without or with heparin mixture and found a cocktail of insulin lispro and heparin could reduce blood glucose levels markedly.	Heparin	163-170	insulin	Homo sapiens	64-71
32267995-5	2020	In summary, the insulin and heparin challenge tests are useful for choosing an optimal insulin regimen in cases of SIR.	Heparin	28-35	insulin	Homo sapiens	87-94
32797846-2	2020	hFGF-2 is produced in Escherichia coli and purified via three different chromatography steps, which include a strong cation exchange chromatography as a capture step, followed by heparin affinity chromatography and an anion exchange chromatography as a polishing step.	Heparin	179-186	fibroblast growth factor 2	Homo sapiens	0-6
32668058-8	2020	RESULTS AND CONCLUSIONS: We observed two key findings: a high thrombin generation capacity that remained within normal values despite heparin therapy and a hypofibrinolysis mainly associated with increased PAI-1 levels.	Heparin	134-141	coagulation factor II, thrombin	Homo sapiens	62-70
32863239-6	2020	Exposure of fibronectin to MPO/H2O2/Cl- is shown to result in damage to the functionally important cell-binding and heparin-binding fragments, gross structural changes to the protein, and altered HCAEC adhesion and activity.	Heparin	116-123	fibronectin 1	Homo sapiens	12-23
32863239-6	2020	Exposure of fibronectin to MPO/H2O2/Cl- is shown to result in damage to the functionally important cell-binding and heparin-binding fragments, gross structural changes to the protein, and altered HCAEC adhesion and activity.	Heparin	116-123	myeloperoxidase	Homo sapiens	27-30
32496552-7	2020	Our simulations attribute the previously-observed platelet-recruitment reduction and heparin-size modulation, upon establishment of DNA-vWF interactions, to indirect steric hindrance and partial overlap of the binding sites, respectively.	Heparin	85-92	von Willebrand factor	Homo sapiens	136-139
32847073-9	2020	MDK is a heparin-binding growth factor that promotes angiogenesis and carcinogenesis.	Heparin	9-16	midkine	Homo sapiens	0-3
32824699-3	2020	Previous reports have suggested that the glycosaminoglycan heparin is a ligand for the natural cytotoxicity receptors NKp30, NKp44 (human), and NKp46 (both human and mouse).	Heparin	59-66	natural cytotoxicity triggering receptor 2	Homo sapiens	125-130
32824699-7	2020	In human NK cells, heparin promisingly increased interferon (IFN)-gamma production in synergy with IL-12, although the mechanism remains elusive.	Heparin	19-26	interferon gamma	Homo sapiens	49-71
32179141-11	2020	Caspase-3 immunoexpression was lower in the heparin than the non-heparin group for both liver and kidney.	Heparin	44-51	caspase 3	Sus scrofa	0-9
32179141-11	2020	Caspase-3 immunoexpression was lower in the heparin than the non-heparin group for both liver and kidney.	Heparin	65-72	caspase 3	Sus scrofa	0-9
32779783-0	2020	Effect of low or high doses of low-molecular-weight heparin on thrombin generation and other haemostasis parameters in critically ill patients with COVID-19.	Heparin	52-59	coagulation factor II, thrombin	Homo sapiens	63-71
32751642-5	2020	Hsp22 wild-type (WT) protein had a significant inhibitory effect on heparin-induced aggregation in vitro and the pseudophosphorylated mutant Hsp22 demonstrated a similar effect.	Heparin	68-75	heat shock protein family B (small) member 8	Homo sapiens	0-5
32649510-2	2020	In this study, we aimed at investigating the effects of unfractionated heparin (UFH) on the lipopolysaccharide (LPS)-induced changes of vascular endothelial-cadherin (VE-cadherin) and the potential underlying mechanisms.	Heparin	71-78	cadherin 5	Mus musculus	136-165
32649510-2	2020	In this study, we aimed at investigating the effects of unfractionated heparin (UFH) on the lipopolysaccharide (LPS)-induced changes of vascular endothelial-cadherin (VE-cadherin) and the potential underlying mechanisms.	Heparin	71-78	cadherin 5	Mus musculus	167-178
32649510-2	2020	In this study, we aimed at investigating the effects of unfractionated heparin (UFH) on the lipopolysaccharide (LPS)-induced changes of vascular endothelial-cadherin (VE-cadherin) and the potential underlying mechanisms.	Heparin	80-83	cadherin 5	Mus musculus	136-165
32649510-2	2020	In this study, we aimed at investigating the effects of unfractionated heparin (UFH) on the lipopolysaccharide (LPS)-induced changes of vascular endothelial-cadherin (VE-cadherin) and the potential underlying mechanisms.	Heparin	80-83	cadherin 5	Mus musculus	167-178
32649510-12	2020	CONCLUSIONS: The protective effect of UFH against LPS-induced pulmonary endothelial barrier dysfunction involves VE-cadherin stabilization and PI3K/Akt/NF-kappaB signaling.	Heparin	38-41	cadherin 5	Homo sapiens	113-124
32649510-12	2020	CONCLUSIONS: The protective effect of UFH against LPS-induced pulmonary endothelial barrier dysfunction involves VE-cadherin stabilization and PI3K/Akt/NF-kappaB signaling.	Heparin	38-41	AKT serine/threonine kinase 1	Homo sapiens	148-151
32649510-12	2020	CONCLUSIONS: The protective effect of UFH against LPS-induced pulmonary endothelial barrier dysfunction involves VE-cadherin stabilization and PI3K/Akt/NF-kappaB signaling.	Heparin	38-41	nuclear factor kappa B subunit 1	Homo sapiens	152-161
32289504-5	2020	Furthermore, phospholipid hydrolysis, mild oxidation and/or glycation of LDL in vitro increase the proteolytic susceptibility of apoB and its heparin binding affinity, perhaps by unmasking additional heparin-binding sites.	Heparin	142-149	apolipoprotein B	Homo sapiens	129-133
32289504-5	2020	Furthermore, phospholipid hydrolysis, mild oxidation and/or glycation of LDL in vitro increase the proteolytic susceptibility of apoB and its heparin binding affinity, perhaps by unmasking additional heparin-binding sites.	Heparin	200-207	apolipoprotein B	Homo sapiens	129-133
32289504-6	2020	For LDL from hyperglycemic type-2 diabetic patients, heparin binding was particularly destabilizing and caused apoB fragmentation and LDL fusion.	Heparin	53-60	apolipoprotein B	Homo sapiens	111-115
32289504-9	2020	In summary, binding to heparin alters apoB conformation, perhaps by partially peeling it off the lipid, and triggers pro-atherogenic LDL modifications including hydrolysis, oxidation, and destabilization.	Heparin	23-30	apolipoprotein B	Homo sapiens	38-42
32767339-3	2020	The aim of this study was to search for associations between serum Pfn1 and a number of parameters in MI patients: symptom onset to PCI time (OPT), myocardial necrosis markers, thrombolysis in myocardial infarction (TIMI) flow, antiplatelet drugs, heparin administration and typical atherosclerosis risk factors.	Heparin	248-255	profilin 1	Homo sapiens	67-71
32459011-8	2020	The total heparin requirement per body surface area had significant correlations with the anti-factor Chia activity (r=-0.36) and DOAC concentration (r=-0.32).	Heparin	10-17	chitinase acidic	Homo sapiens	102-106
32459011-9	2020	Two different multiple linear regression models (adjusted R2 =0.56 and 0.6, respectively) revealed that the anti-factor Chia activity (beta=-0.28; P=0.002) and DOAC concentration (beta=-0.38; P <0.001) were independent determinants of the total heparin requirement.	Heparin	245-252	chitinase acidic	Homo sapiens	120-124
32525079-5	2020	Herein, insulin was encapsulated into different poly(lactic-co-glycolic acid) (PLGA) nanoparticles (NPs) formulations prepared by microfluidic technique, which were further appended with heparin sulfate for oral insulin delivery.	Heparin	187-194	insulin	Homo sapiens	8-15
32525079-13	2020	Mucopenetrating heparin sulfate conjugated PLGA NPs significantly improved insulin permeability in triple co-cultured intestinal model compared to unmodified and free insulin with two and three-fold increase.	Heparin	16-23	insulin	Homo sapiens	75-82
32764936-12	2020	Sdc-2 might be an important heparin-sensitive cell membrane regulator in osteoblastic cell adhesion, specifically on NanoZr, through the organization of actin cytoskeleton and affects osteoblastic cell proliferation.	Heparin	28-35	syndecan 2	Mus musculus	0-5
32377957-4	2020	The second aim was to assess a potential correlation between plasma pre-treatment coagulation parameters and anti-Xa levels in an assumption that heparanase degradation activity towards heparins and HS chains could affect anti-Xa levels.	Heparin	186-194	heparanase	Homo sapiens	146-156
32544388-6	2020	In this direction, additional simulations provide evidence that 1) a surface-localized enzyme, speculatively identified as meizothrombin, is significantly active toward the fluorescent thrombin substrate used in the experiments or, less likely, 2) thrombin is irreversibly inhibited at a faster-than-expected rate, possibly explained by a stimulatory effect of plasma heparin on antithrombin.	Heparin	368-375	coagulation factor II, thrombin	Homo sapiens	128-136
32544388-6	2020	In this direction, additional simulations provide evidence that 1) a surface-localized enzyme, speculatively identified as meizothrombin, is significantly active toward the fluorescent thrombin substrate used in the experiments or, less likely, 2) thrombin is irreversibly inhibited at a faster-than-expected rate, possibly explained by a stimulatory effect of plasma heparin on antithrombin.	Heparin	368-375	coagulation factor II, thrombin	Homo sapiens	185-193
32668719-8	2020	Combined C1-INH/heparin coatings yielded similarly low levels of thrombin-antithrombin III complex formation as heparin coating.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	65-73
32515141-0	2020	Thermosensitive heparin-poloxamer hydrogel encapsulated bFGF and NGF to treat spinal cord injury.	Heparin	16-23	fibroblast growth factor 2	Homo sapiens	56-60
32515141-0	2020	Thermosensitive heparin-poloxamer hydrogel encapsulated bFGF and NGF to treat spinal cord injury.	Heparin	16-23	nerve growth factor	Homo sapiens	65-68
32656428-3	2020	In this study, in situ heparin (HeP) hydrogel injection containing bFGF and DPSCs (HeP-bFGF-DPSCs), as well as in vitro studies of bFGF and DPSCs, proved an effective control over inflammation.	Heparin	83-86	fibroblast growth factor 2	Homo sapiens	87-91
32422680-7	2020	Kinetic analysis revealed the stoichiometry of AT-T90S inhibition of both thrombin and factor Xa has been elevated by three- to fourfold in both the absence and presence of heparin, suggesting that the reactivity of coagulation proteases with AT-T90S has been elevated in the substrate pathway.	Heparin	173-180	coagulation factor II, thrombin	Homo sapiens	74-82
32549254-1	2020	We report dual therapeutic effects of a synthetic heparin-binding peptide (HBP) corresponding to residues 15-24 of the heparin binding site in BMP4 in a collagen-induced rheumatic arthritis model (CIA) for the first time.	Heparin	50-57	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	75-78
32292283-1	2020	Introduction: Serum samples of haemodialysed patients collected through vascular access devices, e.g. central venous catheter (CVC) can contain residual heparin, which can cause incomplete clotting and consequently fibrinogen interference in serum protein electrophoresis (SPE).	Heparin	153-160	fibrinogen beta chain	Homo sapiens	215-225
32292283-7	2020	Conclusion: Fibrinogen interference caused by incomplete clotting because of residual heparin can be overcome by addition of thrombin.	Heparin	86-93	fibrinogen beta chain	Homo sapiens	12-22
32292283-7	2020	Conclusion: Fibrinogen interference caused by incomplete clotting because of residual heparin can be overcome by addition of thrombin.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	125-133
32549254-1	2020	We report dual therapeutic effects of a synthetic heparin-binding peptide (HBP) corresponding to residues 15-24 of the heparin binding site in BMP4 in a collagen-induced rheumatic arthritis model (CIA) for the first time.	Heparin	50-57	bone morphogenetic protein 4	Mus musculus	143-147
32526859-1	2020	Fibroblast growth factor 2 (FGF2) is a heparin-binding growth factor with broad mitogenic and cell survival activities.	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	0-26
32458960-2	2020	Vascular endothelial growth factor A (VEGF-A) is a kind of protein with heparin affinity involved in the pathogenesis and progression of many angiogenesis-dependent diseases including cancer.	Heparin	72-79	vascular endothelial growth factor A	Homo sapiens	0-36
32458960-2	2020	Vascular endothelial growth factor A (VEGF-A) is a kind of protein with heparin affinity involved in the pathogenesis and progression of many angiogenesis-dependent diseases including cancer.	Heparin	72-79	vascular endothelial growth factor A	Homo sapiens	38-44
32458960-3	2020	As an important step in the angiogenesis-related cascade, it is necessary to clarify the interaction between VEGF165 (the major form of VEGF-A) and heparin.	Heparin	148-155	vascular endothelial growth factor A	Homo sapiens	136-142
32526859-1	2020	Fibroblast growth factor 2 (FGF2) is a heparin-binding growth factor with broad mitogenic and cell survival activities.	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	28-32
31471680-6	2020	SELENOP was interacted with apolipoprotein E (ApoE) through heparin-binding sites of SELENOP, and the interaction regulated the secretion of exosomal SELENOP.	Heparin	60-67	apolipoprotein E	Mus musculus	28-44
31471680-6	2020	SELENOP was interacted with apolipoprotein E (ApoE) through heparin-binding sites of SELENOP, and the interaction regulated the secretion of exosomal SELENOP.	Heparin	60-67	apolipoprotein E	Mus musculus	46-50
32064767-0	2020	Heparin/ Poly-l-lysine nanoplatform with growth factor delivery for surface modification of cardiovascular stents: the influence of VEGF loading.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	132-136
32466274-0	2020	Studies on the Mechanisms of Anti-Inflammatory Activity of Heparin- and Hyaluronan-Containing Multilayer Coatings-Targeting NF-kappaB Signalling Pathway.	Heparin	59-66	nuclear factor kappa B subunit 1	Homo sapiens	124-133
32302701-7	2020	RESULTS: Low-dose heparin posttreatment improved neurobehavioral function, brain edema, blood-brain barrier disruption and death in the cortex, associated with an increase in SphK1 and phosphorylated Akt, and a decrease in cleaved caspase-3.	Heparin	18-25	thymoma viral proto-oncogene 1	Mus musculus	200-203
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	49-56	interleukin 6	Homo sapiens	145-158
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	49-56	interleukin 6	Homo sapiens	160-164
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	49-56	C-X-C motif chemokine ligand 8	Homo sapiens	167-180
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	49-56	C-X-C motif chemokine ligand 8	Homo sapiens	182-186
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	84-91	interleukin 6	Homo sapiens	145-158
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	84-91	interleukin 6	Homo sapiens	160-164
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	84-91	C-X-C motif chemokine ligand 8	Homo sapiens	167-180
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	84-91	C-X-C motif chemokine ligand 8	Homo sapiens	182-186
32466274-5	2020	Moreover, multilayers containing either HA or Hep dampened the inflammatory response visible by reduced adhesion, formation of multinucleated giant cells (MNGCs) and IL-1beta release, which was studied using THP-1 derived macrophages.	Heparin	46-49	GLI family zinc finger 2	Homo sapiens	208-213
32550069-6	2020	Patients" resistance to prophylactic doses of heparin could be due to low levels of anti-thrombin and high levels of fibrinogen, which would reinforce the use of therapeutic doses of heparin in the early stages of hospitalization.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	89-97
32550069-6	2020	Patients" resistance to prophylactic doses of heparin could be due to low levels of anti-thrombin and high levels of fibrinogen, which would reinforce the use of therapeutic doses of heparin in the early stages of hospitalization.	Heparin	46-53	fibrinogen beta chain	Homo sapiens	117-127
32550069-6	2020	Patients" resistance to prophylactic doses of heparin could be due to low levels of anti-thrombin and high levels of fibrinogen, which would reinforce the use of therapeutic doses of heparin in the early stages of hospitalization.	Heparin	183-190	coagulation factor II, thrombin	Homo sapiens	89-97
32550069-6	2020	Patients" resistance to prophylactic doses of heparin could be due to low levels of anti-thrombin and high levels of fibrinogen, which would reinforce the use of therapeutic doses of heparin in the early stages of hospitalization.	Heparin	183-190	fibrinogen beta chain	Homo sapiens	117-127
32088260-4	2020	Commercial heparins were shown to be strong inhibitors of hepcidin expression, by interfering with BMP6/SMAD pathway.	Heparin	11-19	bone morphogenetic protein 6	Homo sapiens	99-103
32420975-3	2020	CASE REPORT: A woman affected by stage IV breast cancer with lower extremity deep vein thrombosis treated with low-molecular-weight-heparin, currently in therapy with Palbociclib/Fulvestrant (antiCDK4 and 6/estrogen receptor antagonist) but previously treated with several other chemotherapy lines (including VEGF inhibitor bevacizumab), was admitted to our Internal Medicine department because of ascites and abdominal pain.	Heparin	132-139	vascular endothelial growth factor A	Homo sapiens	309-313
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	21-28	vascular endothelial growth factor A	Homo sapiens	142-146
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	21-28	transforming growth factor beta 1	Homo sapiens	148-157
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	21-28	transforming growth factor beta 1	Homo sapiens	327-336
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	102-109	vascular endothelial growth factor A	Homo sapiens	142-146
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	102-109	transforming growth factor beta 1	Homo sapiens	148-157
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	102-109	transforming growth factor beta 1	Homo sapiens	327-336
32355037-5	2020	The capabilities of the individual LAR fragments to interact with heparin was examined using microscale thermophoresis and heparin-affinity chromatography.	Heparin	66-73	protein tyrosine phosphatase receptor type F	Homo sapiens	35-38
32355037-5	2020	The capabilities of the individual LAR fragments to interact with heparin was examined using microscale thermophoresis and heparin-affinity chromatography.	Heparin	123-130	protein tyrosine phosphatase receptor type F	Homo sapiens	35-38
32355037-8	2020	Together, the presented results suggest the presence of an additional heparin-binding site in human LAR.	Heparin	70-77	protein tyrosine phosphatase receptor type F	Homo sapiens	100-103
32088260-5	2020	The non-anti-coagulant heparins, modified to abolish the anti-thrombin binding site, were equally potent and could be used to improve iron status.	Heparin	23-31	coagulation factor II, thrombin	Homo sapiens	62-70
32344508-7	2020	Microscale thermophoresis (MST) measurements revealed high-affinity binding to polyphosphate 45 (KD: 466 +- 75 nM) and activation of vaspin in a heparin-like manner.	Heparin	145-152	serpin family A member 12	Homo sapiens	133-139
32153221-5	2020	Thrombin generation was evaluated in vitro in rat and NHP plasmas with ascending doses of unfractionated heparin (UFH), recombinant tissue factor, and anticoagulant compounds.	Heparin	105-112	coagulation factor II	Rattus norvegicus	0-8
32153221-5	2020	Thrombin generation was evaluated in vitro in rat and NHP plasmas with ascending doses of unfractionated heparin (UFH), recombinant tissue factor, and anticoagulant compounds.	Heparin	114-117	coagulation factor II	Rattus norvegicus	0-8
32153221-6	2020	Thrombin generation was decreased with UFH and anticoagulant compounds, but was increased in the presence of tissue factor, in a dose-dependent manner.	Heparin	39-42	coagulation factor II	Rattus norvegicus	0-8
32576355-8	2020	On the 6th day of treatment, the plasma thrombin time (TT) in the heparin treatment group was significantly shorter than that on the 3rd day of treatment [s: 30.3 (20.4, 37.0) vs. 34.7 (24.0, 73.4), P < 0.05], and the fibrinogen (FIB) in the heparin treatment group was significantly higher than that in the non-heparin treatment group [g/L: 0.60 (0.31, 1.07) vs. 0.20 (0.14, 0.60), P < 0.01].	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	40-48
32576355-8	2020	On the 6th day of treatment, the plasma thrombin time (TT) in the heparin treatment group was significantly shorter than that on the 3rd day of treatment [s: 30.3 (20.4, 37.0) vs. 34.7 (24.0, 73.4), P < 0.05], and the fibrinogen (FIB) in the heparin treatment group was significantly higher than that in the non-heparin treatment group [g/L: 0.60 (0.31, 1.07) vs. 0.20 (0.14, 0.60), P < 0.01].	Heparin	66-73	fibrinogen beta chain	Homo sapiens	218-228
32576355-8	2020	On the 6th day of treatment, the plasma thrombin time (TT) in the heparin treatment group was significantly shorter than that on the 3rd day of treatment [s: 30.3 (20.4, 37.0) vs. 34.7 (24.0, 73.4), P < 0.05], and the fibrinogen (FIB) in the heparin treatment group was significantly higher than that in the non-heparin treatment group [g/L: 0.60 (0.31, 1.07) vs. 0.20 (0.14, 0.60), P < 0.01].	Heparin	66-73	fibrinogen beta chain	Homo sapiens	230-233
32107314-6	2020	Both cell types expressed increased levels of pro-inflammatory markers - inducible nitric oxide synthase (iNOS), and tumor necrosis factor-alpha (TNF-alpha)- when cultured under hyperglycemic stress, which was inhibited by heparin.	Heparin	223-230	nitric oxide synthase 2	Rattus norvegicus	73-104
32107314-6	2020	Both cell types expressed increased levels of pro-inflammatory markers - inducible nitric oxide synthase (iNOS), and tumor necrosis factor-alpha (TNF-alpha)- when cultured under hyperglycemic stress, which was inhibited by heparin.	Heparin	223-230	tumor necrosis factor	Rattus norvegicus	117-144
32182331-10	2020	Heparin downregulates hepcidin, and reduces TGF-beta2-mediated increase in ferritin and ROS.	Heparin	0-7	transforming growth factor beta 2	Bos taurus	44-53
32107314-6	2020	Both cell types expressed increased levels of pro-inflammatory markers - inducible nitric oxide synthase (iNOS), and tumor necrosis factor-alpha (TNF-alpha)- when cultured under hyperglycemic stress, which was inhibited by heparin.	Heparin	223-230	tumor necrosis factor	Rattus norvegicus	146-155
32107314-9	2020	Of note, heparin increased the anti-inflammatory markers arginase 1 (ARG1) and interleukin-10 (IL-10) in murine BMDMs.	Heparin	9-16	interleukin 10	Mus musculus	79-93
32107314-9	2020	Of note, heparin increased the anti-inflammatory markers arginase 1 (ARG1) and interleukin-10 (IL-10) in murine BMDMs.	Heparin	9-16	interleukin 10	Mus musculus	95-100
32091872-0	2020	Fibrin Glue/Fibronectin/Heparin-Based Delivery System of BMP2 Induces Osteogenesis in MC3T3-E1 Cells and Bone Formation in Rat Calvarial Critical-Sized Defects.	Heparin	24-31	bone morphogenetic protein 2	Mus musculus	57-61
32091872-3	2020	In this study, an innovative and efficient fibrin glue/fibronectin/heparin (FG/Fn/Hep)-based delivery system was developed for controlled release of BMP2.	Heparin	67-74	bone morphogenetic protein 2	Mus musculus	149-153
32091872-4	2020	The incorporation of heparin can significantly slow the release of BMP2 without substantially affecting the structure and stiffness of the FG/Fn.	Heparin	21-28	bone morphogenetic protein 2	Mus musculus	67-71
32182331-11	2020	Notably, both heparin and N-acetyl carnosine reduce TGF-beta2-mediated reciprocal upregulation of TGF-beta2.	Heparin	14-21	transforming growth factor beta 2	Bos taurus	98-107
32077913-1	2020	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder mediated by complexes between platelet factor 4 (PF4) and heparin or other polyanions, but the risk of thrombosis extends beyond exposure to heparin implicating other PF4 partners.	Heparin	0-7	platelet factor 4	Mus musculus	116-119
32077913-1	2020	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder mediated by complexes between platelet factor 4 (PF4) and heparin or other polyanions, but the risk of thrombosis extends beyond exposure to heparin implicating other PF4 partners.	Heparin	0-7	platelet factor 4	Mus musculus	234-237
32077913-1	2020	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder mediated by complexes between platelet factor 4 (PF4) and heparin or other polyanions, but the risk of thrombosis extends beyond exposure to heparin implicating other PF4 partners.	Heparin	208-215	platelet factor 4	Mus musculus	116-119
32289862-5	2020	Analysis of a series of megakaryocytic differentiation-related heparin-binding proteins (HBPs) in the cell culture medium revealed an exclusive positive correlation between the level of interleukin 6 (IL-6) and HPSE expression.	Heparin	63-70	interleukin 6	Homo sapiens	186-199
32289862-5	2020	Analysis of a series of megakaryocytic differentiation-related heparin-binding proteins (HBPs) in the cell culture medium revealed an exclusive positive correlation between the level of interleukin 6 (IL-6) and HPSE expression.	Heparin	63-70	interleukin 6	Homo sapiens	201-205
32289862-5	2020	Analysis of a series of megakaryocytic differentiation-related heparin-binding proteins (HBPs) in the cell culture medium revealed an exclusive positive correlation between the level of interleukin 6 (IL-6) and HPSE expression.	Heparin	63-70	heparanase	Homo sapiens	211-215
31998886-6	2020	Further, heparin and the heparin-binding angiogenic factors VEGF, FGF-2 and CXCL12 were immobilized onto the peptide in a modular assembly.	Heparin	25-32	vascular endothelial growth factor A	Homo sapiens	60-64
31998886-8	2020	In subsequent investigations, peptide-heparin-complexes loaded with CXCL12 or VEGF had an additional increasing effect on cell viability, differentiation and migration.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	78-82
32182331-11	2020	Notably, both heparin and N-acetyl carnosine reduce TGF-beta2-mediated reciprocal upregulation of TGF-beta2.	Heparin	14-21	transforming growth factor beta 2	Bos taurus	52-61
31794784-12	2020	This paper summarizes research progress on the IFN-gamma signalling pathway, heparin interference with IFN-gamma activity and the structure-activity relationship between heparin and IFN-gamma.	Heparin	77-84	interferon gamma	Homo sapiens	103-112
31794784-12	2020	This paper summarizes research progress on the IFN-gamma signalling pathway, heparin interference with IFN-gamma activity and the structure-activity relationship between heparin and IFN-gamma.	Heparin	77-84	interferon gamma	Homo sapiens	103-112
31794784-0	2020	The role of heparin/heparan sulphate in the IFN-gamma-led Arena.	Heparin	12-19	interferon gamma	Homo sapiens	44-53
31794784-7	2020	The structural similarity provides a basis for modelling exogenous heparin dependence for interference with IFN-gamma function.	Heparin	67-74	interferon gamma	Homo sapiens	108-117
32024165-3	2020	Presence of heparin into the structure can significantly increase the encapsulation efficiency up to 95% and lower the release rate of encapsulated VEGF.	Heparin	12-19	vascular endothelial growth factor A	Homo sapiens	148-152
31794784-9	2020	Second, the principle of priority occupancy; heparin can occupy the receptor binding site on cytokines, partially preventing the IFN-gamma-IFN-gammaR interaction.	Heparin	45-52	interferon gamma	Homo sapiens	129-138
31794784-11	2020	To decipher the mechanism by which heparin influences IFN-gamma activity, studies of the structure-activity relationship are in progress.	Heparin	35-42	interferon gamma	Homo sapiens	54-63
31843715-4	2020	An injectable, self-assembling peptide/heparin (SAP/Hep) hydrogel was used to co-deliver TNF-alpha neutralizing antibody (anti-TNF-alpha) and hepatocyte growth factor (HGF).	Heparin	39-46	SH2 domain containing 1A	Mus musculus	48-51
31843715-4	2020	An injectable, self-assembling peptide/heparin (SAP/Hep) hydrogel was used to co-deliver TNF-alpha neutralizing antibody (anti-TNF-alpha) and hepatocyte growth factor (HGF).	Heparin	39-46	tumor necrosis factor	Mus musculus	89-98
31843715-4	2020	An injectable, self-assembling peptide/heparin (SAP/Hep) hydrogel was used to co-deliver TNF-alpha neutralizing antibody (anti-TNF-alpha) and hepatocyte growth factor (HGF).	Heparin	39-46	tumor necrosis factor	Mus musculus	127-136
31444563-5	2020	There was a significant correlation between delta whole blood passage time {(heparin tube) - (EDTA-2Na + heparin)} and serum levels of myeloperoxidase and adhesive leukocyte number, respectively, even in blood from patients with DM or ACS, who suffered from inflammation.	Heparin	77-84	myeloperoxidase	Homo sapiens	135-150
31444563-5	2020	There was a significant correlation between delta whole blood passage time {(heparin tube) - (EDTA-2Na + heparin)} and serum levels of myeloperoxidase and adhesive leukocyte number, respectively, even in blood from patients with DM or ACS, who suffered from inflammation.	Heparin	105-112	myeloperoxidase	Homo sapiens	135-150
31846202-10	2020	We also found a biological impact on the results in case of hemolyzed sample: Fibrinogen was decreased when the hemoglobin level was superior to 1.8 g/L, PT was prolonged beyond 5 g/L, and aPTT was shortened beyond 1.5 g/L hemoglobin concentration, especially in patients treated with heparin.	Heparin	285-292	fibrinogen beta chain	Homo sapiens	78-88
31606923-2	2020	Binding VEGF with heparin could protect it from rapid degradation, subsequently allowing it to be controlled release.	Heparin	18-25	vascular endothelial growth factor A	Homo sapiens	8-12
31801970-1	2020	Midkine is a heparin-binding growth factor, originally reported as the product of a retinoic acid-responsive gene during embryogenesis, but currently viewed as a multifaceted factor contributing to both normal tissue homeostasis and disease development.	Heparin	13-20	midkine	Homo sapiens	0-7
32000579-6	2020	Cleaved osteopontin was higher in plasma from patients with aortic stenosis receiving crystalloid compared with blood cardioplegia, likely because of less heparin-induced inhibition of thrombin.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	185-193
31559512-1	2020	The parenterally administered direct thrombin inhibitors (DTIs) argatroban and bivalirudin are effective anticoagulants for acute heparin-induced thrombocytopenia (HIT) treatment.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	37-45
31749252-0	2020	Bivalirudin during thrombolysis with catheter-directed tPA in a heparin-refractory patient: A case report.	Heparin	64-71	plasminogen activator, tissue type	Homo sapiens	55-58
31471127-0	2020	From unfractionated heparin to pentasaccharide: Paradigm of rigorous science growing in the understanding of the in vivo thrombin generation.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	121-129
32274706-1	2020	Heparanase was discovered during a study of the heparin proteoglycan (serglycin) in mast cells.	Heparin	48-55	heparanase	Homo sapiens	0-10
32274706-7	2020	More unexpectedly, heparanase also influences heparan sulfate biosynthesis, such that overexpression of the enzyme results in generation of highly sulfated, heparin-like oligosaccharides.	Heparin	157-164	heparanase	Homo sapiens	19-29
32274717-1	2020	Heparanase is upregulated in various tumors, and its expression is closely associated with tumor growth, angiogenesis and metastasis, which accomplishes this mainly through degrading heparan sulfate and releasing heparin-binding growth factors thereby influencing multiple signaling pathways.	Heparin	213-220	heparanase	Homo sapiens	0-10
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	nuclear receptor subfamily 4 group A member 1	Homo sapiens	0-5
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	nuclear receptor subfamily 4 group A member 1	Homo sapiens	224-230
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	interleukin 1 beta	Homo sapiens	458-477
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	hypoxia inducible factor 1 subunit alpha	Homo sapiens	587-597
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	hypoxia inducible factor 1 subunit alpha	Homo sapiens	599-630
31915322-1	2020	BACKGROUND: Midkine (MK), a heparin-binding protein, participates in multiple cellular processes, such as immunity, cellular growth and apoptosis.	Heparin	28-35	midkine	Homo sapiens	12-19
31915322-1	2020	BACKGROUND: Midkine (MK), a heparin-binding protein, participates in multiple cellular processes, such as immunity, cellular growth and apoptosis.	Heparin	28-35	midkine	Homo sapiens	21-23
31979118-6	2020	The highest affinity interaction was with the 30-kDa (heparin-binding) FN fragment, which also showed the greatest colocalization in cells and accommodated both HSP90 and heparin in the complex.	Heparin	54-61	fibronectin 1	Homo sapiens	71-73
31979118-6	2020	The highest affinity interaction was with the 30-kDa (heparin-binding) FN fragment, which also showed the greatest colocalization in cells and accommodated both HSP90 and heparin in the complex.	Heparin	171-178	fibronectin 1	Homo sapiens	71-73
32306365-4	2020	This chapter describes three protocols that measure the Ca2+-dependent activities using recombinant annexins: solid-phase heparin-binding assay using bovine serum albumin-conjugated heparin, solid-phase phosphatidylserine-binding assay, and plasma coagulation inhibition assay.	Heparin	122-129	albumin	Homo sapiens	157-170
31634770-3	2020	In contrast, midkine (MK), a heparin-binding growth factor and cytokine, which induces carcinogenesis and chemoresistance, promotes the development and progression of many malignant tumours by increasing diverse cell functions such as cell proliferation, cell survival and antiapoptotic activities via mainly the activation of phosphatidyl inositol 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) pathways.	Heparin	29-36	midkine	Homo sapiens	13-20
31634770-3	2020	In contrast, midkine (MK), a heparin-binding growth factor and cytokine, which induces carcinogenesis and chemoresistance, promotes the development and progression of many malignant tumours by increasing diverse cell functions such as cell proliferation, cell survival and antiapoptotic activities via mainly the activation of phosphatidyl inositol 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) pathways.	Heparin	29-36	midkine	Homo sapiens	22-24
33030036-0	2020	Comparative Anticoagulant and Thrombin Generation Inhibitory Profile of Heparin, Sulodexide and Its Components.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	30-38
33030036-10	2020	In the thrombin generation assay, FMH and UFH produced comparable inhibition of thrombin generation as measured by various parameters.	Heparin	42-45	coagulation factor II, thrombin	Homo sapiens	80-88
31785466-3	2020	Heparanase is a heparin sulfate degrading endoglycosidase that has an important role in various biological processes and is a key component of extracellular matrix.	Heparin	16-23	heparanase	Homo sapiens	0-10
32306365-4	2020	This chapter describes three protocols that measure the Ca2+-dependent activities using recombinant annexins: solid-phase heparin-binding assay using bovine serum albumin-conjugated heparin, solid-phase phosphatidylserine-binding assay, and plasma coagulation inhibition assay.	Heparin	182-189	albumin	Homo sapiens	157-170
31921844-2	2019	Using heparan sulfates (HS)/heparin as a cofactor, FGF2 binds to FGF receptor (FGFR) and induces downstream signaling pathways, such as ERK pathway, that regulate cellular behavior.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	51-55
31881749-4	2019	Thrombin aptamers such as NU172 might be used during extracorporeal circulation (ECC) in combination with a reduced heparin concentration or for patients with heparin-induced thrombocytopenia (HIT).	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	0-8
31881749-4	2019	Thrombin aptamers such as NU172 might be used during extracorporeal circulation (ECC) in combination with a reduced heparin concentration or for patients with heparin-induced thrombocytopenia (HIT).	Heparin	159-166	coagulation factor II, thrombin	Homo sapiens	0-8
31921844-8	2019	FGF2-STABs showed higher efficiency in induction of FGFR-mediated proliferation, lower affinity to heparin and were less dependent on heparin than wild-type FGF2 (FGF2-wt) for induction of FGFR-mediated mitogenic response.	Heparin	99-106	fibroblast growth factor 2	Homo sapiens	0-4
31921844-0	2019	Fibroblast Growth Factor 2 Protein Stability Provides Decreased Dependence on Heparin for Induction of FGFR Signaling and Alters ERK Signaling Dynamics.	Heparin	78-85	fibroblast growth factor 2	Homo sapiens	0-26
31921844-8	2019	FGF2-STABs showed higher efficiency in induction of FGFR-mediated proliferation, lower affinity to heparin and were less dependent on heparin than wild-type FGF2 (FGF2-wt) for induction of FGFR-mediated mitogenic response.	Heparin	134-141	fibroblast growth factor 2	Homo sapiens	0-4
31642823-5	2019	The specific binding of HSPG with bFGF protein was demonstrated, which was about 6-fold stronger than the binding of bFGF with heparin.	Heparin	127-134	syndecan 2	Rattus norvegicus	24-28
31797980-1	2019	Heparin is a widely used anticoagulant which inhibits factor Xa and thrombin through potentiation of antithrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	68-76
31568878-3	2019	PAMSPF was able to condense DNA and encapsulate RG7388 to form spherical nanoparticles (PAMSPF/p53/RG) with particle sizes of around 200 nm, and remain stable in the presence of heparin and nuclease.	Heparin	178-185	tumor protein p53	Homo sapiens	95-98
31642823-7	2019	Our results indicate that HSPG has potential clinical utility as a delivery agent for heparin-binding growth factors.	Heparin	86-93	syndecan 2	Rattus norvegicus	26-30
30879129-9	2019	Heparin induced nuclear accumulation of the forkhead transcription factor FOXO1 and expression of its downstream target, the ROS scavenger superoxide dismutase 2.	Heparin	0-7	forkhead box O1	Homo sapiens	74-79
31587337-1	2019	BACKGROUND: Bivalirudin, a direct thrombin inhibitor, is a treatment option for the management of heparin-induced thrombocytopenia (HIT) and other coagulation disorders.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	34-42
31536840-0	2019	An injectable heparin-conjugated hyaluronan scaffold for local delivery of Transforming Growth Factor beta1 promotes successful chondrogenesis.	Heparin	14-21	transforming growth factor beta 1	Homo sapiens	75-107
31582210-1	2019	We examined whether chondroitin sulfates (CSs) exert inhibitory effects on heparanase (Hpse), the sole endoglycosidase that cleaves heparan sulfate (HS) and heparin, which also stimulates chemokine production.	Heparin	157-164	heparanase	Mus musculus	75-85
31601651-6	2019	We observed that Avastin slightly enhanced VEGF binding to heparin and that heparin increased VEGF binding to Avastin.	Heparin	59-66	vascular endothelial growth factor A	Homo sapiens	43-47
31601651-6	2019	We observed that Avastin slightly enhanced VEGF binding to heparin and that heparin increased VEGF binding to Avastin.	Heparin	76-83	vascular endothelial growth factor A	Homo sapiens	94-98
31601651-9	2019	Interestingly, the reduced Avastin-VEGF binding at acidic pH was rescued by heparin, as was Avastin"s ability to inhibit VEGF binding to cells.	Heparin	76-83	vascular endothelial growth factor A	Homo sapiens	35-39
31803745-4	2019	Consequently, the therapeutic potency of a heparin is determined by its aIIa activity, i.e., the concentration of a domain in which 12 sugar flank the high affinity antithrombin-binding pentasaccharide (HA5) at one side.	Heparin	43-50	keratin 35	Homo sapiens	203-206
31536840-6	2019	We show that heparin, a GAG known to bind a wide range of GFs, covalently conjugated to a hyaluronan hydrogel, leads to a sustained release of TGF-beta1.	Heparin	13-20	transforming growth factor beta 1	Homo sapiens	143-152
31536840-7	2019	Using this heparin-conjugated hyaluronan hydrogel, 0.25 to 50 ng TGF-beta1 per scaffold was loaded and cell viability, proliferation and cartilaginous matrix deposition of the encapsulated chondroprogenitor cells were measured.	Heparin	11-18	transforming growth factor beta 1	Homo sapiens	65-74
31536840-13	2019	Here we show development of an injectable hyaluronan hydrogel, which achieves a sustained release of TGF-beta1 due to covalent conjugation of heparin.	Heparin	142-149	transforming growth factor beta 1	Homo sapiens	101-110
31781622-4	2019	In this study, based on the structure and function of extracellular matrix on vascular injury healing, a novel fibronectin-loaded poly-l-lysine/heparin nanoparticles was constructed for stent surface modification.	Heparin	144-151	fibronectin 1	Homo sapiens	111-122
31471526-6	2019	Adoptively transferred Treg cells prevented spontaneous production of PF4/heparin-specific Abs in Foxp3-deficient mice and inhibited PF4/heparin complex-induced production of PF4/heparin-specific IgGs in wild-type mice.	Heparin	137-144	platelet factor 4	Mus musculus	133-136
31671632-5	2019	Results demonstrate that attenuation of PDGF-induced intracellular calcium release by the fibronectin matrix mimetic, FNIII1H,8-10 requires alpha5beta1 integrin ligation, but is not dependent upon the matricryptic, heparin-binding site of FNIII1.	Heparin	215-222	fibronectin 1	Homo sapiens	90-101
31645190-1	2021	BACKGROUND: Argatroban and bivalirudin are direct thrombin inhibitors (DTIs) used for the treatment of heparin-induced thrombocytopenia (HIT).	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	50-58
31420170-3	2019	Using a wide range of biophysical and biochemical techniques, we demonstrate that reversal of charge on a well-conserved positively charged amino acid, R136, in the heparin binding pocket drastically increases the resistance to proteases, thermal stability, and cell proliferation activity of the human acidic fibroblast growth factor (hFGF1).	Heparin	165-172	fibroblast growth factor 1	Homo sapiens	336-341
31420170-7	2019	Isothermal titration calorimetry data show that the R136E mutation markedly decreases the heparin binding affinity of hFGF1.	Heparin	90-97	fibroblast growth factor 1	Homo sapiens	118-123
31578149-4	2019	Herein, a heparin-immobilized fibroin hydrogel was fabricated to deliver FGF1 (human acidic fibroblast growth factor 1) on top of wound in rats with full-thickness skin excision by performing comprehensive preclinical studies to fully evaluate its safety and effectiveness.	Heparin	10-17	fibroblast growth factor 1	Homo sapiens	73-77
31471526-6	2019	Adoptively transferred Treg cells prevented spontaneous production of PF4/heparin-specific Abs in Foxp3-deficient mice and inhibited PF4/heparin complex-induced production of PF4/heparin-specific IgGs in wild-type mice.	Heparin	74-81	platelet factor 4	Mus musculus	70-73
31673058-2	2019	Since the bioactive form of several cytokines is represented by dimers/oligomers and oligomerization is promoted by binding to heparin or HSPGs, here we evaluated if heparin/HSPGs also promote p17 oligomerization.	Heparin	166-173	family with sequence similarity 72 member B	Homo sapiens	193-196
31673058-4	2019	Heparin-induced p17 oligomerization is of electrostatic nature, being it prevented by NaCl, by removing negative sulfated groups of heparin and by neutralizing positive lysine residues in the p17 N-terminus.	Heparin	132-139	family with sequence similarity 72 member B	Homo sapiens	16-19
31673058-5	2019	A new computational protocol has been implemented to study heparin chains up to 24-mer accommodating a p17 dimer.	Heparin	59-66	family with sequence similarity 72 member B	Homo sapiens	103-106
31673058-6	2019	Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization.	Heparin	49-56	family with sequence similarity 72 member B	Homo sapiens	62-65
31673058-6	2019	Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization.	Heparin	49-56	family with sequence similarity 72 member B	Homo sapiens	208-211
31673058-6	2019	Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization.	Heparin	170-177	family with sequence similarity 72 member B	Homo sapiens	62-65
31673058-6	2019	Molecular dynamics show that, in the presence of heparin, two p17 molecules undergo conformational modifications creating a continuous "electropositive channel" in which heparin sulfated groups interact with p17 basic amino acids, promoting its dimerization.	Heparin	170-177	family with sequence similarity 72 member B	Homo sapiens	208-211
31449398-5	2019	THP-1-derived macrophages were used to study short-term anti-inflammatory activity (time scale 48 h), showing that PEM that contained heparin reduced cell adhesion and IL1-beta secretion, when compared to those with polystyrenesulfonate, used as alternative polyanion in multilayer formation.	Heparin	134-141	GLI family zinc finger 2	Homo sapiens	0-5
31449398-5	2019	THP-1-derived macrophages were used to study short-term anti-inflammatory activity (time scale 48 h), showing that PEM that contained heparin reduced cell adhesion and IL1-beta secretion, when compared to those with polystyrenesulfonate, used as alternative polyanion in multilayer formation.	Heparin	134-141	interleukin 1 beta	Homo sapiens	168-176
31471526-6	2019	Adoptively transferred Treg cells prevented spontaneous production of PF4/heparin-specific Abs in Foxp3-deficient mice and inhibited PF4/heparin complex-induced production of PF4/heparin-specific IgGs in wild-type mice.	Heparin	137-144	platelet factor 4	Mus musculus	133-136
31471526-9	2019	Moreover, bone marrow chimeric mice with CD4 T cell-specific deletion of IL-10 increased PF4/heparin-specific IgG production upon PF4/heparin complex challenge.	Heparin	93-100	interleukin 10	Mus musculus	73-78
31471526-9	2019	Moreover, bone marrow chimeric mice with CD4 T cell-specific deletion of IL-10 increased PF4/heparin-specific IgG production upon PF4/heparin complex challenge.	Heparin	93-100	platelet factor 4	Mus musculus	89-92
31471526-9	2019	Moreover, bone marrow chimeric mice with CD4 T cell-specific deletion of IL-10 increased PF4/heparin-specific IgG production upon PF4/heparin complex challenge.	Heparin	93-100	platelet factor 4	Mus musculus	130-133
31471526-9	2019	Moreover, bone marrow chimeric mice with CD4 T cell-specific deletion of IL-10 increased PF4/heparin-specific IgG production upon PF4/heparin complex challenge.	Heparin	134-141	interleukin 10	Mus musculus	73-78
31471526-9	2019	Moreover, bone marrow chimeric mice with CD4 T cell-specific deletion of IL-10 increased PF4/heparin-specific IgG production upon PF4/heparin complex challenge.	Heparin	134-141	platelet factor 4	Mus musculus	89-92
31771729-10	2019	Fluorescence microscopy observation showed that LPS stimulation could promote the adhesion of THP-1 to HUVEC; heparin preconditioning could inhibit the adhesion of THP-1 to HUVEC stimulated by LPS.	Heparin	110-117	GLI family zinc finger 2	Homo sapiens	164-169
31771729-11	2019	CONCLUSIONS: Heparin preconditioning could inhibit the MCP-1 mRNA expression , thereby reduce the adhesion of THP-1 to HUVEC, thus play a protective role in sepsis.	Heparin	13-20	GLI family zinc finger 2	Homo sapiens	110-115
31527216-0	2019	A catastrophic antiphospholipid syndrome complicated with heparin-induced thrombocytopaenia, successfully managed with double filtration plasmapheresis, steroids and a direct thrombin inhibitor.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	175-183
30824278-3	2019	OBJECTIVE: To assess the effectiveness of TNF-alpha blockers in 18 aPL-positive women with recurrent infertility after therapy with low-molecular-weight heparin (LMWH) plus aspirin (LDA) plus hydroxychloroquine (HCQ).	Heparin	153-160	tumor necrosis factor	Homo sapiens	42-51
31527216-5	2019	Heparin-induced thrombocytopaenia was managed by administration of argatroban, a direct thrombin inhibitor with an increase in platelet count.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	88-96
31215255-1	2019	Objective: Heparanase (HPA) is an endo-beta-D-glucuronidase capable of degrading heparin sulphate (HS) and heparin side chains.	Heparin	107-114	heparanase	Homo sapiens	11-21
31284097-3	2019	Vascular endothelial growth factor (VEGF) was further conjugated to the immobilized heparin.	Heparin	84-91	vascular endothelial growth factor A	Homo sapiens	0-34
31284097-3	2019	Vascular endothelial growth factor (VEGF) was further conjugated to the immobilized heparin.	Heparin	84-91	vascular endothelial growth factor A	Homo sapiens	36-40
33654855-3	2019	We reasoned that a simpler heparanase assay could be developed using heparin labeled with Dabcyl and EDANS as donor and acceptor fluorophores so as to generate a FRET signal.	Heparin	69-76	heparanase	Homo sapiens	27-37
33654855-4	2019	Our results show that a more robust heparanase assay could be developed based on the principle studied herein and more homogeneous preparation of heparin.	Heparin	146-153	heparanase	Homo sapiens	36-46
31302300-5	2019	The HA hydrogels are complexed with heparin to achieve sustained presentation and controlled release of bone morphogenetic protein 6 (BMP-6).	Heparin	36-43	bone morphogenetic protein 6	Homo sapiens	104-132
31302300-5	2019	The HA hydrogels are complexed with heparin to achieve sustained presentation and controlled release of bone morphogenetic protein 6 (BMP-6).	Heparin	36-43	bone morphogenetic protein 6	Homo sapiens	134-139
31302300-7	2019	Using quartz crystal microbalance and enzyme-linked immunosorbent assay, we measured an initial surface density of 400 ng BMP6/cm2, corresponding to two BMP-6 per heparin molecule, with 50% release within two weeks.	Heparin	163-170	bone morphogenetic protein 6	Homo sapiens	122-126
31302300-13	2019	Here we present hydrogels which mimic the physico-chemical properties of the bone marrow, consisting of hyaluronic acid with crosslinked heparin for the controlled presentation of bioactive BMP-6.	Heparin	137-144	bone morphogenetic protein 6	Homo sapiens	190-195
31215255-1	2019	Objective: Heparanase (HPA) is an endo-beta-D-glucuronidase capable of degrading heparin sulphate (HS) and heparin side chains.	Heparin	107-114	heparanase	Homo sapiens	23-26
31166803-3	2019	The present study investigates the effect of thermosensitive heparin-poloxamer (HP) hydrogel-encapsulated recombinant human fibroblast growth factor 21 (rhFGF21) on wound healing in mice with streptozotocin-induced diabetes mellitus.	Heparin	61-68	fibroblast growth factor 21	Homo sapiens	124-151
31215255-1	2019	Objective: Heparanase (HPA) is an endo-beta-D-glucuronidase capable of degrading heparin sulphate (HS) and heparin side chains.	Heparin	81-88	heparanase	Homo sapiens	11-21
31215255-1	2019	Objective: Heparanase (HPA) is an endo-beta-D-glucuronidase capable of degrading heparin sulphate (HS) and heparin side chains.	Heparin	81-88	heparanase	Homo sapiens	23-26
31322172-4	2019	By contrast, treatment with heparin, an inositol 1,4,5-triphosphate receptor inhibitor, remarkably attenuated cytotoxicity and decreased the intracellular level of Ca2+, the apoptosis rate and the expression levels of GRP78, CHOP and Caspases.	Heparin	28-35	heat shock protein family A (Hsp70) member 5	Homo sapiens	218-223
31002379-3	2019	Then, high-dose LL37 (10 mumol L-1 ) was bound to varying concentrations of three GAGs, heparin, chondroitin sulphate and hyaluronic acid, and their cytotoxic effects on hDPCs and antimicrobial effects were evaluated and compared.	Heparin	88-95	cathelicidin antimicrobial peptide	Homo sapiens	16-20
31002379-4	2019	Furthermore, the LPS-neutralizing ability of heparin (5 mug mL-1 )-LL37 (10 mumol L-1 ) complexes, which were found to be less cytotoxic for hDPCs with undiminished antimicrobial ability, was investigated.	Heparin	45-52	cathelicidin antimicrobial peptide	Homo sapiens	67-71
31002379-8	2019	LL37 (10 mumol L-1 ) binding to heparin within a limited concentration range (2~6 mug mL-1 ) eliminated the cytotoxicity for hDPCs (P &lt; 0.01) whilst exerting potent antimicrobial effects against Streptococcus mutans, Streptococcus sobrinus, Streptococcus salivarius, Aggegatibacter actinomycetemcomitans and Escherichia coli.	Heparin	32-39	cathelicidin antimicrobial peptide	Homo sapiens	0-4
31125187-6	2019	RESULTS AND CONCLUSIONS: Plasma FXI increased 5- to 10-fold in wild-type mice after infusion of heparin, polyphosphates, protamine, or GAG-digesting enzymes, but not saline.	Heparin	96-103	coagulation factor XI	Mus musculus	32-35
31322172-4	2019	By contrast, treatment with heparin, an inositol 1,4,5-triphosphate receptor inhibitor, remarkably attenuated cytotoxicity and decreased the intracellular level of Ca2+, the apoptosis rate and the expression levels of GRP78, CHOP and Caspases.	Heparin	28-35	DNA damage inducible transcript 3	Homo sapiens	225-229
31508535-5	2019	Conclusions: Previous in vitro and in vivo studies have reported that the Fc portion of anti-VEGF drugs activates platelets with heparin.	Heparin	129-136	vascular endothelial growth factor A	Homo sapiens	93-97
31508535-6	2019	Therefore, careful anti-VEGF drug selection may be necessary in cases with concomitant heparin treatment.	Heparin	87-94	vascular endothelial growth factor A	Homo sapiens	24-28
31405005-2	2019	To reduce the dose of BMP-2, complexation with heparin is a promising approach, because heparin enhances the osteoinductivity of BMP-2.	Heparin	47-54	bone morphogenetic protein 2	Mus musculus	22-27
31434430-16	2019	Conclusion: Higher dosage of heparin is required during AF ablation to achieve the satisfactory anticoagulant intensity for AF patients under dabigatran etexilate (110 mg, Bid), low-molecular-weight heparin and rivaroxaban (20 mg, Qd) anticoagulation therapy before AF ablation.	Heparin	29-36	BH3 interacting domain death agonist	Homo sapiens	172-175
31405005-2	2019	To reduce the dose of BMP-2, complexation with heparin is a promising approach, because heparin enhances the osteoinductivity of BMP-2.	Heparin	47-54	bone morphogenetic protein 2	Mus musculus	129-134
31405005-2	2019	To reduce the dose of BMP-2, complexation with heparin is a promising approach, because heparin enhances the osteoinductivity of BMP-2.	Heparin	88-95	bone morphogenetic protein 2	Mus musculus	22-27
31405005-2	2019	To reduce the dose of BMP-2, complexation with heparin is a promising approach, because heparin enhances the osteoinductivity of BMP-2.	Heparin	88-95	bone morphogenetic protein 2	Mus musculus	129-134
31472056-7	2019	In addition to above  mechanisms, possibly  the infused protamine binds heparin and causes the coagulation cascade to activate heparin-AT complex on thrombin beside activating FXIa, FXa and FIXa and causing the re-use of Ca2+.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	149-157
31271519-5	2019	Therefore, we analyzed the interactions of FGF1 and FGF2 with four sulfated polysaccharides: heparin, dextran sulfate (DXS), lambda-carrageenan, and chondroitin sulfate.	Heparin	93-100	fibroblast growth factor 1	Homo sapiens	43-47
30561017-4	2019	Heparin can influence the catalytic properties of chymase.	Heparin	0-7	chymase 1	Homo sapiens	50-57
30561017-14	2019	Immunofluorescence staining positivity of fibrin in vasculitis cryosections decreased after pretreatment with rh-chymase for 24 h, and heparin enhanced this effect.	Heparin	135-142	chymase 1	Homo sapiens	113-120
31033049-9	2019	We found that a positive feedback loop of heparin-binding epidermal growth factor-like growth factor (HBEGF) and epidermal growth factor receptor (EGFR) signaling regulates astrocytes maturation.	Heparin	42-49	epidermal growth factor receptor	Homo sapiens	147-151
31472056-7	2019	In addition to above  mechanisms, possibly  the infused protamine binds heparin and causes the coagulation cascade to activate heparin-AT complex on thrombin beside activating FXIa, FXa and FIXa and causing the re-use of Ca2+.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	149-157
30907752-1	2019	Bivalirudin is a direct thrombin inhibitor that is used as a procedural anticoagulant during percutaneous coronary interventions and cardiac surgery for patients with heparin-resistant thrombosis or heparin-induced thrombocytopenia.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	24-32
30667535-3	2019	In this study, for the first time, microsecond-scale MD simulations are reported for a complex between fibroblast growth factor 1 and heparin.	Heparin	134-141	fibroblast growth factor 1	Homo sapiens	103-129
30667535-7	2019	Our data provide novel significant insights into the interactions in the fibroblast growth factor 1 complex with heparin, in particular, and into the physical-chemical nature of protein-glycosaminoglycan systems in general, which have potential applicability for biomaterials development in the area of regenerative medicine.	Heparin	113-120	fibroblast growth factor 1	Homo sapiens	73-99
31441407-0	2019	[Effect of unfractionated heparin on high mobility group box 1-mediated expression of vascular endothelial cadherin].	Heparin	26-33	cadherin 5	Homo sapiens	86-115
30793294-0	2019	Effect of heparin thromboprophylaxis on thrombin generation in multiple myeloma patients.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	40-48
30565254-9	2019	BMP-2 and OC mRNA expressions were significantly higher in cells exposed to heparin than control group after 1 day (P &lt; 0.05).	Heparin	76-83	bone gamma-carboxyglutamate protein	Homo sapiens	10-12
33405584-2	2019	In this study, multilayers of heparin and collagen (HEP/COL) were used as a bioactive surface coating to enhance human MSC (hMSC) response to soluble interferon-gamma (IFN-gamma).	Heparin	30-37	interferon gamma	Homo sapiens	150-166
33405584-2	2019	In this study, multilayers of heparin and collagen (HEP/COL) were used as a bioactive surface coating to enhance human MSC (hMSC) response to soluble interferon-gamma (IFN-gamma).	Heparin	30-37	interferon gamma	Homo sapiens	168-177
30928673-3	2019	The majority of extracellularLPAis produced locally by the secreted lysophospholipase D, autotaxin (ATX), through its binding to various beta integrins or heparin sulfate on cell surface and hydrolyzing various lysophospholipids.	Heparin	155-162	ectonucleotide pyrophosphatase/phosphodiesterase 2	Homo sapiens	89-98
30928673-3	2019	The majority of extracellularLPAis produced locally by the secreted lysophospholipase D, autotaxin (ATX), through its binding to various beta integrins or heparin sulfate on cell surface and hydrolyzing various lysophospholipids.	Heparin	155-162	ectonucleotide pyrophosphatase/phosphodiesterase 2	Homo sapiens	100-103
30869126-0	2019	Recombinant dermatan sulfate is a potent activator of heparin cofactor II-dependent inhibition of thrombin.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	98-106
30869126-1	2019	The glycosaminoglycan dermatan sulfate (DS) is a well-known activator of heparin cofactor II-dependent inactivation of thrombin.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	119-127
30869126-5	2019	Importantly, the recombinant highly 2,4-O-sulfated DS inhibits thrombin via heparin cofactor II, approximately 20 times better than heparin, enabling manipulation of vascular and extravascular coagulation.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	63-71
30565254-7	2019	After 3 days, heparin had significantly higher ALP activity in comparison with the control (P &lt; 0.05).	Heparin	14-21	alkaline phosphatase, placental	Homo sapiens	47-50
30565254-10	2019	CONCLUSIONS: Heparin was biocompatible in hDPCs, induced osteogenic bioactivity and enhanced mRNA expression of osteo/odontogenic markers BMP-2 and OC.	Heparin	13-20	bone gamma-carboxyglutamate protein	Homo sapiens	148-150
31294321-1	2019	Background: Low-molecular-weight heparin has been the preferred treatment of cancer-associated thrombosis (CAT); however, emerging data support the use of direct oral anticoagulants (DOACs).	Heparin	33-40	catalase	Homo sapiens	77-112
30771687-10	2019	UFH also protected TJs against lipopolysaccharide-stimulated damage and functioned upstream by inhibiting the ERK1/2 MAPK pathway to attenuate endothelial hyperpermeability and downregulating the expression of TJ proteins such as claudin-5, occludin, and ZO-1.	Heparin	0-3	mitogen-activated protein kinase 3	Homo sapiens	110-116
30771687-10	2019	UFH also protected TJs against lipopolysaccharide-stimulated damage and functioned upstream by inhibiting the ERK1/2 MAPK pathway to attenuate endothelial hyperpermeability and downregulating the expression of TJ proteins such as claudin-5, occludin, and ZO-1.	Heparin	0-3	mitogen-activated protein kinase 3	Homo sapiens	117-121
31100859-2	2019	The glycosaminoglycan heparin, widely used as a clinical anticoagulant, has previously been shown to inhibit the Alzheimer"s disease-relevant beta-secretase 1 (BACE1).	Heparin	22-29	beta-secretase 1	Homo sapiens	160-165
31239595-0	2019	Fibrinogen levels measured by the dry hematology method are lower than those measured by the Clauss method under a high concentration of heparin.	Heparin	137-144	fibrinogen beta chain	Homo sapiens	0-10
30852423-4	2019	Our studies show that a hyaluronan and heparin-based hydrogel system locally delivers IL-10 by capitalizing on the ability of heparin to reversibly bind IL-10 without bleeding or other complications.	Heparin	39-46	interleukin 10	Mus musculus	86-91
30852423-4	2019	Our studies show that a hyaluronan and heparin-based hydrogel system locally delivers IL-10 by capitalizing on the ability of heparin to reversibly bind IL-10 without bleeding or other complications.	Heparin	39-46	interleukin 10	Mus musculus	153-158
30852423-4	2019	Our studies show that a hyaluronan and heparin-based hydrogel system locally delivers IL-10 by capitalizing on the ability of heparin to reversibly bind IL-10 without bleeding or other complications.	Heparin	126-133	interleukin 10	Mus musculus	86-91
30852423-4	2019	Our studies show that a hyaluronan and heparin-based hydrogel system locally delivers IL-10 by capitalizing on the ability of heparin to reversibly bind IL-10 without bleeding or other complications.	Heparin	126-133	interleukin 10	Mus musculus	153-158
31173322-10	2019	A standardized pro-weight pharmacological protocol is proposed; it allows to increase blood flow by volume expander action (Dextran) and thrombin inhibition (Heparin).	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	137-145
30543545-0	2019	Direct-Thrombin Inhibitor Utilization in Patients With Heparin-Induced Thrombocytopenia and Undergoing Catheter-Directed Thrombolysis: A Summary of Published Case Reports.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	7-15
30821921-8	2019	When the VEGF-ADSCs are seeded on WH-C, sustained release of VEGF is observed due to the specific affinity of VEGF to heparin.	Heparin	118-125	vascular endothelial growth factor A	Homo sapiens	9-13
30821921-8	2019	When the VEGF-ADSCs are seeded on WH-C, sustained release of VEGF is observed due to the specific affinity of VEGF to heparin.	Heparin	118-125	vascular endothelial growth factor A	Homo sapiens	61-65
31157200-7	2019	The dose-dependent thrombin clotting time (TCT) delay caused by Supra-TBA15/29-GO was &gt;10 times longer than that of common anticoagulant drugs including heparin, argatroban, hirudin, and warfarin.	Heparin	156-163	coagulation factor II	Rattus norvegicus	19-27
30773129-8	2019	The successful HE/CH deposition was confirmed by ATR-FTIR and X-ray photoelectron spectroscopy (XPS) analyses.	Heparin	15-17	ATR serine/threonine kinase	Homo sapiens	49-52
30326523-9	2019	While therapeutic versus low-dose heparin infusion was associated with improved flap survival following intraoperative microvascular compromise (86 vs. 25%, p = 0.04), salvage rates in the setting of postoperative thrombosis remained 0%, regardless of protocol.	Heparin	34-41	arachidonate 5-lipoxygenase activating protein	Homo sapiens	80-84
31239595-9	2019	In patients on high-dose heparin, the mean fibrinogen level measured by the DH method was significantly lower than that measured by the Clauss method.	Heparin	25-32	fibrinogen beta chain	Homo sapiens	43-53
30936586-1	2019	Direct thrombin inhibitors (DTIs), such as bivalirudin and dabigatran, have maintained steady inpatient and outpatient use as substitutes for heparin and warfarin, respectively, because of their high bioavailability and relatively safe "on-therapy" range.	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	7-15
30725510-15	2019	Based upon locations of the sulfate ions, we modeled heparin binding to FIXa, which is similar to the heparin binding in thrombin.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	121-129
30725510-15	2019	Based upon locations of the sulfate ions, we modeled heparin binding to FIXa, which is similar to the heparin binding in thrombin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	121-129
30725510-17	2019	The heparin binding mode in FIXa is similar to that in thrombin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	55-63
31019940-7	2019	The preoperative administration of heparin group (PH group) had received heparin 5,000 IU, BID (twice a day) both pre- and post-operatively.	Heparin	35-42	BH3 interacting domain death agonist	Homo sapiens	91-94
30714261-6	2019	Maintenance of patient-specific heparin concentrations during bypass is another key goal, since neonates have lower baseline antithrombin concentrations and, therefore, a higher risk for inadequate thrombin inhibition and postoperative bleeding.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	129-137
30727756-2	2019	Previous studies implied that thrombin exosite II, known as a binding site for heparin, may be involved in thrombin-induced PAR4 activation.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	30-38
30727756-2	2019	Previous studies implied that thrombin exosite II, known as a binding site for heparin, may be involved in thrombin-induced PAR4 activation.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	107-115
30727756-3	2019	In the present study, a heparin octasaccharide analog containing the thrombin exosite II-binding domain of heparin was chemically synthesized and investigated for anti-PAR4 effect.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	69-77
30850576-2	2019	This is a severe hypercoagulable state triggering massive thrombin storm needing additional therapies and aggressive anticoagulation apart from stopping heparin.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	58-66
30600066-4	2019	Thus, we conjugated ES2 to glycol-split heparin derivatives (GSHPs) to yield the polymer-peptide conjugate, GSHP-ES2.	Heparin	40-47	ess-2 splicing factor homolog	Homo sapiens	20-23
30600066-4	2019	Thus, we conjugated ES2 to glycol-split heparin derivatives (GSHPs) to yield the polymer-peptide conjugate, GSHP-ES2.	Heparin	40-47	ess-2 splicing factor homolog	Homo sapiens	113-116
30168023-6	2019	TSP-2/FGF2 binding was inhibited by calcium and heparin.	Heparin	48-55	fibroblast growth factor 2	Homo sapiens	6-10
30713119-9	2019	Target endogenous thrombin potential reduction from baseline was more frequently obtained in the enoxaparin group versus UFH (50% versus 27.7%, respectively; P = .12).	Heparin	121-124	coagulation factor II, thrombin	Homo sapiens	18-26
30573633-6	2019	Fibronectin levels were measured in 4 patient groups exhibiting different degrees of heparin-dependent immunization and expression of HIT.	Heparin	85-92	fibronectin 1	Homo sapiens	0-11
30573633-8	2019	Fibronectin also inhibited PF4/heparin binding to platelets, anti-PF4/heparin antibody binding to PF4/heparin complexes, and anti-PF4/heparin antibody-induced platelet activation as a result of PF4/heparin complex disruption.	Heparin	31-38	fibronectin 1	Homo sapiens	0-11
30573633-8	2019	Fibronectin also inhibited PF4/heparin binding to platelets, anti-PF4/heparin antibody binding to PF4/heparin complexes, and anti-PF4/heparin antibody-induced platelet activation as a result of PF4/heparin complex disruption.	Heparin	70-77	fibronectin 1	Homo sapiens	0-11
30573633-8	2019	Fibronectin also inhibited PF4/heparin binding to platelets, anti-PF4/heparin antibody binding to PF4/heparin complexes, and anti-PF4/heparin antibody-induced platelet activation as a result of PF4/heparin complex disruption.	Heparin	70-77	fibronectin 1	Homo sapiens	0-11
30168023-11	2019	Binding of TSP-2 to FGF2 impaired the growth factor ability to interact with its cellular receptors, since TSP-2-derived fragments prevented the binding of FGF2 to both heparin (used as a structural analog of heparan sulfate proteoglycans) and FGFR-1.	Heparin	169-176	fibroblast growth factor 2	Homo sapiens	156-160
30692962-5	2018	Heparin inhibits the thrombin generation and suppresses EAE.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	21-29
30056611-1	2019	U3-1565 is a monoclonal antibody directed against heparin-binding epidermal growth factor-like growth factor (HB-EGF), which mediates angiogenesis via induction of vascular endothelial growth factor (VEGF-A).	Heparin	50-57	vascular endothelial growth factor A	Homo sapiens	164-198
30056611-1	2019	U3-1565 is a monoclonal antibody directed against heparin-binding epidermal growth factor-like growth factor (HB-EGF), which mediates angiogenesis via induction of vascular endothelial growth factor (VEGF-A).	Heparin	50-57	vascular endothelial growth factor A	Homo sapiens	200-206
30407650-1	2019	Current management of heparin-induced thrombocytopenia (HIT) involves prompt discontinuation of all heparin products and concomitant initiation of a direct thrombin or anti-Xa inhibitor for anticoagulation.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	156-164
30573233-4	2019	Due to the similar groups as heparin-like structure, the modified membrane effectively prolonged the activated partial thromboplastin time, thrombin time, and prothrombin time.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	140-148
31020242-0	2019	A case report of atrial fibrillation in a patient with heparin resistance associated with an antithrombin III deficiency successfully treated by radiofrequency catheter ablation using a direct thrombin inhibitor.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	97-105
31626243-6	2019	Complex of heparin and antithrombin III increases inhibitory effect of antithrombin against thrombin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	27-35
31561344-1	2019	Hyperlipidemic heart transplant patients who develop cardiac allograft vasculopathy (CAV) benefit from HELP-apheresis (Heparin-induced Extracorporeal LDL Precipitation) which enables drastic lowering of plasma low-density lipoprotein, lipoprotein (a), and fibrinogen.	Heparin	119-126	fibrinogen beta chain	Homo sapiens	256-266
31679218-1	2019	Midkine (MK) is a heparin-binding anti-apoptotic growth factor or cytokine also known as neurite growth-promoting factor 2 (NEGF2).	Heparin	18-25	midkine	Homo sapiens	0-7
31679218-1	2019	Midkine (MK) is a heparin-binding anti-apoptotic growth factor or cytokine also known as neurite growth-promoting factor 2 (NEGF2).	Heparin	18-25	midkine	Homo sapiens	9-11
31679218-1	2019	Midkine (MK) is a heparin-binding anti-apoptotic growth factor or cytokine also known as neurite growth-promoting factor 2 (NEGF2).	Heparin	18-25	midkine	Homo sapiens	89-122
31679218-1	2019	Midkine (MK) is a heparin-binding anti-apoptotic growth factor or cytokine also known as neurite growth-promoting factor 2 (NEGF2).	Heparin	18-25	midkine	Homo sapiens	124-129
31030761-4	2019	Heparin inhibits both thrombin generation and thrombin activity, releases tissue factor pathway inhibitor, and possesses anti-inflammatory, anti-viral, anti-angiogenesis, anti-neoplastic, and anti-metastatic properties though high affinity interactions with a variety of proteins in the blood circulation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	22-30
29999558-1	2019	Heparin plays a significant role in wound healing and tissue regeneration applications, through stabilization of fibroblast growth factors (FGF).	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	140-143
29999558-5	2019	Nonetheless, the heparin-mimicking nanoparticles outperformed both heparin and linear P(AMPS) in cellular proliferation assays, suggesting increased bFGF stabilization efficiencies, possibly due to the high density of sulfonated moieties at the particle surface.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	149-153
30569872-11	2019	CONCLUSION: The findings in the present study demonstrate that PSTD domain is a potential target of heparin and may provide new insights into the molecular rationale of heparin-inhibiting NCAM polysialylation.	Heparin	100-107	neuronal cell adhesion molecule	Homo sapiens	188-192
30569872-11	2019	CONCLUSION: The findings in the present study demonstrate that PSTD domain is a potential target of heparin and may provide new insights into the molecular rationale of heparin-inhibiting NCAM polysialylation.	Heparin	169-176	neuronal cell adhesion molecule	Homo sapiens	188-192
31030744-6	2019	The anticoagulant activity of heparin is attributable to a 3-O-sulfate and 6-O-sulfate containing pentasaccharide sequence or a minimum eight-repeating disaccharide units containing the pentasaccharide sequence that catalyzes the suicidal inactivation of factor Xa or thrombin by a serpin or serine protease inhibitor named antithrombin III, respectively.	Heparin	30-37	serpin family C member 1	Bos taurus	324-340
31030761-4	2019	Heparin inhibits both thrombin generation and thrombin activity, releases tissue factor pathway inhibitor, and possesses anti-inflammatory, anti-viral, anti-angiogenesis, anti-neoplastic, and anti-metastatic properties though high affinity interactions with a variety of proteins in the blood circulation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	46-54
29730503-6	2018	In Fbln7-expressing CHO-K1 cells, exogenous heparin increased the release of Fbln7 into conditioned media in a dose-dependent manner.	Heparin	44-51	fibulin-7	Cricetulus griseus	77-82
30809279-5	2019	Thus, low-molecular-weight heparin-coated lipid-siRNA complex (LH-Lip/siBCL-2) was constructed to inhibit cancer metastasis and silence BCL-2 by BCL-2 siRNA (siBCL-2).	Heparin	27-34	BCL2 apoptosis regulator	Homo sapiens	72-77
30809279-5	2019	Thus, low-molecular-weight heparin-coated lipid-siRNA complex (LH-Lip/siBCL-2) was constructed to inhibit cancer metastasis and silence BCL-2 by BCL-2 siRNA (siBCL-2).	Heparin	27-34	BCL2 apoptosis regulator	Homo sapiens	136-141
29985837-1	2018	Concerns remain regarding the use of direct thrombin inhibitors for cardiopulmonary bypass anticoagulation in pediatric patients with heparin-induced thrombocytopenia undergoing complex cardiac surgery.	Heparin	134-141	coagulation factor II, thrombin	Homo sapiens	44-52
30543092-3	2018	Additionally, we evaluated the roles  of  heparin-binding  epidermal-like  growth  factor  (HB-EGF)  and  matrix  metalloproteinases  (MMPs)  in  Ang  II-induced  EGFR  transactivation.	Heparin	42-49	angiotensinogen	Rattus norvegicus	146-153
29069492-1	2018	Zymogen granule protein 16 (ZG16p) is a soluble lectin that binds to both mannose and heparin/heparan sulfate.	Heparin	86-93	zymogen granule protein 16	Homo sapiens	0-26
29069492-1	2018	Zymogen granule protein 16 (ZG16p) is a soluble lectin that binds to both mannose and heparin/heparan sulfate.	Heparin	86-93	zymogen granule protein 16	Homo sapiens	28-33
30539834-5	2018	Results: Significant difference was noted in the messenger RNA expression of VEGF, VEGFR, and HIF-1alpha after treating with heparin with a concentration of 15, 50, or 150 IU/ml in the A549 cell line at 24 and 48 h, respectively.	Heparin	125-132	vascular endothelial growth factor A	Homo sapiens	77-81
30539834-5	2018	Results: Significant difference was noted in the messenger RNA expression of VEGF, VEGFR, and HIF-1alpha after treating with heparin with a concentration of 15, 50, or 150 IU/ml in the A549 cell line at 24 and 48 h, respectively.	Heparin	125-132	hypoxia inducible factor 1 subunit alpha	Homo sapiens	94-104
29730503-6	2018	In Fbln7-expressing CHO-K1 cells, exogenous heparin increased the release of Fbln7 into conditioned media in a dose-dependent manner.	Heparin	44-51	fibulin-7	Cricetulus griseus	3-8
29730503-7	2018	This heparin-induced Fbln7 release was abrogated in CHO-745 cells lacking heparan sulfate proteoglycan or in CHO-K1 cells expressing the Fbln7 mutant lacking the N-terminal coiled-coil domain, suggesting that Fbln7 was tethered to pericellular matrix via this domain.	Heparin	5-12	fibulin-7	Cricetulus griseus	21-26
29730503-7	2018	This heparin-induced Fbln7 release was abrogated in CHO-745 cells lacking heparan sulfate proteoglycan or in CHO-K1 cells expressing the Fbln7 mutant lacking the N-terminal coiled-coil domain, suggesting that Fbln7 was tethered to pericellular matrix via this domain.	Heparin	5-12	fibulin-7	Cricetulus griseus	137-142
29730503-7	2018	This heparin-induced Fbln7 release was abrogated in CHO-745 cells lacking heparan sulfate proteoglycan or in CHO-K1 cells expressing the Fbln7 mutant lacking the N-terminal coiled-coil domain, suggesting that Fbln7 was tethered to pericellular matrix via this domain.	Heparin	5-12	fibulin-7	Cricetulus griseus	137-142
29777805-1	2018	Safe and efficient carboxymethyl chitosan (CMC)-based heparin-mimicking cross-linked beads (CMC/PAMPS) as adsorbents for the clearance of low-density lipoprotein-cholesterol (LDL-c) in blood purification were prepared through hydrogen bonding interactions followed with in situ cross-linking with 2-acrylamido-2-methyl-1-propanesulfonicacid (AMPS).	Heparin	54-61	component of oligomeric golgi complex 2	Homo sapiens	138-173
29481840-2	2018	Selenoprotein P (SELENOP) is a secreted heparin-binding glycoprotein which serves as the main Se transport protein in mammals.	Heparin	40-47	selenoprotein P	Homo sapiens	0-15
29481840-2	2018	Selenoprotein P (SELENOP) is a secreted heparin-binding glycoprotein which serves as the main Se transport protein in mammals.	Heparin	40-47	selenoprotein P	Homo sapiens	17-24
30519022-4	2018	Methods: The chitosan oligosaccharide/heparin nanoparticles (CSO/H NPs) were first prepared via self-assembly.	Heparin	38-45	twist family bHLH transcription factor 1	Homo sapiens	61-70
29956017-4	2018	Compared to the absence of heparin, treatment with heparin decreased the vascular endothelial growth factor (VEGF)-mediated activation of VEGFR2 and mitogenic effect on human lung microvascular endothelial cells in vitro.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	73-107
29956017-4	2018	Compared to the absence of heparin, treatment with heparin decreased the vascular endothelial growth factor (VEGF)-mediated activation of VEGFR2 and mitogenic effect on human lung microvascular endothelial cells in vitro.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	109-113
29173042-1	2018	Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	4-12
30194803-10	2018	Results Mouse TFPI and human TFPI are similar in regard to: (i) the mechanisms for FVIIa/TF and FXa inhibition; (ii) TFPIalpha is a soluble form and TFPIbeta is glycosyl phosphatidyl inositol (GPI) membrane anchored; (iii) the predominant circulating form of TFPI in plasma is lipoprotein-associated; (iv) low levels of TFPIalpha circulate in plasma and increase following heparin treatment; and (v) TFPIalpha is the isoform in platelets.	Heparin	373-380	tissue factor pathway inhibitor	Mus musculus	14-18
30260627-0	2018	The Structure in Solution of Fibronectin Type III Domain 14 Reveals Its Synergistic Heparin Binding Site.	Heparin	84-91	fibronectin 1	Homo sapiens	29-40
30260627-1	2018	Fibronectin is a large multidomain protein of the extracellular matrix that harbors two heparin binding sites, Hep-I and Hep-II, which support the heparin-dependent adhesion of melanoma and neuroblastoma cells [Barkalow, F. J.	Heparin	88-95	fibronectin 1	Homo sapiens	0-11
30260627-1	2018	Fibronectin is a large multidomain protein of the extracellular matrix that harbors two heparin binding sites, Hep-I and Hep-II, which support the heparin-dependent adhesion of melanoma and neuroblastoma cells [Barkalow, F. J.	Heparin	147-154	fibronectin 1	Homo sapiens	0-11
30260627-10	2018	The stronger heparin/HS binding site on fibronectin, Hep-II, spans fibronectin type III domains 12-14.	Heparin	13-20	fibronectin 1	Homo sapiens	40-51
30260627-10	2018	The stronger heparin/HS binding site on fibronectin, Hep-II, spans fibronectin type III domains 12-14.	Heparin	13-20	fibronectin 1	Homo sapiens	67-78
30260627-11	2018	Previous site-directed mutagenesis, nuclear magnetic resonance (NMR) chemical shift perturbation, and crystallographic structural studies all agree that the main heparin binding site is located on the surface of fibronectin type III domain 13 [Ingham, K. C., et al.	Heparin	162-169	fibronectin 1	Homo sapiens	212-223
30260627-18	2018	However, the "synergy site" for heparin binding located on fibronectin type III domain 14 remained elusive because the actual binding sites could not be identified.	Heparin	32-39	fibronectin 1	Homo sapiens	59-70
30102144-3	2018	This current work aims at determining whether warfarin and heparin, two other anticoagulants inhibiting thrombin formation and activities, may also be used for treatment against hMPV in vivo.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	104-112
30172259-8	2018	RESULTS: Sulfated-non-anticoagulant heparin administration in mice promoted a robust reduction in airway eosinophilia, mucus production, and airway hyperresponsiveness even after chronic repeated challenges with ovalbumin.	Heparin	36-43	serine (or cysteine) peptidase inhibitor, clade B, member 1, pseudogene	Mus musculus	212-221
30237127-6	2018	Here we show, using a newly-developed MS protocol, that HOCl and an enzymatic MPO system, generate site-specific dose-dependent Tyr chlorination and dichlorination (up to 16 of 100 residues modified), and oxidation of Trp (7 of 39 residues), Met (3 of 26) and His (1 of 55) within selected FN domains, and particularly the heparin- and cell-binding regions.	Heparin	323-330	myeloperoxidase	Homo sapiens	78-81
30237127-7	2018	These alterations increase FN binding to heparin-containing columns.	Heparin	41-48	fibronectin 1	Homo sapiens	27-29
29494334-4	2018	In conclusion, vaspin represents a multi-specific serpin targeting the kallikrein proteases KLK7 and KLK14, with distinct exosites regulating recognition of these target proteases and opposing effects of heparin binding on the inhibition reaction.	Heparin	204-211	serpin family A member 12	Homo sapiens	15-21
29717364-3	2018	The heparin effect on EC adhesion molecule (ICAM-1, VCAM-1, E-selectin) expression was also assessed.	Heparin	4-11	vascular cell adhesion molecule 1	Homo sapiens	52-58
29554021-12	2018	It is noteworthy that full neurological recovery is likely in surviving patients, and rechallenge with L-asparaginase is safe with heparin prophylaxis.	Heparin	131-138	asparaginase and isoaspartyl peptidase 1	Homo sapiens	103-117
30280291-4	2018	In this study, heparin was immobilized to the collagen part of decellularized scaffold with collagen-binding peptide (CBP).	Heparin	15-22	CREB binding protein	Homo sapiens	92-116
30280291-4	2018	In this study, heparin was immobilized to the collagen part of decellularized scaffold with collagen-binding peptide (CBP).	Heparin	15-22	CREB binding protein	Homo sapiens	118-121
30280291-7	2018	Taken together, our results reveal that the whole kidney can be modified by CBP-heparin composite to reduce the thrombosis and provide the better conditions for neovascularization.	Heparin	80-87	CREB binding protein	Homo sapiens	76-79
30031837-2	2018	In this study, we investigate the effect(s) of understanding the role of a conserved proline (P135), located in the heparin binding pocket, on the structure, stability, heparin binding affinity, and cell proliferation activity of hFGF1.	Heparin	116-123	fibroblast growth factor 1	Homo sapiens	230-235
30031837-4	2018	Interestingly, upon heparin binding, an increase in thermal stability equivalent to that of wt-hFGF1 was observed when P135 was replaced with a positive (P135K) or a negative charge (P135E), or with a polar amino acid (P135Q).	Heparin	20-27	fibroblast growth factor 1	Homo sapiens	95-100
30031837-5	2018	Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity.	Heparin	53-60	fibroblast growth factor 1	Homo sapiens	110-115
30031837-5	2018	Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity.	Heparin	131-138	fibroblast growth factor 1	Homo sapiens	110-115
30031837-5	2018	Surprisingly, introduction of negative charge in the heparin-binding pocket at position 135 (P135E) increased hFGF1"s affinity for heparin by 3-fold, while the P135K mutation, did not alter the heparin-binding affinity.	Heparin	131-138	fibroblast growth factor 1	Homo sapiens	110-115
30031837-9	2018	Overall, the results of this study suggest that while heparin is useful for stabilizing hFGF1 on the cell surface, this interaction is not mandatory for activation of the FGF receptor.	Heparin	54-61	fibroblast growth factor 1	Homo sapiens	88-93
29853648-0	2018	Epigallocatechin-3-gallate remodels apolipoprotein A-I amyloid fibrils into soluble oligomers in the presence of heparin.	Heparin	113-120	apolipoprotein A1	Homo sapiens	36-54
30086574-8	2018	RESULTS/CONCLUSION:  The most striking changes were observed following heparin administration and were associated with the appearance of inactive forms of anti-thrombin and an increase in the plasma concentration of TFPI.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	160-168
29853648-2	2018	Using CD analysis, solid-state NMR spectroscopy, and transmission EM, we report here a surprising cooperative effect of heparin and the green tea polyphenol (-)-epigallocatechin-3-gallate (EGCG), a known inhibitor and modulator of amyloid formation, on apoA-I fibrils.	Heparin	120-127	apolipoprotein A1	Homo sapiens	253-259
29853648-3	2018	We found that heparin, a proxy for glycosaminoglycan (GAG) polysaccharides that co-localize ubiquitously with amyloid in vivo, accelerates the rate of apoA-I formation from monomeric protein and associates with insoluble fibrils.	Heparin	14-21	apolipoprotein A1	Homo sapiens	151-157
29853648-5	2018	EGCG selectively increased the mobility of specific backbone and side-chain sites of apoA-I fibrils formed in the absence of heparin, but the fibrils largely retained their original morphology and remained insoluble.	Heparin	125-132	apolipoprotein A1	Homo sapiens	85-91
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	mitogen-activated protein kinase 14	Homo sapiens	185-189
29914979-1	2018	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder initiated by antibodies to platelet factor 4 (PF4)/heparin complexes.	Heparin	0-7	platelet factor 4	Mus musculus	113-116
29923498-0	2018	Interactions of methacryloylated gelatin and heparin modulate physico-chemical properties of hydrogels and release of vascular endothelial growth factor.	Heparin	45-52	vascular endothelial growth factor A	Homo sapiens	118-152
29812912-8	2018	We found that FGF1 binds CD44 through its heparin-binding moiety.	Heparin	42-49	fibroblast growth factor 1	Homo sapiens	14-18
29730577-2	2018	After treated by ammonia plasma, Poly(lactic-co-glycolic acid) (PLGA) electrospun nanofibers were immobilized with VEGF through heparin to fulfil the sustained release.	Heparin	128-135	vascular endothelial growth factor A	Homo sapiens	115-119
29707901-1	2018	INTRODUCTION: Argatroban is a direct thrombin inhibitor used as an anticoagulant for patients who have Heparin induced thrombocytopenia.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	37-45
29164398-2	2018	MATERIALS AND METHODS: We have prospectively followed up a 42-patient cohort for surgical treatment by osteosynthesis or hip arthroplasty, and CRP was dosed at admission, on day 1, day 3, day 5 and then twice weekly for 30 days at the same time as a platelet count control of low molecular weight heparins.	Heparin	297-305	C-reactive protein	Homo sapiens	143-146
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	96-103	epidermal growth factor receptor	Homo sapiens	23-27
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	140-147	epidermal growth factor receptor	Homo sapiens	23-27
29274275-8	2018	In conclusion, the heparin-binding domain of HB-EGF was responsible for EGFR-mediated Stat5 activation, resulting in a more potent cellular proliferation, and migration than that mediated by EGF.	Heparin	19-26	epidermal growth factor receptor	Homo sapiens	72-76
30016181-11	2018	UFH inhibited LPS-induced phosphorylation of IkappaB-alpha, c-Jun, ERK1/2, JNK, and p38 MAPK but not c-fos.	Heparin	0-3	NFKB inhibitor alpha	Homo sapiens	45-58
30016181-11	2018	UFH inhibited LPS-induced phosphorylation of IkappaB-alpha, c-Jun, ERK1/2, JNK, and p38 MAPK but not c-fos.	Heparin	0-3	mitogen-activated protein kinase 3	Homo sapiens	67-73
30016181-11	2018	UFH inhibited LPS-induced phosphorylation of IkappaB-alpha, c-Jun, ERK1/2, JNK, and p38 MAPK but not c-fos.	Heparin	0-3	mitogen-activated protein kinase 8	Homo sapiens	75-78
30016181-12	2018	UFH also suppressed LPS-induced nuclear translocation of NF-kappaB.	Heparin	0-3	nuclear factor kappa B subunit 1	Homo sapiens	57-66
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	tumor necrosis factor	Homo sapiens	49-58
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	interleukin 6	Homo sapiens	60-64
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	C-X-C motif chemokine ligand 8	Homo sapiens	66-70
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	nuclear factor kappa B subunit 1	Homo sapiens	191-200
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	114-117	tumor necrosis factor	Homo sapiens	49-58
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	114-117	C-X-C motif chemokine ligand 8	Homo sapiens	66-70
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	114-117	mitogen-activated protein kinase 14	Homo sapiens	185-189
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	114-117	nuclear factor kappa B subunit 1	Homo sapiens	191-200
29930947-2	2018	Trisulfated heparin disaccharide (TD) and Low Molecular Weight Heparins (LMWHs) can directly interact with the NCX and accelerate its activity.	Heparin	63-71	solute carrier family 8 member A1	Rattus norvegicus	111-114
29689163-3	2018	Herein, we developed an injectable cryogel by conjugating heparin to gelatin as a carrier for vascular endothelial growth factor (VEGF) and fibroblasts in hindlimb ischemic disease.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	94-128
29689163-3	2018	Herein, we developed an injectable cryogel by conjugating heparin to gelatin as a carrier for vascular endothelial growth factor (VEGF) and fibroblasts in hindlimb ischemic disease.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	130-134
29790645-2	2018	FIBPT-d method overestimates fibrinogen in rivaroxaban and low molecular weight heparin samples.	Heparin	80-87	fibrinogen beta chain	Homo sapiens	29-39
29782703-4	2018	This 3D micropatterning method could be applied to various heparin binding growth factors, such as fibroblast growth factor-2, vascular endothelial growth factor, transforming growth factor-betas and bone morphogenetic proteins while retaining the hydrogel"s natural degradability and cytocompability.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	99-125
29738889-1	2018	We present a computational model of the Vascular Endothelial Growth Factor (VEGF), an important regulator of blood vessels formation, which function is affected by its heparin interactions.	Heparin	168-175	vascular endothelial growth factor A	Homo sapiens	40-74
29738889-1	2018	We present a computational model of the Vascular Endothelial Growth Factor (VEGF), an important regulator of blood vessels formation, which function is affected by its heparin interactions.	Heparin	168-175	vascular endothelial growth factor A	Homo sapiens	76-80
29738889-2	2018	Although structures of a receptor binding (RBD) and a heparin binding domain (HBD) of VEGF are known, there are structural data neither on the 12 amino acids interdomain linker nor on its complexes with heparin.	Heparin	54-61	vascular endothelial growth factor A	Homo sapiens	86-90
29645318-5	2018	Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions.	Heparin	44-51	fibroblast growth factor 1	Homo sapiens	22-27
29645318-5	2018	Crystal structures of FGF-1 in complex with heparin have shown that heparin binds to N-terminal Asn18 and to C-terminal Lys105, Tryp107, Lys112, Lys113, Arg119, Pro121, Arg122, Gln127, and Lys128 indicating electrostatic forces as dominant interactions.	Heparin	68-75	fibroblast growth factor 1	Homo sapiens	22-27
29645318-7	2018	Previous studies have also shown that other polyanions including low MW heparin, phytic acid and ATP dramatically increase the thermal stability of FGF-1.	Heparin	72-79	fibroblast growth factor 1	Homo sapiens	148-153
29645318-8	2018	Using HX-MS, we find other poly anions tested bind in a similar manner to heparin, primarily targeting the turns in the lysine rich C-terminal region of FGF-1 along with two distinct N-terminal regions that contains lysines and arginines/histidines.	Heparin	74-81	fibroblast growth factor 1	Homo sapiens	153-158
29744595-8	2018	However, heparin can inhibit plasma-free thrombin, and cause the occurrence of heparin-induced thrombocytopenia (HIT), which increases the risk of bleeding during dialysis in critical care patients.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	41-49
29476751-8	2018	injection of lipopolysaccharides from Rhodobacter sphaeroides (LPS-RS, a TLR4 antagonist) and low-molecular-weight heparin (LMWH, a RAGE antagonist) significantly blocked mechanical allodynia on day 3 after BCAO.	Heparin	115-122	MOK protein kinase	Mus musculus	132-136
33445317-4	2018	The biocompatibility evaluation results indicated that the SEMA4D-heparin-modified surfaces displayed less platelet adhesion and activation, prolonged activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) and reduced fibrinogen gamma chain (FGG) exposure and fibrinogen adhesion.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	200-208
33445317-4	2018	The biocompatibility evaluation results indicated that the SEMA4D-heparin-modified surfaces displayed less platelet adhesion and activation, prolonged activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) and reduced fibrinogen gamma chain (FGG) exposure and fibrinogen adhesion.	Heparin	66-73	fibrinogen gamma chain	Homo sapiens	254-276
33445317-4	2018	The biocompatibility evaluation results indicated that the SEMA4D-heparin-modified surfaces displayed less platelet adhesion and activation, prolonged activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) and reduced fibrinogen gamma chain (FGG) exposure and fibrinogen adhesion.	Heparin	66-73	fibrinogen gamma chain	Homo sapiens	278-281
33445317-4	2018	The biocompatibility evaluation results indicated that the SEMA4D-heparin-modified surfaces displayed less platelet adhesion and activation, prolonged activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) and reduced fibrinogen gamma chain (FGG) exposure and fibrinogen adhesion.	Heparin	66-73	fibrinogen beta chain	Homo sapiens	254-264
33445338-4	2018	Using the layer-by-layer (LbL) assembly technique with fibronectin, heparin, and tannic acid, we prepared a VEGF-incorporated multilayer film (VEGF film) that is smooth and stable and increases cell proliferation by up to 2.5 times that of the control group cells.	Heparin	68-75	vascular endothelial growth factor A	Homo sapiens	108-112
29760942-4	2018	hFDM was then conjugated with heparin via N-(3-Dimethylaminopropyl)-N"-ethylcarbodiimide hydrochloride (EDC) chemistry and subject to transforming growth factor (TGF)-beta1 immobilization.	Heparin	30-37	transforming growth factor beta 1	Homo sapiens	134-172
29723248-10	2018	Heparin inhibited HBP expression during sepsis-induced AKI.	Heparin	0-7	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	18-21
29095088-5	2018	2 There is conflicting evidence in the literature as to whether only heparin-binding VEGF-A isoforms - that is, isoforms with domains encoded by exons 6 and/or 7 plus 8a - bind to Neuropilins on endothelial cells.	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	85-91
29723248-11	2018	The suppression of HBP expression by heparin injection after the establishment of sepsis-induced AKI resulted in a reduction in renal injury severity accompanied with a significant repression of M1 macrophage activation and expression of TNF-alpha and IL-6.	Heparin	37-44	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	19-22
29723248-11	2018	The suppression of HBP expression by heparin injection after the establishment of sepsis-induced AKI resulted in a reduction in renal injury severity accompanied with a significant repression of M1 macrophage activation and expression of TNF-alpha and IL-6.	Heparin	37-44	tumor necrosis factor	Mus musculus	238-247
29723248-11	2018	The suppression of HBP expression by heparin injection after the establishment of sepsis-induced AKI resulted in a reduction in renal injury severity accompanied with a significant repression of M1 macrophage activation and expression of TNF-alpha and IL-6.	Heparin	37-44	interleukin 6	Mus musculus	252-256
29550439-7	2018	Heparin functionalization increased the amount of TGF-beta2 and GDF5 remaining attached to the scaffold matrix and resulted in biological effects at low growth factor doses.	Heparin	0-7	growth differentiation factor 5	Homo sapiens	64-68
29139224-4	2018	Then, heparin-terminated/fibronectin-coated PEMs were used to deliver varying concentrations of an adsorbed model GF, transforming growth factor beta (TGFbeta), to PHH monocultures while using soluble TGFbeta delivery via culture medium as the conventional control.	Heparin	6-13	transforming growth factor beta 1	Homo sapiens	118-149
29574610-0	2018	Platelet response to direct thrombin inhibitor or fondaparinux treatment in patients with suspected heparin-induced thrombocytopenia.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	28-36
29573721-0	2018	Novel heparin mimetics reveal cooperativity between exosite 2 and sodium-binding site of thrombin.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	89-97
29622761-1	2018	BACKGROUND New oral anticoagulants like direct thrombin inhibitors are an attractive alternative to vitamin K antagonists as anticoagulation therapy and can be used in heparin-induced thrombocytopenia.	Heparin	168-175	coagulation factor II, thrombin	Homo sapiens	47-55
29459207-3	2018	We present the design of a group of sulfated benzofuran dimers that display heparin-binding site-dependent partial allosteric inhibition of thrombin against fibrinogen (DeltaY = 55-75%), the first time that a small molecule (MW  &lt; 800) has been found to thwart macromolecular cleavage by a monomeric protease in a controlled manner.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	140-148
29459207-3	2018	We present the design of a group of sulfated benzofuran dimers that display heparin-binding site-dependent partial allosteric inhibition of thrombin against fibrinogen (DeltaY = 55-75%), the first time that a small molecule (MW  &lt; 800) has been found to thwart macromolecular cleavage by a monomeric protease in a controlled manner.	Heparin	76-83	fibrinogen beta chain	Homo sapiens	157-167
29139224-4	2018	Then, heparin-terminated/fibronectin-coated PEMs were used to deliver varying concentrations of an adsorbed model GF, transforming growth factor beta (TGFbeta), to PHH monocultures while using soluble TGFbeta delivery via culture medium as the conventional control.	Heparin	6-13	transforming growth factor beta 1	Homo sapiens	151-158
29784539-2	2018	Its activity is highly enhanced by heparin, through binding to the pentasaccharide sequences, for inhibition of all coagulation proteases, except thrombin, which inhibition requires its additional binding to the heparin polysaccharide chain.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	146-154
29064332-0	2018	Use of prothrombin complex concentrate containing heparin for emergency reversal of bivalirudin anticoagulation: a word of caution.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	7-18
28898897-7	2018	Several studies report unselective antagonism of VWF for drugs used in daily clinical practice, including heparin and statins.	Heparin	106-113	von Willebrand factor	Homo sapiens	49-52
29461035-8	2018	Heparin immobilization on the positively charged nanofiber yarns was visualized using fluorescein-conjugated heparin (F-Hep), and the amount of immobilized F-Hep was higher on both PLGA/PEO/PgP3.7 and PLGA/PEO/PgP1 than yarns without PgP (PLGA/PEO).	Heparin	0-7	twinkle mtDNA helicase	Homo sapiens	181-189
29636721-4	2018	Different mechanisms of action for heparin have been proposed including, but not limited to the binding and neutralization of oxyhemoglobin, decreased transcription and signal transduction of endothelin-1, inhibition of binding to vessel wall selectins and vascular leakage into the subarachnoid space as well as direct binding and neutralization of inflammatory molecules.	Heparin	35-42	endothelin 1	Homo sapiens	192-204
29441779-10	2018	These results suggested that the heparin moiety within the nanocavity provided HBD selectivity and the polymer matrix composed of the molecularly imprinted nanocavity provided size/shape selectivity, which resulted in the highly selective discrimination of VEGF isoforms.	Heparin	33-40	vascular endothelial growth factor A	Homo sapiens	257-261
29413981-10	2018	The AFM, XPS, and QCM measurements show that the PIP process facilitates macromolecularly surface imprinting of template heparin where the template is easily removed and is rapidly rebound to PIP-MIP without a diffusional barrier.	Heparin	121-128	prolactin induced protein	Homo sapiens	49-52
29413981-10	2018	The AFM, XPS, and QCM measurements show that the PIP process facilitates macromolecularly surface imprinting of template heparin where the template is easily removed and is rapidly rebound to PIP-MIP without a diffusional barrier.	Heparin	121-128	prolactin induced protein	Homo sapiens	192-195
29413981-11	2018	The heparin-PIP-MIP specifically binds to heparin compared with heparin analog chondroitin sulfate C (selective factor: 4.0) and a detectable range of heparin in the presence of CS (0.1 wt%) was 0.001-0.1 wt%.	Heparin	4-11	prolactin induced protein	Homo sapiens	12-15
29413981-11	2018	The heparin-PIP-MIP specifically binds to heparin compared with heparin analog chondroitin sulfate C (selective factor: 4.0) and a detectable range of heparin in the presence of CS (0.1 wt%) was 0.001-0.1 wt%.	Heparin	42-49	prolactin induced protein	Homo sapiens	12-15
29413981-11	2018	The heparin-PIP-MIP specifically binds to heparin compared with heparin analog chondroitin sulfate C (selective factor: 4.0) and a detectable range of heparin in the presence of CS (0.1 wt%) was 0.001-0.1 wt%.	Heparin	42-49	prolactin induced protein	Homo sapiens	12-15
29414786-6	2018	The most abundant apoE fragments were 25- and 28-kDa N-terminal fragments that both contained sialylated glycosylation and bound to heparin.	Heparin	132-139	apolipoprotein E	Homo sapiens	18-22
29073518-0	2018	An aptasensor based on heparin-mimicking hyperbranched polyester with anti-biofouling interface for sensitive thrombin detection.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	110-118
29461035-8	2018	Heparin immobilization on the positively charged nanofiber yarns was visualized using fluorescein-conjugated heparin (F-Hep), and the amount of immobilized F-Hep was higher on both PLGA/PEO/PgP3.7 and PLGA/PEO/PgP1 than yarns without PgP (PLGA/PEO).	Heparin	0-7	twinkle mtDNA helicase	Homo sapiens	201-209
29461035-8	2018	Heparin immobilization on the positively charged nanofiber yarns was visualized using fluorescein-conjugated heparin (F-Hep), and the amount of immobilized F-Hep was higher on both PLGA/PEO/PgP3.7 and PLGA/PEO/PgP1 than yarns without PgP (PLGA/PEO).	Heparin	0-7	twinkle mtDNA helicase	Homo sapiens	201-209
28320219-1	2018	Monitoring of direct thrombin inhibitors (DTIs) in patients with heparin-induced thrombocytopenia (HIT) is primarily performed using the activated partial thromboplastin time (aPTT).	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	21-29
29174671-0	2018	Human IGF-I propeptide A promotes articular chondrocyte biosynthesis and employs glycosylation-dependent heparin binding.	Heparin	105-112	insulin like growth factor 1	Homo sapiens	6-11
29174671-8	2018	Of the three IGF-I propeptides, only one, proIGF-IA, strongly bound to heparin.	Heparin	71-78	insulin like growth factor 1	Homo sapiens	13-18
29174671-11	2018	CONCLUSION: The biosynthetic and heparin binding abilities of proIGF-IA, coupled with its generation of IGF-I, suggest that proIGF-IA may have therapeutic value for articular cartilage repair.	Heparin	33-40	insulin like growth factor 1	Homo sapiens	65-70
29361522-7	2018	Similar results were obtained by blocking the heparin-binding stretch FNIII12-13-14 (HepII), adjacent to the ED-A domain in fibronectin.	Heparin	46-53	fibronectin 1	Homo sapiens	124-135
28862812-5	2018	On one occasion, free fatty acid elevation, to cause insulin resistance, was achieved by infusion of Intralipid + heparin.	Heparin	114-121	insulin	Homo sapiens	53-60
29030736-4	2018	Our data demonstrate that BOC2, but not BOC1, inhibits the angiogenic activity of heparin-binding VEGF-A165 with no effect on the activity of the non-heparin-binding VEGF-A121 isoform.	Heparin	82-89	vascular endothelial growth factor A	Homo sapiens	98-104
29315824-4	2018	These particles are enriched by heparin to enable a steady release of interleukin-2 (IL-2), the major T-cell growth factor, over 10+ d. The controlled delivery of cytokines is used to steer lineage specification of cultured T-cells.	Heparin	32-39	interleukin 2	Homo sapiens	70-83
29315824-4	2018	These particles are enriched by heparin to enable a steady release of interleukin-2 (IL-2), the major T-cell growth factor, over 10+ d. The controlled delivery of cytokines is used to steer lineage specification of cultured T-cells.	Heparin	32-39	interleukin 2	Homo sapiens	85-89
29030736-6	2018	In addition, BOC2 inhibits the interaction of a variety of heparin-binding angiogenic growth factors with heparin, including fibroblast growth factor 2 (FGF2) whose angiogenic activity is blocked by the compound.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	125-151
29030736-6	2018	In addition, BOC2 inhibits the interaction of a variety of heparin-binding angiogenic growth factors with heparin, including fibroblast growth factor 2 (FGF2) whose angiogenic activity is blocked by the compound.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	153-157
29254059-3	2018	In this paper, vascular endothelial growth factor (VEGF)-loaded 3D porous bacterial cellulose/gelatin (B/G) scaffolds modified with heparin were firstly prepared.	Heparin	132-139	vascular endothelial growth factor A	Homo sapiens	15-49
29254059-3	2018	In this paper, vascular endothelial growth factor (VEGF)-loaded 3D porous bacterial cellulose/gelatin (B/G) scaffolds modified with heparin were firstly prepared.	Heparin	132-139	vascular endothelial growth factor A	Homo sapiens	51-55
29254059-5	2018	Results showed that the B/G scaffold modified with heparin could provide a prolonged release of VEGF for two weeks.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	96-100
29280610-5	2018	The microsphere was self-assembled with heparin-modified gelatin nanofibers, and interleukin 4 (IL4) was incorporated into the nanofibrous heparin-modified gelatin microsphere (NHG-MS).	Heparin	139-146	interleukin 4	Homo sapiens	81-94
29329093-4	2018	An inhibition percentage of 43.19+-2.02% was obtained using heparin as an anticoagulant, in addition to the determination of the percentage of heparin bonded to thrombin.	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	161-169
29280610-5	2018	The microsphere was self-assembled with heparin-modified gelatin nanofibers, and interleukin 4 (IL4) was incorporated into the nanofibrous heparin-modified gelatin microsphere (NHG-MS).	Heparin	139-146	interleukin 4	Homo sapiens	96-99
29280610-6	2018	IL4 has binding domains with heparin, and the binding of IL4 to heparin stabilizes this cytokine, protects it from denaturation and degradation, and subsequently prolongs its sustained release to modulate macrophage polarization.	Heparin	29-36	interleukin 4	Homo sapiens	0-3
29280610-6	2018	IL4 has binding domains with heparin, and the binding of IL4 to heparin stabilizes this cytokine, protects it from denaturation and degradation, and subsequently prolongs its sustained release to modulate macrophage polarization.	Heparin	64-71	interleukin 4	Homo sapiens	57-60
29346400-8	2018	In defibrinated, recalcified plasma, on the contrary, heparin is able to reduce CXCL5 and CXCL7 release from platelets by thrombin inhibition.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	122-130
29346400-0	2018	The mechanisms how heparin affects the tumor cell induced VEGF and chemokine release from platelets to attenuate the early metastatic niche formation.	Heparin	19-26	vascular endothelial growth factor A	Homo sapiens	58-62
30271699-4	2018	The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated.	Heparin	44-51	fibroblast growth factor 1	Homo sapiens	129-155
29346400-6	2018	Preincubation of platelets with therapeutic concentrations of unfractionated heparin reduces the tumor cell initiated VEGF release from platelets.	Heparin	77-84	vascular endothelial growth factor A	Homo sapiens	118-122
30271699-4	2018	The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated.	Heparin	44-51	fibroblast growth factor 1	Homo sapiens	157-161
29460830-0	2018	[Exocytosis of myeloperoxidase from activated neutrophils in the presence of heparin].	Heparin	77-84	myeloperoxidase	Homo sapiens	15-30
29460830-3	2018	It was found that after preincubation of cells with heparin (0.1 u/ml) the exocytosis of MPO from neutrophils activated by various stimulants (fMLP, PMA, plant lectins CABA and PHA-L) increased compared to that under the action of activators alone.	Heparin	52-59	myeloperoxidase	Homo sapiens	89-92
30271699-4	2018	The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated.	Heparin	44-51	fibroblast growth factor 2	Homo sapiens	167-193
29460830-3	2018	It was found that after preincubation of cells with heparin (0.1 u/ml) the exocytosis of MPO from neutrophils activated by various stimulants (fMLP, PMA, plant lectins CABA and PHA-L) increased compared to that under the action of activators alone.	Heparin	52-59	formyl peptide receptor 1	Homo sapiens	143-147
29460830-5	2018	Thus, the use of heparin at a concentration of 0.1 u/ml avoids the artifact caused by the "loss" of MPO in a result of its binding to neutrophils, and increases the accuracy of the method of registration the degranulation of azurophilic granules of neutrophils based on determination of the concentration or peroxidase activity of MPO in cell supernatants.	Heparin	17-24	myeloperoxidase	Homo sapiens	100-103
29460830-5	2018	Thus, the use of heparin at a concentration of 0.1 u/ml avoids the artifact caused by the "loss" of MPO in a result of its binding to neutrophils, and increases the accuracy of the method of registration the degranulation of azurophilic granules of neutrophils based on determination of the concentration or peroxidase activity of MPO in cell supernatants.	Heparin	17-24	myeloperoxidase	Homo sapiens	331-334
30271699-4	2018	The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated.	Heparin	44-51	fibroblast growth factor 2	Homo sapiens	195-199
29895019-4	2018	METHODS: To more efficiently deliver bFGF and NGF, we used a coacervate (synthesized with heparin and a biodegradable polycation at mass ratio of 500: 100).	Heparin	90-97	fibroblast growth factor 2	Homo sapiens	37-41
29719300-0	2018	Unfractionated Heparin Alleviates Human Lung Endothelial Barrier Dysfunction Induced by High Mobility Group Box 1 Through Regulation of P38-GSK3beta-Snail Signaling Pathway.	Heparin	15-22	mitogen-activated protein kinase 14	Homo sapiens	136-139
29719300-0	2018	Unfractionated Heparin Alleviates Human Lung Endothelial Barrier Dysfunction Induced by High Mobility Group Box 1 Through Regulation of P38-GSK3beta-Snail Signaling Pathway.	Heparin	15-22	snail family transcriptional repressor 1	Homo sapiens	149-154
29719300-13	2018	In addition, we found that UFH was able to reverse the effect of HMGB1 on EndoMT and endothelial permeability through inhibition of p38 signaling in a dose-dependent manner.	Heparin	27-30	mitogen-activated protein kinase 14	Homo sapiens	132-135
29284430-10	2017	However, asymptomatic DIC developed after 47 days, and her serum fibrinogen level declined to 42 mg/dL, which was successfully treated with anticoagulant therapy by a therapeutic dose of intravenous heparin for 22 days (postoperative days 48-69).	Heparin	199-206	fibrinogen beta chain	Homo sapiens	65-75
28457186-5	2018	We explored the effects of heparin on FGF-2 enhancement of bioactive ECM scaffold biomaterials for its antifibrotic effect on attenuating human cardiac myofibroblast activation.	Heparin	27-34	fibroblast growth factor 2	Homo sapiens	38-43
28457186-6	2018	Increasing heparin concentration at a fixed concentration of FGF-2 markedly increased the amount of FGF-2 retained and eluted by ECM scaffolds.	Heparin	11-18	fibroblast growth factor 2	Homo sapiens	61-66
28457186-6	2018	Increasing heparin concentration at a fixed concentration of FGF-2 markedly increased the amount of FGF-2 retained and eluted by ECM scaffolds.	Heparin	11-18	fibroblast growth factor 2	Homo sapiens	100-105
28457186-12	2018	In summary, heparin is an effective adjuvant to enhance FGF-2 loading and elution of acellular ECM scaffold biomaterials.	Heparin	12-19	fibroblast growth factor 2	Homo sapiens	56-61
28457186-13	2018	Heparin increases the bioactive effects of FGF-2 in attenuating human cardiac myofibroblast activation in response to profibrotic TGF-beta1.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	43-48
28457186-13	2018	Heparin increases the bioactive effects of FGF-2 in attenuating human cardiac myofibroblast activation in response to profibrotic TGF-beta1.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	130-139
29216941-0	2017	[Impact of unfractionated heparin on serum and liver tissue expression of heparanase in the liver injury of mice with sepsis].	Heparin	26-33	heparanase	Mus musculus	74-84
29556563-4	2018	In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is examined by extending the heparin binding pocket through selective engineering via charge reversal mutations (D82R, D84R and D82R/D84R).	Heparin	56-63	fibroblast growth factor 1	Homo sapiens	116-121
29556563-4	2018	In this context, in this study, the correlation between heparin binding affinity and cell proliferation activity of hFGF1 is examined by extending the heparin binding pocket through selective engineering via charge reversal mutations (D82R, D84R and D82R/D84R).	Heparin	151-158	fibroblast growth factor 1	Homo sapiens	116-121
29556563-9	2018	However, despite the increased affinity of D82R for heparin, the cell proliferation activity of the D82R variant is observed to be reduced compared to the wild type hFGF1.	Heparin	52-59	fibroblast growth factor 1	Homo sapiens	165-170
29556563-10	2018	The results of this study clearly demonstrate that heparin binding affinity of hFGF1 is not strongly correlated to its cell proliferation activity.	Heparin	51-58	fibroblast growth factor 1	Homo sapiens	79-84
29066620-8	2017	Finally, these AutoAbs enhance tumor growth in mice bearing human prostate cancer xenografts, and heparin derivatives specifically abrogate this effect by blocking AutoAb binding to cell-surface GRP78 and decreasing TF expression/activity.	Heparin	98-105	heat shock protein family A (Hsp70) member 5	Homo sapiens	195-200
28859966-10	2017	Finally, CXCL4L1(1-70) and CXCL4L1(-4-70) showed the same affinity for heparin.	Heparin	71-78	platelet factor 4 variant 1	Homo sapiens	9-16
28859966-10	2017	Finally, CXCL4L1(1-70) and CXCL4L1(-4-70) showed the same affinity for heparin.	Heparin	71-78	platelet factor 4 variant 1	Homo sapiens	27-34
29285085-8	2017	In addition, UFH inhibited the LPS-induced activation of mitogen-activated protein kinase 14, proto-oncogene tyrosine-protein kinase Src and nuclear factor kappaB signaling in HUVECs.	Heparin	13-16	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	94-136
29216941-1	2017	OBJECTIVE: To investigate the effect of unfractionated heparin on the expression of serum and liver tissue heparanase (HPA) in mice with liver injury induced by sepsis.	Heparin	55-62	heparanase	Mus musculus	107-117
29016740-1	2017	Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI).	Heparin	43-50	fibroblast growth factor 1	Homo sapiens	6-32
28864252-3	2017	Inspired by this naturally occurring stabilization process, we propose the use of diblock copolymers of heparin and polyethylene glycol (Hep-b-PEG) for protection and delivery of FGF-2.	Heparin	104-111	fibroblast growth factor 2	Homo sapiens	179-184
28742513-7	2017	Kallistatin attenuates organ injury and apoptosis in animal models, and its heparin-binding site is essential for blocking tumor necrosis factor (TNF)-alpha-induced apoptosis in endothelial cells.	Heparin	76-83	tumor necrosis factor	Mus musculus	123-156
28742513-11	2017	Kallistatin via the heparin-binding domain antagonizes TNF-alpha-induced oxidative stress, whereas its active site is crucial for stimulating antioxidant enzyme expression.	Heparin	20-27	tumor necrosis factor	Mus musculus	55-64
29016740-1	2017	Aims: Fibroblast growth factor 1 (FGF1), a heparin/heparan sulfate-binding growth factor, is a potent cardioprotective agent against myocardial infarction (MI).	Heparin	43-50	fibroblast growth factor 1	Homo sapiens	34-38
29016740-7	2017	Both native and modified FGF1 restored contractile and relaxation function (P &lt; 0.05 versus saline or heparin).	Heparin	105-112	fibroblast growth factor 1	Homo sapiens	25-29
29016740-9	2017	Heparin negatively impacted the cardioprotective effects (infarct size, post-ischemic recovery of function) of FGF1 (P &lt; 0.05) but not of FGF1DeltaHBS.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	111-115
29016740-10	2017	Heparin also reduced the biodistribution of FGF1, but not FGF1DeltaHBS, to the left ventricle.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	44-48
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	0-4
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	9-13
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	fibroblast growth factor receptor 1	Homo sapiens	42-47
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	mitogen-activated protein kinase 3	Homo sapiens	81-87
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	9-13
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	mitogen-activated protein kinase 3	Homo sapiens	153-159
29016740-11	2017	FGF1 and FGF1DeltaHBS bound and triggered FGFR1-induced downstream activation of ERK1/2 (P &lt; 0.05); yet, heparin co-treatment decreased FGF1-produced ERK1/2 activation, but not that activated by FGF1DeltaHBS.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	9-21
29016740-12	2017	Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease.	Heparin	64-71	fibroblast growth factor 1	Homo sapiens	90-94
29016740-12	2017	Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease.	Heparin	64-71	fibroblast growth factor 1	Homo sapiens	90-93
29016740-12	2017	Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease.	Heparin	173-180	fibroblast growth factor 1	Homo sapiens	90-94
29091276-3	2017	Based on the structural knowledge available from the FGF1-heparin interaction studies, we have designed a novel heparin-binding peptide (HBP) affinity tag that can be used for the simple, efficient, and cost-effective purification of recombinant proteins of interest.	Heparin	58-65	fibroblast growth factor 1	Homo sapiens	53-57
29016740-12	2017	Conclusion: These findings demonstrate that modification of the heparin-binding region of FGF1 significantly improves the cardioprotective efficacy, even in the presence of heparin, identifying a novel FGF ligand available for therapeutic use in ischemic heart disease.	Heparin	173-180	fibroblast growth factor 1	Homo sapiens	90-93
28646555-3	2017	In the present study, heparin was covalently attached to a fibrin mesh grown from a polyvinyl chloride (PVC) substrate surface by the catalytic action of surface immobilized thrombin on a fibrinogen solution.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	174-182
29202212-10	2017	In lung tissue, nebulized heparin attenuated ALI through decreasing procoagulant (tissue factor, thrombin-anti-thrombin complexes, fibrin degradation products) and proinflammatory (interleukin 6, tumour necrosis factor alpha) pathways.	Heparin	26-33	interleukin 6	Rattus norvegicus	181-224
29202212-11	2017	In alveolar macrophages, nebulized heparin reduced expression of procoagulant genes and the effectors of transforming growth factor beta (Smad 2, Smad 3) and nuclear factor kappa B (p-selectin, CCL-2).	Heparin	35-42	SMAD family member 3	Rattus norvegicus	146-152
29202212-11	2017	In alveolar macrophages, nebulized heparin reduced expression of procoagulant genes and the effectors of transforming growth factor beta (Smad 2, Smad 3) and nuclear factor kappa B (p-selectin, CCL-2).	Heparin	35-42	selectin P	Rattus norvegicus	182-192
33440554-0	2017	Fibroblast Growth Factor-1 Released from a Heparin Coacervate Improves Cardiac Function in a Mouse Myocardial Infarction Model.	Heparin	43-50	fibroblast growth factor 1	Mus musculus	0-26
30920532-0	2017	Controlled Release of Vascular Endothelial Growth Factor from Heparin-Functionalized Gelatin Type A and Albumin Hydrogels.	Heparin	62-69	vascular endothelial growth factor A	Homo sapiens	22-56
30920532-2	2017	In this study, we investigated heparin-functionalized hydrogels based on gelatin type A or albumin as storage and release systems for vascular endothelial growth factor (VEGF).	Heparin	31-38	vascular endothelial growth factor A	Homo sapiens	134-168
30920532-2	2017	In this study, we investigated heparin-functionalized hydrogels based on gelatin type A or albumin as storage and release systems for vascular endothelial growth factor (VEGF).	Heparin	31-38	vascular endothelial growth factor A	Homo sapiens	170-174
30920532-12	2017	Both heparin-functionalized biomaterial systems, chemically crosslinked gelatin type A or albumin, had tunable physicochemical properties, and can be considered for controlled delivery of the pro-angiogenic growth factor VEGF.	Heparin	5-12	vascular endothelial growth factor A	Homo sapiens	221-225
29089529-6	2017	Surprisingly, we found that heparin at physiological concentration can enhance HBV infection in a PreS1-peptide sensitive, NTCP-dependent manner in both HepaRG and HepG2-NTCP-AS cells.	Heparin	28-35	solute carrier family 10 member 1	Homo sapiens	123-127
29089529-6	2017	Surprisingly, we found that heparin at physiological concentration can enhance HBV infection in a PreS1-peptide sensitive, NTCP-dependent manner in both HepaRG and HepG2-NTCP-AS cells.	Heparin	28-35	solute carrier family 10 member 1	Homo sapiens	170-174
28872172-5	2017	Interestingly, the naked eye alone can judge the presence of 0.02 muM heparin without the aid of any advanced instruments by color change.	Heparin	70-77	latexin	Homo sapiens	66-69
28230633-13	2017	The proinflammatory tumor necrosis factor (TNF-alpha) reduced by cryotherapy in both cryotherapy groups but Interleukin 1beta was only reduced in heparin group.	Heparin	146-153	interleukin-1 beta	Oryctolagus cuniculus	108-125
28809108-0	2017	Dual Regulations of Thermosensitive Heparin-Poloxamer Hydrogel Using epsilon-Polylysine: Bioadhesivity and Controlled KGF Release for Enhancing Wound Healing of Endometrial Injury.	Heparin	36-43	fibroblast growth factor 7	Homo sapiens	118-121
28870205-10	2017	Heparin in combination with chemotherapy has a synergic effect and could be a treatment choice for HCCs with a high CCN2 expression.	Heparin	0-7	holocytochrome c synthase	Homo sapiens	99-103
28877477-4	2017	Our results support a model whereby heparin competes with insulin for insulin receptor binding on AgRP neurons, and by doing so it inhibits FoxO1 activity to promote AgRP release and feeding.	Heparin	36-43	forkhead box O1	Homo sapiens	140-145
28668641-0	2017	Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability.	Heparin	77-84	serpin family A member 12	Homo sapiens	23-29
28586719-0	2017	A heparin conjugate, LHbisD4, inhibits lymphangiogenesis and attenuates lymph node metastasis by blocking VEGF-C signaling pathway.	Heparin	2-9	vascular endothelial growth factor C	Homo sapiens	106-112
28668641-0	2017	Glycosylation of human vaspin (SERPINA12) and its impact on serpin activity, heparin binding and thermal stability.	Heparin	77-84	serpin family A member 12	Homo sapiens	31-40
29276283-2	2017	Inhibition of thrombin serves as a unique mechanism for anticoagulation when compared to heparin as thrombin serves as the final common pathway for the intrinsic and extrinsic coagulation cascades.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	100-108
28578969-8	2017	The pre-immobilization of heparin in chitosan scaffolds could enhance the stability of subsequently loaded NGF.	Heparin	26-33	nerve growth factor	Homo sapiens	107-110
28442532-7	2017	Our data showed that compared with saline and heparin controls, monotherapy of simvastatin and the adjunctive therapy with simvastatin and heparin significantly improved the thrombus resolution and reduced inflammatory cells migration into the venous wall, the release of the inflammatory cell adhesion molecule (P-selectin), inflammatory chemokine (MCP-1) and pleiotropic proinflammatory cytokines (IL-6) into the blood, and the local expression of P-selectin and MCP-1 in the venous wall.	Heparin	139-146	interleukin-6	Oryctolagus cuniculus	400-404
29181096-0	2017	Structure Activity Relationship of Heparin Mimicking Polymer p(SS-co-PEGMA): Effect of Sulfonation and Polymer Size on FGF2-Receptor Binding.	Heparin	35-42	fibroblast growth factor 2	Homo sapiens	119-123
29181096-2	2017	Heparin, a highly sulfated glycosaminoglycan, is required for FGF2 to bind to its receptor.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	62-66
29181096-3	2017	Therefore, polymeric mimics of heparin are widely studied for their ability to manipulate FGF2-induced biological interactions.	Heparin	31-38	fibroblast growth factor 2	Homo sapiens	90-94
29806444-3	2017	Results: Many growth factors involved in fracture healing especially heparin-binding growth factors, such as fibroblast growth factors, bone morphogenetic protein, and transforming growth factor beta, are connected noncovalently with long HS chains.	Heparin	69-76	transforming growth factor beta 1	Homo sapiens	168-199
28463548-5	2017	In addition, OFA inhibited fragmentation, carbonylation, and nitration of apolipoprotein B-100 (apo B-100) in the oxidized LDL, in which heparin-binding activity of apo B-100 was protected by OFA.	Heparin	137-144	apolipoprotein B	Homo sapiens	74-94
28463548-5	2017	In addition, OFA inhibited fragmentation, carbonylation, and nitration of apolipoprotein B-100 (apo B-100) in the oxidized LDL, in which heparin-binding activity of apo B-100 was protected by OFA.	Heparin	137-144	apolipoprotein B	Homo sapiens	96-105
28463548-5	2017	In addition, OFA inhibited fragmentation, carbonylation, and nitration of apolipoprotein B-100 (apo B-100) in the oxidized LDL, in which heparin-binding activity of apo B-100 was protected by OFA.	Heparin	137-144	apolipoprotein B	Homo sapiens	165-174
27341635-0	2017	Low molecular weight heparin inhibits sickle erythrocyte adhesion to VCAM-1 through VLA-4 blockade in a standardized microfluidic flow adhesion assay.	Heparin	21-28	vascular cell adhesion molecule 1	Homo sapiens	69-75
27715399-7	2017	Further purification of the TSP1-containing high-molecular weight fraction of the BM-MSC secretome with heparin-affinity chromatography recovered bioactivity with highly restricted bands on polyacrylamide gel electrophoresis, determined by mass spectroscopy to be proteolytic fragments of fibronectin (FN).	Heparin	104-111	thrombospondin 1	Homo sapiens	28-32
28316275-10	2017	Furthermore, migration experiments with endothelial cells revealed a relationship between the degree of VEGF retention and migration distance: cells invaded deepest in scaffolds containing a heparin-based depot indicating that the formation of a steep gradient is crucial for cell attraction.	Heparin	191-198	vascular endothelial growth factor A	Homo sapiens	104-108
28624802-0	2017	Heparin-based coacervate of bFGF facilitates peripheral nerve regeneration by inhibiting endoplasmic reticulum stress following sciatic nerve injury.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	28-32
28624802-9	2017	This heparin-based delivery platform leads to increased bFGF loading efficiency and better controls its release, which will provide an effective strategy for peripheral nerve injury regeneration therapy.	Heparin	5-12	fibroblast growth factor 2	Homo sapiens	56-60
29296764-8	2017	Treatment with UFH and LMWH reduced thrombin generation and restored angiogenesis but decreased cell growth.	Heparin	15-18	coagulation factor II, thrombin	Homo sapiens	36-44
28629128-2	2017	The overall structure of the ternary complex Heparin:FGF-1:FGFR has been finally elucidated after some controversy and the interactions within the ternary complex have been deeply described.	Heparin	45-52	fibroblast growth factor 1	Homo sapiens	53-58
28745782-6	2017	At the end of follow-up, the high concentration heparin group had reduced fibrinogen (FIB) and increased D-D compared with the other groups, and the differences were statistically significant (p&lt;0.05).	Heparin	48-55	fibrinogen beta chain	Homo sapiens	74-84
28745782-6	2017	At the end of follow-up, the high concentration heparin group had reduced fibrinogen (FIB) and increased D-D compared with the other groups, and the differences were statistically significant (p&lt;0.05).	Heparin	48-55	fibrinogen beta chain	Homo sapiens	86-89
28498476-0	2017	Effects of unfractionated heparin and rivaroxaban on the expression of heparanase and fibroblast growth factor 2 in human osteoblasts.	Heparin	26-33	heparanase	Homo sapiens	71-81
28498476-0	2017	Effects of unfractionated heparin and rivaroxaban on the expression of heparanase and fibroblast growth factor 2 in human osteoblasts.	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	86-112
28498476-4	2017	Therefore, the present study was designed to investigate the effects of unfractionated heparin and rivaroxaban on the expression of HPSE and FGF2 in human osteoblasts.	Heparin	87-94	heparanase	Homo sapiens	132-136
28498476-4	2017	Therefore, the present study was designed to investigate the effects of unfractionated heparin and rivaroxaban on the expression of HPSE and FGF2 in human osteoblasts.	Heparin	87-94	fibroblast growth factor 2	Homo sapiens	141-145
28498476-8	2017	Unfractionated heparin alone significantly inhibited the expression of HPSE and FGF2, whereas rivaroxaban inhibited the expression of FGF2 without affecting that of HPSE.	Heparin	15-22	heparanase	Homo sapiens	71-75
28498476-8	2017	Unfractionated heparin alone significantly inhibited the expression of HPSE and FGF2, whereas rivaroxaban inhibited the expression of FGF2 without affecting that of HPSE.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	80-84
28498476-9	2017	Furthermore, the overexpression of HPSE or FGF2 significantly reversed the inhibitory effects of unfractionated heparin and rivaroxaban on osteoblasts.	Heparin	112-119	heparanase	Homo sapiens	35-39
28498476-9	2017	Furthermore, the overexpression of HPSE or FGF2 significantly reversed the inhibitory effects of unfractionated heparin and rivaroxaban on osteoblasts.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	43-47
28498476-10	2017	These findings suggested that HPSE and FGF2 signals were involved in the detrimental role of unfractionated heparin and rivaroxaban in human osteoblasts, providing novel information on the side effects of anticoagulants.	Heparin	108-115	heparanase	Homo sapiens	30-34
28498476-10	2017	These findings suggested that HPSE and FGF2 signals were involved in the detrimental role of unfractionated heparin and rivaroxaban in human osteoblasts, providing novel information on the side effects of anticoagulants.	Heparin	108-115	fibroblast growth factor 2	Homo sapiens	39-43
28561086-5	2017	Here, we showed that the heparin-mimetic PA gel can support tissue neovascularization, enhance the deposition of collagen and expression of alpha-smooth muscle actin (alpha-SMA), and eliminate the sustained presence of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) in the diabetic wound site.	Heparin	25-32	actin alpha 2, smooth muscle, aorta	Mus musculus	140-165
28561086-5	2017	Here, we showed that the heparin-mimetic PA gel can support tissue neovascularization, enhance the deposition of collagen and expression of alpha-smooth muscle actin (alpha-SMA), and eliminate the sustained presence of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) in the diabetic wound site.	Heparin	25-32	actin alpha 2, smooth muscle, aorta	Mus musculus	167-176
28561086-5	2017	Here, we showed that the heparin-mimetic PA gel can support tissue neovascularization, enhance the deposition of collagen and expression of alpha-smooth muscle actin (alpha-SMA), and eliminate the sustained presence of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) in the diabetic wound site.	Heparin	25-32	interleukin 6	Mus musculus	219-232
28561086-5	2017	Here, we showed that the heparin-mimetic PA gel can support tissue neovascularization, enhance the deposition of collagen and expression of alpha-smooth muscle actin (alpha-SMA), and eliminate the sustained presence of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) in the diabetic wound site.	Heparin	25-32	interleukin 6	Mus musculus	234-238
28561086-5	2017	Here, we showed that the heparin-mimetic PA gel can support tissue neovascularization, enhance the deposition of collagen and expression of alpha-smooth muscle actin (alpha-SMA), and eliminate the sustained presence of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) in the diabetic wound site.	Heparin	25-32	tumor necrosis factor	Mus musculus	244-271
28561086-5	2017	Here, we showed that the heparin-mimetic PA gel can support tissue neovascularization, enhance the deposition of collagen and expression of alpha-smooth muscle actin (alpha-SMA), and eliminate the sustained presence of interleukin-6 (IL-6) and tumor necrosis factor-alpha (TNF-alpha) in the diabetic wound site.	Heparin	25-32	tumor necrosis factor	Mus musculus	273-282
28623309-4	2017	We here show that high directional persistence necessitates a combination of the cell-binding and C-terminal heparin-binding domains of FN, but does not require the engagement of syndecan-4 or integrin alpha4beta1.	Heparin	109-116	fibronectin 1	Homo sapiens	136-138
28662704-1	2017	BACKGROUND: Vitamin K inhibitors (e.g. warfarin) and indirect thrombin inhibitors (e.g. heparin) are widely used to prevent thromboembolic disorders (e.g. myocardial infarction, venous thromboembolism, and stroke).	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	62-70
27975162-0	2017	The regulatory role of heparin on c-Met signaling in hepatocellular carcinoma cells.	Heparin	23-30	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	34-39
28289828-0	2017	Is low serum albumin level a significant predictor for the development of heparin-induced thrombocytopenia-thrombosis?	Heparin	74-81	albumin	Homo sapiens	13-20
28289828-1	2017	The present study investigates the effect of albumin levels in patients who have developed heparin-induced thrombocytopenia (HIT) and heparin-induced thrombocytopenia-thrombosis (HITT).	Heparin	91-98	albumin	Homo sapiens	45-52
28428352-5	2017	RESULTS: The comparison of cTnT isolated from AMI heparin plasma and serum samples showed that cTnT in the plasma samples was mainly present as the full-sized molecule (approximately 35 kDa), while in serum samples it was present as a 29-kDa fragment.	Heparin	50-57	troponin T2, cardiac type	Homo sapiens	27-31
28428352-5	2017	RESULTS: The comparison of cTnT isolated from AMI heparin plasma and serum samples showed that cTnT in the plasma samples was mainly present as the full-sized molecule (approximately 35 kDa), while in serum samples it was present as a 29-kDa fragment.	Heparin	50-57	troponin T2, cardiac type	Homo sapiens	95-99
33429571-2	2017	A single molecular analysis served as a basis to decipher the nanomechanical mechanism of the interaction between FGF-2 and the heparan sulfate surrogate, heparin, with a modular atomic force microscope (AFM) design combining magnetic actuators with force measurements at the low force regime (1 x 101 to 1 x 104 pN/s).	Heparin	155-162	fibroblast growth factor 2	Homo sapiens	114-119
33429571-3	2017	Unbinding events between FGF-2-heparin complexes were specific and short-lived.	Heparin	31-38	fibroblast growth factor 2	Homo sapiens	25-30
33429571-4	2017	Binding between FGF-2 and heparin had strong slip bond characteristics as demonstrated by a decrease of lifetime with tensile force on the complex.	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	16-21
33429571-6	2017	An acidic pH environment (5.5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	41-46
33429571-6	2017	An acidic pH environment (5.5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	124-129
33429571-6	2017	An acidic pH environment (5.5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	124-129
33429571-6	2017	An acidic pH environment (5.5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions.	Heparin	139-146	fibroblast growth factor 2	Homo sapiens	41-46
33429571-6	2017	An acidic pH environment (5.5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions.	Heparin	139-146	fibroblast growth factor 2	Homo sapiens	124-129
33429571-6	2017	An acidic pH environment (5.5) modulated FGF-2-heparin binding as demonstrated by enhanced rupture forces needed to release FGF-2 from the heparin-FGF-2 complex as compared to physiological conditions.	Heparin	139-146	fibroblast growth factor 2	Homo sapiens	124-129
28366713-0	2017	Influence of Heparin on the Fibrinogen Level Measured by the Prothrombin Time-Derived Method During Cardiac Surgery With Cardiopulmonary Bypass.	Heparin	13-20	fibrinogen beta chain	Homo sapiens	28-38
27975162-5	2017	In the absence of HGF, heparin activated HGF/c-Met signaling and promoted motility and invasion in HCC cells.	Heparin	23-30	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	45-50
27975162-6	2017	Heparin treatment led to c-Met receptor dimerization and activated c-Met signaling in an HGF independent manner.	Heparin	0-7	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	25-30
27975162-6	2017	Heparin treatment led to c-Met receptor dimerization and activated c-Met signaling in an HGF independent manner.	Heparin	0-7	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	67-72
27975162-7	2017	Heparin-induced c-Met activation increased migration and invasion through ERK1/2, early growth response factor 1 (EGR1) and Matrix Metalloproteinases (MMP) axis.	Heparin	0-7	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	16-21
27975162-7	2017	Heparin-induced c-Met activation increased migration and invasion through ERK1/2, early growth response factor 1 (EGR1) and Matrix Metalloproteinases (MMP) axis.	Heparin	0-7	mitogen-activated protein kinase 3	Homo sapiens	74-80
27975162-8	2017	Interestingly, heparin modestly decreased the proliferation of HCC cells by inhibiting activatory phosphorylation of Akt.	Heparin	15-22	AKT serine/threonine kinase 1	Homo sapiens	117-120
27975162-9	2017	The inhibition of c-Met signaling reversed heparin-induced increase in motility and invasion and, proliferation inhibition.	Heparin	43-50	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	18-23
27975162-10	2017	Our study provides a new perspective into the role of heparin on c-Met signaling in HCC.	Heparin	54-61	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	65-70
28397565-1	2017	OBJECTIVE: This study describes a case of a successful free flap repair using argatroban for local intraluminal irrigation as a substitute to heparin in a patient with heparin-induced thrombocytopenia.	Heparin	142-149	arachidonate 5-lipoxygenase activating protein	Homo sapiens	60-64
28565914-1	2017	The heparin binding site (Hep II) of fibronectin plays a major role in tumor cell metastasis.	Heparin	4-11	fibronectin 1	Homo sapiens	37-48
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	tumor necrosis factor	Homo sapiens	60-69
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	interleukin 6	Homo sapiens	74-78
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	interleukin 6	Homo sapiens	199-203
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	C-X-C motif chemokine ligand 8	Homo sapiens	215-219
28397565-0	2017	Local Intraluminal Irrigation With Argatroban During Free Flap Repair in a Patient With Heparin-Induced Thrombocytopenia.	Heparin	88-95	arachidonate 5-lipoxygenase activating protein	Homo sapiens	58-62
28397565-1	2017	OBJECTIVE: This study describes a case of a successful free flap repair using argatroban for local intraluminal irrigation as a substitute to heparin in a patient with heparin-induced thrombocytopenia.	Heparin	168-175	arachidonate 5-lipoxygenase activating protein	Homo sapiens	60-64
28279966-10	2017	Finally, we demonstrate that VWF susceptibility to plasmin proteolysis at K1491-R1492 is modulated by local N-linked glycan expression within A1A2A3, and specifically inhibited by heparin binding to the A1 domain.	Heparin	180-187	von Willebrand factor	Homo sapiens	29-32
28043992-11	2017	Conclusions: Direct thrombin and FXa inhibitors exhibit distinct effects on assay results when used concomitantly with heparins.	Heparin	119-127	coagulation factor II, thrombin	Homo sapiens	20-28
28413728-10	2017	In consistent with the attenuation of [Ca2+]i elevation, we found that Akt/eNOS phosphorylation was also dramatically decreased by Heparin or PKC 412, but not affected by Nifedipine or H89.	Heparin	131-138	AKT serine/threonine kinase 1	Homo sapiens	71-74
28174207-7	2017	Heparan sulfate proteoglycans and heparin derivatives further enhance HBEGF-induced differentiation by forming a complex with the epidermal growth factor receptor, leading to activation of the ERK1/2 and STAT3 pathways and up-regulation of the inhibitor of DNA binding transcription factor.	Heparin	34-41	epidermal growth factor receptor	Homo sapiens	130-162
28174207-7	2017	Heparan sulfate proteoglycans and heparin derivatives further enhance HBEGF-induced differentiation by forming a complex with the epidermal growth factor receptor, leading to activation of the ERK1/2 and STAT3 pathways and up-regulation of the inhibitor of DNA binding transcription factor.	Heparin	34-41	mitogen-activated protein kinase 3	Homo sapiens	193-199
28174207-7	2017	Heparan sulfate proteoglycans and heparin derivatives further enhance HBEGF-induced differentiation by forming a complex with the epidermal growth factor receptor, leading to activation of the ERK1/2 and STAT3 pathways and up-regulation of the inhibitor of DNA binding transcription factor.	Heparin	34-41	signal transducer and activator of transcription 3	Homo sapiens	204-209
28468283-1	2017	Of the circa 40 cytokines of the TGF-beta superfamily, around a third are currently known to bind to heparin and heparan sulphate.	Heparin	101-108	transforming growth factor beta 1	Homo sapiens	33-41
28445754-8	2017	Antithrombin (2.6 muM) plus heparin (4 U/mL) inhibits 72% of the active clot-bound thrombin after ~10 min at 92 s-1, while no inhibition is observed in the absence of heparin.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	4-12
28209711-7	2017	Binding of Hic to hTSP-1 is inhibited by heparin and chondroitin sulfate A, indicating binding to the N-terminal globular domain or type I repeats of hTSP-1.	Heparin	41-48	thrombospondin 1	Homo sapiens	18-24
28052306-3	2017	The parenteral direct thrombin inhibitors (DTIs) can be used in a variety of settings, including heparin-induced thrombocytopenia (HIT) or an allergy to heparin, and patients requiring anticoagulation for an invasive cardiovascular intervention.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	22-30
28007564-2	2017	The mechanism for heparin"s anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	231-266
28052306-3	2017	The parenteral direct thrombin inhibitors (DTIs) can be used in a variety of settings, including heparin-induced thrombocytopenia (HIT) or an allergy to heparin, and patients requiring anticoagulation for an invasive cardiovascular intervention.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	22-30
27899064-0	2017	Growth Differentiation Factor 5-Mediated Enhancement of Chondrocyte Phenotype Is Inhibited by Heparin: Implications for the Use of Heparin in the Clinic and in Tissue Engineering Applications.	Heparin	94-101	growth differentiation factor 5	Homo sapiens	0-31
27899064-0	2017	Growth Differentiation Factor 5-Mediated Enhancement of Chondrocyte Phenotype Is Inhibited by Heparin: Implications for the Use of Heparin in the Clinic and in Tissue Engineering Applications.	Heparin	131-138	growth differentiation factor 5	Homo sapiens	0-31
27899064-2	2017	Growth differentiation factor 5 (GDF5) belongs to the bone morphogenetic protein family of proteins and is vital for skeletal formation; however, its interaction with heparin and heparan sulfate (HS) has not been studied.	Heparin	167-174	growth differentiation factor 5	Homo sapiens	0-31
27899064-2	2017	Growth differentiation factor 5 (GDF5) belongs to the bone morphogenetic protein family of proteins and is vital for skeletal formation; however, its interaction with heparin and heparan sulfate (HS) has not been studied.	Heparin	167-174	growth differentiation factor 5	Homo sapiens	33-37
27899064-4	2017	Clinically relevant doses of heparin (&gt;=10 nM), but not equivalent concentrations of HS, were found to inhibit GDF5"s biological activity in both human mesenchymal stem/stromal cell-derived chondrocyte pellet cultures and the skeletal cell line ATDC5.	Heparin	29-36	growth differentiation factor 5	Homo sapiens	114-118
27899064-5	2017	We also found that heparin inhibited both GDF5 binding to cell surface HS and GDF5-induced induction of Smad 1/5/8 signaling.	Heparin	19-26	growth differentiation factor 5	Homo sapiens	42-46
27899064-5	2017	We also found that heparin inhibited both GDF5 binding to cell surface HS and GDF5-induced induction of Smad 1/5/8 signaling.	Heparin	19-26	growth differentiation factor 5	Homo sapiens	78-82
27992182-7	2017	We propose a model for apoA-I aggregation in which perturbations of a four-helix bundle-like structure, induced by interactions of heparin or methionine oxidation, cause the partially helical N-terminal residues to disengage from the remaining, intact helices, thereby allowing self-assembly via beta-strand associations.	Heparin	131-138	apolipoprotein A1	Homo sapiens	23-29
28104757-2	2017	Similar to the BMP ligands, certain DAN family members have been shown to interact with heparin and heparan sulfate (HS).	Heparin	88-95	NBL1, DAN family BMP antagonist	Homo sapiens	36-39
27992182-0	2017	Heparin and Methionine Oxidation Promote the Formation of Apolipoprotein A-I Amyloid Comprising alpha-Helical and beta-Sheet Structures.	Heparin	0-7	apolipoprotein A1	Homo sapiens	58-76
28063222-5	2017	As a proxy for gliotransmission, we found that long-term potentiation (LTP) was impaired by dialyzing astrocytes with the broad IP3 R blocker heparin, and rescued by exogenous d-serine, indicating that astrocytic IP3 Rs regulate d-serine release.	Heparin	142-149	inositol 1,4,5-triphosphate receptor 2	Mus musculus	128-133
28282887-0	2017	New Insights in Thrombin Inhibition Structure-Activity Relationships by Characterization of Octadecasaccharides from Low Molecular Weight Heparin.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	16-24
28181797-0	2017	A Thermosensitive Heparin-Poloxamer Hydrogel Bridges aFGF to Treat Spinal Cord Injury.	Heparin	18-25	fibroblast growth factor 1	Homo sapiens	53-57
27291835-6	2017	This process used a peptide sequence derived from the heparin-binding domain of FGF2 as a substrate to affinity-isolate HS8 from a commercially available source of porcine mucosal HS.	Heparin	54-61	fibroblast growth factor 2	Homo sapiens	80-84
27878865-2	2017	The members of this subfamily, FGF19, FGF21 and FGF23, are characterized by their reduced binding affinity for heparin that enables them to be transported in the circulation and function in an endocrine manner.	Heparin	111-118	fibroblast growth factor 21	Homo sapiens	38-43
28205621-2	2017	Here we propose an innovative immunotherapeutic organoid by housing human mesenchymal stromal cells (MSCs), gene-modified for the secretion of an anti-CD33-anti-CD3 bispecific antibody (bsAb), in a small biocompatible star-shaped poly(ethylene glycol)-heparin cryogel scaffold as a transplantable and low invasive therapeutic machinery for the treatment of acute myeloid leukemia (AML).	Heparin	252-259	CD33 molecule	Homo sapiens	151-155
28414674-15	2017	Suppression of TNF-alpha expression by low molecular weight heparin has been shown to inhibit the inflammatory cascade and reduce thrombus formation in animal models.	Heparin	60-67	tumor necrosis factor	Homo sapiens	15-24
32263874-4	2017	Indomethacin (IMC) and/or basic fibroblast growth factor (bFGF) are/is entrapped into the PECL micelle cross-linked hydrogel network primarily through hydrophobic interaction and specific affinity to thiolated heparin, respectively.	Heparin	210-217	fibroblast growth factor 2	Homo sapiens	26-63
28199387-7	2017	The competitive effect of heparin on DS binding to TG2 suggests that both glycosaminoglycans occupy the same binding site(s) on the protein molecule.	Heparin	26-33	transglutaminase 2	Homo sapiens	51-54
28181209-8	2017	Pre-loading of the scaffolds with VEGF influenced formation and stability of the pre-vascular structures depending on the presence of heparin: In heparin-free scaffolds, induction of tubule formation and sprouting was more pronounced whereas heparin-modified scaffolds seemed to promote stabilisation of the pre-vascular structures.	Heparin	134-141	vascular endothelial growth factor A	Homo sapiens	34-38
28181209-8	2017	Pre-loading of the scaffolds with VEGF influenced formation and stability of the pre-vascular structures depending on the presence of heparin: In heparin-free scaffolds, induction of tubule formation and sprouting was more pronounced whereas heparin-modified scaffolds seemed to promote stabilisation of the pre-vascular structures.	Heparin	146-153	vascular endothelial growth factor A	Homo sapiens	34-38
28181209-8	2017	Pre-loading of the scaffolds with VEGF influenced formation and stability of the pre-vascular structures depending on the presence of heparin: In heparin-free scaffolds, induction of tubule formation and sprouting was more pronounced whereas heparin-modified scaffolds seemed to promote stabilisation of the pre-vascular structures.	Heparin	146-153	vascular endothelial growth factor A	Homo sapiens	34-38
27881214-3	2017	SOD3 has the heparin binding domain associating cell surface.	Heparin	13-20	superoxide dismutase 3	Homo sapiens	0-4
27881214-4	2017	Interestingly, we found that Zn2+ promotes transduction effects of recombinant human SOD3 (rhSOD3) by increasing uptake via the heparin binding domain (HBD).	Heparin	128-135	superoxide dismutase 3	Homo sapiens	85-89
28178124-1	2017	RATIONALE: The case reported the rapid remission of disease recurrence achieved adding foscarnet, a DNA polymerase inhibitor that interacts with fibroblast growth factor 2, to low molecular weight heparin and sunitinib for the first time in a patient with an anaplastic thyroid cancer (ATC).	Heparin	197-204	fibroblast growth factor 2	Homo sapiens	145-171
28067354-0	2017	Heparin acts as a structural component of beta-endorphin amyloid fibrils rather than a simple aggregation promoter.	Heparin	0-7	proopiomelanocortin	Homo sapiens	42-56
28067354-3	2017	In the case of the neuropeptide beta-endorphin that can reversibly adopt a functional amyloid form in nature, aggregation in the presence of heparin leads to a loss of function.	Heparin	141-148	proopiomelanocortin	Homo sapiens	32-46
28067354-4	2017	Applying correlative optical super-resolution microscopy methods, we show that heparin incorporates into emerging beta-endorphin fibrils forming an integral component and is essential for amyloid templating.	Heparin	79-86	proopiomelanocortin	Homo sapiens	114-128
27885722-1	2017	A thrombin-responsive closed-loop patch is developed for prolonged heparin delivery in a feedback-controlled manner.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	2-10
27992192-7	2017	The heparin-treated Tr4 polyplexes exhibited more than 50% higher cellular internalization with HepG2 cells while showing minimal increases with U87 and primary fibroblasts.	Heparin	4-11	nuclear receptor subfamily 2 group C member 2	Homo sapiens	20-23
27992192-10	2017	Heparin appears to also modify the nuclear localization behavior of Tr4 polyplexes, which likely contributes to increased efficiency and transgene expression.	Heparin	0-7	nuclear receptor subfamily 2 group C member 2	Homo sapiens	68-71
27885722-3	2017	This "smart" heparin patch can be transcutaneously inserted into skin without drug leakage and can sustainably regulate blood coagulation in response to thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	153-161
27741500-3	2017	We show that compliant starPEG-heparin matrices promote the development of polarized MEC acini.	Heparin	31-38	C-C motif chemokine ligand 28	Homo sapiens	85-88
27741500-4	2017	Both the presence of heparin and MMP-cleavable crosslinks are essential in facilitating MEC morphogenesis without supplementation of exogenous adhesion ligands.	Heparin	21-28	C-C motif chemokine ligand 28	Homo sapiens	88-91
27224670-10	2017	In the heparin cohort, CDH5 was stable over time whereas FABP1 was elevated.	Heparin	7-14	cadherin 5	Homo sapiens	23-27
27758044-2	2017	Heparanase accomplishes this by degrading heparan sulfate which regulates the abundance and location of heparin-binding growth factors thereby influencing multiple signaling pathways that control gene expression, syndecan shedding and cell behavior.	Heparin	104-111	heparanase	Homo sapiens	0-10
27323268-5	2017	Instead, their data demonstrate the effect of heparin addition and changing ECM stiffness on both VEGF binding to fibronectin and VEGF binding to endothelial receptors.	Heparin	46-53	vascular endothelial growth factor A	Homo sapiens	98-102
27798934-6	2017	Using recombinant fragments of Vn, we found the C-terminal part of Vn, including heparin-binding domain 3, to be responsible for binding to YadA.	Heparin	81-88	Adhesin	Yersinia enterocolitica	140-144
27770914-8	2017	As compared to the pristine magnesium alloy, the samples modified by the immobilization of PEG and fibronectin/heparin complex presented better blood compatibility according to the results of hemolysis assay and platelet adhesion as well as the activated partial thromboplastin time (APTT).	Heparin	111-118	fibronectin 1	Homo sapiens	99-110
27917715-4	2017	The direct oral anticoagulants (DOACs) inhibiting factor Xa or thrombin activity represent an alternative for heparins and VKAs.	Heparin	110-118	coagulation factor II, thrombin	Homo sapiens	63-71
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	157-164	CREB binding protein	Homo sapiens	131-134
28744338-2	2017	Kallistatin via its heparin-binding site inhibits vascular inflammation and oxidative stress by antagonizing TNF-alpha-induced NADPH oxidase activity, NF-kappaB activation, and inflammatory gene expression in endothelial cells.	Heparin	20-27	tumor necrosis factor	Mus musculus	109-118
28170190-6	2017	Delivery of IFN-gamma via heparin-microparticles within MSC aggregates induced sustained IDO expression during 1 week of culture, whereas IDO expression by IFN-gamma-pretreated MSC spheroids rapidly decreased during 2 days.	Heparin	26-33	interferon gamma	Homo sapiens	12-21
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	139-146	CREB binding protein	Homo sapiens	105-129
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	139-146	CREB binding protein	Homo sapiens	131-134
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	139-146	CREB binding protein	Homo sapiens	177-180
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	157-164	CREB binding protein	Homo sapiens	105-129
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	157-164	CREB binding protein	Homo sapiens	177-180
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	157-164	CREB binding protein	Homo sapiens	131-134
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	157-164	CREB binding protein	Homo sapiens	177-180
27936727-3	2016	Modification of ECM with CBP-heparin leads to increased deposition of functional heparin (by ~7.2-fold measured by glycosaminoglycan composition) and a corresponding reduction in platelet binding (&gt;70%) and whole blood clotting (&gt;80%) onto the ECM.	Heparin	29-36	CREB binding protein	Homo sapiens	25-28
27936727-2	2016	Here we describe an easy-to-implement strategy to chemically modify vascular ECM by covalently linking a collagen binding peptide (CBP) to heparin to form a heparin derivative (CBP-heparin) that selectively binds a subset of collagens.	Heparin	157-164	CREB binding protein	Homo sapiens	105-129
27936727-3	2016	Modification of ECM with CBP-heparin leads to increased deposition of functional heparin (by ~7.2-fold measured by glycosaminoglycan composition) and a corresponding reduction in platelet binding (&gt;70%) and whole blood clotting (&gt;80%) onto the ECM.	Heparin	81-88	CREB binding protein	Homo sapiens	25-28
27936727-4	2016	Furthermore, addition of CBP-heparin to the ECM stabilizes long-term endothelial cell attachment to the lumen of ECM-derived vascular conduits, potentially through recruitment of heparin-binding growth factors that ultimately improve the durability of endothelialization in vitro.	Heparin	29-36	CREB binding protein	Homo sapiens	25-28
27936727-4	2016	Furthermore, addition of CBP-heparin to the ECM stabilizes long-term endothelial cell attachment to the lumen of ECM-derived vascular conduits, potentially through recruitment of heparin-binding growth factors that ultimately improve the durability of endothelialization in vitro.	Heparin	179-186	CREB binding protein	Homo sapiens	25-28
28057952-11	2016	Conclusion: Direct thrombin inhibitors may be subject to resistance mechanisms similar to those previously described in patients receiving heparin.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	19-27
27860466-4	2016	Heparin-containing hydrogels retain significantly higher amounts of the Interleukin-4 protein thus exhibiting a significantly higher specific activity than the heparin-free controls.	Heparin	0-7	interleukin 4	Homo sapiens	72-85
27860466-4	2016	Heparin-containing hydrogels retain significantly higher amounts of the Interleukin-4 protein thus exhibiting a significantly higher specific activity than the heparin-free controls.	Heparin	160-167	interleukin 4	Homo sapiens	72-85
27782377-3	2016	WFIKKN1 was found to have no effect on processing of promyostatin by furin, the rate of cleavage of latent myostatin by BMP1, however, was significantly enhanced in the presence of WFIKKN1 and this enhancer activity was superstimulated by heparin.	Heparin	239-246	WAP, follistatin/kazal, immunoglobulin, kunitz and netrin domain containing 1	Homo sapiens	181-188
27459086-4	2016	We hypothesized that DLS-immobilized heparin acts as an antithrombotic coating reagent and binds vascular endothelial growth factor (VEGF) to induce angiogenesis in the DLSs.	Heparin	37-44	vascular endothelial growth factor A	Homo sapiens	97-131
27459086-4	2016	We hypothesized that DLS-immobilized heparin acts as an antithrombotic coating reagent and binds vascular endothelial growth factor (VEGF) to induce angiogenesis in the DLSs.	Heparin	37-44	vascular endothelial growth factor A	Homo sapiens	133-137
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	85-93
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	275-282	coagulation factor II, thrombin	Homo sapiens	85-93
27862941-8	2016	The effect of heparin is almost entirely due to anti-thrombin action (B guin), so anti-factor Xa activity does not reflect the concentration of anticoagulant heparin.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	53-61
28101211-1	2016	Fibroblast growth factor receptor-like 1 (FGFRL1) is a transmembrane receptor that interacts with heparin and FGF ligands.	Heparin	98-105	fibroblast growth factor receptor-like 1	Mus musculus	0-40
28101211-1	2016	Fibroblast growth factor receptor-like 1 (FGFRL1) is a transmembrane receptor that interacts with heparin and FGF ligands.	Heparin	98-105	fibroblast growth factor receptor-like 1	Mus musculus	42-48
27681598-0	2016	Heparin Binds Lamprey Angiotensinogen and Promotes Thrombin Inhibition through a Template Mechanism.	Heparin	0-7	angiotensinogen	Homo sapiens	22-37
27604259-6	2016	The thrombin-AT complex formation, as determined by enzyme-linked immunosorbent assay, was reduced with all tested variants in the presence and absence of heparin.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	4-12
27681598-0	2016	Heparin Binds Lamprey Angiotensinogen and Promotes Thrombin Inhibition through a Template Mechanism.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	51-59
27681598-2	2016	The detailed mechanisms on how angiotensin is carried by l-ANT and how heparin binds l-ANT and mediates thrombin inhibition are unclear.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	104-112
27681598-7	2016	Although l-ANT by itself is a poor thrombin inhibitor with a second order rate constant of 500 m-1 s-1, its interaction with thrombin is accelerated 90-fold by high molecular weight heparin following a bell-shaped dose-dependent curve.	Heparin	182-189	coagulation factor II, thrombin	Homo sapiens	125-133
27681598-9	2016	Furthermore, an l-ANT mutant with the P1 Ile mutated to Arg inhibits thrombin nearly 1500-fold faster than the wild type, which is further accelerated by high molecular weight heparin.	Heparin	176-183	coagulation factor II, thrombin	Homo sapiens	69-77
27681598-10	2016	Taken together, these results suggest that heparin binds l-ANT at a conserved heparin binding site around helix D and promotes the interaction between l-ANT and thrombin through a template mechanism conserved in vertebrates.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	161-169
27808176-3	2016	FN homes several binding sites for sulfated glycosaminoglycans (sGAG), such as heparin (Hep), which was previously shown to influence FN conformation and protein binding.	Heparin	79-86	fibronectin 1	Homo sapiens	0-2
27895888-0	2016	In situ formation of poly(vinyl alcohol)-heparin hydrogels for mild encapsulation and prolonged release of basic fibroblast growth factor and vascular endothelial growth factor.	Heparin	41-48	vascular endothelial growth factor A	Homo sapiens	142-176
27895888-4	2016	Both basic fibroblast growth factor and vascular endothelial growth factor were encapsulated in poly(vinyl alcohol)-heparin hydrogels and demonstrated controlled release.	Heparin	116-123	vascular endothelial growth factor A	Homo sapiens	40-74
27895888-7	2016	The release of vascular endothelial growth factor from poly(vinyl alcohol)-heparin hydrogels promoted human umbilical vein endothelial cell outgrowth but not significant proliferation.	Heparin	75-82	vascular endothelial growth factor A	Homo sapiens	15-49
27895888-8	2016	Dual-growth factor release of basic fibroblast growth factor and vascular endothelial growth factor from poly(vinyl alcohol)-heparin hydrogels resulted in a synergistic effect with significantly higher human umbilical vein endothelial cell outgrowth compared to basic fibroblast growth factor or vascular endothelial growth factor alone.	Heparin	125-132	vascular endothelial growth factor A	Homo sapiens	65-99
27895888-8	2016	Dual-growth factor release of basic fibroblast growth factor and vascular endothelial growth factor from poly(vinyl alcohol)-heparin hydrogels resulted in a synergistic effect with significantly higher human umbilical vein endothelial cell outgrowth compared to basic fibroblast growth factor or vascular endothelial growth factor alone.	Heparin	125-132	vascular endothelial growth factor A	Homo sapiens	296-330
29296696-8	2016	Platelets activated by subaggregating doses of thrombin receptor activating peptide release polyphosphates and PF4, which form antigenic complexes that allow KKO to further activate platelets in the absence of heparin and exogenous PF4.	Heparin	210-217	coagulation factor II, thrombin	Homo sapiens	47-55
29296696-9	2016	These studies suggest that thrombin- or immune complex-mediated release of endogenous antigenic PF4/polyphosphate complexes from platelets may augment the prothrombotic risk of HIT and perpetuate the risk of thrombosis after heparin has been discontinued.	Heparin	225-232	coagulation factor II, thrombin	Homo sapiens	27-35
27808176-3	2016	FN homes several binding sites for sulfated glycosaminoglycans (sGAG), such as heparin (Hep), which was previously shown to influence FN conformation and protein binding.	Heparin	79-86	fibronectin 1	Homo sapiens	134-136
27445159-2	2016	Here we report the biosynthesis of heparin-like heparan sulfate via the recombinant expression of human serglycin in human cells.	Heparin	35-42	serglycin	Homo sapiens	104-113
27566697-3	2016	Aims of the present study are (1) to evaluate a possible role of low-molecular-weight-heparins (LMWHs) in the modulation of the expression of TF, TFPI, TFPI2 and VEGF in placentae from thrombophilic women and (2) to study the possible role of endothelium in the placental expression of markers involved in haemostasis and angiogenesis.	Heparin	86-94	tissue factor pathway inhibitor 2	Homo sapiens	152-157
27566697-3	2016	Aims of the present study are (1) to evaluate a possible role of low-molecular-weight-heparins (LMWHs) in the modulation of the expression of TF, TFPI, TFPI2 and VEGF in placentae from thrombophilic women and (2) to study the possible role of endothelium in the placental expression of markers involved in haemostasis and angiogenesis.	Heparin	86-94	vascular endothelial growth factor A	Homo sapiens	162-166
27445159-4	2016	The recombinantly expressed serglycin produced with 25mM glucose present in the culture medium was found to possess anticoagulant activity one-seventh of that of porcine unfractionated heparin, demonstrating that bioengineered human heparin-like heparan sulfate may be a safe next-generation pharmaceutical heparin.	Heparin	233-240	serglycin	Homo sapiens	28-37
27445159-4	2016	The recombinantly expressed serglycin produced with 25mM glucose present in the culture medium was found to possess anticoagulant activity one-seventh of that of porcine unfractionated heparin, demonstrating that bioengineered human heparin-like heparan sulfate may be a safe next-generation pharmaceutical heparin.	Heparin	233-240	serglycin	Homo sapiens	28-37
27445159-4	2016	The recombinantly expressed serglycin produced with 25mM glucose present in the culture medium was found to possess anticoagulant activity one-seventh of that of porcine unfractionated heparin, demonstrating that bioengineered human heparin-like heparan sulfate may be a safe next-generation pharmaceutical heparin.	Heparin	185-192	serglycin	Homo sapiens	28-37
27474542-0	2016	Low anticoagulant heparin oligosaccharides as inhibitors of BACE-1, the Alzheimer"s beta-secretase.	Heparin	18-25	beta-secretase 1	Homo sapiens	60-66
27783649-7	2016	Further, we found that exosome-fibronectin binding is heparan sulfate-dependent, consistent with our observation that trabecular meshwork exosomes are enriched in the heparin/heparan sulfate binding annexins A2 and A6.	Heparin	167-174	fibronectin 1	Homo sapiens	31-42
27602496-5	2016	Unlike the anticoagulant Fondaparinux, an inhibitor of thrombin generation, the low-molecular-weight heparin (LMWH) Tinzaparin inhibited VWF fiber formation and vessel occlusion in tumor vessels by blocking thrombin-induced EC activation and vascular endothelial growth factor-A (VEGF-A)-mediated VWF release.	Heparin	101-108	coagulation factor II	Mus musculus	207-215
27762591-6	2016	The effective binding of FGF-2 by the heparin-terminated film suggested that other interactions could also contribute to the adsorption process.	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	25-30
27580376-0	2016	A Heparin-Mimicking Block Copolymer Both Stabilizes and Increases the Activity of Fibroblast Growth Factor 2 (FGF2).	Heparin	2-9	fibroblast growth factor 2	Homo sapiens	82-108
27535051-12	2016	A higher apoE level on LVPs conferred more efficient LVP attachment to both the cell surface and heparin beads.	Heparin	97-104	apolipoprotein E	Homo sapiens	9-13
27580376-0	2016	A Heparin-Mimicking Block Copolymer Both Stabilizes and Increases the Activity of Fibroblast Growth Factor 2 (FGF2).	Heparin	2-9	fibroblast growth factor 2	Homo sapiens	110-114
27580376-4	2016	Here we report a heparin mimicking block copolymer, poly(styrenesulfonate-co-poly(ethylene glycol) methyl ether methacrylate)-b-vinyl sulfonate) (p(SS-co-PEGMA)-b-VS, that contains a segment that enhances the stability of FGF2 and one that binds to the FGF2 receptor.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	222-226
27580376-4	2016	Here we report a heparin mimicking block copolymer, poly(styrenesulfonate-co-poly(ethylene glycol) methyl ether methacrylate)-b-vinyl sulfonate) (p(SS-co-PEGMA)-b-VS, that contains a segment that enhances the stability of FGF2 and one that binds to the FGF2 receptor.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	253-257
27521419-0	2016	Extracellular matrix fibronectin mediates an endothelial cell response to shear stress via the heparin-binding, matricryptic RWRPK sequence of FNIII1H.	Heparin	95-102	fibronectin 1	Homo sapiens	21-32
27412887-8	2016	Binding of PF4/heparin complexes to B cells is mediated through the interaction between complement and complement receptor 2 (CR2 [CD21]).	Heparin	15-22	complement C3d receptor 2	Homo sapiens	131-135
27412887-9	2016	To the best of our knowledge, these are the first studies to demonstrate complement activation by PF4/heparin complexes, opsonization of PF4/heparin to B cells via CD21, and the presence of complement activation fragments on circulating B cells in some patients receiving heparin.	Heparin	141-148	complement C3d receptor 2	Homo sapiens	164-168
27412887-9	2016	To the best of our knowledge, these are the first studies to demonstrate complement activation by PF4/heparin complexes, opsonization of PF4/heparin to B cells via CD21, and the presence of complement activation fragments on circulating B cells in some patients receiving heparin.	Heparin	141-148	complement C3d receptor 2	Homo sapiens	164-168
27521419-2	2016	Our earlier studies implicated the extracellular matrix protein fibronectin in mechanosensory signaling to ECs in intact arterioles, via a signaling pathway dependent on the heparin-binding region of the first type III repeat of fibrillar fibronectin (FNIII1H).	Heparin	174-181	fibronectin 1	Homo sapiens	64-75
27521419-2	2016	Our earlier studies implicated the extracellular matrix protein fibronectin in mechanosensory signaling to ECs in intact arterioles, via a signaling pathway dependent on the heparin-binding region of the first type III repeat of fibrillar fibronectin (FNIII1H).	Heparin	174-181	fibronectin 1	Homo sapiens	239-250
27654470-0	2016	Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.	Heparin	0-7	apolipoprotein A1	Homo sapiens	78-96
27301751-4	2016	UFH, the LMWHs enoxaparin and dalteparin, and the low anticoagulant LMWH 2-O, 3-O desulphated heparin (ODSH) all promoted thrombin generation, but fondaparinux did not, and this activity was blocked by a TFPIalpha antibody.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	122-130
27301751-4	2016	UFH, the LMWHs enoxaparin and dalteparin, and the low anticoagulant LMWH 2-O, 3-O desulphated heparin (ODSH) all promoted thrombin generation, but fondaparinux did not, and this activity was blocked by a TFPIalpha antibody.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	122-130
27542222-4	2016	We found that the acidic domain of MZF-1 and the heparin-binding domain of Elk-1 facilitate the heterodimeric interaction between the two genes before the complex formation binds to the PKCalpha promoter.	Heparin	49-56	protein kinase C alpha	Homo sapiens	186-194
27390976-10	2016	Heparin and bivalirudin infusion effectively inhibited thrombin generation during PCI.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	55-63
27599556-0	2016	Heparin inhibits the inflammation and proliferation of human rheumatoid arthritis fibroblast-like synoviocytes through the NF-kappaB pathway.	Heparin	0-7	nuclear factor kappa B subunit 1	Homo sapiens	123-132
27599556-3	2016	In the present study, the effect of heparin on the tumor necrosis factor (TNF)-alpha induced proliferation of FLSs was investigated.	Heparin	36-43	tumor necrosis factor	Homo sapiens	51-84
27599556-6	2016	Heparin inhibited the growth rate of the FLSs induced by TNF-alpha.	Heparin	0-7	tumor necrosis factor	Homo sapiens	57-66
27599556-7	2016	Heparin also decreased the TNF-alpha-induced mRNA and protein expression levels of IL-6, IL-8, TNF-alpha and cyclin D1 in a dose-dependent manner.	Heparin	0-7	tumor necrosis factor	Homo sapiens	27-36
27599556-7	2016	Heparin also decreased the TNF-alpha-induced mRNA and protein expression levels of IL-6, IL-8, TNF-alpha and cyclin D1 in a dose-dependent manner.	Heparin	0-7	interleukin 6	Homo sapiens	83-87
27599556-7	2016	Heparin also decreased the TNF-alpha-induced mRNA and protein expression levels of IL-6, IL-8, TNF-alpha and cyclin D1 in a dose-dependent manner.	Heparin	0-7	C-X-C motif chemokine ligand 8	Homo sapiens	89-93
27599556-7	2016	Heparin also decreased the TNF-alpha-induced mRNA and protein expression levels of IL-6, IL-8, TNF-alpha and cyclin D1 in a dose-dependent manner.	Heparin	0-7	tumor necrosis factor	Homo sapiens	95-104
27599556-8	2016	Immunofluorescence analysis showed that the expression of cytoplasmic TNF-alpha was significantly reduced by heparin treatment.	Heparin	109-116	tumor necrosis factor	Homo sapiens	70-79
27599556-9	2016	Furthermore, the levels of p65 and inhibitor of nuclear factor (NF)-kappaB phosphorylation were inhibited by heparin treatment, suggesting that heparin induced the inhibition of NF-kappaB.	Heparin	109-116	nuclear factor kappa B subunit 1	Homo sapiens	178-187
27599556-9	2016	Furthermore, the levels of p65 and inhibitor of nuclear factor (NF)-kappaB phosphorylation were inhibited by heparin treatment, suggesting that heparin induced the inhibition of NF-kappaB.	Heparin	144-151	nuclear factor kappa B subunit 1	Homo sapiens	178-187
27599556-10	2016	In conclusion, the results of the present study revealed that heparin inhibited the TNF-alpha-induced proliferation, cytokine production, expression of cyclin D1 and activation of NF-kappaB signaling in FLSs, indicating the therapeutic potential of heparin in the treatment of RA.	Heparin	62-69	tumor necrosis factor	Homo sapiens	84-93
27599556-10	2016	In conclusion, the results of the present study revealed that heparin inhibited the TNF-alpha-induced proliferation, cytokine production, expression of cyclin D1 and activation of NF-kappaB signaling in FLSs, indicating the therapeutic potential of heparin in the treatment of RA.	Heparin	62-69	nuclear factor kappa B subunit 1	Homo sapiens	180-189
27599556-10	2016	In conclusion, the results of the present study revealed that heparin inhibited the TNF-alpha-induced proliferation, cytokine production, expression of cyclin D1 and activation of NF-kappaB signaling in FLSs, indicating the therapeutic potential of heparin in the treatment of RA.	Heparin	249-256	tumor necrosis factor	Homo sapiens	84-93
27599556-10	2016	In conclusion, the results of the present study revealed that heparin inhibited the TNF-alpha-induced proliferation, cytokine production, expression of cyclin D1 and activation of NF-kappaB signaling in FLSs, indicating the therapeutic potential of heparin in the treatment of RA.	Heparin	249-256	nuclear factor kappa B subunit 1	Homo sapiens	180-189
27117175-4	2016	RESULTS: Compared with T1, the fibrinogen and MA levels in both groups reduced significantly after heparin reversal and fell within the normal range for most patients.	Heparin	99-106	fibrinogen beta chain	Homo sapiens	31-41
27117175-8	2016	CONCLUSION: Most patients receiving aortic arch replacement with DHCA have normal platelet function and fibrinogen levels after heparin reversal.	Heparin	128-135	fibrinogen beta chain	Homo sapiens	104-114
27564657-5	2016	METHODS: TAFI activation by thrombin or plasmin was studied in the presence of physiological anionic molecules (polyphosphate, heparin, hyaluronan, DNA and dermatan sulfate) and the non-physiological sodium dodecyl sulfate (SDS).	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	28-36
27564657-7	2016	RESULTS: Unfractioned heparin, calcium-saturated polyphosphate with an average chain length of 100 monomers (Ca-PolyP100) and SDS significantly enhanced TAFI activation by thrombin and plasmin.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	172-180
27564657-9	2016	Additionally, unfractioned heparin, Ca-PolyP100 and SDS enhanced thrombin-mediated protein C activation.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	65-73
27338096-4	2016	Like other serpin-protease partners, C1-INH interaction with C1s is accelerated by polyanions such as heparin.	Heparin	102-109	complement C1s	Homo sapiens	61-64
27338096-11	2016	In summary, like heparin, polyP is a naturally occurring cofactor for the C1s:C1-INH interaction and thus an important regulator of complement activation.	Heparin	17-24	complement C1s	Homo sapiens	74-77
27056061-2	2016	Although mutations within the heparin-binding domains of the fibronectin 1 gene (FN1) have been associated with GFND, no mutations have been reported within the integrin-binding domains.	Heparin	30-37	fibronectin 1	Homo sapiens	61-74
26773314-6	2016	Inhibiting VEGF-matrix binding with sucrose octasulfate decreased cell-internalization of VEGF and, inversely, heparin pre-treatment to enhance Fn-matrix binding of VEGF increased cell-internalization of VEGF regardless of matrix stiffness.	Heparin	111-118	vascular endothelial growth factor A	Homo sapiens	11-15
26773314-6	2016	Inhibiting VEGF-matrix binding with sucrose octasulfate decreased cell-internalization of VEGF and, inversely, heparin pre-treatment to enhance Fn-matrix binding of VEGF increased cell-internalization of VEGF regardless of matrix stiffness.	Heparin	111-118	fibronectin 1	Homo sapiens	144-146
27344360-3	2016	Heparin administration resulted in good control of thrombin regulation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	51-59
27378603-5	2016	Triggers for such antibodies remain poorly-defined, but could include preoperative administration of heparin to diabetic patients receiving protamine-insulin as well as recent previous cardiac surgery.	Heparin	101-108	insulin	Homo sapiens	150-157
27056061-2	2016	Although mutations within the heparin-binding domains of the fibronectin 1 gene (FN1) have been associated with GFND, no mutations have been reported within the integrin-binding domains.	Heparin	30-37	fibronectin 1	Homo sapiens	81-84
27056061-2	2016	Although mutations within the heparin-binding domains of the fibronectin 1 gene (FN1) have been associated with GFND, no mutations have been reported within the integrin-binding domains.	Heparin	30-37	fibronectin 1	Homo sapiens	112-116
27585207-5	2016	Self-assembled PECs have been fabricated to provide better control of BMP-2/NELL-1 delivery via heparin binding and further potentiate growth factor bioactivity by enhancing in vivo stability.	Heparin	96-103	neural EGFL like 1	Homo sapiens	76-82
27121983-2	2016	The process of thrombin generation is disturbed during surgery with CPB because of haemodilution, coagulation factor consumption and heparin administration.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	15-23
26953670-0	2016	Heparin-Based Polyelectrolyte Complex Enhances the Therapeutic Efficacy of Bone Morphogenetic Protein-2 for Posterolateral Fusion in a Large Animal Model.	Heparin	0-7	bone morphogenetic protein 2	Sus scrofa	75-103
26953670-5	2016	To reduce the efficacious dose of BMP-2 and its associated complications, heparin-based PEC was introduced.	Heparin	74-81	bone morphogenetic protein 2	Sus scrofa	34-39
27990411-6	2016	Coating both Gram-negative and Gram-positive bacteria with LL-37 significantly potentiated their phagocytosis by macrophages, and this process was blocked by a combination of anti-Mac-1 mAb and heparin.	Heparin	194-201	cathelicidin antimicrobial peptide	Homo sapiens	59-64
27474498-12	2016	administration of a TLR4 antagonist or low molecular weight heparin, known to inhibit RAGE, attenuated the hyperalgesia caused by i.pl.	Heparin	60-67	advanced glycosylation end product-specific receptor	Rattus norvegicus	86-90
27196743-9	2016	The results showed that the HMGB1A/heparin complex reduced pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6), and IL-1beta, more effectively than HMGB1A or heparin alone.	Heparin	35-42	tumor necrosis factor	Homo sapiens	97-124
27196743-9	2016	The results showed that the HMGB1A/heparin complex reduced pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6), and IL-1beta, more effectively than HMGB1A or heparin alone.	Heparin	35-42	tumor necrosis factor	Homo sapiens	126-135
27196743-9	2016	The results showed that the HMGB1A/heparin complex reduced pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6), and IL-1beta, more effectively than HMGB1A or heparin alone.	Heparin	35-42	interleukin 6	Homo sapiens	138-151
27196743-9	2016	The results showed that the HMGB1A/heparin complex reduced pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6), and IL-1beta, more effectively than HMGB1A or heparin alone.	Heparin	35-42	interleukin 6	Homo sapiens	153-157
27196743-9	2016	The results showed that the HMGB1A/heparin complex reduced pro-inflammatory cytokines, including tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6), and IL-1beta, more effectively than HMGB1A or heparin alone.	Heparin	35-42	interleukin 1 beta	Homo sapiens	164-172
27990411-5	2016	The cell adhesion to LL-37 was partially inhibited by specific Mac-1 antagonists, including mAb against the alphaM integrin subunit and neutrophil inhibitory factor, and completely blocked when anti-Mac-1 antibodies were combined with heparin, suggesting that cell surface heparan sulfate proteoglycans act cooperatively with integrin Mac-1.	Heparin	235-242	cathelicidin antimicrobial peptide	Homo sapiens	21-26
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	215-241
27011369-0	2016	The presence of heparins during decidualization modulates the response of human endometrial stromal cells to IL-1beta in vitro.	Heparin	16-24	interleukin 1 beta	Homo sapiens	109-117
27011369-1	2016	PURPOSE: The aim of this paper is to study the impact of heparin on the response of human endometrial stromal cells (ESCs) to interleukin (IL)-1beta during decidualization in vitro.	Heparin	57-64	interleukin 1 beta	Homo sapiens	126-148
27011369-6	2016	Unfractionated heparin as well as tinzaparin attenuated the IL-1beta-mediated induction of IL-6, IL-11, and LIF on protein and messenger RNA (mRNA) levels.	Heparin	15-22	interleukin 1 beta	Homo sapiens	60-68
27011369-6	2016	Unfractionated heparin as well as tinzaparin attenuated the IL-1beta-mediated induction of IL-6, IL-11, and LIF on protein and messenger RNA (mRNA) levels.	Heparin	15-22	interleukin 6	Homo sapiens	91-95
27011369-8	2016	CONCLUSIONS: Unfractionated heparin and the low molecular weight heparin tinzaparin have modulating effects on IL-1beta-induced endometrial cytokines of the IL-6 family during decidualization.	Heparin	28-35	interleukin 1 beta	Homo sapiens	111-119
27011369-8	2016	CONCLUSIONS: Unfractionated heparin and the low molecular weight heparin tinzaparin have modulating effects on IL-1beta-induced endometrial cytokines of the IL-6 family during decidualization.	Heparin	28-35	interleukin 6	Homo sapiens	157-161
27011369-8	2016	CONCLUSIONS: Unfractionated heparin and the low molecular weight heparin tinzaparin have modulating effects on IL-1beta-induced endometrial cytokines of the IL-6 family during decidualization.	Heparin	65-72	interleukin 1 beta	Homo sapiens	111-119
27011369-8	2016	CONCLUSIONS: Unfractionated heparin and the low molecular weight heparin tinzaparin have modulating effects on IL-1beta-induced endometrial cytokines of the IL-6 family during decidualization.	Heparin	65-72	interleukin 6	Homo sapiens	157-161
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	243-248
27146359-7	2016	The concomitant encapsulation of heparin and the use of SC as a nanoparticle matrix contributed to the largest amount of bFGF release (18%) over the time investigated.	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	121-125
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	20-27	transforming growth factor beta 1	Homo sapiens	309-341
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	20-27	transforming growth factor beta 1	Homo sapiens	343-352
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	215-241
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	243-248
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	transforming growth factor beta 1	Homo sapiens	309-341
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	transforming growth factor beta 1	Homo sapiens	343-352
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	215-241
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	243-248
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	transforming growth factor beta 1	Homo sapiens	309-341
26990913-3	2016	We have developed a heparin-based cell coating and we believe that the electrostatic interaction between native heparin and the positively charged growth factors will result in (1) higher cell number in response to fibroblast growth factor-2 (FGF-2) and 2) greater chondrogenic differentiation in response to transforming growth factor-beta1 (TGF-beta1), compared to a desulfated heparin coating.	Heparin	112-119	transforming growth factor beta 1	Homo sapiens	343-352
26990913-4	2016	Results revealed that in the presence of FGF-2, by day 14, heparin-coated MSC aggregates increased in DNA content 8.5 +- 1.6 fold compared to day 1, which was greater than noncoated and desulfated heparin-coated aggregates.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	41-46
26990913-4	2016	Results revealed that in the presence of FGF-2, by day 14, heparin-coated MSC aggregates increased in DNA content 8.5 +- 1.6 fold compared to day 1, which was greater than noncoated and desulfated heparin-coated aggregates.	Heparin	197-204	fibroblast growth factor 2	Homo sapiens	41-46
26990913-5	2016	In contrast, when cultured in the presence of TGF-beta1, by day 21, desulfated heparin-coated aggregates upregulated gene expression of collagen II by 86.5 +- 7.5 fold and collagen X by 37.1 +- 4.7 fold, which was higher than that recorded in the noncoated and heparin-coated aggregates.	Heparin	79-86	transforming growth factor beta 1	Homo sapiens	46-55
26990913-5	2016	In contrast, when cultured in the presence of TGF-beta1, by day 21, desulfated heparin-coated aggregates upregulated gene expression of collagen II by 86.5 +- 7.5 fold and collagen X by 37.1 +- 4.7 fold, which was higher than that recorded in the noncoated and heparin-coated aggregates.	Heparin	261-268	transforming growth factor beta 1	Homo sapiens	46-55
27191965-4	2016	Our data showed that M-MSN(DOX)/PEI-FA could strongly condense VEGF shRNA at weight ratios of 30:1, and possesses higher stability against DNase I digestion and sodium heparin.	Heparin	161-175	moesin	Homo sapiens	23-26
27366296-10	2016	Heparin produces its major anticoagulant effect by inactivating thrombin and factor X through an AT-dependent mechanism.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	64-72
27366296-11	2016	For inhibition of thrombin, heparin must bind to both the coagulation enzyme and the AT.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	18-26
27196997-0	2016	Heparin-Based Coacervate of FGF2 Improves Dermal Regeneration by Asserting a Synergistic Role with Cell Proliferation and Endogenous Facilitated VEGF for Cutaneous Wound Healing.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	28-32
27196997-0	2016	Heparin-Based Coacervate of FGF2 Improves Dermal Regeneration by Asserting a Synergistic Role with Cell Proliferation and Endogenous Facilitated VEGF for Cutaneous Wound Healing.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	145-149
27196997-2	2016	In this study, we develop a heparin-based coacervate consisting of poly(ethylene argininylaspartate digylceride) (PEAD) as a storage matrix, heparin as a bridge, and fibroblast growth factor-2 (FGF2) as a cargo (namely heparin-FGF2@PEAD) for wound healing.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	166-192
27196997-2	2016	In this study, we develop a heparin-based coacervate consisting of poly(ethylene argininylaspartate digylceride) (PEAD) as a storage matrix, heparin as a bridge, and fibroblast growth factor-2 (FGF2) as a cargo (namely heparin-FGF2@PEAD) for wound healing.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	194-198
27196997-2	2016	In this study, we develop a heparin-based coacervate consisting of poly(ethylene argininylaspartate digylceride) (PEAD) as a storage matrix, heparin as a bridge, and fibroblast growth factor-2 (FGF2) as a cargo (namely heparin-FGF2@PEAD) for wound healing.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	227-236
27196997-4	2016	The following in vivo studies examine the wound healing efficiency of the heparin-FGF2@PEAD coacervate upon delivering FGF2 to full-thickness excisional skin wounds in vivo, in comparison with the other three control groups with saline, heparin@PEAD as vehicle, and free FGF2.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	82-86
27196997-4	2016	The following in vivo studies examine the wound healing efficiency of the heparin-FGF2@PEAD coacervate upon delivering FGF2 to full-thickness excisional skin wounds in vivo, in comparison with the other three control groups with saline, heparin@PEAD as vehicle, and free FGF2.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	119-123
27196997-4	2016	The following in vivo studies examine the wound healing efficiency of the heparin-FGF2@PEAD coacervate upon delivering FGF2 to full-thickness excisional skin wounds in vivo, in comparison with the other three control groups with saline, heparin@PEAD as vehicle, and free FGF2.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	119-123
26945629-8	2016	Analysis of the native SAA1.1 structure has led to the identification of a competing site for high-density lipoprotein (HDL) and heparin, thus providing the structural basis for a role of heparin and heparan sulfate in the conversion of SAA1 to AA.	Heparin	188-195	serum amyloid A1	Homo sapiens	237-241
26762172-9	2016	In particular, docking solutions were obtained in which (i) a single roneparstat molecule interacts with both heparin-binding domains (HBDs) of heparanase or (ii) two fragments of roneparstat interact with either HBD-1 or HBD-2, consistent with the possibility of different inhibitor:enzyme binding stoichiometries.	Heparin	110-117	heparanase	Homo sapiens	144-154
26970827-6	2016	We could show that more cells adhered to CXCL8 adsorbed to hydrophobic octadecanethiol than on CXCL8 covalently bound to amino undecanethiol or CXCL8 specifically bound to immobilized heparin on aminothiol.	Heparin	184-191	C-X-C motif chemokine ligand 8	Homo sapiens	41-46
26970827-6	2016	We could show that more cells adhered to CXCL8 adsorbed to hydrophobic octadecanethiol than on CXCL8 covalently bound to amino undecanethiol or CXCL8 specifically bound to immobilized heparin on aminothiol.	Heparin	184-191	C-X-C motif chemokine ligand 8	Homo sapiens	95-100
26970827-6	2016	We could show that more cells adhered to CXCL8 adsorbed to hydrophobic octadecanethiol than on CXCL8 covalently bound to amino undecanethiol or CXCL8 specifically bound to immobilized heparin on aminothiol.	Heparin	184-191	C-X-C motif chemokine ligand 8	Homo sapiens	95-100
26960279-3	2016	Direct oral anticoagulants represent an important advance in anticoagulation therapy, directly inhibiting thrombin (dabigatran) or factor Xa (rivaroxaban, apixaban) they represent an effective and safe alternatives to VKAs and heparins in the prevention and treatment of several thromboembolic disorders.	Heparin	227-235	coagulation factor II, thrombin	Homo sapiens	106-114
26945629-8	2016	Analysis of the native SAA1.1 structure has led to the identification of a competing site for high-density lipoprotein (HDL) and heparin, thus providing the structural basis for a role of heparin and heparan sulfate in the conversion of SAA1 to AA.	Heparin	129-136	serum amyloid A1	Homo sapiens	23-27
26945629-8	2016	Analysis of the native SAA1.1 structure has led to the identification of a competing site for high-density lipoprotein (HDL) and heparin, thus providing the structural basis for a role of heparin and heparan sulfate in the conversion of SAA1 to AA.	Heparin	188-195	serum amyloid A1	Homo sapiens	23-27
32263256-7	2016	ATR-FTIR and XPS spectra demonstrated the successful formation of the heparin-mimetic coatings.	Heparin	70-77	ATR serine/threonine kinase	Homo sapiens	0-3
27148674-3	2016	Heparin activates antithrombin and promotes the inactivation of thrombin and other target proteinases.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	22-30
27065061-11	2016	The residues of apoE that bind heparin are the same as those involved in apoE binding to LDL and LRP-1 receptors.	Heparin	31-38	apolipoprotein E	Homo sapiens	16-20
27151330-8	2016	ApoE3 and apoE4 particles have similar binding affinity to heparin, while apoE4 particles are likely hypolipidated compared to apoE particles.	Heparin	59-66	apolipoprotein E	Mus musculus	10-14
28824983-0	2016	Postoperative Heparin-Mediated Extracorporeal Low-Density Lipoprotein Fibrinogen Precipitation Aphaeresis Prevents Early Graft Occlusion after Coronary Artery Bypass Grafting.	Heparin	14-21	fibrinogen beta chain	Homo sapiens	70-80
28824983-5	2016	(heparin-mediated extracorporeal low-density lipoprotein [LDL] fibrinogen precipitation) aphaeresis could reduce the rate of early graft occlusion in patients with hypercholesterolemia undergoing CABG.	Heparin	1-8	fibrinogen beta chain	Homo sapiens	63-73
26168717-4	2016	This model was used to investigate the impact of surface bound heparin on thrombin generation with and without the additive effects of thrombomodulin (TM).	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	74-82
29920038-0	2016	[Effect of unfractionated heparin on the expression of heme oxygenase-1 in intestinal mucosa of mice with sepsis].	Heparin	26-33	heme oxygenase 1	Mus musculus	55-71
29920038-1	2016	Objective: To investigate the effect of unfractionated heparin (UFH) on the expression of heme oxygenase-1 (HO-1) in intestinal mucosa of mice with sepsis.	Heparin	55-62	heme oxygenase 1	Mus musculus	90-106
29920038-1	2016	Objective: To investigate the effect of unfractionated heparin (UFH) on the expression of heme oxygenase-1 (HO-1) in intestinal mucosa of mice with sepsis.	Heparin	55-62	heme oxygenase 1	Mus musculus	108-112
29920038-1	2016	Objective: To investigate the effect of unfractionated heparin (UFH) on the expression of heme oxygenase-1 (HO-1) in intestinal mucosa of mice with sepsis.	Heparin	64-67	heme oxygenase 1	Mus musculus	90-106
29920038-1	2016	Objective: To investigate the effect of unfractionated heparin (UFH) on the expression of heme oxygenase-1 (HO-1) in intestinal mucosa of mice with sepsis.	Heparin	64-67	heme oxygenase 1	Mus musculus	108-112
27100626-0	2016	Activation of ERK and NF-kappaB during HARE-Mediated Heparin Uptake Require Only One of the Four Endocytic Motifs.	Heparin	53-60	mitogen-activated protein kinase 1	Homo sapiens	14-17
27100626-0	2016	Activation of ERK and NF-kappaB during HARE-Mediated Heparin Uptake Require Only One of the Four Endocytic Motifs.	Heparin	53-60	nuclear factor kappa B subunit 1	Homo sapiens	22-31
27100626-12	2016	NF-kappaB activation by HARE-mediated uptake of Hep, HA, dermatan sulfate or acetylated LDL was unaffected in single-motif deletion mutants lacking M1, M2 or M4.	Heparin	48-51	nuclear factor kappa B subunit 1	Homo sapiens	0-9
26931056-3	2016	In this system, vascular endothelial growth factor (VEGF) binds with heparin and is encapsulated in heparin-conjugated gelatin nanospheres, which are further immobilized in the nanofibers of an injectable poly(l-lactic acid) (PLLA) microsphere.	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	16-50
26931056-3	2016	In this system, vascular endothelial growth factor (VEGF) binds with heparin and is encapsulated in heparin-conjugated gelatin nanospheres, which are further immobilized in the nanofibers of an injectable poly(l-lactic acid) (PLLA) microsphere.	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	52-56
26931056-3	2016	In this system, vascular endothelial growth factor (VEGF) binds with heparin and is encapsulated in heparin-conjugated gelatin nanospheres, which are further immobilized in the nanofibers of an injectable poly(l-lactic acid) (PLLA) microsphere.	Heparin	100-107	vascular endothelial growth factor A	Homo sapiens	16-50
26931056-3	2016	In this system, vascular endothelial growth factor (VEGF) binds with heparin and is encapsulated in heparin-conjugated gelatin nanospheres, which are further immobilized in the nanofibers of an injectable poly(l-lactic acid) (PLLA) microsphere.	Heparin	100-107	vascular endothelial growth factor A	Homo sapiens	52-56
27151330-11	2016	We further demonstrated that apoE particles reduced the internalization of Abeta in mouse primary neurons, an effect that is eliminated by the presence of heparin.	Heparin	155-162	apolipoprotein E	Mus musculus	29-33
26928466-4	2016	In a second step, we took advantage of the heparin-binding domain of vascular endothelial growth factor (VEGF) and hepatocyte growth factor (HGF) to gain advanced re-endothelialization capabilities.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	69-103
26928466-4	2016	In a second step, we took advantage of the heparin-binding domain of vascular endothelial growth factor (VEGF) and hepatocyte growth factor (HGF) to gain advanced re-endothelialization capabilities.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	105-109
29920038-14	2016	Conclusion: UFH can enhance the expression of HO-1 in intestinal mucosa, reduce the release of inflammatory factors, ameliorate the intestinal inflammatory response, and thus play a protective role in intestinal tissue in mice with sepsis.	Heparin	12-15	heme oxygenase 1	Mus musculus	46-50
27097314-3	2016	However, previous studies showed that the accumulation of two heparin-binding growth factors, Vascular Endothelial Cell Growth Factor-A (VEGF-A) and Fibroblast Growth Factor-2 (FGF-2), in combination with the viral protein Tat, can precipitate the progression of HIV-renal diseases.	Heparin	62-69	vascular endothelial growth factor A	Homo sapiens	94-135
27097314-3	2016	However, previous studies showed that the accumulation of two heparin-binding growth factors, Vascular Endothelial Cell Growth Factor-A (VEGF-A) and Fibroblast Growth Factor-2 (FGF-2), in combination with the viral protein Tat, can precipitate the progression of HIV-renal diseases.	Heparin	62-69	vascular endothelial growth factor A	Homo sapiens	137-143
27097314-3	2016	However, previous studies showed that the accumulation of two heparin-binding growth factors, Vascular Endothelial Cell Growth Factor-A (VEGF-A) and Fibroblast Growth Factor-2 (FGF-2), in combination with the viral protein Tat, can precipitate the progression of HIV-renal diseases.	Heparin	62-69	fibroblast growth factor 2	Homo sapiens	149-175
27097314-3	2016	However, previous studies showed that the accumulation of two heparin-binding growth factors, Vascular Endothelial Cell Growth Factor-A (VEGF-A) and Fibroblast Growth Factor-2 (FGF-2), in combination with the viral protein Tat, can precipitate the progression of HIV-renal diseases.	Heparin	62-69	fibroblast growth factor 2	Homo sapiens	177-182
27097314-6	2016	We found that VEGF-A and FGF-2, acting in synergy with HIV-Tat and heparin, affected the cytoskeletal structure and permeability of REc through changes in Rho-A, Src, and Rac-1 activity.	Heparin	67-74	vascular endothelial growth factor A	Homo sapiens	14-20
27097314-6	2016	We found that VEGF-A and FGF-2, acting in synergy with HIV-Tat and heparin, affected the cytoskeletal structure and permeability of REc through changes in Rho-A, Src, and Rac-1 activity.	Heparin	67-74	fibroblast growth factor 2	Homo sapiens	25-30
27097314-6	2016	We found that VEGF-A and FGF-2, acting in synergy with HIV-Tat and heparin, affected the cytoskeletal structure and permeability of REc through changes in Rho-A, Src, and Rac-1 activity.	Heparin	67-74	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	162-165
26774761-5	2016	Mouse ESCs were encapsulated into heparin microgels with a single dose of Nodal and FGF-2, and expressed high levels of endoderm markers Sox17 and FoxA2 after 5 days.	Heparin	34-41	forkhead box A2	Mus musculus	147-152
27069129-0	2016	Unfractionated Heparin Selectively Modulates the Expression of CXCL8, CCL2 and CCL5 in Endometrial Carcinoma Cells.	Heparin	15-22	C-X-C motif chemokine ligand 8	Homo sapiens	63-68
27069129-5	2016	UFH attenuated the secretion of CXCL8 and CCL2, and enhanced that of CCL5.	Heparin	0-3	C-X-C motif chemokine ligand 8	Homo sapiens	32-37
27069129-7	2016	CONCLUSION: UFH has selective modulating effects on the secretion of CXCL8, CCL2 and CCL5 in different endometrial adenocarcinoma cell lines.	Heparin	12-15	C-X-C motif chemokine ligand 8	Homo sapiens	69-74
31245479-0	2016	A heparin-modified thermoresponsive surface with heparin-binding epidermal growth factor-like growth factor for maintaining hepatic functions in vitro and harvesting hepatocyte sheets.	Heparin	2-9	heparin-binding EGF-like growth factor	Rattus norvegicus	49-107
26980324-1	2016	AIM: To perform one-pot synthesis of heparin-immobilized polypyrrole (PPy) nanoparticles and evaluate the use of these nanoparticles for the delivery of VEGF.	Heparin	37-44	vascular endothelial growth factor A	Homo sapiens	153-157
26980324-3	2016	VEGF-bound PPy-heparin nanoparticles were delivered to endothelial cells and bioactivity of VEGF was assessed by Matrigel tube formation.	Heparin	15-22	vascular endothelial growth factor A	Homo sapiens	0-4
26980324-4	2016	RESULTS: Size-controllable synthesis of heparin-doped PPy nanoparticles was achieved, and heparin promoted the conjugation of VEGF.	Heparin	90-97	vascular endothelial growth factor A	Homo sapiens	126-130
26980324-6	2016	CONCLUSION: Heparin-doped PPy nanoparticles can be synthesized using one-pot reaction and provide a delivery platform by which VEGF can be conjugated onto.	Heparin	12-19	vascular endothelial growth factor A	Homo sapiens	127-131
26467272-5	2016	In addition, PF4/heparin-specific IgM B cells were not only found in murine spleen, but also in peritoneum and bone marrow upon in vitro stimulation.	Heparin	17-24	platelet factor 4	Mus musculus	13-16
26467272-8	2016	In conclusion, the anti-PF4/heparin IgM response is a potential innate immune reaction driven by a B cell population distinct from MZ B cells.	Heparin	28-35	platelet factor 4	Mus musculus	24-27
31245479-1	2016	A heparin-modified thermoresponsive surface bound with heparin-binding epidermal growth factor-like growth factor (HB-EGF) was designed to allow creation of transferrable and functional hepatocyte sheets.	Heparin	2-9	heparin-binding EGF-like growth factor	Rattus norvegicus	55-113
31245479-1	2016	A heparin-modified thermoresponsive surface bound with heparin-binding epidermal growth factor-like growth factor (HB-EGF) was designed to allow creation of transferrable and functional hepatocyte sheets.	Heparin	2-9	heparin-binding EGF-like growth factor	Rattus norvegicus	115-121
31245479-8	2016	Hence, heparin-modified thermoresponsive surfaces bound with HB-EGF facilitate the fabrication of transferrable hepatocyte sheets with intact hepatic functions and have the potential to provide an in vitro culture system using functional hepatocyte sheet tissues, which may serve as an effective hepatocyte-based tissue engineering platform for liver disease treatments.	Heparin	7-14	heparin-binding EGF-like growth factor	Rattus norvegicus	61-67
27042064-0	2016	Sustained dual release of placental growth factor-2 and bone morphogenic protein-2 from heparin-based nanocomplexes for direct osteogenesis.	Heparin	88-95	placental growth factor	Homo sapiens	26-51
26769965-2	2016	Studies with vascular smooth muscle cells (VSMCs) indicate a role for induction of dual specificity phosphatase 1 (DUSP1) that decreases ERK activity and results in decreased cell proliferation, which depends on specific heparin binding.	Heparin	221-228	dual specificity phosphatase 1	Homo sapiens	83-113
26769965-2	2016	Studies with vascular smooth muscle cells (VSMCs) indicate a role for induction of dual specificity phosphatase 1 (DUSP1) that decreases ERK activity and results in decreased cell proliferation, which depends on specific heparin binding.	Heparin	221-228	dual specificity phosphatase 1	Homo sapiens	115-120
26769965-0	2016	Heparin Decreases in Tumor Necrosis Factor alpha (TNFalpha)-induced Endothelial Stress Responses Require Transmembrane Protein 184A and Induction of Dual Specificity Phosphatase 1.	Heparin	0-7	tumor necrosis factor	Homo sapiens	21-48
26769965-3	2016	The hypothesis that unfractionated heparin functions to decrease inflammatory signal transduction in endothelial cells (ECs) through heparin-induced expression of DUSP1 was tested.	Heparin	35-42	dual specificity phosphatase 1	Homo sapiens	163-168
26769965-0	2016	Heparin Decreases in Tumor Necrosis Factor alpha (TNFalpha)-induced Endothelial Stress Responses Require Transmembrane Protein 184A and Induction of Dual Specificity Phosphatase 1.	Heparin	0-7	tumor necrosis factor	Homo sapiens	50-58
26769965-0	2016	Heparin Decreases in Tumor Necrosis Factor alpha (TNFalpha)-induced Endothelial Stress Responses Require Transmembrane Protein 184A and Induction of Dual Specificity Phosphatase 1.	Heparin	0-7	dual specificity phosphatase 1	Homo sapiens	149-179
26769965-3	2016	The hypothesis that unfractionated heparin functions to decrease inflammatory signal transduction in endothelial cells (ECs) through heparin-induced expression of DUSP1 was tested.	Heparin	133-140	dual specificity phosphatase 1	Homo sapiens	163-168
26769965-5	2016	Heparin pretreatment of ECs resulted in decreased TNFalpha-induced JNK and p38 activity and downstream target phosphorylation, as identified through Western blotting and immunofluorescence microscopy.	Heparin	0-7	tumor necrosis factor	Homo sapiens	50-58
26769965-5	2016	Heparin pretreatment of ECs resulted in decreased TNFalpha-induced JNK and p38 activity and downstream target phosphorylation, as identified through Western blotting and immunofluorescence microscopy.	Heparin	0-7	mitogen-activated protein kinase 14	Homo sapiens	75-78
26769965-6	2016	Through knockdown strategies, the importance of heparin-induced DUSP1 expression in these effects was confirmed.	Heparin	48-55	dual specificity phosphatase 1	Homo sapiens	64-69
26769965-7	2016	Quantitative fluorescence microscopy indicated that heparin treatment of ECs reduced TNFalpha-induced increases in stress fibers.	Heparin	52-59	tumor necrosis factor	Homo sapiens	85-93
26769966-1	2016	Vascular cell responses to exogenous heparin have been documented to include decreased vascular smooth muscle cell proliferation following decreased ERK pathway signaling.	Heparin	37-44	mitogen-activated protein kinase 1	Homo sapiens	149-152
26916304-0	2016	Heparin supplement counteracts the prohemostatic effect of prothrombin complex concentrate and factor IX concentrate: An in vitro evaluation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	59-70
27134308-1	2016	The direct thrombin inhibitor bivalirudin is an option for anticoagulation in patients with heparin induced thrombocytopenia (HIT) requiring cardiopulmonary bypass (CPB).	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	11-19
26611767-3	2016	FGF-2 is further stabilized by complexation to heparin-based nanoparticles.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	0-5
27030175-3	2016	Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry.	Heparin	119-127	fibroblast growth factor 4	Homo sapiens	60-64
27030175-3	2016	Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry.	Heparin	119-127	fibroblast growth factor 10	Homo sapiens	72-77
26666430-3	2016	Heparin, a highly sulfonated and negatively charged member of glycosaminoglycan family is well established for their anti-thrombin, anticoagulant and many biological activities that make it a highly attractive candidate capable of modifying or tailoring polymer properties.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	122-130
25425223-1	2016	BACKGROUND: Activated clotting time (ACT) has been successfully applied during percutaneous coronary intervention (PCI) to monitor the extent of thrombin inhibition and anti-coagulation from unfractionated heparin (UFH) aiming to reduce the incidence of thrombotic adverse events and hemorrhagic complications.	Heparin	206-213	coagulation factor II, thrombin	Homo sapiens	145-153
26916304-0	2016	Heparin supplement counteracts the prohemostatic effect of prothrombin complex concentrate and factor IX concentrate: An in vitro evaluation.	Heparin	0-7	coagulation factor IX	Homo sapiens	95-104
26927051-3	2016	Thrombin also amplifies the response to the tissue injury, coagulation and platelet response, so the treatment of ACS is based on the combined use of both antiplatelet (such as aspirin, clopidogrel, prasugrel and ticagrelor) and antithrombotic drugs (unfractionated heparin, enoxaparin, fondaparinux and bivalirudin).	Heparin	266-273	coagulation factor II, thrombin	Homo sapiens	0-8
28856196-8	2016	NSA was mediated by the binding of ApoB100 to magnetic particles through its heparin binding sites.	Heparin	77-84	apolipoprotein B	Homo sapiens	35-42
26505285-0	2016	Studies on the interaction of heparin with lysozyme by multi-spectroscopic techniques and atomic force microscopy.	Heparin	30-37	lysozyme	Homo sapiens	43-51
26505285-1	2016	The interaction between heparin (Hep) and lysozyme (Lyso) in vitro was studied by fluorescence, UV-vis, circular dichroism (CD), resonance Rayleigh scattering (RRS) spectroscopy and atomic force microscopy (AFM) under normal physiological conditions.	Heparin	24-31	lysozyme	Homo sapiens	42-50
26505285-1	2016	The interaction between heparin (Hep) and lysozyme (Lyso) in vitro was studied by fluorescence, UV-vis, circular dichroism (CD), resonance Rayleigh scattering (RRS) spectroscopy and atomic force microscopy (AFM) under normal physiological conditions.	Heparin	24-31	lysozyme	Homo sapiens	52-56
26505285-1	2016	The interaction between heparin (Hep) and lysozyme (Lyso) in vitro was studied by fluorescence, UV-vis, circular dichroism (CD), resonance Rayleigh scattering (RRS) spectroscopy and atomic force microscopy (AFM) under normal physiological conditions.	Heparin	33-36	lysozyme	Homo sapiens	42-50
26505285-1	2016	The interaction between heparin (Hep) and lysozyme (Lyso) in vitro was studied by fluorescence, UV-vis, circular dichroism (CD), resonance Rayleigh scattering (RRS) spectroscopy and atomic force microscopy (AFM) under normal physiological conditions.	Heparin	33-36	lysozyme	Homo sapiens	52-56
26505285-3	2016	Fluorescence studies revealed that the emission quenching of Lyso with Hep was initiated by static quenching mechanism.	Heparin	71-74	lysozyme	Homo sapiens	61-65
26505285-4	2016	CD spectral studies showed that Hep induced conformational changes in the secondary structure of Lyso.	Heparin	32-35	lysozyme	Homo sapiens	97-101
26505285-5	2016	RRS spectra of Lyso showed the intensity of scattering was significantly increased with the addition of Hep and the enhanced RRS intensities were proportional to the concentration of Hep in a certain range.	Heparin	104-107	lysozyme	Homo sapiens	15-19
26505285-5	2016	RRS spectra of Lyso showed the intensity of scattering was significantly increased with the addition of Hep and the enhanced RRS intensities were proportional to the concentration of Hep in a certain range.	Heparin	183-186	lysozyme	Homo sapiens	15-19
26616450-6	2016	Heparin evenly distributed on the surface of the films and the heparin content increased with the increase of SPI content, and the hydrophilicity of the films was enhanced due to the grafted heparin.	Heparin	0-7	chromogranin A	Homo sapiens	110-113
26036455-0	2016	Thrombin generation assays for optimizing low molecular weight heparin dosing in pregnant women at risk of thrombosis--response to Ismail et al.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	0-8
26081310-0	2016	Thrombin generation assays for optimizing low molecular weight heparin dosing in pregnant women at risk of thrombosis.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	0-8
26616450-6	2016	Heparin evenly distributed on the surface of the films and the heparin content increased with the increase of SPI content, and the hydrophilicity of the films was enhanced due to the grafted heparin.	Heparin	63-70	chromogranin A	Homo sapiens	110-113
26553458-9	2016	CONCLUSIONS: Low circulating antithrombin activity is associated with lower heparin efficacy, which ultimately leads to a lower ability to suppress thrombin generation during CPB.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	33-41
26911942-17	2016	UFH might suppress LPS-activated NF-KappaB signaling pathway, contributing to the inhibitory effects of chemokines in HPMECs.	Heparin	0-3	nuclear factor kappa B subunit 1	Homo sapiens	33-42
26911942-0	2016	[Unfractionated heparin inhibits lipopolysaccharide-induced expression of chemokines in human endothelial cells through nuclear factor-KappaB signaling pathway].	Heparin	16-23	nuclear factor kappa B subunit 1	Homo sapiens	120-141
26820896-9	2016	CONCLUSIONS: We propose that the increases in the serum activin A, B and follistatin result from a combination of factors; the acute phase response, the reperfusion response and the use of heparin-based anti-coagulants.	Heparin	189-196	follistatin	Homo sapiens	73-84
26911942-1	2016	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of chemokines and nuclear factor-KappaB (NF-KappaB) signaling pathway.	Heparin	53-60	nuclear factor kappa B subunit 1	Homo sapiens	132-153
26911942-1	2016	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of chemokines and nuclear factor-KappaB (NF-KappaB) signaling pathway.	Heparin	53-60	nuclear factor kappa B subunit 1	Homo sapiens	155-164
26911942-1	2016	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of chemokines and nuclear factor-KappaB (NF-KappaB) signaling pathway.	Heparin	62-65	nuclear factor kappa B subunit 1	Homo sapiens	132-153
26911942-1	2016	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of chemokines and nuclear factor-KappaB (NF-KappaB) signaling pathway.	Heparin	62-65	nuclear factor kappa B subunit 1	Homo sapiens	155-164
26911942-7	2016	The cells were harvested 1 hour after LPS challenge, and the nuclear translocation of NF-KappaB was determined by immunofluorescence assay to detect the effect of UFH on NF-KappaB activation.	Heparin	163-166	nuclear factor kappa B subunit 1	Homo sapiens	170-179
26699104-10	2016	In contrast, beta-endorphin amyloid fibrils obtained in the presence of heparin demonstrated distinctly different behavior, which we attributed to a dramatic change of the amyloid structure.	Heparin	72-79	proopiomelanocortin	Homo sapiens	13-27
26643617-7	2016	The thrombin clotting time mediated by SAHM TBA15/TBA29-Au NPs was &gt;10 times longer than that of four commercially available drugs (heparin, argatroban, hirudin, or warfarin).	Heparin	135-142	coagulation factor II, thrombin	Homo sapiens	4-12
26713365-5	2016	In contrast, addition of heparin to the medium suppressed MCP-1 release in a dose-dependent manner.	Heparin	25-32	mast cell protease 1	Mus musculus	58-63
26794266-0	2016	In vivo vascularization of MSC-loaded porous hydroxyapatite constructs coated with VEGF-functionalized collagen/heparin multilayers.	Heparin	112-119	vascular endothelial growth factor A	Homo sapiens	83-87
26551597-12	2016	Moreover, we show that CXCL9(74-103) competes with DENV envelope protein domain III for binding to heparin.	Heparin	99-106	C-X-C motif chemokine ligand 9	Homo sapiens	23-28
26790955-5	2016	Moreover, kallistatin via its heparin-binding site antagonized Wnt3a-induced cancer cell proliferation and increased PPARgamma expression.	Heparin	30-37	peroxisome proliferator activated receptor gamma	Homo sapiens	117-126
26955355-2	2015	Heparins seem to act by interfering with BMP6 signaling pathways that control the expression of liver hepcidin, causing the suppression of SMAD1/5/8 phosphorylation.	Heparin	0-8	bone morphogenetic protein 6	Homo sapiens	41-45
26494902-5	2016	Our results show that heparin treatment of mdx mice caused a significant ~1.5- to 3-fold increase in utrophin A expression in diaphragm, extensor digitorum longus and tibialis anterior (TA) muscles.	Heparin	22-29	utrophin	Mus musculus	101-109
26431853-1	2016	PURPOSE: The immature coagulation system during infancy has age-related physiological differences in proteins that contribute to significant variation in heparin responsiveness through alterations in heparin-enhanced thrombin inhibition.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	217-225
27651974-4	2016	We report three cases of successful deep inferior epigastric perforator (DIEP) flap harvest despite patients injecting therapeutic doses of low molecular weight heparin into their abdomens for thrombosed central venous lines (portacaths ) used for administering primary chemotherapy in breast cancer.	Heparin	161-168	arachidonate 5-lipoxygenase activating protein	Homo sapiens	79-83
26494902-0	2016	Combinatorial therapeutic activation with heparin and AICAR stimulates additive effects on utrophin A expression in dystrophic muscles.	Heparin	42-49	utrophin	Mus musculus	91-99
26476401-1	2016	The glycosaminoglycan heparin and its derivatives act strongly on blood coagulation, controlling the activity of serine protease inhibitors in plasma.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	113-128
26494902-6	2016	In agreement with these findings, heparin-treated diaphragm and TA muscle fibers showed an accumulation of utrophin A and beta-dystroglycan along their sarcolemma and displayed improved morphology and structural integrity.	Heparin	34-41	utrophin	Mus musculus	107-115
26494902-7	2016	Moreover, combinatorial drug treatment using both heparin and 5-amino-4-imidazolecarboxamide riboside (AICAR), the latter targeting 5" adenosine monophosphate-activated protein kinase and the transcriptional activation of utrophin A, caused an additive effect on utrophin A expression in dystrophic muscle.	Heparin	50-57	utrophin	Mus musculus	222-230
26494902-7	2016	Moreover, combinatorial drug treatment using both heparin and 5-amino-4-imidazolecarboxamide riboside (AICAR), the latter targeting 5" adenosine monophosphate-activated protein kinase and the transcriptional activation of utrophin A, caused an additive effect on utrophin A expression in dystrophic muscle.	Heparin	50-57	utrophin	Mus musculus	263-271
26478015-0	2015	Heparin desulfation modulates VEGF release and angiogenesis in diabetic wounds.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	30-34
26494902-8	2016	These findings establish that heparin is a relevant therapeutic agent for treating DMD, and illustrate that combinatorial treatment of heparin with AICAR may serve as an effective strategy to further increase utrophin A expression in dystrophic muscle via activation of distinct signaling pathways.	Heparin	135-142	utrophin	Mus musculus	209-217
26613641-10	2016	The PCCs containing low or no heparin enhanced the area under the curve of thrombin generation and peak thrombin several fold relative to the heparin-containing PCCs (p&lt;0.01).	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	75-83
26613641-10	2016	The PCCs containing low or no heparin enhanced the area under the curve of thrombin generation and peak thrombin several fold relative to the heparin-containing PCCs (p&lt;0.01).	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	104-112
26613641-11	2016	One of the PCCs containing heparin even decreased peak thrombin generation by ~90% compared with baseline (p&lt;0.01).	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	55-63
26525852-0	2015	Affinity of the heparin binding motif of Noggin1 to heparan sulfate and its visualization in the embryonic tissues.	Heparin	16-23	noggin S homeolog	Xenopus laevis	41-48
26627376-0	2015	Mapping the heparin-binding site of the osteoinductive protein NELL1 by site-directed mutagenesis.	Heparin	12-19	neural EGFL like 1	Homo sapiens	63-68
26627376-4	2015	Major heparin-binding sites were identified on the three-dimensional structural model of the TSPN domain of NELL1.	Heparin	6-13	neural EGFL like 1	Homo sapiens	108-113
26627376-5	2015	Mutant analysis of the heparin-binding sites indicated that the heparin-binding activity of the TSPN domain is involved in interaction of NELL1 with cell surface proteoglycans.	Heparin	23-30	neural EGFL like 1	Homo sapiens	138-143
26627376-5	2015	Mutant analysis of the heparin-binding sites indicated that the heparin-binding activity of the TSPN domain is involved in interaction of NELL1 with cell surface proteoglycans.	Heparin	64-71	neural EGFL like 1	Homo sapiens	138-143
33429678-11	2015	Finally, the conjugation of heparin on GelNB led to suppressed Huh7 cell metabolic activity and improved CYP3A4 activity and urea secretion.	Heparin	28-35	cytochrome P450 family 3 subfamily A member 4	Homo sapiens	105-111
26453517-6	2015	The stimulatory effect of IP3 is eliminated by heparin, an IP3 receptor (IP3R) antagonist that blocks the IP3-binding site, but not by xestospongin C, the IP3R antagonist that has no effect on the IP3-binding site.	Heparin	47-54	inositol 1,4,5-trisphosphate receptor type 2	Homo sapiens	59-71
26453517-6	2015	The stimulatory effect of IP3 is eliminated by heparin, an IP3 receptor (IP3R) antagonist that blocks the IP3-binding site, but not by xestospongin C, the IP3R antagonist that has no effect on the IP3-binding site.	Heparin	47-54	inositol 1,4,5-trisphosphate receptor type 2	Homo sapiens	73-77
26525852-2	2015	Here we used synthetic FITC labeled heparin binding motif (HBM peptide) of the Xenopus laevis secreted BMP inhibitor Noggin1 to study its diffusion along the surface of the heparin beads by FRAP method.	Heparin	36-43	noggin S homeolog	Xenopus laevis	117-124
26525852-2	2015	Here we used synthetic FITC labeled heparin binding motif (HBM peptide) of the Xenopus laevis secreted BMP inhibitor Noggin1 to study its diffusion along the surface of the heparin beads by FRAP method.	Heparin	173-180	noggin S homeolog	Xenopus laevis	117-124
26352518-12	2015	The fully formed NGC"s contained plasmin-degradable PEG/heparin scaffolds that developed linear gradients in reversibly bound GDNF.	Heparin	56-63	glial cell derived neurotrophic factor	Homo sapiens	126-130
26141306-12	2015	Mean high-sensitivity C-reactive protein level was 11.6+-5.3 (SE) mg/L lower for patients in the heparin group (P=0.03).	Heparin	97-104	C-reactive protein	Homo sapiens	22-40
26370927-0	2015	Controlled dual delivery of fibroblast growth factor-2 and Interleukin-10 by heparin-based coacervate synergistically enhances ischemic heart repair.	Heparin	77-84	interleukin 10	Mus musculus	59-73
26370927-3	2015	We investigated the bioactivity and therapeutic potential of an injectable, heparin-based coacervate co-delivering an angiogenic factor, fibroblast growth factor-2 (FGF2), and an anti-inflammatory cytokine, Interleukin-10 (IL-10) in a spatially and temporally controlled manner.	Heparin	76-83	interleukin 10	Mus musculus	207-221
26370927-3	2015	We investigated the bioactivity and therapeutic potential of an injectable, heparin-based coacervate co-delivering an angiogenic factor, fibroblast growth factor-2 (FGF2), and an anti-inflammatory cytokine, Interleukin-10 (IL-10) in a spatially and temporally controlled manner.	Heparin	76-83	interleukin 10	Mus musculus	223-228
26272754-2	2015	Here we used isothermal titration calorimetry and screened a set of peptides derived from the extracellular domains of Cav1.2alpha1 to identify putative binding sites between the channel and hyaluronic acid or another class of polyanionic glycans, such as heparin/heparan sulfates.	Heparin	256-263	caveolin 1	Homo sapiens	119-131
25527412-1	2015	Higher levels of fibrinogen or cholesterol were associated with improved hearing recovery in SSHL patients after treatment with HELP-apheresis (Heparin-induced extracorporeal LDL precipitation apheresis).	Heparin	144-151	fibrinogen beta chain	Homo sapiens	17-27
26272754-3	2015	None of the tested peptides showed detectable interaction with hyaluronic acid, but two peptides derived from the first pore-forming domain of Cav1.2alpha1 subunit bound to heparin.	Heparin	173-180	caveolin 1	Homo sapiens	143-155
26272754-5	2015	The Cav1.2alpha1 first pore forming segment that contained both peptides maintained a high affinity for heparin (~23 muM), integrating their enthalpic and entropic binding contributions.	Heparin	104-111	caveolin 1	Homo sapiens	4-16
26272754-5	2015	The Cav1.2alpha1 first pore forming segment that contained both peptides maintained a high affinity for heparin (~23 muM), integrating their enthalpic and entropic binding contributions.	Heparin	104-111	latexin	Homo sapiens	117-120
26272754-6	2015	Interaction between heparin and recombinant as well as native full-length neuronal Cav1.2alpha1 channels was confirmed using the heparin-agarose pull down assay.	Heparin	20-27	caveolin 1	Homo sapiens	83-95
26272754-6	2015	Interaction between heparin and recombinant as well as native full-length neuronal Cav1.2alpha1 channels was confirmed using the heparin-agarose pull down assay.	Heparin	129-136	caveolin 1	Homo sapiens	83-95
26306634-2	2015	Here, we identify the molecular features in the protein and in heparin required for binding and their effects on the potentiation of TGF-beta1"s activity on hMSCs.	Heparin	63-70	transforming growth factor beta 1	Homo sapiens	133-142
26306634-5	2015	Heparin-derived oligosaccharides as short as degree of polymerization (dp) 4 have a weak ability to compete for TGF-beta1 binding to heparin, which increases with the length of the oligosaccharide to reach a maximum between dp18 and dp24.	Heparin	133-140	transforming growth factor beta 1	Homo sapiens	112-121
26306634-6	2015	In cell-based assays, heparin, 2-O-, 6-O- and N-desulfated re-N-acetylated heparin and oligosaccharides 14-24 saccharides (dp14-24) in length all increased the phosphorylation of mothers against decapentaplegic homolog 2 (SMAD2) after 6 h of stimulation with TGF-beta1.	Heparin	22-29	transforming growth factor beta 1	Homo sapiens	259-268
26306634-6	2015	In cell-based assays, heparin, 2-O-, 6-O- and N-desulfated re-N-acetylated heparin and oligosaccharides 14-24 saccharides (dp14-24) in length all increased the phosphorylation of mothers against decapentaplegic homolog 2 (SMAD2) after 6 h of stimulation with TGF-beta1.	Heparin	75-82	transforming growth factor beta 1	Homo sapiens	259-268
26306634-7	2015	The results provide the structural basis for a model of heparin/heparan sulfate binding to TGF-beta1 and demonstrate that the features in the polysaccharide required for binding are not identical to those required for sustaining the signaling by TGF-beta1 in hMSCs.	Heparin	56-63	transforming growth factor beta 1	Homo sapiens	91-100
26396093-1	2015	The CD32a immunoglobulin G (IgG) receptor (Fcgamma receptor IIa) is a potential therapeutic target for diseases in which IgG immune complexes (ICs) mediate inflammation, such as heparin-induced thrombocytopenia, rheumatoid arthritis, and systemic lupus erythematosus.	Heparin	178-185	Fc receptor, IgG, low affinity IIb	Mus musculus	4-8
26713050-3	2015	Basic fibroblast growth factor (bFGF) was loaded onto the heparin-immobilized scaffold by a simple dipping method.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	0-30
26713050-3	2015	Basic fibroblast growth factor (bFGF) was loaded onto the heparin-immobilized scaffold by a simple dipping method.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	32-36
26554451-0	2015	Mechanical fibrinogen-depletion supports heparin-free mesenchymal stem cell propagation in human platelet lysate.	Heparin	41-48	fibrinogen beta chain	Homo sapiens	11-21
26260610-4	2015	The direct thrombin inhibitor bivalirudin overcomes several shortcomings of heparins and has demonstrated a significant reduction in bleeding outcomes and net adverse cardiac events at the cost of increased acute stent thrombosis.	Heparin	76-84	coagulation factor II, thrombin	Homo sapiens	11-19
27785363-0	2015	Hydrolysis and Sulfation Pattern Effects on Release of Bioactive Bone Morphogenetic Protein-2 from Heparin-Based Microparticles.	Heparin	99-106	bone morphogenetic protein 2	Mus musculus	65-93
27785363-1	2015	Glycosaminoglycans (GAGs) such as heparin are promising materials for growth factor delivery due to their ability to efficiently bind positively charged growth factors including bone morphogenetic protein-2 (BMP-2) through their negatively charged sulfate groups.	Heparin	34-41	bone morphogenetic protein 2	Mus musculus	178-206
27785363-1	2015	Glycosaminoglycans (GAGs) such as heparin are promising materials for growth factor delivery due to their ability to efficiently bind positively charged growth factors including bone morphogenetic protein-2 (BMP-2) through their negatively charged sulfate groups.	Heparin	34-41	bone morphogenetic protein 2	Mus musculus	208-213
27785363-2	2015	Therefore, the goal of this study was to examine BMP-2 release from heparin-based microparticles (MPs) after first, incorporating a hydrolytically degradable crosslinker and varying heparin content within MPs to alter MP degradation and second, altering the sulfation pattern of heparin within MPs to vary BMP-2 binding and release.	Heparin	68-75	bone morphogenetic protein 2	Mus musculus	49-54
27785363-5	2015	Similarly, BMP-2 bioactivity in more sulfated heparin MP groups was at least four-fold higher than soluble BMP-2 and less sulfated heparin MP groups, as determined by an established C2C12 cell alkaline phosphatase (ALP) assay.	Heparin	46-53	bone morphogenetic protein 2	Mus musculus	11-16
27785363-6	2015	Ultimately, the two most sulfated 10 wt% heparin MP formulations were able to efficiently load and release BMP-2 while enhancing BMP-2 bioactivity, making them promising candidates for future growth factor delivery applications.	Heparin	41-48	bone morphogenetic protein 2	Mus musculus	107-112
27785363-6	2015	Ultimately, the two most sulfated 10 wt% heparin MP formulations were able to efficiently load and release BMP-2 while enhancing BMP-2 bioactivity, making them promising candidates for future growth factor delivery applications.	Heparin	41-48	bone morphogenetic protein 2	Mus musculus	129-134
26465941-2	2015	Fibroblast growth factor-2 (FGF-2) is one of the prototypes of the large family of growth factors that bind heparin.	Heparin	108-115	fibroblast growth factor 2	Homo sapiens	0-26
26465941-2	2015	Fibroblast growth factor-2 (FGF-2) is one of the prototypes of the large family of growth factors that bind heparin.	Heparin	108-115	fibroblast growth factor 2	Homo sapiens	28-33
26219861-0	2015	TGFbeta functionalized starPEG-heparin hydrogels modulate human dermal fibroblast growth and differentiation.	Heparin	31-38	transforming growth factor beta 1	Homo sapiens	0-7
26219861-10	2015	Reversibly conjugated TGFbeta1 was demonstrated to be constantly released from starPEG-heparin hydrogels for several days and capable of inducing myofibroblast differentiation of fibroblasts as determined by induction of collagen type I, ED-A-Fibronectin expression and incorporation of alpha smooth muscle actin and palladin into F-actin stress fibers.	Heparin	87-94	transforming growth factor beta 1	Homo sapiens	22-30
25736986-13	2015	In univariate and multivariable logistic regression analysis, only the time of the initiation of heparin after admission was associated with the occurrence of VTE (median, IQR) 46 h (17-86) HDG versus 105 h (56-167) TDG; OR 1.2 (1.1-1.3); P &lt; 0.001.	Heparin	97-104	thymine DNA glycosylase	Homo sapiens	216-219
25880826-3	2015	Because it has been shown that heparin modulates binding of KGF to the KGF receptor and subsequently affects cellular proliferation induced by the KGF mitogenic signal, it is critical to understand the drug-drug interactions between palifermin and heparin, particularly because of heparin"s narrow therapeutic margin.	Heparin	31-38	fibroblast growth factor 7	Homo sapiens	60-63
25880826-3	2015	Because it has been shown that heparin modulates binding of KGF to the KGF receptor and subsequently affects cellular proliferation induced by the KGF mitogenic signal, it is critical to understand the drug-drug interactions between palifermin and heparin, particularly because of heparin"s narrow therapeutic margin.	Heparin	31-38	fibroblast growth factor 7	Homo sapiens	71-74
25880826-3	2015	Because it has been shown that heparin modulates binding of KGF to the KGF receptor and subsequently affects cellular proliferation induced by the KGF mitogenic signal, it is critical to understand the drug-drug interactions between palifermin and heparin, particularly because of heparin"s narrow therapeutic margin.	Heparin	31-38	fibroblast growth factor 7	Homo sapiens	71-74
26276817-11	2015	These findings define new mechanisms through which FGF-2 and Ang-1* modulate the outcome of intestinal bleeding complications induced by PPS in mice and may have wider clinical implications for critically ill children treated with heparin-like drugs.	Heparin	231-238	angiopoietin 1	Mus musculus	61-66
25804370-1	2015	Heparin-induced thrombocytopenia (HIT) is a prothrombotic condition and it is associated with increased in vivo thrombin generation that needs to be treated with non-heparin anticoagulants such as direct thrombin inhibitors (DTIs).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	112-120
25804370-1	2015	Heparin-induced thrombocytopenia (HIT) is a prothrombotic condition and it is associated with increased in vivo thrombin generation that needs to be treated with non-heparin anticoagulants such as direct thrombin inhibitors (DTIs).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	204-212
25969127-8	2015	Heparin reduced MSC-associated thrombosis incorporating platelets and VWF within the microvasculature.	Heparin	0-7	von Willebrand factor	Homo sapiens	70-73
26199422-7	2015	We also show that the vaspin-inhibition rate for KLK7 can be modestly increased by heparin and demonstrate that vaspin is a heparin-binding serpin.	Heparin	83-90	serpin family A member 12	Homo sapiens	22-28
26212474-4	2015	Various sulfated and sulfonated polymers were screened, and poly(vinyl sulfonate) (pVS) was identified as the strongest heparin-mimicking polymer in its ability to enhance binding of basic fibroblast growth factor (bFGF) to FGFR.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	183-213
26212474-4	2015	Various sulfated and sulfonated polymers were screened, and poly(vinyl sulfonate) (pVS) was identified as the strongest heparin-mimicking polymer in its ability to enhance binding of basic fibroblast growth factor (bFGF) to FGFR.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	215-219
25998703-4	2015	The present study confirmed the anti-inflammatory effects of heparin in lipopolysaccharide (LPS)-induced murine peritoneal macrophages through decreasing the levels of the inflammatory cytokines tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL-6), IL-8 and IL-1beta.	Heparin	61-68	tumor necrosis factor	Mus musculus	195-222
25998703-4	2015	The present study confirmed the anti-inflammatory effects of heparin in lipopolysaccharide (LPS)-induced murine peritoneal macrophages through decreasing the levels of the inflammatory cytokines tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL-6), IL-8 and IL-1beta.	Heparin	61-68	tumor necrosis factor	Mus musculus	224-233
25998703-4	2015	The present study confirmed the anti-inflammatory effects of heparin in lipopolysaccharide (LPS)-induced murine peritoneal macrophages through decreasing the levels of the inflammatory cytokines tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL-6), IL-8 and IL-1beta.	Heparin	61-68	interleukin 6	Mus musculus	236-249
25998703-4	2015	The present study confirmed the anti-inflammatory effects of heparin in lipopolysaccharide (LPS)-induced murine peritoneal macrophages through decreasing the levels of the inflammatory cytokines tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL-6), IL-8 and IL-1beta.	Heparin	61-68	interleukin 6	Mus musculus	251-255
25998703-4	2015	The present study confirmed the anti-inflammatory effects of heparin in lipopolysaccharide (LPS)-induced murine peritoneal macrophages through decreasing the levels of the inflammatory cytokines tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL-6), IL-8 and IL-1beta.	Heparin	61-68	interleukin 1 beta	Mus musculus	267-275
26156753-9	2015	Kallistatin via its heparin-binding site blocked TGF-beta-induced miR-21, Snail1 expression, and ROS formation, as wild-type kallistatin, but not heparin-binding site mutant kallistatin, exerted the effect.	Heparin	20-27	transforming growth factor beta 1	Homo sapiens	49-57
26156753-11	2015	This is the first study to demonstrate that kallistatin"s heparin-binding site is crucial for preventing TGF-beta-induced miR-21 and oxidative stress, while its active site is key for stimulating the expression of antioxidant genes via interaction with an endothelial surface tyrosine kinase.	Heparin	58-65	transforming growth factor beta 1	Homo sapiens	105-113
25959412-6	2015	Interestingly, heparin did not only significantly increase mRNA expression and enzyme activity of the osteogenic marker alkaline phosphatase (ALP), but it also promoted mineralization during osteogenic differentiation and conversion.	Heparin	15-22	alkaline phosphatase, placental	Homo sapiens	120-140
25959412-6	2015	Interestingly, heparin did not only significantly increase mRNA expression and enzyme activity of the osteogenic marker alkaline phosphatase (ALP), but it also promoted mineralization during osteogenic differentiation and conversion.	Heparin	15-22	alkaline phosphatase, placental	Homo sapiens	142-145
25959412-9	2015	Moreover, luciferase reporter assays, inhibitor experiments and gene expression analyses revealed that heparin had putative permissive effects on osteogenic signaling via the BMP pathway and reduced the mRNA expression of the Wnt pathway inhibitors dickkopf 1 (DKK1) and sclerostin (SOST).	Heparin	103-110	sclerostin	Homo sapiens	271-281
25959412-9	2015	Moreover, luciferase reporter assays, inhibitor experiments and gene expression analyses revealed that heparin had putative permissive effects on osteogenic signaling via the BMP pathway and reduced the mRNA expression of the Wnt pathway inhibitors dickkopf 1 (DKK1) and sclerostin (SOST).	Heparin	103-110	sclerostin	Homo sapiens	283-287
25483839-1	2015	While antithrombin (AT) has small basal inhibitory activity, it reaches its full inhibitory potential against activated blood coagulation factors, FXa, FIXa, and FIIa (thrombin), via an allosteric and/or template (bridging) mechanism by the action of heparin, heparan sulfate, or heparin-mimetic pentasaccharides (PS).	Heparin	251-258	coagulation factor II, thrombin	Homo sapiens	10-18
26408899-0	2015	Report: Heparin-induced thrombocytopenia associated with cardiopulmonary bypass: Preliminary attempt with recombinant human thrombopoietin therapy.	Heparin	8-15	thrombopoietin	Homo sapiens	124-138
26186963-1	2015	INTRODUCTION: beta-antithrombin, the minor antithrombin glycoform in plasma, is probably the major thrombin inhibitor in vivo because of its high heparin affinity.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	23-31
26605215-2	2015	MATERIALS AND METHODS: In the present work, hBFGF produced by engineered Escherichia coli and purified by cation exchange and heparin affinity chromatography, was PEGylated under appropriate condition employing 10 kD polyethylene glycol.	Heparin	126-133	fibroblast growth factor 2	Homo sapiens	44-49
26251446-5	2015	A panel of six Myc-tagged gremlin mutants, MGR-1-MGR-6 (MGR, mutant gremlin), each containing different combinations of targeted substitutions, all showed markedly reduced affinity for heparin as demonstrated by their NaCl elution on heparin affinity chromatography, thus verifying our predictions.	Heparin	185-192	MGR1	Homo sapiens	43-54
26045608-8	2015	In particular, blockage of thrombin exosites with compounds specific for exosite I (hirudin and HD1 aptamer) or exosite II (heparin and HD22 aptamer) impaired the COMP-thrombin interaction, indicating a 2-site binding mechanism.	Heparin	124-131	coagulation factor II	Mus musculus	27-35
26251446-0	2015	Mapping the heparin-binding site of the BMP antagonist gremlin by site-directed mutagenesis based on predictive modelling.	Heparin	12-19	gremlin 1, DAN family BMP antagonist	Homo sapiens	55-62
26251446-3	2015	Gremlin binds strongly to heparin and heparan sulfate and, in the present study, we sought to investigate its heparin-binding site.	Heparin	26-33	gremlin 1, DAN family BMP antagonist	Homo sapiens	0-7
26251446-3	2015	Gremlin binds strongly to heparin and heparan sulfate and, in the present study, we sought to investigate its heparin-binding site.	Heparin	110-117	gremlin 1, DAN family BMP antagonist	Homo sapiens	0-7
26251446-5	2015	A panel of six Myc-tagged gremlin mutants, MGR-1-MGR-6 (MGR, mutant gremlin), each containing different combinations of targeted substitutions, all showed markedly reduced affinity for heparin as demonstrated by their NaCl elution on heparin affinity chromatography, thus verifying our predictions.	Heparin	185-192	gremlin 1, DAN family BMP antagonist	Homo sapiens	26-33
26251446-5	2015	A panel of six Myc-tagged gremlin mutants, MGR-1-MGR-6 (MGR, mutant gremlin), each containing different combinations of targeted substitutions, all showed markedly reduced affinity for heparin as demonstrated by their NaCl elution on heparin affinity chromatography, thus verifying our predictions.	Heparin	185-192	gremlin 1, DAN family BMP antagonist	Homo sapiens	68-75
26045608-8	2015	In particular, blockage of thrombin exosites with compounds specific for exosite I (hirudin and HD1 aptamer) or exosite II (heparin and HD22 aptamer) impaired the COMP-thrombin interaction, indicating a 2-site binding mechanism.	Heparin	124-131	coagulation factor II	Mus musculus	168-176
25782437-9	2015	In conclusion, thrombin inhibition with bivalirudin alone was associated with reduced 30-day major bleeding and 1-year all-cause mortality compared with heparin plus GPI in diabetic patients undergoing PCI.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	15-23
25913754-0	2015	Evaluation of a multi-target direct thrombin inhibitor dosing and titration guideline for patients with suspected heparin-induced thrombocytopenia.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	36-44
25701313-2	2015	METHODS: A heparin-functionalized murine anti-CEA monoclonal antibody (mAb), T84.66-heparin (T84.66-Hep), was chemically synthesized and characterized for specific binding to CEA overexpressed cells.	Heparin	11-18	CEA cell adhesion molecule 3	Homo sapiens	46-49
25960020-5	2015	Complexes of PF4/low-molecular-weight heparin and complexes composed of heparin and murine PF4, protamine or lysozyme are internalized similarly, suggesting a common endocytic pathway.	Heparin	38-45	platelet factor 4	Mus musculus	13-16
26280503-1	2015	BACKGROUND: It has been known for decades that many cytokines, such as IL-2, IL-6, and IL-12, bind to heparin.	Heparin	102-109	interleukin 2	Homo sapiens	71-75
26280503-1	2015	BACKGROUND: It has been known for decades that many cytokines, such as IL-2, IL-6, and IL-12, bind to heparin.	Heparin	102-109	interleukin 6	Homo sapiens	77-81
25701313-2	2015	METHODS: A heparin-functionalized murine anti-CEA monoclonal antibody (mAb), T84.66-heparin (T84.66-Hep), was chemically synthesized and characterized for specific binding to CEA overexpressed cells.	Heparin	11-18	CEA cell adhesion molecule 3	Homo sapiens	175-178
25701313-2	2015	METHODS: A heparin-functionalized murine anti-CEA monoclonal antibody (mAb), T84.66-heparin (T84.66-Hep), was chemically synthesized and characterized for specific binding to CEA overexpressed cells.	Heparin	84-91	CEA cell adhesion molecule 3	Homo sapiens	46-49
26134993-14	2015	Postoperative thrombin generation capacity correlates to residual heparin effect.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	14-22
25925992-9	2015	However, median values for thrombin-antithrombin complex passed above the URL with increasing tendency, starting at 2 h post-PCI in the UFH-alone arm but not in rivaroxaban-treated patients.	Heparin	136-139	coagulation factor II, thrombin	Homo sapiens	27-35
26201468-10	2015	RESULTS: We demonstrate that IMB-R1 is minimally cross-reactive for other FGFRs, and that it potently and specifically inhibits binding of heparin to FGFR1.	Heparin	139-146	fibroblast growth factor receptor 1	Homo sapiens	150-155
26201468-15	2015	CONCLUSION: Our study suggests that blocking HS interaction with the heparin-binding domains of FGFR1 inhibited cancer cell growth, which can be an attractive strategy to inactivate cancer-related heparin-binding proteins.	Heparin	69-76	fibroblast growth factor receptor 1	Homo sapiens	96-101
25931306-4	2015	At equal concentrations, high MW heparin both loaded and retained the greatest amount of TGFbeta1, and had the slowest release kinetics, primarily due to the higher affinity with TGFbeta1 compared to low MW or unfractionated heparin.	Heparin	33-40	transforming growth factor beta 1	Homo sapiens	89-97
25931306-4	2015	At equal concentrations, high MW heparin both loaded and retained the greatest amount of TGFbeta1, and had the slowest release kinetics, primarily due to the higher affinity with TGFbeta1 compared to low MW or unfractionated heparin.	Heparin	33-40	transforming growth factor beta 1	Homo sapiens	179-187
25931306-5	2015	Subsequently, we tested the effect of TGFbeta1, presented from various heparin-containing matrices, to differentiate a versatile population of Sca-1(+)/CD45(-) cardiac progenitor cells (CPCs) into endothelial cells and form vascular-like networks in vitro.	Heparin	71-78	transforming growth factor beta 1	Homo sapiens	38-46
26138239-12	2015	Both alone and in the presence of heparin, FGF1 led to increased MAPK-signaling in primary lung fibroblasts.	Heparin	34-41	fibroblast growth factor 1	Homo sapiens	43-47
26138239-14	2015	In addition, FGF1 + heparin increased apoptosis and cell migration.	Heparin	20-27	fibroblast growth factor 1	Homo sapiens	13-17
25810046-2	2015	Negatively charged heparin is known to form polyelectrolyte complexes with BMP-2 to prevent deactivation and enhance the osteoinduction capability of BMP-2.	Heparin	19-26	bone morphogenetic protein 2	Mus musculus	75-80
25495659-7	2015	After a hemodialytic standard procedure with heparin, we demonstrated a significant reduction of triglyceride, an increase of HDL-cholesterol levels, and a raise of small very-low-density lipoprotein, intermediate-density lipoproteins (IDL), apoE-rich particles, and non-HDL-cholesterol levels.	Heparin	45-52	apolipoprotein E	Homo sapiens	242-246
25810046-2	2015	Negatively charged heparin is known to form polyelectrolyte complexes with BMP-2 to prevent deactivation and enhance the osteoinduction capability of BMP-2.	Heparin	19-26	bone morphogenetic protein 2	Mus musculus	150-155
25585956-0	2015	Enhanced Anti-Angiogenic Effect of Low Molecular Weight Heparin-Bile Acid Conjugates by Co-Administration of a Selective COX-2 Inhibitor.	Heparin	56-63	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	121-126
25891187-7	2015	A similar acceleration can also be achieved by a stabilized mutant form of FGF-1 formulated in the absence of heparin.	Heparin	110-117	fibroblast growth factor 1	Mus musculus	75-80
25893351-4	2015	Heparin-modified PEC carrying reduced BMP-2 doses of 0.5 mug was demonstrated to achieve consistent spinal fusion with reduction of complications in rodent model.	Heparin	0-7	bone morphogenetic protein 2	Sus scrofa	38-43
25893351-7	2015	The BMP-2 was delivered using heparin-modified alginate microbeads loaded into biodegradable cage.	Heparin	30-37	bone morphogenetic protein 2	Sus scrofa	4-9
25647100-1	2015	BACKGROUND: The interaction between heparin and thrombin is a vital step in the blood (anti)coagulation process.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	48-56
25979342-0	2015	Synergistic Binding of Vascular Endothelial Growth Factor-A and Its Receptors to Heparin Selectively Modulates Complex Affinity.	Heparin	81-88	vascular endothelial growth factor A	Homo sapiens	23-59
25979342-5	2015	We defined interactions and structural requirements for heparin/HS interactions with VEGF receptor (VEGFR)-1, NRP-1, and VEGF165 in complex with VEGFR-2 and NRP-1.	Heparin	56-63	fms related receptor tyrosine kinase 1	Homo sapiens	85-108
26036990-7	2015	In binding to dynorphins A and B, Mac-1 cooperated with cell surface proteoglycans since both anti-Mac-1 function-blocking reagents and heparin were required to block adhesion.	Heparin	136-143	integrin alpha M	Mus musculus	34-39
25897078-7	2015	Binding of hTSP-1 is charge-dependent and inhibited by heparin.	Heparin	55-62	thrombospondin 1	Homo sapiens	11-17
25647100-4	2015	RESULTS: Well-separated single molecules of heparin covalently attached to mixed self-assembled monolayers are demonstrated, whereby interaction forces with thrombin can be measured via atomic force microscopy-based spectroscopy.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	157-165
25647100-8	2015	GENERAL SIGNIFICANCE: These results contribute to understanding the role of specific and nonspecific forces that drive heparin-thrombin interactions under applied force or flow conditions.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	127-135
25846343-10	2015	Prothrombin complex concentrates contain small amounts of heparin and are contraindicated in patients with heparin-induced thrombocytopenia.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	0-11
25256819-0	2015	Tailoring of the dopamine coated surface with VEGF loaded heparin/poly-L-lysine particles for anticoagulation and accelerate in situ endothelialization.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	46-50
25256819-4	2015	In this study, novel VEGF-loaded heparin/poly-L-lysine (Hep/PLL) particles were developed and immobilized on a dopamine coated titanium surface.	Heparin	33-40	vascular endothelial growth factor A	Homo sapiens	21-25
25873395-7	2015	Heparin dissociated LPL from the N-terminal domain, and partially from wild type GPIHBP1, but was unable to elute the enzyme from the Ly6 domain.	Heparin	0-7	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	81-88
25702768-8	2015	Heparin (Sdc1 analogue) and SB203580 (a p38 MAPK inhibitor), instead of insulin, alleviated Sdc1 destruction and HPSE overexpression, and effectively prevented against the reductions of tight junctions and the abnormality of intestinal permeability in HG conditions.	Heparin	0-7	heparanase	Mus musculus	113-117
25894217-1	2015	Heparin is a highly sulfated, long, and linear polysaccharide, which can inhibit tumor growth by interacting with growth factors such as bFGF and VEGF.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	137-141
25894217-1	2015	Heparin is a highly sulfated, long, and linear polysaccharide, which can inhibit tumor growth by interacting with growth factors such as bFGF and VEGF.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	146-150
25813285-10	2015	The stimulating effect of thrombin on CXCL8 could be inhibited by heparin, whereas heparin had no impact on thrombin-induced CXCL1 and CCL2.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	26-34
25945799-0	2015	Cellular Responses Modulated by FGF-2 Adsorbed on Albumin/Heparin Layer-by-Layer Assemblies.	Heparin	58-65	fibroblast growth factor 2	Bos taurus	32-37
25945799-2	2015	In this paper, we report on the fabrication of albumin/heparin (Alb/Hep) assemblies for controlled binding of basic fibroblast growth factor (FGF-2).	Heparin	55-62	fibroblast growth factor 2	Bos taurus	110-140
25945799-2	2015	In this paper, we report on the fabrication of albumin/heparin (Alb/Hep) assemblies for controlled binding of basic fibroblast growth factor (FGF-2).	Heparin	55-62	fibroblast growth factor 2	Bos taurus	142-147
25771020-2	2015	To this end, we engineered a surface consisting of heparin bound to poly-l-lysine to permit immobilization of VEGF through the C-terminal heparin-binding domain.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	110-114
25771020-2	2015	To this end, we engineered a surface consisting of heparin bound to poly-l-lysine to permit immobilization of VEGF through the C-terminal heparin-binding domain.	Heparin	138-145	vascular endothelial growth factor A	Homo sapiens	110-114
25633564-4	2015	Dorsomorphin, heparin, and cobalt chloride, known inhibitors of hepcidin expression, significantly suppressed green fluorescence intensity, and these inhibitory effects were more prominent when the cells were stimulated with BMP-6.	Heparin	14-21	bone morphogenetic protein 6	Homo sapiens	225-230
26056441-5	2015	METHODS: Four groups of self-assembled chitosan oligosaccharide/heparin (CSO/H) nanoparticles were prepared with various volume ratios of chitosan oligosaccharide to heparin (5:2, 5:4, 4:15, 1:5) and characterized by laser diffraction, particle size analysis, and transmission electron microscopy.	Heparin	64-71	twist family bHLH transcription factor 1	Homo sapiens	73-76
25950566-6	2015	While the binding to this detergent is higher for the mutant as compared to wt apoA-I, the interaction of the Arg173Pro variant with heparin depends on pH, being lower at pH 5.0 and higher than wt under physiological pH conditions.	Heparin	133-140	apolipoprotein A1	Homo sapiens	79-85
25950566-7	2015	We suggest that binding to ligands as heparin or other glycosaminoglycans could be key events tuning the fine details of the interaction of apoA-I variants with the micro-environment, and probably eliciting the toxicity of these variants in hereditary amyloidoses.	Heparin	38-45	apolipoprotein A1	Homo sapiens	140-146
25938026-3	2015	Clinical trials attempting to improve outcomes in patients with severe sepsis by inhibiting thrombin generation with heparin and or endogenous anticoagulants are reviewed.	Heparin	117-124	coagulation factor II, thrombin	Homo sapiens	92-100
25818573-0	2015	Heparin reduces overcirculation-induced pulmonary artery remodeling through p38 MAPK in piglet.	Heparin	0-7	mitogen-activated protein kinase 14	Homo sapiens	76-79
25818573-13	2015	Both heparin and P38 MAPK inhibitor suppressed VSMC growth and P38 MAPK expression in the cultured VSMC, but they did not present additive effects when the two treatments were combined.	Heparin	5-12	mitogen-activated protein kinase 14	Homo sapiens	63-66
25818573-14	2015	CONCLUSIONS: Heparin reduces overcirculation-induced pulmonary artery remodeling through a P38 MAPK-dependent pathway.	Heparin	13-20	mitogen-activated protein kinase 14	Homo sapiens	91-94
25813285-0	2015	Heparin modulates chemokines in human endometrial stromal cells by interaction with tumor necrosis factor alpha and thrombin.	Heparin	0-7	tumor necrosis factor	Homo sapiens	84-111
25813285-0	2015	Heparin modulates chemokines in human endometrial stromal cells by interaction with tumor necrosis factor alpha and thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	116-124
25813285-9	2015	Unfractionated heparin and LMWHs attenuated the TNF-alpha-mediated induction of CXCL8 and enhanced CXCL5, CCL2, and CCL5.	Heparin	15-22	tumor necrosis factor	Homo sapiens	48-57
25813285-9	2015	Unfractionated heparin and LMWHs attenuated the TNF-alpha-mediated induction of CXCL8 and enhanced CXCL5, CCL2, and CCL5.	Heparin	15-22	C-X-C motif chemokine ligand 8	Homo sapiens	80-85
25813285-10	2015	The stimulating effect of thrombin on CXCL8 could be inhibited by heparin, whereas heparin had no impact on thrombin-induced CXCL1 and CCL2.	Heparin	66-73	C-X-C motif chemokine ligand 8	Homo sapiens	38-43
25813285-13	2015	CONCLUSION(S): Heparins have modulating effects on TNF-alpha- and thrombin-induced endometrial chemokines, which might have implications in the regulation of endometrial receptivity and early implantation.	Heparin	15-23	tumor necrosis factor	Homo sapiens	51-60
25813285-13	2015	CONCLUSION(S): Heparins have modulating effects on TNF-alpha- and thrombin-induced endometrial chemokines, which might have implications in the regulation of endometrial receptivity and early implantation.	Heparin	15-23	coagulation factor II, thrombin	Homo sapiens	66-74
25582887-4	2015	In this study, we show that EC-SOD exposed to physiologically relevant concentrations of HOCl remains enzymatically active and retains the heparin-binding capacity, although HOCl exposure established oxidative modification of the N-terminal region (Met32) and the formation of an intermolecular cross-link in a fraction of the molecules.	Heparin	139-146	superoxide dismutase 3	Homo sapiens	28-34
25541466-3	2015	Heparins, a heterogeneous mixture of glycosaminoglycans, can inhibit metastatic cascades by blocking P-selectin-mediated intercellular adhesion between tumor cells and PTs.	Heparin	0-8	selectin, platelet	Mus musculus	101-111
25680756-3	2015	When platelet aggregation tests (PATs) were performed with platelet-rich plasma (PRP), a shorter lag time was measured in 131RR donors compared to individuals with the HR and HH genotypes in response to HIT plasma or 5B9, a recently developed humanized monoclonal antibody to PF4/heparin.	Heparin	280-287	complement component 4 binding protein alpha	Homo sapiens	81-84
25682155-3	2015	Using a versatile population of Sca-1(+)/CD45(-) cardiac progenitor cells (CPCs), we demonstrated that the addition of heparin in the HyA hydrogels was necessary to coordinate the presentation of TGFbeta1 and to support the trophic functions of the CPCs via endothelial cell differentiation and vascular like tubular network formation.	Heparin	119-126	ataxin 1	Homo sapiens	32-37
25682155-3	2015	Using a versatile population of Sca-1(+)/CD45(-) cardiac progenitor cells (CPCs), we demonstrated that the addition of heparin in the HyA hydrogels was necessary to coordinate the presentation of TGFbeta1 and to support the trophic functions of the CPCs via endothelial cell differentiation and vascular like tubular network formation.	Heparin	119-126	transforming growth factor beta 1	Homo sapiens	196-204
25682155-4	2015	Presentation of exogenous TGFbeta1 by binding with heparin improved differentiated CPC function by sequestering additional endogenously-produced angiogenic factors.	Heparin	51-58	transforming growth factor beta 1	Homo sapiens	26-34
26131136-3	2015	They were intervened by heparin and the expression levels of soluble thrombomodulin (sTM) and serum activated protein C (APC) were detected by ELISA, the regulatory mechanism of heparin improving vascular endothelial cells injury induced by TNFalpha was detected by Western Blotting method, the methylation of histone in the gene promoter region of endothelial nitric oxide synthase (eNOS) and monocyte chemotactic protein-1 (MCP-1) were detected using chromatin immunoprecipitation method.	Heparin	178-185	tumor necrosis factor	Homo sapiens	241-249
26131136-3	2015	They were intervened by heparin and the expression levels of soluble thrombomodulin (sTM) and serum activated protein C (APC) were detected by ELISA, the regulatory mechanism of heparin improving vascular endothelial cells injury induced by TNFalpha was detected by Western Blotting method, the methylation of histone in the gene promoter region of endothelial nitric oxide synthase (eNOS) and monocyte chemotactic protein-1 (MCP-1) were detected using chromatin immunoprecipitation method.	Heparin	178-185	nitric oxide synthase 3	Homo sapiens	349-382
26131136-5	2015	Conclusions Heparin could protect vascular endothelial cells from injury induced by TNFalpha and sepsis, the mechanisms were related with the effects of heparin on the histone methylation of promoter region and the regulation of heparin on the MAPK and NF-kappaB signal pathways.	Heparin	12-19	tumor necrosis factor	Homo sapiens	84-92
26131136-5	2015	Conclusions Heparin could protect vascular endothelial cells from injury induced by TNFalpha and sepsis, the mechanisms were related with the effects of heparin on the histone methylation of promoter region and the regulation of heparin on the MAPK and NF-kappaB signal pathways.	Heparin	153-160	tumor necrosis factor	Homo sapiens	84-92
26131136-5	2015	Conclusions Heparin could protect vascular endothelial cells from injury induced by TNFalpha and sepsis, the mechanisms were related with the effects of heparin on the histone methylation of promoter region and the regulation of heparin on the MAPK and NF-kappaB signal pathways.	Heparin	229-236	tumor necrosis factor	Homo sapiens	84-92
25867530-8	2015	MPO contributed only in heparin-treated patients, suggesting a more significant role for endothelial-bound MPO than for circulating MPO or elastase with respect to blood pressure regulation.	Heparin	24-31	myeloperoxidase	Homo sapiens	0-3
25787740-0	2015	The incorporation of bFGF mediated by heparin into PCL/gelatin composite fiber meshes for guided bone regeneration.	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	21-25
25787740-5	2015	Release of bFGF from electrospun nanofibers without heparin resulted in a spontaneous burst, while the heparin-mediated release of bFGF decreased the burst release in 24 h. The bFGF released from the nanofibers enhanced the proliferation and migration of human mesenchymal stem cells as well as the tubule formation of human umbilical cord blood cells.	Heparin	103-110	fibroblast growth factor 2	Homo sapiens	131-135
25787740-5	2015	Release of bFGF from electrospun nanofibers without heparin resulted in a spontaneous burst, while the heparin-mediated release of bFGF decreased the burst release in 24 h. The bFGF released from the nanofibers enhanced the proliferation and migration of human mesenchymal stem cells as well as the tubule formation of human umbilical cord blood cells.	Heparin	103-110	fibroblast growth factor 2	Homo sapiens	131-135
25604035-7	2015	RESULTS: PF4:heparin complexes caused release of the biomarker interleukin 8 in whole blood, and the level of response varied with the stoichiometric ratio of PF4 to heparin.	Heparin	13-20	C-X-C motif chemokine ligand 8	Homo sapiens	63-76
25604035-7	2015	RESULTS: PF4:heparin complexes caused release of the biomarker interleukin 8 in whole blood, and the level of response varied with the stoichiometric ratio of PF4 to heparin.	Heparin	166-173	C-X-C motif chemokine ligand 8	Homo sapiens	63-76
25498198-4	2015	The heparin nanoparticles were demonstrated to bind with Abeta through a variety of techniques including enzyme-linked immunosorbent assay, gel electrophoresis, and thioflavin T assay.	Heparin	4-11	amyloid beta precursor protein	Homo sapiens	57-62
25811371-9	2015	AT purified from patient"s plasma on hi-trap heparin column showed a marked decrease in heparin affinity and thrombin inhibition rates.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	109-117
25528069-11	2015	Prophylactic use of heparin might be considered in patients with ISTH DIC score&lt;5, bcr3 isoform, FLT3-ITD mutation and PAI 4G/4G.	Heparin	20-27	BCR pseudogene 3	Homo sapiens	86-90
25528069-11	2015	Prophylactic use of heparin might be considered in patients with ISTH DIC score&lt;5, bcr3 isoform, FLT3-ITD mutation and PAI 4G/4G.	Heparin	20-27	fms related receptor tyrosine kinase 3	Homo sapiens	100-104
25498198-6	2015	These results suggest that heparin nanoparticles can be a very useful tool for Abeta studies.	Heparin	27-34	amyloid beta precursor protein	Homo sapiens	79-84
25562836-6	2015	Heparin blocked the binding of HMGB1 to the surface of macrophages, and suppressed the phosphorylation of p38 and ERK1/2, but not JNK; TNF-alpha secretion was also decreased.	Heparin	0-7	tumor necrosis factor	Mus musculus	135-144
25595736-3	2015	Here, we showed that induction of PF4/heparin-specific antibodies by PF4/heparin complexes was markedly impaired in mice depleted of CD4 T cells by anti-CD4 antibodies.	Heparin	38-45	platelet factor 4	Mus musculus	34-37
25595736-3	2015	Here, we showed that induction of PF4/heparin-specific antibodies by PF4/heparin complexes was markedly impaired in mice depleted of CD4 T cells by anti-CD4 antibodies.	Heparin	38-45	platelet factor 4	Mus musculus	69-72
25595736-4	2015	Furthermore, Rag1-deficient recipient mice produced PF4/heparin-specific antibodies upon PF4/heparin challenge when reconstituted with a mixture of wild-type splenic B cells and splenocytes from B-cell-deficient (muMT) mice but not splenocytes from T- and B-cell-deficient (Rag1 knockout) mice.	Heparin	56-63	platelet factor 4	Mus musculus	89-92
25595736-4	2015	Furthermore, Rag1-deficient recipient mice produced PF4/heparin-specific antibodies upon PF4/heparin challenge when reconstituted with a mixture of wild-type splenic B cells and splenocytes from B-cell-deficient (muMT) mice but not splenocytes from T- and B-cell-deficient (Rag1 knockout) mice.	Heparin	93-100	platelet factor 4	Mus musculus	52-55
25595736-5	2015	Lastly, mice with B cells lacking CD40, a B-cell costimulatory molecule that helps T-cell-dependent B-cell responses, displayed a marked reduction of PF4/heparin-specific antibody production following PF4/heparin challenge.	Heparin	154-161	platelet factor 4	Mus musculus	150-153
25147059-4	2015	As an anticoagulant, heparin enhances inhibition of thrombin by the serpin antithrombin III.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	52-60
25621929-6	2015	The resulting alkaline phosphatase activity data demonstrated that native heparin maintained a significant amount of BMP-2 bioactivity and the effect appeared to be heparin concentration dependent.	Heparin	74-81	bone morphogenetic protein 2	Mus musculus	117-122
25723475-0	2015	Low molecular weight heparin (LMWH) improves peritoneal function and inhibits peritoneal fibrosis possibly through suppression of HIF-1alpha, VEGF and TGF-beta1.	Heparin	21-28	transforming growth factor, beta 1	Rattus norvegicus	151-160
25621929-0	2015	Effect of selective heparin desulfation on preservation of bone morphogenetic protein-2 bioactivity after thermal stress.	Heparin	20-27	bone morphogenetic protein 2	Mus musculus	59-87
25621929-2	2015	Heparin can interact electrostatically with BMP-2 and thus has been explored for controlled release and potential stabilization of this growth factor in vivo.	Heparin	0-7	bone morphogenetic protein 2	Mus musculus	44-49
25454806-0	2015	Unfractionated heparin attenuates LPS-induced IL-8 secretion via PI3K/Akt/NF-kappaB signaling pathway in human endothelial cells.	Heparin	15-22	C-X-C motif chemokine ligand 8	Homo sapiens	46-50
25454806-0	2015	Unfractionated heparin attenuates LPS-induced IL-8 secretion via PI3K/Akt/NF-kappaB signaling pathway in human endothelial cells.	Heparin	15-22	AKT serine/threonine kinase 1	Homo sapiens	70-73
25454806-0	2015	Unfractionated heparin attenuates LPS-induced IL-8 secretion via PI3K/Akt/NF-kappaB signaling pathway in human endothelial cells.	Heparin	15-22	nuclear factor kappa B subunit 1	Homo sapiens	74-83
25454806-2	2015	While UFH has been shown to suppress lipopolysaccharide (LPS)-induced nuclear factor-kappaB (NF-kappaB) activation, intracellular upstream events that cause NF-kappaB down-regulation in response to UFH remain unclear.	Heparin	6-9	nuclear factor kappa B subunit 1	Homo sapiens	93-102
25454806-2	2015	While UFH has been shown to suppress lipopolysaccharide (LPS)-induced nuclear factor-kappaB (NF-kappaB) activation, intracellular upstream events that cause NF-kappaB down-regulation in response to UFH remain unclear.	Heparin	198-201	nuclear factor kappa B subunit 1	Homo sapiens	157-166
25454806-4	2015	Pretreatment with UFH (0.1-1U/ml) significantly inhibited LPS (10mug/ml)-stimulated interleukin (IL)-6 and IL-8 production in HPMECs.	Heparin	18-21	interleukin 6	Homo sapiens	84-102
25454806-4	2015	Pretreatment with UFH (0.1-1U/ml) significantly inhibited LPS (10mug/ml)-stimulated interleukin (IL)-6 and IL-8 production in HPMECs.	Heparin	18-21	C-X-C motif chemokine ligand 8	Homo sapiens	107-111
24860124-7	2015	RESULTS: After heparin neutralization, there were significantly elevated levels of fibrinogen in the FFP group, which were manifested by r-TEG parameters MAf and FLEV.	Heparin	15-22	fibrinogen beta chain	Homo sapiens	83-93
25621929-5	2015	The goal of this study was to characterize three selectively desulfated heparin species (N-desulfated (Hep(-N)), 6-O,N-desulfated (Hep(-N,-6O)), and completely desulfated heparin (Hep(-))) and determine if the sulfation level of heparin affected the level of BMP-2 bioactivity after heat treatment at 65  C. BMP-2 bioactivity was evaluated using the established C2C12 cell assay.	Heparin	72-79	bone morphogenetic protein 2	Mus musculus	259-264
25621929-5	2015	The goal of this study was to characterize three selectively desulfated heparin species (N-desulfated (Hep(-N)), 6-O,N-desulfated (Hep(-N,-6O)), and completely desulfated heparin (Hep(-))) and determine if the sulfation level of heparin affected the level of BMP-2 bioactivity after heat treatment at 65  C. BMP-2 bioactivity was evaluated using the established C2C12 cell assay.	Heparin	72-79	bone morphogenetic protein 2	Mus musculus	308-313
25621929-8	2015	These findings can be used to better select desulfated heparin species that exhibit low anticoagulant activity while extending the half-life of BMP-2 in solution and in delivery systems.	Heparin	55-62	bone morphogenetic protein 2	Mus musculus	144-149
25472936-10	2015	CONCLUSION: At 24-month, this trial in PAD patients with long femoropopliteal lesions demonstrated a significantly improved primary patency rate for heparin-bonded covered stents compared to BMS, however, without a significant impact on clinical outcomes and TLR rate (Reg.	Heparin	149-156	regenerating family member 1 alpha	Homo sapiens	269-272
25555501-0	2015	Low molecular weight heparin therapy during pregnancy is associated with elevated circulatory levels of placental growth factor.	Heparin	21-28	placental growth factor	Homo sapiens	104-127
25314695-1	2015	Bivalirudin is a direct thrombin inhibitor used in the cardiac intensive care unit when heparin is contraindicated due to heparin-induced thrombocytopenia.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	24-32
25314695-1	2015	Bivalirudin is a direct thrombin inhibitor used in the cardiac intensive care unit when heparin is contraindicated due to heparin-induced thrombocytopenia.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	24-32
24692161-10	2015	Heparin-treated rats had increased thrombin clotting times, factor Xa inhibition and activated partial thromboplastin times, indicating systemic absorption of heparin.	Heparin	0-7	coagulation factor II	Rattus norvegicus	35-43
26214191-0	2015	Heparin-induced conformational changes of fibronectin within the extracellular matrix promote hMSC osteogenic differentiation.	Heparin	0-7	fibronectin 1	Homo sapiens	42-53
25594496-2	2015	The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	130-138
25642384-3	2015	In this study, we have synthesized hPRM1 and determined how its CEST MRI contrast varies as a function of pH, phosphorylation state, and upon noncovalent interaction with nucleic acids and heparin (as antagonist).	Heparin	189-196	protamine 1	Homo sapiens	35-40
25453957-0	2015	LHT7, a chemically modified heparin, inhibits multiple stages of angiogenesis by blocking VEGF, FGF2 and PDGF-B signaling pathways.	Heparin	28-35	vascular endothelial growth factor A	Homo sapiens	90-94
25453957-0	2015	LHT7, a chemically modified heparin, inhibits multiple stages of angiogenesis by blocking VEGF, FGF2 and PDGF-B signaling pathways.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	96-100
25453957-5	2015	In previous study, we reported a heparin-derived angiogenesis inhibitor, LHT7, as a potent angiogenesis inhibitor and showed that it blocked VEGF signaling pathway.	Heparin	33-40	vascular endothelial growth factor A	Homo sapiens	141-145
26214191-3	2015	By probing the conformation of fibronectin (Fn) using fluorescence resonance energy transfer (FRET), we show here that heparin treatment of the fibroblast-derived ECM scaffolds resulted in more extended conformations of fibrillar Fn in ECM.	Heparin	119-126	fibronectin 1	Homo sapiens	31-42
26214191-4	2015	Since heparin is a highly negatively charged molecule while fibronectin contains segments of positively charged modules, including FnIII13, electrostatic interactions between Fn and heparin might interfere with residual quaternary structure in relaxed fibronectin fibers thereby opening up buried sites.	Heparin	6-13	fibronectin 1	Homo sapiens	252-263
26214191-4	2015	Since heparin is a highly negatively charged molecule while fibronectin contains segments of positively charged modules, including FnIII13, electrostatic interactions between Fn and heparin might interfere with residual quaternary structure in relaxed fibronectin fibers thereby opening up buried sites.	Heparin	182-189	fibronectin 1	Homo sapiens	60-71
26214191-4	2015	Since heparin is a highly negatively charged molecule while fibronectin contains segments of positively charged modules, including FnIII13, electrostatic interactions between Fn and heparin might interfere with residual quaternary structure in relaxed fibronectin fibers thereby opening up buried sites.	Heparin	182-189	fibronectin 1	Homo sapiens	252-263
26214191-8	2015	We hypothesize that fibronectin"s conformations within the ECM are activated by heparin such as to coordinate with other factors to upregulate hMSC osteogenic differentiation.	Heparin	80-87	fibronectin 1	Homo sapiens	20-31
25218699-4	2015	Patients and methods CBS activity was measured in EDTA or heparin plasma using either a previously described or a newly developed LC-MS/MS method optimized for analysis of the reaction product, 3,3-(2)H2-cystathionine, as its butyl ester derivative.	Heparin	58-65	cystathionine beta-synthase	Homo sapiens	21-24
25883978-4	2015	The gelatin fibers were further functionalized by heparin immobilization, which provides binding sites for VEGF and thus enables the sustained release of VEGF.	Heparin	50-57	vascular endothelial growth factor A	Homo sapiens	107-111
25883978-4	2015	The gelatin fibers were further functionalized by heparin immobilization, which provides binding sites for VEGF and thus enables the sustained release of VEGF.	Heparin	50-57	vascular endothelial growth factor A	Homo sapiens	154-158
26495958-6	2015	In H292 cells, fully-sulfated HMW heparin significantly reduced LPS-induced gene expression of both COX-2 and CXCL-8 for up to 48 hours, while desulfated heparin had little to no significant suppressive effect on signaling or on COX-2 gene or protein expression.	Heparin	34-41	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	100-105
25332209-4	2015	By analyzing heparin-binding HPLC fractions of psoriatic scales, we found that human beta-defensin (hBD)2, hBD3, and lysozyme are additional triggers of pDC activation in psoriatic skin lesions.	Heparin	13-20	defensin beta 4A	Homo sapiens	100-105
26495958-8	2015	In contrast, in normal HBE-1 cells, fully sulfated heparin significantly suppressed only ERK signaling, COX-2 gene expression at 12 hours, and CXCL-8 gene expression at 6 and 12 hours, while desulfated heparin had no significant effects on LPS-stimulated signaling or on gene or protein expression.	Heparin	51-58	mitogen-activated protein kinase 3	Homo sapiens	89-92
26495958-6	2015	In H292 cells, fully-sulfated HMW heparin significantly reduced LPS-induced gene expression of both COX-2 and CXCL-8 for up to 48 hours, while desulfated heparin had little to no significant suppressive effect on signaling or on COX-2 gene or protein expression.	Heparin	34-41	C-X-C motif chemokine ligand 8	Homo sapiens	110-116
26495958-8	2015	In contrast, in normal HBE-1 cells, fully sulfated heparin significantly suppressed only ERK signaling, COX-2 gene expression at 12 hours, and CXCL-8 gene expression at 6 and 12 hours, while desulfated heparin had no significant effects on LPS-stimulated signaling or on gene or protein expression.	Heparin	51-58	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	104-109
26495958-8	2015	In contrast, in normal HBE-1 cells, fully sulfated heparin significantly suppressed only ERK signaling, COX-2 gene expression at 12 hours, and CXCL-8 gene expression at 6 and 12 hours, while desulfated heparin had no significant effects on LPS-stimulated signaling or on gene or protein expression.	Heparin	51-58	C-X-C motif chemokine ligand 8	Homo sapiens	143-149
26495958-6	2015	In H292 cells, fully-sulfated HMW heparin significantly reduced LPS-induced gene expression of both COX-2 and CXCL-8 for up to 48 hours, while desulfated heparin had little to no significant suppressive effect on signaling or on COX-2 gene or protein expression.	Heparin	34-41	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	229-234
26495958-7	2015	Desulfated heparin, initially ineffective at preventing LPS-induced CXCL8 up-regulation, reduced CXCL8 transcription at 24 hours.	Heparin	11-18	C-X-C motif chemokine ligand 8	Homo sapiens	97-102
25669059-0	2014	[Assessment of in vitro impact of low molecular weight heparin on expression of heparanase and heparin binding growth factors in the endometrium of women with impaired reproduction].	Heparin	55-62	heparanase	Homo sapiens	80-90
26065539-0	2015	Preparation and preliminary in vitro evaluation of a bFGF-releasing heparin-conjugated poly(epsilon-caprolactone) membrane for guided bone regeneration.	Heparin	68-75	fibroblast growth factor 2	Homo sapiens	53-57
26065539-1	2015	In an effort to improve guided bone regeneration (GBR), we successfully fabricated a novel basic fibroblast growth factor (bFGF)-releasing heparin-conjugated poly(epsilon-caprolactone) membrane (hep-PCL/bFGF).	Heparin	139-146	fibroblast growth factor 2	Homo sapiens	123-127
26065539-1	2015	In an effort to improve guided bone regeneration (GBR), we successfully fabricated a novel basic fibroblast growth factor (bFGF)-releasing heparin-conjugated poly(epsilon-caprolactone) membrane (hep-PCL/bFGF).	Heparin	139-146	fibroblast growth factor 2	Homo sapiens	203-207
25863018-1	2015	With the aim to determine the binding affinity of a new generation of recombinant antithrombin (AT) toward heparin, we developed a dynamic equilibrium-affinity capillary electrophoresis (DE-ACE) method.	Heparin	107-114	angiotensin I converting enzyme	Homo sapiens	190-193
25325941-4	2015	Heparins with other sulfation patterns are able to bind to a variety of other proteins such as FGF, VEGF, and CXCL-3.	Heparin	0-8	vascular endothelial growth factor A	Homo sapiens	100-104
25325941-4	2015	Heparins with other sulfation patterns are able to bind to a variety of other proteins such as FGF, VEGF, and CXCL-3.	Heparin	0-8	C-X-C motif chemokine ligand 3	Homo sapiens	110-116
25673124-1	2014	In a previous issue of Critical Care, Schilder and colleagues report the results of their multicenter trial (Citrate Anticoagulation Versus Systemic Heparinization; CASH) comparing regional anticoagulation with citrate to heparin anticoagulation.	Heparin	222-229	CASP8 and FADD like apoptosis regulator	Homo sapiens	165-169
25503134-0	2014	Growth-modulatory effects of heparin and VEGF165 on the choriocarcinoma cell-line JEG-3 and its expression of heparanase.	Heparin	29-36	heparanase	Homo sapiens	110-120
25503134-3	2014	Vascular endothelial growth factor (VEGF) and heparin are known to alter HPSE expression, with heparin given prophylactically to women with a history of placenta-mediated complications in subsequent pregnancies.	Heparin	46-53	heparanase	Homo sapiens	73-77
25503134-4	2014	MATERIALS AND METHODS: We examined the growth-modulatory effects of different concentrations of heparin and VEGF on the choriocarcinoma cell-line JEG-3 and the expression of heparanase under VEGF and heparin by proliferation assays, PCR, and western blot.	Heparin	200-207	heparanase	Homo sapiens	174-184
25286301-2	2014	PCPE-1 consists of two CUB domains that bind to the procollagen C-propeptide and are responsible for enhancing activity and a netrin-like (NTR) domain that binds to BMP-1 as well as heparin and heparan sulfate.	Heparin	182-189	procollagen C-endopeptidase enhancer	Homo sapiens	0-6
25286301-3	2014	The NTR domain also mediates binding of PCPE-1 to cells, an interaction inhibited by heparin, thus suggesting involvement of cell membrane heparan-sulfate proteoglycans (HSPGs).	Heparin	85-92	procollagen C-endopeptidase enhancer	Homo sapiens	40-46
24911927-1	2014	Published data provide strong evidence that heparin treatment of proliferating vascular smooth muscle cells results in decreased signaling through the ERK pathway and decreases in cell proliferation.	Heparin	44-51	mitogen-activated protein kinase 1	Homo sapiens	151-154
24911927-5	2014	In addition, protein kinase G inhibitors decrease heparin effects on ERK activity, phosphorylation of the transcription factor Elk-1, and heparin-induced MKP-1 synthesis.	Heparin	50-57	mitogen-activated protein kinase 1	Homo sapiens	69-72
24911927-5	2014	In addition, protein kinase G inhibitors decrease heparin effects on ERK activity, phosphorylation of the transcription factor Elk-1, and heparin-induced MKP-1 synthesis.	Heparin	138-145	dual specificity phosphatase 1	Homo sapiens	154-159
25673124-7	2014	Nevertheless, the CASH trial is the third large randomized trial showing superiority of citrate over heparin, supporting the recommendation of citrate as first choice anticoagulant.	Heparin	101-108	CASP8 and FADD like apoptosis regulator	Homo sapiens	18-22
25669059-2	2014	Several studies have indicated that heparin, by blocking the enzymatic activity of heparanase, may affect the structure and function of the extracellular matrix (ECM) and related growth factors.	Heparin	36-43	heparanase	Homo sapiens	83-93
25669059-11	2014	CONCLUSIONS: Our results show that the importance of the HPSE hydrolytic activity in the endometrium, during the implantation window, may have a secondary function, and/or that beneficial effects of LMWH in women with impaired reproduction have no significant, direct connection with the, catalyzed by HPSE, reconstruction of the ECM and with release of heparin-binding growth factors.	Heparin	354-361	heparanase	Homo sapiens	57-61
25220364-5	2014	In this study, we explore the binding of DNA and heparin, two types of essential life polyanions, to A4V, an ALS-linked SOD1 mutant, under acidic conditions, and its consequences.	Heparin	49-56	superoxide dismutase 1	Homo sapiens	120-124
25364825-18	2014	CONCLUSIONS: From this balb/c mice study, the analyses of mRNA and cytokines revealed that both intranasal heparin and lmw heparin treatment decreased the expression of Th1, Th2, and Th17 in spleen.	Heparin	107-114	negative elongation factor complex member C/D, Th1l	Mus musculus	169-172
25204286-4	2014	On the other hand, a chemically synthesized conjugate of heparin and a murine anti-CEA mAb, T84.66 (termed T84.66-Hep) was found able to bind highly specifically to CEA over-expressing LS174T colorectal cancer cells.	Heparin	57-64	CEA cell adhesion molecule 3	Homo sapiens	83-86
25204286-4	2014	On the other hand, a chemically synthesized conjugate of heparin and a murine anti-CEA mAb, T84.66 (termed T84.66-Hep) was found able to bind highly specifically to CEA over-expressing LS174T colorectal cancer cells.	Heparin	57-64	CEA cell adhesion molecule 3	Homo sapiens	165-168
25234820-2	2014	In the present investigation, we found that heparin nanoparticles are selective Toll-like receptor 4 (TLR-4) antagonists and have a much greater anti-inflammatory effect than native heparin.	Heparin	44-51	toll-like receptor 4	Mus musculus	80-100
25234820-2	2014	In the present investigation, we found that heparin nanoparticles are selective Toll-like receptor 4 (TLR-4) antagonists and have a much greater anti-inflammatory effect than native heparin.	Heparin	44-51	toll-like receptor 4	Mus musculus	102-107
25242730-10	2014	These results suggest that selective inhibition of TLR4-NF-kappaB signaling with lipid modified heparin derivatives composited to nanostructures provides an effective therapeutic approach to inhibit chronic inflammation in an animal model of rheumatoid arthritis.	Heparin	96-103	toll-like receptor 4	Mus musculus	51-55
25230248-2	2014	The most common affinity-based systems use heparin-based scaffolds to sustain the release of heparin-binding proteins, such as fibroblast growth factor-2 (FGF2) and vascular endothelial growth factor (VEGF).	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	127-153
25230248-2	2014	The most common affinity-based systems use heparin-based scaffolds to sustain the release of heparin-binding proteins, such as fibroblast growth factor-2 (FGF2) and vascular endothelial growth factor (VEGF).	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	155-159
25230248-2	2014	The most common affinity-based systems use heparin-based scaffolds to sustain the release of heparin-binding proteins, such as fibroblast growth factor-2 (FGF2) and vascular endothelial growth factor (VEGF).	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	165-199
25230248-2	2014	The most common affinity-based systems use heparin-based scaffolds to sustain the release of heparin-binding proteins, such as fibroblast growth factor-2 (FGF2) and vascular endothelial growth factor (VEGF).	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	201-205
25364825-18	2014	CONCLUSIONS: From this balb/c mice study, the analyses of mRNA and cytokines revealed that both intranasal heparin and lmw heparin treatment decreased the expression of Th1, Th2, and Th17 in spleen.	Heparin	123-130	negative elongation factor complex member C/D, Th1l	Mus musculus	169-172
25225890-9	2014	Of those patients receiving BID SC UFH, 186 (11.7%) had aPTT values drawn on the basis of risk factors.	Heparin	35-38	BH3 interacting domain death agonist	Homo sapiens	28-31
24960155-7	2014	RESULTS: Compared with paired aliquots, significant differences were observed for ALT, AST, bilirubin, calcium, chloride, CK, glucose, LDH, potassium and urea nitrogen in lithium-heparin gel tubes, and for calcium, chloride, CK, LDH, potassium and urea nitrogen in serum gel tubes.	Heparin	179-186	solute carrier family 17 member 5	Homo sapiens	87-90
25115442-9	2014	The heparin-binding domain of GEP was mapped to RRH(555-557) in the C-terminal region.	Heparin	4-11	granulin precursor	Homo sapiens	30-33
24960155-8	2014	When percentage variations were compared with the desirable specifications, significant bias was found for AST (+7.8%), calcium (+1.2%), glucose (-3.3%) and LDH (+35%) in lithium-heparin gel tubes.	Heparin	179-186	solute carrier family 17 member 5	Homo sapiens	107-110
25289058-8	2014	Heparin administration decreased the levels of the liver enzymes, IR, superoxide generation, hepatic TG, hydroxyproline and iNOS expression when compared with the HF diet group.	Heparin	0-7	nitric oxide synthase 2, inducible	Mus musculus	124-128
25731059-3	2014	She suffered multiple right brain infarctions, a pulmonary embolism, a right renal infarction with bilateral hydronephrosis and deep venous thromboses and exhibited increased D-dimer and fibrinogen levels and so was administered heparin (10,000 U x day(-1)).	Heparin	229-236	fibrinogen beta chain	Homo sapiens	187-197
25116951-6	2014	Citrullination of fibronectin was in one study suggested to affect cell adhesion by modifying the heparin-binding site and not the RGD site.	Heparin	98-105	fibronectin 1	Homo sapiens	18-29
24832962-6	2014	It is postulated that heparin binding to the CD11b receptor facilitates the internalisation of the QDs into the nucleus of THP-1 cells.	Heparin	22-29	GLI family zinc finger 2	Homo sapiens	123-128
25242245-0	2014	Sulfated low molecular weight lignins, allosteric inhibitors of coagulation proteinases via the heparin binding site, significantly alter the active site of thrombin and factor xa compared to heparin.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	157-165
24961476-0	2014	Heparin inhibits melanosome uptake and inflammatory response coupled with phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways in human epidermal keratinocytes.	Heparin	0-7	AKT serine/threonine kinase 1	Homo sapiens	109-112
24961476-0	2014	Heparin inhibits melanosome uptake and inflammatory response coupled with phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways in human epidermal keratinocytes.	Heparin	0-7	mitogen-activated protein kinase kinase 7	Homo sapiens	117-120
24961476-0	2014	Heparin inhibits melanosome uptake and inflammatory response coupled with phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways in human epidermal keratinocytes.	Heparin	0-7	mitogen-activated protein kinase 1	Homo sapiens	121-124
24961476-3	2014	Heparin exhibited the inhibitory effect on keratinocyte phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways.	Heparin	0-7	AKT serine/threonine kinase 1	Homo sapiens	91-94
24961476-3	2014	Heparin exhibited the inhibitory effect on keratinocyte phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways.	Heparin	0-7	mitogen-activated protein kinase kinase 7	Homo sapiens	99-102
24961476-3	2014	Heparin exhibited the inhibitory effect on keratinocyte phagocytosis through blocking PI3k/Akt and MEK/ERK signaling pathways.	Heparin	0-7	mitogen-activated protein kinase 1	Homo sapiens	103-106
24961476-4	2014	In fact, the heparin-treated NHEKs showed impaired activation of Akt and ERK during phagocytosis, whereas PI3k and MEK inhibitors significantly suppressed melanosome uptake by NHEKs.	Heparin	13-20	AKT serine/threonine kinase 1	Homo sapiens	65-68
24961476-4	2014	In fact, the heparin-treated NHEKs showed impaired activation of Akt and ERK during phagocytosis, whereas PI3k and MEK inhibitors significantly suppressed melanosome uptake by NHEKs.	Heparin	13-20	mitogen-activated protein kinase 1	Homo sapiens	73-76
32481910-3	2014	The dose-dependence of thrombin clotting time (TCT) delay caused by TBA29-Au NPs/heparin/GO is 21.4, 17.0 and >100 times higher than that caused by the TBA29-Au NPs, TBA29-Au NPs/GO and commercially available drugs (heparin, argatroban, hirudin or warfarin), respectively.	Heparin	216-223	coagulation factor II, thrombin	Homo sapiens	23-31
25399896-18	2014	RT-PCR showed that the expression of iNOS mRNA in the heparin treatment group was significantly lower than that in the model group (2 (-Delta DeltaCt): 3.04 +- 0.18 vs. 4.37 +- 0.15, P &lt; 0.05).	Heparin	54-61	nitric oxide synthase 2	Rattus norvegicus	37-41
25399896-20	2014	Immunohistochemistry showed that positive expressions of iNOS in alveolar epithelial cell and capillary endothelial cell in the heparin treatment group were significantly lower than those in the model group.	Heparin	128-135	nitric oxide synthase 2	Rattus norvegicus	57-61
25399896-21	2014	CONCLUSIONS: Heparin significantly ameliorated the lung injury induced by LPS in rats via the inhibition of nitric oxide synthase expression and the TGF-beta/Smad pathway.	Heparin	13-20	transforming growth factor, beta 1	Rattus norvegicus	149-157
32481910-3	2014	The dose-dependence of thrombin clotting time (TCT) delay caused by TBA29-Au NPs/heparin/GO is 21.4, 17.0 and >100 times higher than that caused by the TBA29-Au NPs, TBA29-Au NPs/GO and commercially available drugs (heparin, argatroban, hirudin or warfarin), respectively.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	23-31
25172430-1	2014	FgfrL1, which interacts with Fgf ligands and heparin, is a member of the fibroblast growth factor receptor (Fgfr) family.	Heparin	45-52	fibroblast growth factor receptor-like 1	Mus musculus	0-6
32481910-2	2014	To further improve anticoagulation efficiency in human plasma, TBA29-Au NPs/heparin/GO has been prepared from TBA29-Au NPs/GO and heparin that can also bind thrombin.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	157-165
32481910-2	2014	To further improve anticoagulation efficiency in human plasma, TBA29-Au NPs/heparin/GO has been prepared from TBA29-Au NPs/GO and heparin that can also bind thrombin.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	157-165
25299071-3	2014	Analyzing the NMR HSQC spectra for different FGF2 concentrations, heparin-affinity purified FGF2 showed perturbations that indicate dimerization and are a higher-order oligomerization state.	Heparin	66-73	fibroblast growth factor 2	Homo sapiens	45-49
25299071-3	2014	Analyzing the NMR HSQC spectra for different FGF2 concentrations, heparin-affinity purified FGF2 showed perturbations that indicate dimerization and are a higher-order oligomerization state.	Heparin	66-73	fibroblast growth factor 2	Homo sapiens	92-96
25299071-4	2014	HSQC perturbation observed with different FGF2 concentrations revealed a heparin-binding site and two dimer interfaces.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	42-46
25299071-6	2014	On the contrary, FGF2 purified with ion-exchange chromatography did not show similar perturbation indicating that self-association of FGF2 is eliminated if purification is done without heparin-affinity chromatography.	Heparin	185-192	fibroblast growth factor 2	Homo sapiens	134-138
25299071-7	2014	The HSQC spectra of heparin-affinity purified FGF2 can be reproduced to some extent by adding heparin tetra-saccharide to ion exchange chromatography purified FGF2.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	46-50
25299071-7	2014	The HSQC spectra of heparin-affinity purified FGF2 can be reproduced to some extent by adding heparin tetra-saccharide to ion exchange chromatography purified FGF2.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	159-163
25299071-8	2014	Heparin-affinity purified FGF2 bound to acceptor and donor beads in a tagged form using His-tagged or GST-tagged proteins, also dimerized in the AlphaScreen  assay.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	26-30
25117899-0	2014	NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding.	Heparin	100-107	fibroblast growth factor 2	Homo sapiens	88-92
25117899-4	2014	We used the H2CN NMR pulse sequence to detect heparin binding through the side-chain resonances Hepsilon-Cepsilon-Nzeta of Lys and Hdelta-Cdelta-Nepsilon of Arg in the two proteins of hepatoma-derived growth factor (HDGF) and basic fibroblast growth factor (FGF2).	Heparin	46-53	fibroblast growth factor 2	Homo sapiens	258-262
24837008-2	2014	We studied if low-molecular-weight heparin enoxaparin administered for hemodialysis (HD) anticoagulation causes systemic MPO activation.	Heparin	35-42	myeloperoxidase	Homo sapiens	121-124
25085920-2	2014	A nonsynonomous single-nucleotide polymorphism in EC-SOD (rs1799895) leads to an arginine to glycine amino acid substitution at position 213 (R213G) in the heparin-binding domain.	Heparin	156-163	superoxide dismutase 3	Homo sapiens	50-56
24837008-7	2014	The increase in plasma MPO during systemic heparin-free HD was significantly less pronounced.	Heparin	43-50	myeloperoxidase	Homo sapiens	23-26
24178515-0	2014	Heparin modification of a biomimetic bone matrix for controlled release of VEGF.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	75-79
24178515-5	2014	Investigations of binding and release of the vascular endothelial growth factor (VEGF-A165) loaded onto the scaffolds revealed an enhanced binding capacity as well as a sustained and nearly constant delivery of VEGF as result of both heparin modification methods.	Heparin	234-241	vascular endothelial growth factor A	Homo sapiens	45-79
24178515-5	2014	Investigations of binding and release of the vascular endothelial growth factor (VEGF-A165) loaded onto the scaffolds revealed an enhanced binding capacity as well as a sustained and nearly constant delivery of VEGF as result of both heparin modification methods.	Heparin	234-241	vascular endothelial growth factor A	Homo sapiens	81-85
25043635-3	2014	First, acidic fibroblast growth factor (FGF-1) was incubated under conditions known to promote (40 C) and inhibit (heparin addition) molten globule formation.	Heparin	115-122	fibroblast growth factor 1	Homo sapiens	40-45
24865175-4	2014	In lithium-heparin tubes, statistically significant differences were observed in S-BIM values of all parameters, except urea nitrogen, CRP, and sodium, compared with S-NO-BIM.	Heparin	11-18	C-reactive protein	Homo sapiens	135-138
25043635-4	2014	Heat exposed (40 C) FGF-1 exhibited binding to GroEL-biosensors, which was significantly diminished in the presence of heparin.	Heparin	119-126	fibroblast growth factor 1	Homo sapiens	20-25
32262189-9	2014	However, after dip coating with VEGF, the heparin coated scaffold supported both attachment and colony growth of HDMEC; no such colony formation occurred in the absence of VEGF.	Heparin	42-49	vascular endothelial growth factor A	Homo sapiens	32-36
25123642-11	2014	Isothermal titration calorimetry data show that IL-12 exhibits a moderate binding affinity (Kd(app)=69+-1 muM) to heparin.	Heparin	114-121	latexin	Homo sapiens	106-109
24976018-7	2014	Heparin-induced MPO-release from patient-derived RBCs was significantly increased compared to controls.	Heparin	0-7	myeloperoxidase	Homo sapiens	16-19
25171706-1	2014	CONTEXT: Parenteral direct thrombin inhibitors (DTIs) may be used in pediatric patients with contraindications to heparin therapy, such as heparin-induced thrombocytopenia.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	27-35
25171706-1	2014	CONTEXT: Parenteral direct thrombin inhibitors (DTIs) may be used in pediatric patients with contraindications to heparin therapy, such as heparin-induced thrombocytopenia.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	27-35
25153385-5	2014	CrataBL prolongs the activated partial thromboplastin time on human and mouse plasma, and it impairs the heparin-induced potentiation of antithrombin III and heparin-induced platelet activation in the presence of low-dose ADP.	Heparin	105-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	137-153
25153385-6	2014	It is likely that the dense track of positive charge on CrataBL surface competes with the heparin ability to bind to antithrombin III and to stimulate platelets.	Heparin	90-97	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	117-133
25081127-6	2014	Furthermore, anticoagulant therapy before, during and after PCI can be performed by the use of unfractionated heparin, low molecular weight heparins, such as enoxaparin, the synthetic pentasaccharide fondaparinux and the direct thrombin inhibitor bivalirudin with or without additional administration of glycoprotein IIb/IIIa inhibitors.	Heparin	140-148	coagulation factor II, thrombin	Homo sapiens	228-236
24435659-5	2014	Surface plasmon resonance demonstrated specific interaction of heparin with Proteinase K having Kd in muM range.	Heparin	63-70	latexin	Homo sapiens	102-105
25126760-4	2014	Similar to the classical Fgfrs, the FgfrL1 protein contains an extracellular part composed of three Ig-like domains that interact with Fgf ligands and heparin.	Heparin	151-158	fibroblast growth factor receptor-like 1	Mus musculus	36-42
32261746-7	2014	Moreover, the linear light-up response of AIE probe/GO enables heparin quantification in the range of 0-13.2 muM with a detection limit of 10 nM, which is of practical importance for heparin monitoring during surgery or therapy.	Heparin	63-70	latexin	Homo sapiens	109-112
24469066-3	2014	We studied the effects of heparin and low anticoagulant 2-O, 3-O desulfated heparin (ODSH) on thrombin-induced increases in paracellular permeability of cultured human pulmonary endothelial cells (ECs).	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	94-102
24469066-4	2014	Pretreatment with heparin or ODSH blocked thrombin-induced decrease in the EC transendothelial electrical resistance (TER), attenuated thrombin-stimulated paracellular gap formation and actin cytoskeletal rearrangement.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	42-50
24469066-4	2014	Pretreatment with heparin or ODSH blocked thrombin-induced decrease in the EC transendothelial electrical resistance (TER), attenuated thrombin-stimulated paracellular gap formation and actin cytoskeletal rearrangement.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	135-143
24469066-5	2014	Our data demonstrated that heparin and ODSH had inhibitory effects on thrombin-induced RhoA activation and intracellular calcium elevation.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	70-78
24469066-5	2014	Our data demonstrated that heparin and ODSH had inhibitory effects on thrombin-induced RhoA activation and intracellular calcium elevation.	Heparin	27-34	ras homolog family member A	Homo sapiens	87-91
24469066-8	2014	Heparin or ODSH alone produced decreases in the EC TER that were abolished by siRNA-mediated depletion of the thrombin receptor, PAR-1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	110-118
24469066-8	2014	Heparin or ODSH alone produced decreases in the EC TER that were abolished by siRNA-mediated depletion of the thrombin receptor, PAR-1.	Heparin	0-7	coagulation factor II thrombin receptor	Homo sapiens	129-134
24583690-8	2014	Under optimal conditions (5 muM coralyne, 1 muM poly A20, and 10mM HEPES), this probe exhibited high selectivity (&gt;90-fold) toward heparin over hyaluronic acid and chondroitin sulfate.	Heparin	134-141	latexin	Homo sapiens	28-31
24583690-8	2014	Under optimal conditions (5 muM coralyne, 1 muM poly A20, and 10mM HEPES), this probe exhibited high selectivity (&gt;90-fold) toward heparin over hyaluronic acid and chondroitin sulfate.	Heparin	134-141	latexin	Homo sapiens	44-47
24816282-3	2014	We have covalently bound heparin to poly(ethylene glycol) (PEG) microspheres to create useful spatial patterns of glial-cell derived human neurotrophic factor (GDNF) in scaffolds to promote peripheral nerve regeneration.	Heparin	25-32	glial cell derived neurotrophic factor	Homo sapiens	114-158
24816282-3	2014	We have covalently bound heparin to poly(ethylene glycol) (PEG) microspheres to create useful spatial patterns of glial-cell derived human neurotrophic factor (GDNF) in scaffolds to promote peripheral nerve regeneration.	Heparin	25-32	glial cell derived neurotrophic factor	Homo sapiens	160-164
32261746-7	2014	Moreover, the linear light-up response of AIE probe/GO enables heparin quantification in the range of 0-13.2 muM with a detection limit of 10 nM, which is of practical importance for heparin monitoring during surgery or therapy.	Heparin	183-190	latexin	Homo sapiens	109-112
24628114-5	2014	KEY RESULTS: Functional analyses showed that heparin was a competitive antagonist of all IP3R subtypes with different affinities for each (IP3R3 &gt; IP3R1 &gt;= IP3R2).	Heparin	45-52	inositol 1,4,5-trisphosphate receptor type 1	Homo sapiens	89-93
24522239-5	2014	High molecular weight heparin bound to alpha1-PI/D-helix and accelerated the inhibition of thrombin by the serpin mutant by a template mechanism reminiscent of the cofactor effect of heparin on inhibition of thrombin by AT.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	91-99
24522239-5	2014	High molecular weight heparin bound to alpha1-PI/D-helix and accelerated the inhibition of thrombin by the serpin mutant by a template mechanism reminiscent of the cofactor effect of heparin on inhibition of thrombin by AT.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	208-216
24522239-5	2014	High molecular weight heparin bound to alpha1-PI/D-helix and accelerated the inhibition of thrombin by the serpin mutant by a template mechanism reminiscent of the cofactor effect of heparin on inhibition of thrombin by AT.	Heparin	183-190	coagulation factor II, thrombin	Homo sapiens	208-216
24790143-9	2014	Moreover, DNA-VWF interaction can be blocked using unfractionated and low-molecular-weight heparin, and DNA-VWF complexes attenuate platelet binding to VWF.	Heparin	91-98	von Willebrand factor	Homo sapiens	14-17
24628114-5	2014	KEY RESULTS: Functional analyses showed that heparin was a competitive antagonist of all IP3R subtypes with different affinities for each (IP3R3 &gt; IP3R1 &gt;= IP3R2).	Heparin	45-52	inositol 1,4,5-trisphosphate receptor type 1	Homo sapiens	150-155
24628114-5	2014	KEY RESULTS: Functional analyses showed that heparin was a competitive antagonist of all IP3R subtypes with different affinities for each (IP3R3 &gt; IP3R1 &gt;= IP3R2).	Heparin	45-52	inositol 1,4,5-trisphosphate receptor type 2	Homo sapiens	162-167
24628114-9	2014	CONCLUSIONS AND IMPLICATIONS: Heparin competes with IP3, but its access to the IP3-binding core is substantially hindered by additional IP3R residues.	Heparin	30-37	inositol 1,4,5-trisphosphate receptor type 1	Homo sapiens	136-140
24816371-0	2014	New insights in heparin-induced thrombocytopenia by the use of fluid-phase assays to detect specifically platelet factor 4/heparin complex antibodies and antibody-secreting cells.	Heparin	16-23	platelet factor 4	Mus musculus	105-122
25346984-4	2014	The application of low-molecular heparins (Klexan and Fraxiparine) prior to operation and during post-operative period decreases activation of pro-coagulant (prolongation of activated partial thromboplastin time, pro-prothrombin activity and concentration of fibrinogen) and platelet-derived components of system of hemostasis, level of markers of intravascular coagulation of blood, von Willebrand factor.	Heparin	33-41	fibrinogen beta chain	Homo sapiens	259-269
25346984-5	2014	The low-molecular heparins favor preservation of natural inhibitors of thrombin and support protective function of fibrinolytic system.	Heparin	18-26	coagulation factor II, thrombin	Homo sapiens	71-79
24801362-2	2014	The capacity of antithrombin to inhibit thrombin is known to increase a 1000-fold whilst in the presence of unfractionated heparin.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	20-28
24816371-2	2014	These Ab are directed against neoepitopes of the PF4 tetramer, which are induced by the complex formation with heparin.	Heparin	111-118	platelet factor 4	Mus musculus	49-52
24816371-6	2014	This fluid-phase approach applied to the detection of specific murine PF4/heparin Ab-secreting cells (ASC) identified the spleen as the main lymphatic organ that contributes to the PF4/heparin Ab response in mice.	Heparin	74-81	platelet factor 4	Mus musculus	181-184
24816371-1	2014	INTRODUCTION: The key feature of heparin-induced thrombocytopenia (HIT) is the production of antibodies (Ab) against the platelet factor 4 (PF4)/heparin complex.	Heparin	33-40	platelet factor 4	Mus musculus	121-138
24816371-1	2014	INTRODUCTION: The key feature of heparin-induced thrombocytopenia (HIT) is the production of antibodies (Ab) against the platelet factor 4 (PF4)/heparin complex.	Heparin	33-40	platelet factor 4	Mus musculus	140-143
24516233-0	2014	Heparin use during dialysis sessions induces an increase in the antiangiogenic factor soluble Flt1.	Heparin	0-7	fms related receptor tyrosine kinase 1	Homo sapiens	94-98
25024924-8	2014	Fc rNRP-1 bound to heparin with high affinity (2.5 nM) and fast ka (9.8 x 10(6) M(-1)s(-1)).	Heparin	19-26	neuropilin 1	Rattus norvegicus	3-9
26015966-3	2014	To achieve this, we selected the heparin-binding domain (HBD) of extracellular superoxide dismutase as a molecule to anchor IFNgamma to the cell surface.	Heparin	33-40	interferon gamma	Mus musculus	124-132
24561712-3	2014	We demonstrate here that all GAGs studied except for heparin were able to modulate interferon-gamma/lipopolysaccharide (IFN-gamma/LPS)-induced NO release by mphi to varying extents after 24h of incubation.	Heparin	53-60	interferon gamma	Mus musculus	120-129
24718936-8	2014	Inhibition of candidate signaling pathways that may link GPER activation to proliferation revealed a dependence on Src, epidermal growth factor receptor transactivation by heparin-bound EGF and subsequent ERK phosphorylation.	Heparin	172-179	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	115-118
24718936-8	2014	Inhibition of candidate signaling pathways that may link GPER activation to proliferation revealed a dependence on Src, epidermal growth factor receptor transactivation by heparin-bound EGF and subsequent ERK phosphorylation.	Heparin	172-179	epidermal growth factor receptor	Homo sapiens	120-152
24790092-8	2014	Solution NMR analysis using (15)N-labeled ZG16p defined the heparin-binding region, which is on an adjacent flat surface of the protein.	Heparin	60-67	zymogen granule protein 16	Homo sapiens	42-47
24561026-1	2014	Heparin and low-molecular-weight heparins (LMWHs) are anticoagulant drugs that mainly inhibit the coagulation cascade by indirectly interacting with factor Xa and factor IIa (thrombin).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	175-183
24671416-0	2014	Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing alpha-synuclein oligomeric species toxicity.	Heparin	31-38	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	47-87
24561026-1	2014	Heparin and low-molecular-weight heparins (LMWHs) are anticoagulant drugs that mainly inhibit the coagulation cascade by indirectly interacting with factor Xa and factor IIa (thrombin).	Heparin	33-41	coagulation factor II, thrombin	Homo sapiens	175-183
24827719-0	2014	Thrombin generation increasing with age and decreasing with use of heparin indicated by calibrated automated thrombogram conducted in Chinese.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	0-8
24664406-3	2014	Here, we report our study using saturation transfer difference (STD) nuclear magnetic resonance (NMR) to map out the interactions of synthetic heparin oligosaccharides with HBPs, such as basic fibroblast growth factor (FGF2) and fibroblast growth factor 10 (FGF10), to provide insight into the critical epitopes of heparin ligands involved.	Heparin	143-150	fibroblast growth factor 2	Homo sapiens	219-223
24664406-3	2014	Here, we report our study using saturation transfer difference (STD) nuclear magnetic resonance (NMR) to map out the interactions of synthetic heparin oligosaccharides with HBPs, such as basic fibroblast growth factor (FGF2) and fibroblast growth factor 10 (FGF10), to provide insight into the critical epitopes of heparin ligands involved.	Heparin	143-150	fibroblast growth factor 10	Homo sapiens	229-256
24664406-3	2014	Here, we report our study using saturation transfer difference (STD) nuclear magnetic resonance (NMR) to map out the interactions of synthetic heparin oligosaccharides with HBPs, such as basic fibroblast growth factor (FGF2) and fibroblast growth factor 10 (FGF10), to provide insight into the critical epitopes of heparin ligands involved.	Heparin	143-150	fibroblast growth factor 10	Homo sapiens	258-263
25126416-3	2014	Heparin coating does not affect cell viability (seen through LIVE/DEAD staining), cell anti-inflammatory properties (seen through co-culture with activated monocytes)and facilitates sequestration by coated cells of a growth factor (TGF-beta1) that remains bioactive.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	232-241
24630837-0	2014	Differentiation of endothelial progenitor cells into endothelial cells by heparin-modified supramolecular pluronic nanogels encapsulating bFGF and complexed with VEGF165 genes.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	138-142
24827719-3	2014	This study aims to determine the normal ranges of CAT parameters in Chinese, and evaluate whether thrombin generation is correlated with the concentration of heparin/low molecular weight heparin.	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	98-106
24827719-3	2014	This study aims to determine the normal ranges of CAT parameters in Chinese, and evaluate whether thrombin generation is correlated with the concentration of heparin/low molecular weight heparin.	Heparin	187-194	coagulation factor II, thrombin	Homo sapiens	98-106
25237354-5	2014	SERUM CONCENTRATIONS OF SAA (P: 0.02), CRP (P: 0.02) and ferritin (P: 0.01) significantly reduced in heparin group during measurements compared to baseline, circulating levels of IL-6 (P: 0.002), SAA (P: 0.009), CRP (P: 0.01) were significantly decreased in enoxaparin group.	Heparin	101-108	C-reactive protein	Homo sapiens	39-42
24435510-6	2014	Rec-BSPH1 was found to share many characteristics with other members of the BSP superfamily, as it was able to bind gelatin and heparin as well as capacitate sperm.	Heparin	128-135	binder of sperm protein homolog 1	Homo sapiens	4-9
24562839-6	2014	METHODS: Sclerostin levels were assessed in 20 paired serum, EDTA, and heparin plasma convenience samples from hospitalized patients.	Heparin	71-78	sclerostin	Homo sapiens	9-19
23900850-5	2014	Similar to an experiment with XCL1 that identified the two structural forms, we probed for multiple forms of zCXL1 using heparin affinity.	Heparin	121-128	CX chemokine ligand 34b, duplicate 11	Danio rerio	109-114
23900850-10	2014	We analyzed the electrostatic potential of the zCXL1 structure and identified the likely heparin-binding site for glycosaminoglycans (GAGs).	Heparin	89-96	CX chemokine ligand 34b, duplicate 11	Danio rerio	47-52
24613697-14	2014	Thrombin inhibitors argatroban, heparin (in vitro) and dabigatran (in vivo) all prolonged both OT and OT-H.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	0-8
24636486-1	2014	INTRODUCTION: Heparin is known to efficiently attenuate metastasis in various tumour models by different mechanisms including inhibition of tumour cell contacts with soluble and cellular components such as inhibition of heparanase or P- and L-selectin.	Heparin	14-21	selectin, lymphocyte	Mus musculus	241-251
24636486-10	2014	The use of N-acetylated heparin, which has no VLA-4 binding activity but blocks P- and L-selectin was less efficient than Tinzaparin in mice injected with B16F10 cells and B16F10-VLA-4kd cells.	Heparin	24-31	selectin, lymphocyte	Mus musculus	87-97
24636486-11	2014	CONCLUSION: These findings provide evidence that heparin inhibits experimental melanoma metastasis primarily by blocking VLA-4 and P-selectin.	Heparin	49-56	selectin, platelet	Mus musculus	131-141
24832898-6	2014	In the presence of heparin, a well-known activator of FGF signaling, cystic morphology with lumen expansion was observed in cultures containing FGF1, FGF7, or FGF10, but growth arrest was observed in cultures containing FGF2 or FGF9.	Heparin	19-26	fibroblast growth factor 1	Mus musculus	54-57
24832898-6	2014	In the presence of heparin, a well-known activator of FGF signaling, cystic morphology with lumen expansion was observed in cultures containing FGF1, FGF7, or FGF10, but growth arrest was observed in cultures containing FGF2 or FGF9.	Heparin	19-26	fibroblast growth factor 1	Mus musculus	144-148
24832898-6	2014	In the presence of heparin, a well-known activator of FGF signaling, cystic morphology with lumen expansion was observed in cultures containing FGF1, FGF7, or FGF10, but growth arrest was observed in cultures containing FGF2 or FGF9.	Heparin	19-26	fibroblast growth factor 9	Mus musculus	228-232
24508079-5	2014	The heparin-modified scaffolds had a greater capacity to absorb basic fibroblast growth factor (bFGF) and showed better release kinetics for up to 20 days.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	64-94
24508079-5	2014	The heparin-modified scaffolds had a greater capacity to absorb basic fibroblast growth factor (bFGF) and showed better release kinetics for up to 20 days.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	96-100
24657928-3	2014	In this paper, a density gradient of basic fibroblast growth factor (bFGF) was fabricated using an injection method and the bio-conjugation between heparin and bFGF.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	37-67
24657928-3	2014	In this paper, a density gradient of basic fibroblast growth factor (bFGF) was fabricated using an injection method and the bio-conjugation between heparin and bFGF.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	69-73
24616065-3	2014	ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra).	Heparin	103-111	angiotensin I converting enzyme	Homo sapiens	0-3
24604304-4	2014	DTIs appear to overcome the disadvantages of indirect thrombin inhibitors such as unfractionated heparins (UFH).	Heparin	107-110	coagulation factor II, thrombin	Homo sapiens	54-62
24808863-13	2014	In this review we summarized the biochemical interactions of the proteins involved in the BMP/HJV/SMAD pathway and its natural inhibitors, the murine and rat models with high hepcidin levels currently available and finally the progresses in the development of hepcidin antagonists, with particular attention to the role of heparins and heparin sulfate proteoglycans in hepcidin expression and modulation of the BMP6/SMAD pathway.	Heparin	323-331	hepcidin antimicrobial peptide	Rattus norvegicus	260-268
24808863-13	2014	In this review we summarized the biochemical interactions of the proteins involved in the BMP/HJV/SMAD pathway and its natural inhibitors, the murine and rat models with high hepcidin levels currently available and finally the progresses in the development of hepcidin antagonists, with particular attention to the role of heparins and heparin sulfate proteoglycans in hepcidin expression and modulation of the BMP6/SMAD pathway.	Heparin	323-331	hepcidin antimicrobial peptide	Rattus norvegicus	260-268
24297394-13	2014	LDL receptor blocking agent heparin decreased lipid droplets induced by LPS significantly in THP-1 macrophages and VSMCs.	Heparin	28-35	GLI family zinc finger 2	Homo sapiens	93-98
25237354-5	2014	SERUM CONCENTRATIONS OF SAA (P: 0.02), CRP (P: 0.02) and ferritin (P: 0.01) significantly reduced in heparin group during measurements compared to baseline, circulating levels of IL-6 (P: 0.002), SAA (P: 0.009), CRP (P: 0.01) were significantly decreased in enoxaparin group.	Heparin	101-108	interleukin 6	Homo sapiens	179-183
25237354-5	2014	SERUM CONCENTRATIONS OF SAA (P: 0.02), CRP (P: 0.02) and ferritin (P: 0.01) significantly reduced in heparin group during measurements compared to baseline, circulating levels of IL-6 (P: 0.002), SAA (P: 0.009), CRP (P: 0.01) were significantly decreased in enoxaparin group.	Heparin	101-108	C-reactive protein	Homo sapiens	212-215
24433416-7	2014	Podocin localization at cell-cell contact sites became conspicuous in the presence of heparin.	Heparin	86-93	NPHS2 stomatin family member, podocin	Homo sapiens	0-7
24530399-3	2014	We demonstrated in a previous study that, in rat heart and post-heparin plasma (PHP), LPL consists of a pattern of more than 8 forms of the same apparent molecular weight, but different isoelectric point (pI).	Heparin	64-71	lipoprotein lipase	Rattus norvegicus	86-89
24262631-8	2014	Low molecular weight heparin, known to inhibit the receptor for advanced glycation end products (RAGE), but not lipopolysaccharide from Rhodobacter sphaeroides, an inhibitor of toll-like receptor 4 (TLR4), blocked the cyclophosphamide-induced bladder pain and referred hyperalgesia.	Heparin	21-28	advanced glycosylation end product-specific receptor	Mus musculus	97-101
24525311-0	2014	Low molecular weight heparin-induced increase in chylomicron-remnants clearance, is associated with decreased plasma TNF-alpha level and increased hepatic lipase activity.	Heparin	21-28	tumor necrosis factor	Homo sapiens	117-126
24482224-8	2014	The results are as follows: 1) heparin blocks synthesis of hyaluronan in intracellular compartments, which prevents the autophagy and cyclin D3 responses thereby allowing RMCs to complete cell division and sustain function; 2) interaction of heparin with RMCs in early G1 phase is sufficient to induce signaling pathway(s) for its functions; and 3) influxed macrophages effectively remove the hyaluronan matrix without inducing pro-fibrotic responses that lead to nephropathy and proteinurea in diabetic kidneys.	Heparin	31-38	cyclin D3	Rattus norvegicus	134-143
24641672-0	2014	Heparin binding VEGF isoforms attenuate hyperoxic embryonic lung growth retardation via a FLK1-neuropilin-1-PKC dependent pathway.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	16-20
24641672-5	2014	RESULTS: Heparin-binding VEGF isoforms (VEGF164/Vegf165 and VEGF188) but not Vegf121 selectively reduced epithelial apoptosis and partially rescued lung bud branching and growth.	Heparin	9-16	vascular endothelial growth factor A	Homo sapiens	25-29
24595027-4	2014	We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site.	Heparin	159-166	fibroblast growth factor 1	Homo sapiens	32-36
24398330-3	2014	We studied nonanticoagulant heparins produced by N-acetylation and oxidation/reduction (glycol-split) that lost antithrombin-binding affinity.	Heparin	28-36	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	112-124
24595027-4	2014	We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site.	Heparin	159-166	fibroblast growth factor 1	Homo sapiens	105-109
22914811-6	2014	CONCLUSION: Bivalirudin, as a direct thrombin inhibitor, could circumvent the increased antiheparin/PF4 antibody level in circulation due to the heparin administration.	Heparin	92-99	coagulation factor II	Rattus norvegicus	37-45
24344642-0	2014	Heparanase-mediated cleavage of macromolecular heparin accelerates release of granular components of mast cells from extracellular matrices.	Heparin	47-54	heparanase	Mus musculus	0-10
24344642-1	2014	Heparanase cleaves macromolecular heparin in the secretory granules of connective tissue-type mast cells.	Heparin	34-41	heparanase	Mus musculus	0-10
24344642-4	2014	The cells expressing heparanase stored fragmented heparin (~10 kDa) due to heparanase-dependent cleavage of the heparin.	Heparin	50-57	heparanase	Mus musculus	21-31
24344642-8	2014	Purified chymase mixed with fragmented heparin derived from heparanase-expressing cells showed greater release from collagen gels than the enzyme alone or mixed with macromolecular heparin derived from mock cells.	Heparin	39-46	heparanase	Mus musculus	60-70
24344642-9	2014	We propose that the cleavage of macromolecular heparin by heparanase accelerates the release of heparin and chymase from extracellular matrices.	Heparin	47-54	heparanase	Mus musculus	58-68
24520253-8	2014	Prothrombin fragment and thrombin-antithrombin complex levels in the heparin group were significantly decreased.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	0-11
24423299-10	2014	RESULTS: In nonpregnant women, heparin increased plasma sFLT1 by 250-fold (P &lt; .01), increased placental growth factor by 7-fold (P &lt; .01), and decreased free vascular endothelial growth factor (P &lt; .01).	Heparin	31-38	placental growth factor	Homo sapiens	98-121
24193793-4	2014	Heparin has been shown to interfere with the binding of the integrin Very Late Antigen 4 (VLA-4) to its ligand Vascular Cell Adhesion Molecule 1 (VCAM-1) and in a recent paper the laboratory of Bendas (Thrombosis and Haemostasis, Prepublished online) demonstrated that CCN1 binds to VLA-4 and interference in this binding by heparin results in reduced strength of the VLA-4/VCAM-1 binding.	Heparin	0-7	vascular cell adhesion molecule 1	Homo sapiens	111-144
24193793-4	2014	Heparin has been shown to interfere with the binding of the integrin Very Late Antigen 4 (VLA-4) to its ligand Vascular Cell Adhesion Molecule 1 (VCAM-1) and in a recent paper the laboratory of Bendas (Thrombosis and Haemostasis, Prepublished online) demonstrated that CCN1 binds to VLA-4 and interference in this binding by heparin results in reduced strength of the VLA-4/VCAM-1 binding.	Heparin	0-7	vascular cell adhesion molecule 1	Homo sapiens	146-152
24193793-4	2014	Heparin has been shown to interfere with the binding of the integrin Very Late Antigen 4 (VLA-4) to its ligand Vascular Cell Adhesion Molecule 1 (VCAM-1) and in a recent paper the laboratory of Bendas (Thrombosis and Haemostasis, Prepublished online) demonstrated that CCN1 binds to VLA-4 and interference in this binding by heparin results in reduced strength of the VLA-4/VCAM-1 binding.	Heparin	0-7	vascular cell adhesion molecule 1	Homo sapiens	374-380
24193793-4	2014	Heparin has been shown to interfere with the binding of the integrin Very Late Antigen 4 (VLA-4) to its ligand Vascular Cell Adhesion Molecule 1 (VCAM-1) and in a recent paper the laboratory of Bendas (Thrombosis and Haemostasis, Prepublished online) demonstrated that CCN1 binds to VLA-4 and interference in this binding by heparin results in reduced strength of the VLA-4/VCAM-1 binding.	Heparin	325-332	vascular cell adhesion molecule 1	Homo sapiens	111-144
24193793-4	2014	Heparin has been shown to interfere with the binding of the integrin Very Late Antigen 4 (VLA-4) to its ligand Vascular Cell Adhesion Molecule 1 (VCAM-1) and in a recent paper the laboratory of Bendas (Thrombosis and Haemostasis, Prepublished online) demonstrated that CCN1 binds to VLA-4 and interference in this binding by heparin results in reduced strength of the VLA-4/VCAM-1 binding.	Heparin	325-332	vascular cell adhesion molecule 1	Homo sapiens	146-152
24423299-10	2014	RESULTS: In nonpregnant women, heparin increased plasma sFLT1 by 250-fold (P &lt; .01), increased placental growth factor by 7-fold (P &lt; .01), and decreased free vascular endothelial growth factor (P &lt; .01).	Heparin	31-38	vascular endothelial growth factor A	Homo sapiens	165-199
24057103-3	2014	FGF2 activates FGFRs in cooperation with heparin or heparin sulfate proteoglycan to induce its pleiotropic effects in different tissues and organs, which include potent angiogenic effects and important roles in the differentiation and function of the central nervous system (CNS).	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	0-4
24048373-9	2014	Thus, the relationship between atherosclerosis and PlGF signaling, as regulated by sFlt-1, underscores the underappreciated role of heparin in sFlt-1 release.	Heparin	132-139	placental growth factor	Homo sapiens	51-55
32261321-3	2014	Compared to the pristine titanium, a highly hydrophilic layer was achieved after the immobilization, and the resulting heparin-PEG layer can significantly prevent human plasma fibrinogen adsorption.	Heparin	119-126	fibrinogen beta chain	Homo sapiens	176-186
24352373-2	2014	METHODS: We tested how the in vitro release of FGF-2 from heparin-conjugated poly(L-lactide-co-glycolide) (PLGA)-conjugated nanospheres (HCPNs) affected the growth of human bone marrow-derived mesenchymal stem cells (hBMSCs), as well as the effects of their co-transplantation in an animal model of SCI.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	47-52
24471746-8	2014	The ELISA substance P immunoreactivity was typically lower for blood samples with heparin versus samples with other inhibitors processed at 1 hour of holding in either temperature condition.	Heparin	82-89	tachykinin precursor 1	Bos taurus	10-21
24013828-1	2014	Bivalirudin, used in patients with heparin-induced thrombocytopenia, is a direct thrombin inhibitor.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	81-89
24359968-7	2014	RESULTS: Our study shows that detection of ECC-mediated changes in free thrombin is possible in blood anticoagulated with 0.75 or 1 IU/ml heparin, whereas no thrombin was detectable at higher heparin concentrations.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	72-80
24423090-1	2014	Heparin is a widely used anticoagulant due to its ability to inhibit key components in the coagulation cascade such as Factor Xa and thrombin (Factor IIa).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	133-141
24242364-2	2014	Heparin and heparan sulfates (HS) have been reported to be high-affinity ligands for fibronectin.	Heparin	0-7	fibronectin 1	Homo sapiens	85-96
24242364-3	2014	The strongest heparin/HS-binding site, named Hep-II, is located in the C-terminal repeat units FN12-14 of fibronectin.	Heparin	14-21	fibronectin 1	Homo sapiens	106-117
24242364-5	2014	Heparin, which is more sulfated than HS, is a better ligand for fibronectin, indicating that the sulfate density is important for the interactions.	Heparin	0-7	fibronectin 1	Homo sapiens	64-75
24242364-7	2014	In the current work, we used molecular docking of Hep-II domain of fibronectin with a series of differently sulfated dodecasaccharides of heparin to determine the implication of each sulfate position in the interaction.	Heparin	138-145	fibronectin 1	Homo sapiens	67-78
24325876-7	2014	Moreover, warfarinized plasmas from 2 heterozygous patients with prothrombin Yukuhashi mutation clearly showed higher values of the relative residual thrombin activity than those from 5 thrombosis patients lacking the mutation in the presence or absence of heparin.	Heparin	257-264	coagulation factor II, thrombin	Homo sapiens	68-76
24148804-2	2014	Heparin and heparan sulfate, for example, have been shown to regulate the sequestration and presentation of numerous growth factors, including vascular endothelial growth factor, on the heparin 2 binding domain in fibronectin (Fn).	Heparin	0-7	fibronectin 1	Homo sapiens	227-229
24148804-3	2014	However, mechanical force also alters Fn conformation, indicating that the growth factor binding region may be co-regulated by both heparin and mechanical force.	Heparin	132-139	fibronectin 1	Homo sapiens	38-40
24148804-4	2014	Herein, we describe a simple antibody-based method for evaluating the conformation of the heparin 2 binding domain in Fn, and use it to determine the relative contributions of heparin and mechanical strain to the regulation of Fn conformation.	Heparin	90-97	fibronectin 1	Homo sapiens	118-120
24148804-4	2014	Herein, we describe a simple antibody-based method for evaluating the conformation of the heparin 2 binding domain in Fn, and use it to determine the relative contributions of heparin and mechanical strain to the regulation of Fn conformation.	Heparin	90-97	fibronectin 1	Homo sapiens	227-229
24148804-7	2014	Using our dual antibody approach, we show that heparin and mechanical strain co-regulate Fn conformation in matrix fibrils, which is the first demonstration of heparin-dependent regulation of Fn in its physiologically-relevant fibrillar state.	Heparin	47-54	fibronectin 1	Homo sapiens	89-91
24148804-7	2014	Using our dual antibody approach, we show that heparin and mechanical strain co-regulate Fn conformation in matrix fibrils, which is the first demonstration of heparin-dependent regulation of Fn in its physiologically-relevant fibrillar state.	Heparin	47-54	fibronectin 1	Homo sapiens	192-194
24148804-7	2014	Using our dual antibody approach, we show that heparin and mechanical strain co-regulate Fn conformation in matrix fibrils, which is the first demonstration of heparin-dependent regulation of Fn in its physiologically-relevant fibrillar state.	Heparin	160-167	fibronectin 1	Homo sapiens	89-91
24148804-7	2014	Using our dual antibody approach, we show that heparin and mechanical strain co-regulate Fn conformation in matrix fibrils, which is the first demonstration of heparin-dependent regulation of Fn in its physiologically-relevant fibrillar state.	Heparin	160-167	fibronectin 1	Homo sapiens	192-194
24430559-4	2014	Herein, a novel polymeric nanoparticle delivery system composed of heparin and e-poly-L-lysine (PL) was prepared for control release of nerve growth factor (NGF) and basic fibroblast growth factor (bFGF).	Heparin	67-74	fibroblast growth factor 2	Homo sapiens	166-196
24430559-4	2014	Herein, a novel polymeric nanoparticle delivery system composed of heparin and e-poly-L-lysine (PL) was prepared for control release of nerve growth factor (NGF) and basic fibroblast growth factor (bFGF).	Heparin	67-74	fibroblast growth factor 2	Homo sapiens	198-202
24196373-1	2014	Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE).	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	21-29
24148803-2	2014	Although LTBP-2 binds fibrillin-1, fibulin-5, and heparin/heparan sulfate, molecules critical for normal elastic fiber assembly, it does not interact directly with elastin or its precursor, tropoelastin.	Heparin	50-57	latent transforming growth factor beta binding protein 2	Homo sapiens	9-15
24148803-7	2014	In parallel experiments heparin was shown to have minor inhibitory effects on fibulin-5 interactions with tropoelastin and LTBP-2.	Heparin	24-31	latent transforming growth factor beta binding protein 2	Homo sapiens	123-129
24148803-8	2014	However, LTBP-2 was shown to significantly inhibit the binding of heparin to tropoelastin with 50% inhibition achieved with 10 fold molar excess of LTBP-2.	Heparin	66-73	latent transforming growth factor beta binding protein 2	Homo sapiens	9-15
24148803-8	2014	However, LTBP-2 was shown to significantly inhibit the binding of heparin to tropoelastin with 50% inhibition achieved with 10 fold molar excess of LTBP-2.	Heparin	66-73	latent transforming growth factor beta binding protein 2	Homo sapiens	148-154
24148804-2	2014	Heparin and heparan sulfate, for example, have been shown to regulate the sequestration and presentation of numerous growth factors, including vascular endothelial growth factor, on the heparin 2 binding domain in fibronectin (Fn).	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	143-177
24148804-2	2014	Heparin and heparan sulfate, for example, have been shown to regulate the sequestration and presentation of numerous growth factors, including vascular endothelial growth factor, on the heparin 2 binding domain in fibronectin (Fn).	Heparin	0-7	fibronectin 1	Homo sapiens	214-225
24287143-6	2014	Both heparin treatments decreased the accumulation of T cells and macrophages (P &lt; .03), and the activation of NF-kappaB and pERK (P &lt; .04) in the diverted colon.	Heparin	5-12	nuclear factor kappa B subunit 1	Homo sapiens	114-123
24287143-7	2014	The high levels of cytokines IL-1beta, TNF-alpha, and IL-6 from the diversion colitis explants decreased (P &lt; .05) to near normal values with heparin treatments.	Heparin	145-152	interleukin 1 beta	Homo sapiens	29-37
24287143-7	2014	The high levels of cytokines IL-1beta, TNF-alpha, and IL-6 from the diversion colitis explants decreased (P &lt; .05) to near normal values with heparin treatments.	Heparin	145-152	tumor necrosis factor	Homo sapiens	39-48
24287143-7	2014	The high levels of cytokines IL-1beta, TNF-alpha, and IL-6 from the diversion colitis explants decreased (P &lt; .05) to near normal values with heparin treatments.	Heparin	145-152	interleukin 6	Homo sapiens	54-58
26316665-3	2014	The ACC/AHA/SCAI PCI guidelines2 recommend a 70-100 IU/kg bolus of heparin to achieve an activated clotting time (ACT) of 250-300 seconds for Hemotec and 300-350 seconds for Hemochron systems, when glycoprotein IIb/IIIa inhibitors are not used.	Heparin	67-74	suppressor of cancer cell invasion	Homo sapiens	12-16
24440699-5	2014	All SAA1 isoforms adopted alpha-helix structures at 4 C, but were unstructured at 37 C. Heparin-induced amyloid fibril formation of SAA1 was observed at 37 C, as evidenced by the increased thioflavin T (ThT) fluorescence and beta-sheet structure formation.	Heparin	88-95	serum amyloid A1	Homo sapiens	4-8
24440699-5	2014	All SAA1 isoforms adopted alpha-helix structures at 4 C, but were unstructured at 37 C. Heparin-induced amyloid fibril formation of SAA1 was observed at 37 C, as evidenced by the increased thioflavin T (ThT) fluorescence and beta-sheet structure formation.	Heparin	88-95	serum amyloid A1	Homo sapiens	132-136
24438360-5	2014	RESULTS: In the heparin group, there was C5a production across the filter which most decreased over time as compared to other groups (P = 0.007).	Heparin	16-23	complement C5a receptor 1	Homo sapiens	41-44
24438360-6	2014	There was also net production of elastase and MPO across the filter during heparin anticoagulation (P = 0.049 or lower), while production was minimal and absent in the no anticoagulation and citrate group, respectively.	Heparin	75-82	myeloperoxidase	Homo sapiens	46-49
24438360-7	2014	During heparin anticoagulation, plasma concentrations of MPO at the inlet increased in the first 10 minutes of CVVH (P = 0.024).	Heparin	7-14	myeloperoxidase	Homo sapiens	57-60
24065244-4	2014	Our data revealed that platelets exposed to heparins released significantly decreased vascular endothelial growth factor (VEGF) in response to adenosine 5"-diphosphate or tumor cells (MCF-7 cells) and exhibited a decreased angiogenic potential.	Heparin	44-52	vascular endothelial growth factor A	Homo sapiens	86-120
24065244-4	2014	Our data revealed that platelets exposed to heparins released significantly decreased vascular endothelial growth factor (VEGF) in response to adenosine 5"-diphosphate or tumor cells (MCF-7 cells) and exhibited a decreased angiogenic potential.	Heparin	44-52	vascular endothelial growth factor A	Homo sapiens	122-126
24307707-5	2014	Rec-BSPH2 was found to share some binding characteristics with other BSP proteins, such as binding to gelatin, heparin, and epididymal sperm.	Heparin	111-118	binder of sperm protein homolog 2	Mus musculus	4-9
24325674-8	2014	Treatment of recombinant rat apoE with a 10-fold molar excess of acrolein resulted in (i) a significant decrease in lipid-binding and cholesterol efflux abilities, (ii) impairment in the LDLr- and heparin-binding capabilities, and (iii) significant alterations in the overall stability of the protein.	Heparin	197-204	apolipoprotein E	Rattus norvegicus	29-33
23828859-7	2014	Cultivation of hepatocytes followed by analysis of hepatic markers (urea production, albumin synthesis, and E-cadherin expression) reveals that the all-heparin gel microwells are most conducive to hepatic phenotype maintenance.	Heparin	152-159	cadherin 1	Homo sapiens	108-118
24253450-6	2014	Among the ABC system, heparin treatment caused significant inhibition of the ATPase activity of ABCG2 and ABCC1, and of the efflux function observed as enhanced intracellular accumulation of specific substrates.	Heparin	22-29	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	96-101
24099708-4	2014	This study examined the potential of low molecular weight heparin as a material for refining silk properties by acting as a carrier for vascular endothelial growth factor (VEGF) and improving silk hemocompatibility.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	136-170
24099708-4	2014	This study examined the potential of low molecular weight heparin as a material for refining silk properties by acting as a carrier for vascular endothelial growth factor (VEGF) and improving silk hemocompatibility.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	172-176
24253450-6	2014	Among the ABC system, heparin treatment caused significant inhibition of the ATPase activity of ABCG2 and ABCC1, and of the efflux function observed as enhanced intracellular accumulation of specific substrates.	Heparin	22-29	ATP binding cassette subfamily C member 1	Homo sapiens	106-111
24985584-10	2014	Heparin markedly decreased both IL-1alpha and IL-1beta expression in the spleens and serum of burned mice.	Heparin	0-7	interleukin 1 beta	Mus musculus	46-54
28890953-6	2014	The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7).	Heparin	125-132	fibroblast growth factor 1	Homo sapiens	144-170
24211016-10	2014	Heparin treatment further reduced RANTES binding of all three M-T7 mutants.	Heparin	0-7	chemokine (C-C motif) ligand 5	Mus musculus	34-40
24014620-5	2014	Antithrombin (AT) binds to heparin and increases the rate at which it binds to thrombin.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	4-12
28890953-6	2014	The results showed that under non-physiological of metal ion concentration, different metal ions showed different effects on heparin binding to fibroblast growth factor-1 (FGF1) and interleakin-7 (IL7).	Heparin	125-132	fibroblast growth factor 1	Homo sapiens	172-176
24266905-0	2014	Early heparin administration attenuates tissue factor-mediated thrombin generation during simulated cardiopulmonary bypass.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	63-71
24266905-1	2014	BACKGROUND: We tested the hypothesis that heparin administration prior to the emergence of tissue factor (TF) would increase plasma TF pathway inhibitor (TFPI) and attenuate TF-mediated thrombin generation during simulated cardiopulmonary bypass (CPB).	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	186-194
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	48-56
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	61-69
28890953-7	2014	While the effects of individual metal ion at physiological concentrations had little impact on protein binding, the mixed metal ions reduced the FGF1/heparin or IL7/heparin binding affinity, changing its binding profile.	Heparin	150-157	fibroblast growth factor 1	Homo sapiens	145-149
24266905-10	2014	CONCLUSIONS: Heparin-induced TFPI elevation attenuates TF-mediated thrombin generation.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	67-75
24266905-11	2014	Early heparin administration prior to the emergence of plasma TF may represent a novel strategy for controlling thrombin generation by the extrinsic coagulation pathway during CPB.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	112-120
24247246-1	2013	HS3st1 (heparan sulfate 3-O-sulfotransferase isoform-1) is a critical enzyme involved in the biosynthesis of the antithrombin III (AT)-binding site in the biopharmaceutical drug heparin.	Heparin	178-185	heparan sulfate glucosamine 3-O-sulfotransferase 1	Cricetulus griseus	0-6
24247246-1	2013	HS3st1 (heparan sulfate 3-O-sulfotransferase isoform-1) is a critical enzyme involved in the biosynthesis of the antithrombin III (AT)-binding site in the biopharmaceutical drug heparin.	Heparin	178-185	heparan sulfate glucosamine 3-O-sulfotransferase 1	Cricetulus griseus	8-54
24247246-4	2013	As part of an effort to bioengineer CHO cells to produce heparin, we previously showed that the introduction of both HS3st1 and NDST2 (N-deacetylase/N-sulfotransferase isoform-2) afforded HS with a very low level of anticoagulant activity.	Heparin	57-64	heparan sulfate glucosamine 3-O-sulfotransferase 1	Cricetulus griseus	117-123
24247246-6	2013	Moreover, stable overexpression of HS3st1 also results in up-regulation of 2-O-, 6-O-, and N-sulfo group-containing disaccharides, further emphasizing a previously unknown concerted interplay between the HS biosynthetic enzymes and suggesting the need to control the expression level of all of the biosynthetic enzymes to produce heparin in CHO cells.	Heparin	330-337	heparan sulfate glucosamine 3-O-sulfotransferase 1	Cricetulus griseus	35-41
24178304-0	2013	3D structure of a heparin mimetic analogue of a FGF-1 activator.	Heparin	18-25	fibroblast growth factor 1	Homo sapiens	48-53
23848206-9	2013	The effects of xanthochymol were enhanced by U0126, at low doses, and were blocked by heparin, indicating that the MEK pathway is involved, while the ER IP3 receptor is critical for its action.	Heparin	86-93	mitogen-activated protein kinase kinase 7	Homo sapiens	115-118
24351527-9	2014	RESULTS: In vitro studies revealed increased fibrinogen reversed the effects of heparin as measured by TEG.	Heparin	80-87	fibrinogen beta chain	Homo sapiens	45-55
24351527-13	2014	Moreover, there was a moderate inverse correlation between fibrinogen level and the effect of heparin (RF), which was significant on study days 1 and 3, implicating hyperfibrinogenemia in heparin resistance.	Heparin	94-101	fibrinogen beta chain	Homo sapiens	59-69
24351527-13	2014	Moreover, there was a moderate inverse correlation between fibrinogen level and the effect of heparin (RF), which was significant on study days 1 and 3, implicating hyperfibrinogenemia in heparin resistance.	Heparin	188-195	fibrinogen beta chain	Homo sapiens	59-69
24351527-15	2014	The preclinical and clinical relationships between fibrinogen levels and hypercoagulability implicate hyperfibrinogenemia as a potential factor in heparin resistance.	Heparin	147-154	fibrinogen beta chain	Homo sapiens	51-61
24078129-0	2013	Impact of heparin-binding domain of recombinant human osteocalcin-fibronectinIII9-14 on the osteoblastic cell response.	Heparin	10-17	bone gamma-carboxyglutamate protein	Homo sapiens	54-65
24267251-8	2013	CONCLUSION: Our data demonstrate that heparin-induced mobilization of vessel-bound MPO is closely linked to coronary plaque burden and thus further corroborate the evidence for the intimate involvement of this enzyme in vascular pathophysiology, as well as the importance of inflammation in atherosclerosis.	Heparin	38-45	myeloperoxidase	Homo sapiens	83-86
24205388-5	2013	Heparin-binding domains within Fg (residues 15-66 of the beta chain, Fg beta15-66) and FN (FNI1-5, but not FNIII12-14) were involved in binding to CXCL10 and CXCL11 but not CXCL9.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	31-33
24371161-1	2013	The heparan sulfate 6-O-sulfotransferase 3 (HS6ST3) gene is involved in heparan sulphate and heparin metabolism, and has been reported to be associated with diabetic retinopathy in type 2 diabetes.We hypothesized that HS6ST3 gene polymorphisms might play an important role in obesity and related phenotypes (such as triglycerides).	Heparin	93-100	heparan sulfate 6-O-sulfotransferase 3	Homo sapiens	4-42
24371161-1	2013	The heparan sulfate 6-O-sulfotransferase 3 (HS6ST3) gene is involved in heparan sulphate and heparin metabolism, and has been reported to be associated with diabetic retinopathy in type 2 diabetes.We hypothesized that HS6ST3 gene polymorphisms might play an important role in obesity and related phenotypes (such as triglycerides).	Heparin	93-100	heparan sulfate 6-O-sulfotransferase 3	Homo sapiens	44-50
24371161-1	2013	The heparan sulfate 6-O-sulfotransferase 3 (HS6ST3) gene is involved in heparan sulphate and heparin metabolism, and has been reported to be associated with diabetic retinopathy in type 2 diabetes.We hypothesized that HS6ST3 gene polymorphisms might play an important role in obesity and related phenotypes (such as triglycerides).	Heparin	93-100	heparan sulfate 6-O-sulfotransferase 3	Homo sapiens	218-224
24068708-0	2013	The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	46-54
24118982-3	2013	Each FXIa subunit contains anion-binding sites (ABSs) on the apple 3 (A3) and catalytic domains that are required for normal heparin-mediated enhancement of FXIa inhibition by antithrombin.	Heparin	125-132	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	176-188
23690274-8	2013	The mechanisms by which unfractionated heparin exerts its anti-inflammatory effect are correlated with inhibition of IL-1beta and IL-6 production via inactivation of NF-kappaB.	Heparin	39-46	interleukin 1 beta	Rattus norvegicus	117-125
23690274-8	2013	The mechanisms by which unfractionated heparin exerts its anti-inflammatory effect are correlated with inhibition of IL-1beta and IL-6 production via inactivation of NF-kappaB.	Heparin	39-46	interleukin 6	Rattus norvegicus	130-134
24048327-9	2013	In the presence of fibrin, the k2 values decreased to 1.45 +- 0.10 x 106 M-1 min-1 and 3.07 +- 0.19 x 106 M-1 min-1 for AT+UFH and ATH, respectively.	Heparin	123-126	myoregulin	Homo sapiens	73-88
24077357-1	2013	In order to find novel potent inhibitors for signal pathways of FGF/FGFR, nineteen N-(3-aryl acryloyl)aminosaccharide derivatives were designed and synthesized based on the binding sites of FGF and oligosaccharides of heparin.	Heparin	218-225	fibroblast growth factor 10	Gallus gallus	64-67
24077357-1	2013	In order to find novel potent inhibitors for signal pathways of FGF/FGFR, nineteen N-(3-aryl acryloyl)aminosaccharide derivatives were designed and synthesized based on the binding sites of FGF and oligosaccharides of heparin.	Heparin	218-225	fibroblast growth factor 10	Gallus gallus	68-71
23942551-10	2013	These data indicate a role for Src in a high glucose-Src-TACE-heparin-binding epidermal growth factor-EGFR-MAPK-signaling pathway to collagen accumulation.	Heparin	62-69	a disintegrin and metallopeptidase domain 17	Mus musculus	57-61
23942551-10	2013	These data indicate a role for Src in a high glucose-Src-TACE-heparin-binding epidermal growth factor-EGFR-MAPK-signaling pathway to collagen accumulation.	Heparin	62-69	mitogen-activated protein kinase 1	Mus musculus	107-111
24205388-5	2013	Heparin-binding domains within Fg (residues 15-66 of the beta chain, Fg beta15-66) and FN (FNI1-5, but not FNIII12-14) were involved in binding to CXCL10 and CXCL11 but not CXCL9.	Heparin	0-7	C-X-C motif chemokine ligand 9	Homo sapiens	173-178
23990470-0	2013	Zn2+ mediates high affinity binding of heparin to the alphaC domain of fibrinogen.	Heparin	39-46	fibrinogen beta chain	Homo sapiens	71-81
23990470-2	2013	In addition, interaction of heparin with fibrin promotes formation of a ternary heparin-thrombin-fibrin complex that protects fibrin-bound thrombin from inhibition by the heparin-antithrombin complex.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	88-96
23990470-2	2013	In addition, interaction of heparin with fibrin promotes formation of a ternary heparin-thrombin-fibrin complex that protects fibrin-bound thrombin from inhibition by the heparin-antithrombin complex.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	139-147
23990470-3	2013	Previous studies have shown that heparin binds the E domain of fibrinogen.	Heparin	33-40	fibrinogen beta chain	Homo sapiens	63-73
23990470-5	2013	Zn(2+) promotes heparin binding to fibrinogen, as determined by chromatography, fluorescence, and surface plasmon resonance.	Heparin	16-23	fibrinogen beta chain	Homo sapiens	35-45
23990470-6	2013	Compared with intact fibrinogen, there is reduced heparin binding to fragment X, a clottable plasmin degradation product of fibrinogen.	Heparin	50-57	fibrinogen beta chain	Homo sapiens	21-31
23990470-6	2013	Compared with intact fibrinogen, there is reduced heparin binding to fragment X, a clottable plasmin degradation product of fibrinogen.	Heparin	50-57	fibrinogen beta chain	Homo sapiens	124-134
23990470-7	2013	A monoclonal antibody directed against a portion of the fibrinogen alphaC domain removed by plasmin attenuates binding of heparin to fibrinogen and a peptide analog of this region binds heparin in a Zn(2+)-dependent fashion.	Heparin	122-129	fibrinogen beta chain	Homo sapiens	56-66
23990470-7	2013	A monoclonal antibody directed against a portion of the fibrinogen alphaC domain removed by plasmin attenuates binding of heparin to fibrinogen and a peptide analog of this region binds heparin in a Zn(2+)-dependent fashion.	Heparin	122-129	fibrinogen beta chain	Homo sapiens	133-143
23990470-7	2013	A monoclonal antibody directed against a portion of the fibrinogen alphaC domain removed by plasmin attenuates binding of heparin to fibrinogen and a peptide analog of this region binds heparin in a Zn(2+)-dependent fashion.	Heparin	186-193	fibrinogen beta chain	Homo sapiens	56-66
23990470-8	2013	These results indicate that the alphaC domain of fibrinogen harbors a Zn(2+)-dependent heparin binding site.	Heparin	87-94	fibrinogen beta chain	Homo sapiens	49-59
23990470-9	2013	As a consequence, heparin-catalyzed inhibition of factor Xa by antithrombin is compromised by fibrinogen to a greater extent when Zn(2+) is present.	Heparin	18-25	fibrinogen beta chain	Homo sapiens	94-104
23990470-10	2013	These results reveal the mechanism by which Zn(2+) augments the capacity of fibrinogen to impair the anticoagulant activity of heparin.	Heparin	127-134	fibrinogen beta chain	Homo sapiens	76-86
23559035-1	2013	(hbd) PRELP is a peptide corresponding to the N-terminal heparin binding domain of the matrix protein proline/arginine-rich end leucine-rich repeat protein (PRELP).	Heparin	57-64	exocyst complex component 6	Mus musculus	1-4
24247801-1	2013	BACKGROUND: Over-diagnosis of heparin-induced thrombocytopenia (HIT) results in costly and unnecessary laboratory screening and treatment with direct thrombin inhibitors.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	150-158
24273488-7	2013	CONCLUSION: Heparin can significantly enhance the stimulating effects of a combination of TPO, SCF, FL, IL-6, and IL-11 supplemented with autologous serum on CFU-MK, MK, and platelet production from CB CD34+ cells.	Heparin	12-19	thrombopoietin	Homo sapiens	90-93
24273488-7	2013	CONCLUSION: Heparin can significantly enhance the stimulating effects of a combination of TPO, SCF, FL, IL-6, and IL-11 supplemented with autologous serum on CFU-MK, MK, and platelet production from CB CD34+ cells.	Heparin	12-19	interleukin 6	Homo sapiens	104-108
24273488-7	2013	CONCLUSION: Heparin can significantly enhance the stimulating effects of a combination of TPO, SCF, FL, IL-6, and IL-11 supplemented with autologous serum on CFU-MK, MK, and platelet production from CB CD34+ cells.	Heparin	12-19	CD34 molecule	Homo sapiens	202-206
23897813-4	2013	Deletion of the C-terminal cytoplasmic domain of CD82 (CD82DeltaC mutant) inhibits endocytic trafficking of the tetraspanin and compromises its activity toward heparin-binding EGF-activated EGFR.	Heparin	160-167	epidermal growth factor receptor	Homo sapiens	190-194
23897813-8	2013	Our data identify CD82 as a new regulator of c-Cbl, which discriminatively controls the activity of this E3 ubiquitin ligase toward heparin-binding ligand-EGFR pairs.	Heparin	132-139	epidermal growth factor receptor	Homo sapiens	155-159
24273488-0	2013	Promoting Effects of Heparin on ex vivo Expansion of Megakaryocytopoiesis from Human Cord Blood CD34+ Cells.	Heparin	21-28	CD34 molecule	Homo sapiens	96-100
24163620-6	2013	The critical concentrations of 4RMBD and its S305N mutant are 5.26 muM and 4.04 muM respectively, indicating point mutation S305N, which is associated with FTDP-17, appear to enhance the heparin-induced tau aggregation in vitro.	Heparin	187-194	latexin	Homo sapiens	80-83
24039769-5	2013	To this end, the C2IN-p53 fusion construct was overexpressed in E. coli with good solubility, purified by heparin affinity chromatography and protein identity was confirmed by immunoblotting.	Heparin	106-113	tumor protein p53	Homo sapiens	22-25
23844141-9	2013	Likewise, the HSPG-binding peptide prevented apoE from binding to heparin in a dose-dependent manner, as determined by an in vitro heparin pull-down assay.	Heparin	66-73	apolipoprotein E	Homo sapiens	45-49
23625867-7	2013	CONCLUSION: An individualized and stable heparin concentration and appropriate dosing of protamine can reduce thrombin generation and preserve platelet function, even in short-time CPB.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	110-118
23884640-6	2013	Prolonged exposure to BMP2 released by the PEAD:heparin delivery system promoted the differentiation of MDSCs to an osteogenic lineage in vitro and induced the formation of viable bone at an ectopic site in vivo.	Heparin	48-55	bone morphogenetic protein 2	Mus musculus	22-26
23748000-9	2013	The rate of uptake and the level of GCIP-27 in the cells decreased significantly after treatment with energy inhibitors, methyl-ss-cyclodextrin chlorpromazine or heparin.	Heparin	162-169	cyclin D1 binding protein 1	Homo sapiens	36-40
23712900-10	2013	In the presence of heparin, KGF-2 interfacial gels formed too quickly for gelation time to be determined.	Heparin	19-26	fibroblast growth factor 10	Homo sapiens	28-33
23597922-9	2013	In order to understand the mechanism of heparin-induced stabilization of p27(kip1) in VSMC, we examined the involvement of the Signal Transducer and Activator of Transcription-1 (STAT1), which is an important player in mediating antiproliferative effects of IFNs.	Heparin	40-47	zinc ribbon domain containing 2	Homo sapiens	73-76
23110868-6	2013	In the second protocol, insulin was accompanied by Intralipid, which is mainly a mixture of triacylglycerols, and heparin, given as an activator of lipoprotein lipase, inducing insulin resistance.	Heparin	114-121	insulin	Homo sapiens	177-184
23864653-4	2013	To address some of this missing knowledge, we have characterized the structural basis of heparin binding to the murine CXCL1 dimer.	Heparin	89-96	chemokine (C-X-C motif) ligand 1	Mus musculus	119-124
23712256-7	2013	VEGF-A165 in the presence of heparin, was the most potent inducer of pHEndEC proliferation, angiogenesis, and wound healing in vitro.	Heparin	29-36	vascular endothelial growth factor A	Homo sapiens	0-4
23712256-8	2013	1.31 nM VEGF-A165 induced ~110 % increase in cell proliferation relative to basal conditions (~51 % without heparin).	Heparin	108-115	vascular endothelial growth factor A	Homo sapiens	8-14
23712256-12	2013	This study demonstrates that VEGF-A165, in the presence of heparin, is a potent inducer of pHEndEC proliferation, angiogenesis, and wound healing in vitro.	Heparin	59-66	vascular endothelial growth factor A	Homo sapiens	29-33
23874391-0	2013	Low molecular weight heparin relieves experimental colitis in mice by downregulating IL-1beta and inhibiting syndecan-1 shedding in the intestinal mucosa.	Heparin	21-28	interleukin 1 beta	Mus musculus	85-93
23801765-5	2013	Activation of heparin-binding EGF or Kit ligand 2 shedding by ADAM17 in iRhom2(-/-) mEFs can be rescued by wild-type iRhom2 but not by iRhom2 lacking its N-terminal cytoplasmic domain.	Heparin	14-21	a disintegrin and metallopeptidase domain 17	Mus musculus	62-68
23801765-5	2013	Activation of heparin-binding EGF or Kit ligand 2 shedding by ADAM17 in iRhom2(-/-) mEFs can be rescued by wild-type iRhom2 but not by iRhom2 lacking its N-terminal cytoplasmic domain.	Heparin	14-21	rhomboid 5 homolog 2	Mus musculus	72-78
23801765-5	2013	Activation of heparin-binding EGF or Kit ligand 2 shedding by ADAM17 in iRhom2(-/-) mEFs can be rescued by wild-type iRhom2 but not by iRhom2 lacking its N-terminal cytoplasmic domain.	Heparin	14-21	rhomboid 5 homolog 2	Mus musculus	117-123
23801765-5	2013	Activation of heparin-binding EGF or Kit ligand 2 shedding by ADAM17 in iRhom2(-/-) mEFs can be rescued by wild-type iRhom2 but not by iRhom2 lacking its N-terminal cytoplasmic domain.	Heparin	14-21	rhomboid 5 homolog 2	Mus musculus	117-123
23401334-4	2013	METHODS: Recombinant human estrogen receptor-alpha protein (rhERalpha) was expressed in Saccharomyces cervisiae as an ubiquitin fusion under control of a CUP1 promoter and partially purified with heparin affinity chromatography in the unliganded state.	Heparin	196-203	estrogen receptor 1	Homo sapiens	27-50
23974171-3	2013	For the dynamic control of the multivalent affinity binding between heparin and heparin-binding proteins, thermoresponsive cell culture surface modified with heparin, which interacts with heparin-binding proteins such as basic fibroblast growth factor (bFGF), has been proposed.	Heparin	68-75	fibroblast growth factor 2	Homo sapiens	221-251
23974171-3	2013	For the dynamic control of the multivalent affinity binding between heparin and heparin-binding proteins, thermoresponsive cell culture surface modified with heparin, which interacts with heparin-binding proteins such as basic fibroblast growth factor (bFGF), has been proposed.	Heparin	68-75	fibroblast growth factor 2	Homo sapiens	253-257
23974171-4	2013	Heparin-functionalized thermoresponsive cell culture surface induces (1) the multivalent affinity binding of bFGF in active form and (2) accelerating cell sheet formation in the state of shrunken PIPAAm chains at 37 C. By lowering temperature to 20 C, the affinity binding between bFGF and immobilized heparin is reduced with increasing the mobility of heparin and the swollen PIPAAm chains, leading to the detachment of cultured cells.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	109-113
23974171-4	2013	Heparin-functionalized thermoresponsive cell culture surface induces (1) the multivalent affinity binding of bFGF in active form and (2) accelerating cell sheet formation in the state of shrunken PIPAAm chains at 37 C. By lowering temperature to 20 C, the affinity binding between bFGF and immobilized heparin is reduced with increasing the mobility of heparin and the swollen PIPAAm chains, leading to the detachment of cultured cells.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	281-285
23974171-4	2013	Heparin-functionalized thermoresponsive cell culture surface induces (1) the multivalent affinity binding of bFGF in active form and (2) accelerating cell sheet formation in the state of shrunken PIPAAm chains at 37 C. By lowering temperature to 20 C, the affinity binding between bFGF and immobilized heparin is reduced with increasing the mobility of heparin and the swollen PIPAAm chains, leading to the detachment of cultured cells.	Heparin	302-309	fibroblast growth factor 2	Homo sapiens	109-113
23974171-4	2013	Heparin-functionalized thermoresponsive cell culture surface induces (1) the multivalent affinity binding of bFGF in active form and (2) accelerating cell sheet formation in the state of shrunken PIPAAm chains at 37 C. By lowering temperature to 20 C, the affinity binding between bFGF and immobilized heparin is reduced with increasing the mobility of heparin and the swollen PIPAAm chains, leading to the detachment of cultured cells.	Heparin	353-360	fibroblast growth factor 2	Homo sapiens	109-113
23974171-6	2013	A cell cultivation system using heparin-functionalized thermoresponsive cell culture surface is versatile for immobilizing other heparin-binding proteins such as vascular endothelial growth factor, fibronectin, antithrombin III, and hepatocyte growth factor, etc.	Heparin	32-39	vascular endothelial growth factor A	Homo sapiens	162-196
23974171-6	2013	A cell cultivation system using heparin-functionalized thermoresponsive cell culture surface is versatile for immobilizing other heparin-binding proteins such as vascular endothelial growth factor, fibronectin, antithrombin III, and hepatocyte growth factor, etc.	Heparin	32-39	fibronectin 1	Homo sapiens	198-209
23734709-2	2013	To understand the forces that drive such interactions the binding of heparin to interferon-gamma (IFNgamma), used as a model system, was investigated.	Heparin	69-76	interferon gamma	Homo sapiens	80-96
23734709-2	2013	To understand the forces that drive such interactions the binding of heparin to interferon-gamma (IFNgamma), used as a model system, was investigated.	Heparin	69-76	interferon gamma	Homo sapiens	98-106
23179258-6	2013	When heparin was administered concurrently with steroid, psychiatric events developed less frequently either in all of the patients (2/17 vs. 11/28, p = 0.048) or in patients positive for the anti-SS-A antibody (2/15 vs. 7/14, p = 0.041).	Heparin	5-12	tripartite motif containing 21	Homo sapiens	197-201
28510155-0	2013	A historical perspective of the biophysics of the thrombin-heparin system: an example of nonspecific binding and the consequent parking problem in action.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	50-58
28510155-4	2013	Results for the thrombin-heparin interaction have been used to illustrate a thermodynamic characterization of nonspecific binding that takes into account these consequences of the parking problem.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	16-24
22915548-10	2013	CONCLUSIONS: Thrombin generation was enhanced in patients who did not receive UFH, which may increase the risk of thrombotic complications.	Heparin	78-81	coagulation factor II, thrombin	Homo sapiens	13-21
22915548-12	2013	UFH prevented an increase in prothrombin to thrombin conversion, resulting in unaltered fibrin formation.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	32-40
23494053-0	2013	Transient heparin-induced platelet activation linked to generation of platelet 12-lipoxygenase.	Heparin	10-17	arachidonate 15-lipoxygenase	Homo sapiens	79-94
23571852-0	2013	Perturbation of the heparin/heparin-sulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3K/Akt and MAPK/ERK signalling.	Heparin	20-27	AKT serine/threonine kinase 1	Homo sapiens	141-144
23571852-0	2013	Perturbation of the heparin/heparin-sulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3K/Akt and MAPK/ERK signalling.	Heparin	20-27	mitogen-activated protein kinase 1	Homo sapiens	154-157
23571852-0	2013	Perturbation of the heparin/heparin-sulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3K/Akt and MAPK/ERK signalling.	Heparin	28-35	AKT serine/threonine kinase 1	Homo sapiens	141-144
23571852-0	2013	Perturbation of the heparin/heparin-sulfate interactome of human breast cancer cells modulates pro-tumourigenic effects associated with PI3K/Akt and MAPK/ERK signalling.	Heparin	28-35	mitogen-activated protein kinase 1	Homo sapiens	154-157
22358112-7	2013	Remarkably lower level of TNF-alpha (P = 0.003) and ICAM-1 (P = 0.006) was detected in HA-treated rats compared with heparin-treated rats.	Heparin	117-124	tumor necrosis factor	Rattus norvegicus	26-35
23603906-0	2013	The choline-binding protein PspC of Streptococcus pneumoniae interacts with the C-terminal heparin-binding domain of vitronectin.	Heparin	91-98	surfactant protein C	Homo sapiens	28-32
23603906-3	2013	In this study, we identified PspC as a vitronectin-binding protein interacting with the C-terminal heparin-binding domain of vitronectin.	Heparin	99-106	surfactant protein C	Homo sapiens	29-33
23478040-6	2013	Heparin coupled nanoceria were found to be biologically active due to their ability to bind fibroblast growth factor 2 and signal through FGF receptor 1.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	92-118
23494053-9	2013	Heparin administration during CEA generates AA that is metabolised to 12-HETE via the 12-LOX pathway, possibly explaining the phenomenon of transient heparin-induced platelet activation.	Heparin	0-7	arachidonate 15-lipoxygenase	Homo sapiens	86-92
23494053-9	2013	Heparin administration during CEA generates AA that is metabolised to 12-HETE via the 12-LOX pathway, possibly explaining the phenomenon of transient heparin-induced platelet activation.	Heparin	150-157	arachidonate 15-lipoxygenase	Homo sapiens	86-92
23571852-8	2013	The modulatory effect of heparin on HS-associated activity was confirmed with one example of heparin/HS interactomes, transforming growth factor beta (TGFbeta).	Heparin	25-32	transforming growth factor beta 1	Homo sapiens	118-149
23571852-8	2013	The modulatory effect of heparin on HS-associated activity was confirmed with one example of heparin/HS interactomes, transforming growth factor beta (TGFbeta).	Heparin	25-32	transforming growth factor beta 1	Homo sapiens	151-158
23571852-9	2013	The innate TGFbeta activity of MCF-7 cells was reduced by heparin treatment, with specific interruption of the TGFbeta-Smad signalling pathway.	Heparin	58-65	transforming growth factor beta 1	Homo sapiens	11-18
23673387-0	2013	Impact of antithrombin deficiency on efficacy of edoxaban and antithrombin-dependent anticoagulants, fondaparinux, enoxaparin, and heparin.	Heparin	131-138	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	10-22
23734081-5	2013	The effect of the vitreal HS level on the binding of exogenous VEGF to surface-bound heparin was determined in vitro.	Heparin	85-92	vascular endothelial growth factor A	Homo sapiens	63-67
22210807-6	2013	Perfusion of the surfaces with human platelet-rich plasma showed that the immobilized heparin surfaces also reduce both dynamic thrombin levels in the circulating plasma and residual thrombin generated at the material surface.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	128-136
23410540-1	2013	AIMS: Within a clinical trial population, direct thrombin inhibition using bivalirudin in patients undergoing primary percutaneous coronary intervention (PCI) for ST-elevation myocardial infarction (STEMI) is associated with a reduction in mortality and major bleeding compared to heparin/glycoprotein IIb/IIIa receptor inhibition (GPI), but a higher incidence of acute stent thrombosis (ST), particularly in the absence of pre-procedural heparin.	Heparin	281-288	coagulation factor II, thrombin	Homo sapiens	49-57
23053899-3	2013	SULF1 is a heparin-degrading endosulfatase which can modulate the sulfation of HSPGs.	Heparin	11-18	sulfatase 1	Homo sapiens	0-5
22210807-6	2013	Perfusion of the surfaces with human platelet-rich plasma showed that the immobilized heparin surfaces also reduce both dynamic thrombin levels in the circulating plasma and residual thrombin generated at the material surface.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	183-191
23637968-4	2013	Our group has shown that the heparin-binding fibronectin type III domains of fibronectin (FNIII), specifically FNIII12-14, possess affinity towards a large number of growth factors.	Heparin	29-36	fibronectin 1	Homo sapiens	45-56
22223475-6	2013	We found that EPC adhesion and spreading on CD34 Ab-immobilized HA-heparin hydrogels was significantly higher than their non-modified analogues.	Heparin	67-74	CD34 molecule	Homo sapiens	44-48
22223475-7	2013	Once adhered, EPCs spread and formed an endothelial layer on both non-modified and CD34 Ab-modified HA-heparin hydrogels after 3 days of culture.	Heparin	103-110	CD34 molecule	Homo sapiens	83-87
23549826-5	2013	After heparin reversal, however, significantly higher fibrinogen levels and less reduced ROTEM parameters, which reflect clot formation and firmness, were demonstrated in the treatment groups of infants and children.	Heparin	6-13	fibrinogen beta chain	Homo sapiens	54-64
23637968-4	2013	Our group has shown that the heparin-binding fibronectin type III domains of fibronectin (FNIII), specifically FNIII12-14, possess affinity towards a large number of growth factors.	Heparin	29-36	fibronectin 1	Homo sapiens	77-88
23211566-0	2013	Heparin inhibits TNF-alpha signaling in human endometrial stromal cells by interaction with NF-kappaB.	Heparin	0-7	tumor necrosis factor	Homo sapiens	17-26
22886070-1	2013	Recently, we demonstrated that the human xylosyltransferase II (XT-II) has enzymatic activity and is able to catalyze the initial and rate-limiting step in the biosynthesis of glycosaminoglycans (GAGs) like chondroitin and dermatan sulfate, as well as heparan sulfate and heparin.	Heparin	272-279	xylosyltransferase 2	Homo sapiens	41-62
22886070-1	2013	Recently, we demonstrated that the human xylosyltransferase II (XT-II) has enzymatic activity and is able to catalyze the initial and rate-limiting step in the biosynthesis of glycosaminoglycans (GAGs) like chondroitin and dermatan sulfate, as well as heparan sulfate and heparin.	Heparin	272-279	xylosyltransferase 2	Homo sapiens	64-69
23601319-0	2013	Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes.	Heparin	12-19	fibroblast growth factor 1	Homo sapiens	48-74
23601319-0	2013	Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes.	Heparin	12-19	fibroblast growth factor 1	Homo sapiens	76-80
23601319-3	2013	Heparin fragments of defined length are used as chemical analogs of the sulfated domains of heparan sulfate and examined for their ability to oligomerize FGF1.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	154-158
23601319-7	2013	The thermodynamics and stoichiometry of the ternary complex suggest that in solution FGF1 binds to heparin in a trans-dimeric manner before FGFR recruitment.	Heparin	99-106	fibroblast growth factor 1	Homo sapiens	85-89
23482736-1	2013	OBJECTIVE: To report a case of heparin-induced thrombocytopenia (HIT) in a patient with concurrent liver dysfunction and a prolonged baseline activated partial thromboplastin time (aPTT) in whom argatroban therapy was monitored with aPTT and a novel plasma-diluted thrombin assay.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	265-273
23348428-0	2013	Differential profiles of thrombin inhibitors (heparin, hirudin, bivalirudin, and dabigatran) in the thrombin generation assay and thromboelastography in vitro.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	25-33
23348428-0	2013	Differential profiles of thrombin inhibitors (heparin, hirudin, bivalirudin, and dabigatran) in the thrombin generation assay and thromboelastography in vitro.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	100-108
23211566-0	2013	Heparin inhibits TNF-alpha signaling in human endometrial stromal cells by interaction with NF-kappaB.	Heparin	0-7	nuclear factor kappa B subunit 1	Homo sapiens	92-101
23211566-3	2013	Therefore, we examined the impact of heparin on TNF-alpha signaling in human endometrial stromal cells (ESCs) in vitro.	Heparin	37-44	tumor necrosis factor	Homo sapiens	48-57
23211566-10	2013	Unfractionated heparin significantly suppressed the TNF-alpha-induced and NF-kappaB-mediated secretion and expression of IL-8 and -6 as well as other molecules in decidualized and undifferentiated human ESCs.	Heparin	15-22	tumor necrosis factor	Homo sapiens	52-61
23211566-10	2013	Unfractionated heparin significantly suppressed the TNF-alpha-induced and NF-kappaB-mediated secretion and expression of IL-8 and -6 as well as other molecules in decidualized and undifferentiated human ESCs.	Heparin	15-22	nuclear factor kappa B subunit 1	Homo sapiens	74-83
23211566-10	2013	Unfractionated heparin significantly suppressed the TNF-alpha-induced and NF-kappaB-mediated secretion and expression of IL-8 and -6 as well as other molecules in decidualized and undifferentiated human ESCs.	Heparin	15-22	C-X-C motif chemokine ligand 8	Homo sapiens	121-132
23211566-11	2013	Thereby heparin had no influence on the degradation of IkappaBalpha and the phosphorylation of NF-kappaB, but it inhibited the activity of NF-kappaB in the nucleus.	Heparin	8-15	nuclear factor kappa B subunit 1	Homo sapiens	139-148
23211566-13	2013	Unfractionated heparin is able to inhibit TNF-alpha/NF-kappaB-mediated inflammatory effects in the human endometrium independently of its classical function as an anticoagulant.	Heparin	15-22	tumor necrosis factor	Homo sapiens	42-51
23211566-13	2013	Unfractionated heparin is able to inhibit TNF-alpha/NF-kappaB-mediated inflammatory effects in the human endometrium independently of its classical function as an anticoagulant.	Heparin	15-22	nuclear factor kappa B subunit 1	Homo sapiens	52-61
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	167-174	fibroblast growth factor 2	Homo sapiens	73-77
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	167-174	fibroblast growth factor 2	Homo sapiens	79-109
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	167-174	vascular endothelial growth factor A	Homo sapiens	115-119
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	314-321	fibroblast growth factor 2	Homo sapiens	73-77
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	314-321	vascular endothelial growth factor A	Homo sapiens	115-119
23357298-6	2013	Enhanced secretion of anosmin-1 in the presence of TGF-beta and heparin was also observed in other ocular cells such as corneal epithelial and corneal fibroblast cultures.	Heparin	64-71	anosmin 1	Homo sapiens	22-31
23268358-0	2013	Heparin inhibits angiotensin II-induced vasoconstriction on isolated mouse mesenteric resistance arteries through Rho-A- and PKA-dependent pathways.	Heparin	0-7	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	17-31
23268358-3	2013	However, the mechanisms by which heparin modulates vascular reactivity of Ang II remain unclear.	Heparin	33-40	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	74-80
23268358-4	2013	We hypothesized that heparin may offset Ang II-induced vasoconstriction on mesenteric resistance arteries through modulating the Rho-A/Rho kinase pathway.	Heparin	21-28	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	40-46
23268358-7	2013	We found that heparin significantly attenuated vasoconstriction induced by Ang II but not that by KCl.	Heparin	14-21	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	75-81
23268358-9	2013	Ang II stimulated Rho-A activation and myosin light chain phosphorylation, both responses were antagonized by heparin.	Heparin	110-117	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	0-6
23268358-10	2013	Moreover, the inhibitory effect of heparin on Ang II-induced vasoconstriction was reversed by Rp-cAMPS (cAMP-dependent PKA inhibitor), blunted by ODQ (soluble guanylate cyclase inhibitor), and mimicked by a cell-permeable cGMP analogue, 8-Br-cGMP, but not by a cAMP analogue.	Heparin	35-42	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	46-52
23268358-12	2013	We conclude that heparin inhibits Ang II-induced vasoconstriction through Rho-A/Rho kinase- and cGMP/PKA-dependent pathways.	Heparin	17-24	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	34-40
23268358-12	2013	We conclude that heparin inhibits Ang II-induced vasoconstriction through Rho-A/Rho kinase- and cGMP/PKA-dependent pathways.	Heparin	17-24	Rho-associated coiled-coil containing protein kinase 2	Mus musculus	80-100
23445515-6	2013	The ratio of the current decrease shows a linear relationship with heparin concentration with a concentration range from 0.5 to 10 muM.	Heparin	67-74	latexin	Homo sapiens	131-134
23274362-3	2013	The obtained heparin sensor shows high-selectivity monitoring of heparin, shorter response time (&lt;4 min), wider linear range (0.003-0.7 muM), lower detection limit (0.001 muM), and satisfactory long-term stability (&gt;2 months).	Heparin	13-20	latexin	Homo sapiens	139-142
23274362-3	2013	The obtained heparin sensor shows high-selectivity monitoring of heparin, shorter response time (&lt;4 min), wider linear range (0.003-0.7 muM), lower detection limit (0.001 muM), and satisfactory long-term stability (&gt;2 months).	Heparin	13-20	latexin	Homo sapiens	174-177
23598032-1	2013	Heparin, a highly sulfated polydispersed glycosaminoglycan (GAG), is the most widespread clinical anticoagulant; it binds antithrombin III (AT), a member of serine proteinases superfamily, accelerating its antagonist effect on blood coagulation.	Heparin	0-7	serpin family C member 1	Bos taurus	122-138
23755647-7	2013	Interestingly, prolonged prothrombin time, thrombin time, and activated partial thromboplastin time were observed in the heparin-reduced gold nanoparticles when compared to a control heparin, suggesting the enhancement of anticoagulant activity in heparin-reduced gold nanoparticles.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	28-36
23338621-0	2013	Recombinant hemangiopoietin promotes cell adhesion and binds heparin             in its multimeric form.	Heparin	61-68	proteoglycan 4	Homo sapiens	12-27
23307015-0	2013	Exogenous heparin binds and inhibits bone morphogenetic protein 6 biological activity.	Heparin	10-17	bone morphogenetic protein 6	Rattus norvegicus	37-65
23307015-1	2013	PURPOSE: The purpose of this study was to explore the effect of heparin on bone morphogenetic protein 6 (BMP6) osteogenic activity.	Heparin	64-71	bone morphogenetic protein 6	Rattus norvegicus	75-103
23307015-1	2013	PURPOSE: The purpose of this study was to explore the effect of heparin on bone morphogenetic protein 6 (BMP6) osteogenic activity.	Heparin	64-71	bone morphogenetic protein 6	Rattus norvegicus	105-109
23307015-2	2013	METHODS: Western blot analysis was used to confirm the binding of BMP6 to heparin and to observe its effect on BMP6 signaling in C2C12-BRE-Luc myoblasts.	Heparin	74-81	bone morphogenetic protein 6	Rattus norvegicus	66-70
23307015-3	2013	Real-time RT-PCR was performed for the expression analysis of alkaline phosphatase (ALP) and osteocalcin (OC) in C2C12 myoblasts treated with BMP6 and heparin for 72 hours.	Heparin	151-158	bone gamma-carboxyglutamate protein	Rattus norvegicus	93-104
23307015-3	2013	Real-time RT-PCR was performed for the expression analysis of alkaline phosphatase (ALP) and osteocalcin (OC) in C2C12 myoblasts treated with BMP6 and heparin for 72 hours.	Heparin	151-158	bone gamma-carboxyglutamate protein	Rattus norvegicus	106-108
23307015-4	2013	Rat ectopic bone formation assay was performed to explore the effect of heparin on BMP6 osteogenic activity.	Heparin	72-79	bone morphogenetic protein 6	Rattus norvegicus	83-87
23307015-8	2013	RESULTS: BMP6 specifically bound to heparin and induced Smad1/5/8 phosphorylation which was inhibited by heparin.	Heparin	36-43	bone morphogenetic protein 6	Rattus norvegicus	9-13
23307015-8	2013	RESULTS: BMP6 specifically bound to heparin and induced Smad1/5/8 phosphorylation which was inhibited by heparin.	Heparin	105-112	bone morphogenetic protein 6	Rattus norvegicus	9-13
23307015-10	2013	Heparin dose dependently inhibited BMP6-induced new bone and cartilage formation in the rat ectopic bone formation assay, while in osteoporotic mice heparin inhibited the BMP6 potential to improve the bone quality as evidenced by decreased bone mineral density and trabecular bone parameters.	Heparin	0-7	bone morphogenetic protein 6	Rattus norvegicus	35-39
23307015-11	2013	Interestingly, BMP6 prevented the effect of heparin on the blood coagulation parameters.	Heparin	44-51	bone morphogenetic protein 6	Rattus norvegicus	15-19
23307015-12	2013	CONCLUSION: The interaction of BMP6 with heparin might contribute to the heparin-induced osteoporosis and blood coagulation.	Heparin	41-48	bone morphogenetic protein 6	Rattus norvegicus	31-35
23307015-12	2013	CONCLUSION: The interaction of BMP6 with heparin might contribute to the heparin-induced osteoporosis and blood coagulation.	Heparin	73-80	bone morphogenetic protein 6	Rattus norvegicus	31-35
23422564-0	2013	A heparin-mimicking polymer conjugate stabilizes basic fibroblast growth factor.	Heparin	2-9	fibroblast growth factor 2	Homo sapiens	49-79
23422564-3	2013	Here, we describe the stabilization of bFGF by covalent conjugation with a heparin-mimicking polymer, a copolymer consisting of styrene sulfonate units and methyl methacrylate units bearing poly(ethylene glycol) side chains.	Heparin	75-82	fibroblast growth factor 2	Homo sapiens	39-43
22687193-6	2013	RESULTS: Q40P/S47I/H93G could activate all subtypes of FGF receptors in vitro much more strongly than the wild-type without endogenous or exogenous heparin.	Heparin	148-155	fibroblast growth factor 1	Homo sapiens	55-58
23408233-3	2013	Current anticoagulant therapy includes the use of indirect thrombin inhibitors (e.g., heparins, low-molecular-weight-heparins) and vitamin K antagonists such as warfarin.	Heparin	86-94	coagulation factor II, thrombin	Homo sapiens	59-67
23408233-3	2013	Current anticoagulant therapy includes the use of indirect thrombin inhibitors (e.g., heparins, low-molecular-weight-heparins) and vitamin K antagonists such as warfarin.	Heparin	117-125	coagulation factor II, thrombin	Homo sapiens	59-67
23074088-6	2013	Here, the ability to resolve sub-molecular binding specificity between sulfate and carboxyl groups of dopants and heparin binding domains of human plasma fibronectin is demonstrated.	Heparin	114-121	fibronectin 1	Homo sapiens	154-165
23228448-4	2013	This indicates binding of foscarnet at the heparin-binding domain of FGF2.	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	69-73
23292752-12	2013	Dabigatran has an advantage over the indirect thrombin inhibitors, unfractionated heparin and low-molecular-weight heparin, in that it inhibits free and fibrin-bound thrombin.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	166-174
22687193-9	2013	The level of stability of FGF1 mutants correlated with their mitogenic activities in vitro in the absence of heparin; however, preirradiation treatment with the mutants increased the crypt number to almost the same level as Q40P/S47I/H93G.	Heparin	109-116	fibroblast growth factor 1	Homo sapiens	26-30
23284011-7	2013	Concomitant Intralipid/heparin infusion, which caused a reduction of insulin sensitivity by 40% (P &lt; .0001), resulted in a marked increase in serum visfatin (P &lt; .0001), which was already observed after 2 hours of FFAs increase (P &lt; .0001).	Heparin	23-30	insulin	Homo sapiens	69-76
23020251-5	2013	We previously developed biomimetics of ECM fibronectin by directly coupling the heparin-binding fragment of the first type III repeat of fibronectin (FNIII1H) to the integrin-binding repeats (FNIII8-10).	Heparin	80-87	fibronectin 1	Homo sapiens	43-54
23135410-0	2013	Evaluation of collagen/heparin coated TCP/HA granules for long-term delivery of BMP-2.	Heparin	23-30	serine peptidase inhibitor Kazal type 1	Homo sapiens	38-41
23135410-4	2013	We covalently attached heparin to a cross-linked collagen type I coated tricalciumphosphate/hydroxyapatite (TCP/HA) bone substitute and subsequently loaded it with BMP-2.	Heparin	23-30	serine peptidase inhibitor Kazal type 1	Homo sapiens	108-111
23020251-5	2013	We previously developed biomimetics of ECM fibronectin by directly coupling the heparin-binding fragment of the first type III repeat of fibronectin (FNIII1H) to the integrin-binding repeats (FNIII8-10).	Heparin	80-87	fibronectin 1	Homo sapiens	137-148
23200896-5	2013	Melagatran, heparin, and enoxaparin all inhibited thrombin-induced platelet aggregation at clinically relevant concentrations.	Heparin	12-19	coagulation factor II	Rattus norvegicus	50-58
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-81	family with sequence similarity 72 member B	Homo sapiens	18-21
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-81	family with sequence similarity 72 member B	Homo sapiens	227-230
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-81	family with sequence similarity 72 member B	Homo sapiens	227-230
23166320-0	2013	Molecular interaction studies of HIV-1 matrix protein p17 and heparin: identification of the heparin-binding motif of p17 as a target for the development of multitarget antagonists.	Heparin	62-69	family with sequence similarity 72 member B	Homo sapiens	118-121
23166320-2	2013	By exploiting an approach integrating computational modeling, site-directed mutagenesis of p17, chemical desulfation of heparin, and surface plasmon resonance, we characterized the interaction of p17 with heparin, a HSPG structural analog, and CXCR1.	Heparin	120-127	family with sequence similarity 72 member B	Homo sapiens	196-199
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-80	family with sequence similarity 72 member B	Homo sapiens	18-21
23166320-2	2013	By exploiting an approach integrating computational modeling, site-directed mutagenesis of p17, chemical desulfation of heparin, and surface plasmon resonance, we characterized the interaction of p17 with heparin, a HSPG structural analog, and CXCR1.	Heparin	205-212	family with sequence similarity 72 member B	Homo sapiens	196-199
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-80	family with sequence similarity 72 member B	Homo sapiens	227-230
23166320-3	2013	p17 binds to heparin with an affinity (K(d) = 190 nm) that is similar to those of other heparin-binding viral proteins.	Heparin	13-20	family with sequence similarity 72 member B	Homo sapiens	0-3
23166320-5	2013	Neutralization (Arg Ala substitution) of the N-terminal, but not of the C-terminal basic motif, causes the loss of p17 heparin-binding capacity.	Heparin	119-126	family with sequence similarity 72 member B	Homo sapiens	115-118
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-80	family with sequence similarity 72 member B	Homo sapiens	227-230
23166320-6	2013	The N-terminal heparin-binding motif of p17 partially overlaps the CXCR1-binding domain.	Heparin	15-22	family with sequence similarity 72 member B	Homo sapiens	40-43
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	239-246	family with sequence similarity 72 member B	Homo sapiens	18-21
23166320-8	2013	Competition experiments demonstrated that free heparin and heparan sulfate (HS), but not selectively 2-O-, 6-O-, and N-O desulfated heparins, prevent p17 binding to substrate-immobilized heparin, indicating that the sulfate groups of the glycosaminoglycan mediate p17 interaction.	Heparin	47-54	family with sequence similarity 72 member B	Homo sapiens	150-153
23166320-8	2013	Competition experiments demonstrated that free heparin and heparan sulfate (HS), but not selectively 2-O-, 6-O-, and N-O desulfated heparins, prevent p17 binding to substrate-immobilized heparin, indicating that the sulfate groups of the glycosaminoglycan mediate p17 interaction.	Heparin	47-54	family with sequence similarity 72 member B	Homo sapiens	264-267
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	239-246	family with sequence similarity 72 member B	Homo sapiens	227-230
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	239-246	family with sequence similarity 72 member B	Homo sapiens	227-230
23166320-10	2013	Here, we characterized at a molecular level the interaction of p17 with its cellular receptors, laying the basis for the development of heparin-mimicking p17 antagonists.	Heparin	136-143	family with sequence similarity 72 member B	Homo sapiens	63-66
23166320-10	2013	Here, we characterized at a molecular level the interaction of p17 with its cellular receptors, laying the basis for the development of heparin-mimicking p17 antagonists.	Heparin	136-143	family with sequence similarity 72 member B	Homo sapiens	154-157
23172228-1	2013	Chondroadherin, a leucine-rich repeat family member, contains a very C-terminal sequence CKFPTKRSKKAGRH(359), now shown to bind to heparin with a K(D) of 13 mum.	Heparin	131-138	chondroadherin	Homo sapiens	0-14
23172228-2	2013	This observation led us to investigate whether chondroadherin interacts via this C-terminal heparin-binding domain with glycosaminoglycan chains of proteoglycans at the cell surface.	Heparin	92-99	chondroadherin	Homo sapiens	47-61
23273505-3	2013	Measurement of thrombin time reflects the anti-IIa effect of heparin and has to be monitored immediately and 1hour after the injection of protamine.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	15-23
24151519-6	2013	Heparin treatment of B/W mice reduced the in vivo expression of CCR2, IL1 beta , and TLR7 compared to untreated B/W mice.	Heparin	0-7	interleukin 1 beta	Mus musculus	70-78
23690810-0	2013	Dabigatran, a direct thrombin inhibitor, can be a life-saving treatment in heparin-induced thrombocytopenia.	Heparin	75-82	coagulation factor II, thrombin	Homo sapiens	21-29
22753043-1	2013	Our aim was to synthesize a biomaterial that stimulates angiogenesis for tissue engineering applications by exploiting the ability of heparin to bind and release vascular endothelial growth factor (VEGF).	Heparin	134-141	vascular endothelial growth factor A	Homo sapiens	162-196
22753043-1	2013	Our aim was to synthesize a biomaterial that stimulates angiogenesis for tissue engineering applications by exploiting the ability of heparin to bind and release vascular endothelial growth factor (VEGF).	Heparin	134-141	vascular endothelial growth factor A	Homo sapiens	198-202
23160925-0	2013	Heparins modulate the IFN-gamma-induced production of chemokines in human breast cancer cells.	Heparin	0-8	interferon gamma	Homo sapiens	22-31
23160925-4	2013	We therefore wanted to test whether heparins have an impact on the chemokines CXCL9 and CXCL10 as well as the IFN-gamma signalling in human breast cancer cells in vitro.	Heparin	36-44	C-X-C motif chemokine ligand 9	Homo sapiens	78-83
23160925-8	2013	UFH dose dependently inhibited the effect of IFN-gamma on the secretion and expression of CXCL9 and CXCL10.	Heparin	0-3	interferon gamma	Homo sapiens	45-54
23160925-8	2013	UFH dose dependently inhibited the effect of IFN-gamma on the secretion and expression of CXCL9 and CXCL10.	Heparin	0-3	C-X-C motif chemokine ligand 9	Homo sapiens	90-95
23160925-9	2013	LMWHs and heparin-related compounds differentially modulated IFN-gamma-effects-the results depended on their molecular size and charge, but were independent of their anticoagulatory properties.	Heparin	10-17	interferon gamma	Homo sapiens	61-70
23160925-10	2013	As a reason for these heparin effects, we could show that the IFN-gamma-induced phosphorylation of STAT1 was modulated by heparins, caused by an interaction with the cellular binding of IFN-gamma.	Heparin	22-29	interferon gamma	Homo sapiens	62-71
23160925-10	2013	As a reason for these heparin effects, we could show that the IFN-gamma-induced phosphorylation of STAT1 was modulated by heparins, caused by an interaction with the cellular binding of IFN-gamma.	Heparin	22-29	interferon gamma	Homo sapiens	186-195
23160925-10	2013	As a reason for these heparin effects, we could show that the IFN-gamma-induced phosphorylation of STAT1 was modulated by heparins, caused by an interaction with the cellular binding of IFN-gamma.	Heparin	122-130	interferon gamma	Homo sapiens	62-71
23160925-10	2013	As a reason for these heparin effects, we could show that the IFN-gamma-induced phosphorylation of STAT1 was modulated by heparins, caused by an interaction with the cellular binding of IFN-gamma.	Heparin	122-130	interferon gamma	Homo sapiens	186-195
26012208-10	2013	They interact with heparin but have a different binding domain from that of VEGF-A.	Heparin	19-26	vascular endothelial growth factor A	Homo sapiens	76-82
23069711-8	2013	POC-Heparin supported EC and BOEC adhesion, viability, proliferation, NO production, and expression of endothelial cell-specific markers von Willebrand factor (vWF) and vascular endothelial-cadherin (VE-cadherin).	Heparin	4-11	von Willebrand factor	Homo sapiens	160-163
23069711-8	2013	POC-Heparin supported EC and BOEC adhesion, viability, proliferation, NO production, and expression of endothelial cell-specific markers von Willebrand factor (vWF) and vascular endothelial-cadherin (VE-cadherin).	Heparin	4-11	cadherin 5	Homo sapiens	169-198
23069711-8	2013	POC-Heparin supported EC and BOEC adhesion, viability, proliferation, NO production, and expression of endothelial cell-specific markers von Willebrand factor (vWF) and vascular endothelial-cadherin (VE-cadherin).	Heparin	4-11	cadherin 5	Homo sapiens	200-211
23565598-7	2013	The amount of bFGF was increased according to the presence of heparin within the hydrogel, but the amount of released bFGF was decreased by increasing the content of COS.	Heparin	62-69	fibroblast growth factor 2	Homo sapiens	14-18
23907946-10	2013	Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis.	Heparin	14-21	von Willebrand factor	Homo sapiens	94-97
23907946-10	2013	Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis.	Heparin	31-34	von Willebrand factor	Homo sapiens	94-97
22936459-2	2013	Treatment with the anticoagulant heparin protects against hepatitis, despite healthy production of IFN-gamma and TNF.	Heparin	33-40	interferon gamma	Mus musculus	99-108
22936459-2	2013	Treatment with the anticoagulant heparin protects against hepatitis, despite healthy production of IFN-gamma and TNF.	Heparin	33-40	tumor necrosis factor	Mus musculus	113-116
23061730-9	2013	Heparin has been proposed as a treatment for senile dementia and exhibits anti-inflammatory action as well as inhibitory effects on Abeta assembly.	Heparin	0-7	amyloid beta precursor protein	Homo sapiens	132-137
23565598-8	2013	The hydrogel containing bFGF with heparin showed higher proliferation of cells compared to the hydrogel without heparin at 20% COS.	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	24-28
23546710-1	2013	Thrombin clotting time (TCT) is a coagulation assay used to diagnose congenital and acquired fibrinogen deficiency (Adcock et al., Coagulation handbook, Esoterix Coagulation, Austin, TX, 2002), as well as to identify contamination by heparin, prior to performing additional coagulation assays.	Heparin	234-241	coagulation factor II, thrombin	Homo sapiens	0-8
23868446-2	2013	Here we show that a blood coagulation-responsive hydrogel system can deliver heparin in amounts triggered by the environmental levels of thrombin, the key enzyme of the coagulation cascade, which--in turn--becomes inactivated due to released heparin.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	137-145
23868446-2	2013	Here we show that a blood coagulation-responsive hydrogel system can deliver heparin in amounts triggered by the environmental levels of thrombin, the key enzyme of the coagulation cascade, which--in turn--becomes inactivated due to released heparin.	Heparin	242-249	coagulation factor II, thrombin	Homo sapiens	137-145
23409021-1	2013	We report a method for production of soluble heparin binding domain (HBD) of human vascular endothelial growth factor VEGF-A165.	Heparin	45-52	vascular endothelial growth factor A	Homo sapiens	83-117
24247664-0	2013	Heparin inhibits activation of latent transforming growth factor-beta1.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	38-70
24247664-13	2013	CONCLUSION: The findings suggest that heparin renders LTGF-beta1 resistant to activation, possibly by binding simultaneously to TGF-beta1 and LAP.	Heparin	38-45	transforming growth factor beta 1	Homo sapiens	55-64
24247664-13	2013	CONCLUSION: The findings suggest that heparin renders LTGF-beta1 resistant to activation, possibly by binding simultaneously to TGF-beta1 and LAP.	Heparin	38-45	transforming growth factor beta 1	Homo sapiens	142-145
23883774-3	2013	In vitro analysis also revealed the tight binding of ArsA to heparin.	Heparin	61-68	arylsulfatase A	Mus musculus	53-57
24145081-11	2013	RESULTS: "Washed blood" anticoagulated with low molecular weight heparin demonstrated the best discrimination between circulating (resting) platelets and upon their in vitro response to thrombin, collagen or ADP in freshly-stained unfixed cell suspensions.	Heparin	65-72	coagulation factor II	Mus musculus	186-194
22750107-5	2012	In addition, a higher grafting concentration of heparin yielded a weaker expression of stage-specific embryonic antigen 1 in constructs, indicating that the grafted heparin accelerated differentiation and reduced the number of phenotypic iPS cells after cultivation.	Heparin	48-55	fucosyltransferase 4	Homo sapiens	87-121
23010574-3	2012	In this study, we show the structural correlation of LHT7, a previously developed heparin-based angiogenesis inhibitor, with its influence on VEGF blockade and its decreased anticoagulant activity.	Heparin	82-89	vascular endothelial growth factor A	Homo sapiens	142-146
23341879-3	2013	In this study, we investigated the binding affinity of a previously selected 26-mer DNA aptamer sequence (SL(2)-B) against heparin binding domain (HBD) of VEGF(165) protein.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	155-159
23359625-9	2013	In vitro biological tests demonstrated that EPCs achieved better adhesion, proliferation and migration on the coatings with Heparin-VEGF multilayer film.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	132-136
23494756-1	2012	AIM: To evaluate the effect of chronic thrombin inhibition by heparin on experimentally induced chronic liver injury (liver fibrosis) in rats.	Heparin	62-69	coagulation factor II	Rattus norvegicus	39-47
23494756-3	2012	Intravenous administration of the thrombin antagonist (heparin) started 1 wk after the start of CCl4 intoxication for 6 wk.	Heparin	55-62	coagulation factor II	Rattus norvegicus	34-42
23494756-9	2012	CONCLUSION: Heparin, a thrombin antagonist, preserved hepatic function and reduced severity of hepatic dysfunction/fibrogenesis.	Heparin	12-19	coagulation factor II	Rattus norvegicus	23-31
23667909-1	2012	Mast cell (MC) granules contain large amounts of proteases of the chymase, tryptase and carboxypeptidase A (MC-CPA) type that are stored in complex with serglycin,a proteoglycan with heparin side chains.	Heparin	183-190	carboxypeptidase A3	Homo sapiens	108-114
23667909-4	2012	Indeed, we found that wild-type MCs efficiently degraded exogenous or endogenously produced IL-13 upon degranulation,whereas serglycin -/- MCs completely lacked this ability.Moreover, MC-mediated IL-13 degradation was blocked both by a serine protease inhibitor and by a heparin antagonist,which suggests that IL-13 degradation is catalyzed by serglycin-dependent serine proteases and that optimal IL-13 degradation is dependent on both the serglycin and the protease component of the serglycin-protease complex.Moreover, IL-13 degradation was abrogated in MC-CPA -/-MC cultures, but was normal in cultures of MCs with an inactivating mutation of MC-CPA, which suggests that the IL-13-degrading serine proteases rely on MC-CPA protein.Together, our data implicate a serglycin-serine protease axis in the regulation of extracellular levels of IL-13.	Heparin	271-278	interleukin 13	Homo sapiens	196-201
23667909-4	2012	Indeed, we found that wild-type MCs efficiently degraded exogenous or endogenously produced IL-13 upon degranulation,whereas serglycin -/- MCs completely lacked this ability.Moreover, MC-mediated IL-13 degradation was blocked both by a serine protease inhibitor and by a heparin antagonist,which suggests that IL-13 degradation is catalyzed by serglycin-dependent serine proteases and that optimal IL-13 degradation is dependent on both the serglycin and the protease component of the serglycin-protease complex.Moreover, IL-13 degradation was abrogated in MC-CPA -/-MC cultures, but was normal in cultures of MCs with an inactivating mutation of MC-CPA, which suggests that the IL-13-degrading serine proteases rely on MC-CPA protein.Together, our data implicate a serglycin-serine protease axis in the regulation of extracellular levels of IL-13.	Heparin	271-278	interleukin 13	Homo sapiens	196-201
23667909-4	2012	Indeed, we found that wild-type MCs efficiently degraded exogenous or endogenously produced IL-13 upon degranulation,whereas serglycin -/- MCs completely lacked this ability.Moreover, MC-mediated IL-13 degradation was blocked both by a serine protease inhibitor and by a heparin antagonist,which suggests that IL-13 degradation is catalyzed by serglycin-dependent serine proteases and that optimal IL-13 degradation is dependent on both the serglycin and the protease component of the serglycin-protease complex.Moreover, IL-13 degradation was abrogated in MC-CPA -/-MC cultures, but was normal in cultures of MCs with an inactivating mutation of MC-CPA, which suggests that the IL-13-degrading serine proteases rely on MC-CPA protein.Together, our data implicate a serglycin-serine protease axis in the regulation of extracellular levels of IL-13.	Heparin	271-278	interleukin 13	Homo sapiens	196-201
23667909-4	2012	Indeed, we found that wild-type MCs efficiently degraded exogenous or endogenously produced IL-13 upon degranulation,whereas serglycin -/- MCs completely lacked this ability.Moreover, MC-mediated IL-13 degradation was blocked both by a serine protease inhibitor and by a heparin antagonist,which suggests that IL-13 degradation is catalyzed by serglycin-dependent serine proteases and that optimal IL-13 degradation is dependent on both the serglycin and the protease component of the serglycin-protease complex.Moreover, IL-13 degradation was abrogated in MC-CPA -/-MC cultures, but was normal in cultures of MCs with an inactivating mutation of MC-CPA, which suggests that the IL-13-degrading serine proteases rely on MC-CPA protein.Together, our data implicate a serglycin-serine protease axis in the regulation of extracellular levels of IL-13.	Heparin	271-278	interleukin 13	Homo sapiens	196-201
23667909-4	2012	Indeed, we found that wild-type MCs efficiently degraded exogenous or endogenously produced IL-13 upon degranulation,whereas serglycin -/- MCs completely lacked this ability.Moreover, MC-mediated IL-13 degradation was blocked both by a serine protease inhibitor and by a heparin antagonist,which suggests that IL-13 degradation is catalyzed by serglycin-dependent serine proteases and that optimal IL-13 degradation is dependent on both the serglycin and the protease component of the serglycin-protease complex.Moreover, IL-13 degradation was abrogated in MC-CPA -/-MC cultures, but was normal in cultures of MCs with an inactivating mutation of MC-CPA, which suggests that the IL-13-degrading serine proteases rely on MC-CPA protein.Together, our data implicate a serglycin-serine protease axis in the regulation of extracellular levels of IL-13.	Heparin	271-278	interleukin 13	Homo sapiens	196-201
23667909-4	2012	Indeed, we found that wild-type MCs efficiently degraded exogenous or endogenously produced IL-13 upon degranulation,whereas serglycin -/- MCs completely lacked this ability.Moreover, MC-mediated IL-13 degradation was blocked both by a serine protease inhibitor and by a heparin antagonist,which suggests that IL-13 degradation is catalyzed by serglycin-dependent serine proteases and that optimal IL-13 degradation is dependent on both the serglycin and the protease component of the serglycin-protease complex.Moreover, IL-13 degradation was abrogated in MC-CPA -/-MC cultures, but was normal in cultures of MCs with an inactivating mutation of MC-CPA, which suggests that the IL-13-degrading serine proteases rely on MC-CPA protein.Together, our data implicate a serglycin-serine protease axis in the regulation of extracellular levels of IL-13.	Heparin	271-278	interleukin 13	Homo sapiens	196-201
22750107-5	2012	In addition, a higher grafting concentration of heparin yielded a weaker expression of stage-specific embryonic antigen 1 in constructs, indicating that the grafted heparin accelerated differentiation and reduced the number of phenotypic iPS cells after cultivation.	Heparin	165-172	fucosyltransferase 4	Homo sapiens	87-121
22782595-4	2012	In addition, heparin also inhibited the release of tumor necrosis factor (TNF)-alpha, interleukin-6 (IL-6) and IL-1beta in serum and decreased the expression of p-p38, nuclear factor kappaB (NF-kappaB) and p-c-SRC kinase in lungs of septic mice.	Heparin	13-20	tumor necrosis factor	Mus musculus	51-84
22782595-4	2012	In addition, heparin also inhibited the release of tumor necrosis factor (TNF)-alpha, interleukin-6 (IL-6) and IL-1beta in serum and decreased the expression of p-p38, nuclear factor kappaB (NF-kappaB) and p-c-SRC kinase in lungs of septic mice.	Heparin	13-20	interleukin 6	Mus musculus	86-99
22782595-4	2012	In addition, heparin also inhibited the release of tumor necrosis factor (TNF)-alpha, interleukin-6 (IL-6) and IL-1beta in serum and decreased the expression of p-p38, nuclear factor kappaB (NF-kappaB) and p-c-SRC kinase in lungs of septic mice.	Heparin	13-20	interleukin 6	Mus musculus	101-105
22782595-4	2012	In addition, heparin also inhibited the release of tumor necrosis factor (TNF)-alpha, interleukin-6 (IL-6) and IL-1beta in serum and decreased the expression of p-p38, nuclear factor kappaB (NF-kappaB) and p-c-SRC kinase in lungs of septic mice.	Heparin	13-20	interleukin 1 beta	Mus musculus	111-119
23019343-5	2012	For interaction with heparin, the FGFs exhibit K(D) values varying between 38 nM (FGF-18) and 620 nM (FGF-9) and association rate constants spanning over 20-fold (FGF-1, 2,900,000 M(-1) s(-1) and FGF-9, 130,000 M(-1) s(-1)).	Heparin	21-28	fibroblast growth factor 1	Homo sapiens	82-87
23019343-8	2012	These data suggest that the differences in heparin-binding sites in both the protein and the sugar are greatest between subfamilies and may be more restricted within a FGF subfamily in accord with the known conservation of function within FGF subfamilies.	Heparin	43-50	fibroblast growth factor 1	Homo sapiens	168-171
23019343-8	2012	These data suggest that the differences in heparin-binding sites in both the protein and the sugar are greatest between subfamilies and may be more restricted within a FGF subfamily in accord with the known conservation of function within FGF subfamilies.	Heparin	43-50	fibroblast growth factor 1	Homo sapiens	239-242
23130841-6	2012	Plasma levels of thrombin-antithrombin complex, fibrin and/or fibrinogen degradation products and D-dimers decreased after administration of low-molecular-weight heparin.	Heparin	162-169	fibrinogen beta chain	Homo sapiens	62-72
22877639-1	2012	The direct thrombin inhibitor of bivalirudin (BVLD), a short peptide derived from hirudin, has drawn an increasing attention in clinical application because it is safer and more effective than heparin for diabetic patients with moderate- or high-risk for acute coronary syndromes (ACS).	Heparin	193-200	coagulation factor II, thrombin	Homo sapiens	11-19
22672269-0	2012	Heparin affin regulatory peptide modulates the endogenous anticoagulant activity of heparin and heparan sulphate mimetics.	Heparin	84-91	pleiotrophin	Homo sapiens	0-32
22672269-2	2012	In this work, HARP was tested for its capacity to modulate the anticoagulant activity of heparin and heparan sulphate mimetics (OTR4120).	Heparin	89-96	pleiotrophin	Homo sapiens	14-18
22672269-4	2012	HARP was found to be differently effective for neutralization of the anticoagulant activity of the mimetic heparan sulphate (OTR4120) and heparin in purified system and human plasma.	Heparin	138-145	pleiotrophin	Homo sapiens	0-4
22672269-5	2012	HARP was shown to compete with both antithrombin and thrombin for binding to heparin and to OTR4120, respectively.	Heparin	77-84	pleiotrophin	Homo sapiens	0-4
22672269-5	2012	HARP was shown to compete with both antithrombin and thrombin for binding to heparin and to OTR4120, respectively.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	40-48
22672269-12	2012	Taken together, these data provide the first evidence for a physiological role of HARP in the modulation of anticoagulant activity of heparin and heparin-like material.	Heparin	134-141	pleiotrophin	Homo sapiens	82-86
22672269-12	2012	Taken together, these data provide the first evidence for a physiological role of HARP in the modulation of anticoagulant activity of heparin and heparin-like material.	Heparin	146-153	pleiotrophin	Homo sapiens	82-86
23095131-4	2012	Well known Heparanase-1 inhibitors are heparin(s) and sulodexide, a low-molecular weight heparin - dermatan sulphate blend, which is effective in the treatment of DN.	Heparin	39-46	heparanase	Homo sapiens	11-23
22261474-0	2012	Sustained heparin effect contributes to reduced plasma thrombin generation capacity early after cardiac surgery.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	55-63
22261474-6	2012	Heparin effect was assessed by anti-Xa activity, APTT and thrombin time.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	58-66
22261474-12	2012	The results indicate that a sustained heparin effect contributes to the postoperative reduction in thrombin generation capacity.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	99-107
22365560-0	2012	Thrombin generation post elective caesarean section: effect of low molecular weight heparin.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	0-8
22978548-0	2012	By increasing the affinity of heparin for fibrin, Zn(2+) promotes the formation of a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	101-109
22978548-0	2012	By increasing the affinity of heparin for fibrin, Zn(2+) promotes the formation of a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	139-147
22978548-5	2012	In contrast, in the presence of heparin, Zn(2+) increased the affinity of thrombin for gamma(A)/gamma(A)-fibrin 4-fold (from a K(d) value of 0.8 to 0.2 muM) and slowed the rate of thrombin dissociation from gamma(A)/gamma(A)-fibrin clots.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	74-82
22978548-8	2012	Therefore, by enhancing the binding of heparin to fibrin, physiological concentrations of Zn(2+) render fibrin-bound thrombin more protected from inhibition by antithrombin.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	117-125
22978548-9	2012	Because fibrin-bound thrombin can trigger thrombus expansion, these findings help to explain why recurrent thrombosis can occur despite heparin treatment.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	21-29
22692045-9	2012	Because HS-PF4 complexes are the initiating cause of heparin-induced thrombocytopenia, this finding provides a promising strategy for developing heparin therapies with reduced side effects.	Heparin	53-60	DnaJ heat shock protein family (Hsp40) member A1	Homo sapiens	8-14
22763042-0	2012	Unfractionated heparin inhibits lipopolysaccharide-induced inflammatory response through blocking p38 MAPK and NF-kappaB activation on endothelial cell.	Heparin	15-22	mitogen-activated protein kinase 14	Homo sapiens	98-101
22763042-11	2012	The inhibition of p38 MAPK and NF-kappaB activation certainly represents one of the mechanisms by which UFH exerts its anti-inflammatory effect.	Heparin	104-107	mitogen-activated protein kinase 14	Homo sapiens	18-21
22330584-0	2012	Comment on: heparin protects against septic mortality via apoE-antagonism.	Heparin	12-19	apolipoprotein E	Homo sapiens	58-62
22879585-5	2012	Consistent with ligand shedding, circulating heparin-bound EGF was elevated in the plasma of AS monkeys but not in those on regression diet.	Heparin	45-52	pro-epidermal growth factor	Macaca fascicularis	59-62
22692045-9	2012	Because HS-PF4 complexes are the initiating cause of heparin-induced thrombocytopenia, this finding provides a promising strategy for developing heparin therapies with reduced side effects.	Heparin	145-152	DnaJ heat shock protein family (Hsp40) member A1	Homo sapiens	8-14
22905983-0	2012	Low molecular weight heparin inhibits plasma thrombin generation via direct targeting of factor IXa: contribution of the serpin-independent mechanism.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	45-53
22641607-9	2012	On PEO-ATH surfaces fibrinogen adsorption was minimal while AT adsorption was high showing the selectivity of the heparin moiety of ATH for AT.	Heparin	114-121	twinkle mtDNA helicase	Homo sapiens	3-6
22871361-3	2012	MDK and PTN belong to a newly evolving family of secreted neurotrophic and developmentally regulated heparin-binding molecules.	Heparin	101-108	midkine	Homo sapiens	0-3
22819639-1	2012	BACKGROUND: We have shown that administration of heparin-binding EGF (epidermal growth factor)-like growth factor (HB-EGF) protects the intestines from experimental necrotizing enterocolitis (NEC).	Heparin	49-56	heparin-binding EGF-like growth factor	Rattus norvegicus	115-121
22887691-3	2012	Heparin-binding growth factors [basic fibroblast growth factor (bFGF) in this study] can be immobilized through interaction with heparin, which was covalently attached to the CVD surface through an aldehyde-hydrazide reaction.	Heparin	129-136	fibroblast growth factor 2	Homo sapiens	32-62
22576950-1	2012	Midkine (MDK) is a heparin-binding molecule involved in the regulation of growth and differentiation during embryogenesis, which is overexpressed in most of human malignant tumors and may act as an oncoprotein.	Heparin	19-26	midkine	Homo sapiens	0-7
22576950-1	2012	Midkine (MDK) is a heparin-binding molecule involved in the regulation of growth and differentiation during embryogenesis, which is overexpressed in most of human malignant tumors and may act as an oncoprotein.	Heparin	19-26	midkine	Homo sapiens	9-12
22887691-3	2012	Heparin-binding growth factors [basic fibroblast growth factor (bFGF) in this study] can be immobilized through interaction with heparin, which was covalently attached to the CVD surface through an aldehyde-hydrazide reaction.	Heparin	129-136	fibroblast growth factor 2	Homo sapiens	64-68
22117815-9	2012	Moreover, depletion of extracellular FGF-2 by heparin prevented pravastatin-induced phosphorylation of Akt and MAPK.	Heparin	46-53	fibroblast growth factor 2	Homo sapiens	37-42
22641106-5	2012	In this work we report a three-dimensional porous polyethylene glycol (PEG) diacrylate hydrogel bioactivated with heparin that is able to deliver vascular endothelial growth factor (VEGF) in a sustained and controlled manner.	Heparin	114-121	vascular endothelial growth factor A	Homo sapiens	146-180
22641106-5	2012	In this work we report a three-dimensional porous polyethylene glycol (PEG) diacrylate hydrogel bioactivated with heparin that is able to deliver vascular endothelial growth factor (VEGF) in a sustained and controlled manner.	Heparin	114-121	vascular endothelial growth factor A	Homo sapiens	182-186
22641771-0	2012	The C-terminal fragment of axon guidance molecule Slit3 binds heparin and neutralizes heparin"s anticoagulant activity.	Heparin	62-69	slit guidance ligand 3	Homo sapiens	50-55
22759380-4	2012	In vitro maturation of cumulus oocyte complexes in the presence of exogenous heparin, which antagonizes HSPG signaling, prevented cumulus expansion and blocked the induction of cumulus-specific matrix genes, Has2 and Tnfaip6, whereas conversely, the mural granulosa-specific genes, Lhcgr and Cyp11a1, were strongly up-regulated.	Heparin	77-84	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	292-299
22117815-9	2012	Moreover, depletion of extracellular FGF-2 by heparin prevented pravastatin-induced phosphorylation of Akt and MAPK.	Heparin	46-53	AKT serine/threonine kinase 1	Homo sapiens	103-106
22739141-1	2012	Heparins have been reported to cause elevations in serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) but have not been associated with clinically significant liver injury.	Heparin	0-8	solute carrier family 17 member 5	Homo sapiens	92-118
22773834-2	2012	Heparin is a commonly used anticoagulant drug that inhibits the activities of factors Xa and IIa (also known as thrombin) to prevent blood clot formation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	112-120
22497885-9	2012	In addition, unfractionated heparin but not bemiparin was able to increase AKT phosphorylation.	Heparin	28-35	AKT serine/threonine kinase 1	Homo sapiens	75-78
22809401-2	2012	Follistatin (FS) is an autocrine protein with a heparin-binding motif that serves to regulate the cell proliferative activity of the paracrine hormone, and member of the TGF-beta family, activin A (ActA).	Heparin	48-55	follistatin	Homo sapiens	0-11
22809401-7	2012	Full chain heparin or large oligosaccharides, having 18-20 sugar residues, show the highest binding activity for FS288 and the FS288-ActA complex, whereas smaller heparin molecules could interact with the FS288-Mstn complex.	Heparin	11-18	myostatin	Homo sapiens	211-215
22809401-10	2012	The binding of heparin to the FS288-ActA complex was disrupted at 500 mM salt, whereas it was actually strengthened for the FS288-Mstn complex.	Heparin	15-22	myostatin	Homo sapiens	130-134
22809401-12	2012	While slightly acidic pH values (pH 6.2 and 5.2) enhanced the binding of the FS288-Mstn complex to heparin, at pH 4 heparin binding was inhibited.	Heparin	99-106	myostatin	Homo sapiens	83-87
22427536-7	2012	Studies performed using BEAS-2B cells showed that pretreatment with heparin and syndecan-4 decreased the expression of CXCL8 mRNA in response to LPS and TNF-alpha.	Heparin	68-75	C-X-C motif chemokine ligand 8	Homo sapiens	119-124
22427536-7	2012	Studies performed using BEAS-2B cells showed that pretreatment with heparin and syndecan-4 decreased the expression of CXCL8 mRNA in response to LPS and TNF-alpha.	Heparin	68-75	tumor necrosis factor	Homo sapiens	153-162
24750917-5	2012	Like heparin, they inhibited thrombin by a mechanism dependent on AT and HCII.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	29-37
22739141-1	2012	Heparins have been reported to cause elevations in serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) but have not been associated with clinically significant liver injury.	Heparin	0-8	solute carrier family 17 member 5	Homo sapiens	120-123
22330023-9	2012	The causal relationship between NEFA concentration and MAPK activation was evaluated by injecting mice with heparin.	Heparin	108-115	mitogen-activated protein kinase 1	Mus musculus	55-59
22920489-4	2012	Unfractionated heparin traditionally has been the most commonly used anticoagulant but is fast being replaced by relatively newer agents like LMWH, direct thrombin inhibitors, and Factor Xa inhibitors.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	155-163
22871410-0	2012	[Therapeutic effects of unfractionated heparin on lipopolysaccharide-activated matrix metalloproteinase-9 and tissue inhibitors of metalloproteinase-1 in endothelial cells].	Heparin	39-46	TIMP metallopeptidase inhibitor 1	Homo sapiens	110-150
22762190-5	2012	HBPs like lactoferrin (LF), fibronectin fragment (FNIII), semenogelinI (SGI) and prostate specific antigen (PSA) all bind heparin with different binding kinetics and affinities.	Heparin	122-129	fibronectin 1	Homo sapiens	28-39
22871410-1	2012	OBJECTIVE: To investigate the expressions of matrix metalloproteinase-9 and tissue inhibitors of metalloproteinase-1 (TIMP-1) in injured endothelial cells induced by lipopolysaccharide (LPS) and the effects of unfractionated heparin (UFH) on the level of expressions.	Heparin	225-232	TIMP metallopeptidase inhibitor 1	Homo sapiens	118-124
22871410-1	2012	OBJECTIVE: To investigate the expressions of matrix metalloproteinase-9 and tissue inhibitors of metalloproteinase-1 (TIMP-1) in injured endothelial cells induced by lipopolysaccharide (LPS) and the effects of unfractionated heparin (UFH) on the level of expressions.	Heparin	234-237	TIMP metallopeptidase inhibitor 1	Homo sapiens	118-124
22871410-7	2012	While as UFH pretreatment could significantly down-regulated the mRNA expressions of MMP-9 and TIMP-1 (UFH 0.1 U/ml group MMP-9 mRNA: 2.74+-0.30, TIMP-1 mRNA: 2.96+-0.13; UFH 1 U/ml group MMP-9 mRNA: 3.08+-0.48, TIMP-1 mRNA: 2.93+-0.27, all P&lt;0.05).	Heparin	9-12	TIMP metallopeptidase inhibitor 1	Homo sapiens	95-101
22871410-7	2012	While as UFH pretreatment could significantly down-regulated the mRNA expressions of MMP-9 and TIMP-1 (UFH 0.1 U/ml group MMP-9 mRNA: 2.74+-0.30, TIMP-1 mRNA: 2.96+-0.13; UFH 1 U/ml group MMP-9 mRNA: 3.08+-0.48, TIMP-1 mRNA: 2.93+-0.27, all P&lt;0.05).	Heparin	9-12	TIMP metallopeptidase inhibitor 1	Homo sapiens	146-152
22871410-7	2012	While as UFH pretreatment could significantly down-regulated the mRNA expressions of MMP-9 and TIMP-1 (UFH 0.1 U/ml group MMP-9 mRNA: 2.74+-0.30, TIMP-1 mRNA: 2.96+-0.13; UFH 1 U/ml group MMP-9 mRNA: 3.08+-0.48, TIMP-1 mRNA: 2.93+-0.27, all P&lt;0.05).	Heparin	9-12	TIMP metallopeptidase inhibitor 1	Homo sapiens	146-152
22444322-6	2012	In addition, the influence of long-chain hyaluronan, chondroitin sulfate, and heparin on IL-8-induced chemotaxis and oxidative activity of neutrophils was examined.	Heparin	78-85	C-X-C motif chemokine ligand 8	Homo sapiens	89-93
22444322-7	2012	Only the incubation of heparin with IL-8 affected the IL-8-mediated chemotaxis of neutrophils.	Heparin	23-30	C-X-C motif chemokine ligand 8	Homo sapiens	36-40
22444322-7	2012	Only the incubation of heparin with IL-8 affected the IL-8-mediated chemotaxis of neutrophils.	Heparin	23-30	C-X-C motif chemokine ligand 8	Homo sapiens	54-58
22372949-3	2012	In this study, we compared the quality of regenerated bone when BMP-2 was delivered with either beta-tricalcium phosphate (beta-TCP) or heparin-conjugated fibrin (HCF), both of which are shown to be excellent carriers for BMP-2.	Heparin	136-143	bone morphogenetic protein 2	Mus musculus	64-69
22465575-5	2012	In order to evaluate the release capacity of the heparin-conjugated scaffolds, lysozyme was used as a model protein for conjugation.	Heparin	49-56	lysozyme	Homo sapiens	79-87
22465575-6	2012	The heparin-conjugated scaffolds provided high loading efficiency and cumulative release of lysozyme with a relatively linear relationship.	Heparin	4-11	lysozyme	Homo sapiens	92-100
22564978-3	2012	Here we investigated the role of the heparin-binding growth factor midkine (MK) on PGC development, first using our established model of porcine stem cell-derived PGC-like cells and then confirming our findings in PGC.	Heparin	37-44	midkine	Homo sapiens	67-74
22564978-3	2012	Here we investigated the role of the heparin-binding growth factor midkine (MK) on PGC development, first using our established model of porcine stem cell-derived PGC-like cells and then confirming our findings in PGC.	Heparin	37-44	midkine	Homo sapiens	76-78
22313597-2	2012	IGFBP5, one of these IGFBPs, has special structural features, including a nuclear transport domain, heparin-binding motif, and IGF/extracellular matrix/acid-labile subunit-binding sites.	Heparin	100-107	insulin like growth factor binding protein 5	Homo sapiens	0-6
22532692-9	2012	More importantly, mutations of the arginine and lysine to alanine or glutamic acid in the receptor-binding region ablated the heparin-binding activity of apoE, as determined by an in vitro heparin pulldown assay.	Heparin	126-133	apolipoprotein E	Homo sapiens	154-158
22532692-9	2012	More importantly, mutations of the arginine and lysine to alanine or glutamic acid in the receptor-binding region ablated the heparin-binding activity of apoE, as determined by an in vitro heparin pulldown assay.	Heparin	189-196	apolipoprotein E	Homo sapiens	154-158
22909136-15	2012	Heparin at 1 IU/ml and LMWH at 10 IU/ml in all species almost completely abrogated thrombin-induced platelet aggregation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	83-91
22909136-21	2012	Even a concentration of heparin of 1 IU/ml, which is probably the maximal concentration that is clinically-applicable, prevented platelet aggregation induced by thrombin, but was less effective in preventing aggregation induced by collagen, ADP, or, particularly, ristocetin.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	161-169
22669117-18	2012	Heparin 125 mug/mL decreased vimentin and E-cadherin mRNA transcription while increased TGF-beta mRNA transcription in the PC-3M cells, but the differences were not significant.	Heparin	0-7	cadherin 1	Homo sapiens	42-52
22313597-2	2012	IGFBP5, one of these IGFBPs, has special structural features, including a nuclear transport domain, heparin-binding motif, and IGF/extracellular matrix/acid-labile subunit-binding sites.	Heparin	100-107	insulin like growth factor binding protein 5	Homo sapiens	21-27
22646534-1	2012	BACKGROUND: Membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields soluble HB-EGF, which is an epidermal growth factor receptor (EGFR) ligand, and a carboxy-terminal fragment of HB-EGF (HB-EGF-CTF) after ectodomain shedding.	Heparin	30-37	epidermal growth factor receptor	Homo sapiens	136-168
21898414-7	2012	In addition, heparin induces ERK1/2 phosphorylation and inhibitors of Ras and MEK decreased heparin-dependent HSPG synthesis.	Heparin	13-20	mitogen-activated protein kinase 3	Homo sapiens	29-35
21898414-7	2012	In addition, heparin induces ERK1/2 phosphorylation and inhibitors of Ras and MEK decreased heparin-dependent HSPG synthesis.	Heparin	13-20	mitogen-activated protein kinase kinase 7	Homo sapiens	78-81
21898414-7	2012	In addition, heparin induces ERK1/2 phosphorylation and inhibitors of Ras and MEK decreased heparin-dependent HSPG synthesis.	Heparin	92-99	mitogen-activated protein kinase kinase 7	Homo sapiens	78-81
21898414-8	2012	Moreover, heparin also induced intracellular Ca(2+) release, PLCgamma1 (phospholipase Cgamma1) and CaMKII (calcium calmodulin kinase II) activation, as well as an increase in nitric oxide (NO) production.	Heparin	10-17	phospholipase C gamma 1	Homo sapiens	61-70
21898414-10	2012	In conclusion, the heparin-induced up-regulation of HSPG expression is associated with the phosphorylation of focal adhesion proteins and Ras/Raf/MEK/ERK MAP and Ca(2+) /NO pathways.	Heparin	19-26	mitogen-activated protein kinase kinase 7	Homo sapiens	146-149
21898414-10	2012	In conclusion, the heparin-induced up-regulation of HSPG expression is associated with the phosphorylation of focal adhesion proteins and Ras/Raf/MEK/ERK MAP and Ca(2+) /NO pathways.	Heparin	19-26	mitogen-activated protein kinase 1	Homo sapiens	150-153
22322342-0	2012	Comparison between heparin-conjugated fibrin and collagen sponge as bone morphogenetic protein-2 carriers for bone regeneration.	Heparin	19-26	bone morphogenetic protein 2	Mus musculus	68-96
22322342-3	2012	Previously, we have developed heparin- conjugated fibrin (HCF), a vehicle for long-term delivery of BMP-2 and demonstrated that long-term delivery of BMP-2 enhanced its osteogenic efficacy as compared to short-term delivery at an equivalent dose.	Heparin	30-37	bone morphogenetic protein 2	Mus musculus	100-105
22322342-3	2012	Previously, we have developed heparin- conjugated fibrin (HCF), a vehicle for long-term delivery of BMP-2 and demonstrated that long-term delivery of BMP-2 enhanced its osteogenic efficacy as compared to short-term delivery at an equivalent dose.	Heparin	30-37	bone morphogenetic protein 2	Mus musculus	150-155
22406166-11	2012	A similar agreement between the total TGF-beta1 and the LAP ELISA was found with citrate- and heparin-containing plasma.	Heparin	94-101	transforming growth factor beta 1	Homo sapiens	38-47
22646534-1	2012	BACKGROUND: Membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields soluble HB-EGF, which is an epidermal growth factor receptor (EGFR) ligand, and a carboxy-terminal fragment of HB-EGF (HB-EGF-CTF) after ectodomain shedding.	Heparin	30-37	epidermal growth factor receptor	Homo sapiens	170-174
22497483-2	2012	Turbidimetric data show that heparin is capable of inhibiting and reversing the native aggregation of bovine serum albumin (BSA), beta-lactoglobulin (BLG), and Zn-insulin at a pH near pI and at low ionic strength I; however, the results vary with regard to the range of pH, I, and protein-heparin stoichiometry required to achieve these effects.	Heparin	29-36	albumin	Homo sapiens	109-122
22442151-0	2012	Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix.	Heparin	36-43	transglutaminase 2	Homo sapiens	0-18
22442151-0	2012	Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix.	Heparin	36-43	transglutaminase 2	Homo sapiens	130-148
22442151-0	2012	Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix.	Heparin	65-72	transglutaminase 2	Homo sapiens	0-18
22442151-0	2012	Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 matrix.	Heparin	65-72	transglutaminase 2	Homo sapiens	130-148
22497483-2	2012	Turbidimetric data show that heparin is capable of inhibiting and reversing the native aggregation of bovine serum albumin (BSA), beta-lactoglobulin (BLG), and Zn-insulin at a pH near pI and at low ionic strength I; however, the results vary with regard to the range of pH, I, and protein-heparin stoichiometry required to achieve these effects.	Heparin	29-36	insulin	Homo sapiens	163-170
22497483-2	2012	Turbidimetric data show that heparin is capable of inhibiting and reversing the native aggregation of bovine serum albumin (BSA), beta-lactoglobulin (BLG), and Zn-insulin at a pH near pI and at low ionic strength I; however, the results vary with regard to the range of pH, I, and protein-heparin stoichiometry required to achieve these effects.	Heparin	289-296	albumin	Homo sapiens	109-122
22285427-5	2012	Human adipose-derived stem cell (hASC) adhesion to MBP-bFGF immobilized on a PS surface (PS-MBP-bFGF) was inhibited by heparin.	Heparin	119-126	PYD and CARD domain containing	Homo sapiens	33-37
22583667-12	2012	DcR3 binding was inhibited by heparin and heparinase.	Heparin	30-37	TNF receptor superfamily member 6b	Homo sapiens	0-4
22285427-5	2012	Human adipose-derived stem cell (hASC) adhesion to MBP-bFGF immobilized on a PS surface (PS-MBP-bFGF) was inhibited by heparin.	Heparin	119-126	fibroblast growth factor 2	Homo sapiens	55-59
22285427-5	2012	Human adipose-derived stem cell (hASC) adhesion to MBP-bFGF immobilized on a PS surface (PS-MBP-bFGF) was inhibited by heparin.	Heparin	119-126	fibroblast growth factor 2	Homo sapiens	96-100
22285427-9	2012	These results suggest that the mechanism of hASC adhesion to MBP-bFGF immobilized on a PS substrate is mediated by a specific interaction between bFGF and heparin, and that the adhesion mechanism might provide an insight into the design of biomaterials to control the fate of stem cells.	Heparin	155-162	PYD and CARD domain containing	Homo sapiens	44-48
22285427-9	2012	These results suggest that the mechanism of hASC adhesion to MBP-bFGF immobilized on a PS substrate is mediated by a specific interaction between bFGF and heparin, and that the adhesion mechanism might provide an insight into the design of biomaterials to control the fate of stem cells.	Heparin	155-162	fibroblast growth factor 2	Homo sapiens	65-69
22370276-2	2012	The binding is mediated by apolipoprotein apoB-100 and/or apoE, both of which have binding affinity toward heparin.	Heparin	107-114	apolipoprotein B	Homo sapiens	42-50
22370276-2	2012	The binding is mediated by apolipoprotein apoB-100 and/or apoE, both of which have binding affinity toward heparin.	Heparin	107-114	apolipoprotein E	Homo sapiens	58-62
22370276-6	2012	Both techniques showed heparin interactions to be stronger with apoB-100 peptide than with apoE peptide fragment, and they confirmed that the sulfate groups in heparin play an especially important role in interactions with apoB-100 peptide fragments.	Heparin	23-30	apolipoprotein B	Homo sapiens	64-72
22370276-6	2012	Both techniques showed heparin interactions to be stronger with apoB-100 peptide than with apoE peptide fragment, and they confirmed that the sulfate groups in heparin play an especially important role in interactions with apoB-100 peptide fragments.	Heparin	23-30	apolipoprotein B	Homo sapiens	223-231
22370276-6	2012	Both techniques showed heparin interactions to be stronger with apoB-100 peptide than with apoE peptide fragment, and they confirmed that the sulfate groups in heparin play an especially important role in interactions with apoB-100 peptide fragments.	Heparin	160-167	apolipoprotein B	Homo sapiens	223-231
22447354-2	2012	We aimed to delineate the heparin-binding regions of human TG2 by studying binding kinetics of the predicted heparin-binding peptides using surface plasmon resonance method.	Heparin	26-33	transglutaminase 2	Homo sapiens	59-62
21953059-0	2012	Thrombin induces osteosarcoma growth, a function inhibited by low molecular weight heparin in vitro and in vivo: procoagulant nature of osteosarcoma.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	0-8
21953059-6	2012	The efficacy of low molecular weight heparin (LMWH) attenuation of tumor-dependent thrombin generation and growth in vitro and in vivo was determined.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	83-91
22643054-1	2012	To synthesize long-acting and antiangiogenic erythropoietin to be clinically applied for treatment of patients with solid tumors, we synthesized a hybrid molecule of human erythropoietin added onto the C-terminus with a heparin-binding motif of human PLGF-2 to develop a novel derivative of long-acting and antiangiogenic erythropoietin: heparin-binding erythropoietin (HEPO), and studied the characteristics of this novel erythropoietin derivative.	Heparin	220-227	erythropoietin	Homo sapiens	45-59
22643054-1	2012	To synthesize long-acting and antiangiogenic erythropoietin to be clinically applied for treatment of patients with solid tumors, we synthesized a hybrid molecule of human erythropoietin added onto the C-terminus with a heparin-binding motif of human PLGF-2 to develop a novel derivative of long-acting and antiangiogenic erythropoietin: heparin-binding erythropoietin (HEPO), and studied the characteristics of this novel erythropoietin derivative.	Heparin	220-227	erythropoietin	Homo sapiens	172-186
22643054-1	2012	To synthesize long-acting and antiangiogenic erythropoietin to be clinically applied for treatment of patients with solid tumors, we synthesized a hybrid molecule of human erythropoietin added onto the C-terminus with a heparin-binding motif of human PLGF-2 to develop a novel derivative of long-acting and antiangiogenic erythropoietin: heparin-binding erythropoietin (HEPO), and studied the characteristics of this novel erythropoietin derivative.	Heparin	220-227	erythropoietin	Homo sapiens	172-186
22643054-1	2012	To synthesize long-acting and antiangiogenic erythropoietin to be clinically applied for treatment of patients with solid tumors, we synthesized a hybrid molecule of human erythropoietin added onto the C-terminus with a heparin-binding motif of human PLGF-2 to develop a novel derivative of long-acting and antiangiogenic erythropoietin: heparin-binding erythropoietin (HEPO), and studied the characteristics of this novel erythropoietin derivative.	Heparin	220-227	erythropoietin	Homo sapiens	172-186
22643054-1	2012	To synthesize long-acting and antiangiogenic erythropoietin to be clinically applied for treatment of patients with solid tumors, we synthesized a hybrid molecule of human erythropoietin added onto the C-terminus with a heparin-binding motif of human PLGF-2 to develop a novel derivative of long-acting and antiangiogenic erythropoietin: heparin-binding erythropoietin (HEPO), and studied the characteristics of this novel erythropoietin derivative.	Heparin	220-227	erythropoietin	Homo sapiens	172-186
22643054-7	2012	In conclusion, the heparin-binding motif of PLGF-2 may act as, so to speak, a superendostatin.	Heparin	19-26	placental growth factor	Homo sapiens	44-50
22475438-3	2012	Resulting antibodies against these PF4/heparin complexes can activate platelets via the platelet FcgammaIIa receptor, leading to thrombin generation and thus to the paradox of a prothrombotic state despite thrombocytopenia and application of heparin.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	129-137
22389099-6	2012	The results showed not only thromboresistant activity and a stable state of heparin on the surfaces after investigation with toluidine blue and thrombin activation assay but also proliferation of HUVEC in vitro.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	144-152
22447354-4	2012	The high-affinity binding of human TG2 to the immobilized heparin was observed, and two TG2 peptides, P1 (amino acids 202-215) and P2 (261-274), were found to bind heparin.	Heparin	58-65	transglutaminase 2	Homo sapiens	35-38
22447354-4	2012	The high-affinity binding of human TG2 to the immobilized heparin was observed, and two TG2 peptides, P1 (amino acids 202-215) and P2 (261-274), were found to bind heparin.	Heparin	164-171	transglutaminase 2	Homo sapiens	35-38
22447354-4	2012	The high-affinity binding of human TG2 to the immobilized heparin was observed, and two TG2 peptides, P1 (amino acids 202-215) and P2 (261-274), were found to bind heparin.	Heparin	164-171	transglutaminase 2	Homo sapiens	88-91
22447354-9	2012	High immunoreactivity of the corresponding heparin-binding peptides of TG2 with CD patient"s IgA supports the previously described role of anti-TG2 autoantibodies interfering with this interaction.	Heparin	43-50	transglutaminase 2	Homo sapiens	71-74
22447354-9	2012	High immunoreactivity of the corresponding heparin-binding peptides of TG2 with CD patient"s IgA supports the previously described role of anti-TG2 autoantibodies interfering with this interaction.	Heparin	43-50	transglutaminase 2	Homo sapiens	144-147
22099706-5	2012	MATERIALS AND METHODS: A series of non-anticoagulant heparin derivatives were investigated concerning their inhibitory capacities for VLA-4 mediated binding of human melanoma MV3 cells to VCAM-1 under physiological flow conditions in vitro.	Heparin	53-60	vascular cell adhesion molecule 1	Homo sapiens	188-194
22522458-5	2012	We subsequently showed how heparin and a high-molecular-weight Escherichia coli K5-derived heparin-like polysaccharide (K5-NSOS) inhibited TGF-beta-induced IL-11 production in MDA-MB-231(SA) cells.	Heparin	27-34	transforming growth factor beta 1	Homo sapiens	139-147
22522458-5	2012	We subsequently showed how heparin and a high-molecular-weight Escherichia coli K5-derived heparin-like polysaccharide (K5-NSOS) inhibited TGF-beta-induced IL-11 production in MDA-MB-231(SA) cells.	Heparin	91-98	transforming growth factor beta 1	Homo sapiens	139-147
22328518-5	2012	Using IGFBP5 mutants we demonstrate that the effect is IGF-independent but requires the heparin-binding domain in the C-terminus of IGFBP5.	Heparin	88-95	insulin like growth factor binding protein 5	Homo sapiens	6-12
22433083-0	2012	Solid-phase N-terminus PEGylation of recombinant human fibroblast growth factor 2 on heparin-sepharose column.	Heparin	85-92	fibroblast growth factor 2	Homo sapiens	55-81
22298777-0	2012	Characterization of heparin-binding site of tissue transglutaminase: its importance in cell surface targeting, matrix deposition, and cell signaling.	Heparin	20-27	transglutaminase 2	Homo sapiens	44-67
22210184-0	2012	Preservation of FGF-2 bioactivity using heparin-based nanoparticles, and their delivery from electrospun chitosan fibers.	Heparin	40-47	fibroblast growth factor 2	Homo sapiens	16-21
22210184-2	2012	Chitosan electrospun fiber networks are decorated with heparin-containing polyelectrolyte complex nanoparticles (PCNs) that present basic fibroblast growth factor (FGF-2), both stably adsorbed to the surfaces and released into solution.	Heparin	55-62	fibroblast growth factor 2	Homo sapiens	164-169
22009636-4	2012	GPIHBP1-deficient mice and humans exhibit severe hypertriglyceridemia and diminished heparin-releasable LPL, pointing to the critical role of GPIHBP1 in regulation of LPL activity.	Heparin	85-92	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	0-7
22328518-5	2012	Using IGFBP5 mutants we demonstrate that the effect is IGF-independent but requires the heparin-binding domain in the C-terminus of IGFBP5.	Heparin	88-95	insulin like growth factor binding protein 5	Homo sapiens	132-138
22235124-1	2012	The mouse and human TPSB2 and TPSAB1 genes encode tetramer-forming tryptases stored in the secretory granules of mast cells (MCs) ionically bound to heparin-containing serglycin proteoglycans.	Heparin	149-156	tryptase alpha/beta 1	Homo sapiens	30-36
22262798-10	2012	In addition to NOS2 expression, BMMC(SCF/IL-4) were distinguished from BMMC(IL-3) in heparin and MMCP expression.	Heparin	85-92	interleukin 3	Mus musculus	71-80
22035631-0	2012	Heparin attenuates lipopolysaccharide-induced acute lung injury by inhibiting nitric oxide synthase and TGF-beta/Smad signaling pathway.	Heparin	0-7	transforming growth factor, beta 1	Rattus norvegicus	104-112
22035631-7	2012	Heparin also inhibited the release of tumor necrosis factor (TNF)-alpha and interleukin (IL)-6, and markedly decreased the expression of inducible nitric oxide synthase (iNOS) in lung tissues and thus prevented nitric oxide (NO) release in response to LPS challenge.	Heparin	0-7	tumor necrosis factor	Rattus norvegicus	38-71
22035631-7	2012	Heparin also inhibited the release of tumor necrosis factor (TNF)-alpha and interleukin (IL)-6, and markedly decreased the expression of inducible nitric oxide synthase (iNOS) in lung tissues and thus prevented nitric oxide (NO) release in response to LPS challenge.	Heparin	0-7	interleukin 6	Rattus norvegicus	76-94
22035631-7	2012	Heparin also inhibited the release of tumor necrosis factor (TNF)-alpha and interleukin (IL)-6, and markedly decreased the expression of inducible nitric oxide synthase (iNOS) in lung tissues and thus prevented nitric oxide (NO) release in response to LPS challenge.	Heparin	0-7	nitric oxide synthase 2	Rattus norvegicus	137-168
22035631-7	2012	Heparin also inhibited the release of tumor necrosis factor (TNF)-alpha and interleukin (IL)-6, and markedly decreased the expression of inducible nitric oxide synthase (iNOS) in lung tissues and thus prevented nitric oxide (NO) release in response to LPS challenge.	Heparin	0-7	nitric oxide synthase 2	Rattus norvegicus	170-174
22035631-8	2012	Additionally, heparin decreased the expression of transforming growth factor-beta1 (TGF-beta1), p-Smad 2, and p-Smad 3, which are all important molecules of the TGF-beta1/Smad signaling pathway.	Heparin	14-21	transforming growth factor, beta 1	Rattus norvegicus	50-82
22035631-8	2012	Additionally, heparin decreased the expression of transforming growth factor-beta1 (TGF-beta1), p-Smad 2, and p-Smad 3, which are all important molecules of the TGF-beta1/Smad signaling pathway.	Heparin	14-21	transforming growth factor, beta 1	Rattus norvegicus	84-93
22035631-8	2012	Additionally, heparin decreased the expression of transforming growth factor-beta1 (TGF-beta1), p-Smad 2, and p-Smad 3, which are all important molecules of the TGF-beta1/Smad signaling pathway.	Heparin	14-21	transforming growth factor, beta 1	Rattus norvegicus	161-170
22035631-9	2012	CONCLUSIONS: Heparin significantly ameliorated the lung injury induced by LPS in rats via the inhibition of nitric oxide synthase expression and the TGF-beta/Smad pathway.	Heparin	13-20	transforming growth factor, beta 1	Rattus norvegicus	149-157
22330806-4	2012	In contrast, secreted VEGF(120) lacking a heparin-binding domain was markedly increased 2.0-fold (p&lt;0.01).	Heparin	42-49	vascular endothelial growth factor A	Homo sapiens	22-26
21749932-5	2012	The apoA-I binding to ABCA1 and the cross-linking between them were inhibited by the highly charged molecules heparin and poly-L-lysine.	Heparin	110-117	apolipoprotein A1	Homo sapiens	4-10
22381096-23	2012	Heparin is currently the standard therapy, but we showed that the direct thrombin inhibitor bivalirudin may be an attractive alternative by causing less bleeding events, and a higher frequency of preprocedure thrombolysis in myocardial infarction (TIMI) 3 flow.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	73-81
22718631-5	2012	Preincubation with heparin and the receptor-associated protein, both of which prevented the apoA5 interaction with members of the low-density lipoprotein receptor gene family, markedly reduced the uptake of apoA5 by 61% and 52%, respectively, which were subsequently confirmed by Western blot analysis.	Heparin	19-26	apolipoprotein A5	Homo sapiens	92-97
22718631-5	2012	Preincubation with heparin and the receptor-associated protein, both of which prevented the apoA5 interaction with members of the low-density lipoprotein receptor gene family, markedly reduced the uptake of apoA5 by 61% and 52%, respectively, which were subsequently confirmed by Western blot analysis.	Heparin	19-26	apolipoprotein A5	Homo sapiens	207-212
22113934-1	2012	Acidic fibroblast growth factor-1 (FGF-1) is an angiogenic protein which requires binding to a polyanion such as heparin for its mitogenic activity and physicochemical stability.	Heparin	113-120	fibroblast growth factor 1	Homo sapiens	35-40
22393937-3	2012	A specific pentasaccharide sequence is responsible for heparin"s high affinity towards anti-thrombin III, which undergoes a conformational change and, as a result, inhibits the blood coagulation Factor Xa, a critical serine protease at the convergence on the intrinsic and extrinsic activation pathway of the coagulation cascade.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	217-232
22326251-8	2012	An antithrombin III (ATIII) binding assay using flow cytometry, designed to recognize a key sugar structure characteristic of heparin, indicated that Hs3st1 transfection was capable of increasing ATIII binding.	Heparin	126-133	heparan sulfate glucosamine 3-O-sulfotransferase 1	Cricetulus griseus	150-156
22113934-4	2012	FGF-1 mutants were identified with stability profiles in the absence of heparin comparable to that of wild-type FGF-1 in the presence of heparin while still retaining their biological activity.	Heparin	72-79	fibroblast growth factor 1	Homo sapiens	0-5
22113934-4	2012	FGF-1 mutants were identified with stability profiles in the absence of heparin comparable to that of wild-type FGF-1 in the presence of heparin while still retaining their biological activity.	Heparin	137-144	fibroblast growth factor 1	Homo sapiens	0-5
22206940-1	2012	Thrombin inactivation by heparin cofactor II (HCII) is accelerated by ternary complex formation with heparin.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	0-8
22206940-5	2012	Stopped-flow analysis demonstrated ordered assembly of HCII and the [6F]FFR-T heparin complex, in agreement with tighter heparin binding to thrombin than to HCII.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	140-148
22206940-6	2012	Saturating HCII dependences and bell-shaped heparin dependences of the fluorescence change reported ternary complex formation, consistent with a template mechanism in which the thrombin heparin complex binds HCII and allowing for interaction of thrombin (heparin)2 complexes with HCII.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	177-185
22690296-4	2012	The reliable association of coronary artery disease with decreased level of heparin-released EC-SOD was established in clinical research.	Heparin	76-83	superoxide dismutase 3	Homo sapiens	93-99
22206940-6	2012	Saturating HCII dependences and bell-shaped heparin dependences of the fluorescence change reported ternary complex formation, consistent with a template mechanism in which the thrombin heparin complex binds HCII and allowing for interaction of thrombin (heparin)2 complexes with HCII.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	245-253
22206940-8	2012	These studies demonstrate that binding of HCII to the thrombin heparin complex is dramatically enhanced compared with heparin binding alone and that exosite I is still available for ligand or HCII binding when both heparin binding sites on thrombin are saturated.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	54-62
22505551-0	2012	Effects of subcutaneous low molecular weight heparin and intravenous unfractionated heparin on serum S100 concentrations in patients with cerebrovascular diseases.	Heparin	45-52	S100 calcium binding protein A1	Homo sapiens	101-105
22505551-0	2012	Effects of subcutaneous low molecular weight heparin and intravenous unfractionated heparin on serum S100 concentrations in patients with cerebrovascular diseases.	Heparin	84-91	S100 calcium binding protein A1	Homo sapiens	101-105
22505551-2	2012	The objective was to investigate the effects of clinical heparins administrations on serum S100 concentrations in patients with cerebrovascular diseases.	Heparin	57-65	S100 calcium binding protein A1	Homo sapiens	91-95
22505551-5	2012	RESULTS: A rapid increase of serum S100 (median, 1.74-fold, p&lt;0.05) was observed in group A1 within 15 min of UFH administration.	Heparin	113-116	S100 calcium binding protein A1	Homo sapiens	35-39
22505551-7	2012	CONCLUSIONS: Both intravenous UFH and subcutaneous LMWH administration induced increases in serum S100 concentrations.	Heparin	30-33	S100 calcium binding protein A1	Homo sapiens	98-102
21847613-0	2012	Autoantibodies from patients with celiac disease inhibit transglutaminase 2 binding to heparin/heparan sulfate and interfere with intestinal epithelial cell adhesion.	Heparin	87-94	transglutaminase 2	Homo sapiens	57-75
21847613-2	2012	Our objective was to study whether autoantibodies could modulate TG2 binding to heparin/heparan sulfate (HS) and intestinal epithelial cell attachment to fibronectin-TG2 matrix.	Heparin	80-87	transglutaminase 2	Homo sapiens	65-68
23207953-0	2012	Low molecular weight heparin inhibits circulating fibrocytes differentiation by modulating neuronal nitric oxide synthase and TGF-beta1/Smad pathway.	Heparin	21-28	transforming growth factor beta 1	Homo sapiens	126-135
21658003-8	2012	The range of relative apparent binding affinities among VEGF and the panel of heparin-derived oligosaccharides demonstrate that the VEGF binding affinity likely depends on the specific structural features of these oligosaccharides, including their degree of sulfation, sugar-ring stereochemistry and conformation.	Heparin	78-85	vascular endothelial growth factor A	Homo sapiens	132-136
21658003-10	2012	These findings afford new insight into the inherent kinetics and affinities for VEGF association with heparin and heparin-derived oligosaccharides with key residue-specific modifications and may potentially benefit the future design of oligosaccharide-based anti-angiogenesis drugs.	Heparin	102-109	vascular endothelial growth factor A	Homo sapiens	80-84
22315264-3	2012	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	70-78
22210566-7	2012	RESULTS: Insulin sensitivity was reduced by ~40% after 6 h of intralipid/heparin infusion (P &lt; 0.001).	Heparin	73-80	insulin	Homo sapiens	9-16
22740939-0	2012	Chemically modified heparins inhibit fibrinogen-bridged indirect adhesion between tumor cells and platelets.	Heparin	20-28	fibrinogen beta chain	Homo sapiens	37-47
22740939-3	2012	In the present study, we aimed to detect the effects of 8 chemically modified heparins on the binding of fibrinogen to platelets or tumor cells using flow cytometry assays, as well as the fibrinogen-bridged adhesion of platelets and tumor cells using flow chamber assays.	Heparin	78-86	fibrinogen beta chain	Homo sapiens	105-115
22740939-6	2012	These data indicate that chemically modified heparins should be potential inhibitors for the fibrinogen-bridged indirect adhesion of platelets and tumor cells, which provides a novel explanation of the anti-adhesion property of heparin and proposes a new anti-metastatic target for cancer treatment.	Heparin	45-53	fibrinogen beta chain	Homo sapiens	93-103
22740939-6	2012	These data indicate that chemically modified heparins should be potential inhibitors for the fibrinogen-bridged indirect adhesion of platelets and tumor cells, which provides a novel explanation of the anti-adhesion property of heparin and proposes a new anti-metastatic target for cancer treatment.	Heparin	45-52	fibrinogen beta chain	Homo sapiens	93-103
22214372-9	2012	Prophylactic heparin treatment significantly improved the morphologic changes, myeloperoxidase (MPO), TNF-alpha and malondialdehyde (MDA) activities.	Heparin	13-20	tumor necrosis factor	Rattus norvegicus	102-111
22155248-1	2012	Sulfated low molecular weight lignins (LMWLs), designed as oligomeric mimetics of low molecular weight heparins (LMWHs), have been found to bind in exosite II of thrombin.	Heparin	103-111	coagulation factor II, thrombin	Homo sapiens	162-170
22085638-4	2012	SPR results revealed that heparin binds with higher affinity to human IL-7 than murine IL-7 through a different kinetic mechanism.	Heparin	26-33	interleukin 7	Homo sapiens	70-74
22085638-4	2012	SPR results revealed that heparin binds with higher affinity to human IL-7 than murine IL-7 through a different kinetic mechanism.	Heparin	26-33	interleukin 7	Mus musculus	87-91
22085638-5	2012	The optimal oligosaccharide length of heparin for the interactions to human and murine IL-7 involves a sequence larger than a tetrasaccharide.	Heparin	38-45	interleukin 7	Mus musculus	87-91
22085638-6	2012	These results further demonstrate that while IL-7 is principally a heparin/heparan sulfate binding protein, it also interacts with dermatan sulfate, chondroitin sulfates C, D, and E, indicating that this cytokine preferentially interacts with GAGs having a higher degree of sulfation.	Heparin	67-74	interleukin 7	Mus musculus	45-49
22466566-1	2012	Natural cytotoxicity receptor 2 (NCR2 or natural killer (NK)p44) and NCR3 (NKp30) bind to heparin and heparin sulfate; however, other natural ligands have yet to be identified.	Heparin	90-97	natural cytotoxicity triggering receptor 2	Homo sapiens	33-37
22466566-1	2012	Natural cytotoxicity receptor 2 (NCR2 or natural killer (NK)p44) and NCR3 (NKp30) bind to heparin and heparin sulfate; however, other natural ligands have yet to be identified.	Heparin	90-97	natural cytotoxicity triggering receptor 2	Homo sapiens	41-63
22466566-7	2012	These results suggest that NKp44 binds to alpha2,3-sialylated N-glycans through ionic interactions, and that these binding sites might have some overlap with heparin binding sites.	Heparin	158-165	natural cytotoxicity triggering receptor 2	Homo sapiens	27-32
21740405-1	2012	New direct and indirect acting factor Xa (FXa) and thrombin inhibitors are being developed to overcome the downsides of the conventional anticoagulants - unfractionated and low molecular weight heparins and vitamin K antagonists.	Heparin	194-202	coagulation factor II, thrombin	Homo sapiens	51-59
21669031-4	2012	Heparin-conjugated poly(lactic-co-glycolic acid) nanospheres (HCPNs) suspended in fibrin gel were used as a TGF-beta1 delivery system.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	108-117
22171556-8	2012	CONCLUSION: We have shown that the thrombin clotting time test can be modified and used as a cheap and reliable marker for heparin contamination.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	35-43
22040724-0	2012	Potentiation of C1-esterase inhibitor by heparin and interactions with C1s protease as assessed by surface plasmon resonance.	Heparin	41-48	complement C1s	Homo sapiens	16-27
22040724-5	2012	MAJOR CONCLUSIONS: Our SPR experiments conducted in three different design versions showed marked acceleration in C1-INH interactions with complement protease C1s as a result of potentiation of C1-INH by heparin (from 5- to 11-fold increase of the association rate).	Heparin	204-211	complement C1s	Homo sapiens	159-162
22040724-8	2012	GENERAL SIGNIFICANCE: This is the first report that directly demonstrates a significant acceleration of the C1-INH interactions with C1s due to heparin by using a consecutive double capture SPR approach.	Heparin	144-151	complement C1s	Homo sapiens	133-136
21822978-5	2012	Reducing tumor angiogenesis by combining the somatostatin analog octreotide with small doses of heparin is one approach in decreasing metastasis rates by targeting VEGF and heparinase, respectively.	Heparin	96-103	vascular endothelial growth factor A	Homo sapiens	164-168
22008103-7	2012	Heparin with low affinity for antithrombin was equally as effective as standard heparin, which indicates antithrombin independent effects.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	30-42
22008103-7	2012	Heparin with low affinity for antithrombin was equally as effective as standard heparin, which indicates antithrombin independent effects.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	105-117
22008103-7	2012	Heparin with low affinity for antithrombin was equally as effective as standard heparin, which indicates antithrombin independent effects.	Heparin	80-87	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	105-117
22888341-0	2012	Effect of non-anticoagulant N-desulfated heparin on basic fibroblast growth factor expression, angiogenesis, and metastasis of gastric carcinoma in vitro and in vivo.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	52-82
22888341-12	2012	In vitro, N-desulfated heparin inhibited significantly bFGF protein and mRNA expression of gastric carcinoma cells (P &lt; 0.05).	Heparin	23-30	fibroblast growth factor 2	Homo sapiens	55-59
21863223-1	2012	The life-threatening consequences of heparin induced thrombocytopenia (HIT) may be prevented with early recognition, prompt heparin withdrawal and direct thrombin inhibitor use.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	154-162
22052169-0	2012	In vitro determination of apoptotic effect of heparin on lymphoblasts by using flow cytometric DNA analysis and measurements of caspase-9 activation and cytochrome C level.	Heparin	46-53	cytochrome c, somatic	Homo sapiens	153-165
22052169-4	2012	Cytochrome C level and caspase-9 activity were concomitantly determined with the percentage of apoptotic lymphoblasts when incubated in 0, 10, and 20 U/mL heparin concentrations at 0, 1, and 2 hours.	Heparin	155-162	cytochrome c, somatic	Homo sapiens	0-12
22052169-11	2012	The mean cytochrome C level at the first hour was significantly higher than those at 0 and 2 hours in 10 and 20 U/mL heparin concentrations, separately (P&lt;0.05).	Heparin	117-124	cytochrome c, somatic	Homo sapiens	9-21
22052169-12	2012	The highest cytochrome C level was determined in 20 U/mL heparin concentration at the first hour.	Heparin	57-64	cytochrome c, somatic	Homo sapiens	12-24
22566220-1	2012	The molecular basis for the anticoagulant action of heparin lies in its ability to bind to and enhance the inhibitory activity of the plasma protein antithrombin against several serine proteases of the coagulation system, most importantly factors IIa (thrombin), Xa and IXa.	Heparin	52-59	coagulation factor II, thrombin	Homo sapiens	153-161
22566226-2	2012	Heparin exerts its antithrombotic effects by facilitating the ability of antithrombin (AT), a plasma serum protease inhibitor, to inhibit thrombin (factor IIa) and factor Xa.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	138-173
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	epidermal growth factor receptor	Homo sapiens	108-112
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	epidermal growth factor receptor	Homo sapiens	120-124
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	epidermal growth factor receptor	Homo sapiens	179-183
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	epidermal growth factor receptor	Homo sapiens	179-183
21984036-11	2012	Heparin can decrease the level of Duox1, ROS production and block the PMA-induced activation of EGFR, thus inhibiting the overexpression of mucin MUC5AC in a dose-dependent manner.	Heparin	0-7	epidermal growth factor receptor	Homo sapiens	96-100
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	epidermal growth factor receptor	Homo sapiens	161-165
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	epidermal growth factor receptor	Homo sapiens	161-165
22026648-3	2012	We found that MEK-ERK signaling is necessary for their cell-cycle entry, and signaling pathways whose activities can be modulated by heparin, such as Wnt-, Shh-, and thrombin-mediated pathways, are capable of regulating the cell-cycle entry.	Heparin	133-140	mitogen-activated protein kinase kinase 7	Homo sapiens	14-17
22026648-3	2012	We found that MEK-ERK signaling is necessary for their cell-cycle entry, and signaling pathways whose activities can be modulated by heparin, such as Wnt-, Shh-, and thrombin-mediated pathways, are capable of regulating the cell-cycle entry.	Heparin	133-140	mitogen-activated protein kinase 1	Homo sapiens	18-21
22026648-3	2012	We found that MEK-ERK signaling is necessary for their cell-cycle entry, and signaling pathways whose activities can be modulated by heparin, such as Wnt-, Shh-, and thrombin-mediated pathways, are capable of regulating the cell-cycle entry.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	166-174
23152789-2	2012	BACKGROUND: The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	20-28
23133616-2	2012	FGF-1 has low intrinsic thermostability and is characteristically formulated with heparin as a stabilizing agent.	Heparin	82-89	fibroblast growth factor 1	Homo sapiens	0-5
23133616-4	2012	Mutations that increase the thermostability of FGF-1 may obviate the need for heparin in formulation and may prove to be useful "2nd-generation" forms for therapeutic use.	Heparin	78-85	fibroblast growth factor 1	Homo sapiens	47-52
23133647-5	2012	We previously showed that TB5 binds heparin.	Heparin	36-43	transforming growth factor beta regulator 1	Homo sapiens	26-29
23133616-7	2012	The addition of heparin to FGF-1 is shown to increase endocrine-like properties of distribution.	Heparin	16-23	fibroblast growth factor 1	Homo sapiens	27-32
22912725-12	2012	Therefore, heparin treatment might be a therapeutic approach to inhibit invasion and metastasis of HCC, especially for patients with active HGF/c-Met signaling.	Heparin	11-18	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	144-149
23133647-7	2012	This finding enabled us to map heparin/heparan sulfate binding to two sites on fibrillin-1 TB5 using a mutagenesis approach.	Heparin	31-38	transforming growth factor beta regulator 1	Homo sapiens	91-94
23133647-9	2012	We show that a WMS deletion mutant, and five AD and GD point mutants all have disrupted heparin binding to TB5.	Heparin	88-95	transforming growth factor beta regulator 1	Homo sapiens	107-110
22988498-1	2012	Argatroban is a thrombin inhibitor used as anticoagulant in patients with heparin-induced thrombocytopenia.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	16-24
22912725-7	2012	In addition, heparin reduced HGF-induced activation of c-Met and MAPK in a dose-dependent manner, as well as decreased transcriptional activation and expression of Early growth response factor 1 (Egr1).	Heparin	13-20	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	55-60
22509290-5	2012	Compared to baseline values, sFLT1 and PlGF levels increased by 2629+-313% and 253+-54%, respectively, within 30 minutes of UFH therapy (p&lt;0.01 for both; n = 8).	Heparin	124-127	placental growth factor	Homo sapiens	39-43
22509290-6	2012	VEGF levels decreased by 93.2+-5% in patients treated with UFH (p&lt;0.01 versus baseline).	Heparin	59-62	vascular endothelial growth factor A	Homo sapiens	0-4
22509290-12	2012	To study the cellular origin of peptides after anticoagulant therapy, human coronary endothelial cells were treated with UFH and demonstrated increased sFLT1 and PlGF levels (ANOVA p&lt;0.01 for both) with reduced VEGF levels (ANOVA p&lt;0.05).	Heparin	121-124	placental growth factor	Homo sapiens	162-166
22509290-12	2012	To study the cellular origin of peptides after anticoagulant therapy, human coronary endothelial cells were treated with UFH and demonstrated increased sFLT1 and PlGF levels (ANOVA p&lt;0.01 for both) with reduced VEGF levels (ANOVA p&lt;0.05).	Heparin	121-124	vascular endothelial growth factor A	Homo sapiens	214-218
22509290-14	2012	CONCLUSIONS/SIGNIFICANCE: Circulating levels of sFLT1, PlGF, and VEGF are significantly altered by UFH, while bivalirudin therapy has no effect.	Heparin	99-102	placental growth factor	Homo sapiens	55-59
22509290-14	2012	CONCLUSIONS/SIGNIFICANCE: Circulating levels of sFLT1, PlGF, and VEGF are significantly altered by UFH, while bivalirudin therapy has no effect.	Heparin	99-102	vascular endothelial growth factor A	Homo sapiens	65-69
23227740-0	2012	[Assessment of endogenous thrombin potential and influence on it of different regimens of heparin therapy in patients with abdominal sepsis].	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	26-34
22844424-0	2012	Low molecular weight heparin ablates lung cancer cisplatin-resistance by inducing proteasome-mediated ABCG2 protein degradation.	Heparin	21-28	ATP binding cassette subfamily G member 2 (Junior blood group)	Homo sapiens	102-107
22606323-4	2012	NMR and MD data demonstrate that sm27 engages the heparin-binding site of FGF2 and induces long-range dynamics perturbations along FGF2/FGFR1 interface regions.	Heparin	50-57	fibroblast growth factor 2	Homo sapiens	74-78
23339859-2	2012	The SOD3 protein contains a heparin-binding domain and resides in a microenvironment rich in other  heparin-bound growth factors, raising the possibility that SOD3 may have some biological role independent of its catalytic activity.	Heparin	28-35	superoxide dismutase 3	Homo sapiens	4-8
23339859-2	2012	The SOD3 protein contains a heparin-binding domain and resides in a microenvironment rich in other  heparin-bound growth factors, raising the possibility that SOD3 may have some biological role independent of its catalytic activity.	Heparin	100-107	superoxide dismutase 3	Homo sapiens	4-8
24278706-7	2012	Oral administration, predictable anticoagulant responses, and few drug-drug interactions of direct thrombin and factor Xa inhibitors may further simplify PE home therapy avoiding administration of low-molecular-weight heparin.	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	99-107
23227740-4	2012	The test of thrombin generation (TTG) used in patients with AS allows assessment of changes in the hemostasis system and control of the heparin dose.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	12-20
23227740-6	2012	In the patients given 25 000 IU of heparin the TTG indices showed a reliably decreased endogenous thrombin potential and peak thrombin concentration as compared with a group of patients given 10 000 IU of heparin.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	98-106
23227740-6	2012	In the patients given 25 000 IU of heparin the TTG indices showed a reliably decreased endogenous thrombin potential and peak thrombin concentration as compared with a group of patients given 10 000 IU of heparin.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	126-134
22032622-3	2011	This nanoparticle delivery system possesses the following unique properties: (i) succinic anhydride-modified heparin is biocompatible and biodegradable with no anticoagulant activity; (ii) single-chain variable fragment anti-EGFR antibody (ScFvEGFR) was conjugated to the nanoparticles as an EGFR-targeting ligand.	Heparin	109-116	epidermal growth factor receptor	Homo sapiens	225-229
22032622-3	2011	This nanoparticle delivery system possesses the following unique properties: (i) succinic anhydride-modified heparin is biocompatible and biodegradable with no anticoagulant activity; (ii) single-chain variable fragment anti-EGFR antibody (ScFvEGFR) was conjugated to the nanoparticles as an EGFR-targeting ligand.	Heparin	109-116	epidermal growth factor receptor	Homo sapiens	244-248
21906873-0	2011	Low molecular weight heparin inhibits melanoma cell adhesion and migration through a PKCa/JNK signaling pathway inducing actin cytoskeleton changes.	Heparin	21-28	protein kinase C alpha	Homo sapiens	85-89
21906873-0	2011	Low molecular weight heparin inhibits melanoma cell adhesion and migration through a PKCa/JNK signaling pathway inducing actin cytoskeleton changes.	Heparin	21-28	mitogen-activated protein kinase 8	Homo sapiens	90-93
22082677-9	2011	Western blot analysis demonstrated that heparin induced shedding of the N-terminus of Flt-1 both in vivo and in vitro as indicated by a predominant band of 100-112 kDa.	Heparin	40-47	fms related receptor tyrosine kinase 1	Homo sapiens	86-91
22082677-10	2011	By using an in vitro angiogenesis assay, we demonstrated that serum of heparin-treated cases inhibited both basal and vascular endothelial growth factor-induced capillary-like tube formation.	Heparin	71-78	vascular endothelial growth factor A	Homo sapiens	118-152
22082677-11	2011	CONCLUSIONS: Heparin likely increases the maternal sFlt-1 through shedding of the extracellular domain of Flt-1 receptor.	Heparin	13-20	fms related receptor tyrosine kinase 1	Homo sapiens	52-57
22089237-4	2011	We demonstrate that EGFR transactivation and downstream ERK activation depends on increased shedding of heparin-binding EGF.	Heparin	104-111	epidermal growth factor receptor	Homo sapiens	20-24
22089237-4	2011	We demonstrate that EGFR transactivation and downstream ERK activation depends on increased shedding of heparin-binding EGF.	Heparin	104-111	mitogen-activated protein kinase 1	Homo sapiens	56-59
21995946-1	2011	The cytosolic chaperonin TRiC was isolated from ovine testes using ultracentrifugation and heparin-Sepharose chromatography.	Heparin	91-98	MARVEL domain containing 2	Homo sapiens	25-29
21981655-0	2011	Heparin promotes soluble VEGF receptor expression in human placental villi to impair endothelial VEGF signaling.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	25-29
21315618-7	2011	MEASUREMENTS AND MAIN RESULTS: The present results show that the prothrombin time (PT) and fibrinogen measurements are altered significantly by heparin concentrations above 2 IU/mL.	Heparin	144-151	fibrinogen beta chain	Homo sapiens	91-101
21315618-18	2011	In particular, fibrinogen values are falsely low at heparin levels of 2 IU/mL and above.	Heparin	52-59	fibrinogen beta chain	Homo sapiens	15-25
21956413-7	2011	INTERVENTIONS: Glucose-induced insulin response was assessed on three occasions after 4 h saline (low insulin/sham) or isoglycemic-hyperinsulinemic (high insulin) clamps with or without intralipid and heparin infusion, using B28 Asp-insulin that could be distinguished from endogenous insulin immunologically.	Heparin	201-208	insulin	Homo sapiens	31-38
21956413-12	2011	After preexposure to insulin with intralipid/heparin infusion to maintain FFA concentration, GSIS was 21% higher compared with sham clamp (P &lt; 0.04) and similar to preexposure to insulin without intralipid/heparin (P = 0.2).	Heparin	209-216	insulin	Homo sapiens	21-28
21914461-7	2011	Angiotensin II and LPA induced EGF receptor transactivation as evidenced by Akt/PKB phosphorylation through metalloproteinase-catalyzed membrane shedding of heparin-binding EGF and autocrine/paracrine activation of EGF receptors.	Heparin	157-164	angiotensinogen	Homo sapiens	0-14
21914461-7	2011	Angiotensin II and LPA induced EGF receptor transactivation as evidenced by Akt/PKB phosphorylation through metalloproteinase-catalyzed membrane shedding of heparin-binding EGF and autocrine/paracrine activation of EGF receptors.	Heparin	157-164	epidermal growth factor receptor	Homo sapiens	31-43
21885262-8	2011	The results indicated reasonably that the 15-mer aptamer bound to fibrinogen-binding site of thrombin using a G-quadruplex structure and was dominated by electrostatic interactions, while the 29-mer aptamer bound to heparin-binding site thrombin using a duplex structure and was driven mainly by hydrophobic effects.	Heparin	216-223	coagulation factor II, thrombin	Homo sapiens	93-101
21885262-8	2011	The results indicated reasonably that the 15-mer aptamer bound to fibrinogen-binding site of thrombin using a G-quadruplex structure and was dominated by electrostatic interactions, while the 29-mer aptamer bound to heparin-binding site thrombin using a duplex structure and was driven mainly by hydrophobic effects.	Heparin	216-223	coagulation factor II, thrombin	Homo sapiens	237-245
21981655-0	2011	Heparin promotes soluble VEGF receptor expression in human placental villi to impair endothelial VEGF signaling.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	97-101
22107692-7	2011	In the heparin group, the post-filter serum MPO levels were significantly higher than the pre-filter (median 49.0 vs. 60.5 ng/mL, P&lt;0.05) at 6 h. There were no significant differences between pre- and post-dialyzer MPO levels in the citrate group.	Heparin	7-14	myeloperoxidase	Homo sapiens	44-47
21615240-5	2011	CART analysis showed that CHADS(2) &gt; 2, history of stroke/TIA, no preoperative use of aspirin and preoperative use of low molecular weight heparins were associated with an increased risk of stroke (area under the ROC curve of 0.77).	Heparin	142-150	CART prepropeptide	Homo sapiens	0-4
22107692-7	2011	In the heparin group, the post-filter serum MPO levels were significantly higher than the pre-filter (median 49.0 vs. 60.5 ng/mL, P&lt;0.05) at 6 h. There were no significant differences between pre- and post-dialyzer MPO levels in the citrate group.	Heparin	7-14	myeloperoxidase	Homo sapiens	218-221
22110207-5	2011	RESULTS: Mouse 4T1 cells expressed ADAMTS1 and its substrates amphiregulin and heparin-binding EGF.	Heparin	79-86	a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1	Mus musculus	35-42
22122911-4	2011	A peptide including the HBM of PvDBP had similar affinity for heparin as RANTES and V3 loop peptides, and could be specifically inhibited from heparin binding by the same polyanions that inhibit DBP binding to DARC.	Heparin	62-69	D-box binding PAR bZIP transcription factor	Homo sapiens	33-36
22122911-4	2011	A peptide including the HBM of PvDBP had similar affinity for heparin as RANTES and V3 loop peptides, and could be specifically inhibited from heparin binding by the same polyanions that inhibit DBP binding to DARC.	Heparin	143-150	D-box binding PAR bZIP transcription factor	Homo sapiens	33-36
22122911-6	2011	Three other members of the DBP family have an HBM sequence that is necessary for erythrocyte binding, however only the protein which binds to DARC, the P. knowlesi alpha protein, is inhibited by heparin from binding to erythrocytes.	Heparin	195-202	D-box binding PAR bZIP transcription factor	Homo sapiens	27-30
21931955-8	2011	The binding affinities of these heparins to antithrombin III and thrombin were evaluated by using a surface plasmon resonance competitive binding assay.	Heparin	32-40	coagulation factor II, thrombin	Homo sapiens	48-56
21860019-3	2011	Heparin prevents mucin binding to P- and L-selectin and mucin-induced microthrombi.	Heparin	0-7	selectin, lymphocyte	Mus musculus	41-51
22015869-6	2011	RESULTS: Low molecular weight heparin improved basal trophoblast migration and induced potent increases in growth-regulated oncogene-alpha and soluble FMS-like tyrosine kinase-1.	Heparin	30-37	fms related receptor tyrosine kinase 1	Homo sapiens	151-177
21742756-3	2011	The study assessed the effects of heparin-coated CPB systems on the level and function of fibrinogen as measured by thromboelastography (TEG), as compared with non-coated systems.	Heparin	34-41	fibrinogen beta chain	Homo sapiens	90-100
21736375-5	2011	SOS binds thrombin with a K(d) of ~1.4 muM, comparable to that of the much larger polymeric heparin measured under the same conditions.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	10-18
21799400-6	2011	Lag time, time to peak and peak height of thrombin generation in neonatal cord samples were significantly less affected by different heparin concentrations than in adult samples, whereas the impact on reduction of endogenous thrombin potential was higher in neonatal cord samples.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	42-50
21741028-0	2011	Heparin protects against septic mortality via apoE-antagonism.	Heparin	0-7	apolipoprotein E	Mus musculus	46-50
21741028-3	2011	To determine whether apoE antagonism would protect against septic mortality in mice, apoE-LDLR binding was antagonized using heparin, which can inhibit apoE"s LDLR-binding site.	Heparin	125-132	apolipoprotein E	Mus musculus	85-89
21741028-3	2011	To determine whether apoE antagonism would protect against septic mortality in mice, apoE-LDLR binding was antagonized using heparin, which can inhibit apoE"s LDLR-binding site.	Heparin	125-132	apolipoprotein E	Mus musculus	85-89
21741028-9	2011	LDLR+/+ fibroblasts displayed decreased uptake of apoE when treated concurrently with heparin for 12 hours.	Heparin	86-93	apolipoprotein E	Mus musculus	50-54
21496084-10	2011	The addition of heparin significantly reduced levels of IGF-1, TNF-alpha and TGF-beta, and significantly elevated levels of IL-1ra.	Heparin	16-23	tumor necrosis factor	Equus caballus	63-72
22053247-10	2011	RESULTS: The combination of rhPDGF-BB and heparin stimulated alkaline phosphatase activity and OCN mRNA expression in osteoblastic cells ((*)P&lt;.05 and (**)P&lt;.001).	Heparin	42-49	bone gamma-carboxyglutamate protein	Homo sapiens	95-98
21676168-2	2011	Heparin is the mostly clinically used anticoagulant/antithrombotic drug, and has recently been shown to exhibit antimetastatic and anti-inflammatory activities that are linked to inhibition of P-selectin and/or L-selectin.	Heparin	0-7	selectin, platelet	Mus musculus	193-203
21676168-2	2011	Heparin is the mostly clinically used anticoagulant/antithrombotic drug, and has recently been shown to exhibit antimetastatic and anti-inflammatory activities that are linked to inhibition of P-selectin and/or L-selectin.	Heparin	0-7	selectin, lymphocyte	Mus musculus	211-221
21959589-2	2011	C1 inhibitor inhibits thrombin with a low second-order rate constant that can be increased by heparin.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	22-30
21959589-10	2011	Our results indicate that C1 inhibitor can inhibit thrombin activity on vascular endothelium via binding to selectins and potentiation by heparins.	Heparin	138-146	coagulation factor II, thrombin	Homo sapiens	51-59
21728235-2	2011	An atmospheric pressure glow discharge generator is used to activate the PSf membrane surface, with subsequent chemical binding of heparin in the presence of EDC and NHS.	Heparin	131-138	insulin like growth factor binding protein 7	Homo sapiens	73-76
21924126-3	2011	The first objective of our study was to measure and to characterize the kinetic profile of bradykinin release in human plasma incubated with OSCS and contaminated heparin.	Heparin	163-170	kininogen 1	Homo sapiens	91-101
21826315-4	2011	Here we show that VEGF covalently bound through a modified heparin molecule elicits an extended response of pVEGFR-2 in human umbilical vein endothelial cells (HUVECs) and that the covalent linkage reduces internalization of the growth factor during receptor endocytosis.	Heparin	59-66	vascular endothelial growth factor A	Homo sapiens	18-22
21826315-5	2011	Optical tweezer measurements show that the rupture force required to disrupt the heparin-VEGF-VEGFR-2 interaction increases from 3-8 pN to 6-12 pN when a covalent bond is introduced between VEGF and heparin.	Heparin	81-88	vascular endothelial growth factor A	Homo sapiens	89-93
21826315-5	2011	Optical tweezer measurements show that the rupture force required to disrupt the heparin-VEGF-VEGFR-2 interaction increases from 3-8 pN to 6-12 pN when a covalent bond is introduced between VEGF and heparin.	Heparin	81-88	vascular endothelial growth factor A	Homo sapiens	94-98
21826315-6	2011	Importantly, by covalently binding VEGF to a heparin substrate, the stability (half-life) of VEGF is extended over three-fold.	Heparin	45-52	vascular endothelial growth factor A	Homo sapiens	35-39
21826315-6	2011	Importantly, by covalently binding VEGF to a heparin substrate, the stability (half-life) of VEGF is extended over three-fold.	Heparin	45-52	vascular endothelial growth factor A	Homo sapiens	93-97
21801147-4	2011	These include binding of heparin to angiogenic growth factors (e.g., basic fibroblast growth factor and vascular endothelial growth factor); modulation of tissue factor (TF); and enhanced TF-pathway-inhibitor release, and inhibition of matrix-degrading enzymes.	Heparin	25-32	vascular endothelial growth factor A	Homo sapiens	104-138
21736375-9	2011	In the X-ray crystal structure, two molecules of SOS are bound nonequivalently to exosite II portions of a thrombin dimer, in contrast to the 1:2 stoichiometry of the heparin-thrombin complex, which has a different monomer association mode in the dimer.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	175-183
21736375-10	2011	SOS and heparin binding to exosite II of thrombin differ on both chemical and structural levels and, perhaps most significantly, in thrombin inhibition.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	41-49
21736375-10	2011	SOS and heparin binding to exosite II of thrombin differ on both chemical and structural levels and, perhaps most significantly, in thrombin inhibition.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	132-140
21642433-7	2011	Using quartz crystal microbalance analysis, we show that heparin binds to thrombin, thereby inhibiting thrombin-induced expression of Twist and miR-10b.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	74-82
21659867-4	2011	RECENT FINDINGS: Heparin, a thrombin inhibitor, is still the drug of choice for preventing coagulation following, for example, cardiovascular surgery.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	28-36
21773727-9	2011	A solution competition SPR study was performed to test the ability of different O-acylated LMWHP derivatives to inhibit fibroblast growth factor (FGF) 1 and FGF2 binding to surface-immobilized heparin.	Heparin	193-200	fibroblast growth factor 2	Bos taurus	157-161
21659541-1	2011	Platelet factor 4 (PF4) and heparin (H) form PF4/H complexes, the target of the immune reaction in heparin-induced thrombocytopenia (HIT).	Heparin	28-35	platelet factor 4	Mus musculus	45-48
21659541-1	2011	Platelet factor 4 (PF4) and heparin (H) form PF4/H complexes, the target of the immune reaction in heparin-induced thrombocytopenia (HIT).	Heparin	99-106	platelet factor 4	Mus musculus	0-17
21659541-1	2011	Platelet factor 4 (PF4) and heparin (H) form PF4/H complexes, the target of the immune reaction in heparin-induced thrombocytopenia (HIT).	Heparin	99-106	platelet factor 4	Mus musculus	19-22
21659541-1	2011	Platelet factor 4 (PF4) and heparin (H) form PF4/H complexes, the target of the immune reaction in heparin-induced thrombocytopenia (HIT).	Heparin	99-106	platelet factor 4	Mus musculus	45-48
21659541-2	2011	HIT seems to be a secondary immune response as anti-PF4/H-IgG antibodies occur as early as day 4 of heparin treatment.	Heparin	100-107	platelet factor 4	Mus musculus	52-55
21550426-0	2011	Heparin-decorated, hyaluronic acid-based hydrogel particles for the controlled release of bone morphogenetic protein 2.	Heparin	0-7	bone morphogenetic protein 2	Mus musculus	90-118
21600196-9	2011	In addition, a variety of known UB branching morphogens (i.e., pleiotrophin, heregulin, FGF1 and GDNF) were found to have a higher affinity for 6-O sulfated heparin providing additional support for the notion that this HS modification is important for robust UB branching morphogenesis.	Heparin	157-164	fibroblast growth factor 1	Mus musculus	88-92
21416466-2	2011	A new method to follow loss in heparin binding to the serine protease inhibitor, antithrombin III, and the serine protease, thrombin, was developed using a surface plasmon resonance competitive binding assay.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	54-69
21416466-2	2011	A new method to follow loss in heparin binding to the serine protease inhibitor, antithrombin III, and the serine protease, thrombin, was developed using a surface plasmon resonance competitive binding assay.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	85-93
21416466-6	2011	It is this sulfo group loss that probably accounts for a decrease in the binding of autoclaved heparin to antithrombin III and thrombin as well as the observed decrease in its amidolytic activity.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	110-118
21642433-7	2011	Using quartz crystal microbalance analysis, we show that heparin binds to thrombin, thereby inhibiting thrombin-induced expression of Twist and miR-10b.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	103-111
21642433-9	2011	Interestingly, we find that heparin attenuates miR-10b expression and induces HoxD10 expression in vivo to inhibit angiogenesis and impair the growth of MDA-MB-231 tumor xenografts.	Heparin	28-35	homeobox D10	Homo sapiens	78-84
21565253-11	2011	Heparin-assisted cell-PMCA of vCJD represents a significant step toward detecting very minute amounts of PrP(Sc) in the body fluids of asymptomatic vCJD patients.	Heparin	0-7	prion protein	Homo sapiens	105-108
21672195-9	2011	HD5 and HD6 blocked anti-HIV activities of soluble glycosaminoglycans including heparin, chondroitin sulfate, and dextran sulfate.	Heparin	80-87	defensin alpha 5	Homo sapiens	0-3
21833458-2	2011	Heparin and dermatan sulfate (DS) bind and block P- and L-selectin function in vitro.	Heparin	0-7	selectin, lymphocyte	Mus musculus	56-66
21577096-0	2011	Differential coagulation inhibitory effect of fondaparinux, enoxaparin and unfractionated heparin in cell models of thrombin generation.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	116-124
21577096-6	2011	Thrombin generation inhibition was dose-dependent with a differential effect according to the drug: the highest for UFH, the lowest for fondaparinux.	Heparin	116-119	coagulation factor II, thrombin	Homo sapiens	0-8
21555785-0	2011	Mechanism of amylin fibrillization enhancement by heparin.	Heparin	50-57	islet amyloid polypeptide	Mus musculus	13-19
21555785-1	2011	We characterized the interaction of amylin with heparin fragments of defined length, which model the glycosaminoglycan chains associated with amyloid deposits found in type 2 diabetes.	Heparin	48-55	islet amyloid polypeptide	Mus musculus	36-42
21555785-2	2011	Binding of heparin fragments to the positively charged N-terminal half of monomeric amylin depends on the concentration of negatively charged saccharides but is independent of oligosaccharide length.	Heparin	11-18	islet amyloid polypeptide	Mus musculus	84-90
21555785-4	2011	The length dependence suggests that the negatively charged helical structure of heparin electrostatically complements the positively charged surface of the fibrillar amylin cross-beta structure.	Heparin	80-87	islet amyloid polypeptide	Mus musculus	166-172
21555785-5	2011	Fluorescence resonance energy transfer and total internal reflection fluorescence microscopy experiments indicate that heparin associates with amylin fibrils, rather than enhancing fibrillogenesis catalytically.	Heparin	119-126	islet amyloid polypeptide	Mus musculus	143-149
21555785-6	2011	Short heparin fragments containing two- or eight-saccharide monomers protect against amylin cytotoxicity toward a MIN6 mouse cell model of pancreatic beta-cells.	Heparin	6-13	islet amyloid polypeptide	Mus musculus	85-91
21562164-7	2011	Heparin promoted tryptase tetramer formation and protected tryptase from degradation by CTSB and CTSL.	Heparin	0-7	cathepsin L	Homo sapiens	97-101
21672195-10	2011	However, heparin, at a high concentration, diminished the HIV enhancing effect of HD5, but not HD6.	Heparin	9-16	defensin alpha 5	Homo sapiens	82-85
21482826-1	2011	HIV-1 p17 contains C- and N-terminal sequences with positively charged residues and a consensus cluster for heparin binding.	Heparin	108-115	family with sequence similarity 72 member B	Homo sapiens	6-9
21545128-0	2011	Dynamics of a heparin-binding domain of VEGF(165) complexed with its inhibitor triamterene.	Heparin	14-21	vascular endothelial growth factor A	Homo sapiens	40-44
21545128-2	2011	It is known that Abeta binds to the heparin-binding domain (HBD) of the 165-amino acid VEGF variant, VEGF(165).	Heparin	36-43	amyloid beta precursor protein	Homo sapiens	17-22
21545128-2	2011	It is known that Abeta binds to the heparin-binding domain (HBD) of the 165-amino acid VEGF variant, VEGF(165).	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	87-91
21545128-2	2011	It is known that Abeta binds to the heparin-binding domain (HBD) of the 165-amino acid VEGF variant, VEGF(165).	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	101-105
21482826-2	2011	We have previously demonstrated by affinity chromatography that HIV-1 p17 binds strongly to heparin-agarose at physiological pH and to human activated CD4(+) T cells.	Heparin	92-99	family with sequence similarity 72 member B	Homo sapiens	70-73
20211924-6	2011	Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined.	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	4-12
21622289-5	2011	For example, heparin modulates the binding of FGF-2 to its tyrosine kinase receptor during tumor proliferation, and the binding of growth factors involved in epithelial to mesenchymal transition during tumor invasion.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	46-51
21611915-8	2011	Elevated laboratory parameters were observed in both treatment groups for thrombin time which is very likely attributable to the therapy with low molecular weight heparin, due to the substantially parallel course of this parameter in both treatment groups.	Heparin	163-170	coagulation factor II, thrombin	Homo sapiens	74-82
21220249-5	2011	Like heparin, thrombin and FXa cause an increase in IGF-I in ESCs, suggesting an action of heparin independent from its anticoagulatory effects.	Heparin	5-12	insulin like growth factor 1	Homo sapiens	52-57
21220249-5	2011	Like heparin, thrombin and FXa cause an increase in IGF-I in ESCs, suggesting an action of heparin independent from its anticoagulatory effects.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	14-22
21220249-5	2011	Like heparin, thrombin and FXa cause an increase in IGF-I in ESCs, suggesting an action of heparin independent from its anticoagulatory effects.	Heparin	91-98	insulin like growth factor 1	Homo sapiens	52-57
21845882-0	2011	[Effects of ambroxol combined with low-dose heparin on TNF-alpha and IL-1beta in rabbits with acute lung injury].	Heparin	44-51	interleukin-1 beta	Oryctolagus cuniculus	69-77
21296829-0	2011	Suppression of choroidal neovascularization and quantitative and qualitative inhibition of VEGF and CCL2 by heparin.	Heparin	108-115	vascular endothelial growth factor A	Homo sapiens	91-95
21296829-9	2011	Relative decreases in VEGF and CCL2 levels were observed in media of ARPE19 cells at higher heparin concentrations.	Heparin	92-99	vascular endothelial growth factor A	Homo sapiens	22-26
21296829-12	2011	Reduced VEGF and CCL2 secretion by RPE cells and suppression of VEGF-VEGFR2 and CCL2-CCR2 interactions at the laser site mediated by heparin may contribute to the pharmacologic effect.	Heparin	133-140	vascular endothelial growth factor A	Homo sapiens	64-68
21548923-8	2011	The synthesized aFGF was purified by heparin-affinity chromatography and its mitogenic activity on NIH 3T3 cells confirmed to be similar to a commercial product.	Heparin	37-44	fibroblast growth factor 1	Mus musculus	16-20
21685696-7	2011	CONCLUSION: Transplantation of hepatic stem cells combined with heparin can promote the liver recovery in rats with acute liver injury induced by CCl4.	Heparin	64-71	C-C motif chemokine ligand 4	Rattus norvegicus	146-150
21845882-1	2011	OBJECTIVE: To investigate the intervention and mechanism of ambroxol combined with low-dose heparin on oxidative stress, TNF-alpha and IL-1beta in rabbits with acute lung injury (ALI).	Heparin	92-99	interleukin-1 beta	Oryctolagus cuniculus	135-143
21845882-16	2011	Ambroxol combined with low-dose heparin can reduce lung cells oxidative stress to inhibit the release of IL-1beta and TNF-alpha, which play a role in the treatment of ALI.	Heparin	32-39	interleukin-1 beta	Oryctolagus cuniculus	105-113
22477834-1	2011	Bivalirudin is a direct thrombin inhibitor approved for use in adult patients with heparin-induced thrombocytopenia (HIT) undergoing percutaneous coronary intervention.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	24-32
21343305-6	2011	We demonstrate that VEGF-C binds to heparan sulfate purified from primary lymphatic endothelia, and activation of lymphatic endothelial Erk1/2 in response to VEGF-C is reduced by interference with heparin or pretreatment of cells with heparinase, which destroys heparan sulfate.	Heparin	197-204	vascular endothelial growth factor C	Mus musculus	20-26
21343305-6	2011	We demonstrate that VEGF-C binds to heparan sulfate purified from primary lymphatic endothelia, and activation of lymphatic endothelial Erk1/2 in response to VEGF-C is reduced by interference with heparin or pretreatment of cells with heparinase, which destroys heparan sulfate.	Heparin	197-204	vascular endothelial growth factor C	Mus musculus	158-164
21343308-3	2011	Thrombospondin-1 bound in a heparin-inhibitable manner to this proteoglycan and to a soluble form released into the medium.	Heparin	28-35	thrombospondin 1	Homo sapiens	0-16
20558775-0	2011	Heparin inhibits pulmonary artery smooth muscle cell proliferation through guanine nucleotide exchange factor-H1/RhoA/Rho kinase/p27.	Heparin	0-7	Rho-associated coiled-coil containing protein kinase 2	Mus musculus	118-128
21415391-0	2011	Local retention versus systemic release of soluble VEGF receptor-1 are mediated by heparin-binding and regulated by heparanase.	Heparin	83-90	vascular endothelial growth factor A	Homo sapiens	51-55
21346090-1	2011	Fibroblast growth factor 21 (FGF21) was originally identified as a member of the FGF family in homology studies and is a member of the endocrine FGF subfamily that lacks heparin binding domains and is released into the circulation.	Heparin	170-177	fibroblast growth factor 21	Homo sapiens	29-32
21185801-3	2011	Using a combination of biophysical and functional assays, we found that the fluorescently labeled mutant aFGF is characterized by essentially the same global folding, mitogenic activity, and association behavior with heparin, its physiological activator, as the unlabeled wild-type protein.	Heparin	217-224	fibroblast growth factor 1	Homo sapiens	105-109
21185801-4	2011	We used this new tracer protein mutant to determine the association behavior of aFGF with heparin in the presence of high concentrations of albumin that mimicked more closely the plasma medium in which aFGF is naturally located and in which it has evolved to function.	Heparin	90-97	fibroblast growth factor 1	Homo sapiens	80-84
21185801-5	2011	By exposing the aFGF-Cys2-heparin complex to increasing concentrations of albumin up to physiological plasma levels, we were able to demonstrate that macromolecular crowding does not affect the stoichiometry of the interaction.	Heparin	26-33	fibroblast growth factor 1	Homo sapiens	16-20
22477834-3	2011	As heparin products produce great inter- and intraindividual variability in pediatric patients, often due to decreased anti-thrombin concentrations in the first year of life, some practitioners have turned to direct thrombin inhibitors, such as bivalirudin, for more predictable pharmacokinetics and effects on bound and circulating thrombin.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	124-132
22477834-3	2011	As heparin products produce great inter- and intraindividual variability in pediatric patients, often due to decreased anti-thrombin concentrations in the first year of life, some practitioners have turned to direct thrombin inhibitors, such as bivalirudin, for more predictable pharmacokinetics and effects on bound and circulating thrombin.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	216-224
22477834-3	2011	As heparin products produce great inter- and intraindividual variability in pediatric patients, often due to decreased anti-thrombin concentrations in the first year of life, some practitioners have turned to direct thrombin inhibitors, such as bivalirudin, for more predictable pharmacokinetics and effects on bound and circulating thrombin.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	216-224
21447157-3	2011	Beside the well-known stabilization of FGF2 by heparin or heparan sulphate, the recently discovered binding to ATP also shows a stabilizing and protective effect on this growth factor.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	39-43
20542267-0	2011	Heparin inhibits interferon-gamma signaling in human endometrial stromal cells by interference with the cellular binding of interferon-gamma.	Heparin	0-7	interferon gamma	Homo sapiens	17-33
21552458-10	2011	The presented study gives first hints that direct thrombin inhibitors may help prevent heparin-induced negative effects on bone metabolism.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	50-58
20542267-0	2011	Heparin inhibits interferon-gamma signaling in human endometrial stromal cells by interference with the cellular binding of interferon-gamma.	Heparin	0-7	interferon gamma	Homo sapiens	124-140
20542267-1	2011	OBJECTIVE: To examine the impact of heparins on interferon-gamma (IFN-gamma) signaling in human endometrial stromal cells (ESCs) in vitro.	Heparin	36-44	interferon gamma	Homo sapiens	48-64
20542267-1	2011	OBJECTIVE: To examine the impact of heparins on interferon-gamma (IFN-gamma) signaling in human endometrial stromal cells (ESCs) in vitro.	Heparin	36-44	interferon gamma	Homo sapiens	66-75
20542267-9	2011	RESULT(S): Heparin and LMWHs inhibit the IFN-gamma-mediated induction of IRF-1, but not Nmi in undifferentiated and decidualized ESCs.	Heparin	11-18	interferon gamma	Homo sapiens	41-50
20542267-9	2011	RESULT(S): Heparin and LMWHs inhibit the IFN-gamma-mediated induction of IRF-1, but not Nmi in undifferentiated and decidualized ESCs.	Heparin	11-18	interferon regulatory factor 1	Homo sapiens	73-78
20542267-11	2011	Heparin has no effect on the IFN-gamma receptor in ESCs, but inhibits the binding of IFN-gamma to the cells.	Heparin	0-7	interferon gamma	Homo sapiens	85-94
20542267-12	2011	CONCLUSION(S): Unfractionated heparin, as well as LMWHs, are able to inhibit IFN-gamma signaling in human ESCs and therefore might be clinically interesting agents to modulate the actions of this proinflammatory cytokine at the implantation site.	Heparin	30-37	interferon gamma	Homo sapiens	77-86
21227626-7	2011	The results showed that low-molecular-weight heparin oral colon-specific delivery capsule significantly decreased the serum levels of TNF-alpha, IL-6 as well as FXa, while increased the expression of Musashi-1 in colon compared with acetic acid-induced ulcerative colitis model group.	Heparin	45-52	tumor necrosis factor	Mus musculus	134-143
21679503-12	2011	UFH or LMWH inhibited tumor necrosis factor alpha (10 ng/mL)-induced secretion of MUC5AC and IL-8 from NCI-H292 cells in a dose-dependent manner (0.01-10 IU/mL).	Heparin	0-3	tumor necrosis factor	Homo sapiens	22-49
21679503-12	2011	UFH or LMWH inhibited tumor necrosis factor alpha (10 ng/mL)-induced secretion of MUC5AC and IL-8 from NCI-H292 cells in a dose-dependent manner (0.01-10 IU/mL).	Heparin	0-3	C-X-C motif chemokine ligand 8	Homo sapiens	93-97
21679503-14	2011	CONCLUSION: These results indicate that heparin inhibits airway mucus hypersecretion in airway epithelial cells directly and indirectly through the suppression of IL-8 secretion and neutrophil infiltration.	Heparin	40-47	C-X-C motif chemokine ligand 8	Homo sapiens	163-167
21227626-7	2011	The results showed that low-molecular-weight heparin oral colon-specific delivery capsule significantly decreased the serum levels of TNF-alpha, IL-6 as well as FXa, while increased the expression of Musashi-1 in colon compared with acetic acid-induced ulcerative colitis model group.	Heparin	45-52	interleukin 6	Mus musculus	145-149
21182858-5	2011	In vitro coagulation time tests showed that the activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) of the heparin-modified scaffolds were much higher than those of the pure silk fibroin scaffolds.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	94-105
21080029-4	2011	FGFRL1 binds to FGF ligands and heparin with high affinity.	Heparin	32-39	fibroblast growth factor receptor like 1	Homo sapiens	0-6
21182858-5	2011	In vitro coagulation time tests showed that the activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) of the heparin-modified scaffolds were much higher than those of the pure silk fibroin scaffolds.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	97-105
21386996-0	2011	PKCalpha and PKCdelta regulate ADAM17-mediated ectodomain shedding of heparin binding-EGF through separate pathways.	Heparin	70-77	protein kinase C alpha	Homo sapiens	0-8
21174001-8	2011	Thus, under high shear conditions and excessive thrombin generation as they occur in atherosclerotic vascular compartments and acute vascular syndromes, heparin and bivalirudin inhibit thrombin-induced platelet adhesion and aggregation to a similar extent, while they have opposite effects on platelet adhesion in the absence of thrombin.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	48-56
21174001-8	2011	Thus, under high shear conditions and excessive thrombin generation as they occur in atherosclerotic vascular compartments and acute vascular syndromes, heparin and bivalirudin inhibit thrombin-induced platelet adhesion and aggregation to a similar extent, while they have opposite effects on platelet adhesion in the absence of thrombin.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	185-193
21174001-8	2011	Thus, under high shear conditions and excessive thrombin generation as they occur in atherosclerotic vascular compartments and acute vascular syndromes, heparin and bivalirudin inhibit thrombin-induced platelet adhesion and aggregation to a similar extent, while they have opposite effects on platelet adhesion in the absence of thrombin.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	185-193
21159365-0	2011	The contribution of tissue factor pathway inhibitor to thrombin generation in children receiving unfractionated heparin.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	55-63
21174001-7	2011	Thrombin-inducible platelet adhesion and size of aggregates was equally inhibited by heparin and bivalirudin.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	0-8
21048158-0	2011	Development of a recombinant antithrombin variant as a potent antidote to fondaparinux and other heparin derivatives.	Heparin	97-104	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	29-41
21048158-3	2011	To make the use of fondaparinux safer, we developed an antithrombin (AT) variant as a potent antidote to heparin derivatives.	Heparin	105-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	55-67
21048158-3	2011	To make the use of fondaparinux safer, we developed an antithrombin (AT) variant as a potent antidote to heparin derivatives.	Heparin	105-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	69-71
21347292-10	2011	The pre-incubation with CB1 or TRPV1 antagonists inhibited heparin-induced sperm capacitation; moreover the activity of FAAH was 30% lower in heparin-capacitated spermatozoa as compared to control conditions.	Heparin	59-66	TRPV1	Bos taurus	31-36
21048158-4	2011	This variant (AT-N135Q-Pro394) combines 2 mutations: substitution of Asn135 by a Gln to remove a glycosylation site and increase affinity for heparins, and the insertion of a Pro between Arg393 and Ser394 to abolish its anticoagulant activity.	Heparin	142-150	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	14-16
21347292-10	2011	The pre-incubation with CB1 or TRPV1 antagonists inhibited heparin-induced sperm capacitation; moreover the activity of FAAH was 30% lower in heparin-capacitated spermatozoa as compared to control conditions.	Heparin	142-149	TRPV1	Bos taurus	31-36
21289173-8	2011	Heparin, which antagonizes HSPG, significantly inhibited cellular Abeta uptake.	Heparin	0-7	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	27-31
21104785-1	2011	The heparin-degrading endosulfatases sulfatase 1 (SULF1) and sulfatase 2 (SULF2) have opposing effects in hepatocarcinogenesis despite structural similarity.	Heparin	4-11	sulfatase 1	Homo sapiens	37-48
21074845-0	2011	The use of low molecular weight heparin-pluronic nanogels to impede liver fibrosis by inhibition the TGF-beta/Smad signaling pathway.	Heparin	32-39	transforming growth factor, beta 1	Rattus norvegicus	101-109
21226633-10	2011	In primary PCI, bivalirudin has the advantage over UFH of inhibiting clot bound thrombin and reduces bleeding and mortality compared with the use of UFH plus glycoprotein IIb/IIIa inhibitors.	Heparin	51-54	coagulation factor II, thrombin	Homo sapiens	80-88
21104785-1	2011	The heparin-degrading endosulfatases sulfatase 1 (SULF1) and sulfatase 2 (SULF2) have opposing effects in hepatocarcinogenesis despite structural similarity.	Heparin	4-11	sulfatase 1	Homo sapiens	50-55
21095260-3	2011	Since HMGB1 also exhibits heparin-binding activity, we investigated whether heparin interferes with HMGB1/RAGE interaction and prevents the cytokine activity.	Heparin	76-83	advanced glycosylation end product-specific receptor	Mus musculus	106-110
21095260-8	2011	The amount of HMGB1 and RAGE bound forms reduced after treatment with heparin.	Heparin	70-77	advanced glycosylation end product-specific receptor	Mus musculus	24-28
21095260-9	2011	ELISA revealed that addition of heparin inhibited the TNF-alpha and IL-6 released by macrophages RAW264.7 and HUVEC; 10 U/L and 50 U/L of heparin showed the most marked inhibitory effect in RAW264.7 cells and in HUVEC, respectively.	Heparin	32-39	tumor necrosis factor	Mus musculus	54-63
21095260-9	2011	ELISA revealed that addition of heparin inhibited the TNF-alpha and IL-6 released by macrophages RAW264.7 and HUVEC; 10 U/L and 50 U/L of heparin showed the most marked inhibitory effect in RAW264.7 cells and in HUVEC, respectively.	Heparin	32-39	interleukin 6	Mus musculus	68-72
21095260-9	2011	ELISA revealed that addition of heparin inhibited the TNF-alpha and IL-6 released by macrophages RAW264.7 and HUVEC; 10 U/L and 50 U/L of heparin showed the most marked inhibitory effect in RAW264.7 cells and in HUVEC, respectively.	Heparin	138-145	tumor necrosis factor	Mus musculus	54-63
21095260-9	2011	ELISA revealed that addition of heparin inhibited the TNF-alpha and IL-6 released by macrophages RAW264.7 and HUVEC; 10 U/L and 50 U/L of heparin showed the most marked inhibitory effect in RAW264.7 cells and in HUVEC, respectively.	Heparin	138-145	interleukin 6	Mus musculus	68-72
21095260-10	2011	In conclusion, heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE by changing the conformation of HMGB1.	Heparin	15-22	advanced glycosylation end product-specific receptor	Mus musculus	79-83
20959601-3	2011	These antibodies probably result from bacterial infections, as (1) PF4 bound charge-dependently to various bacteria, (2) human heparin-induced anti-PF4/heparin antibodies cross-reacted with PF4-coated Staphylococcus aureus and Escherichia coli, and (3) mice developed anti-PF4/heparin antibodies during polymicrobial sepsis without heparin application.	Heparin	127-134	platelet factor 4	Mus musculus	148-151
21093446-7	2011	Interleukin-8 is purified via cation exchange chromatography and heparin affinity chromatography using a single inexpensive buffer system.	Heparin	65-72	C-X-C motif chemokine ligand 8	Homo sapiens	0-13
21360640-0	2011	Heparin plays a key regulatory role via a p53/FAK-dependent signaling in melanoma cell adhesion and migration.	Heparin	0-7	tumor protein p53	Homo sapiens	42-45
21360640-6	2011	Moreover, heparin stimulated the p53 expression (P &lt;= 0.001) of M5 cells and its increased accumulation in the nucleus.	Heparin	10-17	tumor protein p53	Homo sapiens	33-36
21360640-8	2011	In conclusion, the results of this study clearly demonstrate that the action of heparin in the regulation of melanoma cell adhesion and migration involves a p53/FAK/signaling pathway, which may be of importance in molecular targeted therapy of the disease.	Heparin	80-87	tumor protein p53	Homo sapiens	157-160
21086021-1	2011	Heparin compounds, to include fractionated and unfractionated preparations, exert both antithrombotic and antiinflammatory effects through combined inhibition of factor Xa and thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	176-184
21076043-4	2011	Moreover, we observed a strong reduction of serum hepcidin in 5 patients treated with heparin to prevent deep vein thrombosis, which was accompanied by an increase of serum iron and a reduction of C-reactive protein levels.	Heparin	86-93	C-reactive protein	Homo sapiens	197-215
20980681-2	2011	We found that CXCL4L1 has lower affinity for heparin and chondroitin sulfate-E than platelet factor-4 (CXCL4) and showed that CXCL10 and CXCL4L1 could displace each other on microvascular endothelial cells.	Heparin	45-52	platelet factor 4 variant 1	Homo sapiens	14-21
20980681-2	2011	We found that CXCL4L1 has lower affinity for heparin and chondroitin sulfate-E than platelet factor-4 (CXCL4) and showed that CXCL10 and CXCL4L1 could displace each other on microvascular endothelial cells.	Heparin	45-52	platelet factor 4 variant 1	Homo sapiens	137-144
20801240-3	2011	An injectable, heparin-based hydrogel that has proved to be effective in the culture of chondrocytes as well as the sustained release of growth factor was employed to locally deliver fibrochondrocytes and osteoinductive bone morphogenetic protein-2 (BMP-2) into the FC region, to promote FC regeneration.	Heparin	15-22	bone morphogenetic protein 2	Mus musculus	220-248
20878965-1	2011	Heparin was covalently immobilized on PSf membranes to obtain a dialysis membrane with high affinity for LDL.	Heparin	0-7	insulin like growth factor binding protein 7	Homo sapiens	38-41
20886548-1	2011	In this study, we fabricated non-woven matrices using blends of polycaprolactone and gelatin with various spinning volumes to control the immobilized heparin content, which was ultimately intended to increase the immobilization efficiency of bFGF.	Heparin	150-157	fibroblast growth factor 2	Homo sapiens	242-246
20886548-2	2011	The amount of bFGF on the heparin conjugated fibrous matrices depended on the thicknesses of the swollen matrices ranging from 35.4 +- 6.5 to 162.3 +- 14.0 ng and  90% of the bFGF was gradually released over a period of up to 56 d. The released bFGF enhanced the proliferation of human umbilical vein endothelial cells and human mesenchymal stem cells.	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	14-18
20886548-2	2011	The amount of bFGF on the heparin conjugated fibrous matrices depended on the thicknesses of the swollen matrices ranging from 35.4 +- 6.5 to 162.3 +- 14.0 ng and  90% of the bFGF was gradually released over a period of up to 56 d. The released bFGF enhanced the proliferation of human umbilical vein endothelial cells and human mesenchymal stem cells.	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	175-179
20886548-2	2011	The amount of bFGF on the heparin conjugated fibrous matrices depended on the thicknesses of the swollen matrices ranging from 35.4 +- 6.5 to 162.3 +- 14.0 ng and  90% of the bFGF was gradually released over a period of up to 56 d. The released bFGF enhanced the proliferation of human umbilical vein endothelial cells and human mesenchymal stem cells.	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	175-179
20801240-3	2011	An injectable, heparin-based hydrogel that has proved to be effective in the culture of chondrocytes as well as the sustained release of growth factor was employed to locally deliver fibrochondrocytes and osteoinductive bone morphogenetic protein-2 (BMP-2) into the FC region, to promote FC regeneration.	Heparin	15-22	bone morphogenetic protein 2	Mus musculus	250-255
20801240-9	2011	In summary, the use of a heparin-based hydrogel for the local delivery of fibrochondrocytes and BMP-2 could accelerate the maturation and differentiation of LTB-specific FC tissues, and it was also possible to recreate the unique stratification of calcified FC and LIG tissues in a single porous PLCL scaffold in terms of both biochemical and biomechanical properties.	Heparin	25-32	bone morphogenetic protein 2	Mus musculus	96-101
21969185-4	2011	The difference of two main human PlGF isoforms, PlGF1 and PlGF2, consist in the exclusive ability of PlGF2 to bind heparin and Neuropilin receptors.	Heparin	115-122	placental growth factor	Homo sapiens	33-37
21969185-4	2011	The difference of two main human PlGF isoforms, PlGF1 and PlGF2, consist in the exclusive ability of PlGF2 to bind heparin and Neuropilin receptors.	Heparin	115-122	placental growth factor	Homo sapiens	58-63
21969185-4	2011	The difference of two main human PlGF isoforms, PlGF1 and PlGF2, consist in the exclusive ability of PlGF2 to bind heparin and Neuropilin receptors.	Heparin	115-122	placental growth factor	Homo sapiens	101-106
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	fibroblast growth factor 1	Homo sapiens	97-128
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	fibroblast growth factor 1	Homo sapiens	130-134
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	vascular endothelial growth factor A	Homo sapiens	137-171
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	vascular endothelial growth factor A	Homo sapiens	173-177
20827464-6	2011	These heparin-immobilized microspheres exhibited broad dynamic ranges for binding to the four cytokines (aFGF, 1.0-1,000 ng/mL; VEGF, 0.5-1,000 ng/mL; CCL2, 1.95-1,000 ng/mL; CCL5, 1.95-500 ng/mL).	Heparin	6-13	fibroblast growth factor 1	Homo sapiens	105-109
20827464-6	2011	These heparin-immobilized microspheres exhibited broad dynamic ranges for binding to the four cytokines (aFGF, 1.0-1,000 ng/mL; VEGF, 0.5-1,000 ng/mL; CCL2, 1.95-1,000 ng/mL; CCL5, 1.95-500 ng/mL).	Heparin	6-13	vascular endothelial growth factor A	Homo sapiens	128-132
21467632-3	2011	rGST-NKG2A and rGST-NKG2C directly bound to heparin-BSA with K(d) values of 20 and 40 nM, respectively.	Heparin	44-51	killer cell lectin like receptor C2	Homo sapiens	20-25
20964630-2	2011	Although HDGF was initially identified as a secretory heparin-binding protein, the biological significance of its heparin-binding ability remains to be determined.	Heparin	54-61	heparin binding growth factor	Mus musculus	9-13
22254265-1	2011	Bivalirudin is direct thrombin inhibitor used in patients with heparin-induced thrombocytopenia.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	22-30
21467632-4	2011	Binding of rGST-NKG2A and rGST-NKG2C to heparin-BSA was suppressed in the presence of soluble heparin, heparan sulfate, fucoidan, lambda-carrageenan, and dextran sulfate.	Heparin	40-47	killer cell lectin like receptor C2	Homo sapiens	31-36
21467632-4	2011	Binding of rGST-NKG2A and rGST-NKG2C to heparin-BSA was suppressed in the presence of soluble heparin, heparan sulfate, fucoidan, lambda-carrageenan, and dextran sulfate.	Heparin	94-101	killer cell lectin like receptor C2	Homo sapiens	31-36
21467632-5	2011	2-O-Sulfate residues in heparin were essential for the binding of rGST-NKG2A and rGST-NKG2C.	Heparin	24-31	killer cell lectin like receptor C2	Homo sapiens	86-91
21467632-7	2011	This is the first report showing that NKG2A and NKG2C bind to heparin and alpha2,3-NeuAc-containing glycoproteins.	Heparin	62-69	killer cell lectin like receptor C2	Homo sapiens	48-53
20566037-0	2011	Heparin-Conjugated PCL Scaffolds Fabricated by Electrospinning and Loaded with Fibroblast Growth Factor 2.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	79-105
21147877-4	2011	We used primary adult rat cardiomyocytes and demonstrate that adiponectin increased LPL translocation to the cell surface where it could be released at least partly in its active form, as evidenced by measuring basal and heparin-releasable LPL activity.	Heparin	221-228	lipoprotein lipase	Rattus norvegicus	84-87
21147877-4	2011	We used primary adult rat cardiomyocytes and demonstrate that adiponectin increased LPL translocation to the cell surface where it could be released at least partly in its active form, as evidenced by measuring basal and heparin-releasable LPL activity.	Heparin	221-228	lipoprotein lipase	Rattus norvegicus	240-243
20854434-8	2011	RESULTS: PBMC from individuals with hypersensitivity reactions to contaminated heparin secreted considerable amounts of IL-2 in vitro.	Heparin	79-86	interleukin 2	Homo sapiens	120-124
21166821-0	2011	Cutaneous adverse drug reaction to heparins with hypereosinophilia and high IgE level.	Heparin	35-43	immunoglobulin heavy constant epsilon	Homo sapiens	76-79
20961394-9	2011	As evidenced by the reduction of the activated partial thromboplastin time, CXCL4L1 showed a tendency towards less heparin-neutralizing activity than CXCL4 (IC(50) 2.45 vs 0.98 mug mL(-1)).	Heparin	115-122	platelet factor 4	Mus musculus	76-81
21052795-0	2011	Heparin-functionalized collagen matrices with controlled release of basic fibroblast growth factor.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	68-98
21052795-6	2011	These results suggest that heparin-functionalized collagen matrices can support a controlled release of bFGF and thus, have potential as a tissue engineering scaffold.	Heparin	27-34	fibroblast growth factor 2	Homo sapiens	104-108
20955806-13	2011	CONCLUSIONS: In conclusion, alternative splicing of SZP is regulated by TGF-beta1 signaling and may regulate SZP interaction with heparin/heparan sulfate or other components in the extracellular matrix of articular cartilage by splicing out of the heparin binding domain.	Heparin	130-137	proteoglycan 4	Homo sapiens	52-55
20153488-8	2011	Heparin-releasable LPL was increased after treatment with AICAR (P &lt; .05) and high-dose metformin (P &lt; .01).	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-22
20153488-11	2011	After heparin pretreatment, the rate of recruitment of LPL to the cardiac endothelium was increased by AICAR (P &lt; .05) but not by high-dose metformin.	Heparin	6-13	lipoprotein lipase	Rattus norvegicus	55-58
20955806-13	2011	CONCLUSIONS: In conclusion, alternative splicing of SZP is regulated by TGF-beta1 signaling and may regulate SZP interaction with heparin/heparan sulfate or other components in the extracellular matrix of articular cartilage by splicing out of the heparin binding domain.	Heparin	130-137	transforming growth factor beta 1	Homo sapiens	72-81
20955806-13	2011	CONCLUSIONS: In conclusion, alternative splicing of SZP is regulated by TGF-beta1 signaling and may regulate SZP interaction with heparin/heparan sulfate or other components in the extracellular matrix of articular cartilage by splicing out of the heparin binding domain.	Heparin	130-137	proteoglycan 4	Homo sapiens	109-112
20955806-13	2011	CONCLUSIONS: In conclusion, alternative splicing of SZP is regulated by TGF-beta1 signaling and may regulate SZP interaction with heparin/heparan sulfate or other components in the extracellular matrix of articular cartilage by splicing out of the heparin binding domain.	Heparin	248-255	proteoglycan 4	Homo sapiens	52-55
20955806-13	2011	CONCLUSIONS: In conclusion, alternative splicing of SZP is regulated by TGF-beta1 signaling and may regulate SZP interaction with heparin/heparan sulfate or other components in the extracellular matrix of articular cartilage by splicing out of the heparin binding domain.	Heparin	248-255	transforming growth factor beta 1	Homo sapiens	72-81
22180365-2	2011	We have previously reported that heparin competitively inhibits the binding activity of bone morphogenic protein-2 (BMP-2) to BMP and the BMP receptor (BMPR) and suppresses BMP-2 osteogenic activity.	Heparin	33-40	bone morphogenetic protein 2	Mus musculus	173-178
22180365-3	2011	In the present study, we examined whether heparin affects osteoblast differentiation induced by BMP-2 at various time points in vitro.	Heparin	42-49	bone morphogenetic protein 2	Mus musculus	96-101
22180365-0	2011	Dual effects of heparin on BMP-2-induced osteogenic activity in MC3T3-E1 cells.	Heparin	16-23	bone morphogenetic protein 2	Mus musculus	27-32
22180365-7	2011	In addition, 72 h of treatment with heparin enhanced the mRNA expression of runx2 and osterix in BMP-2-stimulated MC3T3-E1 cells.	Heparin	36-43	bone morphogenetic protein 2	Mus musculus	97-102
22180365-2	2011	We have previously reported that heparin competitively inhibits the binding activity of bone morphogenic protein-2 (BMP-2) to BMP and the BMP receptor (BMPR) and suppresses BMP-2 osteogenic activity.	Heparin	33-40	bone morphogenetic protein 2	Mus musculus	88-114
22180365-2	2011	We have previously reported that heparin competitively inhibits the binding activity of bone morphogenic protein-2 (BMP-2) to BMP and the BMP receptor (BMPR) and suppresses BMP-2 osteogenic activity.	Heparin	33-40	bone morphogenetic protein 2	Mus musculus	116-121
22180365-9	2011	These findings indicate biphasic effects of heparin on BMP-2 activity and suggest that heparin has complex effects on the BMP-2 osteogenic bioactivities.	Heparin	44-51	bone morphogenetic protein 2	Mus musculus	55-60
22180365-9	2011	These findings indicate biphasic effects of heparin on BMP-2 activity and suggest that heparin has complex effects on the BMP-2 osteogenic bioactivities.	Heparin	87-94	bone morphogenetic protein 2	Mus musculus	122-127
22180365-10	2011	Prolonged culture with heparin stimulated BMP-2-induced osteogenic activity via down-regulation of BMP-2 antagonists and inhibitory Smads.	Heparin	23-30	bone morphogenetic protein 2	Mus musculus	42-47
22180365-10	2011	Prolonged culture with heparin stimulated BMP-2-induced osteogenic activity via down-regulation of BMP-2 antagonists and inhibitory Smads.	Heparin	23-30	bone morphogenetic protein 2	Mus musculus	99-104
21740395-3	2011	When heparin induced thrombocytopenia is suspected, heparin should be discontinued and treatment with a direct thrombin inhibitor should be initiated.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	111-119
21731773-0	2011	Mechanism of heparin acceleration of tissue inhibitor of metalloproteases-1 (TIMP-1) degradation by the human neutrophil elastase.	Heparin	13-20	TIMP metallopeptidase inhibitor 1	Homo sapiens	37-75
21731773-0	2011	Mechanism of heparin acceleration of tissue inhibitor of metalloproteases-1 (TIMP-1) degradation by the human neutrophil elastase.	Heparin	13-20	TIMP metallopeptidase inhibitor 1	Homo sapiens	77-83
21731773-2	2011	We have assessed the regulatory effect of heparin on Tissue Inhibitor of Metalloproteases-1 [TIMP-1] hydrolysis by HNE employing the recombinant form of TIMP-1 and correlated FRET-peptides comprising the TIMP-1 cleavage site.	Heparin	42-49	TIMP metallopeptidase inhibitor 1	Homo sapiens	53-91
21731773-2	2011	We have assessed the regulatory effect of heparin on Tissue Inhibitor of Metalloproteases-1 [TIMP-1] hydrolysis by HNE employing the recombinant form of TIMP-1 and correlated FRET-peptides comprising the TIMP-1 cleavage site.	Heparin	42-49	TIMP metallopeptidase inhibitor 1	Homo sapiens	93-99
21731773-3	2011	Heparin accelerates 2.5-fold TIMP-1 hydrolysis by HNE.	Heparin	0-7	TIMP metallopeptidase inhibitor 1	Homo sapiens	29-35
21731773-14	2011	Here, we are showing for the first time that heparin is able to accelerate the hydrolysis of TIMP-1 by HNE.	Heparin	45-52	TIMP metallopeptidase inhibitor 1	Homo sapiens	93-99
21853101-1	2011	BACKGROUND: Human sulfatase 1 (hSulf-1) is a heparin-degrading endosulfatase that desulfates cell surface heparan sulfate proteoglycans (HSPGs) in extracellular matrix and negatively modulates heparin-binding growth factor and cytokine signaling in cell proliferation.	Heparin	45-52	sulfatase 1	Homo sapiens	18-29
21853101-1	2011	BACKGROUND: Human sulfatase 1 (hSulf-1) is a heparin-degrading endosulfatase that desulfates cell surface heparan sulfate proteoglycans (HSPGs) in extracellular matrix and negatively modulates heparin-binding growth factor and cytokine signaling in cell proliferation.	Heparin	45-52	sulfatase 1	Homo sapiens	31-38
21904597-8	2011	The truncated forms CXCL8(2-77) and CXCL8(3-77) had higher affinity for heparin than CXCL8(1-77), a property important for the presentation of CXCL8 on endothelial layers.	Heparin	72-79	C-X-C motif chemokine ligand 8	Homo sapiens	20-25
21904597-8	2011	The truncated forms CXCL8(2-77) and CXCL8(3-77) had higher affinity for heparin than CXCL8(1-77), a property important for the presentation of CXCL8 on endothelial layers.	Heparin	72-79	C-X-C motif chemokine ligand 8	Homo sapiens	36-41
21904597-8	2011	The truncated forms CXCL8(2-77) and CXCL8(3-77) had higher affinity for heparin than CXCL8(1-77), a property important for the presentation of CXCL8 on endothelial layers.	Heparin	72-79	C-X-C motif chemokine ligand 8	Homo sapiens	36-41
21904597-8	2011	The truncated forms CXCL8(2-77) and CXCL8(3-77) had higher affinity for heparin than CXCL8(1-77), a property important for the presentation of CXCL8 on endothelial layers.	Heparin	72-79	C-X-C motif chemokine ligand 8	Homo sapiens	36-41
20800586-12	2010	Samples containing heparin had significantly higher levels of corin than that in samples with EDTA or sodium citrate.	Heparin	19-26	corin, serine peptidase	Homo sapiens	62-67
21062008-5	2010	We used NMR spectroscopy of (15)N-labeled HBD2 to map the binding sites for two GAG model compounds, a heparin/HS pentasaccharide (fondaparinux sodium; FX) and enzymatically prepared DS hexasaccharide (DSdp6).	Heparin	103-111	defensin beta 4A	Homo sapiens	42-46
21168759-0	2010	Engineered thrombin aims to take on heparin.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	11-19
21050017-2	2010	Here we report the first successful use of solution NMR in mapping the binding sites in arrestin-1 (visual arrestin) for two polyanionic compounds that mimic phosphorylated light-activated rhodopsin: inositol hexaphosphate (IP6) and heparin.	Heparin	233-240	rhodopsin	Homo sapiens	189-198
21062008-4	2010	Using a gel mobility shift assay, we found that HBD2 bound to a range of GAGs including heparin/heparan sulfate (HS), dermatan sulfate (DS), and chondroitin sulfate.	Heparin	88-95	defensin beta 4A	Homo sapiens	48-52
20966404-7	2010	Site-specific mutations in the heparin-binding region of apoA-V (amino acids 186 to 227) attenuated apoA-V rHDL TG-lowering activity by 50%, suggesting that this sequence element is required for optimal TG-lowering activity in vivo.	Heparin	31-38	apolipoprotein A-V	Mus musculus	57-63
20724543-0	2010	Monocyte-bound PF4 in the pathogenesis of heparin-induced thrombocytopenia.	Heparin	42-49	platelet factor 4	Mus musculus	15-18
20722014-0	2010	Intraarticular injection of heparin-binding insulin-like growth factor 1 sustains delivery of insulin-like growth factor 1 to cartilage through binding to chondroitin sulfate.	Heparin	28-35	insulin like growth factor 1	Homo sapiens	44-72
20722014-0	2010	Intraarticular injection of heparin-binding insulin-like growth factor 1 sustains delivery of insulin-like growth factor 1 to cartilage through binding to chondroitin sulfate.	Heparin	28-35	insulin like growth factor 1	Homo sapiens	94-122
21030022-1	2010	OBJECTIVE: We recently described anti-atherogenic properties of the dual domain peptide Ac-hE18A-NH(2) derived by covalently linking the heparin binding domain 141-150 of apoE to 18A, a class A amphipathic helical peptide.	Heparin	137-144	apolipoprotein E	Mus musculus	171-175
20966404-7	2010	Site-specific mutations in the heparin-binding region of apoA-V (amino acids 186 to 227) attenuated apoA-V rHDL TG-lowering activity by 50%, suggesting that this sequence element is required for optimal TG-lowering activity in vivo.	Heparin	31-38	apolipoprotein A-V	Mus musculus	100-106
21030022-2	2010	In this paper we have compared the properties of Ac-hE18A-NH(2) with the non-heparin binding 151-160 region of apoE linked to 18A (Ac-nhE18A-NH(2)).	Heparin	77-84	apolipoprotein E	Mus musculus	111-115
20847691-4	2010	RECENT FINDINGS: Oral administration, predictable anticoagulant responses, low potential for drug-drug interactions render direct thrombin and factor Xa inhibitors good candidates to replace UFH, LMWH and fondaparinux for VTE prophylaxis.	Heparin	191-194	coagulation factor II, thrombin	Homo sapiens	130-138
20863557-2	2010	In this study, heparin-functionalized chitosan (CS)/poly(gamma-glutamic acid) (gamma-PGA) nanoparticles (HP-CS/gamma-PGA nanoparticles) were prepared for multi-functional delivery of basic fibroblast growth factor (bFGF) and heparin.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	183-213
20863557-2	2010	In this study, heparin-functionalized chitosan (CS)/poly(gamma-glutamic acid) (gamma-PGA) nanoparticles (HP-CS/gamma-PGA nanoparticles) were prepared for multi-functional delivery of basic fibroblast growth factor (bFGF) and heparin.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	215-219
20863557-3	2010	The mean particle sizes and bFGF loading efficiency increased with the increase of functionalized heparin contents.	Heparin	98-105	fibroblast growth factor 2	Homo sapiens	28-32
20864170-6	2010	Binding basic fibroblast growth factor (bFGF) to the heparin layer inhibited neurons but promoted proliferation and migration of precursor cells.	Heparin	53-60	fibroblast growth factor 2	Homo sapiens	8-38
20864170-6	2010	Binding basic fibroblast growth factor (bFGF) to the heparin layer inhibited neurons but promoted proliferation and migration of precursor cells.	Heparin	53-60	fibroblast growth factor 2	Homo sapiens	40-44
20688960-2	2010	Because interactions with glycosaminoglycans play a crucial role in chemokines activity, we determined the binding parameters of CXCL4 and CXCL4L1 for heparin, heparan sulfate, and chondroitin sulfate B.	Heparin	151-158	platelet factor 4 variant 1	Homo sapiens	139-146
21112526-1	2010	In patients on high-level anticoagulant therapy (prothrombin time-international normalized ratio [PT-INR] &gt;= 4.5), surgical procedures can be carried out with bridging therapy using heparin.	Heparin	185-192	coagulation factor II, thrombin	Homo sapiens	49-60
20797432-0	2010	Carbon monoxide-releasing molecule CORM-3 suppresses vascular endothelial cell SOD-1/SOD-2 activity while up-regulating the cell surface levels of SOD-3 in a heparin-dependent manner.	Heparin	158-165	superoxide dismutase 3	Homo sapiens	147-152
20797432-9	2010	However, in the presence of heparin, total cell-associated SOD activity was significantly increased by CORM-3, because of increased binding of SOD-3 to HUVECs.	Heparin	28-35	superoxide dismutase 3	Homo sapiens	59-62
20797432-9	2010	However, in the presence of heparin, total cell-associated SOD activity was significantly increased by CORM-3, because of increased binding of SOD-3 to HUVECs.	Heparin	28-35	superoxide dismutase 3	Homo sapiens	143-148
20729008-7	2010	RESULTS: The effect of FGFC was equal to or slightly superior to FGF1 with heparin.	Heparin	75-82	fibroblast growth factor 1	Mus musculus	65-69
20692134-4	2010	The immobilized heparin amount was probed by toluidine blue O binding, fibronectin by immunochemistry.	Heparin	16-23	fibronectin 1	Homo sapiens	71-82
20634491-13	2010	Unfractionated heparin and an inhibitor of activated factor X abolished the effect of heparanase, while tissue factor pathway inhibitor and tissue factor pathway inhibitor-2 only attenuated the procoagulant effect.	Heparin	15-22	heparanase	Homo sapiens	86-173
20538990-9	2010	Either the matrix metalloproteinase (MMP) inhibitor GM6001 or the specific heparin-bound EGF-like growth factor inhibitor CRM197 suppressed RvE1-induced stimulation of EGFR/PI3-K/Akt phosphorylation and cell migration.	Heparin	75-82	epidermal growth factor receptor	Homo sapiens	168-172
20538990-9	2010	Either the matrix metalloproteinase (MMP) inhibitor GM6001 or the specific heparin-bound EGF-like growth factor inhibitor CRM197 suppressed RvE1-induced stimulation of EGFR/PI3-K/Akt phosphorylation and cell migration.	Heparin	75-82	AKT serine/threonine kinase 1	Homo sapiens	179-182
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	35-43
20674970-0	2010	FGF-2 and VEGF functionalization of starPEG-heparin hydrogels to modulate biomolecular and physical cues of angiogenesis.	Heparin	44-51	fibroblast growth factor 2	Homo sapiens	0-5
20674970-0	2010	FGF-2 and VEGF functionalization of starPEG-heparin hydrogels to modulate biomolecular and physical cues of angiogenesis.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	10-14
21076620-4	2010	Flow cytometric analysis revealed that B-Raf activation led to loss of the cell surface HS, which could be blocked by two HPR1 inhibitors: heparin and PI-88.	Heparin	139-146	B-Raf proto-oncogene, serine/threonine kinase	Homo sapiens	39-44
20724654-4	2010	Heparin-Sepharose (H-S) affinity chromatography was used for specific PLTP binding, and coeluted proteins were identified with MALDI-TOF mass spectrometry or Western blot analysis.	Heparin	0-7	phospholipid transfer protein	Homo sapiens	70-74
21076620-4	2010	Flow cytometric analysis revealed that B-Raf activation led to loss of the cell surface HS, which could be blocked by two HPR1 inhibitors: heparin and PI-88.	Heparin	139-146	heparanase	Homo sapiens	122-126
20939933-0	2010	N-terminal and C-terminal heparin-binding domain polypeptides derived from fibronectin reduce adhesion and invasion of liver cancer cells.	Heparin	26-33	fibronectin 1	Homo sapiens	75-86
20843543-6	2010	Thrombin generation was dose dependently diminished by low molecular weight heparin and increased by high concentrations of exogenous factor VIII i.e. the assay can detect both hypo- and hypercoagulability.	Heparin	76-83	coagulation factor II	Mus musculus	0-8
20729553-7	2010	Both 3T3 mouse fibroblasts and human embryonic kidney cells (HEK-293) attached to PCPE-1, an interaction that was inhibited by heparin.	Heparin	127-134	procollagen C-endopeptidase enhancer	Homo sapiens	82-88
20679343-9	2010	Because the regular incorporation of negative charges by GSK3beta leads to a potential parallel between phospho-Tau and heparin, we investigated its interaction with the heparin/low density lipoprotein receptor binding domain of human apolipoprotein E.	Heparin	120-127	apolipoprotein E	Homo sapiens	235-251
20679343-9	2010	Because the regular incorporation of negative charges by GSK3beta leads to a potential parallel between phospho-Tau and heparin, we investigated its interaction with the heparin/low density lipoprotein receptor binding domain of human apolipoprotein E.	Heparin	170-177	apolipoprotein E	Homo sapiens	235-251
20939933-1	2010	BACKGROUND: Fibronectin (FN) is known to be a large multifunction glycoprotein with binding sites for many substances, including N-terminal and C-terminal heparin-binding domains.	Heparin	155-162	fibronectin 1	Homo sapiens	12-23
20939933-1	2010	BACKGROUND: Fibronectin (FN) is known to be a large multifunction glycoprotein with binding sites for many substances, including N-terminal and C-terminal heparin-binding domains.	Heparin	155-162	fibronectin 1	Homo sapiens	25-27
20795698-8	2010	On PEM-coated TCPS, we found that FGF-2 adsorbed to heparin-terminated PEMs with adsorbed fibronectin induces greater cell density and a higher proliferation rate of MSCs than any of the other conditions tested, including delivery of the FGF-2 in solution, at an optimally mitogenic dose.	Heparin	52-59	fibroblast growth factor 2	Homo sapiens	34-39
20682766-4	2010	Pikachurin-dystroglycan binding is calcium-dependent and relatively less sensitive to inhibition by heparin and high NaCl concentration, as compared with other dystroglycan ligand proteins.	Heparin	100-107	dystroglycan 1	Mus musculus	11-23
20795698-8	2010	On PEM-coated TCPS, we found that FGF-2 adsorbed to heparin-terminated PEMs with adsorbed fibronectin induces greater cell density and a higher proliferation rate of MSCs than any of the other conditions tested, including delivery of the FGF-2 in solution, at an optimally mitogenic dose.	Heparin	52-59	fibronectin 1	Homo sapiens	90-101
20795698-8	2010	On PEM-coated TCPS, we found that FGF-2 adsorbed to heparin-terminated PEMs with adsorbed fibronectin induces greater cell density and a higher proliferation rate of MSCs than any of the other conditions tested, including delivery of the FGF-2 in solution, at an optimally mitogenic dose.	Heparin	52-59	fibroblast growth factor 2	Homo sapiens	238-243
20524207-0	2010	Multiple mechanisms for exogenous heparin modulation of vascular endothelial growth factor activity.	Heparin	34-41	vascular endothelial growth factor A	Homo sapiens	56-90
20621352-7	2010	These results suggest that the identified heparin binding domain peptide (HBD) stimulated osteoblastic differentiation via interaction with heparin and the ERK signaling.	Heparin	42-49	mitogen-activated protein kinase 3	Homo sapiens	156-159
21057164-0	2010	The preventive effect of low molecular weight heparin on CCL4-induced necrosis and apoptosis in rat liver.	Heparin	46-53	C-C motif chemokine ligand 4	Rattus norvegicus	57-61
21057164-2	2010	The present study investigated the effect of low molecular weight heparin (Enoxaparin) on carbon tetrachloride (CCl4) induced hepatic necrosis and apoptosis in rats.	Heparin	66-73	C-C motif chemokine ligand 4	Rattus norvegicus	112-116
20524207-2	2010	In this study, we investigated the likely mechanisms for heparin"s influence on the biological activity of VEGF-A.	Heparin	57-64	vascular endothelial growth factor A	Homo sapiens	107-113
20524207-3	2010	Previous studies have shown that exogenous heparin"s effects on the biological activity of VEGF-A are many and varied, in part due to the endogenous cell-surface heparan sulfates.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	91-97
20524207-5	2010	We showed that VEGF-induced cellular responses are dependent in part on the presence of the heparan sulfates, and that exogenous heparin significantly augments VEGF"s cellular effects especially when endogenous heparan sulfates are absent.	Heparin	129-136	vascular endothelial growth factor A	Homo sapiens	160-164
20524207-6	2010	Exogenous heparin was also found to play a cross-bridging role between VEGF-A(165) and putative heparin-binding sites within its cognate receptor, VEGFR2 when they were examined in isolation.	Heparin	10-17	vascular endothelial growth factor A	Homo sapiens	71-77
20524207-9	2010	Finally, studies of the far-UV circular dichroism spectra of VEGF-A(165) showed that heparin can also modulate the conformation and secondary structure of the protein.	Heparin	85-92	vascular endothelial growth factor A	Homo sapiens	61-67
20599451-3	2010	A chondrogenic growth factor, transforming growth factor-beta 1 (TGF-beta1) was then coupled to the heparin-conjugated F127.	Heparin	100-107	transforming growth factor beta 1	Homo sapiens	65-74
20427081-0	2010	Bradykinin forming capacity of oversulfated chondroitin sulfate contaminated heparin in vitro.	Heparin	77-84	kininogen 1	Homo sapiens	0-10
20870869-6	2010	Those associated with pain are often responsive to low-molecular-weight heparin, which should also be used to avoid disseminated intravascular coagulopathy secondary to intervention, especially if fibrinogen level is low.	Heparin	72-79	fibrinogen beta chain	Homo sapiens	197-207
20486788-2	2010	Specifically, heparin was covalently conjugated onto the surface of fibrous matrices (composites of poly[caprolactone] and gelatin crosslinked with genipin), and basic fibroblast growth factor (bFGF) was then reversibly immobilized.	Heparin	14-21	fibroblast growth factor 2	Homo sapiens	162-199
20486788-3	2010	The immobilization of bFGF was controlled as a function of the amount of conjugated heparin.	Heparin	84-91	fibroblast growth factor 2	Homo sapiens	22-26
20233649-4	2010	The 500 MHz 1D-(1)H NMR spectra of heparin spiked with 1.0-10% CSA, CSB, OS-CSA, or OS-CSB showed unique signal pattern changes while the samples spiked with HS, OS-HS, OS-Heparin or partially sulfated CSA were more difficult to identify using NMR data.	Heparin	35-42	ERCC excision repair 6, chromatin remodeling factor	Homo sapiens	68-71
20233649-4	2010	The 500 MHz 1D-(1)H NMR spectra of heparin spiked with 1.0-10% CSA, CSB, OS-CSA, or OS-CSB showed unique signal pattern changes while the samples spiked with HS, OS-HS, OS-Heparin or partially sulfated CSA were more difficult to identify using NMR data.	Heparin	35-42	ERCC excision repair 6, chromatin remodeling factor	Homo sapiens	87-90
20854738-0	2010	[Effect of heparin on the levels of interleukin-6, tumor necrosis factor-alpha and angiotensin II in rat with sepsis].	Heparin	11-18	interleukin 6	Rattus norvegicus	36-78
20854738-0	2010	[Effect of heparin on the levels of interleukin-6, tumor necrosis factor-alpha and angiotensin II in rat with sepsis].	Heparin	11-18	angiotensinogen	Rattus norvegicus	83-97
20712376-10	2010	This dimeric vMIP-II mutant binds to heparin much more tightly than wild-type vMIP-II and provides a new model for studying the relationship between chemokine quaternary structure and various aspects of function.	Heparin	37-44	K4	Human gammaherpesvirus 8	13-20
20547765-8	2010	Mechanistically, Wnt3a-heparin signaling strongly activates the phosphoinositide 3-kinase/Akt pathway and requires the bone-related transcription factor RUNX2 to stimulate alkaline phosphatase activity, which parallels canonical beta-catenin signaling.	Heparin	23-30	AKT serine/threonine kinase 1	Homo sapiens	90-93
20547765-8	2010	Mechanistically, Wnt3a-heparin signaling strongly activates the phosphoinositide 3-kinase/Akt pathway and requires the bone-related transcription factor RUNX2 to stimulate alkaline phosphatase activity, which parallels canonical beta-catenin signaling.	Heparin	23-30	RUNX family transcription factor 2	Homo sapiens	153-158
20547765-9	2010	Collectively, our findings establish the osteo-inductive potential of a heparin-mediated Wnt3a-phosphoinositide 3-kinase/Akt-RUNX2 signaling network and suggest that heparan sulfate supplementation may selectively reduce the therapeutic doses of peptide factors required to promote bone formation.	Heparin	72-79	AKT serine/threonine kinase 1	Homo sapiens	121-124
20547765-9	2010	Collectively, our findings establish the osteo-inductive potential of a heparin-mediated Wnt3a-phosphoinositide 3-kinase/Akt-RUNX2 signaling network and suggest that heparan sulfate supplementation may selectively reduce the therapeutic doses of peptide factors required to promote bone formation.	Heparin	72-79	RUNX family transcription factor 2	Homo sapiens	125-130
20643239-7	2010	Administration of heparin caused a marked increase of plasma MPO.	Heparin	18-25	myeloperoxidase	Homo sapiens	61-64
20643239-8	2010	Even so, it was still possible to detect an increase of plasma MPO at culprit lesion in patients with STEMI (n = 54, 171 ng/ml, 122 to 230) versus controls (n = 12, 136 ng/ml, 109 to 151, p &lt;0.05) after heparin and before PCI.	Heparin	206-213	myeloperoxidase	Homo sapiens	63-66
20576607-6	2010	Notably, the full-length Hpa2c protein inhibits heparanase enzymatic activity, likely due to its high affinity to heparin and heparan sulfate and its ability to associate physically with heparanase.	Heparin	114-121	heparanase	Homo sapiens	48-58
20686010-1	2010	Direct thrombin inhibitors are heparin alternatives for anticoagulation during cardiopulmonary bypass in patients with heparin-induced thrombocytopenia.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	7-15
20686010-1	2010	Direct thrombin inhibitors are heparin alternatives for anticoagulation during cardiopulmonary bypass in patients with heparin-induced thrombocytopenia.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	7-15
20505748-7	2010	Furthermore, our data indicate a protective effect of heparins on EC activation as shown by reduced VWF release in response to MV3 supernatant.	Heparin	54-62	von Willebrand factor	Homo sapiens	100-103
21567562-3	2010	Taking advantage of the high affinity of vascular endothelial growth factor to heparin, we illustrate the applicability of our hydrogels as a novel system that is supportive of cellular remodeling and three-dimensional migration of human endothelial cells.	Heparin	79-86	vascular endothelial growth factor A	Homo sapiens	41-75
20547765-0	2010	Synergism between Wnt3a and heparin enhances osteogenesis via a phosphoinositide 3-kinase/Akt/RUNX2 pathway.	Heparin	28-35	AKT serine/threonine kinase 1	Homo sapiens	90-93
20547765-0	2010	Synergism between Wnt3a and heparin enhances osteogenesis via a phosphoinositide 3-kinase/Akt/RUNX2 pathway.	Heparin	28-35	RUNX family transcription factor 2	Homo sapiens	94-99
20163908-7	2010	Quartz crystal microbalance data confirmed SM4/P-selectin liposome binding that was inhibited dose-dependently by heparin.	Heparin	114-121	selectin, platelet	Mus musculus	47-57
20427081-6	2010	We demonstrate a highly significant correlation between the concentration of OSCS present in the contaminated heparin and BK released concentration.	Heparin	110-117	kininogen 1	Homo sapiens	122-124
20427081-7	2010	In conclusion, for the first time, we show that OSCS contaminated heparin incubated with human plasma has the capacity to liberate BK at a concentration that could explain the role of this inflammatory peptide in the pathophysiology of AR associated with OSCS contaminated heparin.	Heparin	66-73	kininogen 1	Homo sapiens	131-133
20427081-7	2010	In conclusion, for the first time, we show that OSCS contaminated heparin incubated with human plasma has the capacity to liberate BK at a concentration that could explain the role of this inflammatory peptide in the pathophysiology of AR associated with OSCS contaminated heparin.	Heparin	273-280	kininogen 1	Homo sapiens	131-133
20659659-5	2010	This review proposes that alternative anticoagulants (danaparoid, fondaparinux) that share certain properties of heparin-namely its irreversible antithrombin-mediated inhibition of factor Xa-and that have relatively long half-lives, have several advantages in the therapy for HIT over short-acting agents that inhibit thrombin directly (recombinant hirudin, argatroban, and bivalirudin).	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	149-157
20177819-7	2010	Although BID UFH shows some efficacy in one primary study, it is no more beneficial than no prophylaxis in another study.	Heparin	13-16	BH3 interacting domain death agonist	Homo sapiens	9-12
20566960-8	2010	These results indicate that kallistatin"s heparin-binding site plays an essential role in preventing TNF-alpha-mediated endothelial activation and reducing vascular endothelial growth factor-induced vascular permeability, resulting in attenuation of vascular inflammation in cultured endothelial cells and animal models.	Heparin	42-49	tumor necrosis factor	Homo sapiens	101-110
20566960-8	2010	These results indicate that kallistatin"s heparin-binding site plays an essential role in preventing TNF-alpha-mediated endothelial activation and reducing vascular endothelial growth factor-induced vascular permeability, resulting in attenuation of vascular inflammation in cultured endothelial cells and animal models.	Heparin	42-49	vascular endothelial growth factor A	Homo sapiens	156-190
20177819-14	2010	Newly published risk-assessment models may be beneficial in determining which patients would best benefit from BID UFH or TID UFH.	Heparin	115-118	BH3 interacting domain death agonist	Homo sapiens	111-114
20367289-6	2010	To combine the biochemical and biophysical cues, bFGF and EGF were either adsorbed or bound to heparin on nanofibrous scaffolds.	Heparin	95-102	fibroblast growth factor 2	Homo sapiens	49-53
20432446-0	2010	Low-concentration heparin suppresses ionomycin-activated CAMK-II/EGF receptor- and ERK-mediated signaling in mesangial cells.	Heparin	18-25	epidermal growth factor receptor	Homo sapiens	65-77
20432446-0	2010	Low-concentration heparin suppresses ionomycin-activated CAMK-II/EGF receptor- and ERK-mediated signaling in mesangial cells.	Heparin	18-25	mitogen-activated protein kinase 1	Homo sapiens	83-86
20432446-1	2010	Heparin and endogenous heparinoids inhibit the proliferation of smooth muscle cells, including renal mesangial cells; multiple effects on signaling pathways are well established, including effects on PKC, Erk, and CaMK-II.	Heparin	0-7	mitogen-activated protein kinase 1	Homo sapiens	205-208
20432446-5	2010	Low-dose heparin suppresses the ionomycin-dependent phosphorylation of EGFR, c-Src, and Erk 1/2, but not of CaMK-II, whereas inhibition of activated CaMK-II reduces phosphorylation of EGFR, c-Src, and Erk.	Heparin	9-16	epidermal growth factor receptor	Homo sapiens	71-75
20432446-5	2010	Low-dose heparin suppresses the ionomycin-dependent phosphorylation of EGFR, c-Src, and Erk 1/2, but not of CaMK-II, whereas inhibition of activated CaMK-II reduces phosphorylation of EGFR, c-Src, and Erk.	Heparin	9-16	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	77-82
20432446-5	2010	Low-dose heparin suppresses the ionomycin-dependent phosphorylation of EGFR, c-Src, and Erk 1/2, but not of CaMK-II, whereas inhibition of activated CaMK-II reduces phosphorylation of EGFR, c-Src, and Erk.	Heparin	9-16	mitogen-activated protein kinase 3	Homo sapiens	88-95
20432446-5	2010	Low-dose heparin suppresses the ionomycin-dependent phosphorylation of EGFR, c-Src, and Erk 1/2, but not of CaMK-II, whereas inhibition of activated CaMK-II reduces phosphorylation of EGFR, c-Src, and Erk.	Heparin	9-16	epidermal growth factor receptor	Homo sapiens	184-188
20432446-5	2010	Low-dose heparin suppresses the ionomycin-dependent phosphorylation of EGFR, c-Src, and Erk 1/2, but not of CaMK-II, whereas inhibition of activated CaMK-II reduces phosphorylation of EGFR, c-Src, and Erk.	Heparin	9-16	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	190-195
20432446-5	2010	Low-dose heparin suppresses the ionomycin-dependent phosphorylation of EGFR, c-Src, and Erk 1/2, but not of CaMK-II, whereas inhibition of activated CaMK-II reduces phosphorylation of EGFR, c-Src, and Erk.	Heparin	9-16	mitogen-activated protein kinase 1	Homo sapiens	88-91
20432446-6	2010	Our data support a mechanism whereby heparin acts at the cell surface to suppress downstream targets of CaMK-II, including EGFR, leading in turn to a decrease in Erk- (but not c-Src-) dependent induction of c-fos.	Heparin	37-44	epidermal growth factor receptor	Homo sapiens	123-127
20432446-6	2010	Our data support a mechanism whereby heparin acts at the cell surface to suppress downstream targets of CaMK-II, including EGFR, leading in turn to a decrease in Erk- (but not c-Src-) dependent induction of c-fos.	Heparin	37-44	mitogen-activated protein kinase 1	Homo sapiens	162-165
20546854-3	2010	Low molecular weight heparin (LMWH) has been found to be effective and safe in children with ALL during L-asparaginase treatment.	Heparin	21-28	asparaginase and isoaspartyl peptidase 1	Homo sapiens	104-118
20367289-9	2010	In contrast, immobilization of bFGF or EGF onto nanofibers using heparin as the adapter molecule significantly promoted axon growth.	Heparin	65-72	fibroblast growth factor 2	Homo sapiens	31-35
20416374-9	2010	This is approached through a few illustrative examples, including the interaction of HS and heparin-derived species with the chemokine IL-8, the growth factors FGF1 and FGF2, and the modulation of the activity of the enzyme heparanase by these species.	Heparin	92-99	C-X-C motif chemokine ligand 8	Homo sapiens	135-139
21567519-1	2010	We have previously reported a novel polymeric delivery vehicle that is assembled via interaction between heparin and the vascular endothelial growth factor (VEGF).	Heparin	105-112	vascular endothelial growth factor A	Homo sapiens	121-155
21567519-1	2010	We have previously reported a novel polymeric delivery vehicle that is assembled via interaction between heparin and the vascular endothelial growth factor (VEGF).	Heparin	105-112	vascular endothelial growth factor A	Homo sapiens	157-161
21567519-4	2010	The [PEG-LMWH/VEGF] hydrogel (PEG = poly(ethylene glycol), LMWH = low molecular weight heparin) correspondingly prompted increases in VEGFR-2 phosphorylation and proliferation of PAE/KDR cells.	Heparin	87-94	vascular endothelial growth factor A	Homo sapiens	14-18
20445443-1	2010	Earlier studies of addition of naturally sulfated polysaccharides including unfractionated heparin showed a significant enhancement of the in-vitro activation of glutamic plasminogen (Glu-Plg) by tissue plasminogen activator (t-PA) or urokinase plasminogen activator (u-PA).	Heparin	91-98	plasminogen activator, tissue type	Homo sapiens	226-230
20445443-1	2010	Earlier studies of addition of naturally sulfated polysaccharides including unfractionated heparin showed a significant enhancement of the in-vitro activation of glutamic plasminogen (Glu-Plg) by tissue plasminogen activator (t-PA) or urokinase plasminogen activator (u-PA).	Heparin	91-98	plasminogen activator, urokinase	Homo sapiens	235-266
20445443-1	2010	Earlier studies of addition of naturally sulfated polysaccharides including unfractionated heparin showed a significant enhancement of the in-vitro activation of glutamic plasminogen (Glu-Plg) by tissue plasminogen activator (t-PA) or urokinase plasminogen activator (u-PA).	Heparin	91-98	plasminogen activator, urokinase	Homo sapiens	268-272
20445443-6	2010	In-vitro studies were conducted on comparing the effect of oversulfated chondroitin-6-sulfate (S-2) with native compound (N-2) and unfractionated heparin in enhancing the activation of Glu-Plg by t-PA or u-PA using 0.05 mol/l Tris buffer (pH 7.3) containing 0.9% of NaCl.	Heparin	146-153	plasminogen activator, tissue type	Homo sapiens	196-200
20445443-6	2010	In-vitro studies were conducted on comparing the effect of oversulfated chondroitin-6-sulfate (S-2) with native compound (N-2) and unfractionated heparin in enhancing the activation of Glu-Plg by t-PA or u-PA using 0.05 mol/l Tris buffer (pH 7.3) containing 0.9% of NaCl.	Heparin	146-153	plasminogen activator, urokinase	Homo sapiens	204-208
20530110-3	2010	OBJECTIVE: The goal of this study was to evaluate the effect of heparin on the frequency of episodes of catheter-related sepsis (CRS) in infants receiving total parenteral nutrition (TPN) through a neonatal long line.	Heparin	64-71	twist family bHLH transcription factor 1	Homo sapiens	104-127
20416374-9	2010	This is approached through a few illustrative examples, including the interaction of HS and heparin-derived species with the chemokine IL-8, the growth factors FGF1 and FGF2, and the modulation of the activity of the enzyme heparanase by these species.	Heparin	92-99	fibroblast growth factor 1	Homo sapiens	160-164
20416374-9	2010	This is approached through a few illustrative examples, including the interaction of HS and heparin-derived species with the chemokine IL-8, the growth factors FGF1 and FGF2, and the modulation of the activity of the enzyme heparanase by these species.	Heparin	92-99	fibroblast growth factor 2	Homo sapiens	169-173
20547553-0	2010	Oversulfated heparin by-products induce thrombin generation in human plasmas through contact system activation.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	40-48
20458441-0	2010	The effects of low-molecular-weight heparin at two different dosages on thrombin generation in cancer patients.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	72-80
20543985-4	2010	We set out to explore the use of heparin, a well-characterized sulfated glycosaminoglycan, for the controlled release of fibroblast growth factor-2 (FGF-2).	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	121-147
20543985-4	2010	We set out to explore the use of heparin, a well-characterized sulfated glycosaminoglycan, for the controlled release of fibroblast growth factor-2 (FGF-2).	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	149-154
20543985-6	2010	We used a biocompatible polycation to precipitate out the [heparin:FGF-2] complex from neutral buffer to form a release matrix.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	67-72
20547553-3	2010	Here we present evidence for a new route to thrombin formation that begins with the activation of the contact system protein prekallikrein by oversulfated heparin (OS-HB).	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	44-52
20460351-5	2010	This study showed that although oversulfated heparin byproduct induced thrombin activities in both normal and HIT patient plasmas through the contact system activation, authentic heparin induced thrombin activities only in HIT patient plasmas containing autoantibodies against protein/ heparin complex.	Heparin	179-186	coagulation factor II, thrombin	Homo sapiens	195-203
20460351-7	2010	The newly discovered mechanism of heparin-induced thrombin activity could explain the increased incidence of HIT in patients exposed to contaminated heparin.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	50-58
20460351-7	2010	The newly discovered mechanism of heparin-induced thrombin activity could explain the increased incidence of HIT in patients exposed to contaminated heparin.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	50-58
20460351-0	2010	Heparin and oversulfated heparin byproduct induce thrombin generation through contact system activation in plasma of patients with HIT.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	50-58
20460351-0	2010	Heparin and oversulfated heparin byproduct induce thrombin generation through contact system activation in plasma of patients with HIT.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	50-58
20460351-5	2010	This study showed that although oversulfated heparin byproduct induced thrombin activities in both normal and HIT patient plasmas through the contact system activation, authentic heparin induced thrombin activities only in HIT patient plasmas containing autoantibodies against protein/ heparin complex.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	71-79
20547553-7	2010	Oversulfated heparin by-product-induced thrombin generation may have had a role in the adverse reactions associated with the recent clinical use of contaminated heparin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	40-48
20547553-7	2010	Oversulfated heparin by-product-induced thrombin generation may have had a role in the adverse reactions associated with the recent clinical use of contaminated heparin.	Heparin	161-168	coagulation factor II, thrombin	Homo sapiens	40-48
19338998-12	2010	The expression of alpha-smooth muscle actin, Ras homology (Rho) A, Rho-associated coiled-coil-forming protein kinase (ROCK)-I, and ROCK-II was down-regulated by heparin administration.	Heparin	161-168	ras homolog family member A	Homo sapiens	45-65
20026666-2	2010	LPL activity and mass in pre- and postheparin plasma were low, and LPL release into plasma after heparin injection was delayed.	Heparin	38-45	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	0-3
20382221-9	2010	Inhibition studies with synthetic peptides identified three major heparin binding sequences in fragment LTBP-2 NT(H), including sequence LTEKIKKIKIV in the first large cysteine-free domain of LTBP-2, adjacent to the previously identified fibulin-5 binding site.	Heparin	66-73	latent transforming growth factor beta binding protein 2	Homo sapiens	104-110
20218985-6	2010	The results also suggest, for the first time, that there are age-related differences of heparin binding to antithrombin and thrombin.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	111-119
20382221-0	2010	LTBP-2 has multiple heparin/heparan sulfate binding sites.	Heparin	20-27	latent transforming growth factor beta binding protein 2	Homo sapiens	0-6
20382221-9	2010	Inhibition studies with synthetic peptides identified three major heparin binding sequences in fragment LTBP-2 NT(H), including sequence LTEKIKKIKIV in the first large cysteine-free domain of LTBP-2, adjacent to the previously identified fibulin-5 binding site.	Heparin	66-73	latent transforming growth factor beta binding protein 2	Homo sapiens	192-198
20382221-2	2010	In this study we investigated the molecular interactions of LTBP-2 with heparin and heparan sulfate proteoglycans (HSPGs) since unidentified cell surface HSPGs are critical for normal fiber assembly.	Heparin	72-79	latent transforming growth factor beta binding protein 2	Homo sapiens	60-66
20382221-3	2010	In solid phase assays, heparin conjugated to albumin (HAC) bound strongly to recombinant full-length human LTBP-2.	Heparin	23-30	latent transforming growth factor beta binding protein 2	Homo sapiens	107-113
20382221-10	2010	LTBP-2 was found to interact strongly in a heparin-inhibitable manner with cell surface HSPG syndecan-4, but showed no interaction with recombinant syndecan-2.	Heparin	43-50	latent transforming growth factor beta binding protein 2	Homo sapiens	0-6
20382221-7	2010	Kds for heparin binding were calculated for full-length LTBP-2, LTBP-2 NT(H) and LTBP-2 C(H) as 0.9 nM, 0.7 nM and 80 nM respectively.	Heparin	8-15	latent transforming growth factor beta binding protein 2	Homo sapiens	56-62
20382221-7	2010	Kds for heparin binding were calculated for full-length LTBP-2, LTBP-2 NT(H) and LTBP-2 C(H) as 0.9 nM, 0.7 nM and 80 nM respectively.	Heparin	8-15	latent transforming growth factor beta binding protein 2	Homo sapiens	64-70
20235148-0	2010	Heparin treatment of vascular smooth muscle cells results in the synthesis of the dual-specificity phosphatase MKP-1.	Heparin	0-7	dual specificity phosphatase 1	Homo sapiens	111-116
20382221-7	2010	Kds for heparin binding were calculated for full-length LTBP-2, LTBP-2 NT(H) and LTBP-2 C(H) as 0.9 nM, 0.7 nM and 80 nM respectively.	Heparin	8-15	latent transforming growth factor beta binding protein 2	Homo sapiens	64-70
20136400-1	2010	Heparin-conjugated fibrin (HCF, a mixture of heparin-conjugated fibrinogen and thrombin) was developed as an injectable carrier for long-term delivery of fibroblast growth factor 2 (FGF2), and the therapeutic potential of the HCF system was investigated by evaluating neovascularization in a mouse hind limb ischemia model.	Heparin	0-7	coagulation factor II	Mus musculus	79-87
19853891-10	2010	CONCLUSION: A positive family history of VTE, carriership of the prothrombin mutation and elevated FVIII or Hcy levels were significantly associated with failure to prevent VTE by heparin therapy following ATSCI.	Heparin	180-187	coagulation factor II, thrombin	Homo sapiens	65-76
20117945-3	2010	Anosmin-1, the KAL-1 gene product underlying X-linked KS, modulates FGFR1 signalling via regulation of FGF2/FGFR1/heparin signalling complex assembly and activity.	Heparin	114-121	anosmin 1	Homo sapiens	0-9
20117945-3	2010	Anosmin-1, the KAL-1 gene product underlying X-linked KS, modulates FGFR1 signalling via regulation of FGF2/FGFR1/heparin signalling complex assembly and activity.	Heparin	114-121	anosmin 1	Homo sapiens	15-20
20207734-4	2010	In contrast, we report that the NTR domain within PCPE-1 leads to superstimulation of bone morphogenetic protein-1 activity in the presence of heparin and heparan sulfate.	Heparin	143-150	procollagen C-endopeptidase enhancer	Homo sapiens	50-56
19962139-9	2010	RESULT(S): Heparin dose- and time-dependently delayed the production of IGFBP-1 and amplified the levels of PRL and IGF-I in ESCs during decidualization in vitro.	Heparin	11-18	prolactin	Homo sapiens	108-111
19962139-9	2010	RESULT(S): Heparin dose- and time-dependently delayed the production of IGFBP-1 and amplified the levels of PRL and IGF-I in ESCs during decidualization in vitro.	Heparin	11-18	insulin like growth factor 1	Homo sapiens	116-121
20235148-2	2010	It is clear that heparin treatment can decrease the level of ERK activity in vascular smooth muscle cells that are sensitive to heparin.	Heparin	17-24	mitogen-activated protein kinase 1	Homo sapiens	61-64
20235148-2	2010	It is clear that heparin treatment can decrease the level of ERK activity in vascular smooth muscle cells that are sensitive to heparin.	Heparin	128-135	mitogen-activated protein kinase 1	Homo sapiens	61-64
20235148-3	2010	In this study, the mechanism by which heparin induces decreases in ERK activity was investigated by evaluating the dual specificity phosphatase, MKP-1, in heparin treated cells.	Heparin	38-45	mitogen-activated protein kinase 1	Homo sapiens	67-70
20235148-3	2010	In this study, the mechanism by which heparin induces decreases in ERK activity was investigated by evaluating the dual specificity phosphatase, MKP-1, in heparin treated cells.	Heparin	38-45	dual specificity phosphatase 1	Homo sapiens	145-150
20235148-3	2010	In this study, the mechanism by which heparin induces decreases in ERK activity was investigated by evaluating the dual specificity phosphatase, MKP-1, in heparin treated cells.	Heparin	155-162	mitogen-activated protein kinase 1	Homo sapiens	67-70
20235148-3	2010	In this study, the mechanism by which heparin induces decreases in ERK activity was investigated by evaluating the dual specificity phosphatase, MKP-1, in heparin treated cells.	Heparin	155-162	dual specificity phosphatase 1	Homo sapiens	145-150
20235148-4	2010	Heparin induced MKP-1 synthesis in a time and concentration dependent manner.	Heparin	0-7	dual specificity phosphatase 1	Homo sapiens	16-21
20235148-8	2010	Blocking either phosphatase activity or synthesis also blocked heparin-induced decreases in ERK activity.	Heparin	63-70	mitogen-activated protein kinase 1	Homo sapiens	92-95
20235148-9	2010	Consistent with a role for MKP-1, a nuclear phosphatase, heparin treated cells exhibited decreases in nuclear ERK activity more rapidly than cells not treated with heparin.	Heparin	57-64	dual specificity phosphatase 1	Homo sapiens	27-32
20235148-9	2010	Consistent with a role for MKP-1, a nuclear phosphatase, heparin treated cells exhibited decreases in nuclear ERK activity more rapidly than cells not treated with heparin.	Heparin	57-64	mitogen-activated protein kinase 1	Homo sapiens	110-113
20235148-9	2010	Consistent with a role for MKP-1, a nuclear phosphatase, heparin treated cells exhibited decreases in nuclear ERK activity more rapidly than cells not treated with heparin.	Heparin	164-171	dual specificity phosphatase 1	Homo sapiens	27-32
20235148-10	2010	The data support MKP-1 as a heparin-induced phosphatase that dephosphorylates ERK, decreasing ERK activity, in vascular smooth muscle cells.	Heparin	28-35	dual specificity phosphatase 1	Homo sapiens	17-22
20235148-10	2010	The data support MKP-1 as a heparin-induced phosphatase that dephosphorylates ERK, decreasing ERK activity, in vascular smooth muscle cells.	Heparin	28-35	mitogen-activated protein kinase 1	Homo sapiens	78-81
20235148-10	2010	The data support MKP-1 as a heparin-induced phosphatase that dephosphorylates ERK, decreasing ERK activity, in vascular smooth muscle cells.	Heparin	28-35	mitogen-activated protein kinase 1	Homo sapiens	94-97
20302899-0	2010	Efficient delivery of VEGF via heparin-functionalized nanoparticle-fibrin complex.	Heparin	31-38	vascular endothelial growth factor A	Homo sapiens	22-26
20132164-10	2010	Heparin was able to reverse aPL-dependent inhibition of trophoblast IL-6 secretion and migration.	Heparin	0-7	interleukin 6	Homo sapiens	68-72
20408165-5	2010	The inhibition effect of heparin on T4 PNKP and theophylline on CIP is also quantitatively characterized.	Heparin	25-32	polynucleotide kinase 3'-phosphatase	Bos taurus	39-43
20230412-8	2010	Thromboelastographic and thrombin generation parameters concurred with APTT, demonstrating a genuine heparin resistance in the presence of high FVIII levels.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	25-33
20153840-5	2010	Injection of APOA5 Tg mice with heparin increased plasma apoA-V protein levels by approximately 25% indicating the existence of a heparin-releasable pool.	Heparin	32-39	apolipoprotein A-V	Mus musculus	13-18
20153840-5	2010	Injection of APOA5 Tg mice with heparin increased plasma apoA-V protein levels by approximately 25% indicating the existence of a heparin-releasable pool.	Heparin	32-39	apolipoprotein A-V	Mus musculus	57-63
20153840-5	2010	Injection of APOA5 Tg mice with heparin increased plasma apoA-V protein levels by approximately 25% indicating the existence of a heparin-releasable pool.	Heparin	130-137	apolipoprotein A-V	Mus musculus	13-18
20153840-5	2010	Injection of APOA5 Tg mice with heparin increased plasma apoA-V protein levels by approximately 25% indicating the existence of a heparin-releasable pool.	Heparin	130-137	apolipoprotein A-V	Mus musculus	57-63
20032204-1	2010	Pleiotrophin (PTN) is a polypeptide that belongs to a family of heparin-binding growth factors; it displays mitogenic activity for a wide variety of cells.	Heparin	64-71	pleiotrophin	Homo sapiens	0-12
20032204-1	2010	Pleiotrophin (PTN) is a polypeptide that belongs to a family of heparin-binding growth factors; it displays mitogenic activity for a wide variety of cells.	Heparin	64-71	pleiotrophin	Homo sapiens	14-17
20083103-8	2010	In addition, MAB730 was more efficient than heparin at inhibiting CXCL14 binding to low affinity receptors on THP-1 cells.	Heparin	44-51	C-X-C motif chemokine ligand 14	Homo sapiens	66-72
20381830-3	2010	In the platelets of rats and humans, HMWF-Q demonstrated a pro-aggregation response, whereas F-Q (like the commercially purchased fucoidan (F-S) and heparin), showed an inhibitory effect on thrombin-induced aggregation with an IC(50) of 8 microg/mL, approximately five times lower than those of F-S and heparin.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	190-198
20381830-3	2010	In the platelets of rats and humans, HMWF-Q demonstrated a pro-aggregation response, whereas F-Q (like the commercially purchased fucoidan (F-S) and heparin), showed an inhibitory effect on thrombin-induced aggregation with an IC(50) of 8 microg/mL, approximately five times lower than those of F-S and heparin.	Heparin	303-310	coagulation factor II, thrombin	Homo sapiens	190-198
20381830-6	2010	The inhibitory effects of F-Q and heparin on thrombin activity were strikingly enhanced by either antithrombin (AT) or heparin cofactor II (HCII).	Heparin	34-41	coagulation factor II	Rattus norvegicus	45-53
20422052-2	2010	We recently discovered that 1) FGF1 directly binds to integrin alphavbeta3, 2) the integrin-binding site and FGF receptor (FGFR) binding site are distinct, and 3) the integrin-binding-defective FGF1 mutant (R50E) is defective in inducing FGF signaling although R50E still binds to FGFR and heparin and induces transient ERK1/2 activation.	Heparin	290-297	fibroblast growth factor 1	Mus musculus	31-35
20351192-8	2010	C1s also bound to heparin, with lower affinity (K(D) = 108 x 10(-8) M).	Heparin	18-25	complement C1s	Homo sapiens	0-3
20351192-9	2010	Using the same technique, 50% inhibition of the binding of C1 inhibitor and C1s to heparin was achieved using heparin oligomers containing eight and six saccharide units, respectively.	Heparin	83-90	complement C1s	Homo sapiens	76-79
20351192-9	2010	Using the same technique, 50% inhibition of the binding of C1 inhibitor and C1s to heparin was achieved using heparin oligomers containing eight and six saccharide units, respectively.	Heparin	110-117	complement C1s	Homo sapiens	76-79
20351192-11	2010	Using a thermal shift assay, heparin was shown to interact with the C1s serine protease domain and the C1 inhibitor serpin domain, increasing and decreasing their thermal stability, respectively.	Heparin	29-36	complement C1s	Homo sapiens	68-71
20124439-5	2010	When the GPIHBP1-C65Y homozygote was given an intravenous bolus of heparin, only trace amounts of LPL entered the plasma.	Heparin	67-74	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	9-16
20155947-4	2010	It was observed that the amount of heparin and bFGF bound to aortic heart valve leaflets was directly proportional to the concentration of heparin and bFGF in the incubation medium.	Heparin	35-42	fibroblast growth factor 2	Homo sapiens	151-155
20155947-4	2010	It was observed that the amount of heparin and bFGF bound to aortic heart valve leaflets was directly proportional to the concentration of heparin and bFGF in the incubation medium.	Heparin	139-146	fibroblast growth factor 2	Homo sapiens	47-51
20463930-0	2010	Preparation and characterization of low-molecular-weight heparin/protamine nanoparticles (LMW-H/P NPs) as FGF-2 carrier.	Heparin	57-64	fibroblast growth factor 2	Homo sapiens	106-111
20463930-1	2010	We produced low-molecular-weight heparin/protamine nanoparticles (LMW-H/P NPs) as a carrier for heparin-binding growth factors, such as fibroblast growth factor-2 (FGF-2).	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	136-162
20463930-1	2010	We produced low-molecular-weight heparin/protamine nanoparticles (LMW-H/P NPs) as a carrier for heparin-binding growth factors, such as fibroblast growth factor-2 (FGF-2).	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	164-169
20463930-1	2010	We produced low-molecular-weight heparin/protamine nanoparticles (LMW-H/P NPs) as a carrier for heparin-binding growth factors, such as fibroblast growth factor-2 (FGF-2).	Heparin	96-103	fibroblast growth factor 2	Homo sapiens	136-162
20463930-1	2010	We produced low-molecular-weight heparin/protamine nanoparticles (LMW-H/P NPs) as a carrier for heparin-binding growth factors, such as fibroblast growth factor-2 (FGF-2).	Heparin	96-103	fibroblast growth factor 2	Homo sapiens	164-169
20497684-13	2010	High- and low-dose Danshensu"s significant effects on reduced thrombin time level are same to heparin.	Heparin	94-101	coagulation factor II	Mus musculus	62-70
20390444-7	2010	RESULTS: Unfractionated heparin (UFH), the historical standard of care for anticoagulation in STEMI and NSTEMI patients undergoing PCI, is sub-optimal and the list of anticoagulants recommended for alternatives in the current guidelines has expanded to include superior anticoagulants, including the low-molecular-weight heparin enoxaparin and the direct thrombin inhibitor bivalirudin.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	355-363
20390444-7	2010	RESULTS: Unfractionated heparin (UFH), the historical standard of care for anticoagulation in STEMI and NSTEMI patients undergoing PCI, is sub-optimal and the list of anticoagulants recommended for alternatives in the current guidelines has expanded to include superior anticoagulants, including the low-molecular-weight heparin enoxaparin and the direct thrombin inhibitor bivalirudin.	Heparin	33-36	coagulation factor II, thrombin	Homo sapiens	355-363
20124439-7	2010	When the GPIHBP1-Q115P homozygote was given a 6-hour infusion of heparin, a significant amount of LPL appeared in the plasma, resulting in a fall in the plasma triglyceride levels from 1780 to 120 mg/dL.	Heparin	65-72	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	9-16
19049846-2	2010	Unfractionated heparins release vessel-bound MPO and increase endothelial NO bioavailability.	Heparin	15-23	myeloperoxidase	Homo sapiens	45-48
19049846-3	2010	Whether low molecular weight heparins also affect circulating MPO levels and NO dependent vasoreactivity however remains elusive.	Heparin	29-37	myeloperoxidase	Homo sapiens	62-65
19049846-7	2010	DISCUSSION: This study confirms the concept that heparins improve endothelial function, an established read-out of vascular NO bioavailability, by mobilizing vessel bound MPO.	Heparin	49-57	myeloperoxidase	Homo sapiens	171-174
19886733-3	2010	The heparin-conjugated fibrinogen formed an injectable, heparin-conjugated fibrin (HCF) gel when mixed with thrombin.	Heparin	4-11	coagulation factor II	Rattus norvegicus	108-116
20059668-3	2010	The classic anticoagulant unfractionated heparin is giving way to low-molecular-weight heparin, the pentasaccharide fondaparinux and the direct thrombin inhibitor bivalirudin.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	144-152
20036698-6	2010	Of all GAGs tested, heparin was the strongest inducer of aggregation of DAbeta(1-40) in the different aggregation assays, with both heparin and heparan sulfate reducing Abeta-induced cellular toxicity.	Heparin	20-27	amyloid beta precursor protein	Homo sapiens	73-78
20036698-9	2010	We conclude that sulfate moieties within GAGs, like heparin and HS, have an important role in Abeta aggregation in CAA and in Abeta-mediated toxicity of cerebrovascular cells.	Heparin	52-59	amyloid beta precursor protein	Homo sapiens	94-99
20036698-9	2010	We conclude that sulfate moieties within GAGs, like heparin and HS, have an important role in Abeta aggregation in CAA and in Abeta-mediated toxicity of cerebrovascular cells.	Heparin	52-59	amyloid beta precursor protein	Homo sapiens	126-131
19886733-3	2010	The heparin-conjugated fibrinogen formed an injectable, heparin-conjugated fibrin (HCF) gel when mixed with thrombin.	Heparin	56-63	coagulation factor II	Rattus norvegicus	108-116
20010091-1	2010	Whereas heparin functions as an antithrombotic agent by promoting antithrombin III-based inhibition of thrombin and factor Xa, there is less appreciation for the combination behavior with small-molecule, direct inhibitors of these proteases.	Heparin	8-15	coagulation factor II	Rattus norvegicus	70-78
20053992-1	2010	Inactivation of thrombin (T) by the serpins heparin cofactor II (HCII) and antithrombin (AT) is accelerated by a heparin template between the serpin and thrombin exosite II.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	16-24
20212142-0	2010	Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein.	Heparin	42-49	amyloid beta precursor protein	Homo sapiens	74-99
20064650-3	2010	Affinity to GAG has been evaluated by sorption on heparin-Sepharose.	Heparin	50-57	melanoma antigen	Mus musculus	12-15
22993547-5	2010	Quantitative PCR showed that PDL cells expressed mRNA for the EC-specific markers, VE-cadherin and VEGFR2, when cultured in the presence of heparin alone or with FGF-2.	Heparin	140-147	cadherin 5	Homo sapiens	83-94
20028946-5	2010	When the decline in FFAs was prevented by concomitant infusion of Intralipid and heparin, the production rates of VLDL1 and VLDL2-apoB48 and -apoB100 were intermediate between insulin and glucose infusion and saline control.	Heparin	81-88	apolipoprotein B	Homo sapiens	130-136
20028946-5	2010	When the decline in FFAs was prevented by concomitant infusion of Intralipid and heparin, the production rates of VLDL1 and VLDL2-apoB48 and -apoB100 were intermediate between insulin and glucose infusion and saline control.	Heparin	81-88	apolipoprotein B	Homo sapiens	142-149
20028946-5	2010	When the decline in FFAs was prevented by concomitant infusion of Intralipid and heparin, the production rates of VLDL1 and VLDL2-apoB48 and -apoB100 were intermediate between insulin and glucose infusion and saline control.	Heparin	81-88	insulin	Homo sapiens	176-183
20177350-0	2010	Insulin-heparin infusions peritransplant substantially improve single-donor clinical islet transplant success.	Heparin	8-15	insulin	Homo sapiens	0-7
20124102-8	2010	In kinetic binding studies, KC, MIP-2, and rhCXCL8 bound heparin differently, with KC associating and dissociating more rapidly from immobilized heparin than the other chemokines.	Heparin	57-64	chemokine (C-X-C motif) ligand 2	Mus musculus	32-37
20002544-10	2010	CONCLUSION: Polyphosphate interacts with thrombin"s exosite II at a site that partially overlaps with, but is not identical to, the heparin-binding site.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	41-49
20021270-0	2010	Anchoring of vascular endothelial growth factor to surface-immobilized heparin on pancreatic islets: implications for stimulating islet angiogenesis.	Heparin	71-78	vascular endothelial growth factor A	Homo sapiens	13-47
20021270-3	2010	In this study, we have investigated the ability of an immobilized conjugate composed of heparin to bind the angiogenic growth factor vascular endothelial growth factor-A (VEGF-A) as a means of attracting endothelial cells (ECs) to induce angiogenesis and revascularization.	Heparin	88-95	vascular endothelial growth factor A	Homo sapiens	133-167
20021270-3	2010	In this study, we have investigated the ability of an immobilized conjugate composed of heparin to bind the angiogenic growth factor vascular endothelial growth factor-A (VEGF-A) as a means of attracting endothelial cells (ECs) to induce angiogenesis and revascularization.	Heparin	88-95	vascular endothelial growth factor A	Homo sapiens	171-177
20021270-4	2010	We analyzed the capacity of VEGF-A to bind to immobilized heparin and how this affected the proliferation and adherence of ECs to both artificial glass surfaces and islets.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	28-34
20021270-5	2010	Quartz crystal microbalance with dissipation monitoring and slot-blot demonstrated the binding of VEGF-A to heparin-coated surfaces upon which ECs showed protein-dependent proliferation.	Heparin	108-115	vascular endothelial growth factor A	Homo sapiens	98-104
19811766-3	2010	During the manufacturing process heparin and heparin-binding growth factors, such as VEGF(165) and bFGF, were incorporated into the fibrin layer.	Heparin	33-40	vascular endothelial growth factor A	Homo sapiens	85-89
19811766-3	2010	During the manufacturing process heparin and heparin-binding growth factors, such as VEGF(165) and bFGF, were incorporated into the fibrin layer.	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	99-103
19811766-3	2010	During the manufacturing process heparin and heparin-binding growth factors, such as VEGF(165) and bFGF, were incorporated into the fibrin layer.	Heparin	45-52	vascular endothelial growth factor A	Homo sapiens	85-89
19811766-3	2010	During the manufacturing process heparin and heparin-binding growth factors, such as VEGF(165) and bFGF, were incorporated into the fibrin layer.	Heparin	45-52	fibroblast growth factor 2	Homo sapiens	99-103
20177350-5	2010	Using multivariate analysis, only the use of insulin and heparin infusions peritransplant was a significant factor associated with insulin independence, with an adjusted odds ratio of 8.6 (95% confidence interval 2.0-37.0).	Heparin	57-64	insulin	Homo sapiens	131-138
20177350-6	2010	Patients who had received insulin and heparin infusions peritransplant had greater indices of islet engraftment and a greater reduction in insulin use (80.1% + or - 4.3% vs. 54.2% + or - 2.8%, P&lt;0.001) even if insulin independence was not achieved.	Heparin	38-45	insulin	Homo sapiens	139-146
20177350-6	2010	Patients who had received insulin and heparin infusions peritransplant had greater indices of islet engraftment and a greater reduction in insulin use (80.1% + or - 4.3% vs. 54.2% + or - 2.8%, P&lt;0.001) even if insulin independence was not achieved.	Heparin	38-45	insulin	Homo sapiens	139-146
19054792-2	2010	Direct thrombin inhibitors are now standard therapy for the prevention of thrombosis in heparin-induced thrombocytopenia.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	7-15
20103015-2	2010	However, a common limitation of unfractionated heparin and low-molecular-weight heparin is that neither can neutralize clot-bound thrombin.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	130-138
19845689-0	2010	Heparin regulates colon cancer cell growth through p38 mitogen-activated protein kinase signalling.	Heparin	0-7	mitogen-activated protein kinase 14	Homo sapiens	51-54
19845689-4	2010	RESULTS: Treatment with a highly specific p38 kinase inhibitor, SB203580, significantly (50-70%) inhibited heparin-induced colon cancer cell growth, demonstrating that p38 MAPK signalling is involved in their heparin-induced proliferative response.	Heparin	107-114	mitogen-activated protein kinase 14	Homo sapiens	42-45
19845689-4	2010	RESULTS: Treatment with a highly specific p38 kinase inhibitor, SB203580, significantly (50-70%) inhibited heparin-induced colon cancer cell growth, demonstrating that p38 MAPK signalling is involved in their heparin-induced proliferative response.	Heparin	107-114	mitogen-activated protein kinase 14	Homo sapiens	168-171
19845689-4	2010	RESULTS: Treatment with a highly specific p38 kinase inhibitor, SB203580, significantly (50-70%) inhibited heparin-induced colon cancer cell growth, demonstrating that p38 MAPK signalling is involved in their heparin-induced proliferative response.	Heparin	209-216	mitogen-activated protein kinase 14	Homo sapiens	42-45
19845689-4	2010	RESULTS: Treatment with a highly specific p38 kinase inhibitor, SB203580, significantly (50-70%) inhibited heparin-induced colon cancer cell growth, demonstrating that p38 MAPK signalling is involved in their heparin-induced proliferative response.	Heparin	209-216	mitogen-activated protein kinase 14	Homo sapiens	168-171
19845689-6	2010	Furthermore, heparin inhibited cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and p53 tumour suppressor gene and protein expression up to 2-fold or 1.8-fold, respectively, and stimulated cyclin D1 expression up to 1.8-fold, in these cell lines through a p38-mediated mechanism.	Heparin	13-20	cyclin dependent kinase inhibitor 1A	Homo sapiens	65-68
19845689-6	2010	Furthermore, heparin inhibited cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and p53 tumour suppressor gene and protein expression up to 2-fold or 1.8-fold, respectively, and stimulated cyclin D1 expression up to 1.8-fold, in these cell lines through a p38-mediated mechanism.	Heparin	13-20	cyclin dependent kinase inhibitor 1A	Homo sapiens	69-73
19845689-6	2010	Furthermore, heparin inhibited cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and p53 tumour suppressor gene and protein expression up to 2-fold or 1.8-fold, respectively, and stimulated cyclin D1 expression up to 1.8-fold, in these cell lines through a p38-mediated mechanism.	Heparin	13-20	cyclin dependent kinase inhibitor 1A	Homo sapiens	74-78
19845689-6	2010	Furthermore, heparin inhibited cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and p53 tumour suppressor gene and protein expression up to 2-fold or 1.8-fold, respectively, and stimulated cyclin D1 expression up to 1.8-fold, in these cell lines through a p38-mediated mechanism.	Heparin	13-20	tumor protein p53	Homo sapiens	84-87
19845689-6	2010	Furthermore, heparin inhibited cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and p53 tumour suppressor gene and protein expression up to 2-fold or 1.8-fold, respectively, and stimulated cyclin D1 expression up to 1.8-fold, in these cell lines through a p38-mediated mechanism.	Heparin	13-20	mitogen-activated protein kinase 14	Homo sapiens	256-259
19845689-8	2010	CONCLUSIONS: This study demonstrates that an extracellular glycosaminoglycan, heparin, finely modulates expression of genes crucial to cell cycle regulation through specific activation of p38 MAP kinase to stimulate colon cancer cell growth.	Heparin	78-85	mitogen-activated protein kinase 14	Homo sapiens	188-191
19959474-0	2010	Heparin enhances serpin inhibition of the cysteine protease cathepsin L.	Heparin	0-7	cathepsin L	Homo sapiens	60-71
19959474-2	2010	As an anticoagulant, heparin enhances inhibition of thrombin by the serpin antithrombin III, but a similar cofactor role has not been previously investigated for proteases linked to metastasis.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	52-60
19959474-5	2010	The presence of heparin accelerated inhibition of cathepsin L by both serpins, and in the case of SCCA-1, heparin increased the second order inhibition rate constant from 5.4 x 10(5) to &gt;10(8), indicating a rate enhancement of at least 180-fold.	Heparin	16-23	cathepsin L	Homo sapiens	50-61
19959474-5	2010	The presence of heparin accelerated inhibition of cathepsin L by both serpins, and in the case of SCCA-1, heparin increased the second order inhibition rate constant from 5.4 x 10(5) to &gt;10(8), indicating a rate enhancement of at least 180-fold.	Heparin	106-113	cathepsin L	Homo sapiens	50-61
19959474-7	2010	Furthermore, SCCA-1 inhibition of cathepsin L-like proteolytic activity secreted from breast and melanoma cancer cell lines was significantly enhanced by heparin.	Heparin	154-161	cathepsin L	Homo sapiens	34-45
19937274-4	2010	The objectives of this study were to examine: (1) the conditions over which delivery of bFGF can be controlled from a heparin-binding delivery system (HBDS) and (2) the effect of bFGF and PDGF-BB released from this system on tendon fibroblast proliferation and matrix gene expression in vitro over a 10-day interval.	Heparin	118-125	fibroblast growth factor 2	Homo sapiens	88-92
20083913-5	2010	Heparin-induced thrombocytopenia represents a unique clinical situation in which all sources of heparin must be discontinued and the patient started on an alternative anticoagulant (e.g., a direct thrombin inhibitor) in the acute setting.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	197-205
20024502-7	2010	The same results were obtained for the mutant AT inhibition of thrombin and factor VIIa, however, heparin accelerated the mutant AT inhibition of factor XIa ~10-fold.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	63-71
19942256-1	2010	BACKGROUND: Point of care (POC) devices measuring the international normalized ratio (INR) are accurate for patients with stable disease, but their efficiency has not been prospectively assessed during the "bridging period" when patients are receiving a low molecular weight heparin (LMWH) on top of a vitamin K antagonist (VKA) until the target INR is reached.	Heparin	275-282	proopiomelanocortin	Homo sapiens	27-30
20000697-7	2010	The anticoagulant effect of heparin on the prothrombin time was exemplarily shown as well as the reverse effect of the heparin antagonist polybrene.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	43-54
20186683-1	2010	The direct thrombin inhibitor lepirudin is mainly applied in heparin-induced thrombocytopenia.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	11-19
20110884-8	2010	We also produced an aptamer heterodimer consisting of our previously derived aptamer (del5-1), which binds to the heparin-binding domain of VEGF, linked to V7t1.	Heparin	114-121	vascular endothelial growth factor A	Homo sapiens	140-144
19906646-0	2010	Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site.	Heparin	132-139	amyloid beta precursor protein	Homo sapiens	97-122
19928997-7	2010	Adhesion of cells to DP-4 was strongly inhibited by heparin.	Heparin	52-59	transcription factor Dp family member 3	Homo sapiens	21-25
19928997-9	2010	DP-4 specifically interacted with biotinylated heparin, and this interaction was inhibited by unlabeled heparin.	Heparin	47-54	transcription factor Dp family member 3	Homo sapiens	0-4
19928997-9	2010	DP-4 specifically interacted with biotinylated heparin, and this interaction was inhibited by unlabeled heparin.	Heparin	104-111	transcription factor Dp family member 3	Homo sapiens	0-4
20134155-1	2010	BACKGROUND: Philadelphia-negative myeloproliferative disorders (Ph-MPD) are common causes of unusual splanchnic or cerebral vein thrombosis, which is treated with unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	216-223	mevalonate diphosphate decarboxylase	Homo sapiens	67-70
20134155-1	2010	BACKGROUND: Philadelphia-negative myeloproliferative disorders (Ph-MPD) are common causes of unusual splanchnic or cerebral vein thrombosis, which is treated with unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	178-185	mevalonate diphosphate decarboxylase	Homo sapiens	67-70
20134155-1	2010	BACKGROUND: Philadelphia-negative myeloproliferative disorders (Ph-MPD) are common causes of unusual splanchnic or cerebral vein thrombosis, which is treated with unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	187-190	mevalonate diphosphate decarboxylase	Homo sapiens	67-70
20134155-2	2010	Heparin-induced thrombocytopenia (HIT) is a dangerous potential complication of this therapy, but it has rarely been reported in Ph-MPD.	Heparin	0-7	mevalonate diphosphate decarboxylase	Homo sapiens	132-135
20134155-3	2010	PATIENTS AND METHODS: We retrospectively reviewed clinical records of 29 patients with Ph-MPD who have been treated with UFH or LMWH for unusual splanchnic or cerebral vein thrombosis (3 cerebral sinus, 6 portal and 20 hepatic vein).	Heparin	121-124	mevalonate diphosphate decarboxylase	Homo sapiens	90-93
20134155-7	2010	CONCLUSIONS: Ph-MPD patients on heparin warrant careful monitoring and HIT has to be suspected whenever platelet counts drop or a new thrombosis is detectable.	Heparin	32-39	mevalonate diphosphate decarboxylase	Homo sapiens	16-19
20103278-2	2010	Thrombin formation and fibrinolysis primarily occur in the surgical wound and peak at the time heparin is reversed by protamine.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	0-8
20238034-10	2010	VEGF inhibition drugs have been used successfully in clinical treatment, but the cost is prohibitive.Protamine sulfate is a common, inexpensive anti-coagulation drug widely used for anti-coagulation in cases when heparin has been overused in the clinic.	Heparin	213-220	vascular endothelial growth factor A	Homo sapiens	0-4
20068292-10	2010	CONCLUSION: CLS with heparin/gentamicin tended to decrease CRI compared to citrate 46% and heparin and frankly improved the CRP course after catheter insertion.	Heparin	21-28	C-reactive protein	Homo sapiens	124-127
20232702-4	2010	As a serine protease, it inactivates thrombin and the efficiency of this reaction is intensified by heparin.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	37-45
19641290-3	2010	Here, we report on collagen sponges in which vascular endothelial growth factor (VEGF) was immobilized through physical binding to heparin, covalently incorporated in the matrix via cross-linking with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysuccinimide.	Heparin	131-138	vascular endothelial growth factor A	Homo sapiens	45-79
19641290-3	2010	Here, we report on collagen sponges in which vascular endothelial growth factor (VEGF) was immobilized through physical binding to heparin, covalently incorporated in the matrix via cross-linking with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and N-hydroxysuccinimide.	Heparin	131-138	vascular endothelial growth factor A	Homo sapiens	81-85
19907188-6	2010	HLP or heparin significantly reduced vascular intervention-induced increases in C-reactive protein, P-selectin and interleukin-6 in serum.	Heparin	7-14	C-reactive protein	Rattus norvegicus	80-98
19634004-0	2010	Loading of VEGF to the heparin cross-linked demineralized bone matrix improves vascularization of the scaffold.	Heparin	23-30	vascular endothelial growth factor A	Homo sapiens	11-15
19634004-2	2010	Here, heparin cross-linked demineralized bone matrices (HC-DBM) pre-loaded with vascular endothelial growth factor (VEGF) were designed to promote cells and new microvessels invasion into the matrices.	Heparin	6-13	vascular endothelial growth factor A	Homo sapiens	80-114
19634004-2	2010	Here, heparin cross-linked demineralized bone matrices (HC-DBM) pre-loaded with vascular endothelial growth factor (VEGF) were designed to promote cells and new microvessels invasion into the matrices.	Heparin	6-13	vascular endothelial growth factor A	Homo sapiens	116-120
19634004-3	2010	After being chemical crosslinked with heparin by N-hydroxysuccinimide and N-(3-di-methylaminopropyl)-N"-ethylcarbodiimide, the scaffold could bind more VEGF than the non-crosslinked one and achieve localized and sustained delivery.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	152-156
19634004-7	2010	The results demonstrated that heparin cross-linked DBM binding VEGF could be a useful strategy to stimulate cells and blood vessels invasion into the scaffolds.	Heparin	30-37	vascular endothelial growth factor A	Homo sapiens	63-67
21694935-3	2010	Moreover, angiotensin II inhibits heparan sulfate synthesis, while heparins modulate angiotensin II signaling in glomerular cells, inhibiting aldosterone synthesis and lowering proteinuria in diabetes patients.	Heparin	67-75	angiotensinogen	Homo sapiens	85-99
19907188-6	2010	HLP or heparin significantly reduced vascular intervention-induced increases in C-reactive protein, P-selectin and interleukin-6 in serum.	Heparin	7-14	selectin P	Rattus norvegicus	100-110
19907188-6	2010	HLP or heparin significantly reduced vascular intervention-induced increases in C-reactive protein, P-selectin and interleukin-6 in serum.	Heparin	7-14	interleukin 6	Rattus norvegicus	115-128
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	224-231	coagulation factor II, thrombin	Homo sapiens	134-142
20816204-1	2010	Sulf-1 and Sulf-2 are extracellular endoglucosamine 6-sulfatases, which selectively liberate the 6-O-sulfate groups on glucosamines present in N, 6-O, and 2-O trisulfated disaccharides of intact heparan sulfate (HS)/heparin chains.	Heparin	216-223	sulfatase 1	Homo sapiens	0-6
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	224-231	coagulation factor II, thrombin	Homo sapiens	166-174
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	224-231	coagulation factor II, thrombin	Homo sapiens	166-174
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	259-266	coagulation factor II, thrombin	Homo sapiens	134-142
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	259-266	coagulation factor II, thrombin	Homo sapiens	166-174
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	259-266	coagulation factor II, thrombin	Homo sapiens	166-174
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	259-266	coagulation factor II, thrombin	Homo sapiens	134-142
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	259-266	coagulation factor II, thrombin	Homo sapiens	166-174
20807654-5	2010	This chapter shows that: (1) the contact system can be activated by a variety of unrelated molecules; (2) kallikrein directly cuts prothrombin to generate functional thrombin through contact system activation; and (3) while heparin contaminants, oversulfated heparin by-product (OS-HB), induce thrombin generation in both normal and HIT patient plasmas through contact system activation, authentic heparin induces thrombin activities only in HIT patient plasmas containing autoantibodies against protein/heparin complex.	Heparin	259-266	coagulation factor II, thrombin	Homo sapiens	166-174
20807654-7	2010	The newly discovered mechanism of heparin-induced thrombin activity could explain the increased incidence of HIT in patients exposed to contaminated heparin.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	50-58
20807654-7	2010	The newly discovered mechanism of heparin-induced thrombin activity could explain the increased incidence of HIT in patients exposed to contaminated heparin.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	50-58
19748283-8	2009	Further in vitro experiments indicate that heparin prevents the activation of latent TGF-beta into its bioactive form probably by virtue of accelerating the complex-formation between AT-III and thrombin.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	194-202
19961422-6	2009	The identified proteinases contained heparin-binding motifs inherent in the complex-forming partners of CP, such as lactoferrin, myeloperoxidase, and serprocidines.	Heparin	37-44	myeloperoxidase	Homo sapiens	129-144
20062740-7	2009	CASE PRESENTATION: We describe the case of a 60-year-old female, Caucasian patient suffering from lipoprotein glomerulopathy, carrier of a new mutation on the Apolipoprotein E gene (Apolipoprotein E(MODENA)), and treated successfully with low density lipoprotein-apheresis with the Heparin induced extracorporeal lipoprotein precipitation system.	Heparin	282-289	apolipoprotein E	Homo sapiens	159-175
20062740-7	2009	CASE PRESENTATION: We describe the case of a 60-year-old female, Caucasian patient suffering from lipoprotein glomerulopathy, carrier of a new mutation on the Apolipoprotein E gene (Apolipoprotein E(MODENA)), and treated successfully with low density lipoprotein-apheresis with the Heparin induced extracorporeal lipoprotein precipitation system.	Heparin	282-289	apolipoprotein E	Homo sapiens	182-198
19748283-7	2009	Importantly, levels of bioactive TGF-beta in blood collected into heparin but not EDTA tubes remained stable up to 18 h, even when kept at RT.	Heparin	66-73	transforming growth factor beta 1	Homo sapiens	33-41
19748283-8	2009	Further in vitro experiments indicate that heparin prevents the activation of latent TGF-beta into its bioactive form probably by virtue of accelerating the complex-formation between AT-III and thrombin.	Heparin	43-50	transforming growth factor beta 1	Homo sapiens	85-93
19826702-1	2009	Using an acoustic method we showed that the aptamer configuration, especially those comprised of dimers with binding exosites sensitive to heparin and fibrinogen at thrombin, substantially increases the aptasensor sensitivity.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	165-173
19465079-9	2009	Thus, the N-terminal portion of B-CK is critical to mediate its affinity to heparin and control enzyme activity, which may be important for regulating energy metabolism in neural tissues such as brain and retina, unique organs abundant in heparan sulfates.	Heparin	76-83	creatine kinase B	Gallus gallus	32-36
19929245-0	2009	Thrombin-inducible platelet adhesion and regulation of the platelet seven-transmembrane thrombin receptor-1 (PAR-1): effects of unfractionated heparin and lepirudin.	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	0-8
19929245-8	2009	Further, heparin and lepirudin inhibited thrombin-inducible cleavage and internalization of PAR-1 at a dosage of 1.0 U/ml and 1.6 microg/ml, respectively (p = 0.004).	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	41-49
19929245-8	2009	Further, heparin and lepirudin inhibited thrombin-inducible cleavage and internalization of PAR-1 at a dosage of 1.0 U/ml and 1.6 microg/ml, respectively (p = 0.004).	Heparin	9-16	coagulation factor II thrombin receptor	Homo sapiens	92-97
19929245-9	2009	Thus, heparin and lepirudin inhibit thrombin-inducible platelet activation in vitro to a similar extent.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	36-44
19819428-3	2009	Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures.	Heparin	197-204	fibroblast growth factor 1	Homo sapiens	123-128
19819428-3	2009	Molecular docking calculations showed that the predicted locations of the disaccharide sulfo groups in the binding site of FGF-1 and FGF-2 are similar to the positions observed for co-crystallized heparin-derived oligosaccharides obtained from published crystal structures.	Heparin	197-204	fibroblast growth factor 2	Homo sapiens	133-138
19925675-13	2009	In vitro clot strength and clot kinetics, as determined by TEG in heparin + clopidogrel samples, were positively associated with the amount of rThrombin activity added for clot initiation.	Heparin	66-73	coagulation factor II	Rattus norvegicus	143-152
19925675-14	2009	CONCLUSION: In an animal model designed to replicate the anti-coagulation regimens encountered in clinical settings, topical rThrombin at 1000 IU/mL more reliably controlled the pharmacological effects of heparin or heparin + clopidogrel on hemostasis than rThrombin at 125 IU/mL.	Heparin	205-212	coagulation factor II	Rattus norvegicus	125-134
19925675-14	2009	CONCLUSION: In an animal model designed to replicate the anti-coagulation regimens encountered in clinical settings, topical rThrombin at 1000 IU/mL more reliably controlled the pharmacological effects of heparin or heparin + clopidogrel on hemostasis than rThrombin at 125 IU/mL.	Heparin	216-223	coagulation factor II	Rattus norvegicus	125-134
19542565-6	2009	ANGPTL3 also inhibited heparin-stabilized LPL but with less potency than nonstabilized LPL.	Heparin	23-30	angiopoietin-like 3	Mus musculus	0-7
19925675-8	2009	RESULTS: TTH decreased with increasing concentrations of rThrombin in heparin-treated animals and was shorter after treatment with 1000 IU/mL rThrombin (73 seconds) than with 125 IU/mL rThrombin (78 seconds; p = 0.007).	Heparin	70-77	coagulation factor II	Rattus norvegicus	57-66
19925675-9	2009	TTH also decreased with increasing concentrations of rThrombin in heparin + clopidogrel treated animals; again it was significantly shorter after treatment with 1000 IU/mL rThrombin (71 seconds) than with 125 IU/mL rThrombin (177 seconds; p &lt; 0.001).	Heparin	66-73	coagulation factor II	Rattus norvegicus	53-62
19925675-9	2009	TTH also decreased with increasing concentrations of rThrombin in heparin + clopidogrel treated animals; again it was significantly shorter after treatment with 1000 IU/mL rThrombin (71 seconds) than with 125 IU/mL rThrombin (177 seconds; p &lt; 0.001).	Heparin	66-73	coagulation factor II	Rattus norvegicus	172-181
19925675-9	2009	TTH also decreased with increasing concentrations of rThrombin in heparin + clopidogrel treated animals; again it was significantly shorter after treatment with 1000 IU/mL rThrombin (71 seconds) than with 125 IU/mL rThrombin (177 seconds; p &lt; 0.001).	Heparin	66-73	coagulation factor II	Rattus norvegicus	172-181
19925675-10	2009	Variability in TTH was significantly smaller after treatment with 1000 IU/mL rThrombin than after 125 IU/mL rThrombin, indicating greater reliability of clot formation (p &lt; 0.001 for heparin or heparin + clopidogrel treatments).	Heparin	186-193	coagulation factor II	Rattus norvegicus	77-86
19902129-1	2009	Human tissue factor pathway inhibitor-2 (hTFPI-2) is a serine protease inhibitor and its inhibitory activity is enhanced by heparin.	Heparin	124-131	tissue factor pathway inhibitor 2	Homo sapiens	6-39
19818773-4	2009	We propose a quite different mechanism in which heparin activates antithrombin by mitigating an unfavorable surface interaction, by altering its nature, and by moving the attached proteinase away from the site of the unfavorable interaction through RCL expulsion.	Heparin	48-55	endogenous retrovirus group K member 25	Homo sapiens	180-190
19902129-1	2009	Human tissue factor pathway inhibitor-2 (hTFPI-2) is a serine protease inhibitor and its inhibitory activity is enhanced by heparin.	Heparin	124-131	tissue factor pathway inhibitor 2	Homo sapiens	41-48
19902129-2	2009	The Kunitz domain 3 and Cterminal of hTFPI-2 (hTFPI-2/KD3C), which has the activity toward heparin calcium, have been successfully expressed in Pichia pastoris and purified by SPSepharose and heparin-Sepharose chromatography.	Heparin	91-98	tissue factor pathway inhibitor 2	Homo sapiens	37-44
19902129-2	2009	The Kunitz domain 3 and Cterminal of hTFPI-2 (hTFPI-2/KD3C), which has the activity toward heparin calcium, have been successfully expressed in Pichia pastoris and purified by SPSepharose and heparin-Sepharose chromatography.	Heparin	91-98	tissue factor pathway inhibitor 2	Homo sapiens	46-58
19795099-0	2009	[Heparin-induced thrombocytopenia type II with thrombosis in an intensive care patient: therapy management using the direct thrombin inhibitor argatroban].	Heparin	1-8	coagulation factor II, thrombin	Homo sapiens	124-132
19399370-0	2009	M118, a novel low-molecular weight heparin with decreased polydispersity leads to enhanced anticoagulant activity and thrombotic occlusion in ApoE knockout mice.	Heparin	35-42	apolipoprotein E	Mus musculus	142-146
19810698-3	2009	The impact of structure and time-dependent changes in the structural elements in FGF1and FGF1-heparin in the presence of the AuNP is probed by a molecular beacon fluorescence assay, circular dichroism, and NMR spectroscopy.	Heparin	94-101	fibroblast growth factor 1	Homo sapiens	89-93
19540231-16	2009	Heparin abolished responses to Vn, IGFBP-5 and non-glycosylated IGFBP-3, but only partially inhibited the response to glycosylated IGFBP-3.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	35-42
19634127-5	2009	The heparin analog sucrose octasulfate inhibited hexafin binding to FGFR1-IIIc-Ig2-3 indicating overlapping binding sites.	Heparin	4-11	fibroblast growth factor receptor 1	Homo sapiens	68-73
19598263-0	2009	Modified heparins inhibit integrin alpha(IIb)beta(3) mediated adhesion of melanoma cells to platelets in vitro and in vivo.	Heparin	9-17	integrin alpha-IIb	Cricetulus griseus	26-44
19598263-8	2009	These data suggest that modified heparins can inhibit tumor cell-platelet interaction mediated by platelet integrin alpha(IIb)beta(3) and modified heparins may be a potential substitute for heparin in inhibiting tumor metastasis.	Heparin	33-41	integrin alpha-IIb	Cricetulus griseus	107-125
19598263-8	2009	These data suggest that modified heparins can inhibit tumor cell-platelet interaction mediated by platelet integrin alpha(IIb)beta(3) and modified heparins may be a potential substitute for heparin in inhibiting tumor metastasis.	Heparin	33-40	integrin alpha-IIb	Cricetulus griseus	107-125
20137346-0	2009	[Inhibitory effect of low molecular weight heparin on the secretion of vascular endothelial growth factor by tumor cells in vitro].	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	71-105
19923058-5	2009	RESULTS: Platinum coils were prepared by successive deposition of P(DLLA-co-TMC) copolymer and anionic heparin, and VEGF was immobilized through affinity interaction with heparin.	Heparin	171-178	vascular endothelial growth factor A	Homo sapiens	116-120
20137346-1	2009	OBJECTIVE: To investigate whether low molecular weight heparin (LMWH) may suppress the expression and secretion of vascular endothelial growth factor (VEGF) from tumor cells in vitro and inhibit the VEGF-induced proliferation of human tumor vascular endothelial cells.	Heparin	55-62	vascular endothelial growth factor A	Homo sapiens	115-149
20137346-1	2009	OBJECTIVE: To investigate whether low molecular weight heparin (LMWH) may suppress the expression and secretion of vascular endothelial growth factor (VEGF) from tumor cells in vitro and inhibit the VEGF-induced proliferation of human tumor vascular endothelial cells.	Heparin	55-62	vascular endothelial growth factor A	Homo sapiens	151-155
20137346-1	2009	OBJECTIVE: To investigate whether low molecular weight heparin (LMWH) may suppress the expression and secretion of vascular endothelial growth factor (VEGF) from tumor cells in vitro and inhibit the VEGF-induced proliferation of human tumor vascular endothelial cells.	Heparin	55-62	vascular endothelial growth factor A	Homo sapiens	199-203
20137346-4	2009	The VEGF mRNA level of HepG2 cells cultured with or without LMWH/heparin was determined by RT-PCR and real time PCR.	Heparin	65-72	vascular endothelial growth factor A	Homo sapiens	4-8
20137346-7	2009	RESULTS: The VEGF levels in the control, LMWH, and heparin groups of the pulmonary adenocarcinoma cell line A549 were (1045.89 +/- 165.30) pg/ml, (782.45 +/- 67.17) pg/ml and (916.54 +/- 71.25) pg/ml, respectively.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	13-17
20137346-8	2009	The VEGF levels in the control, LMWH, and heparin groups of the colon adenocarcinoma cell line HCT116 were (955.76 +/- 51.14) pg/ml, (822.89 +/- 142.39) pg/ml and (951.77 +/- 188.22) pg/ml, respectively.	Heparin	42-49	vascular endothelial growth factor A	Homo sapiens	4-8
20137346-9	2009	The VEGF levels in the control, LMWH, and heparin groups in the colon adenocarcinoma cell line HCT8 were (1290.62 +/- 41.23) pg/ml, (1063.34 +/- 63.82) pg/ml and (1257.14 +/- 11.40) pg/ml, respectively.	Heparin	42-49	vascular endothelial growth factor A	Homo sapiens	4-8
20137346-10	2009	The VEGF levels in the control, LMWH, and heparin groups in the liver cancer cell line HepG2 were (1083.00 +/- 134.35) pg/ml, (758.00 +/- 84.85) pg/ml and (874.00 +/- 22.62) pg/ml, respectively.	Heparin	42-49	vascular endothelial growth factor A	Homo sapiens	4-8
19809501-9	2009	CONCLUSIONS: The demonstration of an antimicrobial activity of PrP, localisation of its activity to the N-terminal and heparin-binding region, combined with results showing an increased expression of PrP during wounding, indicate that PrPs could have a previously undisclosed role in host defense.	Heparin	119-126	prion protein	Homo sapiens	63-66
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	13-20	anosmin 1	Homo sapiens	27-36
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	57-61
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	13-20	fibroblast growth factor receptor 1	Homo sapiens	62-67
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	13-20	anosmin 1	Homo sapiens	91-100
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	13-20	fibroblast growth factor receptor 1	Homo sapiens	101-106
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	107-111
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	112-119	anosmin 1	Homo sapiens	27-36
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	57-61
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	112-119	fibroblast growth factor receptor 1	Homo sapiens	62-67
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	112-119	anosmin 1	Homo sapiens	91-100
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	112-119	fibroblast growth factor receptor 1	Homo sapiens	101-106
19696444-9	2009	By contrast, heparin-bound anosmin-1 binds to pre-formed FGF2.FGFR1 complex, generating an anosmin-1.FGFR1.FGF2.heparin complex.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	107-111
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	150-157	anosmin 1	Homo sapiens	78-87
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	150-157	fibroblast growth factor receptor 1	Homo sapiens	91-96
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	150-157	fibroblast growth factor 2	Homo sapiens	225-229
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	230-237	anosmin 1	Homo sapiens	78-87
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	230-237	fibroblast growth factor receptor 1	Homo sapiens	91-96
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	230-237	anosmin 1	Homo sapiens	127-136
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	230-237	fibroblast growth factor receptor 1	Homo sapiens	140-145
19696444-11	2009	Our study provides molecular and cellular evidence for a modulatory action of anosmin-1 on FGFR1 signaling, whereby binding of anosmin-1 to FGFR1 and heparin can play a dual role in assembly and activity of the ternary FGFR1.FGF2.heparin complex.	Heparin	230-237	fibroblast growth factor receptor 1	Homo sapiens	140-145
19563767-5	2009	The method, which was applied to reveal thrombin captured on a substrate containing antithrombin and heparin, resulted in the ability to detect marker concentrations down to the picomolar (pM) level.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	40-48
19648121-8	2009	Thus, our results suggest that AMBN promotes cell binding through the heparin binding sites and plays an important role in preventing odontogenic tumor development by suppressing cell proliferation and maintaining differentiation phenotype through Msx2, p21, and p27.	Heparin	70-77	ameloblastin	Homo sapiens	31-35
19696444-8	2009	We also show that FGFR1-bound anosmin-1, although capable of binding to FGF2 alone, cannot bind to a FGF2.heparin complex, thus preventing FGFR1.FGF2.heparin complex formation.	Heparin	106-113	anosmin 1	Homo sapiens	30-39
19696444-8	2009	We also show that FGFR1-bound anosmin-1, although capable of binding to FGF2 alone, cannot bind to a FGF2.heparin complex, thus preventing FGFR1.FGF2.heparin complex formation.	Heparin	150-157	fibroblast growth factor receptor 1	Homo sapiens	18-23
19696444-8	2009	We also show that FGFR1-bound anosmin-1, although capable of binding to FGF2 alone, cannot bind to a FGF2.heparin complex, thus preventing FGFR1.FGF2.heparin complex formation.	Heparin	150-157	anosmin 1	Homo sapiens	30-39
19754153-1	2009	Extracellular superoxide dismutase (ECSOD) interacts with heparin through its C-terminal domain.	Heparin	58-65	superoxide dismutase 3	Homo sapiens	36-41
19754153-3	2009	We have shown that the interaction between ECSOD and intestinal mucosal heparin (M(w) 6000-30000 Da) is exothermic and driven by enthalpy at physiological salt concentration.	Heparin	72-79	superoxide dismutase 3	Homo sapiens	43-48
19754153-5	2009	By studying different size-defined heparin fragments, we also concluded that a hexasaccharide moiety is sufficient for strong binding to ECSOD.	Heparin	35-42	superoxide dismutase 3	Homo sapiens	137-142
19754153-6	2009	The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively.	Heparin	66-73	superoxide dismutase 3	Homo sapiens	60-65
19754153-6	2009	The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively.	Heparin	66-73	superoxide dismutase 3	Homo sapiens	159-164
19754153-6	2009	The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively.	Heparin	169-176	superoxide dismutase 3	Homo sapiens	60-65
19754153-6	2009	The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively.	Heparin	169-176	superoxide dismutase 3	Homo sapiens	159-164
19754153-6	2009	The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively.	Heparin	169-176	superoxide dismutase 3	Homo sapiens	60-65
19754153-6	2009	The binding involves proton transfer from the buffer to the ECSOD-heparin complex, and the results indicate that the number of ionic interactions made between ECSOD and heparin upon binding varies from three to five for heparin and an octasaccharide fragment, respectively.	Heparin	169-176	superoxide dismutase 3	Homo sapiens	159-164
19700767-4	2009	Two other family members, PRELP and chondroadherin, have distinctly different clusters of basic amino acids in their N and C termini, respectively, and PRELP is known to bind to heparin via this domain.	Heparin	178-185	chondroadherin	Homo sapiens	36-50
19666466-0	2009	Characterization of the human sulfatase Sulf1 and its high affinity heparin/heparan sulfate interaction domain.	Heparin	68-75	sulfatase 1	Homo sapiens	40-45
19729010-5	2009	Acrolein, even at low dose, impaired the anticoagulant function of purified antithrombin by affecting its heparin affinity.	Heparin	106-113	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	76-88
19465032-3	2009	An important single nucleotide polymorphism (SNP), nt.760 G&gt;C of the SOD3 gene (rs#1799895) leads to the amino acid substitution Arg(213)Gly (R213G) in the center of the heparin-binding domain and consequently to a lowered affinity for the endothelium.	Heparin	173-180	superoxide dismutase 3	Homo sapiens	72-76
19723805-3	2009	Indeed, heparin, heparitinase treatment and mutation of the Thy-1 heparin-binding site each inhibited Thy-1-induced RhoA activation, as well as formation of focal adhesions and stress fibers in DI TNC(1) astrocytes.	Heparin	8-15	ras homolog family member A	Homo sapiens	116-120
19690218-13	2009	DISCUSSION: Commonly administered anticoagulants, such as unfractionated heparin, low-molecular-weight heparins, and fondaparinux, exert their effect by complexing with AT and thrombin (Factor IIa), activating AT and preventing thrombin from exerting coagulation effect.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	176-184
19690218-13	2009	DISCUSSION: Commonly administered anticoagulants, such as unfractionated heparin, low-molecular-weight heparins, and fondaparinux, exert their effect by complexing with AT and thrombin (Factor IIa), activating AT and preventing thrombin from exerting coagulation effect.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	228-236
19690218-13	2009	DISCUSSION: Commonly administered anticoagulants, such as unfractionated heparin, low-molecular-weight heparins, and fondaparinux, exert their effect by complexing with AT and thrombin (Factor IIa), activating AT and preventing thrombin from exerting coagulation effect.	Heparin	103-111	coagulation factor II, thrombin	Homo sapiens	176-184
19690218-13	2009	DISCUSSION: Commonly administered anticoagulants, such as unfractionated heparin, low-molecular-weight heparins, and fondaparinux, exert their effect by complexing with AT and thrombin (Factor IIa), activating AT and preventing thrombin from exerting coagulation effect.	Heparin	103-111	coagulation factor II, thrombin	Homo sapiens	228-236
19560816-4	2009	Additionally, secondary conversion of heparin within the biohybrid gels allowed the covalent attachment of cell adhesion mediating RGD peptides and the non-covalent binding of soluble mitogens such as FGF-2.	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	201-206
19751297-10	2009	Interestingly, heparin/lipid infusion also reduced circulating adiponectin levels (P = 0.001), which was primarily the result of reduced MMW adiponectin (P = 0.004), whereas LMW and HMW were not significantly affected.	Heparin	15-22	adiponectin, C1Q and collagen domain containing	Homo sapiens	63-74
19751297-10	2009	Interestingly, heparin/lipid infusion also reduced circulating adiponectin levels (P = 0.001), which was primarily the result of reduced MMW adiponectin (P = 0.004), whereas LMW and HMW were not significantly affected.	Heparin	15-22	adiponectin, C1Q and collagen domain containing	Homo sapiens	141-152
19893601-5	2009	The heparin-dependent induction of angiogenesis by HMGB1 was accompanied by increases in the expression of tumor necrosis factor-alpha (TNF-alpha) and vascular endothelial growth factor-A120 (VEGF-A120).	Heparin	4-11	tumor necrosis factor	Mus musculus	107-134
19893601-5	2009	The heparin-dependent induction of angiogenesis by HMGB1 was accompanied by increases in the expression of tumor necrosis factor-alpha (TNF-alpha) and vascular endothelial growth factor-A120 (VEGF-A120).	Heparin	4-11	tumor necrosis factor	Mus musculus	136-145
19893601-9	2009	Taken together, these results suggested that HMGB1 in complex with heparin possesses remarkable angiogenic activity, probably through the induction of TNF-alpha and VEGF-A120.	Heparin	67-74	tumor necrosis factor	Mus musculus	151-160
19574466-9	2009	Measured FSTL1 concentrations in citrated plasma and heparin-treated plasma were 18% and 17% lower, respectively, than concentrations measured in serum.	Heparin	53-60	follistatin like 1	Homo sapiens	9-14
19723805-3	2009	Indeed, heparin, heparitinase treatment and mutation of the Thy-1 heparin-binding site each inhibited Thy-1-induced RhoA activation, as well as formation of focal adhesions and stress fibers in DI TNC(1) astrocytes.	Heparin	66-73	ras homolog family member A	Homo sapiens	116-120
19567366-7	2009	Thus, analysis of fibroblast growth factor-2 bound to heparin and incubated with N-hydroxysuccinimide acetate showed that lysines involved in the sugar binding are protected against chemical modification.	Heparin	54-61	fibroblast growth factor 2	Homo sapiens	18-44
19567366-10	2009	The analysis of labeled peptides obtained from three well characterized heparin-binding proteins with very different heparin-binding sites, fibroblast growth factor-2, platelet factor-4, and pleiotrophin demonstrates the success of this new approach, which thus provides a rapid and reliable procedure to identify heparin-binding sites.	Heparin	72-79	fibroblast growth factor 2	Homo sapiens	140-166
19567366-10	2009	The analysis of labeled peptides obtained from three well characterized heparin-binding proteins with very different heparin-binding sites, fibroblast growth factor-2, platelet factor-4, and pleiotrophin demonstrates the success of this new approach, which thus provides a rapid and reliable procedure to identify heparin-binding sites.	Heparin	72-79	pleiotrophin	Homo sapiens	191-203
19574212-0	2009	Increased protein stability of FGF1 can compensate for its reduced affinity for heparin.	Heparin	80-87	fibroblast growth factor 1	Homo sapiens	31-35
19968085-3	2009	At the background of administration of the heparin at a dose of 0.2-0.3 U x kg(-1) min(-1), urokinase was intravenously administered with a loading dose of 15-20 U x kg(-1) x min(-1) and a locked time period of 30 minutes, and then the dose was incessantly decreased to 4-10 U x kg(-1) x min(-1).	Heparin	43-50	CD59 molecule (CD59 blood group)	Homo sapiens	83-89
20092760-8	2009	Low molecular weight heparin and heparin were both available to anticoagualte;but dosage required in patients with FAP was much higher than that of SAP (P &lt; 0.05).	Heparin	21-28	SH2 domain containing 1A	Homo sapiens	148-151
19574212-2	2009	Binding to heparin increases the stability of FGF1 and is believed to be important in the formation of FGF1.fibroblast growth factor receptor (FGFR) active complex.	Heparin	11-18	fibroblast growth factor 1	Homo sapiens	46-50
19574212-2	2009	Binding to heparin increases the stability of FGF1 and is believed to be important in the formation of FGF1.fibroblast growth factor receptor (FGFR) active complex.	Heparin	11-18	fibroblast growth factor 1	Homo sapiens	103-107
19574212-3	2009	In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability.	Heparin	35-42	fibroblast growth factor 1	Homo sapiens	46-50
19574212-3	2009	In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability.	Heparin	35-42	fibroblast growth factor 1	Homo sapiens	112-116
19574212-3	2009	In order to reveal the function of heparin in FGF1.FGFR complex formation and signaling, we constructed several FGF1 variants with reduced affinity for heparin and with diverse stability.	Heparin	152-159	fibroblast growth factor 1	Homo sapiens	112-116
19574212-5	2009	Our study showed that increased thermodynamic stability of FGF1 nicely compensates for decreased binding of heparin in FGFR activation, induction of DNA synthesis, and cell proliferation.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	59-63
19574212-6	2009	By stepwise introduction of stabilizing mutations into the K118E (K132E) FGF1 variant that shows reduced affinity for heparin and is inactive in stimulation of DNA synthesis, we were able to restore the full mitogenic activity of this mutant.	Heparin	118-125	fibroblast growth factor 1	Homo sapiens	73-77
19574212-7	2009	Our results indicate that the main role of heparin in FGF-induced signaling is to protect this naturally unstable protein against heat and/or proteolytic degradation and that heparin is not essential for a direct FGF1-FGFR interaction and receptor activation.	Heparin	43-50	fibroblast growth factor 1	Homo sapiens	54-57
19520426-6	2009	The results of in vitro and in vivo studies revealed that chondrogenic differentiation of the hASCs on the complex was induced and sustained by continuous stimulation by TGF-beta1 from the heparin-functionalized nanoparticles.	Heparin	189-196	transforming growth factor beta 1	Homo sapiens	170-179
19540581-8	2009	ELISA experiments confirmed VEGF surface density and showed that electrostatically bound VEGF releases in cell medium and heparin solutions while covalently bound VEGF remains immobilized.	Heparin	122-129	vascular endothelial growth factor A	Homo sapiens	89-93
19540581-8	2009	ELISA experiments confirmed VEGF surface density and showed that electrostatically bound VEGF releases in cell medium and heparin solutions while covalently bound VEGF remains immobilized.	Heparin	122-129	vascular endothelial growth factor A	Homo sapiens	89-93
19644449-5	2009	In addition, a unique continuous electropositive surface is created when myostatin binds Fst288, which significantly increases the affinity for heparin.	Heparin	144-151	myostatin	Homo sapiens	73-82
19520426-2	2009	In this study, we induced chondrogenic differentiation of human adipose tissue-derived stem cells (hASCs) in situ by effective stimulation via the continuous controlled release of TGF-beta1 from a heparin-functionalized nanoparticle-fibrin-poly(lactide-co-caprolactone) (PLCL) complex.	Heparin	197-204	transforming growth factor beta 1	Homo sapiens	180-189
19520426-4	2009	Heparin-functionalized nanoparticles were prepared by a solvent-diffusion method, composed of poly(lactide-co-glycolide) (PLGA), Pluronic F-127, and heparin, and then TGF-beta1 was loaded to the nanoparticles.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	167-176
19520426-8	2009	Consequently, the hybridization of fibrin and PLCL scaffolds for three-dimensional spatial organization of cells and the effective delivery of TGF-beta1 using heparin-functionalized nanoparticles can induce hASCs to differentiate to a chondrogenic lineage and maintain their phenotypes.	Heparin	159-166	transforming growth factor beta 1	Homo sapiens	143-152
19539364-1	2009	In this work, a cocktail of dexamethasone (Dex) and transforming growth factor-beta3 (TGF-beta3) bound with heparin in/on PLGA microspheres was investigated by local dual delivery using rabbit mesenchymal stem cells (rMSCs) for chondrogenic differentiation in in vitro and in vivo study.	Heparin	108-115	transforming growth factor beta-3	Oryctolagus cuniculus	52-84
19539364-1	2009	In this work, a cocktail of dexamethasone (Dex) and transforming growth factor-beta3 (TGF-beta3) bound with heparin in/on PLGA microspheres was investigated by local dual delivery using rabbit mesenchymal stem cells (rMSCs) for chondrogenic differentiation in in vitro and in vivo study.	Heparin	108-115	transforming growth factor beta-3	Oryctolagus cuniculus	86-95
19524564-0	2009	Myeloperoxidase concentrations in EDTA-plasma of healthy subjects are discordant with concentrations in heparin-plasma and serum.	Heparin	104-111	myeloperoxidase	Homo sapiens	0-15
19524564-2	2009	DESIGN AND METHODS: MPO was measured in EDTA-plasma and matched heparin-plasma and serum samples collected from healthy volunteers.	Heparin	64-71	myeloperoxidase	Homo sapiens	20-23
19524564-3	2009	RESULTS: MPO concentrations in heparin-plasma and serum were higher than in EDTA-plasma (both P&lt;0.001).	Heparin	31-38	myeloperoxidase	Homo sapiens	9-12
19573895-9	2009	Hyperglycaemia in vitro induced a transition of antithrombin to a form with low heparin affinity that explained the loss of anticoagulant activity, without generation of abnormal conformers (polymers or latent antithrombin).	Heparin	80-87	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	48-60
19549276-12	2009	CONCLUSION: Our studies illustrate the central paradox of HIT, namely enhancement of thrombin generation in the presence of heparin.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	85-93
19764444-0	2009	[Anesthetic management for a patient with heparin-induced thrombocytopenia (HIT) undergoing off-pump coronary bypass surgery using argatroban, a direct thrombin inhibitor].	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	152-160
19950764-1	2009	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is an acquired, prothrombotic disorder, caused by antibodies to a complex of heparin and platelet factor 4 (PF4) that activates platelets, resulting in the release of procoagulant microparticles, thrombocytopenia occurrence, generation of thrombin, and frequent thromboses.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	292-300
19721725-2	2009	Interestingly, we were able to show that heparin binding domain (HBD), the N-terminal portion of TSP-1, was cleaved and secreted simultaneously in a caspase- and serine protease- dependent manner.	Heparin	41-48	thrombospondin 1	Homo sapiens	97-102
19721725-2	2009	Interestingly, we were able to show that heparin binding domain (HBD), the N-terminal portion of TSP-1, was cleaved and secreted simultaneously in a caspase- and serine protease- dependent manner.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	162-177
19468011-3	2009	Thrombin-inducible cleavage of PAR-1 was inhibited by heparin, but not affected by bivalirudin (P = 0.0001).	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	0-8
19727205-9	2009	These results suggested that heparin"s anti-inflammatory effects can be partly explained by its blocking of the interaction between HMGB1 or S100A12 and RAGE.	Heparin	29-36	S100 calcium binding protein A12	Homo sapiens	141-148
19602586-3	2009	In this study, we investigated the potential use of extracellular superoxide dismutase (EcSOD) to enhance the inhibitory effects of heparin/low molecular weight heparin (LMWH) in breast cancer cells.	Heparin	132-139	superoxide dismutase 3	Homo sapiens	88-93
19602586-3	2009	In this study, we investigated the potential use of extracellular superoxide dismutase (EcSOD) to enhance the inhibitory effects of heparin/low molecular weight heparin (LMWH) in breast cancer cells.	Heparin	161-168	superoxide dismutase 3	Homo sapiens	88-93
19602586-3	2009	In this study, we investigated the potential use of extracellular superoxide dismutase (EcSOD) to enhance the inhibitory effects of heparin/low molecular weight heparin (LMWH) in breast cancer cells.	Heparin	170-174	superoxide dismutase 3	Homo sapiens	88-93
19602586-11	2009	Our study implies that overexpression of EcSOD is a promising strategy to enhance the efficacy of heparin/LMWH by inhibiting heparanase as a novel treatment for breast cancer.	Heparin	98-105	superoxide dismutase 3	Homo sapiens	41-46
19602586-11	2009	Our study implies that overexpression of EcSOD is a promising strategy to enhance the efficacy of heparin/LMWH by inhibiting heparanase as a novel treatment for breast cancer.	Heparin	98-105	heparanase	Homo sapiens	125-135
19602586-11	2009	Our study implies that overexpression of EcSOD is a promising strategy to enhance the efficacy of heparin/LMWH by inhibiting heparanase as a novel treatment for breast cancer.	Heparin	106-110	superoxide dismutase 3	Homo sapiens	41-46
19602586-11	2009	Our study implies that overexpression of EcSOD is a promising strategy to enhance the efficacy of heparin/LMWH by inhibiting heparanase as a novel treatment for breast cancer.	Heparin	106-110	heparanase	Homo sapiens	125-135
19619692-5	2009	Stack-on UFH at 4, 6, or 10 hours after the last enoxaparin dose significantly increased anti-Xa and anti-IIa activities (P &lt; .0001) to well above accepted therapeutic levels and resulted in total inhibition of thrombin generation for &gt; or =2 hours; ACT levels remained within the range commonly observed in subjects receiving UFH.	Heparin	9-12	coagulation factor II, thrombin	Homo sapiens	214-222
19468011-1	2009	Aims We examined the specific effects of unfractionated heparin and bivalirudin on thrombin-inducible platelet PAR-1 in patients undergoing percutaneous coronary intervention (PCI).	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	83-91
19468011-5	2009	Conclusion Heparin has stronger inhibitory effects on thrombin-dependent PAR-1 cleavage and internalization, thus providing a biological explanation for lower clinical bleeding rates with bivalirudin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	54-62
19644604-1	2009	In contrast to heparins and oral anticoagulants, anti IIa inhibitors (thrombin inhibitors) are able to directly inhibit the protease activity of thrombin and can thereby precisely control the blood coagulation process.	Heparin	15-23	coagulation factor II, thrombin	Homo sapiens	145-153
19497853-10	2009	Computational genetic algorithm-based virtual screening study shows that only one sulfated DHP structure, out of the 11 present in a library of plausible sequences, bound in the heparin-binding site with a high calculated score supporting selectivity of recognition.	Heparin	178-185	dihydropyrimidinase	Homo sapiens	91-94
19543696-0	2009	A rationally designed heparin, M118, has anticoagulant activity similar to unfractionated heparin and different from Lovenox in a cell-based model of thrombin generation.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	150-158
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	42-50
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	24-27	coagulation factor II, thrombin	Homo sapiens	42-50
19450670-3	2009	The bFGF-binding efficiency of the chitosan-alginate PEC scaffold, after being conjugated with high concentration of heparin (83.6 microg/mg scaffold), was increased up to 15 times higher than that of original scaffold (65.6 ng bFGF/mg scaffold vs. 4.5 ng bFGF/mg scaffold).	Heparin	117-124	fibroblast growth factor 2	Homo sapiens	4-8
18827975-0	2009	A comparison of direct thrombin inhibitors in the treatment of Heparin-Induced Thrombocytopenia: a single institution experience.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	23-31
19450670-3	2009	The bFGF-binding efficiency of the chitosan-alginate PEC scaffold, after being conjugated with high concentration of heparin (83.6 microg/mg scaffold), was increased up to 15 times higher than that of original scaffold (65.6 ng bFGF/mg scaffold vs. 4.5 ng bFGF/mg scaffold).	Heparin	117-124	fibroblast growth factor 2	Homo sapiens	228-232
19450670-3	2009	The bFGF-binding efficiency of the chitosan-alginate PEC scaffold, after being conjugated with high concentration of heparin (83.6 microg/mg scaffold), was increased up to 15 times higher than that of original scaffold (65.6 ng bFGF/mg scaffold vs. 4.5 ng bFGF/mg scaffold).	Heparin	117-124	fibroblast growth factor 2	Homo sapiens	228-232
19450670-5	2009	By functionalizing the scaffold with various concentrations of heparin (17.6 microg, 50.3 microg and 83.6 microg heparin/mg scaffold), the rate of bFGF release from the scaffold decreased in a controlled manner with reduced burst effect.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	147-151
19719950-0	2009	Low molecular weight heparin suppresses lymphatic endothelial cell proliferation induced by vascular endothelial growth factor C in vitro.	Heparin	21-28	vascular endothelial growth factor C	Homo sapiens	92-128
19450670-5	2009	By functionalizing the scaffold with various concentrations of heparin (17.6 microg, 50.3 microg and 83.6 microg heparin/mg scaffold), the rate of bFGF release from the scaffold decreased in a controlled manner with reduced burst effect.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	147-151
19450670-7	2009	This study shows that a novel bFGF delivery system using the heparin-functionalized chitosan-alginate PEC scaffold exhibits controllable, long-term release of bFGF and could prevent the growth factor from inactivation.	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	30-34
19450670-7	2009	This study shows that a novel bFGF delivery system using the heparin-functionalized chitosan-alginate PEC scaffold exhibits controllable, long-term release of bFGF and could prevent the growth factor from inactivation.	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	159-163
22478907-1	2009	BACKGROUND: Argatroban is a direct thrombin inhibitor approved for the prophylaxis or treatment of thrombosis in patients with heparin-induced thrombocytopenia (HIT).	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	35-43
19543302-2	2009	METHODS: BMP6 was purified via heparin affinity and reverse phase liquid chromatography.	Heparin	31-38	bone morphogenetic protein 6	Homo sapiens	9-13
19435855-2	2009	Two experimental models used to study the mechanisms responsible for insulin resistance in patients are high-fat diet-fed rodents and administration of triglycerides and heparin to raise plasma FFA.	Heparin	170-177	insulin	Homo sapiens	69-76
19435855-6	2009	Incubation of muscles in vitro rapidly reversed insulin resistance induced by administration of triglycerides and heparin, but not by a high-fat diet.	Heparin	114-121	insulin	Homo sapiens	48-55
19449820-4	2009	All the sulfonated polymers showed the heparin-like activities to inhibit the function of thrombin for fibrin formation in the more or less extent while chitosan and PEO did not.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	90-98
19034645-4	2009	The assay is applicable to a wide variety of heparin/HS-binding proteins of diverse structure and function (e.g., FGF-1, FGF-2, VEGF, IL-8, MCP-2, ATIII, PF4) and to ligands of varying molecular weight and degree of sulfation (e.g., heparin, PI-88, sucrose octasulfate, naphthalene trisulfonate) and is thus well suited for the rapid screening of ligands in drug discovery applications.	Heparin	45-52	fibroblast growth factor 1	Homo sapiens	114-119
19398540-8	2009	RevA binding to fibronectin was not inhibited by salt or heparin, suggesting that adhesin-ligand interactions are primarily nonionic and occur through the non-heparin-binding regions of the fibronectin amino-terminal domains.	Heparin	159-166	fibronectin 1	Homo sapiens	190-201
19362143-8	2009	Heparin, which is known to increase MPO plasma levels in patients with stable CAD, had no effect on MPO plasma levels in AMI patients.	Heparin	0-7	myeloperoxidase	Homo sapiens	36-39
19572066-0	2009	Differential inhibition of thrombin generation by vitamin K antagonists alone and associated with low-molecular-weight heparin.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	27-35
19251494-10	2009	Furthermore, vascular endothelial growth factor (VEGF) could be conveniently impregnated into the fibers through specific interactions with the adsorbed heparin in the outer CG layer.	Heparin	153-160	vascular endothelial growth factor A	Homo sapiens	13-47
19400583-2	2009	The conformations of heparin derivatives, as models of HS, are altered via a change in the associated cations, and this can drastically modify their FGF signaling activities.	Heparin	21-28	fibroblast growth factor 1	Homo sapiens	149-152
19251494-10	2009	Furthermore, vascular endothelial growth factor (VEGF) could be conveniently impregnated into the fibers through specific interactions with the adsorbed heparin in the outer CG layer.	Heparin	153-160	vascular endothelial growth factor A	Homo sapiens	49-53
20408718-10	2009	Moreover, a surface with heparin-immobilized FGF2 is shown to retain its bioactivity following drying of the substrate and contact with mineral oil.	Heparin	25-32	fibroblast growth factor 2	Homo sapiens	45-49
19567201-4	2009	Moreover, specific inhibitors, such as staurosporine, H89 and heparin, inhibited internalization of CCR9, which indicated a role of protein kinase C (PKC) and G protein-coupled kinase 2 (GRK2), respectively.	Heparin	62-69	proline rich transmembrane protein 2	Homo sapiens	132-148
19567201-4	2009	Moreover, specific inhibitors, such as staurosporine, H89 and heparin, inhibited internalization of CCR9, which indicated a role of protein kinase C (PKC) and G protein-coupled kinase 2 (GRK2), respectively.	Heparin	62-69	proline rich transmembrane protein 2	Homo sapiens	150-153
19567201-4	2009	Moreover, specific inhibitors, such as staurosporine, H89 and heparin, inhibited internalization of CCR9, which indicated a role of protein kinase C (PKC) and G protein-coupled kinase 2 (GRK2), respectively.	Heparin	62-69	G protein-coupled receptor kinase 2	Homo sapiens	159-185
19567201-4	2009	Moreover, specific inhibitors, such as staurosporine, H89 and heparin, inhibited internalization of CCR9, which indicated a role of protein kinase C (PKC) and G protein-coupled kinase 2 (GRK2), respectively.	Heparin	62-69	G protein-coupled receptor kinase 2	Homo sapiens	187-191
19245419-1	2009	SUMMARY BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a life-threatening thrombotic illness caused by drug-dependent antibodies recognizing complexes of platelet factor 4 (PF4) and heparin.	Heparin	20-27	platelet factor 4	Mus musculus	180-183
19541589-2	2009	Fibroblast growth factor-2 (FGF2) belongs to the family of the heparin-binding FGF growth factors.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	0-26
19541589-2	2009	Fibroblast growth factor-2 (FGF2) belongs to the family of the heparin-binding FGF growth factors.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	28-32
19376607-2	2009	The heparin-degrading endosulfatase SULF1 functions as a liver tumor suppressor.	Heparin	4-11	sulfatase 1	Homo sapiens	36-41
19284310-7	2009	We identified two aptamers, WT-15 and SM-20, that disrupt the interactions between PAI-1 and heparin, as well as PAI-1 and vitronectin, without affecting the antiprotease activity of PAI-1.	Heparin	93-100	egl-9 family hypoxia inducible factor 1	Homo sapiens	38-43
19500510-7	2009	There are significant positive correlation between TF or PAI-1 secretion of HUVEC and corresponding serum TNFalpha level in the group without heparin, the coefficient correlation is 0.902 and 0.939(P&lt;0.05)respectively.	Heparin	142-149	tumor necrosis factor	Homo sapiens	106-114
19806892-6	2009	These results suggested that anti-complementary activity of B3-PS2 was closed to its positive control heparin.	Heparin	102-109	taste 2 receptor member 64 pseudogene	Homo sapiens	63-66
19289103-0	2009	Analysis of xylosyltransferase II binding to the anticoagulant heparin.	Heparin	63-70	xylosyltransferase 2	Homo sapiens	12-33
19289103-3	2009	The identification of unknown amino acids responsible for heparin-binding of XylT-II was addressed in this study.	Heparin	58-65	xylosyltransferase 2	Homo sapiens	77-84
19289103-6	2009	Prolonging of XylT-II fragments did not account for a cooperative effect of multiple heparin-binding motifs and in turn for a stronger heparin-binding.	Heparin	135-142	xylosyltransferase 2	Homo sapiens	14-21
19289127-1	2009	Extracellular superoxide dismutase (SOD3) is a homotetrameric copper- and zinc-containing glycoprotein with affinity for heparin.	Heparin	121-128	superoxide dismutase 3	Homo sapiens	36-40
19289127-4	2009	The common mutation R213G, which reduces the heparin affinity of SOD3, is associated with increased risk of myocardial infarctions and stroke.	Heparin	45-52	superoxide dismutase 3	Homo sapiens	65-69
19351753-8	2009	By replacing heparin, the drug can potentiate the binding of FGF2 to FGFR1 IIIc, and it protects FGF from oxidation and proteolysis.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	61-65
19195682-1	2009	Low-molecular-weight heparins (LMWH) exert their anticoagulant effect by accelerating anti-thrombin (AT) inactivation of factor Xa (fXa) and thrombin.	Heparin	21-29	coagulation factor II, thrombin	Homo sapiens	91-99
19195682-1	2009	Low-molecular-weight heparins (LMWH) exert their anticoagulant effect by accelerating anti-thrombin (AT) inactivation of factor Xa (fXa) and thrombin.	Heparin	21-29	coagulation factor II, thrombin	Homo sapiens	141-149
19195682-8	2009	Inhibition of thrombin by heparin was also neutralized by PF4, albeit to a higher extent than the fXa-AT reaction.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	14-22
19428759-11	2009	Isothermal titration calorimetry reveals the association constant of CB1a bound to low molecular weight heparin is 1.66 x 10(5)M(-1) at physiological ionic strength at 25 degrees C. Binding of CB1a to heparin produces a large conformational change toward a more structural state.	Heparin	104-111	cannabinoid receptor 1	Homo sapiens	69-73
19428759-11	2009	Isothermal titration calorimetry reveals the association constant of CB1a bound to low molecular weight heparin is 1.66 x 10(5)M(-1) at physiological ionic strength at 25 degrees C. Binding of CB1a to heparin produces a large conformational change toward a more structural state.	Heparin	104-111	cannabinoid receptor 1	Homo sapiens	193-197
19428759-11	2009	Isothermal titration calorimetry reveals the association constant of CB1a bound to low molecular weight heparin is 1.66 x 10(5)M(-1) at physiological ionic strength at 25 degrees C. Binding of CB1a to heparin produces a large conformational change toward a more structural state.	Heparin	201-208	cannabinoid receptor 1	Homo sapiens	69-73
19428759-11	2009	Isothermal titration calorimetry reveals the association constant of CB1a bound to low molecular weight heparin is 1.66 x 10(5)M(-1) at physiological ionic strength at 25 degrees C. Binding of CB1a to heparin produces a large conformational change toward a more structural state.	Heparin	201-208	cannabinoid receptor 1	Homo sapiens	193-197
19236847-3	2009	We show that this binding is inhibited by IGF-I and that, for IGFBP-5, binding occurs through the C-terminal heparin binding domain of the protein.	Heparin	109-116	insulin like growth factor 1	Homo sapiens	42-47
19236847-3	2009	We show that this binding is inhibited by IGF-I and that, for IGFBP-5, binding occurs through the C-terminal heparin binding domain of the protein.	Heparin	109-116	insulin like growth factor binding protein 5	Homo sapiens	62-69
19249255-1	2009	In this manuscript we report the binding affinity between two model proteins, human serum albumin (HSA) and ribonuclease A (RNase A), and negatively charged polyelectrolytes, two different heparin fractions and dextran sulfate, by means of partial filling and affinity capillary electrophoresis.	Heparin	189-196	albumin	Homo sapiens	84-97
19129243-1	2009	Heparin-induced thrombocytopenia with thrombosis syndrome is an antibody-mediated disorder that has a high mortality in cardiac surgical patients in spite of early diagnosis and management with direct thrombin inhibitors.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	201-209
19414349-0	2009	Heparin induces apoptosis through suppression of AKt in oral squamous cell carcinoma cells.	Heparin	0-7	AKT serine/threonine kinase 1	Homo sapiens	49-52
19414349-4	2009	Further, such treatment resulted in a significant decrease in phosphorylated AKt, and consequently led to activation of the mitochondrial pathway in heparin-sensitive cells.	Heparin	149-156	AKT serine/threonine kinase 1	Homo sapiens	77-80
19414349-6	2009	CONCLUSION: These findings indicate that heparin induces apoptosis through suppression of AKt, and suggest a potential utility of heparin for development of less toxic chemotherapy in treatment of oral SCC.	Heparin	41-48	AKT serine/threonine kinase 1	Homo sapiens	90-93
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	25-32	fibronectin 1	Homo sapiens	111-122
19015960-1	2009	PURPOSE: The heparin-paclitaxel conjugates using amino acid as linker (HD2), with low anticoagulant activity, the similar anticancer activity as paclitaxel, offer great potential for further investigation.	Heparin	13-20	histone deacetylase 2	Homo sapiens	71-74
19015960-2	2009	METHODS: Two types of heparin-paclitaxel conjugates (HD) have been developed, in which O-acetylated heparin as carrier conjugates with paclitaxel by direct ester bond (HD1) and by inserting different amino acids as spacers, including valine, leucine, and phenylalanine (HD2a, HD2b, and HD2c), respectively.	Heparin	22-29	histone deacetylase 1	Homo sapiens	168-171
19015960-2	2009	METHODS: Two types of heparin-paclitaxel conjugates (HD) have been developed, in which O-acetylated heparin as carrier conjugates with paclitaxel by direct ester bond (HD1) and by inserting different amino acids as spacers, including valine, leucine, and phenylalanine (HD2a, HD2b, and HD2c), respectively.	Heparin	100-107	histone deacetylase 1	Homo sapiens	168-171
19112103-1	2009	We have developed a potent antithrombin (AT)-heparin conjugate (ATH) that is retained in the lung to prevent pulmonary thrombosis associated with respiratory distress in premature newborns.	Heparin	45-52	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
19131102-3	2009	Sulfated polysaccharides, such as native heparin, and heparan sulfate have been found to modulate BMP-2 bioactivity and play pivotal roles in bone metabolism.	Heparin	41-48	bone morphogenetic protein 2	Mus musculus	98-103
19131102-9	2009	Dose-dependent effects on BMP-2 bioactivity were observed in both sulfated chitosan and heparin.	Heparin	88-95	bone morphogenetic protein 2	Mus musculus	26-31
19131102-10	2009	Compared with native heparin, 26SCS showed much stronger simultaneous effects on the BMP-2 bioactivity at low dose.	Heparin	21-28	bone morphogenetic protein 2	Mus musculus	85-90
19112103-0	2009	Effect of covalent antithrombin-heparin complex on developmental mechanisms in the lung.	Heparin	32-39	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	19-31
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	49-56	fibronectin 1	Homo sapiens	111-122
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	49-56	fibronectin 1	Homo sapiens	111-122
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	49-56	fibronectin 1	Homo sapiens	111-122
19499763-1	2009	Heparin is known to attenuate tumor metastasis mainly by inhibiting the interaction between L-selectin and its ligand.	Heparin	0-7	selectin, lymphocyte	Mus musculus	92-102
19309242-7	2009	In contrast, heparin-induced anaphylaxis is caused by activation of the contact system, with formation of vasoactive kinins (bradykinin, des-arg(9)-bradykinin).	Heparin	13-20	kininogen 1	Homo sapiens	125-135
19309242-7	2009	In contrast, heparin-induced anaphylaxis is caused by activation of the contact system, with formation of vasoactive kinins (bradykinin, des-arg(9)-bradykinin).	Heparin	13-20	kininogen 1	Homo sapiens	148-158
19499763-3	2009	This report demonstrates that both L-selectin/h IgG chimeric protein and heparin treatment can significantly inhibit the adhesion of P388D1 cells onto lymphatic sinusoids and marginal sinusoids in vitro, that heparin can attenuate P388D1 cell homing to lymph nodes in vivo at 12 hours, and that heparin significantly reduced P388D1 cells metastasis to lymph nodes 18 days after injection.	Heparin	209-216	selectin, lymphocyte	Mus musculus	35-45
19499763-3	2009	This report demonstrates that both L-selectin/h IgG chimeric protein and heparin treatment can significantly inhibit the adhesion of P388D1 cells onto lymphatic sinusoids and marginal sinusoids in vitro, that heparin can attenuate P388D1 cell homing to lymph nodes in vivo at 12 hours, and that heparin significantly reduced P388D1 cells metastasis to lymph nodes 18 days after injection.	Heparin	209-216	selectin, lymphocyte	Mus musculus	35-45
19499763-4	2009	These results indicate that heparin may act as a ligand for L-selectin on the P388D1 macrophage-like lymphoma cell line to attenuate tumor growth and metastasis.	Heparin	28-35	selectin, lymphocyte	Mus musculus	60-70
19219044-4	2009	We show that the Eks mutation prevents homodimerization of the FGF9 protein and that monomeric FGF9 binds to heparin with a lower affinity than dimeric FGF9.	Heparin	109-116	fibroblast growth factor 9	Mus musculus	95-99
19219044-4	2009	We show that the Eks mutation prevents homodimerization of the FGF9 protein and that monomeric FGF9 binds to heparin with a lower affinity than dimeric FGF9.	Heparin	109-116	fibroblast growth factor 9	Mus musculus	95-99
18855004-3	2009	To elucidate functional properties of myocilin, recombinant myocilin was expressed in 293 EBNA cells and purified by Ni-chelate and heparin chromatography.	Heparin	132-139	myocilin	Homo sapiens	60-68
19066306-10	2009	RESULTS: During heparin plus Intralipid infusion, total and HMW adiponectin was inversely correlated with plasma palmitate appearance rate (r = -0.65; P = 0.01), but this association was lost when expressed per nonlean weight.	Heparin	16-23	adiponectin, C1Q and collagen domain containing	Homo sapiens	64-75
19218095-0	2009	Regulation of thrombin generation by TFPI in plasma without and with heparin.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	14-22
19219378-2	2009	The fact that the N-terminal domain of TSP-1 (heparin-binding domain or HBD) is recognized by a plethora of cell receptors, all of them engaged in proangiogenic responses, strongly suggests that the proteolytic cleavage of HBD may be relevant in certain pathophysiological conditions.	Heparin	46-53	thrombospondin 1	Homo sapiens	39-44
19100717-3	2009	XylT-II was purified from Pichia pastoris by fractionated ammonium sulfate precipitation, heparin affinity and ion exchange chromatography.	Heparin	90-97	xylosyltransferase 2	Homo sapiens	0-7
19267679-5	2009	After cleavage of the thioredoxin/FGF-2 fusion with recombinant human enteropeptidase light chain, the target protein FGF-2 was purified on a heparin-Sepharose column.	Heparin	142-149	fibroblast growth factor 2	Homo sapiens	118-123
18973536-12	2009	CONCLUSION: These results indicate that heparin-binding epidermal growth factor-like growth factor may constitute a critical factor in the wound healing of human periodontal ligament cells by a mechanism that requires the activation of Erk1/2 via specific interaction with epidermal growth factor receptor 1.	Heparin	40-47	mitogen-activated protein kinase 3	Homo sapiens	236-242
19196184-0	2009	Natural cytotoxicity receptors NKp30, NKp44 and NKp46 bind to different heparan sulfate/heparin sequences.	Heparin	88-95	natural cytotoxicity triggering receptor 2	Homo sapiens	38-43
19196184-8	2009	The affinity of NKp30 and NKp44 for synthetic HS/heparin is approximately one order of magnitude higher than the affinity of NKp46.	Heparin	49-56	natural cytotoxicity triggering receptor 2	Homo sapiens	26-31
19109427-3	2009	We compared the inhibitory effects of two adhesion modulatory proteins, fibulin-1 and tenascin-C, both of which bind to the C-terminal heparin-binding (HepII) domain of fibronectin (FN) but are structurally distinct.	Heparin	135-142	fibulin 1	Homo sapiens	72-81
19109427-3	2009	We compared the inhibitory effects of two adhesion modulatory proteins, fibulin-1 and tenascin-C, both of which bind to the C-terminal heparin-binding (HepII) domain of fibronectin (FN) but are structurally distinct.	Heparin	135-142	fibronectin 1	Homo sapiens	169-180
19109427-3	2009	We compared the inhibitory effects of two adhesion modulatory proteins, fibulin-1 and tenascin-C, both of which bind to the C-terminal heparin-binding (HepII) domain of fibronectin (FN) but are structurally distinct.	Heparin	135-142	fibronectin 1	Homo sapiens	182-184
18234290-2	2009	We aimed to investigate the effect of UFH and enoxaparin on plasma levels of prothrombin fragment 1+2 (PF 1+2) and thrombin/antithrombin complex (TAT) as markers of intravascular thrombogenesis during HD.	Heparin	38-41	coagulation factor II, thrombin	Homo sapiens	80-88
20355762-7	2009	Chromogenic assays for heparin activity proved definitively that the inhibition of locally produced thrombin was contributed to the thromboresistance of the surface-bound heparin.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	100-108
19028676-7	2009	Furthermore, heparin was able to overcome the inhibitory effect of ANGPTL3 on LPL but not that of ANGPTL4.	Heparin	13-20	angiopoietin like 3	Homo sapiens	67-74
19013448-4	2009	Heparin, which is known to translocate PACE4 in the extracellular matrix into the medium, and an antibody specific for the catalytic domain of PACE4, both reduced the branching morphogenesis and AQP5 expression in the SMG.	Heparin	0-7	proprotein convertase subtilisin/kexin type 6	Rattus norvegicus	39-44
18988890-6	2009	EL-related apoAI-mediated cholesterol efflux decreased after treatment with heparin or catalytic inactivation (S149A mutation or tetrahydrolipstatin) alone, and completely inhibited in combination.	Heparin	76-83	lipase G, endothelial type	Homo sapiens	0-2
19648086-3	2009	The thrombin clotting time determined in the presence of heparin was evaluated with the use of the heparin-thrombin test.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	4-12
19657754-9	2009	Secretion of IL-8 from cultured cervical fibroblasts was significantly increased after treatment with low molecular weight heparin.	Heparin	123-130	C-X-C motif chemokine ligand 8	Homo sapiens	13-17
19657754-11	2009	CONCLUSIONS: A possible underlying mechanism for the shortened labor time after low molecular weight heparin treatment is enhanced myometrial contractility and an increased IL-8 secretion in cervical fibroblast, mimicking the final cervical ripening in vivo.	Heparin	101-108	C-X-C motif chemokine ligand 8	Homo sapiens	173-177
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	203-211
20339323-1	2009	Measurements of anti-FXa or anti-FIIa (thrombin) activities are conventional tests for biological monitoring of low molecular weight heparin (LMWH) or unfractionated heparin treatment.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	39-47
20339323-1	2009	Measurements of anti-FXa or anti-FIIa (thrombin) activities are conventional tests for biological monitoring of low molecular weight heparin (LMWH) or unfractionated heparin treatment.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	39-47
19067186-2	2009	Anticoagulants, such as Hirudin and low molecular weight heparins (LMWHs), reduce metastasis mainly by inhibition of thrombin formation and L- and P-selectin-mediated cell-cell adhesion.	Heparin	57-65	coagulation factor II	Mus musculus	117-125
19067186-2	2009	Anticoagulants, such as Hirudin and low molecular weight heparins (LMWHs), reduce metastasis mainly by inhibition of thrombin formation and L- and P-selectin-mediated cell-cell adhesion.	Heparin	57-65	selectin, platelet	Mus musculus	147-157
19004623-6	2009	On the contrary, the thick and viscous fibrin layer was altered gradually to more fibrinogen-like layer as the heparin concentration increases at low concentrations of AT, demonstrating the powerful anticoagulant effect by heparin/AT complex.	Heparin	111-118	fibrinogen beta chain	Homo sapiens	82-92
19004623-6	2009	On the contrary, the thick and viscous fibrin layer was altered gradually to more fibrinogen-like layer as the heparin concentration increases at low concentrations of AT, demonstrating the powerful anticoagulant effect by heparin/AT complex.	Heparin	223-230	fibrinogen beta chain	Homo sapiens	82-92
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	255-262	coagulation factor II, thrombin	Homo sapiens	203-211
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	274-282
19860702-2	2009	Fibroblast growth factor-2 (FGF2) is a prototypic angiogenesis inducer belonging to the family of the heparin-binding FGF growth factors.	Heparin	102-109	fibroblast growth factor 2	Homo sapiens	0-26
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	33-36	coagulation factor II, thrombin	Homo sapiens	203-211
19860702-2	2009	Fibroblast growth factor-2 (FGF2) is a prototypic angiogenesis inducer belonging to the family of the heparin-binding FGF growth factors.	Heparin	102-109	fibroblast growth factor 2	Homo sapiens	28-32
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	33-36	coagulation factor II, thrombin	Homo sapiens	274-282
19383258-4	2009	As expected, heparin promoted the expression of the "B" pattern of chlortetracycline binding, increased pHi, [cAMP]i and the phosphotyrosine content of sperm proteins.	Heparin	13-20	glucose-6-phosphate isomerase	Bos taurus	104-107
19338378-1	2009	Argatroban is a hepatically metabolized, direct thrombin inhibitor used for prophylaxis or treatment of thrombosis in heparin-induced thrombocytopenia (HIT) and for patients with or at risk of HIT undergoing percutaneous coronary intervention (PCI).	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	48-56
18983497-8	2009	When sub-active amounts of ADP or thrombin were used to prime platelets (simulating hypercoagulability in patients), Bev IC-induced dense granule release was significantly potentiated, and much lower (sub-therapeutic) heparin concentrations were sufficient for Bev IC-induced platelet aggregation.	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	34-42
19554729-5	2008	Binding of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF) to the polymer via the heparin binding domains was then confirmed by surface plasmon resonance (SPR).	Heparin	118-125	fibroblast growth factor 2	Homo sapiens	11-41
18974053-3	2008	Acceleration of thrombin and APC inhibition by PCI requires that both protease and inhibitor bind to the same heparin chain to form a bridged Michaelis complex.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	16-24
18974053-5	2008	In this study, we investigate how heparin bridges thrombin and APC to PCI by determining the effect of mutations in and around the putative heparin binding site of PCI.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	50-58
18974053-6	2008	We found that heparin binds PCI in a linear fashion along helix H to bridge thrombin, consistent with our recent crystal structure (3B9F), but that it must rotate by approximately 60 degrees to engage Arg-229 to bridge APC.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	76-84
19360949-7	2008	Mean true height values were obtained from the histograms and showed that Fn and Ab(hep) formed complexes on mica, signifying that one of the heparin binding sites on Fn was open when Fn was adsorbed to mica.	Heparin	142-149	fibronectin 1	Homo sapiens	74-76
19360949-7	2008	Mean true height values were obtained from the histograms and showed that Fn and Ab(hep) formed complexes on mica, signifying that one of the heparin binding sites on Fn was open when Fn was adsorbed to mica.	Heparin	142-149	fibronectin 1	Homo sapiens	167-169
19360949-7	2008	Mean true height values were obtained from the histograms and showed that Fn and Ab(hep) formed complexes on mica, signifying that one of the heparin binding sites on Fn was open when Fn was adsorbed to mica.	Heparin	142-149	fibronectin 1	Homo sapiens	167-169
18845535-0	2008	The structure of the glial cell line-derived neurotrophic factor-coreceptor complex: insights into RET signaling and heparin binding.	Heparin	117-124	glial cell derived neurotrophic factor	Homo sapiens	21-64
18845535-2	2008	We have solved the GDNF(2).GFR alpha 1(2) complex structure at 2.35 A resolution in the presence of a heparin mimic, sucrose octasulfate.	Heparin	102-109	glial cell derived neurotrophic factor	Homo sapiens	19-23
18845535-11	2008	This may explain how GDNF.GFR alpha 1 can mediate cell adhesion and how heparin might inhibit GDNF signaling through RET.	Heparin	72-79	glial cell derived neurotrophic factor	Homo sapiens	21-25
18845535-11	2008	This may explain how GDNF.GFR alpha 1 can mediate cell adhesion and how heparin might inhibit GDNF signaling through RET.	Heparin	72-79	glial cell derived neurotrophic factor	Homo sapiens	94-98
18845539-1	2008	We investigated the mechanism by which heparin enhances the binding of vascular endothelial growth factor (VEGF) to the extracellular matrix protein fibronectin.	Heparin	39-46	vascular endothelial growth factor A	Homo sapiens	71-105
19052118-0	2008	Prothrombin time for detection of contaminated heparins.	Heparin	47-55	coagulation factor II, thrombin	Homo sapiens	0-11
18845539-1	2008	We investigated the mechanism by which heparin enhances the binding of vascular endothelial growth factor (VEGF) to the extracellular matrix protein fibronectin.	Heparin	39-46	vascular endothelial growth factor A	Homo sapiens	107-111
18845539-1	2008	We investigated the mechanism by which heparin enhances the binding of vascular endothelial growth factor (VEGF) to the extracellular matrix protein fibronectin.	Heparin	39-46	fibronectin 1	Homo sapiens	149-160
18845539-2	2008	In contrast to other systems, where heparin acts as a protein scaffold, we found that heparin functions catalytically to modulate VEGF binding site availability on fibronectin.	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	130-134
18845539-2	2008	In contrast to other systems, where heparin acts as a protein scaffold, we found that heparin functions catalytically to modulate VEGF binding site availability on fibronectin.	Heparin	36-43	fibronectin 1	Homo sapiens	164-175
18845539-2	2008	In contrast to other systems, where heparin acts as a protein scaffold, we found that heparin functions catalytically to modulate VEGF binding site availability on fibronectin.	Heparin	86-93	vascular endothelial growth factor A	Homo sapiens	130-134
18845539-2	2008	In contrast to other systems, where heparin acts as a protein scaffold, we found that heparin functions catalytically to modulate VEGF binding site availability on fibronectin.	Heparin	86-93	fibronectin 1	Homo sapiens	164-175
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	37-44	fibronectin 1	Homo sapiens	68-79
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	37-44	vascular endothelial growth factor A	Homo sapiens	147-151
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	28-32
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	fibronectin 1	Homo sapiens	68-79
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	147-151
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	fibronectin 1	Homo sapiens	173-184
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	28-32
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	fibronectin 1	Homo sapiens	68-79
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	147-151
18845539-3	2008	By measuring the binding of VEGF and heparin to surface-immobilized fibronectin, we show that substoichiometric amounts of heparin exposed cryptic VEGF binding sites within fibronectin that remain available after heparin removal.	Heparin	123-130	fibronectin 1	Homo sapiens	173-184
18845539-4	2008	Measurement of association and dissociation kinetics for heparin binding to fibronectin indicated that the interaction is rapid and transient.	Heparin	57-64	fibronectin 1	Homo sapiens	76-87
18845539-5	2008	We localized the heparin-responsive element to the C-terminal 40-kDa Hep2 domain of fibronectin.	Heparin	17-24	fibronectin 1	Homo sapiens	84-95
18845539-6	2008	A mathematical model of this catalytic process was constructed that supports a mechanism whereby the heparin-induced conformational change in fibronectin is accompanied by release of heparin.	Heparin	101-108	fibronectin 1	Homo sapiens	142-153
18845539-6	2008	A mathematical model of this catalytic process was constructed that supports a mechanism whereby the heparin-induced conformational change in fibronectin is accompanied by release of heparin.	Heparin	183-190	fibronectin 1	Homo sapiens	142-153
18845539-8	2008	These results indicate a novel mechanism whereby heparin catalyzes the conversion of fibronectin to an open conformation by transiently interacting with fibronectin and progressively hopping from molecule to molecule.	Heparin	49-56	fibronectin 1	Homo sapiens	85-96
18845539-8	2008	These results indicate a novel mechanism whereby heparin catalyzes the conversion of fibronectin to an open conformation by transiently interacting with fibronectin and progressively hopping from molecule to molecule.	Heparin	49-56	fibronectin 1	Homo sapiens	153-164
19554729-5	2008	Binding of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF) to the polymer via the heparin binding domains was then confirmed by surface plasmon resonance (SPR).	Heparin	118-125	fibroblast growth factor 2	Homo sapiens	43-47
19554729-5	2008	Binding of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF) to the polymer via the heparin binding domains was then confirmed by surface plasmon resonance (SPR).	Heparin	118-125	vascular endothelial growth factor A	Homo sapiens	53-87
19554729-5	2008	Binding of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF) to the polymer via the heparin binding domains was then confirmed by surface plasmon resonance (SPR).	Heparin	118-125	vascular endothelial growth factor A	Homo sapiens	89-93
19064561-10	2008	Only IL4, IL6, and IL8 had statistically significant correlations (Spearman rho, 0.42-0.94) between serum and acid citrate dextrose or heparin plasma levels.	Heparin	135-142	interleukin 4	Homo sapiens	5-8
18812191-0	2008	Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines.	Heparin	0-7	signaling lymphocytic activation molecule family member 1	Homo sapiens	74-78
18812191-4	2008	Soluble heparin (HP) inhibited the rMV-EGFP infectivity in SLAM-negative cell lines in a dose-dependent manner.	Heparin	8-15	signaling lymphocytic activation molecule family member 1	Homo sapiens	59-63
18812191-4	2008	Soluble heparin (HP) inhibited the rMV-EGFP infectivity in SLAM-negative cell lines in a dose-dependent manner.	Heparin	17-19	signaling lymphocytic activation molecule family member 1	Homo sapiens	59-63
18812191-7	2008	Taken together, our results suggest that HP-like glycosaminoglycans bind to the H protein of MV and play a key role in the infection of SLAM-negative cells.	Heparin	41-43	signaling lymphocytic activation molecule family member 1	Homo sapiens	136-140
19002046-2	2008	Direct thrombin inhibitors and heparin enhance fibrinolysis by inhibition of activation of thrombin activatable fibrinolysis inhibitor (TAFI); however, the role played by other thrombin-activated proteins [e.g., factor XIII (FXIII)] in fibrinolysis remained to be elucidated.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	91-99
18760333-1	2008	Structural instability of wild-type fibroblast growth factor (FGF)-1 and its dependence on exogenous heparin for optimal activity diminishes its potential utility as a therapeutic agent.	Heparin	101-108	fibroblast growth factor 1	Mus musculus	36-68
19064561-10	2008	Only IL4, IL6, and IL8 had statistically significant correlations (Spearman rho, 0.42-0.94) between serum and acid citrate dextrose or heparin plasma levels.	Heparin	135-142	C-X-C motif chemokine ligand 8	Homo sapiens	19-22
19016244-6	2008	Analyses of associations between SOD genotypes and levels of plasma SOD activity demonstrated that SOD2 Ala16Val, a dimorphism leading to substitution in the mitochondrial targeting sequence of SOD2, significantly influences plasma SOD2 activity, and that SOD3 Arg231Gly, leading to substitution in the heparin-binding domain of SOD3, significantly influences plasma total SOD activity.	Heparin	303-310	superoxide dismutase 3	Homo sapiens	256-260
18926810-0	2008	Heparin affects matrix metalloproteinases and tissue inhibitors of metalloproteinases circulating in peripheral blood.	Heparin	0-7	TIMP metallopeptidase inhibitor 1	Homo sapiens	46-85
18926810-2	2008	The aim of this study is to evaluate the effects of high molecular weight heparin on MMP and TIMP expression in blood.	Heparin	74-81	TIMP metallopeptidase inhibitor 1	Homo sapiens	93-97
18926810-7	2008	CONCLUSIONS: Heparin has direct and indirect effects, altering MMP/TIMP complexes circulating in blood, and increasing the release of TIMP-2.	Heparin	13-20	TIMP metallopeptidase inhibitor 1	Homo sapiens	67-71
19025434-1	2008	Direct thrombin inhibitors are commonly used anticoagulants in patients with known or suspected heparin-induced thrombocytopenia (HIT).	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	7-15
19086847-2	2008	Two recently identified human heparin-degrading endosulfatases, named sulfatase 1 (SULF1) and sulfatase 2 (SULF2), have been found to be involved in liver carcinogenesis.	Heparin	30-37	sulfatase 1	Homo sapiens	70-81
19086847-2	2008	Two recently identified human heparin-degrading endosulfatases, named sulfatase 1 (SULF1) and sulfatase 2 (SULF2), have been found to be involved in liver carcinogenesis.	Heparin	30-37	sulfatase 1	Homo sapiens	83-88
18773185-7	2008	Heparin, a potent G-coupled protein kinase 2 inhibitor, was found to abolish ERM protein phosphorylation and cortical F-actin ring formation in Ang II-treated podocytes, indicating that phosphorylated ERM proteins are the cytoskeletal effector in AT1R signaling.	Heparin	0-7	angiotensinogen	Rattus norvegicus	144-150
19114189-13	2008	Patients with anti-platelet factor 4/heparin levels of 0.45 OD units or greater 14 days after the operation had significantly higher interleukin 6 levels measured 1 hour after protamine administration.	Heparin	37-44	interleukin 6	Homo sapiens	133-146
20443852-6	2008	Intra-arterial infusion of heparin nhibited lymphocyte GRK2 activity and prevented desensitization of betaAR vasodilatation in normotensives.	Heparin	27-34	G protein-coupled receptor kinase 2	Homo sapiens	55-59
18786170-0	2008	Competitive binding of heparin with hyaluronan to a specific motif in SPACR.	Heparin	23-30	interphotoreceptor matrix proteoglycan 1	Homo sapiens	70-75
18801731-3	2008	Here ADAM12, a protease that promotes tumor progression and chondrocyte proliferation in osteoarthritic cartilage, is shown to possess a prodomain/catalytic domain cationic molecular switch, regulated by exogenous heparan sulfate and heparin but also endogenous cell surface proteoglycans and the polyanion, calcium pentosan polysulfate.	Heparin	234-241	ADAM metallopeptidase domain 12	Homo sapiens	5-11
19216269-10	2008	The incorporation of (&gt; or = 3 microg/mL) heparin significantly increased alkaline phosphatase activity and osteocalcin mRNA expression in the cells on apatite-coated titanium containing rhBMP-2.	Heparin	45-52	bone gamma-carboxyglutamate protein	Homo sapiens	111-122
18971322-5	2008	The aptamer, which adheres to thrombin at the binding site for heparin, presents an extended molecular surface that is complementary to the protein.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	30-38
19055570-0	2008	In vitro heparinization of canine whole blood with low molecular weight heparin (dalteparin) significantly and dose-dependently prolongs heparinase-modified tissue factor-activated thromboelastography parameters and prothrombinase-induced clotting time.	Heparin	9-16	coagulation factor III, tissue factor	Canis lupus familiaris	157-170
18976019-8	2008	RESULTS: Tumor necrosis factor alpha level was stable in EDTA plasma for 8 hours, while slightly increasing in heparin plasma and serum.	Heparin	111-118	tumor necrosis factor	Homo sapiens	9-36
18976019-9	2008	Interleukin 6 concentrations were stable for 8 hours in all blood types, whereas interleukin 8 concentrations were stable only in EDTA plasma and were strongly increasing in heparin plasma and serum.	Heparin	174-181	C-X-C motif chemokine ligand 8	Homo sapiens	81-94
18976135-2	2008	Previously we proposed a heparin/protamine-based system for delivery of protease drugs such as tissue-specific plasminogen activator (t-PA).	Heparin	25-32	plasminogen activator, tissue type	Homo sapiens	95-132
18976135-2	2008	Previously we proposed a heparin/protamine-based system for delivery of protease drugs such as tissue-specific plasminogen activator (t-PA).	Heparin	25-32	plasminogen activator, tissue type	Homo sapiens	134-138
18786170-3	2008	A western blotting study in combination with inhibition assays showed that heparin bound specifically to SPACR.	Heparin	75-82	interphotoreceptor matrix proteoglycan 1	Homo sapiens	105-110
18786170-8	2008	The competitive binding between hyaluronan and heparin to SPACR, mediated through the identical HABM, may dominate the functions of SPACR, in turn involving physiological and pathological processes involved in retinal development, aging and other related disorders.	Heparin	47-54	interphotoreceptor matrix proteoglycan 1	Homo sapiens	58-63
18786170-8	2008	The competitive binding between hyaluronan and heparin to SPACR, mediated through the identical HABM, may dominate the functions of SPACR, in turn involving physiological and pathological processes involved in retinal development, aging and other related disorders.	Heparin	47-54	interphotoreceptor matrix proteoglycan 1	Homo sapiens	132-137
18956996-4	2008	Direct thrombin inhibitors represent a newer class of anticoagulants used primarily in the treatment of heparin-induced thrombocytopenia and percutaneous coronary interventions.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	7-15
18715646-7	2008	The DNA lies in a region previously shown to bind C4b and heparin and these molecules (but not C3b) inhibited the DNA-C4BP interaction.	Heparin	58-65	complement component 4 binding protein alpha	Homo sapiens	118-122
18794898-6	2008	Drosophila Ihog and its vertebrate homologues CDO and BOC contain multiple immunoglobulin and fibronectin type III (FNIII) repeats, and the first FNIII repeat of Ihog binds Drosophila HhN in a heparin-dependent manner.	Heparin	193-200	cell adhesion associated, oncogene regulated	Homo sapiens	46-49
18669637-3	2008	We show that the hBP3 protein is secreted from cells, binds to FGF2 in vitro and in intact cells, and inhibits FGF2 binding to heparin.	Heparin	127-134	BP3	Homo sapiens	17-21
18669637-3	2008	We show that the hBP3 protein is secreted from cells, binds to FGF2 in vitro and in intact cells, and inhibits FGF2 binding to heparin.	Heparin	127-134	fibroblast growth factor 2	Homo sapiens	111-115
18669637-8	2008	Interestingly, a C-terminal 66-amino acid fragment (C66) of hBP3, which contains the predicted FGF binding domain, still inhibited binding of FGF2 to heparin similar to full-length hBP3.	Heparin	150-157	BP3	Homo sapiens	60-64
18669637-8	2008	Interestingly, a C-terminal 66-amino acid fragment (C66) of hBP3, which contains the predicted FGF binding domain, still inhibited binding of FGF2 to heparin similar to full-length hBP3.	Heparin	150-157	fibroblast growth factor 2	Homo sapiens	142-146
19080240-9	2008	The heparin therapy group showed lower macroscopical score (2.50 +/- 0.55 vs 4.75 +/- 1.16, P &lt; 0.05), histological scores (3.83 +/- 0.41 vs 7.75 +/- 1.04, P &lt; 0.05) and the level of TNFalpha [(84.75 +/- 18.03) ng/L vs (149.93 +/- 23.52) ng/L, P &lt; 0.05] compared with the colitis group.	Heparin	4-11	tumor necrosis factor	Rattus norvegicus	189-197
18713736-8	2008	Finally, mutation of the positively charged heparin-binding domains within LPL and apolipoprotein AV abolished the ability of these proteins to bind to GPIHBP1.	Heparin	44-51	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	75-78
18713736-8	2008	Finally, mutation of the positively charged heparin-binding domains within LPL and apolipoprotein AV abolished the ability of these proteins to bind to GPIHBP1.	Heparin	44-51	apolipoprotein A-V	Cricetulus griseus	83-100
18160574-7	2008	Plasmas of patients on heparin or coumarin generate about 10-fold less thrombin activity.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	71-79
18669635-4	2008	Rodent embryonic fibroblasts adhered to PF1 and deletion fragments, and, when cells were plated on fibrillin-1 or fibronectin Arg-Gly-Asp cell-binding fragments, cells showed heparin-dependent spreading and focal contact formation in response to soluble PF1.	Heparin	175-182	fibronectin 1	Homo sapiens	114-125
18759461-4	2008	Using an aptamer for the fibrinogen-binding site of thrombin and a second aptamer for the heparin-binding site, a sandwich chromatographic assay was developed, showing improved selectivity of thrombin detection and eliminating the need for labeling thrombin in the sample.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	192-200
18759461-4	2008	Using an aptamer for the fibrinogen-binding site of thrombin and a second aptamer for the heparin-binding site, a sandwich chromatographic assay was developed, showing improved selectivity of thrombin detection and eliminating the need for labeling thrombin in the sample.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	192-200
18722549-5	2008	Cold acclimation significantly increased heparin-releasable LPL (P&lt;0.05) and tissue residual LPL (P&lt;0.01).	Heparin	41-48	lipoprotein lipase	Rattus norvegicus	60-63
18651289-5	2008	Heparin and heparin-bound bFGF uptake and release were evaluated by (123)I radio-labelling.	Heparin	12-19	fibroblast growth factor 2	Homo sapiens	26-30
18615592-4	2008	We determined that amino acids within the heparin-binding domain of vitronectin bind to a cysteine loop (C-loop) region of beta3 and that this interaction is required for the positive effects of alphaVbeta3 ligand occupancy on IGF-I signaling in smooth muscle cells.	Heparin	42-49	insulin like growth factor 1	Homo sapiens	227-232
18651289-3	2008	We investigated biological matrices preloaded with heparin as an ionically attractive template for the binding, activation and sustained release of basic fibroblast growth factor (bFGF).	Heparin	51-58	fibroblast growth factor 2	Homo sapiens	148-178
18651289-3	2008	We investigated biological matrices preloaded with heparin as an ionically attractive template for the binding, activation and sustained release of basic fibroblast growth factor (bFGF).	Heparin	51-58	fibroblast growth factor 2	Homo sapiens	180-184
19967061-0	2008	Heparin Attenuates the Expression of TNFalpha-induced Cerebral Endothelial Cell Adhesion Molecule.	Heparin	0-7	tumor necrosis factor	Homo sapiens	37-45
19967061-0	2008	Heparin Attenuates the Expression of TNFalpha-induced Cerebral Endothelial Cell Adhesion Molecule.	Heparin	0-7	endothelial cell adhesion molecule	Homo sapiens	63-97
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	69-76	tumor necrosis factor	Homo sapiens	161-188
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	69-76	tumor necrosis factor	Homo sapiens	189-197
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	tumor necrosis factor	Homo sapiens	161-188
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	tumor necrosis factor	Homo sapiens	189-197
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	nuclear factor kappa B subunit 1	Homo sapiens	211-233
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	nuclear factor kappa B subunit 1	Homo sapiens	235-244
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	vascular cell adhesion molecule 1	Homo sapiens	345-378
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	vascular cell adhesion molecule 1	Homo sapiens	380-386
19967061-5	2008	Heparin selectively interfered with NF-kappaB DNA-binding activity in the nucleus, which is stimulated by TNFalpha.	Heparin	0-7	nuclear factor kappa B subunit 1	Homo sapiens	36-45
19967061-5	2008	Heparin selectively interfered with NF-kappaB DNA-binding activity in the nucleus, which is stimulated by TNFalpha.	Heparin	0-7	tumor necrosis factor	Homo sapiens	106-114
19967061-6	2008	In addition, non-anticoagulant 2,3-O desulfated heparin (ODS) prevented NF-kappaB activation by TNFalpha, suggesting that the anti-inflammatory mechanism of heparin action in CECs lies in heparin"s ability to inhibit the expression of cell adhesion molecules, as opposed to its anticoagulant actions.	Heparin	48-55	nuclear factor kappa B subunit 1	Homo sapiens	72-81
19967061-6	2008	In addition, non-anticoagulant 2,3-O desulfated heparin (ODS) prevented NF-kappaB activation by TNFalpha, suggesting that the anti-inflammatory mechanism of heparin action in CECs lies in heparin"s ability to inhibit the expression of cell adhesion molecules, as opposed to its anticoagulant actions.	Heparin	48-55	tumor necrosis factor	Homo sapiens	96-104
18685428-0	2008	Predictors of clinical outcome in patients with heparin-induced thrombocytopenia treated with direct thrombin inhibition.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	101-109
18685430-6	2008	The results showed that S-2 interacted with both urokinase or t-PA and glutamic plasminogen favoring a template model, while N-2 or unfractionated heparin interacted only with t-PA.	Heparin	147-154	plasminogen activator, tissue type	Homo sapiens	176-180
18940719-4	2008	We demonstrate that both heparin and its low-molecular-weight derivative enoxaparin (0.5-50 u/mL) inhibited PS(+ve)-RBC adhesion to immobilized TSP in a concentration-dependent manner (21% to 77% inhibition, P &lt; 0.05).	Heparin	25-32	thrombospondin 1	Homo sapiens	144-147
18940719-10	2008	Our results demonstrate that PS-positive erythrocytes bind to both immobilized and soluble TSP via its heparin-binding domain and that both heparin and enoxaparin, at clinically relevant concentrations, block this interaction.	Heparin	103-110	thrombospondin 1	Homo sapiens	91-94
18940719-10	2008	Our results demonstrate that PS-positive erythrocytes bind to both immobilized and soluble TSP via its heparin-binding domain and that both heparin and enoxaparin, at clinically relevant concentrations, block this interaction.	Heparin	140-147	thrombospondin 1	Homo sapiens	91-94
18940719-11	2008	Other studies have shown that heparin inhibited P-selectin- and soluble-TSP-mediated sickle erythrocyte adhesion to endothelial cells.	Heparin	30-37	thrombospondin 1	Homo sapiens	72-75
18599586-8	2008	The proliferative effects of uPA were inhibited by immunoneutralization of the EGF receptor and of heparin-binding EGF (HB-EGF) by the mutant diphtheria toxin CRM197 and an EGF receptor tyrosine kinase inhibitor.	Heparin	99-106	plasminogen activator, urokinase	Homo sapiens	29-32
18698815-1	2008	The aggregation of insulin near its isoelectric point and at low ionic strength was suppressed in the presence of heparin.	Heparin	114-121	insulin	Homo sapiens	19-26
18698815-2	2008	To understand this effect, we used turbidimetry and stopped-flow to study the pH- and ionic strength ( I)-dependence of the aggregation of heparin-free insulin.	Heparin	139-146	insulin	Homo sapiens	152-159
18685444-5	2008	In contrast to the effect of protamine sulfate, heparin promotes a massive increase in the factor IXa-anti-thrombin complex appearing as a doublet.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	107-115
18511454-3	2008	In this study we demonstrated that divalent cations were not necessary for binding of ATP to FGF2, but it could be demonstrated that heparin blocked the labelling of FGF2 with ATP indicating an involvement of the heparin-binding domain (aa 128-144) in ATP-binding.	Heparin	133-140	fibroblast growth factor 2	Homo sapiens	166-170
18664968-2	2008	RECENT FINDINGS: Heparin-induced thrombocytopenia is a severe prothrombotic disease caused by immunoglobulin G antibodies, which bind to platelet factor 4 and activate platelets with subsequent increased thrombin generation.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	204-212
18041720-0	2008	Heparin modification of calcium phosphate bone cements for VEGF functionalization.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	59-63
18041720-5	2008	In the present study, VEGF release from BioD/coll composites modified with different amounts of heparin was investigated.	Heparin	96-103	vascular endothelial growth factor A	Homo sapiens	22-26
18041720-7	2008	Moreover, the heparin modification had a positive impact on the biological activity of released VEGF.	Heparin	14-21	vascular endothelial growth factor A	Homo sapiens	96-100
18041724-3	2008	The coatings containing heparin were tested for their ability to potentiate thrombin inhibition by antithrombin and its dependence on the layer arrangement.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	76-84
18511454-3	2008	In this study we demonstrated that divalent cations were not necessary for binding of ATP to FGF2, but it could be demonstrated that heparin blocked the labelling of FGF2 with ATP indicating an involvement of the heparin-binding domain (aa 128-144) in ATP-binding.	Heparin	213-220	fibroblast growth factor 2	Homo sapiens	166-170
18511454-4	2008	FGF2, bound to Heparin Sepharose, could be eluted with ATP and GTP, but not with cAMP, AMP or ADP.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	0-4
18449905-5	2008	Heparin was found to suppress the mRNA expressions of osterix, Runx2, ALP and osteocalcin, as well as phosphorylation of Smad1/5/8 and p38 MAPK.	Heparin	0-7	RUNX family transcription factor 2	Homo sapiens	63-68
18449905-5	2008	Heparin was found to suppress the mRNA expressions of osterix, Runx2, ALP and osteocalcin, as well as phosphorylation of Smad1/5/8 and p38 MAPK.	Heparin	0-7	alkaline phosphatase, placental	Homo sapiens	70-73
18449905-5	2008	Heparin was found to suppress the mRNA expressions of osterix, Runx2, ALP and osteocalcin, as well as phosphorylation of Smad1/5/8 and p38 MAPK.	Heparin	0-7	bone gamma-carboxyglutamate protein	Homo sapiens	78-89
18449905-4	2008	Our results showed that heparin inhibited alkaline phosphatase (ALP) activity and mineralization in osteoblastic cells cultured with BMP-2.	Heparin	24-31	alkaline phosphatase, placental	Homo sapiens	42-62
18449905-4	2008	Our results showed that heparin inhibited alkaline phosphatase (ALP) activity and mineralization in osteoblastic cells cultured with BMP-2.	Heparin	24-31	alkaline phosphatase, placental	Homo sapiens	64-67
18577456-6	2008	From the culture medium we purified neurotrypsin using heparin-, hydrophobic interaction- and immobilized metal affinity chromatography.	Heparin	55-62	protease, serine 12 neurotrypsin (motopsin)	Mus musculus	36-48
18565684-12	2008	In the delivery system, fibrin glue serves as a scaffold that accommodates the infiltrating tissue, fibronectin provides adhesion sites for tissue repair cells and constitutes a connector for the fibrin glue and heparin, and heparin acts as a storage depot for BMPs and enhances their bioavailability.	Heparin	212-219	fibronectin 1	Homo sapiens	100-111
18301881-6	2008	In situ topographical imaging after the electrochemical treatment suggested the heparin layer became detached to allow the adsorption of proteins, in this case fibronectin.	Heparin	80-87	fibronectin 1	Homo sapiens	160-171
18556661-4	2008	In this study, we show that Arabidopsis HFR1 can be phosphorylated by recombinant casein kinase II (CKII) and plant extract in vitro and that phosphorylation of HFR1 can be effectively reduced by treatments with two CKII-specific inhibitors, 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole (DRB) and heparin.	Heparin	302-309	basic helix-loop-helix (bHLH) DNA-binding superfamily protein	Arabidopsis thaliana	40-44
18556661-4	2008	In this study, we show that Arabidopsis HFR1 can be phosphorylated by recombinant casein kinase II (CKII) and plant extract in vitro and that phosphorylation of HFR1 can be effectively reduced by treatments with two CKII-specific inhibitors, 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole (DRB) and heparin.	Heparin	302-309	basic helix-loop-helix (bHLH) DNA-binding superfamily protein	Arabidopsis thaliana	161-165
18388327-3	2008	Recently, the chemokine variant [44AANA47]-RANTES was shown to impair inflammatory cell recruitment in vivo by interfering with heparin binding and oligomerization.	Heparin	128-135	chemokine (C-C motif) ligand 5	Mus musculus	43-49
18585707-7	2008	Interestingly, heparin was able to reduce the binding of LTBP-4 to FN.	Heparin	15-22	fibronectin 1	Homo sapiens	67-69
18602100-3	2008	The peptides of 18 amino acid residues derived from IGFBP-3 and IGFBP-5, which involve heparin-binding regions, mediated cellular delivery of an exogenous protein into NIH3T3 and HeLa cells.	Heparin	87-94	insulin-like growth factor binding protein 5	Mus musculus	64-71
18602100-5	2008	Heparin inhibited the uptake of the fusion proteins with IGFBP-3 and IGFBP-5, indicating that the delivery pathway is heparin-dependent endocytosis, similar to that of HIV-Tat.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	69-76
18632636-6	2008	Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability.	Heparin	165-172	superoxide dismutase 3	Homo sapiens	26-60
18632636-6	2008	Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability.	Heparin	165-172	superoxide dismutase 3	Homo sapiens	62-68
18632636-6	2008	Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability.	Heparin	165-172	superoxide dismutase 3	Homo sapiens	185-191
18632636-6	2008	Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability.	Heparin	165-172	superoxide dismutase 3	Homo sapiens	185-191
18710495-4	2008	We found that the tagged FGF1s had affinities for heparin that were similar to that of the native form.	Heparin	50-57	fibroblast growth factor 1	Homo sapiens	25-29
19242012-2	2008	The "direct thrombin inhibitor" bivalirudin has been associated with better efficacy and safety than heparin.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	12-20
18301879-14	2008	Pre-operative heparin also increased baseline t-PA levels (p &lt; 0.05).	Heparin	14-21	plasminogen activator, tissue type	Homo sapiens	46-50
18441324-6	2008	We found that the integrin-binding site of FGF1 overlaps with the heparin-binding site but is distinct from the FGFR-binding site using docking simulation and mutagenesis.	Heparin	66-73	fibroblast growth factor 1	Homo sapiens	43-47
18441324-7	2008	We identified an FGF1 mutant (R50E) that was defective in integrin binding but still bound to heparin and FGFR.	Heparin	94-101	fibroblast growth factor 1	Homo sapiens	17-21
18434646-5	2008	RESULTS: The OSCS found in contaminated lots of unfractionated heparin, as well as a synthetically generated OSCS reference standard, directly activated the kinin-kallikrein pathway in human plasma, which can lead to the generation of bradykinin, a potent vasoactive mediator.	Heparin	63-70	kininogen 1	Homo sapiens	235-245
18467328-0	2008	Decidual cells produce a heparin-binding prolactin family cytokine with putative intrauterine regulatory actions.	Heparin	25-32	prolactin	Rattus norvegicus	41-50
18467328-11	2008	Instead, PLP-J interacts with heparin-containing molecules, including syndecan-1, which is expressed in gestation day 8.5 pregnant uteri, as well as in uterine stromal cells and endothelial cells.	Heparin	30-37	prolactin family 3, subfamily C, member 1	Rattus norvegicus	9-14
18638092-3	2008	This study was designed to define the hematologic consequences of using tissue plasminogen activator (t-PA) as an alternative locking solution after heparin-free hemodialysis (HF-HD).	Heparin	149-156	plasminogen activator, tissue type	Homo sapiens	72-106
18413297-3	2008	Thrombin cleavage of OPN was inhibited by unsulfated hirugen (IC(50) = 1.2 +/- 0.2 microm), unfractionated heparin (IC(50) = 56.6 +/- 8.4 microg/ml) and low molecular weight (5 kDa) heparin (IC(50) = 31.0 +/- 7.9 microg/ml), indicating the involvement of both anion-binding exosite I (ABE-I) and anion-binding exosite II (ABE-II).	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	0-8
18413297-3	2008	Thrombin cleavage of OPN was inhibited by unsulfated hirugen (IC(50) = 1.2 +/- 0.2 microm), unfractionated heparin (IC(50) = 56.6 +/- 8.4 microg/ml) and low molecular weight (5 kDa) heparin (IC(50) = 31.0 +/- 7.9 microg/ml), indicating the involvement of both anion-binding exosite I (ABE-I) and anion-binding exosite II (ABE-II).	Heparin	182-189	coagulation factor II, thrombin	Homo sapiens	0-8
18560570-11	2008	In vitro experiments demonstrated a direct binding of EGF to sFRP-3 both on heparin and on the surface of CHO cells where the molecule had been membrane anchored.	Heparin	76-83	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	54-57
18469519-2	2008	We demonstrated that midkine (MK), a retinoic acid-inducible heparin-binding mitogen, promotes EMT in immortalized HaCaT keratinocytes.	Heparin	61-68	midkine	Homo sapiens	21-28
18536736-0	2008	Heparin and structurally related polymers attenuate eotaxin-1 (CCL11) release from human airway smooth muscle.	Heparin	0-7	C-C motif chemokine ligand 11	Homo sapiens	52-61
18536736-0	2008	Heparin and structurally related polymers attenuate eotaxin-1 (CCL11) release from human airway smooth muscle.	Heparin	0-7	C-C motif chemokine ligand 11	Homo sapiens	63-68
18536736-6	2008	KEY RESULTS: Unfractionated heparin attenuated IL-13-dependent eotaxin-1 production and this effect was reproduced with low molecular weight heparins (3 and 6 kDa), demonstrating a minimum activity fragment of at least 3 kDa.	Heparin	28-35	interleukin 13	Homo sapiens	47-52
18536736-6	2008	KEY RESULTS: Unfractionated heparin attenuated IL-13-dependent eotaxin-1 production and this effect was reproduced with low molecular weight heparins (3 and 6 kDa), demonstrating a minimum activity fragment of at least 3 kDa.	Heparin	28-35	C-C motif chemokine ligand 11	Homo sapiens	63-72
18536736-6	2008	KEY RESULTS: Unfractionated heparin attenuated IL-13-dependent eotaxin-1 production and this effect was reproduced with low molecular weight heparins (3 and 6 kDa), demonstrating a minimum activity fragment of at least 3 kDa.	Heparin	141-149	interleukin 13	Homo sapiens	47-52
18536736-10	2008	CONCLUSIONS: Inhibition of IL-13-dependent eotaxin-1 release by heparin involved but did not depend upon sulphation, though loss of N-sulphation reduced the attenuating activity, which could be restored by N-acetylation.	Heparin	64-71	interleukin 13	Homo sapiens	27-32
18536736-10	2008	CONCLUSIONS: Inhibition of IL-13-dependent eotaxin-1 release by heparin involved but did not depend upon sulphation, though loss of N-sulphation reduced the attenuating activity, which could be restored by N-acetylation.	Heparin	64-71	C-C motif chemokine ligand 11	Homo sapiens	43-52
18469519-2	2008	We demonstrated that midkine (MK), a retinoic acid-inducible heparin-binding mitogen, promotes EMT in immortalized HaCaT keratinocytes.	Heparin	61-68	midkine	Homo sapiens	30-32
18574264-2	2008	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	70-78
18509013-8	2008	MPO concentrations were consistently higher in samples collected in serum and heparin plasma tubes than in samples in EDTA or citrate tubes.	Heparin	78-85	myeloperoxidase	Homo sapiens	0-3
18285400-3	2008	In this study, we designed and purified a novel protein, heparin-binding IGF-1 (Xp-HB-IGF-1), which is a fusion protein of native IGF-1 with the heparin-binding domain of heparin-binding epidermal growth factor-like growth factor.	Heparin	57-64	insulin like growth factor 1	Homo sapiens	73-78
18285400-3	2008	In this study, we designed and purified a novel protein, heparin-binding IGF-1 (Xp-HB-IGF-1), which is a fusion protein of native IGF-1 with the heparin-binding domain of heparin-binding epidermal growth factor-like growth factor.	Heparin	57-64	insulin like growth factor 1	Homo sapiens	80-91
18285400-3	2008	In this study, we designed and purified a novel protein, heparin-binding IGF-1 (Xp-HB-IGF-1), which is a fusion protein of native IGF-1 with the heparin-binding domain of heparin-binding epidermal growth factor-like growth factor.	Heparin	57-64	insulin like growth factor 1	Homo sapiens	86-91
18285400-4	2008	Xp-HB-IGF-1 bound selectively to heparin as well as the cell surfaces of 3T3 fibroblasts, neonatal cardiac myocytes and differentiating ES cells.	Heparin	33-40	insulin like growth factor 1	Homo sapiens	0-11
18443237-7	2008	TRL apoB-48 production rate was 69% higher in the Intralipid/heparin study than in the saline control (5.95+/-1.13 versus 3.53+/-0.58 mg/kg per day; P=0.027), and there was no significant difference in TRL apoB-48 clearance.	Heparin	61-68	apolipoprotein B	Homo sapiens	4-11
18391007-8	2008	Both heparin and gelatin could inhibit LipL32 binding to fibronectin in a concentration-dependent manner, indicating that the 30-kDa heparin-binding and 45-kDa gelatin-binding domains of fibronectin are involved in this interaction.	Heparin	5-12	fibronectin 1	Homo sapiens	57-68
18391007-8	2008	Both heparin and gelatin could inhibit LipL32 binding to fibronectin in a concentration-dependent manner, indicating that the 30-kDa heparin-binding and 45-kDa gelatin-binding domains of fibronectin are involved in this interaction.	Heparin	5-12	fibronectin 1	Homo sapiens	187-198
18391007-8	2008	Both heparin and gelatin could inhibit LipL32 binding to fibronectin in a concentration-dependent manner, indicating that the 30-kDa heparin-binding and 45-kDa gelatin-binding domains of fibronectin are involved in this interaction.	Heparin	133-140	fibronectin 1	Homo sapiens	57-68
18200062-2	2008	To search for binding partner(s) of ECM1, we tested the in vitro binding activity of ECM1a, a major isoform of four ECM1 splice variants, to different skin extracellular matrix proteins (such as laminin 332, collagen type IV, and fibronectin) and polysaccharides (such as hyaluronan, heparin, and chondroitin sulfate A) with solid-phase binding assay.	Heparin	284-291	extracellular matrix protein 1	Homo sapiens	85-89
18378683-6	2008	Four heparin binding domains (1-4) were identified in the V2 and V3 loops, in the C-terminal domain, and within the CD4-induced bridging sheet.	Heparin	5-12	CD4 molecule	Homo sapiens	116-119
18443237-8	2008	TRL apoB-100 concentrations were also increased (P&lt;0.001) and TRL apoB-100 production rate was 35% higher in the Intralipid/heparin study compared with saline (28+/-4 versus 21+/-3 mg/kg per day; P=0.020).	Heparin	127-134	apolipoprotein B	Homo sapiens	69-77
18353383-7	2008	Urine interleukin-8 was negatively associated with urothelial heparin-binding epidermal growth factor-like growth factor staining (r = -0.34; 95% CI -0.55, -0.12; p = 0.002) and positively associated with lamina propria mast cell count (r = 0.29; 95% CI 0.06, 0.52; p = 0.01).	Heparin	62-69	C-X-C motif chemokine ligand 8	Homo sapiens	6-19
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Heparin	155-162	von Willebrand factor	Homo sapiens	58-61
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Heparin	155-162	von Willebrand factor	Homo sapiens	128-131
17977030-8	2008	Changes in prevalence of five of the tryptic fragments of VWF with ristocetin and vancomycin correlated closely with changes in VWF binding to GP Ib-IX-V. Heparin also partially inhibited the ristocetin-induced changes in tryptic digestion of VWF.	Heparin	155-162	von Willebrand factor	Homo sapiens	128-131
18424754-7	2008	C5a was optimally generated from C5 at acidic pH by beta-tryptase monomers in the presence of high molecular weight dextran sulfate and heparin polyanions, but also was produced by beta-tryptase tetramers under these conditions.	Heparin	136-143	complement C5a receptor 1	Homo sapiens	0-3
18315554-9	2008	These data are consistent with the hypothesis that rFVIIa/NN1731 are capable of generating sufficient thrombin locally on the surface of activated platelets to induce hemostasis in the presence of heparin/LMWH.	Heparin	197-204	coagulation factor II	Rattus norvegicus	102-110
18205134-0	2008	Determination of lipoprotein lipase activity in post heparin plasma of streptozotocin-induced diabetic rats by high-performance liquid chromatography with fluorescence detection.	Heparin	53-60	lipoprotein lipase	Rattus norvegicus	17-35
18205134-5	2008	The accuracy values for the determination of LPL activity in 10 microL of rat post heparin plasma were 108.73 approximately 114.36%, and the intra- and inter-day precision values were within 1.28% and 2.91%, respectively.	Heparin	83-90	lipoprotein lipase	Rattus norvegicus	45-48
18205134-7	2008	The proposed method was applied to determination of LPL activity in post heparin plasma of normal and streptozotocininduced diabetic rats associated with 52.3% reduction.	Heparin	73-80	lipoprotein lipase	Rattus norvegicus	52-55
18421780-5	2008	Treatment of the tested cell lines with the FGF-2 neutralizing antibody showed that the stimulatory effect of heparin on the cells" growth was not FGF-2-dependent.	Heparin	110-117	fibroblast growth factor 2	Homo sapiens	44-49
18424242-0	2008	Identification of the heparin-binding domain of TNF-alpha and its use for efficient TNF-alpha purification by heparin-Sepharose affinity chromatography.	Heparin	22-29	tumor necrosis factor	Homo sapiens	48-57
18424242-0	2008	Identification of the heparin-binding domain of TNF-alpha and its use for efficient TNF-alpha purification by heparin-Sepharose affinity chromatography.	Heparin	22-29	tumor necrosis factor	Homo sapiens	84-93
18424242-1	2008	The N-terminus of the trimeric TNF-alpha molecule comprises two basic arginines within the short amino-acid sequence VRSSSR, which is here shown to be essential for binding of TNF-alpha to heparin-Sepharose.	Heparin	189-196	tumor necrosis factor	Homo sapiens	31-40
18424242-1	2008	The N-terminus of the trimeric TNF-alpha molecule comprises two basic arginines within the short amino-acid sequence VRSSSR, which is here shown to be essential for binding of TNF-alpha to heparin-Sepharose.	Heparin	189-196	tumor necrosis factor	Homo sapiens	176-185
18424242-3	2008	On the basis of this newly identified heparin-binding domain, a new method for efficient purification of TNF-alpha is described.	Heparin	38-45	tumor necrosis factor	Homo sapiens	105-114
18424242-4	2008	Affinity chromatography on heparin-Sepharose was introduced as a key step for highly purified TNF-alpha at a high yield.	Heparin	27-34	tumor necrosis factor	Homo sapiens	94-103
18310767-3	2008	Low molecular weight heparin (LMWH) inhibits the activity and the generation of thrombin.	Heparin	21-28	coagulation factor II	Rattus norvegicus	80-88
18272520-11	2008	Treatment with heparin rescued a pool of apoB in cells expressing the endocytic mutant, indicating that reuptake of VLDL via apoE still occurs with this mutant.	Heparin	15-22	CD320 antigen	Mus musculus	116-120
18272520-11	2008	Treatment with heparin rescued a pool of apoB in cells expressing the endocytic mutant, indicating that reuptake of VLDL via apoE still occurs with this mutant.	Heparin	15-22	apolipoprotein E	Mus musculus	125-129
18287332-8	2008	Heparin also decreased xanthine oxidase-induced nuclear translocation of NF-kappaB as well as production of proinflammatory cytokines.	Heparin	0-7	nuclear factor kappa B subunit 1	Homo sapiens	73-82
18243143-0	2008	Uteroglobin interacts with the heparin-binding site of fibronectin and prevents fibronectin-IgA complex formation found in IgA-nephropathy.	Heparin	31-38	fibronectin 1	Homo sapiens	55-66
18266273-1	2008	C4b-binding protein (C4BP) is a protein acting as a complement inhibitor and a carrier protein for anticoagulant protein S. Previously, we reported that the in vivo clearance of C4BP involves CD91, and that a CD91-interactive site overlaps the heparin-binding site within C4BP alpha-chains 26.	Heparin	244-251	complement component 4 binding protein alpha	Homo sapiens	0-19
18266273-1	2008	C4b-binding protein (C4BP) is a protein acting as a complement inhibitor and a carrier protein for anticoagulant protein S. Previously, we reported that the in vivo clearance of C4BP involves CD91, and that a CD91-interactive site overlaps the heparin-binding site within C4BP alpha-chains 26.	Heparin	244-251	complement component 4 binding protein alpha	Homo sapiens	21-25
18266273-1	2008	C4b-binding protein (C4BP) is a protein acting as a complement inhibitor and a carrier protein for anticoagulant protein S. Previously, we reported that the in vivo clearance of C4BP involves CD91, and that a CD91-interactive site overlaps the heparin-binding site within C4BP alpha-chains 26.	Heparin	244-251	LDL receptor related protein 1	Homo sapiens	209-213
18279654-2	2008	We demonstrate that degradation due to non-specific cleavage of recombinant protein mediated by thrombin can be completely prevented by separation of thrombin from the recombinant protein on spin columns packed with heparin-sepharose.	Heparin	216-223	coagulation factor II, thrombin	Homo sapiens	96-104
18279654-2	2008	We demonstrate that degradation due to non-specific cleavage of recombinant protein mediated by thrombin can be completely prevented by separation of thrombin from the recombinant protein on spin columns packed with heparin-sepharose.	Heparin	216-223	coagulation factor II, thrombin	Homo sapiens	150-158
18318435-1	2008	UNLABELLED: It has been shown that the heparin-degrading endosulfatase, sulfatase 1 (SULF1), functions as a liver tumor suppressor, but the role of the related sulfatase, sulfatase 2 (SULF2), in liver carcinogenesis remains to be elucidated.	Heparin	39-46	sulfatase 1	Homo sapiens	72-83
18318435-1	2008	UNLABELLED: It has been shown that the heparin-degrading endosulfatase, sulfatase 1 (SULF1), functions as a liver tumor suppressor, but the role of the related sulfatase, sulfatase 2 (SULF2), in liver carcinogenesis remains to be elucidated.	Heparin	39-46	sulfatase 1	Homo sapiens	85-90
18318435-1	2008	UNLABELLED: It has been shown that the heparin-degrading endosulfatase, sulfatase 1 (SULF1), functions as a liver tumor suppressor, but the role of the related sulfatase, sulfatase 2 (SULF2), in liver carcinogenesis remains to be elucidated.	Heparin	39-46	arylsulfatase family member H	Homo sapiens	61-70
18064602-4	2008	Interestingly, FGF-21-mediated effects are heparin independent suggesting that betaKlotho plays a role in FGF-21 activity similar to the one played by heparin in the signaling of conventional FGFs.	Heparin	43-50	fibroblast growth factor 21	Homo sapiens	15-21
17910040-1	2008	Argatroban is a direct thrombin inhibitor approved for the treatment of heparin-induced thrombocytopenia (HIT) type II.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	23-31
18443513-0	2008	Effect of heparin on production of transforming growth factor (TGF)-beta1 and TGF-beta1 mRNA expression by human normal skin and hyperplastic scar fibroblasts.	Heparin	10-17	transforming growth factor beta 1	Homo sapiens	35-73
18443513-0	2008	Effect of heparin on production of transforming growth factor (TGF)-beta1 and TGF-beta1 mRNA expression by human normal skin and hyperplastic scar fibroblasts.	Heparin	10-17	transforming growth factor beta 1	Homo sapiens	78-87
18443513-1	2008	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of transforming growth factor-beta1 (TGF-beta1) production and TGF-beta1 mRNA expression as a wound healing modulator.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	122-154
18443513-1	2008	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of transforming growth factor-beta1 (TGF-beta1) production and TGF-beta1 mRNA expression as a wound healing modulator.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	156-165
18443513-1	2008	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of transforming growth factor-beta1 (TGF-beta1) production and TGF-beta1 mRNA expression as a wound healing modulator.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	182-191
18443513-2	2008	The purpose of this study is to probe the effect of heparin on TGF-beta1 and TGF-beta1 mRNA production by human normal skin and hyperplastic scar fibroblasts.	Heparin	52-59	transforming growth factor beta 1	Homo sapiens	63-72
18443513-2	2008	The purpose of this study is to probe the effect of heparin on TGF-beta1 and TGF-beta1 mRNA production by human normal skin and hyperplastic scar fibroblasts.	Heparin	52-59	transforming growth factor beta 1	Homo sapiens	77-86
18443513-3	2008	This research investigates the effect of heparin on TGF-beta1 and TGF-beta1 mRNA production by human normal skin and hyperplastic scar fibroblasts with exposure to 0 microg/mL, 100 microg/mL, 300 microg/mL, or 600 microg/mL heparin for 24, 48, 72, or 96 hours in a serum-free in vitro model.	Heparin	41-48	transforming growth factor beta 1	Homo sapiens	52-61
18443513-3	2008	This research investigates the effect of heparin on TGF-beta1 and TGF-beta1 mRNA production by human normal skin and hyperplastic scar fibroblasts with exposure to 0 microg/mL, 100 microg/mL, 300 microg/mL, or 600 microg/mL heparin for 24, 48, 72, or 96 hours in a serum-free in vitro model.	Heparin	41-48	transforming growth factor beta 1	Homo sapiens	66-75
18443513-5	2008	Heparin (300 microg/mL and 600 microg/mL) stimulated TGF-beta1 production by normal skin (26% to 83%) and hyperplastic scar fibroblasts (63% to 85%), with statistical significance (P &lt; 0.05) at various time points.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	53-62
18443513-6	2008	Heparin (300 microg/mL and 600 microg/mL) also stimulated TGF-beta1 mRNA expression by normal skin (12% to 53%) and hyperplastic scar fibroblasts (33% to 52%), with statistical significance (P &lt; 0.05) at various time points.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	58-67
18292505-0	2008	Heparan sulfate and heparin enhance ERK phosphorylation and mediate preBCR-dependent events during B lymphopoiesis.	Heparin	20-27	mitogen-activated protein kinase 1	Homo sapiens	36-39
18310767-13	2008	Low molecular weight heparin delays tendon repair if given continuously, but not if injected intermittently, probably because the anti-factor Xa activity between injections returns to normal, allowing sufficient thrombin stimulation for repair.	Heparin	21-28	coagulation factor II	Rattus norvegicus	212-220
18645924-10	2008	As heparins are strong inhibitors of heparanase, in view of the effect of heparanase on TF/TFPI pathway, the role of heparins" anticoagulant activity may potentially be expanded.	Heparin	3-11	heparanase	Homo sapiens	37-47
18088351-13	2008	CONCLUSIONS: These observations suggest that AT might inhibit LPS-induced production of TNF-alpha by inhibiting the increase in Egr-1 expression in monocytes via interaction with heparin-like substances expressed on the cell surface.	Heparin	179-186	tumor necrosis factor	Homo sapiens	88-97
18645924-10	2008	As heparins are strong inhibitors of heparanase, in view of the effect of heparanase on TF/TFPI pathway, the role of heparins" anticoagulant activity may potentially be expanded.	Heparin	3-11	heparanase	Homo sapiens	74-84
18032733-5	2008	In the absence of skeletal muscle contraction, direct application of FNIII-1-containing fibronectin fragments to cremaster muscle arterioles in situ, triggered a rapid, specific, and reversible local dilation that was mediated by nitric oxide and required the cryptic, heparin-binding sequence of FNIII-1.	Heparin	269-276	fibronectin 1	Homo sapiens	88-99
18036696-2	2008	In this work we evaluate the hypothesis that HIV-1 p17 may be a heparin/heparan sulfate-binding protein.	Heparin	64-71	family with sequence similarity 72 member B	Homo sapiens	51-54
18036696-3	2008	HIV-1 p17 contains C- and N-terminal sequences with positively charged residues and a consensus cluster for heparin binding.	Heparin	108-115	family with sequence similarity 72 member B	Homo sapiens	6-9
18036696-4	2008	We demonstrated by affinity chromatography that HIV-1 p17 binds strongly to heparin-agarose at physiological pH.	Heparin	76-83	family with sequence similarity 72 member B	Homo sapiens	54-57
18036696-5	2008	Soluble heparins and heparan sulfate but not chondroitin 4-sulfate and dextran sulfate inhibit binding of HIV-1 p17 to heparin solid phase and to activated CD4(+) T cells.	Heparin	8-16	family with sequence similarity 72 member B	Homo sapiens	112-115
18036696-5	2008	Soluble heparins and heparan sulfate but not chondroitin 4-sulfate and dextran sulfate inhibit binding of HIV-1 p17 to heparin solid phase and to activated CD4(+) T cells.	Heparin	8-16	CD4 molecule	Homo sapiens	156-159
18036696-5	2008	Soluble heparins and heparan sulfate but not chondroitin 4-sulfate and dextran sulfate inhibit binding of HIV-1 p17 to heparin solid phase and to activated CD4(+) T cells.	Heparin	8-15	family with sequence similarity 72 member B	Homo sapiens	112-115
18036696-5	2008	Soluble heparins and heparan sulfate but not chondroitin 4-sulfate and dextran sulfate inhibit binding of HIV-1 p17 to heparin solid phase and to activated CD4(+) T cells.	Heparin	8-15	CD4 molecule	Homo sapiens	156-159
18086562-2	2008	We show that heparin reduces the stability of the pro form of cathepsin L at pH 5 by binding to a putative heparin binding motif (BBXB) in the pro-domain.	Heparin	13-20	cathepsin L	Homo sapiens	62-73
18086562-2	2008	We show that heparin reduces the stability of the pro form of cathepsin L at pH 5 by binding to a putative heparin binding motif (BBXB) in the pro-domain.	Heparin	107-114	cathepsin L	Homo sapiens	62-73
18086562-3	2008	Mutations to this motif on procathepsin L reduce heparin binding affinity and heparin-induced destabilization; in contrast, heparin only slightly destabilizes the mature cathepsin L domain.	Heparin	49-56	cathepsin L	Homo sapiens	30-41
18086562-3	2008	Mutations to this motif on procathepsin L reduce heparin binding affinity and heparin-induced destabilization; in contrast, heparin only slightly destabilizes the mature cathepsin L domain.	Heparin	78-85	cathepsin L	Homo sapiens	30-41
18086562-3	2008	Mutations to this motif on procathepsin L reduce heparin binding affinity and heparin-induced destabilization; in contrast, heparin only slightly destabilizes the mature cathepsin L domain.	Heparin	78-85	cathepsin L	Homo sapiens	30-41
18086562-4	2008	Gel analysis further shows that heparin makes procathepsin L a much better substrate for cathepsin L.	Heparin	32-39	cathepsin L	Homo sapiens	49-60
18327406-8	2008	Under serum-free conditions, heparin demonstrated dose-dependent anti-inflammatory effects, significantly reducing secretion of pro-inflammatory cytokines (IL-1beta, IL-6, IL-8, and TNF-alpha) in response to LPS-stimulation of THP-1 cells and primary monocytes.	Heparin	29-36	interleukin 1 beta	Homo sapiens	156-164
18327406-8	2008	Under serum-free conditions, heparin demonstrated dose-dependent anti-inflammatory effects, significantly reducing secretion of pro-inflammatory cytokines (IL-1beta, IL-6, IL-8, and TNF-alpha) in response to LPS-stimulation of THP-1 cells and primary monocytes.	Heparin	29-36	interleukin 6	Homo sapiens	166-170
18327406-8	2008	Under serum-free conditions, heparin demonstrated dose-dependent anti-inflammatory effects, significantly reducing secretion of pro-inflammatory cytokines (IL-1beta, IL-6, IL-8, and TNF-alpha) in response to LPS-stimulation of THP-1 cells and primary monocytes.	Heparin	29-36	C-X-C motif chemokine ligand 8	Homo sapiens	172-176
18327406-8	2008	Under serum-free conditions, heparin demonstrated dose-dependent anti-inflammatory effects, significantly reducing secretion of pro-inflammatory cytokines (IL-1beta, IL-6, IL-8, and TNF-alpha) in response to LPS-stimulation of THP-1 cells and primary monocytes.	Heparin	29-36	tumor necrosis factor	Homo sapiens	182-191
18065761-7	2008	The formation of cis and trans dimers of the TSPN-1 domain with relatively short segments of heparin further enhances the ability of TSP-1 to participate in high affinity binding to glycosaminoglycans.	Heparin	93-100	thrombospondin 1	Homo sapiens	133-138
18065761-0	2008	Heparin-induced cis- and trans-dimerization modes of the thrombospondin-1 N-terminal domain.	Heparin	0-7	thrombospondin 1	Homo sapiens	57-73
18065761-2	2008	We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra.	Heparin	65-72	thrombospondin 1	Homo sapiens	91-96
18065761-2	2008	We have previously determined the structure of the high affinity heparin-binding domain of TSP-1, designated TSPN-1, in association with the synthetic heparin, Arixtra.	Heparin	151-158	thrombospondin 1	Homo sapiens	91-96
18032733-8	2008	Together, these data provide the first evidence that a matricryptic, heparin-binding site within fibronectin fibrils of adult connective tissue plays a dynamic role in regulating both vascular responses and vascular tone.	Heparin	69-76	fibronectin 1	Homo sapiens	97-108
17961072-8	2008	Chemotaxis in response to oxidatively fragmented heparin was mediated by Toll-like receptor-4.	Heparin	49-56	toll-like receptor 4	Mus musculus	73-93
18252001-5	2008	CASE PRESENTATION: We describe the case of a child who was undergoing surgery for ventricular septal defect, with an anaphylactic reaction to heparin that was refractory to epinephrine infusion and was effectively treated by low dose vasopressin infusion.	Heparin	142-149	arginine vasopressin	Homo sapiens	234-245
18227295-15	2008	Furthermore, higher heparin concentrations were associated with greater suppression of hemostatic activation, as measured by less generation of thrombin and less consumption of factor VIII.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	144-152
18208809-0	2008	Platelet PlA2 Polymorphism and the risk for thrombosis in heparin-induced thrombocytopenia.	Heparin	58-65	phospholipase A2 group IB	Homo sapiens	9-13
18208809-2	2008	A polymorphism of platelet GPIIIa (PlA2, also called HPA1b) has been associated with a higher risk of thrombosis, but its implication in heparin-induced thrombocytopenia (HIT) is unclear.	Heparin	137-144	integrin subunit beta 3	Homo sapiens	27-33
18208809-2	2008	A polymorphism of platelet GPIIIa (PlA2, also called HPA1b) has been associated with a higher risk of thrombosis, but its implication in heparin-induced thrombocytopenia (HIT) is unclear.	Heparin	137-144	phospholipase A2 group IB	Homo sapiens	35-39
18240216-6	2008	Antagonizing heparan sulfate side chain formation with beta-xyloside or the addition of soluble heparin prevented ERK activation, in addition to reducing the expression of these proadhesive/contractile proteins.	Heparin	96-103	mitogen-activated protein kinase 1	Homo sapiens	114-117
18055456-6	2008	Previous studies demonstrated that heparin heightens the affinity of thrombin for fibrin by simultaneously binding to fibrin and exosite 2 on thrombin to generate a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin and heparin cofactor II.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	69-77
18055456-6	2008	Previous studies demonstrated that heparin heightens the affinity of thrombin for fibrin by simultaneously binding to fibrin and exosite 2 on thrombin to generate a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin and heparin cofactor II.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	142-150
18055456-6	2008	Previous studies demonstrated that heparin heightens the affinity of thrombin for fibrin by simultaneously binding to fibrin and exosite 2 on thrombin to generate a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin and heparin cofactor II.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	142-150
18055456-6	2008	Previous studies demonstrated that heparin heightens the affinity of thrombin for fibrin by simultaneously binding to fibrin and exosite 2 on thrombin to generate a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin and heparin cofactor II.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	142-150
18247311-9	2008	bFGF mRNA expression was lower in N-desulfated heparin group(2.60+/-0.56%)than that in 0.9% NaCl solution group(30.65+/-6.84%).	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	0-4
17607752-4	2008	The goal of this research was to determine whether peptide affinity for heparin and the molar ratio of peptide to heparin affected the release rate of NGF from the delivery system and the biological activity of NGF released.	Heparin	72-79	nerve growth factor	Gallus gallus	151-154
17607752-4	2008	The goal of this research was to determine whether peptide affinity for heparin and the molar ratio of peptide to heparin affected the release rate of NGF from the delivery system and the biological activity of NGF released.	Heparin	114-121	nerve growth factor	Gallus gallus	151-154
17607752-9	2008	Furthermore, by modulating the molar ratio of peptide to heparin in the delivery system, similar release rates of NGF were obtained for different affinity peptides and these conditions promoted similar levels of neurite extension, demonstrating that release rate appears to be the main mechanism controlling the biological activity of released NGF.	Heparin	57-64	nerve growth factor	Gallus gallus	114-117
18247311-10	2008	CONCLUSION: N-desulfated heparin can inhibit the metastasis of gastric cancer through inhibiting tumor bFGF gene expression and tumor angiogenesis with no obvious anticoagulant activity.	Heparin	25-32	fibroblast growth factor 2	Homo sapiens	103-107
17689210-0	2008	Controlled dual release of basic fibroblast growth factor and indomethacin from heparin-conjugated polymeric micelle.	Heparin	80-87	fibroblast growth factor 2	Homo sapiens	27-57
17981035-0	2008	Design, synthesis, FGF-1 binding, and molecular modeling studies of conformationally flexible heparin mimetic disaccharides.	Heparin	94-101	fibroblast growth factor 1	Homo sapiens	19-24
17689210-8	2008	Therefore, the release profile results support that TCH micelle could not only incorporate a hydrophobic drug into the core but also bind with bFGF to heparin that exists on its outer shell.	Heparin	151-158	fibroblast growth factor 2	Homo sapiens	143-147
17531997-5	2008	Alterations in the stability of the helix bundle N-terminal domain of apoE that contains the binding site for the low density lipoprotein (LDL) receptor and heparin do not affect the up-regulation of the COX-2 pathway.	Heparin	157-164	apolipoprotein E	Homo sapiens	70-74
18303934-4	2008	Although unfractionated heparin (UFH) has been the mainstay of antithrombin therapy in the past, it has numerous clinical and biochemical limitations, including substantial protein binding (leading to inconsistent bioavailability), a need for frequent monitoring and adjustment, unreliable and variable degrees of anticoagulation, significant platelet activation, risk of heparin-induced thrombocytopenia, and the inability to block clot bound thrombin.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	67-75
18303934-4	2008	Although unfractionated heparin (UFH) has been the mainstay of antithrombin therapy in the past, it has numerous clinical and biochemical limitations, including substantial protein binding (leading to inconsistent bioavailability), a need for frequent monitoring and adjustment, unreliable and variable degrees of anticoagulation, significant platelet activation, risk of heparin-induced thrombocytopenia, and the inability to block clot bound thrombin.	Heparin	33-36	coagulation factor II, thrombin	Homo sapiens	67-75
17846706-0	2008	Kinetic and functional analysis of the heparin-binding domain of fibronectin.	Heparin	39-46	fibronectin 1	Homo sapiens	65-76
18180618-4	2008	The inhibition percentage of aThr to thrombin was prominently increased to 11 of 30 (37%) along with its inhibition rate (100% at the highest) by the co-existence of heparin.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	37-45
18503133-7	2008	Adsorption of fibronectin to the terminal heparin layer could be used to increase cell adhesion in a concentration-dependent manner.	Heparin	42-49	fibronectin 1	Homo sapiens	14-25
18724811-10	2008	CONCLUSIONS: The results of our investigation show that plasma layer stratification might occur in primary lithium-heparin tubes for a limited number of routine clinical chemistry tests, introducing a statistically significant bias in the measurement of GGT, LDH, triglycerides and CRP in the upper vs. the bottom section.	Heparin	115-122	C-reactive protein	Homo sapiens	282-285
18590050-9	2008	For example, the functional complex is fivefold more resistant to heparin than that which forms in the absence of Rrn3.	Heparin	66-73	RRN3 homolog, RNA polymerase I transcription factor	Homo sapiens	114-118
17706452-2	2008	The aim of the present study was to examine the possible participation of various glycosaminoglycans, i.e. chondroitin sulfate, dermatan sulfate and heparin on basal and FGF-2-induced growth of WM9 and M5 human metastatic melanoma cells.	Heparin	149-156	fibroblast growth factor 2	Homo sapiens	170-175
17607711-2	2008	PTN contains a thrombospondin repeat-I (TSR-I) motif in its two beta-sheet domains that are involved in its binding to heparin and its neurite outgrowth activity.	Heparin	119-126	pleiotrophin	Homo sapiens	0-3
18727861-0	2008	Heparin-modified dendrimer cross-linked collagen matrices for the delivery of basic fibroblast growth factor (FGF-2).	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	110-115
18971611-9	2008	In this review article, there are discussed about pathogenesis of heparin-induced thrombocytopenia, other causes of thrombocytopenia, clinical features, laboratory confirmation of diagnosis, and management of patients (direct thrombin inhibitors, other therapies, duration of therapy, and use of oral anticoagulants).	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	226-234
18068655-6	2008	CASE PRESENTATION: We present two cases, one pedicled and one free flap, with venous congestion concomitant to heparin-induced thrombocytopenia syndrome, in conjunction with severe life-threatening sequelae.	Heparin	111-118	arachidonate 5-lipoxygenase activating protein	Homo sapiens	67-71
17899320-5	2008	We analyse the interaction of IGFBP-5 (and IGFBP-3) with heparin and other biomolecules and describe experiments, which were designed to monitor multi-protein complex formation in this molecular axis.	Heparin	57-64	insulin like growth factor binding protein 5	Homo sapiens	30-37
19099244-3	2008	Heparin affinity chromatography is an easy step that provides a major enrichment, particularly for sFRP-1 and sFRP-2.	Heparin	0-7	secreted frizzled related protein 2	Homo sapiens	110-116
18322389-4	2008	METHODS: We tested a number of selectively desulphated and chemically modified heparins for their ability to inhibit BACE1 and other proteases in vitro using APP fluorescent resonance energy transfer peptide substrates RESULTS: Several lead compounds have been identified that are effective beta-secretase inhibitors, but have negligible activity as anticoagulants or as inhibitors of other aspartyl proteases structurally related to beta-secretase.	Heparin	79-87	beta-secretase 1	Homo sapiens	117-122
18949070-0	2008	Heparin alters viral serpin, serp-1, anti-thrombolytic activity to anti-thrombotic activity.	Heparin	0-7	stress associated endoplasmic reticulum protein 1	Homo sapiens	29-35
18949070-5	2008	We demonstrate here that heparin binds to Serp-1 and enhances Serp-1 inhibition of thrombin, a human pro-thrombotic serine protease, in vitro, altering inhibitory activity to a more predominant anti-thrombotic activity.	Heparin	25-32	stress associated endoplasmic reticulum protein 1	Homo sapiens	42-48
18949070-5	2008	We demonstrate here that heparin binds to Serp-1 and enhances Serp-1 inhibition of thrombin, a human pro-thrombotic serine protease, in vitro, altering inhibitory activity to a more predominant anti-thrombotic activity.	Heparin	25-32	stress associated endoplasmic reticulum protein 1	Homo sapiens	62-68
18949070-5	2008	We demonstrate here that heparin binds to Serp-1 and enhances Serp-1 inhibition of thrombin, a human pro-thrombotic serine protease, in vitro, altering inhibitory activity to a more predominant anti-thrombotic activity.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	83-91
18949070-6	2008	Heparin also facilitates the simultaneous thrombin-mediated cleavage of Serp-1 and prevents formation of a serpin-typical SDS-resistant complex, implying mutual neutralization of Serp-1 and thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	42-50
18949070-6	2008	Heparin also facilitates the simultaneous thrombin-mediated cleavage of Serp-1 and prevents formation of a serpin-typical SDS-resistant complex, implying mutual neutralization of Serp-1 and thrombin.	Heparin	0-7	stress associated endoplasmic reticulum protein 1	Homo sapiens	72-78
18949070-6	2008	Heparin also facilitates the simultaneous thrombin-mediated cleavage of Serp-1 and prevents formation of a serpin-typical SDS-resistant complex, implying mutual neutralization of Serp-1 and thrombin.	Heparin	0-7	stress associated endoplasmic reticulum protein 1	Homo sapiens	179-185
18949070-6	2008	Heparin also facilitates the simultaneous thrombin-mediated cleavage of Serp-1 and prevents formation of a serpin-typical SDS-resistant complex, implying mutual neutralization of Serp-1 and thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	190-198
18949070-7	2008	In a cell-based assay, heparin facilitates Serp-1 reversal of cellular activation by stabilizing cellular membrane fluidity in thrombin-activated monocytes.	Heparin	23-30	stress associated endoplasmic reticulum protein 1	Homo sapiens	43-49
18949070-7	2008	In a cell-based assay, heparin facilitates Serp-1 reversal of cellular activation by stabilizing cellular membrane fluidity in thrombin-activated monocytes.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	127-135
18949070-8	2008	In conclusion, heparin and other GAGs serve as cofactors enhancing Serp-1 regulation of local thrombotic and inflammatory pathways.	Heparin	15-22	stress associated endoplasmic reticulum protein 1	Homo sapiens	67-73
17996279-4	2008	Low-molecular-weight heparins are fragments of unfractionated heparin produced by controlled enzymatic or chemical depolymerization processes with the main difference being in their relative inhibitory activity against factor Xa and thrombin.	Heparin	21-29	coagulation factor II, thrombin	Homo sapiens	233-241
22820671-2	2008	When bound to fibrin, thrombin is protected from inhibition by antithrombin (AT) + heparin but is neutralized when AT and heparin are covalently linked (ATH).	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	22-30
22820671-2	2008	When bound to fibrin, thrombin is protected from inhibition by antithrombin (AT) + heparin but is neutralized when AT and heparin are covalently linked (ATH).	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	22-30
18045667-0	2008	Linear diffusion of thrombin and factor Xa along the heparin molecule explains the effects of extended heparin chain lengths.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	20-28
18045667-0	2008	Linear diffusion of thrombin and factor Xa along the heparin molecule explains the effects of extended heparin chain lengths.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	20-28
18045667-1	2008	QUESTION: How does the size of the heparin moiety in the anti-thrombin (AT)-heparin complex influence its anticoagulant properties?	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	62-70
18045667-1	2008	QUESTION: How does the size of the heparin moiety in the anti-thrombin (AT)-heparin complex influence its anticoagulant properties?	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	62-70
18045667-3	2008	RESULTS: The Kd of thrombin or factor Xa is constant when expressed in terms of the concentration of sugar units, i.e. the enzymes bind the better the longer the heparin.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	19-27
18329699-2	2008	First, prothrombin was isolated by the following separation techniques: cryoprecipitation, ion-exchange chromatography (diethyl aminoethyl, DEAE-IEX), heparin affinity chromatography, a second DEAE-IEX step, and immobilized metal-affinity chromatography (IMAC).	Heparin	151-158	coagulation factor II, thrombin	Homo sapiens	7-18
18329699-4	2008	This process is cost-effective because a waste fraction can be used from one of the steps (heparin affinity chromatography) in the commercial production of plasma-derived Factor IX (FIX).	Heparin	91-98	coagulation factor IX	Homo sapiens	171-180
18045667-6	2008	CONCLUSION: The data fit a model in which thrombin and factor Xa bind at a random site on the heparin chain and, via one-dimensional diffusion, reach the AT that is bound to its specific binding site on the heparin.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	42-50
18045667-6	2008	CONCLUSION: The data fit a model in which thrombin and factor Xa bind at a random site on the heparin chain and, via one-dimensional diffusion, reach the AT that is bound to its specific binding site on the heparin.	Heparin	207-214	coagulation factor II, thrombin	Homo sapiens	42-50
17996279-4	2008	Low-molecular-weight heparins are fragments of unfractionated heparin produced by controlled enzymatic or chemical depolymerization processes with the main difference being in their relative inhibitory activity against factor Xa and thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	233-241
17878401-1	2007	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin.	Heparin	104-111	coagulation factor II	Mus musculus	61-69
17959151-0	2007	Single-molecule dynamic force spectroscopy of the fibronectin-heparin interaction.	Heparin	62-69	fibronectin 1	Homo sapiens	50-61
17959151-3	2007	In this report, atomic force spectroscopy was used to gain insight into the compliance and the resistance of the fibronectin-heparin interaction.	Heparin	125-132	fibronectin 1	Homo sapiens	113-124
18827868-1	2008	Previously, indirect thrombin inhibitors such as unfractionated heparin or low-molecular-weight heparin were used as a standard anticoagulation during percutaneous coronary intervention to prevent procedural thrombotic complications but at a risk of hemorrhagic complications.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	21-29
18827868-1	2008	Previously, indirect thrombin inhibitors such as unfractionated heparin or low-molecular-weight heparin were used as a standard anticoagulation during percutaneous coronary intervention to prevent procedural thrombotic complications but at a risk of hemorrhagic complications.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	21-29
17959151-6	2007	Our results indicate that the function of the fibronectin-heparin interaction is supported by its capacity to sustain significant deformations and considerable external mechanical forces.	Heparin	58-65	fibronectin 1	Homo sapiens	46-57
17848616-4	2007	We show that PF4/heparin macromolecular assembly occurs through colloidal interactions, wherein heparin facilitates the growth of complexes through charge neutralization.	Heparin	17-24	platelet factor 4	Mus musculus	13-16
17848616-4	2007	We show that PF4/heparin macromolecular assembly occurs through colloidal interactions, wherein heparin facilitates the growth of complexes through charge neutralization.	Heparin	96-103	platelet factor 4	Mus musculus	13-16
17979153-1	2007	Vascular endothelial growth factor A (VEGF-A) belongs to a family of heparin binding growth factors that include VEGF-B, VEGF-C, VEGF-D, and placental-like growth factor (PLGF).	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	0-36
17848616-5	2007	The size of PF4/heparin macromolecules is governed by the molar ratios of the reactants.	Heparin	16-23	platelet factor 4	Mus musculus	12-15
17848616-6	2007	Maximal complex size occurs at molar ratios of PF4/heparin at which surface charge is neutral.	Heparin	51-58	platelet factor 4	Mus musculus	47-50
17848616-8	2007	These studies suggest that the clinical heterogeneity in the HIT immune response may be due in part to requirements for specific biophysical parameters of the PF4/heparin complexes that occur in settings of intense platelet activation and PF4 release.	Heparin	163-170	platelet factor 4	Mus musculus	159-162
17848616-8	2007	These studies suggest that the clinical heterogeneity in the HIT immune response may be due in part to requirements for specific biophysical parameters of the PF4/heparin complexes that occur in settings of intense platelet activation and PF4 release.	Heparin	163-170	platelet factor 4	Mus musculus	239-242
17580326-0	2007	Characterization of the surface immobilized synthetic heparin binding domain derived from human fibroblast growth factor-2 and its effect on osteoblast differentiation.	Heparin	54-61	fibroblast growth factor 2	Homo sapiens	96-122
17580326-2	2007	FGF-2 is known as a heparin-binding growth factor, but the localization of the heparin binding site has not been fully investigated until now.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	0-5
17580326-3	2007	We used two potential heparin binding domains of FGF-2, the residues 105-111 (F105, YKRSRYT) and 119-135 (F119, KRTGQYKLGSKTGPGQK).	Heparin	22-29	fibroblast growth factor 2	Homo sapiens	49-54
17971291-4	2007	Growth plate perlecan contains chondroitin sulfate (CS) and heparan sulfate (HS) chains and FGF-18 is known to bind to heparin and to heparan sulfate from some sources.	Heparin	119-126	fibroblast growth factor 18	Mus musculus	92-98
17979153-1	2007	Vascular endothelial growth factor A (VEGF-A) belongs to a family of heparin binding growth factors that include VEGF-B, VEGF-C, VEGF-D, and placental-like growth factor (PLGF).	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	38-44
17979153-1	2007	Vascular endothelial growth factor A (VEGF-A) belongs to a family of heparin binding growth factors that include VEGF-B, VEGF-C, VEGF-D, and placental-like growth factor (PLGF).	Heparin	69-76	vascular endothelial growth factor C	Homo sapiens	121-127
17979153-1	2007	Vascular endothelial growth factor A (VEGF-A) belongs to a family of heparin binding growth factors that include VEGF-B, VEGF-C, VEGF-D, and placental-like growth factor (PLGF).	Heparin	69-76	placental growth factor	Homo sapiens	141-169
18036357-11	2007	It suppressed pro-MMP-1 rapidly and decreased myoglobin, whereas heparin suppressed VEGF in patients with acute MI.	Heparin	65-72	vascular endothelial growth factor A	Homo sapiens	84-88
17985932-10	2007	Glycosaminoglycan binding by IGFBPs can affect their IGF binding although the effects appear to differ among different IGFBPs; here, we found that heparin bound to the IGF-I.N-BP-2.C-BP-2 ternary complex, but did not cause it to dissociate.	Heparin	147-154	insulin like growth factor 1	Homo sapiens	168-173
17879163-3	2007	Here we report that an altered matrix, consisting of a mutated, nonfunctional high-affinity heparin-binding domain and the V region of fibronectin (V+H-), induced anoikis in human SCC cells; this response was blocked by inhibitors of caspase-8 and caspase-3.	Heparin	92-99	caspase 3	Homo sapiens	248-257
17879163-8	2007	These findings provide evidence that mutations in the high-affinity heparin-binding domain in association with the V region of fibronectin, or altered fibronectin matrices, induce anoikis in human SCC cells by modulating integrin alpha v-mediated phosphorylation of FAK and ERK.	Heparin	68-75	fibronectin 1	Homo sapiens	127-138
17879163-8	2007	These findings provide evidence that mutations in the high-affinity heparin-binding domain in association with the V region of fibronectin, or altered fibronectin matrices, induce anoikis in human SCC cells by modulating integrin alpha v-mediated phosphorylation of FAK and ERK.	Heparin	68-75	mitogen-activated protein kinase 1	Homo sapiens	274-277
17961179-0	2007	Heparin-induced thrombocytopenia associated with interleukin-8-dependent platelet activation in a patient with antiphospholipid syndrome.	Heparin	0-7	C-X-C motif chemokine ligand 8	Homo sapiens	49-62
18057711-4	2007	OR-heparin also inhibited high glucose-activated ERK1/2 phosphorylation, induced p27(Kip1) expression, and suppressed reactive oxygen species (ROS) accumulation in a dose-dependent manner.	Heparin	3-10	mitogen-activated protein kinase 3	Homo sapiens	49-55
18057711-4	2007	OR-heparin also inhibited high glucose-activated ERK1/2 phosphorylation, induced p27(Kip1) expression, and suppressed reactive oxygen species (ROS) accumulation in a dose-dependent manner.	Heparin	3-10	zinc ribbon domain containing 2	Homo sapiens	81-84
18057711-5	2007	Our results suggest that OR-heparin releases high glucose-arrested cells on G(1) phase and inhibits high glucose-induced mesangial cell proliferation through blocking ERK1/2 phosphorylation and delaying S phase progression, which may be in correlation with OR-heparin suppressing ROS accumulation.	Heparin	28-35	mitogen-activated protein kinase 3	Homo sapiens	167-173
17961179-3	2007	Further analysis revealed anti-interleukin (IL)-8 antibodies and IL-8-dependent platelet activation facilitated by heparin, which may explain this unusual case of heparin-induced thrombocytopenia.	Heparin	115-122	C-X-C motif chemokine ligand 8	Homo sapiens	65-69
17961179-3	2007	Further analysis revealed anti-interleukin (IL)-8 antibodies and IL-8-dependent platelet activation facilitated by heparin, which may explain this unusual case of heparin-induced thrombocytopenia.	Heparin	163-170	C-X-C motif chemokine ligand 8	Homo sapiens	65-69
17503533-1	2007	Photo-crosslinkable and biodegradable Pluronic/heparin composite hydrogels were fabricated for local and sustained delivery of basic fibroblast growth factor (bFGF) to induce angiogenesis.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	127-157
17503533-1	2007	Photo-crosslinkable and biodegradable Pluronic/heparin composite hydrogels were fabricated for local and sustained delivery of basic fibroblast growth factor (bFGF) to induce angiogenesis.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	159-163
17503533-3	2007	An aqueous solution containing the two macromers with different weight ratios was photo-crosslinked in the presence of bFGF to produce in situ formed bFGF loaded Pluronic/heparin hydrogels.	Heparin	171-178	fibroblast growth factor 2	Homo sapiens	119-123
17503533-3	2007	An aqueous solution containing the two macromers with different weight ratios was photo-crosslinked in the presence of bFGF to produce in situ formed bFGF loaded Pluronic/heparin hydrogels.	Heparin	171-178	fibroblast growth factor 2	Homo sapiens	150-154
17503533-5	2007	The incorporation of heparin in the composite hydrogel enabled the controlled release of bFGF over a one month period in a near zero order manner.	Heparin	21-28	fibroblast growth factor 2	Homo sapiens	89-93
17503533-6	2007	The prolonged release of bFGF could be attributed to the specific interaction between bFGF and heparin in the hydrogel matrices.	Heparin	95-102	fibroblast growth factor 2	Homo sapiens	25-29
17503533-6	2007	The prolonged release of bFGF could be attributed to the specific interaction between bFGF and heparin in the hydrogel matrices.	Heparin	95-102	fibroblast growth factor 2	Homo sapiens	86-90
17875649-3	2007	Heparin bound to N,N"-dimethyl-N-(acetyl)-N"-(7-nitrobenz-3-oxa-1,3-diazol-4-yl)ethylenediamine (NBD)-fluorophore-labeled antithrombins and accelerated the reactions of the labeled inhibitor with thrombin and factor Xa similar to wild type.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	126-134
18293809-8	2007	Based on the literature, the treatment for heparin resistance used in the algorithm is anti-thrombin III supplement.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	92-100
17944804-1	2007	The keratinocyte growth factor receptor (KGFR)/fibroblast growth factor receptor 2b is activated by high-affinity-specific interaction with two different ligands, keratinocyte growth factor (KGF)/fibroblast growth factor (FGF)7 and FGF10/KGF2, which are characterized by an opposite requirement of heparan sulfate proteoglycans and heparin for binding to the receptor.	Heparin	332-339	fibroblast growth factor 7	Homo sapiens	4-30
17944804-1	2007	The keratinocyte growth factor receptor (KGFR)/fibroblast growth factor receptor 2b is activated by high-affinity-specific interaction with two different ligands, keratinocyte growth factor (KGF)/fibroblast growth factor (FGF)7 and FGF10/KGF2, which are characterized by an opposite requirement of heparan sulfate proteoglycans and heparin for binding to the receptor.	Heparin	332-339	fibroblast growth factor 7	Homo sapiens	41-44
17944804-1	2007	The keratinocyte growth factor receptor (KGFR)/fibroblast growth factor receptor 2b is activated by high-affinity-specific interaction with two different ligands, keratinocyte growth factor (KGF)/fibroblast growth factor (FGF)7 and FGF10/KGF2, which are characterized by an opposite requirement of heparan sulfate proteoglycans and heparin for binding to the receptor.	Heparin	332-339	fibroblast growth factor 10	Homo sapiens	232-237
17655843-10	2007	In conclusion, alpha(2A)-adrenoreceptor activates ERK and Akt in intestinal cells by a common pathway which depends on PI3-kinase activation and results from EGF receptor transactivation, via an autocrine/paracrine pathway implying MMP activation and heparin-binding-EGF shedding.	Heparin	251-258	mitogen-activated protein kinase 1	Homo sapiens	50-53
17655843-10	2007	In conclusion, alpha(2A)-adrenoreceptor activates ERK and Akt in intestinal cells by a common pathway which depends on PI3-kinase activation and results from EGF receptor transactivation, via an autocrine/paracrine pathway implying MMP activation and heparin-binding-EGF shedding.	Heparin	251-258	epidermal growth factor receptor	Homo sapiens	158-170
17919071-0	2007	In vitro investigation of the apoptotic effect of heparin on lymphoblasts by using flow cytometric DNA analysis and fluorometric caspase-3 and -8 activities.	Heparin	50-57	caspase 3	Homo sapiens	129-145
17920287-5	2007	VEGF(165) significantly decreased during both enoxaparin (chi(2) ANOVA=33.0, P&lt;10(-6)) and UFH (chi(2) ANOVA=27.2, P&lt;10(-6)) anticoagulated HD, while over-HD bFGF remained stable regardless of the type of heparin.	Heparin	94-97	vascular endothelial growth factor A	Homo sapiens	0-4
17920287-5	2007	VEGF(165) significantly decreased during both enoxaparin (chi(2) ANOVA=33.0, P&lt;10(-6)) and UFH (chi(2) ANOVA=27.2, P&lt;10(-6)) anticoagulated HD, while over-HD bFGF remained stable regardless of the type of heparin.	Heparin	211-218	vascular endothelial growth factor A	Homo sapiens	0-4
17920287-6	2007	The switch from enoxaparin to UFH treatment was connected with 34% VEGF(165) decrease after 180min of HD and had no impact on bFGF.	Heparin	30-33	vascular endothelial growth factor A	Homo sapiens	67-71
17920287-7	2007	During UFH-anticoagulated HD 75% VEGF(165) decrease after 10min was negatively associated with heparin dosage and was more profound in patients with ischemic heart disease.	Heparin	7-10	vascular endothelial growth factor A	Homo sapiens	33-37
17920287-7	2007	During UFH-anticoagulated HD 75% VEGF(165) decrease after 10min was negatively associated with heparin dosage and was more profound in patients with ischemic heart disease.	Heparin	95-102	vascular endothelial growth factor A	Homo sapiens	33-37
17920287-8	2007	CONCLUSION: The traditional UFH regimen, in contrast to enoxaparin treatment, is connected with dose-depended VEGF(165) decrease during HD procedure.	Heparin	28-31	vascular endothelial growth factor A	Homo sapiens	110-114
17919071-6	2007	Significantly higher caspase-3 and -8 activities were determined in 10 and 20 U/mL heparin concentrations than those in 0 U/mL heparin concentration at 0, 1, and 2 h (p &lt; 0.001).	Heparin	83-90	caspase 3	Homo sapiens	21-37
17919071-6	2007	Significantly higher caspase-3 and -8 activities were determined in 10 and 20 U/mL heparin concentrations than those in 0 U/mL heparin concentration at 0, 1, and 2 h (p &lt; 0.001).	Heparin	127-134	caspase 3	Homo sapiens	21-37
17919071-9	2007	It was concluded that the apoptotic effect of heparin in vitro on lymphoblasts developed due to the extrinsic pathway of apoptosis via the caspase-3 and -8 activations in newly diagnosed ALL patients.	Heparin	46-53	caspase 3	Homo sapiens	139-155
17699512-2	2007	Heparin, a highly sulfated polymer of uronic acids and glucosamine, binds strongly to the integrin receptor alphaXbeta2 (p150,95, CD11c/CD18).	Heparin	0-7	integrin subunit beta 2	Homo sapiens	136-140
26636224-3	2007	First, we tried to predict the structure of basic fibroblast growth factor (bFGF) bound to heparin, using the docking simulation program AutoDock 3.0.	Heparin	91-98	fibroblast growth factor 2	Homo sapiens	44-74
26636224-3	2007	First, we tried to predict the structure of basic fibroblast growth factor (bFGF) bound to heparin, using the docking simulation program AutoDock 3.0.	Heparin	91-98	fibroblast growth factor 2	Homo sapiens	76-80
26636224-6	2007	We docked a heparin molecule onto the protein simplex and generated many trial structures for the bFGF-heparin complex.	Heparin	12-19	fibroblast growth factor 2	Homo sapiens	98-102
26636224-6	2007	We docked a heparin molecule onto the protein simplex and generated many trial structures for the bFGF-heparin complex.	Heparin	103-110	fibroblast growth factor 2	Homo sapiens	98-102
18070750-4	2007	RESULTS: Incubation of macrophages with heparin- or insulin-treated adipocyte CM increased tumor necrosis factor alpha, interleukin-6, and nitric oxide production by these cells.	Heparin	40-47	interleukin 6	Homo sapiens	120-133
17699512-0	2007	Binding between the integrin alphaXbeta2 (CD11c/CD18) and heparin.	Heparin	58-65	integrin subunit beta 2	Homo sapiens	48-52
17475939-4	2007	RESULTS: Cord insulin concentrations significantly decreased (74% those at baseline by 24 h; P = 0.01) in the samples taken in heparin and stored at room temperature, but those taken on EDTA and refrigerated remained stable for up to 48 h. Insulin propeptides were stable in both.	Heparin	127-134	insulin	Homo sapiens	14-21
17595214-5	2007	When actinomycin was given to fed rats, heparin-releasable LPL activity increased by 160% in heart and by 150% in a skeletal muscle (soleus) in 6 h. Postheparin LPL activity in blood increased by about 200%.	Heparin	40-47	lipoprotein lipase	Rattus norvegicus	59-62
17595214-5	2007	When actinomycin was given to fed rats, heparin-releasable LPL activity increased by 160% in heart and by 150% in a skeletal muscle (soleus) in 6 h. Postheparin LPL activity in blood increased by about 200%.	Heparin	40-47	lipoprotein lipase	Rattus norvegicus	161-164
17898368-0	2007	Thrombin generation assay and viscoelastic coagulation monitors demonstrate differences in the mode of thrombin inhibition between unfractionated heparin and bivalirudin.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	0-8
17898368-0	2007	Thrombin generation assay and viscoelastic coagulation monitors demonstrate differences in the mode of thrombin inhibition between unfractionated heparin and bivalirudin.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	103-111
17898368-4	2007	METHODS: Thrombin formation was evaluated in platelet-poor plasma activated in the presence of heparin (0-5 U/mL) or bivalirudin (0-30 microg/mL) using a thrombin generation assay (Thrombinoscope).	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	9-17
17898368-7	2007	RESULTS: Based on the Thrombinoscope results, increasing concentrations of bivalirudin and heparin progressively delayed the onset of thrombin formation, but only heparin dose-dependently decreased the amount of thrombin generated.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	134-142
17898368-7	2007	RESULTS: Based on the Thrombinoscope results, increasing concentrations of bivalirudin and heparin progressively delayed the onset of thrombin formation, but only heparin dose-dependently decreased the amount of thrombin generated.	Heparin	163-170	coagulation factor II, thrombin	Homo sapiens	212-220
17717013-1	2007	A common gene variant in the heparin-binding domain (HBD) of extracellular superoxide dismutase (ECSOD) may predispose human carriers to ischaemic heart disease.	Heparin	29-36	superoxide dismutase 3	Homo sapiens	97-102
17868672-3	2007	We show that most of the activity can be inhibited by heparin, an inhibitor of CK2.	Heparin	54-61	casein kinase 2 beta	Rattus norvegicus	79-82
17928217-3	2007	Hybrid chondroitin/dermatan sulfate chains are also involved in formation of the neural network by capturing and presenting heparin-binding growth factors like basic fibroblast growth factor, pleiotrophin, and hepatocyte growth factor to stem cells or neuronal cells.	Heparin	124-131	pleiotrophin	Homo sapiens	192-204
18000790-6	2007	Heparins and heparin derivatives, which induce the release of TFPI from the vascular endothelium, also exhibit antitumor effects, and TFPI may contribute significantly to those effects.	Heparin	0-8	tissue factor pathway inhibitor	Mus musculus	62-66
17673511-0	2007	The binding of human betacellulin to heparin, heparan sulfate and related polysaccharides.	Heparin	37-44	betacellulin	Homo sapiens	21-33
17673511-1	2007	Recombinant human betacellulin binds strongly to heparin, requiring of the order of 0.8 M NaCl for its elution from a heparin affinity matrix.	Heparin	49-56	betacellulin	Homo sapiens	18-30
17673511-1	2007	Recombinant human betacellulin binds strongly to heparin, requiring of the order of 0.8 M NaCl for its elution from a heparin affinity matrix.	Heparin	118-125	betacellulin	Homo sapiens	18-30
17673511-8	2007	Heparin protects betacellulin from proteolysis by LysC, but K5 polysaccharide does not.	Heparin	0-7	betacellulin	Homo sapiens	17-29
18000790-6	2007	Heparins and heparin derivatives, which induce the release of TFPI from the vascular endothelium, also exhibit antitumor effects, and TFPI may contribute significantly to those effects.	Heparin	0-8	tissue factor pathway inhibitor	Mus musculus	134-138
18000790-6	2007	Heparins and heparin derivatives, which induce the release of TFPI from the vascular endothelium, also exhibit antitumor effects, and TFPI may contribute significantly to those effects.	Heparin	13-20	tissue factor pathway inhibitor	Mus musculus	62-66
18000790-6	2007	Heparins and heparin derivatives, which induce the release of TFPI from the vascular endothelium, also exhibit antitumor effects, and TFPI may contribute significantly to those effects.	Heparin	13-20	tissue factor pathway inhibitor	Mus musculus	134-138
18000790-7	2007	Indeed, a non-anticoagulant low-molecular-weight heparin with intact TFPI-releasing capacity has been shown to have significant antimetastatic effect in a similar experimental mouse model.	Heparin	49-56	tissue factor pathway inhibitor	Mus musculus	69-73
17496250-14	2007	Phosphorylation and O-glycosylation both affected IGFBP-5 binding to heparin but not insulin-like growth factor binding or ternary complex formation with the acid-labile subunit.	Heparin	69-76	insulin like growth factor binding protein 5	Homo sapiens	50-57
17626017-8	2007	In contrast, the HBD mutants showed slightly decreased binding to the NRP1 (neuropilin-1) receptor, and analyses suggested the heparin and NRP1 binding sites to be distinct but overlapping.	Heparin	127-134	neuropilin 1	Mus musculus	70-74
17664148-7	2007	Blocking binding sites with exogenous heparin enhanced VEGF protein in the medium from RA-grown cells, whereas heparinase digestion of bound VEGF revealed a greater reserve of VEGF protein in RA cells.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	55-59
17969246-1	2007	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of basic fibroblast growth factor (bFGF) and transforming growth factor-beta1 (TGF-beta1) production as a wound healing modulator.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	122-152
17969246-1	2007	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of basic fibroblast growth factor (bFGF) and transforming growth factor-beta1 (TGF-beta1) production as a wound healing modulator.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	154-158
17969246-1	2007	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of basic fibroblast growth factor (bFGF) and transforming growth factor-beta1 (TGF-beta1) production as a wound healing modulator.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	164-196
17969246-1	2007	Heparin affects both dermal fibroblast proliferation and collagen and may mediate these effects by altering the levels of basic fibroblast growth factor (bFGF) and transforming growth factor-beta1 (TGF-beta1) production as a wound healing modulator.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	198-207
17969246-2	2007	The purpose of this study is to probe the effect of heparin on bFGF and TGF-beta1 production by human normal skin and hyperplastic scar fibroblasts.	Heparin	52-59	fibroblast growth factor 2	Homo sapiens	63-67
17969246-2	2007	The purpose of this study is to probe the effect of heparin on bFGF and TGF-beta1 production by human normal skin and hyperplastic scar fibroblasts.	Heparin	52-59	transforming growth factor beta 1	Homo sapiens	72-81
17969246-3	2007	This research investigates the effect of heparin on bFGF and TGF-beta1 production by human normal skin and hyperplastic scar fibroblasts with exposure to 0, 100, 300, or 600 microg/ml heparin for 24, 48, 72, or 96 hours in a serum-free in vitro model.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	52-56
17969246-5	2007	All doses of heparin significantly stimulated production of bFGF by normal skin (393% to 1019% increase) and hyperplastic scar fibroblasts (405% to 899% increase) at all time points (P &lt; .05).	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	60-64
17969246-6	2007	Heparin (300 and 600 microg/ml) also stimulated TGF-beta1 production by normal skin (26% to 83%) and hyperplastic scar fibroblasts (63% to 85%) with statistical significance (P &lt; .05) at various time points.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	48-57
17911567-8	2007	Direct thrombin inhibitors block thrombin (IIa) and are used mostly for heparin-induced thrombosis or during coronary interventions.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	7-15
17658885-0	2007	Glycosaminoglycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers.	Heparin	189-196	coagulation factor II, thrombin	Homo sapiens	142-150
17658885-0	2007	Glycosaminoglycans as naturally occurring combinatorial libraries: developing a mass spectrometry-based strategy for characterization of anti-thrombin interaction with low molecular weight heparin and heparin oligomers.	Heparin	201-208	coagulation factor II, thrombin	Homo sapiens	142-150
17525363-5	2007	In the UFH+eptifibatide, but not the bivalirudin group, myeloperoxidase (MPO) levels were elevated 2.3-fold above baseline (P=0.004) immediately after PCI.	Heparin	7-10	myeloperoxidase	Homo sapiens	56-71
17525363-5	2007	In the UFH+eptifibatide, but not the bivalirudin group, myeloperoxidase (MPO) levels were elevated 2.3-fold above baseline (P=0.004) immediately after PCI.	Heparin	7-10	myeloperoxidase	Homo sapiens	73-76
17525363-6	2007	In an in vitro assay, heparin and to a lesser extent enoxaparin, but not bivalirudin or eptifibatide, stimulated MPO release from and binding to neutrophils and neutrophil activation.	Heparin	22-29	myeloperoxidase	Homo sapiens	113-116
17475322-4	2007	First, soluble heparin was delivered to compete with cell-surface HSPG for the binding of FGF-2.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	90-95
17580303-6	2007	Heparin coupled to bovine serum albumin (heparin-BSA) was able to mediate binding between fibronectin and LTBP1.	Heparin	0-7	albumin	Homo sapiens	26-39
17580303-6	2007	Heparin coupled to bovine serum albumin (heparin-BSA) was able to mediate binding between fibronectin and LTBP1.	Heparin	0-7	fibronectin 1	Homo sapiens	90-101
17580303-7	2007	Treatment of primary osteoblast cultures with heparin or heparin-BSA but not with chondroitin sulfate impaired LTBP1 deposition onto fibronectin without inhibiting expression of LTBP1.	Heparin	46-53	fibronectin 1	Homo sapiens	133-144
17580303-7	2007	Treatment of primary osteoblast cultures with heparin or heparin-BSA but not with chondroitin sulfate impaired LTBP1 deposition onto fibronectin without inhibiting expression of LTBP1.	Heparin	57-64	fibronectin 1	Homo sapiens	133-144
17662276-8	2007	5-Amino-2-NMS binds to the heparin-binding site of FGF1 and FGF2 and thus may be a promising substance for the local treatment of retinal neovascularization.	Heparin	27-34	fibroblast growth factor 1	Mus musculus	51-55
17886208-5	2007	Low molecular weight heparanoid and direct thrombin inhibitors (recombinant hirudin or argatroban) may be useful for anticoagulation of the extracorporeal circuit in the rare patients with confirmed heparin-induced thrombocytopenia type II, who cannot be dialyzed with heparin.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	43-51
17886208-5	2007	Low molecular weight heparanoid and direct thrombin inhibitors (recombinant hirudin or argatroban) may be useful for anticoagulation of the extracorporeal circuit in the rare patients with confirmed heparin-induced thrombocytopenia type II, who cannot be dialyzed with heparin.	Heparin	269-276	coagulation factor II, thrombin	Homo sapiens	43-51
17969246-0	2007	Effect of heparin on production of basic fibroblast growth factor and transforming growth factor-beta1 by human normal skin and hyperplastic scar fibroblasts.	Heparin	10-17	fibroblast growth factor 2	Homo sapiens	35-65
17969246-0	2007	Effect of heparin on production of basic fibroblast growth factor and transforming growth factor-beta1 by human normal skin and hyperplastic scar fibroblasts.	Heparin	10-17	transforming growth factor beta 1	Homo sapiens	70-102
17640335-5	2007	The biological potency of heparin was determined photometrically by the chromogenic substrate Chromozym TH and fibrinogen adsorption to the modified surfaces was researched using the QCM-D (Quartz Crystal Microbalance with Dissipation Monitoring) technique.	Heparin	26-33	fibrinogen beta chain	Homo sapiens	111-121
18634612-7	2007	Expression of vascular endothelial growth factor (VEGF) and EGFR ligands, such as heparin binding-EGF and transforming growth factor alpha, is upregulated in the SVZ after focal demyelination of the CC.	Heparin	82-89	vascular endothelial growth factor A	Homo sapiens	14-48
18634612-7	2007	Expression of vascular endothelial growth factor (VEGF) and EGFR ligands, such as heparin binding-EGF and transforming growth factor alpha, is upregulated in the SVZ after focal demyelination of the CC.	Heparin	82-89	vascular endothelial growth factor A	Homo sapiens	50-54
18634612-7	2007	Expression of vascular endothelial growth factor (VEGF) and EGFR ligands, such as heparin binding-EGF and transforming growth factor alpha, is upregulated in the SVZ after focal demyelination of the CC.	Heparin	82-89	epidermal growth factor receptor	Homo sapiens	60-64
17509717-7	2007	Incorporation of heparin into the scaffold increased the initial burst release of bFGF, while the initial bFGF loading content did not change release kinetics significantly.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	82-86
17580963-7	2007	Acrolein modification impairs the ability of apoE3-NT to interact with heparin and the LDL receptor.	Heparin	71-78	apolipoprotein E	Homo sapiens	45-50
17635698-4	2007	Exosite-2 residues (Arg89, Arg93, Glu94, Arg98, Arg245, Arg248, and Gln251) were critical for heparin-accelerated inhibition of thrombin by PCI.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	128-136
17456194-7	2007	The second-order rate constants (m(-1) min(-1)) of the reaction between HGFA and PCI in the presence or absence of heparin (10 U mL(-1)) were 4.3 x 10(6) and 4.0 x 10(6), respectively.	Heparin	115-122	HGF activator	Homo sapiens	72-76
17456194-9	2007	Exogenous HGFA added to normal human plasma formed a complex with plasma PCI, and this complex formation was competitively inhibited by APC in the presence of heparin, but very weakly in the absence of heparin.	Heparin	159-166	HGF activator	Homo sapiens	10-14
17456194-9	2007	Exogenous HGFA added to normal human plasma formed a complex with plasma PCI, and this complex formation was competitively inhibited by APC in the presence of heparin, but very weakly in the absence of heparin.	Heparin	202-209	HGF activator	Homo sapiens	10-14
17325231-2	2007	A long-held assumption that has guided the use of VEGF isoforms clinically has been that their differences in heparin binding dictate their ability to diffuse through tissue, with VEGF121 moving most freely and that the distribution of recombinant VEGF would have therapeutically relevant consequences.	Heparin	110-117	vascular endothelial growth factor A	Homo sapiens	50-54
17635698-8	2007	CONCLUSIONS: Collectively, these results show that (i) similar thrombin exosite-2 residues are critical for the heparin-catalyzed inhibition by PCI and AT, (ii) PCI and AT are different in their thrombin-TM inhibition properties, and (iii) PCI has a distinct advantage over AT in the regulation of the activity of thrombin-TM.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	195-203
17635698-8	2007	CONCLUSIONS: Collectively, these results show that (i) similar thrombin exosite-2 residues are critical for the heparin-catalyzed inhibition by PCI and AT, (ii) PCI and AT are different in their thrombin-TM inhibition properties, and (iii) PCI has a distinct advantage over AT in the regulation of the activity of thrombin-TM.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	195-203
17635698-7	2007	Using the aforementioned thrombin exosite-2 mutants that were essential for heparin-catalyzed PCI-thrombin inhibition reactions we found no change in PCI inhibition rates for thrombin-TM.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	98-106
17635698-7	2007	Using the aforementioned thrombin exosite-2 mutants that were essential for heparin-catalyzed PCI-thrombin inhibition reactions we found no change in PCI inhibition rates for thrombin-TM.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	98-106
17635698-8	2007	CONCLUSIONS: Collectively, these results show that (i) similar thrombin exosite-2 residues are critical for the heparin-catalyzed inhibition by PCI and AT, (ii) PCI and AT are different in their thrombin-TM inhibition properties, and (iii) PCI has a distinct advantage over AT in the regulation of the activity of thrombin-TM.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	63-71
17388803-4	2007	In models of arterial injury, FXII or FXI null mice are protected from formation of platelet rich occlusive thrombi to a degree similar to that seen in FIX deficient mice (a model for the severe bleeding disorder hemophilia B) or to wild type mice treated with high dose heparin.	Heparin	271-278	coagulation factor XI	Mus musculus	30-33
17629845-0	2007	High-performance liquid chromatographic/mass spectrometric studies on the susceptibility of heparin species to cleavage by heparanase.	Heparin	92-99	heparanase	Homo sapiens	123-133
17629845-2	2007	With the aim of establishing a simple and reliable method for studying the susceptibility of heparin/heparan sulfate oligosaccharides to be cleaved by heparanase, an on-line ion pair reversed-phase high-performance liquid chromatographic/electrospray ionization mass spectrometric method was set up.	Heparin	93-100	heparanase	Homo sapiens	151-161
17629847-1	2007	Prothrombinase-induced clotting time (PiCT) determines the anticoagulant effects of heparins, low molecular weight heparins (LMWHs), and direct thrombin inhibitors.	Heparin	84-92	coagulation factor II, thrombin	Homo sapiens	3-11
17629847-1	2007	Prothrombinase-induced clotting time (PiCT) determines the anticoagulant effects of heparins, low molecular weight heparins (LMWHs), and direct thrombin inhibitors.	Heparin	115-123	coagulation factor II, thrombin	Homo sapiens	3-11
17536787-4	2007	In addition, direct binding of NKp44 to heparin was observed, and soluble heparin/heparan sulfate enhanced the secretion of IFNgamma by NK92 cells activated with anti-NKp44 monoclonal antibody.	Heparin	40-47	natural cytotoxicity triggering receptor 2	Homo sapiens	31-36
17536787-4	2007	In addition, direct binding of NKp44 to heparin was observed, and soluble heparin/heparan sulfate enhanced the secretion of IFNgamma by NK92 cells activated with anti-NKp44 monoclonal antibody.	Heparin	74-81	interferon gamma	Homo sapiens	124-132
17536787-4	2007	In addition, direct binding of NKp44 to heparin was observed, and soluble heparin/heparan sulfate enhanced the secretion of IFNgamma by NK92 cells activated with anti-NKp44 monoclonal antibody.	Heparin	74-81	natural cytotoxicity triggering receptor 2	Homo sapiens	167-172
17536787-5	2007	Basic amino acids, predicted to constitute the putative heparin/heparan sulfate binding site of NKp44, were mutated.	Heparin	56-63	natural cytotoxicity triggering receptor 2	Homo sapiens	96-101
17536787-6	2007	Tumor cell recognition of the mutated NKp44 proteins was significantly reduced and correlated with their lower recognition of heparin.	Heparin	126-133	natural cytotoxicity triggering receptor 2	Homo sapiens	38-43
17330862-7	2007	Predictably, other hydrophilic flexible polyanions such as heparin, polyglutamate, and polyadenylate also have a destabilizing effect on the structure of cyt c.	Heparin	59-66	cytochrome c, somatic	Homo sapiens	154-159
17537059-6	2007	Binding kinetics of thrombin to heparin and to heparin-albumin conjugate were calculated using two different methods.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	20-28
17537059-9	2007	The affinity of thrombin toward the heparin-coated surface proved to be higher than its affinity toward the heparin conjugate.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	16-24
17537059-9	2007	The affinity of thrombin toward the heparin-coated surface proved to be higher than its affinity toward the heparin conjugate.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	16-24
17669856-1	2007	Prothrombin time, expressed as international normalized ratio (INR) and activated partial thromboplastin time (aPTT), are standard methods of monitoring coumadin and heparin administration.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	0-11
17335894-5	2007	Furthermore, we investigated the anti-metastatic effect of heparin-DOCA against lung metastasis induced by B16F10 and SCC7.	Heparin	59-66	colon tumor susceptibility 7	Mus musculus	118-122
17335894-6	2007	Heparin-DOCA inhibited intercellular interactions between B16F10 and activated platelets or activated HUVECs by blocking P- and E-selectin-mediated interactions.	Heparin	0-7	selectin, endothelial cell	Mus musculus	128-138
17335894-8	2007	Heparin-DOCA attenuated lung colony formation on the surfaces and in interior of the lung, and attenuated metastasis by B16F10 and SCC7.	Heparin	0-7	colon tumor susceptibility 7	Mus musculus	131-135
17094138-9	2007	Both heparin and sucrose appear to enhance the thermal stability of FGF-1, although their effects on the phase diagram are quite distinct.	Heparin	5-12	fibroblast growth factor 1	Homo sapiens	68-73
17094138-11	2007	Only heparin appears to protect FGF-1 from acid-induced unfolding to any extent.	Heparin	5-12	fibroblast growth factor 1	Homo sapiens	32-37
17389624-2	2007	In this cross-over study, we compared the effects of enoxaparin and unfractionated heparin (UFH) used as anticoagulants during haemodialysis (HD) on plasma TGF-beta1 levels and some platelet activation markers: platelet-derived growth factor-AB (PDGF-AB), beta-thromboglobulin (beta-TG) and platelet factor-4 (PF-4).	Heparin	92-95	transforming growth factor beta 1	Homo sapiens	156-165
17298301-3	2007	The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRalpha1 (GDNF family receptor alpha1), and heparin-bound GDNF is able to bind GFRalpha1 simultaneously.	Heparin	4-11	glial cell derived neurotrophic factor	Homo sapiens	129-133
18221061-1	2007	Pleiotrophin (PTN) is an 18 kDa growth factor that has high affinity for heparin and together with midkine form a family of structurally related heparin binding growth factors.	Heparin	73-80	pleiotrophin	Homo sapiens	0-12
18221061-1	2007	Pleiotrophin (PTN) is an 18 kDa growth factor that has high affinity for heparin and together with midkine form a family of structurally related heparin binding growth factors.	Heparin	73-80	pleiotrophin	Homo sapiens	14-17
18221061-1	2007	Pleiotrophin (PTN) is an 18 kDa growth factor that has high affinity for heparin and together with midkine form a family of structurally related heparin binding growth factors.	Heparin	145-152	pleiotrophin	Homo sapiens	0-12
18221061-1	2007	Pleiotrophin (PTN) is an 18 kDa growth factor that has high affinity for heparin and together with midkine form a family of structurally related heparin binding growth factors.	Heparin	145-152	pleiotrophin	Homo sapiens	14-17
17546553-1	2007	BACKGROUND: Lepirudin, a recombinant hirudin, is a direct acting thrombin inhibitor that has been used as a heparin alternative in patients with heparin-induced thrombocytopenia requiring on-pump cardiac surgery.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	65-73
17546553-1	2007	BACKGROUND: Lepirudin, a recombinant hirudin, is a direct acting thrombin inhibitor that has been used as a heparin alternative in patients with heparin-induced thrombocytopenia requiring on-pump cardiac surgery.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	65-73
17478733-2	2007	Here, we explored whether the C-terminal heparin-binding domain of the VEGF(165) or VEGF(189) isoform also containing neuropilin-binding sequences could substitute for the silk homology domain of VEGF-C.	Heparin	41-48	vascular endothelial growth factor A	Homo sapiens	71-75
17478733-7	2007	We conclude that the matrix-binding domain of VEGF can target VEGF-C activity to heparin-rich basement membrane structures.	Heparin	81-88	vascular endothelial growth factor A	Homo sapiens	46-50
17478733-7	2007	We conclude that the matrix-binding domain of VEGF can target VEGF-C activity to heparin-rich basement membrane structures.	Heparin	81-88	vascular endothelial growth factor C	Homo sapiens	62-68
17478734-4	2007	VEGF-CAC also bound to neuropilins in a heparin-dependent manner.	Heparin	40-47	vascular endothelial growth factor A	Homo sapiens	0-4
17384413-0	2007	Eotaxin selectively binds heparin.	Heparin	26-33	chemokine (C-C motif) ligand 11	Mus musculus	0-7
17384413-6	2007	Here we report that eotaxin binds selectively to immobilized heparin with high affinity (K(d) = 1.23 x 10(-8) M), but not to heparan sulfate or a range of other GAGs.	Heparin	61-68	chemokine (C-C motif) ligand 11	Mus musculus	20-27
17384413-7	2007	The interaction of eotaxin with heparin does not promote eotaxin oligomerization but protects eotaxin from proteolysis directly by plasmin and indirectly by cathepsin G and elastase.	Heparin	32-39	chemokine (C-C motif) ligand 11	Mus musculus	19-26
17384413-8	2007	In vivo, co-administration of eotaxin and heparin is able to significantly enhance eotaxin-mediated eosinophil recruitment in a mouse air-pouch model.	Heparin	42-49	chemokine (C-C motif) ligand 11	Mus musculus	83-90
17384413-10	2007	In contrast, heparin does not enhance eotaxin-mediated eosinophil chemotaxis in vitro, suggesting protease protection or haptotactic gradient formation as the mechanism by which heparin enhances eotaxin action in vivo.	Heparin	178-185	chemokine (C-C motif) ligand 11	Mus musculus	195-202
17409095-0	2007	Structural and biophysical coupling of heparin and activin binding to follistatin isoform functions.	Heparin	39-46	follistatin	Homo sapiens	70-81
17298301-0	2007	The major determinant of the heparin binding of glial cell-line-derived neurotrophic factor is near the N-terminus and is dispensable for receptor binding.	Heparin	29-36	glial cell derived neurotrophic factor	Homo sapiens	48-91
17298301-1	2007	GDNF (glial cell-line-derived neurotrophic factor), and the closely related cytokines artemin and neurturin, bind strongly to heparin.	Heparin	126-133	glial cell derived neurotrophic factor	Homo sapiens	0-4
17298301-1	2007	GDNF (glial cell-line-derived neurotrophic factor), and the closely related cytokines artemin and neurturin, bind strongly to heparin.	Heparin	126-133	glial cell derived neurotrophic factor	Homo sapiens	6-49
17298301-2	2007	Deletion of a basic amino-acid-rich sequence of 16 residues N-terminal to the first cysteine of the transforming growth factor beta domain of GDNF results in a marked reduction in heparin binding, whereas removal of a neighbouring sequence, and replacement of pairs of other basic residues with alanine had no effect.	Heparin	180-187	glial cell derived neurotrophic factor	Homo sapiens	142-146
17298301-3	2007	The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRalpha1 (GDNF family receptor alpha1), and heparin-bound GDNF is able to bind GFRalpha1 simultaneously.	Heparin	163-170	glial cell derived neurotrophic factor	Homo sapiens	129-133
17298301-4	2007	The heparin-binding sequence of GDNF is dispensable both for GFRalpha1 binding, and for activity for in vitro neurite outgrowth assay.	Heparin	4-11	glial cell derived neurotrophic factor	Homo sapiens	32-36
17298301-5	2007	Surprisingly, the observed inhibition of GDNF bioactivity with the wild-type protein in this assay was still found with the deletion mutant lacking the heparin-binding sequence.	Heparin	152-159	glial cell derived neurotrophic factor	Homo sapiens	41-45
17257606-0	2007	Determination of binding constant and binding region of programmed cell death 5-heparin by capillary zone electrophoresis.	Heparin	80-87	programmed cell death 5	Homo sapiens	56-79
17394193-1	2007	BACKGROUND: Cleavage of membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields a soluble HB-EGF isoform (sHB-EGF), which is an activating epidermal growth factor receptor (EGFR) ligand and a C-terminal fragment HB-EGF-C acting directly in the nucleus.	Heparin	42-49	epidermal growth factor receptor	Homo sapiens	179-211
17394193-1	2007	BACKGROUND: Cleavage of membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields a soluble HB-EGF isoform (sHB-EGF), which is an activating epidermal growth factor receptor (EGFR) ligand and a C-terminal fragment HB-EGF-C acting directly in the nucleus.	Heparin	42-49	epidermal growth factor receptor	Homo sapiens	213-217
19124943-2	2007	Thrombin is resistant to inactivation by heparin when it is bound to fibrin, fibrin degradation products or subendothelial collagen.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	0-8
17158598-8	2007	Activation of the BK-induced current was inhibited by heparin, indicating dependence on intact inositol 1,4,5-triphosphate (IP3)-sensitive intracellular Ca2+ stores.	Heparin	54-61	kininogen 1	Homo sapiens	18-20
17456623-0	2007	Inhibition of thrombin in plasma by heparin or arginine.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	14-22
17456623-3	2007	Using a newly developed physiologic assay system for fibrinogen/thrombin interaction (the FIFTA), the inhibition of plasmatic thrombin by heparin or by arginine was studied.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	126-134
17456623-5	2007	Plasmatic heparin concentrations equal to or greater than 0.63 IU/mL completely inhibit thrombin in the assay system described.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	88-96
17456623-15	2007	This study demonstrates the efficiency of two physiologic thrombin inhibitors: heparin and arginine.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	58-66
17154173-8	2007	P-selectin binding to the 4T1 cells was inhibited by heparin and CS glycosaminoglycans (GAGs).	Heparin	53-60	selectin, platelet	Mus musculus	0-10
17550736-0	2007	[The low molecular weight heparin on rat pulmonary surfactant associated protein A of acute pulmonary embolism].	Heparin	26-33	surfactant protein A1	Rattus norvegicus	41-82
17550736-1	2007	OBJECTIVE: To explore the effect of low molecular weight heparin (LMWH) on the changes of pulmonary surfactant associated protein A (SPA) of rats in acute pulmonary embolism.	Heparin	57-64	surfactant protein A1	Rattus norvegicus	90-131
17550736-1	2007	OBJECTIVE: To explore the effect of low molecular weight heparin (LMWH) on the changes of pulmonary surfactant associated protein A (SPA) of rats in acute pulmonary embolism.	Heparin	57-64	surfactant protein A1	Rattus norvegicus	133-136
17303003-7	2007	In fatty milk-induced hyperlipidemic mice, the post-heparin plasma activities of lipoprotein lipase (LPL), hepatic lipase (HL), and total lipase (TL) significantly increased after treatment with 10-20 mg/kg osthole for 3 weeks (P&lt; 0.05 or P&lt; 0.01).	Heparin	52-59	lipase, hepatic	Mus musculus	107-121
17359933-12	2007	Finally, when clones were cultured on fibronectin in the presence of heparin, a ligand of fibronectin, the inhibitory effect was completely reversed.	Heparin	69-76	fibronectin 1	Homo sapiens	38-49
17359933-12	2007	Finally, when clones were cultured on fibronectin in the presence of heparin, a ligand of fibronectin, the inhibitory effect was completely reversed.	Heparin	69-76	fibronectin 1	Homo sapiens	90-101
17428030-5	2007	In this study, we utilize the heparin binding domain of VEGF to bind the polyanion dextran sulfate, resulting in an enhanced thermal stability of VEGF.	Heparin	30-37	vascular endothelial growth factor A	Homo sapiens	56-60
17428030-5	2007	In this study, we utilize the heparin binding domain of VEGF to bind the polyanion dextran sulfate, resulting in an enhanced thermal stability of VEGF.	Heparin	30-37	vascular endothelial growth factor A	Homo sapiens	146-150
17699453-1	2007	Recombinant hirudin (lepirudin) is a potent direct thrombin inhibitor that is used particularly for treatment of immune-mediated heparin-induced thrombocytopenia.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	51-59
17461929-0	2007	Effect of the anti-factor Xa and anti-factor IIa activities of low-molecular-weight heparins upon the phases of thrombin generation.	Heparin	84-92	coagulation factor II, thrombin	Homo sapiens	112-120
17461929-1	2007	BACKGROUND: Low-molecular-weight heparins (LMWHs), derived from unfractionated heparin (UFH) by different depolymerization procedures, vary in both their relative abilities to enhance the inhibition of FXa (anti-FXa) and thrombin (anti-FIIa), and in their physicochemical properties.	Heparin	33-41	coagulation factor II, thrombin	Homo sapiens	221-229
17461929-1	2007	BACKGROUND: Low-molecular-weight heparins (LMWHs), derived from unfractionated heparin (UFH) by different depolymerization procedures, vary in both their relative abilities to enhance the inhibition of FXa (anti-FXa) and thrombin (anti-FIIa), and in their physicochemical properties.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	221-229
17461929-2	2007	OBJECTIVE: We aimed to profile the inhibition of thrombin generation induced by bemiparin, enoxaparin, nadroparin, dalteparin and tinzaparin in platelet-rich plasma (PRP), and to compare them with UFH and fondaparinux (a synthetic pentasaccharide that specifically enhances FXa inhibition).	Heparin	197-200	coagulation factor II, thrombin	Homo sapiens	49-57
17461929-5	2007	RESULTS: At equivalent anti-FIIa activity concentrations, LMWHs and UFH exhibited similar inhibitory effects upon thrombin generation.	Heparin	68-71	coagulation factor II, thrombin	Homo sapiens	114-122
17226785-0	2007	Heparin suppresses lipid raft-mediated signaling and ligand-independent EGF receptor activation.	Heparin	0-7	epidermal growth factor receptor	Homo sapiens	72-84
17226785-9	2007	In these situations, heparin inhibits phosphorylation of EGFR on the Src-dependent site Tyr(845), but not the autophosphorylation of Tyr(1173), and decreases Ras activation and Erk phosphorylation.	Heparin	21-28	epidermal growth factor receptor	Homo sapiens	57-61
17226785-9	2007	In these situations, heparin inhibits phosphorylation of EGFR on the Src-dependent site Tyr(845), but not the autophosphorylation of Tyr(1173), and decreases Ras activation and Erk phosphorylation.	Heparin	21-28	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	69-72
17226785-9	2007	In these situations, heparin inhibits phosphorylation of EGFR on the Src-dependent site Tyr(845), but not the autophosphorylation of Tyr(1173), and decreases Ras activation and Erk phosphorylation.	Heparin	21-28	mitogen-activated protein kinase 1	Homo sapiens	177-180
17226785-10	2007	We conclude that heparin can suppress Erk signaling in VSMC with effects on site-specific phosphorylation of EGFR localized in caveolin-enriched lipid rafts.	Heparin	17-24	mitogen-activated protein kinase 1	Homo sapiens	38-41
17226785-10	2007	We conclude that heparin can suppress Erk signaling in VSMC with effects on site-specific phosphorylation of EGFR localized in caveolin-enriched lipid rafts.	Heparin	17-24	epidermal growth factor receptor	Homo sapiens	109-113
17229890-4	2007	In a cell culture system, its product facilitated the secretion of heparin-binding epidermal growth factor-like growth factor (HB-EGF), one of the ligands of ErbB4.	Heparin	67-74	erb-b2 receptor tyrosine kinase 4	Gallus gallus	158-163
17255131-6	2007	Furthermore, the effects of removal of HS on TNF-alpha-activated mGEnC-1 by heparinase III treatment, and of different concentrations of heparin, tinzaparin and HS, on the rolling and adhesion of leucocytes were evaluated.	Heparin	76-83	tumor necrosis factor	Mus musculus	45-54
16750851-7	2007	In choriocarcinoma cells the heparin effect was also indirect, inducing a significant decrease in TIMP-1 and TIMP-2 protein expressions and mRNAs.	Heparin	29-36	TIMP metallopeptidase inhibitor 1	Homo sapiens	98-104
17326667-5	2007	Preincubation with heparin decreased the receptor binding of apolipoprotein A-V, indicating that overlap exists between the recognition sites for these receptors and for heparin.	Heparin	19-26	apolipoprotein A5	Homo sapiens	61-79
17326667-5	2007	Preincubation with heparin decreased the receptor binding of apolipoprotein A-V, indicating that overlap exists between the recognition sites for these receptors and for heparin.	Heparin	170-177	apolipoprotein A5	Homo sapiens	61-79
17326667-6	2007	A double mutant, apolipoprotein A-V (Arg210Glu/Lys211Gln), showed decreased binding to heparin and decreased ability to bind the low density lipoprotein receptor-related protein.	Heparin	87-94	apolipoprotein A5	Homo sapiens	17-35
17257606-1	2007	A sensitive and selective high-performance analytical method based on capillary zone electrophoresis (CZE) was developed for investigating interactions between heparin and programmed cell death 5 (PDCD5) qualitatively and quantitatively.	Heparin	160-167	programmed cell death 5	Homo sapiens	172-195
17257606-1	2007	A sensitive and selective high-performance analytical method based on capillary zone electrophoresis (CZE) was developed for investigating interactions between heparin and programmed cell death 5 (PDCD5) qualitatively and quantitatively.	Heparin	160-167	programmed cell death 5	Homo sapiens	197-202
17107942-4	2007	Upon PTH stimulation, metalloprotease cleavage of membrane-bound heparin-binding fragment (HB-EGF) induced EGFR transactivation of ERK.	Heparin	65-72	parathyroid hormone	Homo sapiens	5-8
17107942-4	2007	Upon PTH stimulation, metalloprotease cleavage of membrane-bound heparin-binding fragment (HB-EGF) induced EGFR transactivation of ERK.	Heparin	65-72	epidermal growth factor receptor	Homo sapiens	107-111
17257606-2	2007	The binding constant of the interaction between PDCD5 and heparin calculated by Scatchard analysis was 4.17x10(4) M(-1) and the binding sites located in the C-terminal region of PDCD5 (residues 109-115).	Heparin	58-65	programmed cell death 5	Homo sapiens	48-53
17107942-4	2007	Upon PTH stimulation, metalloprotease cleavage of membrane-bound heparin-binding fragment (HB-EGF) induced EGFR transactivation of ERK.	Heparin	65-72	mitogen-activated protein kinase 1	Homo sapiens	131-134
17257606-2	2007	The binding constant of the interaction between PDCD5 and heparin calculated by Scatchard analysis was 4.17x10(4) M(-1) and the binding sites located in the C-terminal region of PDCD5 (residues 109-115).	Heparin	58-65	programmed cell death 5	Homo sapiens	178-183
17441362-4	2007	ApoE was purified by heparin Sepharose CL-6B affinity chromatography.	Heparin	21-28	apolipoprotein E	Homo sapiens	0-4
17165023-0	2007	Studies on interactions of programmed cell death 5 (PDCD5) and its related peptides with heparin by capillary zone electrophoresis.	Heparin	89-96	programmed cell death 5	Homo sapiens	27-50
17196698-1	2007	Heparin conjugated amphiphilic block copolymer, Tetronic-PCL-heparin (TCH), was developed and its polymeric micelles (PMs) were prepared as an injectable vehicle for long-term delivery of bFGF, which is one of the heparin-binding growth factors (HBGF).	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	188-192
17196698-1	2007	Heparin conjugated amphiphilic block copolymer, Tetronic-PCL-heparin (TCH), was developed and its polymeric micelles (PMs) were prepared as an injectable vehicle for long-term delivery of bFGF, which is one of the heparin-binding growth factors (HBGF).	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	188-192
17196698-7	2007	The bFGF loading amount of TCH PMs was considerably higher than that of TC, caused by specific interactions between heparin and bFGF.	Heparin	116-123	fibroblast growth factor 2	Homo sapiens	4-8
17165023-4	2007	The changes in the signals of PDCD5 and PDCD5-related peptides were monitored by comparing the electropherograms of the mixtures containing PDCD5 and heparin and PDCD5-related peptides and heparin with that of PDCD5 or PDCD5-related peptides only.	Heparin	150-157	programmed cell death 5	Homo sapiens	30-35
17165023-4	2007	The changes in the signals of PDCD5 and PDCD5-related peptides were monitored by comparing the electropherograms of the mixtures containing PDCD5 and heparin and PDCD5-related peptides and heparin with that of PDCD5 or PDCD5-related peptides only.	Heparin	150-157	programmed cell death 5	Homo sapiens	40-45
17165023-4	2007	The changes in the signals of PDCD5 and PDCD5-related peptides were monitored by comparing the electropherograms of the mixtures containing PDCD5 and heparin and PDCD5-related peptides and heparin with that of PDCD5 or PDCD5-related peptides only.	Heparin	150-157	programmed cell death 5	Homo sapiens	40-45
17165023-4	2007	The changes in the signals of PDCD5 and PDCD5-related peptides were monitored by comparing the electropherograms of the mixtures containing PDCD5 and heparin and PDCD5-related peptides and heparin with that of PDCD5 or PDCD5-related peptides only.	Heparin	150-157	programmed cell death 5	Homo sapiens	40-45
17165023-4	2007	The changes in the signals of PDCD5 and PDCD5-related peptides were monitored by comparing the electropherograms of the mixtures containing PDCD5 and heparin and PDCD5-related peptides and heparin with that of PDCD5 or PDCD5-related peptides only.	Heparin	150-157	programmed cell death 5	Homo sapiens	40-45
17264724-2	2007	The purpose of this study was to determine whether a reduced dose of bivalirudin, added as an adjunct to heparin, would reduce thrombin generation and circulating markers of inflammatory system activation during CPB as effectively as full-dose bivalirudin, without adversely affecting postoperative hemostasis.	Heparin	105-112	coagulation factor II	Rattus norvegicus	127-135
17165023-0	2007	Studies on interactions of programmed cell death 5 (PDCD5) and its related peptides with heparin by capillary zone electrophoresis.	Heparin	89-96	programmed cell death 5	Homo sapiens	52-57
17165023-4	2007	The changes in the signals of PDCD5 and PDCD5-related peptides were monitored by comparing the electropherograms of the mixtures containing PDCD5 and heparin and PDCD5-related peptides and heparin with that of PDCD5 or PDCD5-related peptides only.	Heparin	150-157	programmed cell death 5	Homo sapiens	40-45
17165023-5	2007	The binding constant of the interaction between PDCD5 and heparin was calculated as 4.17 x 10(4) M(-1) by Scatchard analysis.	Heparin	58-65	programmed cell death 5	Homo sapiens	48-53
17165023-3	2007	Both qualitative and quantitative characterizations of the binding of PDCD5 and PDCD5-related peptides to heparin were determined.	Heparin	106-113	programmed cell death 5	Homo sapiens	70-75
17165023-6	2007	Our investigations show that it is possible to characterize the interaction between PDCD5 and heparin quantitatively and the interaction between PDCD5-related peptides and heparin qualitatively using CZE.	Heparin	94-101	programmed cell death 5	Homo sapiens	84-89
17165023-6	2007	Our investigations show that it is possible to characterize the interaction between PDCD5 and heparin quantitatively and the interaction between PDCD5-related peptides and heparin qualitatively using CZE.	Heparin	172-179	programmed cell death 5	Homo sapiens	145-150
17165023-3	2007	Both qualitative and quantitative characterizations of the binding of PDCD5 and PDCD5-related peptides to heparin were determined.	Heparin	106-113	programmed cell death 5	Homo sapiens	80-85
17252251-1	2007	Heparin-induced thrombocytopenia (HIT) represents a serious side effect caused by an atypical immune response to platelet factor 4 leading to platelet activation and thrombin formation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	166-174
17110602-5	2007	In vitro, ANGPTL3 inhibited the phospholipase activity of endothelial lipase (EL), which hydrolyzes HDL-PL and hence decreases plasma HDL levels, through a putative heparin-binding site in the N-terminal domain of ANGPTL3.	Heparin	165-172	angiopoietin-like 3	Mus musculus	10-17
17110602-5	2007	In vitro, ANGPTL3 inhibited the phospholipase activity of endothelial lipase (EL), which hydrolyzes HDL-PL and hence decreases plasma HDL levels, through a putative heparin-binding site in the N-terminal domain of ANGPTL3.	Heparin	165-172	angiopoietin-like 3	Mus musculus	214-221
17110602-6	2007	Post-heparin plasma in Angptl3-knockout mice had higher phospholipase activity than did that in wild-type mice, suggesting that the activity of endogenous EL is elevated in Angptl3-deficient mice.	Heparin	5-12	angiopoietin-like 3	Mus musculus	23-30
17296655-9	2007	TID heparin showed a trend toward a decrease in pulmonary embolism (PE) [BID, 1.5; vs TID, 0.5; p = 0.09] and in proximal DVT and PE (BID, 2.3; vs TID, 0.9; p = 0.05).	Heparin	4-11	BH3 interacting domain death agonist	Homo sapiens	73-76
17296655-9	2007	TID heparin showed a trend toward a decrease in pulmonary embolism (PE) [BID, 1.5; vs TID, 0.5; p = 0.09] and in proximal DVT and PE (BID, 2.3; vs TID, 0.9; p = 0.05).	Heparin	4-11	BH3 interacting domain death agonist	Homo sapiens	134-137
17296655-10	2007	The risk for major bleeding was significantly increased with TID heparin (BID, 0.35; vs TID, 0.96; p &lt; 0.001).	Heparin	65-72	BH3 interacting domain death agonist	Homo sapiens	74-77
17296655-11	2007	CONCLUSIONS: BID heparin dosing causes fewer major bleeding episodes, while TID dosing appears to offer somewhat better efficacy in preventing clinically relevant VTE events.	Heparin	17-24	BH3 interacting domain death agonist	Homo sapiens	13-16
17258117-2	2007	Since the discovery of heparin in the early twentieth century, significant advances have been made in the understanding of thrombin structure and function in coagulation system.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	123-131
17020882-6	2007	The addition of exogenous heparin, a widely used anticoagulant, reduced BMP2 signaling.	Heparin	26-33	bone morphogenetic protein 2	Mus musculus	72-76
17308051-5	2007	A PlGF-2/Flt-1-inhibiting peptide, binding peptide 1 (BP1), that binds Flt-1 at or near the heparin-binding site was identified and synthesized.	Heparin	92-99	placental growth factor	Homo sapiens	2-8
17308051-5	2007	A PlGF-2/Flt-1-inhibiting peptide, binding peptide 1 (BP1), that binds Flt-1 at or near the heparin-binding site was identified and synthesized.	Heparin	92-99	fms related receptor tyrosine kinase 1	Homo sapiens	9-14
17308051-5	2007	A PlGF-2/Flt-1-inhibiting peptide, binding peptide 1 (BP1), that binds Flt-1 at or near the heparin-binding site was identified and synthesized.	Heparin	92-99	fms related receptor tyrosine kinase 1	Homo sapiens	71-76
17257225-0	2007	Quantification of S100A12 (EN-RAGE) in blood varies with sampling method, calcium and heparin.	Heparin	86-93	S100 calcium binding protein A12	Homo sapiens	18-25
17257225-0	2007	Quantification of S100A12 (EN-RAGE) in blood varies with sampling method, calcium and heparin.	Heparin	86-93	S100 calcium binding protein A12	Homo sapiens	27-34
17121850-6	2007	Heparin and PI-88, two HPR1 inhibitors, were able to increase cell surface HS levels in PANC-1 cells in a dose-dependent manner.	Heparin	0-7	heparanase	Homo sapiens	23-27
17230619-0	2007	Effect of non-anticoagulant N-desulfated heparin on expression of vascular endothelial growth factor, angiogenesis and metastasis of orthotopic implantation of human gastric carcinoma.	Heparin	41-48	vascular endothelial growth factor A	Homo sapiens	66-100
17696566-1	2007	Direct thrombin inhibitors have several potential advantages over indirect thrombin inhibitors such as heparin.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	75-83
17069767-8	2007	Heparin, an inhibitor for HB-EGF, suppressed PAR1-mediated PGE(2) formation and persistent ERK phosphorylation.	Heparin	0-7	heparin-binding EGF-like growth factor	Rattus norvegicus	26-32
17352253-0	2007	Modulatory effects of heparin on cellular accumulation and cytotoxicity of doxorubicin in MRP1-overexpressing HL60/doxo cells.	Heparin	22-29	ATP binding cassette subfamily C member 1	Homo sapiens	90-94
17352253-5	2007	MATERIALS AND METHODS: The human leukemic doxorubicin-resistant cell line (HL60/doxo), which overexpresses the MRP1 protein was treated with UFH alone or in combination with three different concentrations of doxo.	Heparin	141-144	ATP binding cassette subfamily C member 1	Homo sapiens	111-115
17352253-10	2007	These findings suggest a potential clinical application of heparin as an adjuvant to overcome MRP1-mediated drug resistance in cancer patients.	Heparin	59-66	ATP binding cassette subfamily C member 1	Homo sapiens	94-98
16963119-2	2007	Heparin-functionalized hydrogels supported hMSC viability, as quantified through live/dead imaging, and induced osteogenic differentiation, as measured by increased alkaline phosphatase (ALP) production and osteopontin (OPN) and collagen I (COL I) gene expression over the 5-week study.	Heparin	0-7	alkaline phosphatase, placental	Homo sapiens	165-185
16963119-2	2007	Heparin-functionalized hydrogels supported hMSC viability, as quantified through live/dead imaging, and induced osteogenic differentiation, as measured by increased alkaline phosphatase (ALP) production and osteopontin (OPN) and collagen I (COL I) gene expression over the 5-week study.	Heparin	0-7	alkaline phosphatase, placental	Homo sapiens	187-190
17069767-8	2007	Heparin, an inhibitor for HB-EGF, suppressed PAR1-mediated PGE(2) formation and persistent ERK phosphorylation.	Heparin	0-7	Eph receptor B1	Rattus norvegicus	91-94
17179829-10	2007	The 50% inhibitory concentrations of low-molecular-weight heparin against recalcified thrombin generation are 0.01, 0.025, or 0.035 IU/ml for plasma supplemented with 0, 0.1, or 1 g/l Hb-MP, respectively.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	86-94
17187457-0	2007	Direct thrombin inhibition during percutaneous coronary intervention in patients with heparin-induced thrombocytopenia.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	7-15
17699388-6	2007	Is the antiproteinuric effect of heparins due to its interference with the renin-angiotensin-aldosterone system?	Heparin	33-41	renin	Homo sapiens	75-80
17438357-0	2007	Role of heparin on TNF-alpha and IL-6 levels in liver regeneration after partial hepatic resection.	Heparin	8-15	tumor necrosis factor	Rattus norvegicus	19-28
17438357-0	2007	Role of heparin on TNF-alpha and IL-6 levels in liver regeneration after partial hepatic resection.	Heparin	8-15	interleukin 6	Rattus norvegicus	33-37
17438357-1	2007	OBJECTIVES: The aim of this study was to investigate the effect of heparin on TNF-alpha and interleukin (IL)-6 levels and the complement system in liver regeneration in a murine model.	Heparin	67-74	tumor necrosis factor	Mus musculus	78-87
17438357-1	2007	OBJECTIVES: The aim of this study was to investigate the effect of heparin on TNF-alpha and interleukin (IL)-6 levels and the complement system in liver regeneration in a murine model.	Heparin	67-74	interleukin 6	Mus musculus	92-110
17167048-6	2007	In comparison, UFH or ATH heparin binding (evidence of a template mechanism) was only observed with thrombin, tissue factor, FIXa and FXIa.	Heparin	15-18	coagulation factor II, thrombin	Homo sapiens	100-108
17167048-6	2007	In comparison, UFH or ATH heparin binding (evidence of a template mechanism) was only observed with thrombin, tissue factor, FIXa and FXIa.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	100-108
17245762-8	2007	Our data indicate that Randox full-range CRP measurements using an immunoturbidimetry assay on Olympus systems perform as well for routine diagnostics as other high-sensitivity applications using serum or heparin plasma.	Heparin	205-212	C-reactive protein	Homo sapiens	41-44
17873298-0	2007	Heparin inhibits NF-kappaB activation and increases cell death in cerebral endothelial cells after oxygen-glucose deprivation.	Heparin	0-7	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	17-26
17873298-5	2007	We investigated the effect of heparin on NF-kappaB activation and cell death following oxygen-glucose deprivation (OGD), an experimental model of AIS.	Heparin	30-37	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	41-50
17873298-7	2007	We examined the effect of heparin on OGD-induced NF-kappaB activation and its mechanism of action, using electrophoretic mobility shift assays, reporter gene analysis, real-time RT-PCR, Western blot analysis, and confocal microscopy.	Heparin	26-33	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	49-58
17192873-3	2007	In both the literature and in our cases, platelet count, prothrombin time (PT), and activated partial thromboplastin time (aPTT) in cases of heparin administration showed significant changes (P &lt; 0.05), especially after right lobectomy.	Heparin	141-148	coagulation factor II, thrombin	Homo sapiens	57-68
17873298-9	2007	Heparin inhibited both tumor necrosis factor alpha- and OGD-induced NF-kappaB activation.	Heparin	0-7	tumor necrosis factor	Mus musculus	23-50
17873298-9	2007	Heparin inhibited both tumor necrosis factor alpha- and OGD-induced NF-kappaB activation.	Heparin	0-7	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	68-77
17873298-11	2007	Heparin did not affect the nuclear translocation of NF-kappaB, but instead inhibited the DNA binding of NF-kappaB in the nucleus.	Heparin	0-7	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	104-113
17873298-13	2007	Besides producing an anticoagulation effect, heparin also inhibits NF-kappaB activation, resulting in increased susceptibility to OGD-induced cell death.	Heparin	45-52	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	67-76
17041566-10	2007	Importantly, un-fractionated as well as low molecular weight heparin (enoxaparin), which exhibit a strong inhibitory activity towards heparanase, have proven efficacious in ulcerative colitis and Crohn"s disease patients, suggesting that heparanase is actively involved in these pathologies and thus may be considered as a target for the development of anti-inflammatory therapies.	Heparin	61-68	heparanase	Homo sapiens	134-144
17041566-10	2007	Importantly, un-fractionated as well as low molecular weight heparin (enoxaparin), which exhibit a strong inhibitory activity towards heparanase, have proven efficacious in ulcerative colitis and Crohn"s disease patients, suggesting that heparanase is actively involved in these pathologies and thus may be considered as a target for the development of anti-inflammatory therapies.	Heparin	61-68	heparanase	Homo sapiens	238-248
16712904-6	2007	CONCLUSION: In our in vitro study adding either melagatran, UH or LMWH augmented the capacity of rhAPC to suppress thrombin generation in human plasma.	Heparin	60-62	coagulation factor II, thrombin	Homo sapiens	115-123
17917621-3	2007	UFH was combined with aspirin to suppress thrombin propagation and fibrin formation in patients presenting with acute coronary syndromes (ACS) or patients undergoing percutaneous coronary intervention (PCI).	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	42-50
18023703-0	2007	Heparin attenuates metastasis mainly due to inhibition of P- and L-selectin, but non-anticoagulant heparins can have additional effects.	Heparin	0-7	selectin, lymphocyte	Mus musculus	65-75
16515805-4	2007	This assay was used to distinguish the anti-fXa activity of different molecular weight heparins from their anti-thrombin activity in clotting assays which were initiated by the triggers of either the extrinsic or intrinsic coagulation pathway.	Heparin	87-95	coagulation factor II, thrombin	Homo sapiens	112-120
17222891-3	2007	Heparin was the most potent inhibitor of the thrombin-induced platelet aggregation in platelet-rich plasma (PRP), whereas the oversulfated DS had a higher potency than the native DS.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	45-53
16978685-9	2007	Unlike UFH, clot-bound thrombin is readily inhibited by ATH and, at similar antithrombotic efficacy, the ATH has improved bleeding profiles compared to heparins.	Heparin	152-160	coagulation factor II, thrombin	Homo sapiens	23-31
17512574-9	2007	AT significantly prolonged times until thrombotic vessel occlusion in a dose-dependent manner and more effectively than heparin (p&lt;0.05 vs. NaCl and heparin).	Heparin	152-159	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-2
18023704-6	2007	Studies on relationships between structure and the heparanase-inhibiting activity of nonanticogulant heparins systematically differing in their O-sulfation patterns, degrees of N-acetylation, and glycol-splitting of nonsulfated uronic acid residues, have permitted to select effective inhibitors of the enzymatic activity of heparanase.	Heparin	101-109	heparanase	Homo sapiens	51-61
18023703-8	2007	However, a non-anticoagulant derivative of heparin with P- and L-selectin inhibitory properties reduced metastasis to similar levels as observed in PL -/- mice.	Heparin	43-50	selectin, lymphocyte	Mus musculus	63-73
18023704-7	2007	N-acetylated, glycol-split heparins emerged as highly effective and specific inhibitors of heparanase and tumor growth and metastasis.	Heparin	27-35	heparanase	Homo sapiens	91-101
18023704-13	2007	In addition, pro-heparanase can reverse the anti-coagulant effect of unfractionated heparin and the Factor Xa inhibitory activity of low molecular weight heparin (LMWH).	Heparin	84-91	heparanase	Homo sapiens	17-27
18023703-9	2007	The virtual elimination of metastasis by a single treatment with a modified heparin without anticoagulant activity strongly suggests that heparin primarily reduces metastatic disease by inhibiting P- and L-selectin interactions.	Heparin	76-83	selectin, lymphocyte	Mus musculus	204-214
18023704-13	2007	In addition, pro-heparanase can reverse the anti-coagulant effect of unfractionated heparin and the Factor Xa inhibitory activity of low molecular weight heparin (LMWH).	Heparin	154-161	heparanase	Homo sapiens	17-27
18023703-9	2007	The virtual elimination of metastasis by a single treatment with a modified heparin without anticoagulant activity strongly suggests that heparin primarily reduces metastatic disease by inhibiting P- and L-selectin interactions.	Heparin	138-145	selectin, lymphocyte	Mus musculus	204-214
16950508-7	2006	The HA hydrogels containing Ang-1+VEGF produced the greatest angiogenic response of any treatment group tested at day 14 (NI=7.44 in the absence of Hp and 4.67 in its presence, where NI is a neovascularization index).	Heparin	148-150	angiopoietin 1	Mus musculus	28-38
17040907-3	2006	Cleaved and latent but not native forms of antithrombin blocked the formation of FGF-2-FGF receptor-1 ectodomain-heparin ternary complexes, and the dimerization of these complexes in solution and similarly inhibited the formation of FGF-2-heparin binary complexes and their dimerization.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	81-101
17040907-3	2006	Cleaved and latent but not native forms of antithrombin blocked the formation of FGF-2-FGF receptor-1 ectodomain-heparin ternary complexes, and the dimerization of these complexes in solution and similarly inhibited the formation of FGF-2-heparin binary complexes and their dimerization.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	81-86
17126170-2	2006	Thrombin is the key enzyme in the thrombotic portion of the defense reaction and is only partially suppressed by heparin.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	0-8
16941589-1	2006	Heparin-immobilized porous biodegradable scaffolds were fabricated to release basic fibroblast growth factor (bFGF) in a sustained manner.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	78-108
16941589-1	2006	Heparin-immobilized porous biodegradable scaffolds were fabricated to release basic fibroblast growth factor (bFGF) in a sustained manner.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	110-114
16941589-3	2006	Sustained release of bFGF was successfully achieved for over 20 days due to high affinity of bFGF onto the immobilized heparin.	Heparin	119-126	fibroblast growth factor 2	Homo sapiens	21-25
16941589-3	2006	Sustained release of bFGF was successfully achieved for over 20 days due to high affinity of bFGF onto the immobilized heparin.	Heparin	119-126	fibroblast growth factor 2	Homo sapiens	93-97
16941589-6	2006	When heparin-immobilized scaffolds loaded with bFGF were implanted subcutaneously in vivo, they effectively induced the formation of blood vessels in the vicinity of the implant site.	Heparin	5-12	fibroblast growth factor 2	Homo sapiens	47-51
16914317-11	2006	This work puts forward a novel, non-heparin structure, which may be exploited for the design of potent, dual action inhibitors of coagulation through combinatorial virtual screening on a library of DHP oligomers.	Heparin	36-43	dihydropyrimidinase	Homo sapiens	198-201
17066397-8	2006	These heparin chips aided in the discovery of novel, sulfated sequences that bind FGF, and in the determination of the structural requirements needed for recognition by using picomoles of protein on a single slide.	Heparin	6-13	fibroblast growth factor 1	Homo sapiens	82-85
17139378-1	2006	Low-molecular-weight heparins (LMWH) exhibit potent anticoagulant efficacy via their plasmatic effects on thrombin and factor Xa.	Heparin	21-29	coagulation factor II	Mus musculus	106-114
16766579-4	2006	Heparin was used because it participates in FGF-1 signaling.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	44-49
16679398-4	2006	Heparin and bFGF increased constitutive TER in cultured pHUVEC, and heparin mediated additional increases in constitutive TER in pHUVEC supplemented with bFGF.	Heparin	68-75	fibroblast growth factor 2	Homo sapiens	154-158
16679398-8	2006	Thrombin-mediated barrier dysfunction was attenuated in pHUVEC conditioned in EGF in the presence or absence of heparin.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	0-8
16679398-9	2006	Thrombin-mediated barrier dysfunction was also attenuated when monolayers were exposed to low concentrations of heparin and further attenuated in the presence of bFGF.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	0-8
16982604-4	2006	Evidence suggests that the effect of ECM fibronectin on cell function is mediated in part by a matricryptic heparin-binding site within the first III1 repeat (FNIII1).	Heparin	108-115	fibronectin 1	Homo sapiens	41-52
17073444-10	2006	For oligosaccharides of 14 and 20 nm, two types of complexes are formed with one IFN-gamma and one or two heparin molecules.	Heparin	106-113	interferon gamma	Homo sapiens	81-90
17071598-0	2006	Bovine lactoferricin inhibits basic fibroblast growth factor- and vascular endothelial growth factor165-induced angiogenesis by competing for heparin-like binding sites on endothelial cells.	Heparin	142-149	fibroblast growth factor 2	Bos taurus	30-60
16794256-6	2006	Heparin at low concentrations (5 microg/ml) or desulfated heparin at high concentrations (500 microg/ml) enhanced the effects of FGF-2 and -7, while high heparin concentrations (500 microg/ml) were inhibitory.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	129-134
16794256-6	2006	Heparin at low concentrations (5 microg/ml) or desulfated heparin at high concentrations (500 microg/ml) enhanced the effects of FGF-2 and -7, while high heparin concentrations (500 microg/ml) were inhibitory.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	129-134
16794256-7	2006	In contrast, SP-B mRNA abundance was increased by heparin in a dose- and sulfation-dependent manner when used in combination with FGF-1.	Heparin	50-57	fibroblast growth factor 1	Homo sapiens	130-135
16794256-8	2006	SP-C and AQP-5 mRNA levels were increased by heparin alone in a dose- and sulfation-dependent manner, while all FGFs lacked effect on SP-C or AQP-5 mRNA levels.	Heparin	45-52	surfactant protein C	Homo sapiens	0-4
17071598-7	2006	Rather, LfcinB complexed with heparin-like structures on the HUVEC surface that are involved in the binding of bFGF and VEGF165 to their respective receptors, thereby preventing receptor-stimulated angiogenesis.	Heparin	30-37	fibroblast growth factor 2	Bos taurus	111-115
17046999-8	2006	Binding of exogenous thrombospondin-1 to these structures, to purified versican and to its G1 domain is potently inhibited by heparin.	Heparin	126-133	thrombospondin 1	Homo sapiens	21-37
17102649-2	2006	Here the 50% inhibitory concentration (IC(50)) values of heparin and LMWHs on extrinsic thrombin generation are determined.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	88-96
17146553-2	2006	A heparin-like substance with an anticoagulant activity equivalent to 10% of mammalian heparin and about 5% as potent as the mammalian counterpart for the inhibition of thrombin by antithrombin was isolated from the oocyte test cells.	Heparin	2-9	coagulation factor II, thrombin	Homo sapiens	169-177
17008606-5	2006	Mutation of the heparin-binding residues on FnIII(13-14) abolished VEGF binding, and peptides corresponding to the heparin-binding sequences in FnIII(13-14) inhibited VEGF binding to Fn.	Heparin	16-23	vascular endothelial growth factor A	Homo sapiens	67-71
16930539-6	2006	The T48 aptamer but not a random control aptamer antagonises CCL1 function in a dose-dependent fashion in both heparin binding and chemotaxis assays.	Heparin	111-118	C-C motif chemokine ligand 1	Homo sapiens	61-65
17008606-5	2006	Mutation of the heparin-binding residues on FnIII(13-14) abolished VEGF binding, and peptides corresponding to the heparin-binding sequences in FnIII(13-14) inhibited VEGF binding to Fn.	Heparin	16-23	fibronectin 1	Homo sapiens	44-46
17008606-5	2006	Mutation of the heparin-binding residues on FnIII(13-14) abolished VEGF binding, and peptides corresponding to the heparin-binding sequences in FnIII(13-14) inhibited VEGF binding to Fn.	Heparin	115-122	vascular endothelial growth factor A	Homo sapiens	167-171
17004727-0	2006	Heparin derivatives as inhibitors of BACE-1, the Alzheimer"s beta-secretase, with reduced activity against factor Xa and other proteases.	Heparin	0-7	beta-secretase 1	Homo sapiens	37-43
16919088-2	2006	Regular rinsing of the CVAD with heparin, according to a standard protocol, resulted in systemic anticoagulation, as demonstrated by prolonged thrombin time and therapeutic anti-Xa levels.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	143-151
16996870-0	2006	Effect of heparin on blood vascular endothelial growth factor levels in patients with ST-elevation acute myocardial infarction undergoing primary percutaneous coronary intervention.	Heparin	10-17	vascular endothelial growth factor A	Homo sapiens	27-61
16996870-1	2006	It has been demonstrated that high blood vascular endothelial growth factor (VEGF) levels in patients with myocardial infarction decrease rapidly after reperfusion, possibly in response to heparin administration.	Heparin	189-196	vascular endothelial growth factor A	Homo sapiens	41-75
16996870-1	2006	It has been demonstrated that high blood vascular endothelial growth factor (VEGF) levels in patients with myocardial infarction decrease rapidly after reperfusion, possibly in response to heparin administration.	Heparin	189-196	vascular endothelial growth factor A	Homo sapiens	77-81
16996870-5	2006	To determine whether heparin could decrease VEGF concentration by sequestering VEGF in the endothelium, a fixed dose of recombinant VEGF was incubated for 40 minutes with EA.hy926 endothelial cells in vitro.	Heparin	21-28	vascular endothelial growth factor A	Homo sapiens	44-48
16996870-5	2006	To determine whether heparin could decrease VEGF concentration by sequestering VEGF in the endothelium, a fixed dose of recombinant VEGF was incubated for 40 minutes with EA.hy926 endothelial cells in vitro.	Heparin	21-28	vascular endothelial growth factor A	Homo sapiens	79-83
16996870-5	2006	To determine whether heparin could decrease VEGF concentration by sequestering VEGF in the endothelium, a fixed dose of recombinant VEGF was incubated for 40 minutes with EA.hy926 endothelial cells in vitro.	Heparin	21-28	vascular endothelial growth factor A	Homo sapiens	79-83
16996870-6	2006	Recovery of VEGF from medium after culture was decreased by up to 15% with increasing doses of heparin.	Heparin	95-102	vascular endothelial growth factor A	Homo sapiens	12-16
16996870-8	2006	In conclusion, these results suggest that a rapid decrease in blood VEGF after PCI may be related to the administration of heparin, which binds simultaneously to VEGF and endothelial cells.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	68-72
16996870-8	2006	In conclusion, these results suggest that a rapid decrease in blood VEGF after PCI may be related to the administration of heparin, which binds simultaneously to VEGF and endothelial cells.	Heparin	123-130	vascular endothelial growth factor A	Homo sapiens	162-166
16987243-0	2006	Sequential phosphorylation of tau protein by cAMP-dependent protein kinase and SAPK4/p38delta or JNK2 in the presence of heparin generates the AT100 epitope.	Heparin	121-128	mitogen-activated protein kinase 13	Homo sapiens	79-84
16987243-0	2006	Sequential phosphorylation of tau protein by cAMP-dependent protein kinase and SAPK4/p38delta or JNK2 in the presence of heparin generates the AT100 epitope.	Heparin	121-128	mitogen-activated protein kinase 13	Homo sapiens	85-93
16987243-0	2006	Sequential phosphorylation of tau protein by cAMP-dependent protein kinase and SAPK4/p38delta or JNK2 in the presence of heparin generates the AT100 epitope.	Heparin	121-128	mitogen-activated protein kinase 9	Homo sapiens	97-101
16824188-6	2006	This Fg/VWF-independent aggregation was blocked by thrombin inhibitors (heparin, hirudin, PPACK), and thrombin or thrombin receptor activation peptide (AYPGKF-NH(2)) induced aggregation of gel-filtered Fg/VWF(-/-) platelets in 1 mm Ca(2+) PIPES buffer.	Heparin	72-79	coagulation factor II	Mus musculus	51-59
16904641-5	2006	The growth-modulating effects of heparin and internalized heparin were dependent on cell surface HSGAGs, PI3K, and Erk/Mek.	Heparin	33-40	mitogen-activated protein kinase 1	Homo sapiens	115-118
16904641-5	2006	The growth-modulating effects of heparin and internalized heparin were dependent on cell surface HSGAGs, PI3K, and Erk/Mek.	Heparin	33-40	mitogen-activated protein kinase kinase 7	Homo sapiens	119-122
16904641-5	2006	The growth-modulating effects of heparin and internalized heparin were dependent on cell surface HSGAGs, PI3K, and Erk/Mek.	Heparin	58-65	mitogen-activated protein kinase 1	Homo sapiens	115-118
16904641-5	2006	The growth-modulating effects of heparin and internalized heparin were dependent on cell surface HSGAGs, PI3K, and Erk/Mek.	Heparin	58-65	mitogen-activated protein kinase kinase 7	Homo sapiens	119-122
16797961-9	2006	Finally, our initial work focused on developing non-antibody based enhancement agents using bovine serum albumin-heparin conjugates covalently bound to polystyrene microspheres is presented for the cytokine, tumor necrosis factor-alpha (TNF-alpha).	Heparin	113-120	tumor necrosis factor	Homo sapiens	208-235
16797961-9	2006	Finally, our initial work focused on developing non-antibody based enhancement agents using bovine serum albumin-heparin conjugates covalently bound to polystyrene microspheres is presented for the cytokine, tumor necrosis factor-alpha (TNF-alpha).	Heparin	113-120	tumor necrosis factor	Homo sapiens	237-246
16806456-6	2006	As little as 0.03% Hp in the gels reduced the released VEGF fraction from 30% to 21%, while 3% Hp reduced it to 19%.	Heparin	19-21	vascular endothelial growth factor A	Homo sapiens	55-59
16934788-5	2006	Cardiac LPL activity was determined by retrogradely perfusing the hearts with heparin.	Heparin	78-85	lipoprotein lipase	Rattus norvegicus	8-11
16934788-7	2006	Cardiac myocytes were also isolated, and heparin-releasable LPL activity was measured.	Heparin	41-48	lipoprotein lipase	Rattus norvegicus	60-63
16934788-10	2006	Compared to control (CON) hearts, there was a substantial decrease in heparin-releasable LPL activity at the vascular lumen following 3 h of IL infusion, an effect unrelated to changes in gene and protein expression or whole-body insulin resistance.	Heparin	70-77	lipoprotein lipase	Rattus norvegicus	89-92
16995857-3	2006	The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments.	Heparin	39-46	fibroblast growth factor 1	Homo sapiens	132-135
16995857-3	2006	The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments.	Heparin	39-46	fibroblast growth factor 1	Homo sapiens	245-250
16995857-3	2006	The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments.	Heparin	124-131	fibroblast growth factor 1	Homo sapiens	132-135
16995857-3	2006	The use of this well defined synthetic heparin analogue has allowed us to perform a detailed NMR structural analysis of the heparin-FGF interaction, overcoming the limitations of NMR to deal with the high molecular mass and heterogeneity of the FGF-1 oligomers formed in the presence of natural heparin fragments.	Heparin	124-131	fibroblast growth factor 1	Homo sapiens	245-250
16995857-4	2006	Our results confirm that glycosaminoglycans induced FGF-1 dimerization either in a cis or trans disposition with respect to the heparin chain is not an absolute requirement for biological activity.	Heparin	128-135	fibroblast growth factor 1	Homo sapiens	52-57
16982928-6	2006	Finally, simultaneous cell incubation with the polyanion molecules, poly-L-glutamic acid or heparin, restored MMP-1 gene expression but incompletely inhibited MBP- and EPO-induced transcriptional effects as well as endothelin-1 and PDGF-AB release, suggesting that cationic proteins act partially through their cationic charge.	Heparin	92-99	eosinophil peroxidase	Homo sapiens	168-171
16982928-6	2006	Finally, simultaneous cell incubation with the polyanion molecules, poly-L-glutamic acid or heparin, restored MMP-1 gene expression but incompletely inhibited MBP- and EPO-induced transcriptional effects as well as endothelin-1 and PDGF-AB release, suggesting that cationic proteins act partially through their cationic charge.	Heparin	92-99	endothelin 1	Homo sapiens	215-227
16940188-0	2006	Heparin displaces interferon-gamma-inducible chemokines (IP-10, I-TAC, and Mig) sequestered in the vasculature and inhibits the transendothelial migration and arterial recruitment of T cells.	Heparin	0-7	C-X-C motif chemokine ligand 9	Homo sapiens	75-78
16940188-1	2006	BACKGROUND: Heparin, used clinically as an anticoagulant, also has antiinflammatory properties and has been described to inhibit interferon (IFN)-gamma responses in endothelial cells.	Heparin	12-19	interferon gamma	Homo sapiens	129-151
16940188-2	2006	We investigated the effects of heparin on the IFN-gamma-inducible chemokines IP-10/CXCL10, I-TAC/CXCL11, and Mig/CXCL9, which play important roles in the vascular recruitment of IFN-gamma-producing Th1 cells through interactions with their cognate receptor, CXCR3.	Heparin	31-38	interferon gamma	Homo sapiens	46-55
16940188-4	2006	Plasma levels of IP-10, I-TAC, and Mig increased immediately after heparin administration and diminished promptly after heparin antagonism with protamine.	Heparin	67-74	C-X-C motif chemokine ligand 9	Homo sapiens	35-38
16940188-4	2006	Plasma levels of IP-10, I-TAC, and Mig increased immediately after heparin administration and diminished promptly after heparin antagonism with protamine.	Heparin	120-127	C-X-C motif chemokine ligand 9	Homo sapiens	35-38
16940188-6	2006	We confirmed previous reports that heparin inhibits the IFN-gamma-dependent production of CXCR3 chemokine ligands using atherosclerotic coronary arteries in organ culture.	Heparin	35-42	interferon gamma	Homo sapiens	56-65
16940188-9	2006	CONCLUSIONS: Besides inhibiting IFN-gamma responses, heparin has further immunomodulatory effects by competing for binding with IP-10, I-TAC, and Mig on endothelial cells.	Heparin	53-60	interferon gamma	Homo sapiens	32-41
16940188-9	2006	CONCLUSIONS: Besides inhibiting IFN-gamma responses, heparin has further immunomodulatory effects by competing for binding with IP-10, I-TAC, and Mig on endothelial cells.	Heparin	53-60	C-X-C motif chemokine ligand 9	Homo sapiens	146-149
16820973-2	2006	In the present study, we investigated the biological potency of heparin-binding domain (HBD) of FN spanning the twelfth and fourteenth type III domains.	Heparin	64-71	fibronectin 1	Homo sapiens	96-98
16936199-6	2006	Furthermore, we show that low-molecular weight heparin (LMWH) can bind RAGE at a mean equilibrium dissociation constant (K(d)) value of approximately 17 nmol/l and act as an antagonist to RAGE.	Heparin	47-54	advanced glycosylation end product-specific receptor	Mus musculus	71-75
16936199-6	2006	Furthermore, we show that low-molecular weight heparin (LMWH) can bind RAGE at a mean equilibrium dissociation constant (K(d)) value of approximately 17 nmol/l and act as an antagonist to RAGE.	Heparin	47-54	advanced glycosylation end product-specific receptor	Mus musculus	188-192
16765093-2	2006	Here we demonstrate that an anticoagulant aptamer-antidote pair targeting factor IXa can replace heparin and protamine in a porcine CPB model and also limit the adverse effects on thrombin generation, inflammation, and cardiac physiology associated with heparin and protamine use.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	180-188
16765093-2	2006	Here we demonstrate that an anticoagulant aptamer-antidote pair targeting factor IXa can replace heparin and protamine in a porcine CPB model and also limit the adverse effects on thrombin generation, inflammation, and cardiac physiology associated with heparin and protamine use.	Heparin	254-261	coagulation factor II, thrombin	Homo sapiens	180-188
16945147-8	2006	Competition for this uptake with an LRP ligand-binding antagonist had little or no effect, whereas co-incubation with heparin abolished apoE-VLDL internalization.	Heparin	118-125	apolipoprotein E	Homo sapiens	136-140
16945153-0	2006	Heparin (GAG-hed) inhibits LCR activity of human papillomavirus type 18 by decreasing AP1 binding.	Heparin	0-7	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	86-89
16945153-5	2006	Glycosaminoglycans (GAGs), such as heparin, can inhibit tumour growth; they have also shown antiviral effects and inhibition of AP1 transcriptional activity.	Heparin	35-42	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	128-131
16922507-0	2006	Heparin-mediated conformational changes in fibronectin expose vascular endothelial growth factor binding sites.	Heparin	0-7	fibronectin 1	Homo sapiens	43-54
16922507-0	2006	Heparin-mediated conformational changes in fibronectin expose vascular endothelial growth factor binding sites.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	62-96
16720575-8	2006	Heparin was, however, found to increase Erk1/2 activation in both a time- and dose-dependent manner.	Heparin	0-7	mitogen-activated protein kinase 3	Homo sapiens	40-46
16922507-4	2006	Atomic force microscopy studies revealed that heparin and hydrophilic substrates promoted the extended conformation of fibronectin, leading to increased VEGF binding.	Heparin	46-53	fibronectin 1	Homo sapiens	119-130
16922507-4	2006	Atomic force microscopy studies revealed that heparin and hydrophilic substrates promoted the extended conformation of fibronectin, leading to increased VEGF binding.	Heparin	46-53	vascular endothelial growth factor A	Homo sapiens	153-157
16922507-5	2006	The ability of heparin to enhance VEGF binding to fibronectin was dependent on the chemical composition and chain length of heparin, since long (&gt;22 saccharides) heparin chains with sulfation on the 6-O and N positions of glucosamine units were required for full activity.	Heparin	15-22	vascular endothelial growth factor A	Homo sapiens	34-38
16922507-5	2006	The ability of heparin to enhance VEGF binding to fibronectin was dependent on the chemical composition and chain length of heparin, since long (&gt;22 saccharides) heparin chains with sulfation on the 6-O and N positions of glucosamine units were required for full activity.	Heparin	15-22	fibronectin 1	Homo sapiens	50-61
16922507-5	2006	The ability of heparin to enhance VEGF binding to fibronectin was dependent on the chemical composition and chain length of heparin, since long (&gt;22 saccharides) heparin chains with sulfation on the 6-O and N positions of glucosamine units were required for full activity.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	34-38
16922507-5	2006	The ability of heparin to enhance VEGF binding to fibronectin was dependent on the chemical composition and chain length of heparin, since long (&gt;22 saccharides) heparin chains with sulfation on the 6-O and N positions of glucosamine units were required for full activity.	Heparin	124-131	fibronectin 1	Homo sapiens	50-61
16922507-5	2006	The ability of heparin to enhance VEGF binding to fibronectin was dependent on the chemical composition and chain length of heparin, since long (&gt;22 saccharides) heparin chains with sulfation on the 6-O and N positions of glucosamine units were required for full activity.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	34-38
16922507-5	2006	The ability of heparin to enhance VEGF binding to fibronectin was dependent on the chemical composition and chain length of heparin, since long (&gt;22 saccharides) heparin chains with sulfation on the 6-O and N positions of glucosamine units were required for full activity.	Heparin	124-131	fibronectin 1	Homo sapiens	50-61
16922507-6	2006	Treatment of the complex endothelial extracellular matrix with heparin also increased VEGF binding, suggesting that heparin/heparan sulfate might regulate VEGF interactions within the extracellular matrix by controlling the structure and organization of fibronectin matrices.	Heparin	63-70	vascular endothelial growth factor A	Homo sapiens	86-90
16922507-6	2006	Treatment of the complex endothelial extracellular matrix with heparin also increased VEGF binding, suggesting that heparin/heparan sulfate might regulate VEGF interactions within the extracellular matrix by controlling the structure and organization of fibronectin matrices.	Heparin	63-70	vascular endothelial growth factor A	Homo sapiens	155-159
16922507-6	2006	Treatment of the complex endothelial extracellular matrix with heparin also increased VEGF binding, suggesting that heparin/heparan sulfate might regulate VEGF interactions within the extracellular matrix by controlling the structure and organization of fibronectin matrices.	Heparin	63-70	fibronectin 1	Homo sapiens	254-265
16922507-6	2006	Treatment of the complex endothelial extracellular matrix with heparin also increased VEGF binding, suggesting that heparin/heparan sulfate might regulate VEGF interactions within the extracellular matrix by controlling the structure and organization of fibronectin matrices.	Heparin	116-123	vascular endothelial growth factor A	Homo sapiens	86-90
16922507-6	2006	Treatment of the complex endothelial extracellular matrix with heparin also increased VEGF binding, suggesting that heparin/heparan sulfate might regulate VEGF interactions within the extracellular matrix by controlling the structure and organization of fibronectin matrices.	Heparin	116-123	vascular endothelial growth factor A	Homo sapiens	155-159
16922507-6	2006	Treatment of the complex endothelial extracellular matrix with heparin also increased VEGF binding, suggesting that heparin/heparan sulfate might regulate VEGF interactions within the extracellular matrix by controlling the structure and organization of fibronectin matrices.	Heparin	116-123	fibronectin 1	Homo sapiens	254-265
16845256-0	2006	Greater inhibitory effects of bivalirudin compared with unfractionated heparin plus eptifibitide on thrombin-induced platelet activation.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	100-108
16839836-3	2006	Thus, we assessed the effect of a pronounced increase in circulating FFA levels induced by infusion of lipid/heparin on ACTH and cortisol secretion in young men.	Heparin	109-116	proopiomelanocortin	Homo sapiens	120-124
16720575-0	2006	Heparin synergistically enhances interleukin-11 signaling through up-regulation of the MAPK pathway.	Heparin	0-7	mitogen-activated protein kinase 3	Homo sapiens	87-91
16720575-2	2006	Furthermore, we found that, although heparin alone has no effect, it is able to synergistically enhance Interleukin-11 (IL-11)-induced signal transducer and activator of transcription 3 (STAT3) activation and thus increase osteoclast formation in vitro.	Heparin	37-44	signal transducer and activator of transcription 3	Homo sapiens	135-185
16720575-2	2006	Furthermore, we found that, although heparin alone has no effect, it is able to synergistically enhance Interleukin-11 (IL-11)-induced signal transducer and activator of transcription 3 (STAT3) activation and thus increase osteoclast formation in vitro.	Heparin	37-44	signal transducer and activator of transcription 3	Homo sapiens	187-192
16720575-5	2006	In contrast, PD098059, a MAPK kinase inhibitor, completely abolished the synergy between heparin and IL-11.	Heparin	89-96	mitogen-activated protein kinase 3	Homo sapiens	25-29
16720575-6	2006	In an attempt to resolve the mechanism by which this was occurring, we examined the effect of heparin on STAT3 Ser-727 phosphorylation and extracellular signal-regulated kinases 1 and 2 (Erk1/2) activation, either in the presence or absence of IL-11.	Heparin	94-101	signal transducer and activator of transcription 3	Homo sapiens	105-110
16868144-10	2006	The effect of heparin on free IGF-I was fully reversed by PS.	Heparin	14-21	insulin like growth factor 1	Homo sapiens	30-35
16868144-11	2006	Heparin increased free and bioactive IGF-I in all tested sera (P&lt;0.0001), but the increase was most pronounced in samples from pregnant women (P&lt;0.0001).	Heparin	0-7	insulin like growth factor 1	Homo sapiens	37-42
16937240-0	2006	Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods.	Heparin	94-101	fibroblast growth factor 1	Homo sapiens	49-54
16737974-1	2006	In this study, we present multiple lines of evidence to support a critical role for heparin-bound EGF (epidermal growth factor)-like growth factor (HB-EGF) and tumor necrosis factor-alpha-converting enzyme (TACE) (ADAM17) in the transactivation of EGF receptor (EGFR), ERK phosphorylation, and cellular proliferation induced by the 5-HT(2A) receptor in renal mesangial cells.	Heparin	84-91	epidermal growth factor receptor	Homo sapiens	248-260
16737974-1	2006	In this study, we present multiple lines of evidence to support a critical role for heparin-bound EGF (epidermal growth factor)-like growth factor (HB-EGF) and tumor necrosis factor-alpha-converting enzyme (TACE) (ADAM17) in the transactivation of EGF receptor (EGFR), ERK phosphorylation, and cellular proliferation induced by the 5-HT(2A) receptor in renal mesangial cells.	Heparin	84-91	epidermal growth factor receptor	Homo sapiens	262-266
16720575-9	2006	When taken together, these findings suggest that heparin enhances IL-11-induced STAT3 activation and thus osteoclast formation, by a mechanism that is independent of STAT3 Ser-727 phosphorylation but that involves up-regulation of the MAPK pathway.	Heparin	49-56	signal transducer and activator of transcription 3	Homo sapiens	80-85
16720575-9	2006	When taken together, these findings suggest that heparin enhances IL-11-induced STAT3 activation and thus osteoclast formation, by a mechanism that is independent of STAT3 Ser-727 phosphorylation but that involves up-regulation of the MAPK pathway.	Heparin	49-56	mitogen-activated protein kinase 3	Homo sapiens	235-239
16709187-6	2006	In studies in my laboratory, we have shown that GDNF (glial-cell-line-derived neurotrophic factor) and its close relatives neurturin and artemin bind to heparin and heparan sulphate with high affinity.	Heparin	153-160	glial cell derived neurotrophic factor	Homo sapiens	48-52
16191429-2	2006	METHODS AND RESULTS: EC-SOD was measured in plasma at basal and at post-heparin injection in 315 patients.	Heparin	72-79	superoxide dismutase 3	Homo sapiens	21-27
16191429-5	2006	Although the basal values were similar among the three groups, heparin-released EC-SOD levels were significantly lower in the atherosclerosis group (131.0 +/- 42.8 ng/ml, p = 0.0003) than in the normal group (156.9 +/- 66.2 ng/ml).	Heparin	63-70	superoxide dismutase 3	Homo sapiens	80-86
16191429-6	2006	Moreover, logistic analysis revealed that heparin-released EC-SOD independently contributed to CAD.	Heparin	42-49	superoxide dismutase 3	Homo sapiens	59-65
16191429-7	2006	The coronary score showed a significant correlation with heparin-released EC-SOD.	Heparin	57-64	superoxide dismutase 3	Homo sapiens	74-80
16191429-9	2006	CONCLUSIONS: The results suggest that heparin-released EC-SOD is significantly reduced in CAD and that the tissue-bound location of this enzyme might be important for antioxidative function.	Heparin	38-45	superoxide dismutase 3	Homo sapiens	55-61
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	96-103	vascular endothelial growth factor C	Homo sapiens	47-53
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	96-103	vascular endothelial growth factor C	Homo sapiens	84-90
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	132-139	vascular endothelial growth factor C	Homo sapiens	47-53
16410806-5	2006	At 5-50 microM Abeta1-40 reduced EC population, caused apoptosis, downregulated FGF-2 production, inhibited FGF-2 binding to heparin, and FGFR1 phosphorylation.	Heparin	125-132	fibroblast growth factor 2	Homo sapiens	108-113
16817162-4	2006	We now work out conditions to characterize the binding of Ca(2+) and Mg(2+) and the binding of heparin to SAP in the presence of divalent metal ions by ACE.	Heparin	95-102	angiotensin I converting enzyme	Homo sapiens	152-155
16817162-5	2006	The results show a strong binding of heparin (sub-muM apparent dissociation constants) even in the abscence of Ca(2+) at low ionic strength, pH 8.2.	Heparin	37-44	latexin	Homo sapiens	50-53
16781211-2	2006	Recognition of the limitations of heparin has led to the development of a newer class of anticoagulants, the direct thrombin inhibitors.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	116-124
16709175-5	2006	Thus the presence of heparin increases the potency of HGF/SF in experiments with cells in culture leading to elevated downstream signalling effects and, although not vital for the Met-HGF/SF interaction, heparin or heparan sulphate is essential for the activity of certain isoforms of HGF/SF, such as NK1 and NK2.	Heparin	21-28	NK2 homeobox 1	Homo sapiens	309-312
16709187-6	2006	In studies in my laboratory, we have shown that GDNF (glial-cell-line-derived neurotrophic factor) and its close relatives neurturin and artemin bind to heparin and heparan sulphate with high affinity.	Heparin	153-160	glial cell derived neurotrophic factor	Homo sapiens	54-97
16767070-5	2006	Unfortunately the incidence of immune mediated heparin induced thrombocytopenia appears to be increasing, and these patients require systemic anticoagulation with the direct thrombin inhibitors and/or heparinoids to prevent thrombosis.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	174-182
16753836-1	2006	Both extracellular superoxide dismutase (EC-SOD) and heparin binding EGF like growth factor (HB-EGF) are produced in smooth muscle cells of the arterial wall, and are thought to play pathological roles in atherosclerosis with heparin binding characteristics.	Heparin	53-60	heparin-binding EGF-like growth factor	Rattus norvegicus	93-99
16753836-5	2006	Treatment of the cells with heparin alone decreased HB-EGF expression by 20%, whereas EC-SOD alone and a co-incubation with EC-SOD and heparin suppressed the induction by 60 and 70%, respectively.	Heparin	28-35	heparin-binding EGF-like growth factor	Rattus norvegicus	52-58
16682923-3	2006	To counteract the coagulant effects of thrombin, heparin is used in large doses.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	39-47
16424390-1	2006	Neuropilin-1 (Npn-1) is a receptor shared by class 3 semaphorins and heparin-binding forms of vascular endothelial growth factor (VEGF), protein families that regulate endothelial and neuronal-cell function.	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	94-128
16764594-4	2006	Because dialysis patients receive heparin during dialysis, which could potentially bind to PrP(C), the concentration of PrP(C) was measured in patients receiving heparin for cardiopulmonary bypass and was found to be similar to normal controls.	Heparin	34-41	prion protein	Homo sapiens	91-97
16764594-4	2006	Because dialysis patients receive heparin during dialysis, which could potentially bind to PrP(C), the concentration of PrP(C) was measured in patients receiving heparin for cardiopulmonary bypass and was found to be similar to normal controls.	Heparin	162-169	prion protein	Homo sapiens	120-126
16716081-0	2006	Heparin activates beta-secretase (BACE1) of Alzheimer"s disease and increases autocatalysis of the enzyme.	Heparin	0-7	beta-secretase 1	Homo sapiens	34-39
16716081-5	2006	However, heparin has also been reported to directly inhibit BACE1 activity in vitro.	Heparin	9-16	beta-secretase 1	Homo sapiens	60-65
16716081-6	2006	To clarify the role of heparin in regulating BACE1, we examined the effect of heparin on the activity of recombinant human BACE1 (rBACE1) in vitro.	Heparin	78-85	beta-secretase 1	Homo sapiens	123-128
16716081-9	2006	Heparin affinity chromatography demonstrated that heparin interacted strongly with the zymogen form of rBACE1 and bound to a peptide homologous to the N-terminal pro sequence of BACE1.	Heparin	0-7	beta-secretase 1	Homo sapiens	104-109
16716081-9	2006	Heparin affinity chromatography demonstrated that heparin interacted strongly with the zymogen form of rBACE1 and bound to a peptide homologous to the N-terminal pro sequence of BACE1.	Heparin	50-57	beta-secretase 1	Homo sapiens	104-109
16716081-12	2006	Our results strongly suggest that heparin stimulates the partially active BACE1 zymogen, and we propose that the activation is mediated by high-affinity binding of heparin to the pro domain.	Heparin	34-41	beta-secretase 1	Homo sapiens	74-79
16716081-12	2006	Our results strongly suggest that heparin stimulates the partially active BACE1 zymogen, and we propose that the activation is mediated by high-affinity binding of heparin to the pro domain.	Heparin	164-171	beta-secretase 1	Homo sapiens	74-79
16424390-1	2006	Neuropilin-1 (Npn-1) is a receptor shared by class 3 semaphorins and heparin-binding forms of vascular endothelial growth factor (VEGF), protein families that regulate endothelial and neuronal-cell function.	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	130-134
16517611-4	2006	Importantly, the exosite-defective antithrombins bound heparin with nearly wild-type affinities, and the heparin-activated mutants showed near normal reactivities with thrombin, a protease that does not utilize the exosite.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	39-47
16676057-3	2006	Direct thrombin inhibitors are an alternative to heparin, particularly in the setting of increased risk of bleeding and heparin-induced thrombocytopenia.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	7-15
16314835-6	2006	Taken together, our results suggest that the proteolytic status of ADAMTS-1 determines its effect on tumor metastasis, and that the ADAMTS-1E/Q and the ADAMTS-1 fragments likely inhibit tumor metastasis by negatively regulating the availability and activity of soluble heparin-binding EGF and AR.	Heparin	269-276	a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1	Mus musculus	132-143
16505491-5	2006	IGFBP-5 mutants with reduced affinity for IGF-I (N-term) or deficient in heparin binding (HEP- and C-term E and F) were also effective.	Heparin	73-80	insulin-like growth factor binding protein 5	Mus musculus	0-7
16505491-6	2006	This was surprising because IGFBP-5 reportedly interacts with PAI-1 via its heparin-binding domain.	Heparin	76-83	insulin-like growth factor binding protein 5	Mus musculus	28-35
16314835-6	2006	Taken together, our results suggest that the proteolytic status of ADAMTS-1 determines its effect on tumor metastasis, and that the ADAMTS-1E/Q and the ADAMTS-1 fragments likely inhibit tumor metastasis by negatively regulating the availability and activity of soluble heparin-binding EGF and AR.	Heparin	269-276	a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1	Mus musculus	132-140
16512830-7	2006	The inhibition of NF-kappaB activation certainly represents one of the mechanisms by which heparin exerts its anti-inflammatory effect.	Heparin	91-98	nuclear factor kappa B subunit 1	Homo sapiens	18-27
16368135-4	2006	The capacity of surface bound heparin to promote ATIII-mediated thrombin inactivation was investigated in a parallel plate flow chamber under simulated venous and arterial wall shear rates of 50 and 500 s(-1), respectively.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	64-72
16368135-5	2006	Significantly, we observed that the rate of thrombin inactivation approached a maximum at a heparin surface concentration greater than 4.4 pmol/cm(2) (61 ng/cm(2)).	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	44-52
16368135-6	2006	In the process, mass transport limited regimes were identified for heparin potentiated thrombin inactivation under both simulated venous and arterial conditions.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	87-95
16376423-4	2006	Peak and steady-state levels of thrombin were decreased by antithrombin III (ATIII), as well as by surface bound heparin and TM.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	32-40
16376423-5	2006	Although physiologic concentrations of ATIII have the capacity to significantly inhibit thrombin activity, surface bound TM and heparin nearly abolished steady-state thrombin responses.	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	166-174
16376423-6	2006	In particular, surface bound TM appears to be superior to heparin in reducing local thrombin concentrations.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	84-92
16376423-7	2006	These studies are the first to demonstrate the additive effect of surface bound heparin and TM as a combined interactive strategy to limit TF-induced thrombin formation.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	150-158
16606792-0	2006	Heparins increase endothelial nitric oxide bioavailability by liberating vessel-immobilized myeloperoxidase.	Heparin	0-8	myeloperoxidase	Homo sapiens	92-107
16606792-3	2006	In the present study, we investigated whether heparin mobilizes MPO from vascular compartments in humans and defined whether this translates into increased vascular NO bioavailability and function.	Heparin	46-53	myeloperoxidase	Homo sapiens	64-67
16606792-5	2006	Whereas baseline plasma MPO levels did not differ between patients with or without angiographically detectable coronary artery disease (CAD), the increase in MPO plasma content on bolus heparin administration was higher in patients with CAD (P=0.01).	Heparin	186-193	myeloperoxidase	Homo sapiens	158-161
16606792-7	2006	The extent of heparin-induced MPO release was correlated with improvement in endothelial function (r=0.69, P&lt;0.01).	Heparin	14-21	myeloperoxidase	Homo sapiens	30-33
16606792-8	2006	Moreover, and consistent with this tenet, ex vivo heparin treatment of extracellular matrix proteins, cultured endothelial cells, and saphenous vein graft specimens from CAD patients decreased MPO burden.	Heparin	50-57	myeloperoxidase	Homo sapiens	193-196
16606792-9	2006	CONCLUSIONS: Mobilization of vessel-associated MPO may represent an important mechanism by which heparins exert antiinflammatory effects and increase vascular NO bioavailability.	Heparin	97-105	myeloperoxidase	Homo sapiens	47-50
16768071-0	2006	Cardiac surgery in a patient with heparin-induced thrombocytopenia--cautions with use of the direct thrombin inhibitor, argatroban.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	100-108
16556679-3	2006	We now demonstrate that heparin abrogates apoptosis of primary first trimester villous trophoblast in response to treatment with the pro-inflammatory cytokines interferon (IFN)-gamma and tumour necrosis factor (TNF)-alpha.	Heparin	24-31	interferon gamma	Homo sapiens	160-182
16322097-4	2006	The results presented in this study demonstrate that this heparin binding domain (HBD) is the region of Vn that binds to the cysteine loop region of beta3 and that this region is sufficient to mediate the positive effects of Vn on IGF-I signaling.	Heparin	58-65	insulin like growth factor 1	Homo sapiens	231-236
16556679-3	2006	We now demonstrate that heparin abrogates apoptosis of primary first trimester villous trophoblast in response to treatment with the pro-inflammatory cytokines interferon (IFN)-gamma and tumour necrosis factor (TNF)-alpha.	Heparin	24-31	tumor necrosis factor	Homo sapiens	187-221
16556679-5	2006	Furthermore, heparin attenuated caspase-3 activity, a hallmark of apoptosis, in human first trimester villous and extravillous trophoblast cell lines treated with peptidoglycan, a Toll-like receptor-2 agonist isolated from Staphylococcus aureus.	Heparin	13-20	caspase 3	Homo sapiens	32-41
16556679-5	2006	Furthermore, heparin attenuated caspase-3 activity, a hallmark of apoptosis, in human first trimester villous and extravillous trophoblast cell lines treated with peptidoglycan, a Toll-like receptor-2 agonist isolated from Staphylococcus aureus.	Heparin	13-20	toll like receptor 2	Homo sapiens	180-200
16556679-7	2006	We demonstrate that heparin, like epidermal growth factor (EGF) and heparin-binding EGF (HB-EGF), elicits phosphorylation of the EGF receptor and activation of the phosphatidyl inositol 3-kinase (PI3K)-, the extracellular signal-related kinase 1/2 (ERK1/2)- and the c-Jun NH2 terminal kinase (JNK)-signal transduction pathways in primary villous trophoblast.	Heparin	20-27	mitogen-activated protein kinase 3	Homo sapiens	208-247
16556679-7	2006	We demonstrate that heparin, like epidermal growth factor (EGF) and heparin-binding EGF (HB-EGF), elicits phosphorylation of the EGF receptor and activation of the phosphatidyl inositol 3-kinase (PI3K)-, the extracellular signal-related kinase 1/2 (ERK1/2)- and the c-Jun NH2 terminal kinase (JNK)-signal transduction pathways in primary villous trophoblast.	Heparin	20-27	mitogen-activated protein kinase 3	Homo sapiens	249-255
16556679-7	2006	We demonstrate that heparin, like epidermal growth factor (EGF) and heparin-binding EGF (HB-EGF), elicits phosphorylation of the EGF receptor and activation of the phosphatidyl inositol 3-kinase (PI3K)-, the extracellular signal-related kinase 1/2 (ERK1/2)- and the c-Jun NH2 terminal kinase (JNK)-signal transduction pathways in primary villous trophoblast.	Heparin	20-27	mitogen-activated protein kinase 8	Homo sapiens	266-291
16464886-0	2006	Myeloperoxidase up-regulation during haemodialysis: is heparin the missing link?	Heparin	55-62	myeloperoxidase	Homo sapiens	0-15
16556679-7	2006	We demonstrate that heparin, like epidermal growth factor (EGF) and heparin-binding EGF (HB-EGF), elicits phosphorylation of the EGF receptor and activation of the phosphatidyl inositol 3-kinase (PI3K)-, the extracellular signal-related kinase 1/2 (ERK1/2)- and the c-Jun NH2 terminal kinase (JNK)-signal transduction pathways in primary villous trophoblast.	Heparin	20-27	mitogen-activated protein kinase 8	Homo sapiens	293-296
16562602-4	2006	Danaparoid and thrombin inhibitors should be used mainly in patients suffering from renal failure and heparin-induced thrombocytopenia with regular monitoring of coagulation tests.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	15-23
16553503-0	2006	Evaluation of treatment with direct thrombin inhibitors in patients with heparin-induced thrombocytopenia.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	36-44
16601834-0	2006	Less pronounced enhancement of thrombin-dependent inactivation of plasminogen activator inhibitor type 1 by low molecular weight heparin compared with unfractionated heparin.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	31-39
16601834-1	2006	Plasminogen activator inhibitor type 1 (PAI-1), the primary inhibitor of plasminogen activators, also forms high molecular weight complexes with either thrombin or factor Xa (FXa) in the presence of heparin, resulting in the loss of mutual activities of enzyme and inhibitor.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	152-160
16601834-3	2006	In the present study, we compared the effects of low molecular weight (LMW)- and unfractionated-heparin on the interaction between PAI-1 and either thrombin or FXa.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	148-156
16601834-4	2006	Both types of heparin enhanced the inhibition of thrombin activity by PAI-1 with a bell-shaped pattern, though the magnitude of the enhancement was significantly weaker with LMW-heparin.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	49-57
16601834-6	2006	In the presence of vitronectin (Vn), the inhibition of thrombin and FXa by PAI-1 was further promoted by both types of heparin but to a significantly lesser extent with LMW-heparin.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	55-63
16601834-8	2006	As a consequence of thrombin-dependent inactivation of PAI-1, tPA-induced fibrin clot lysis time in the presence of PAI-1 was shortened by unfractionated-heparin as well as by LMW-heparin with lesser extent, which was further enhanced by Vn.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	20-28
16436282-0	2006	Solution conformation and heparin-induced dimerization of the full-length extracellular domain of the human amyloid precursor protein.	Heparin	26-33	amyloid beta precursor protein	Homo sapiens	108-133
16183114-11	2006	Experiments with matrices containing radioactively labelled heparin suggest that VEGF release results from the consecutive and simultaneous release of three species of VEGF molecules that differ in their binding affinities to the differently modified collagen matrices.	Heparin	60-67	vascular endothelial growth factor A	Homo sapiens	81-85
16183114-11	2006	Experiments with matrices containing radioactively labelled heparin suggest that VEGF release results from the consecutive and simultaneous release of three species of VEGF molecules that differ in their binding affinities to the differently modified collagen matrices.	Heparin	60-67	vascular endothelial growth factor A	Homo sapiens	168-172
16183114-12	2006	The species binding specifically to heparin most likely accounts for the previously observed increases in angiogenic potential between loading VEGF to non-heparinized and heparinized collagen matrices.	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	143-147
16520718-0	2006	Inhibitory effect of C-reactive protein on the release of tissue factor pathway inhibitor from human endothelial cells: reversal by low molecular weight heparin.	Heparin	153-160	C-reactive protein	Homo sapiens	21-39
16493076-0	2006	The B12 anti-tryptase monoclonal antibody disrupts the tetrameric structure of heparin-stabilized beta-tryptase to form monomers that are inactive at neutral pH and active at acidic pH.	Heparin	79-86	NADH:ubiquinone oxidoreductase subunit B3	Homo sapiens	4-7
16515924-1	2006	OBJECTIVES: Unfractionated heparin has many shortcomings, including indirect and partial inhibition of thrombin, antibody formation, and platelet activation.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	103-111
16449547-1	2006	OBJECTIVE: To report the case of a critically ill man with heparin-induced thrombocytopenia (HIT) who received a 125 mg overdose of the direct thrombin inhibitor argatroban.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	143-151
16637459-8	2006	Lastly, inhibitors of thrombin activity are composed of either indirect (UFH, LMWH), or direct thrombin (FIIa) inhibitors including: hirudin, argatroban, melagatran, ximelagatran, dabigatran, and bivalirudin.	Heparin	73-76	coagulation factor II, thrombin	Homo sapiens	22-30
16373349-12	2006	In summary, antibody HS4C3 selectively detects 3-O-sulfated HS structures and interferes with the coagulation activities of heparin by association with the anti-thrombin binding pentasaccharide sequence.	Heparin	124-131	coagulation factor II	Rattus norvegicus	161-169
16469315-3	2006	During the purification of EC-SOD from human aorta, we noticed that material with high affinity for heparin-Sepharose formed not only a tetramer but also an octamer.	Heparin	100-107	superoxide dismutase 3	Homo sapiens	27-33
16223363-4	2006	In the present study, we demonstrate that, in the FGF (fibroblast growth factor)-FGFR (FGF receptor) system, multimers of the minimal complex composed of two FGF1 and two FGFR2 protomers can form on a single chain of the co-receptor heparin.	Heparin	233-240	fibroblast growth factor 1	Homo sapiens	158-162
16553237-5	2006	Unfractionated heparin was the thrombin inhibitor of choice for many years in interventional cardiology but the improvement of our knowledge of the mechanisms of thrombosis has helped define its limitations.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	31-39
16223363-7	2006	However, the doublet of complexes appears to be less co-operative than the formation of the 2:2:1 FGF1:FGFR2:heparin complex, suggesting that this mechanism is one of a number of weaker interactions that might be involved in the formation of a focal complex on the cell surface.	Heparin	109-116	fibroblast growth factor 1	Homo sapiens	98-102
16452210-2	2006	Early tumor cell-platelet interactions can be mediated by P-selectin binding to tumor cell surface ligands and this process is blocked by heparin.	Heparin	138-145	selectin, platelet	Mus musculus	58-68
16434757-9	2006	CONCLUSION: These results indicate that protamine and the heparin-protamine complex stimulated the release of NO from iNOS.	Heparin	58-65	nitric oxide synthase 2	Rattus norvegicus	118-122
16434757-10	2006	As iNOS is induced during CPB, protamine or a heparin-protamine complex might cause systemic hypotension, at least in part, by stimulating iNOS.	Heparin	46-53	nitric oxide synthase 2	Rattus norvegicus	3-7
16452210-9	2006	Thus, heparin apparently works at these time points primarily by blocking L-selectin.	Heparin	6-13	selectin, lymphocyte	Mus musculus	74-84
16434757-10	2006	As iNOS is induced during CPB, protamine or a heparin-protamine complex might cause systemic hypotension, at least in part, by stimulating iNOS.	Heparin	46-53	nitric oxide synthase 2	Rattus norvegicus	139-143
16354105-7	2006	Median EL mass in pre-heparin plasma was 442 (interquartile range = 324-617) ng/ml.	Heparin	22-29	lipase G, endothelial type	Homo sapiens	7-9
16475045-4	2006	Two parenteral direct thrombin inhibitors, lepirudin and argatroban, have FDA approval for the management of heparin-induced thrombocytopenia.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	22-30
16387752-9	2006	Analogous to these findings, heparin-plasma strongly inhibited the antibacterial effect of LL-37.	Heparin	29-36	cathelicidin antimicrobial peptide	Homo sapiens	91-96
16354105-11	2006	EL mass in both routine (odds ratio [OR] = 1.67, p = 0.01) and post-heparin (OR = 2.42, p = 0.003) plasma was associated with CAC as determined by ordinal regression after adjustment for age, gender, waist circumference, vasoactive medications, hormone replacement therapy (women), and established cardiovascular risk factors.	Heparin	68-75	lipase G, endothelial type	Homo sapiens	0-2
16354105-12	2006	CONCLUSIONS: We report, to our knowledge for the first time, that human plasma EL concentrations, in both post-heparin and routine pre-heparin plasma, are significantly associated with metabolic syndrome features and with subclinical atherosclerosis.	Heparin	111-118	lipase G, endothelial type	Homo sapiens	79-81
16354105-12	2006	CONCLUSIONS: We report, to our knowledge for the first time, that human plasma EL concentrations, in both post-heparin and routine pre-heparin plasma, are significantly associated with metabolic syndrome features and with subclinical atherosclerosis.	Heparin	135-142	lipase G, endothelial type	Homo sapiens	79-81
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	177-184	fibroblast growth factor 1	Homo sapiens	52-57
16338223-0	2006	Identification of amino acid residues essential for heparin binding by the A1 domain of human von Willebrand factor.	Heparin	52-59	von Willebrand factor	Homo sapiens	94-115
16338223-2	2006	Previous observations suggested that heparin competitively inhibits the binding of VWF to GPIb and may down-regulate platelet adhesion.	Heparin	37-44	von Willebrand factor	Homo sapiens	83-86
16338223-7	2006	Our findings suggest that heparin may inhibit the binding of VWF to GPIb by interacting with GPIb binding and interpret why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin.	Heparin	26-33	von Willebrand factor	Homo sapiens	61-64
16338223-7	2006	Our findings suggest that heparin may inhibit the binding of VWF to GPIb by interacting with GPIb binding and interpret why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin.	Heparin	158-165	von Willebrand factor	Homo sapiens	61-64
16338223-7	2006	Our findings suggest that heparin may inhibit the binding of VWF to GPIb by interacting with GPIb binding and interpret why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin.	Heparin	158-165	von Willebrand factor	Homo sapiens	61-64
16242830-5	2006	The influence of LMWH on the pro-inflammatory and pro-apoptotic cytokine, TNF-alpha was studied.	Heparin	17-21	tumor necrosis factor	Rattus norvegicus	74-83
16242830-6	2006	Renal and cardiac levels of TNF-alpha showed a significant rise (p&lt;0.001) in the ADR cytotoxic group, while the TNF-alpha values departed towards control levels in the LMWH treated group (p&lt;0.001).	Heparin	171-175	tumor necrosis factor	Rattus norvegicus	115-124
16242830-9	2006	In short, the results suggest that the low-molecular-weight heparin derivative, certoparin exerts beneficial effects on the nitrosative status, and on the biological macromolecules as DNA and curtails the rise of the pro-apoptotic and pro-inflammatory cytokine, TNF-alpha in the cardiac and renal tissues.	Heparin	60-67	tumor necrosis factor	Rattus norvegicus	262-271
16246549-1	2006	The ultrasound velocimetry, densitometry, and differential scanning calorimetry have been used to study the formation of the complexes between human serum albumin (HSA) and polyanions heparin (HEP) and/or dextran sulfate (DS).	Heparin	193-196	albumin	Homo sapiens	149-162
16493483-7	2006	Moreover, the formation of PN-1/(125)I-thrombin complex was increased in the presence of heparin, HMW and LMW fucoidans, but barely by LMW heparin.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	39-47
16417632-2	2006	A considerable body of evidence has established that heparin and heparan sulfate proteoglycans (HSPGs) interact with numerous protein ligands including fibroblast growth factors, vascular endothelial growth factor (VEGF), cytokines, and chemokines.	Heparin	53-60	vascular endothelial growth factor A	Homo sapiens	179-213
16417632-2	2006	A considerable body of evidence has established that heparin and heparan sulfate proteoglycans (HSPGs) interact with numerous protein ligands including fibroblast growth factors, vascular endothelial growth factor (VEGF), cytokines, and chemokines.	Heparin	53-60	vascular endothelial growth factor A	Homo sapiens	215-219
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	113-120	vascular endothelial growth factor A	Homo sapiens	46-50
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	113-120	fibroblast growth factor 1	Homo sapiens	52-57
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	177-184	vascular endothelial growth factor A	Homo sapiens	46-50
16411608-0	2006	PEG-cross-linked heparin is an affinity hydrogel for sustained release of vascular endothelial growth factor.	Heparin	17-24	vascular endothelial growth factor A	Homo sapiens	74-108
16377383-4	2006	In this review, a novel and growing body of evidence indicating that MPO also is a potent blood vessel-bound enzyme that can be mobilized rapidly and extensively into circulating blood by exogenous heparin is discussed.	Heparin	198-205	myeloperoxidase	Homo sapiens	69-72
16377383-7	2006	In view of the plausible clinical importance of the novel MPO-oxidative stress-heparin interaction in this population, the need for additional studies assessing different dialyzer membranes, various heparin types (unfractionated heparin versus low-molecular-weight heparins versus pentasaccharides), as well as different anticoagulation regimens, is emphasized.	Heparin	79-86	myeloperoxidase	Homo sapiens	58-61
16377383-7	2006	In view of the plausible clinical importance of the novel MPO-oxidative stress-heparin interaction in this population, the need for additional studies assessing different dialyzer membranes, various heparin types (unfractionated heparin versus low-molecular-weight heparins versus pentasaccharides), as well as different anticoagulation regimens, is emphasized.	Heparin	265-273	myeloperoxidase	Homo sapiens	58-61
16487077-1	2006	Cu,Zn-superoxide dismutase (SOD) was chemically modified with low molecular weight heparin (LMWH).	Heparin	83-90	superoxide dismutase 1	Homo sapiens	28-31
16373888-4	2006	RESULTS: Insulin-treated diabetic patients were less likely than nondiabetic patients to receive aspirin (adjusted odds ratio 0.83 [95% CI 0.74-0.93]), beta-blockers (0.89 [0.83-0.96]), heparin (0.90 [0.83-0.98]), and glycoprotein IIb/IIIa inhibitors (0.86 [0.79-0.93]).	Heparin	186-193	insulin	Homo sapiens	9-16
16146717-6	2006	Thrombin-specific inhibitors are the current best choice for the treatment of heparin-induced thrombocytopenia (HIT).	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	0-8
16390607-2	2006	Here we aimed to demonstrate that lithium-heparin plasma samples could be used for protein electrophoresis and paraprotein typing without or with ethanol treatment to remove the fibrinogen.	Heparin	42-49	fibrinogen beta chain	Homo sapiens	178-188
16269513-7	2006	Ex vivo copeptin stability (&lt;20% loss of analyte) for at least 7 days at room temperature and 14 days at 4 degrees C was shown for serum and EDTA-, heparin-, and citrate plasma.	Heparin	151-158	arginine vasopressin	Homo sapiens	8-16
16508209-6	2006	In fact, lipoprotein lipase and hepatic lipase activities in the post-heparin plasma of Angptl3-null mice were 1.57 times and 1.42 times higher than those of wild-type mice, respectively.	Heparin	70-77	lipase, hepatic	Mus musculus	32-46
16508209-6	2006	In fact, lipoprotein lipase and hepatic lipase activities in the post-heparin plasma of Angptl3-null mice were 1.57 times and 1.42 times higher than those of wild-type mice, respectively.	Heparin	70-77	angiopoietin-like 3	Mus musculus	88-95
17124098-4	2006	Two parenteral direct thrombin inhibitors, lepirudin and argatroban, have FDA approval for the management of heparin-induced thrombocytopenia (HIT).	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	22-30
16195388-7	2006	As measured from heparin-releasable LPL activity, LPL in the microvasculature of the most oxidative muscles was approximately 90% lower in the inactive group compared with controls, and this suppression was completely blocked by NA.	Heparin	17-24	lipoprotein lipase	Rattus norvegicus	36-39
16195388-7	2006	As measured from heparin-releasable LPL activity, LPL in the microvasculature of the most oxidative muscles was approximately 90% lower in the inactive group compared with controls, and this suppression was completely blocked by NA.	Heparin	17-24	lipoprotein lipase	Rattus norvegicus	50-53
16411608-5	2006	VEGF was directly injected into the heparin gel and the loaded VEGF displayed a slow, controlled release over 3 weeks with little initial burst phase.	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	0-4
16411608-5	2006	VEGF was directly injected into the heparin gel and the loaded VEGF displayed a slow, controlled release over 3 weeks with little initial burst phase.	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	63-67
16365408-3	2006	In this study we found that DcR3.Fc-induced cell adhesion was inhibited by heparin and heparan sulfate, and that DcR3.Fc was unable to bind Chinese hamster ovary K1 mutants defective in glycosaminoglycan (GAG) synthesis.	Heparin	75-82	TNF receptor superfamily member 6b	Homo sapiens	28-32
16139336-7	2006	Platelet-leukocyte aggregation in vivo was greater (PMA=2-fold, p=0.04; PNA=3-fold, p=0.006) with UFH+E as was the concentration in blood of MPO (1.5-fold, p=0.007).	Heparin	98-101	myeloperoxidase	Homo sapiens	141-144
16409456-2	2006	The endogenous thrombin potential (ETP) is a sensitive detector of the heparin effect.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	15-23
15996721-5	2006	During CPB in the modified group thrombin generation was not increased beyond surgical levels, lower heparin concentrations allowed each thrombin to make more fibrin prior to inhibition, while fibrin degradation was suppressed by epsilon-amino-caproic acid.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	137-145
16407063-0	2006	The structures of the thrombospondin-1 N-terminal domain and its complex with a synthetic pentameric heparin.	Heparin	101-108	thrombospondin 1	Homo sapiens	22-38
16407063-4	2006	The crystal structure of the complex of TSPN-1 with heparin indicates that residues R29, R42, and R77 in an extensive positively charged patch at the bottom of the domain specifically associate with the sulfate groups of heparin.	Heparin	52-59	thrombospondin 1	Homo sapiens	40-46
16407063-4	2006	The crystal structure of the complex of TSPN-1 with heparin indicates that residues R29, R42, and R77 in an extensive positively charged patch at the bottom of the domain specifically associate with the sulfate groups of heparin.	Heparin	221-228	thrombospondin 1	Homo sapiens	40-46
16286677-0	2005	Selenoprotein P analysis in human plasma: a discrepancy between HPLC fractionation of human plasma with heparin-affinity chromatography and SDS-PAGE with immunoblot analysis.	Heparin	104-111	selenoprotein P	Homo sapiens	0-15
16260060-7	2005	As a consequence, the resultant modified t-PA possessed a wide range of heparin-binding strength, rendering the inhibition of t-PA activity by heparin binding ineffective.	Heparin	72-79	plasminogen activator, tissue type	Homo sapiens	41-45
16260060-7	2005	As a consequence, the resultant modified t-PA possessed a wide range of heparin-binding strength, rendering the inhibition of t-PA activity by heparin binding ineffective.	Heparin	143-150	plasminogen activator, tissue type	Homo sapiens	41-45
16260060-7	2005	As a consequence, the resultant modified t-PA possessed a wide range of heparin-binding strength, rendering the inhibition of t-PA activity by heparin binding ineffective.	Heparin	143-150	plasminogen activator, tissue type	Homo sapiens	126-130
16051347-6	2005	The thrombin resistance of the heparin modified surfaces was demonstrably greater as measured by a chromogenic thrombin generation assay.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	4-12
16051347-6	2005	The thrombin resistance of the heparin modified surfaces was demonstrably greater as measured by a chromogenic thrombin generation assay.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	111-119
17162536-7	2006	Administration of AG or heparin prior to LPS also decreased liver iNOS expression, hepatic neutrophil infiltration and liver pathology comparable to calpain inhibition.	Heparin	24-31	nitric oxide synthase 2	Rattus norvegicus	66-70
16219767-0	2005	Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes.	Heparin	76-83	fibroblast growth factor 1	Homo sapiens	28-54
16219767-0	2005	Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes.	Heparin	76-83	fibroblast growth factor 1	Homo sapiens	56-60
16219767-0	2005	Cooperative dimerization of fibroblast growth factor 1 (FGF1) upon a single heparin saccharide may drive the formation of 2:2:1 FGF1.FGFR2c.heparin ternary complexes.	Heparin	76-83	fibroblast growth factor 1	Homo sapiens	128-132
16219767-1	2005	The related glycosaminoglycans heparin and heparan sulfate are essential for the activity of the fibroblast growth factor (FGF) family as they form an integral part of the signaling complex at the cell surface.	Heparin	31-38	fibroblast growth factor 1	Homo sapiens	123-126
16219767-6	2005	Heparin hexasaccharide and various selectively desulfated heparin dp12s failed to bind FGFR2c and could only interact with FGF1 monomerically.	Heparin	58-65	fibroblast growth factor 1	Homo sapiens	123-127
16219767-8	2005	We found that FGF1 dimerization upon heparin was favored over monomeric interactions even when a large excess of saccharide was present.	Heparin	37-44	fibroblast growth factor 1	Homo sapiens	14-18
16286677-5	2005	The majority (74.9%) of total selenoprotein P found by immunoblot analysis was contained in the early HPLC fractions, consistent with either poor heparin affinity, which was not evident based on the HPLC-ICP-MS technique alone or nonspecific binding of the antibody.	Heparin	146-153	selenoprotein P	Homo sapiens	30-45
16087389-2	2005	EC-SOD contains a unique heparin-binding domain at its carboxy-terminus that establishes localization to the extracellular matrix where the enzyme scavenges superoxide anion.	Heparin	25-32	superoxide dismutase 3	Homo sapiens	0-6
16338497-6	2005	These data indicate that heparin as effective cofactor for TPO and IL-11 promotes expansion of MK progenitor cells from CB CD34(+) cells.	Heparin	25-32	thrombopoietin	Homo sapiens	59-62
16338497-6	2005	These data indicate that heparin as effective cofactor for TPO and IL-11 promotes expansion of MK progenitor cells from CB CD34(+) cells.	Heparin	25-32	CD34 molecule	Homo sapiens	123-127
16087389-3	2005	The EC-SOD heparin-binding domain can be removed by proteolytic cleavage, releasing active enzyme into the extracellular fluid.	Heparin	11-18	superoxide dismutase 3	Homo sapiens	4-10
16395488-3	2005	These include fibrin formation; binding of heparin to angiogenic growth factors, such as basic fibroblast growth factor (FGF2) and vascular endothelial growth factor (VEGF); modulation of tissue factor; and perhaps other more important modulatory mechanisms, such as enhanced tissue factor pathway inhibitor (TFPI) release and inhibition of various matrix-degrading enzymes.	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	121-125
16364844-2	2005	METHODS: Ten long-term heart transplant recipients were examined with positron emission tomography (PET) to measure myocardial perfusion before and after a single heparin-mediated extracorporeal LDL/fibrinogen precipitation (HELP)-apheresis treatment.	Heparin	163-170	fibrinogen beta chain	Homo sapiens	199-209
16288042-6	2005	Finally, we have shown that peptide A5G27 directly blocks FGF2 binding to heparin.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	58-62
16262248-5	2005	On the basis of both the electrostatic potential map and comparison to the heparin binding site on human fibronectin, we predicted a continuous region containing the basic amino acids K133, R136, H139, R142, and K146 to be involved in NKp46 binding to heparan sulfate.	Heparin	75-82	fibronectin 1	Homo sapiens	105-116
15941584-9	2005	The proposed polymeric coatings are capable of functioning by two complementary anti-thrombotic mechanisms, one based on the potent anti-platelet activity of NO, and the other the result of the ability of immobilized heparin to inhibit Factor Xa and thrombin (Factor IIa).	Heparin	217-224	coagulation factor II, thrombin	Homo sapiens	250-258
16095917-3	2005	However, co-over-expression of E. coli chaperonins GroEL/GroES solubilized approximately 50% of the protein, which was purified by ion-exchange and heparin-affinity chromatography.	Heparin	148-155	GroEL	Escherichia coli	51-56
16155294-0	2005	Heparan sulfate mimicry: a synthetic glycoconjugate that recognizes the heparin binding domain of interferon-gamma inhibits the cytokine activity.	Heparin	72-79	interferon gamma	Homo sapiens	98-114
16395488-3	2005	These include fibrin formation; binding of heparin to angiogenic growth factors, such as basic fibroblast growth factor (FGF2) and vascular endothelial growth factor (VEGF); modulation of tissue factor; and perhaps other more important modulatory mechanisms, such as enhanced tissue factor pathway inhibitor (TFPI) release and inhibition of various matrix-degrading enzymes.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	131-165
16395488-3	2005	These include fibrin formation; binding of heparin to angiogenic growth factors, such as basic fibroblast growth factor (FGF2) and vascular endothelial growth factor (VEGF); modulation of tissue factor; and perhaps other more important modulatory mechanisms, such as enhanced tissue factor pathway inhibitor (TFPI) release and inhibition of various matrix-degrading enzymes.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	167-171
16197992-0	2005	The interaction between heparin and Lys49 phospholipase A2 reveals the natural binding of heparin on the enzyme.	Heparin	24-31	phospholipase A2 group IB	Homo sapiens	42-58
16150822-4	2005	When placental protein extracts were separated by heparin-Sepharose affinity chromatography, the EL protein eluted as a single peak without detectable phospholipid or triglyceride (TG) lipase activity.	Heparin	50-57	lipase G, endothelial type	Homo sapiens	97-99
16197992-0	2005	The interaction between heparin and Lys49 phospholipase A2 reveals the natural binding of heparin on the enzyme.	Heparin	90-97	phospholipase A2 group IB	Homo sapiens	42-58
16197992-1	2005	We have studied at a molecular level the interaction of heparins on bothropstoxin-I (BthTx-I), a phospholipase A2 toxin.	Heparin	56-64	phospholipase A2 group IB	Homo sapiens	97-113
15958243-2	2005	The covalently bound heparin provided a crosslinkable analog of a heparan sulfate proteoglycan, thus providing a multivalent biomaterial capable of controlled release of basic fibroblast growth factor (bFGF).	Heparin	21-28	fibroblast growth factor 2	Homo sapiens	170-200
16131539-1	2005	BACKGROUND: Argatroban, a direct thrombin inhibitor, is used for prophylaxis or treatment of thrombosis in heparin-induced thrombocytopenia (HIT).	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	33-41
15958243-2	2005	The covalently bound heparin provided a crosslinkable analog of a heparan sulfate proteoglycan, thus providing a multivalent biomaterial capable of controlled release of basic fibroblast growth factor (bFGF).	Heparin	21-28	fibroblast growth factor 2	Homo sapiens	202-206
15958243-4	2005	With as little as 1% (w/w) covalently bound heparin (relative to total glycosaminoglycan content), the rate of release of bFGF in vitro was substantially reduced.	Heparin	44-51	fibroblast growth factor 2	Homo sapiens	122-126
15958243-5	2005	Total bFGF released increased with lower percentages of heparin; essentially quantitative release of bFGF was observed from heparin-free hydrogels.	Heparin	56-63	fibroblast growth factor 2	Homo sapiens	6-10
15958243-5	2005	Total bFGF released increased with lower percentages of heparin; essentially quantitative release of bFGF was observed from heparin-free hydrogels.	Heparin	124-131	fibroblast growth factor 2	Homo sapiens	101-105
15812639-3	2005	We present experimental results using SPR for the interaction of insulin-like growth factor-I (IGF-I) with one of its binding proteins, IGF binding protein-3 (IGFBP-3), and show that the dissociation, even with the addition of soluble heparin in the dissociation phase, does not exhibit the expected exponential decay characteristic of a 1:1 binding reaction.	Heparin	235-242	insulin like growth factor 1	Homo sapiens	65-93
16041398-11	2005	Hence, UFH and dalteparin may be more effective than danaparoid at inhibiting cancer progression in DIC patients with solid tumours, due at least in part to their ability to suppress VEGF and heparanase in tumours.	Heparin	7-10	vascular endothelial growth factor A	Homo sapiens	183-187
16203794-5	2005	EXPERIMENTAL DESIGN: Five clinically approved heparins were evaluated for inhibition of P-selectin and L-selectin binding to carcinoma cells.	Heparin	46-54	selectin, platelet	Mus musculus	88-98
16203794-5	2005	EXPERIMENTAL DESIGN: Five clinically approved heparins were evaluated for inhibition of P-selectin and L-selectin binding to carcinoma cells.	Heparin	46-54	selectin, lymphocyte	Mus musculus	103-113
15812639-3	2005	We present experimental results using SPR for the interaction of insulin-like growth factor-I (IGF-I) with one of its binding proteins, IGF binding protein-3 (IGFBP-3), and show that the dissociation, even with the addition of soluble heparin in the dissociation phase, does not exhibit the expected exponential decay characteristic of a 1:1 binding reaction.	Heparin	235-242	insulin like growth factor 1	Homo sapiens	95-100
16270635-7	2005	Thrombin generation was inhibited equally well with heparin or Intimatan when the level of their respective cofactors was within the normal range.	Heparin	52-59	coagulation factor II, thrombin	Homo sapiens	0-8
16039552-4	2005	A cationic peptide (MC2) derived from the heparin-binding sequence of mouse IFN-gamma was previously shown by our laboratory to delay allograft rejection in an animal model.	Heparin	42-49	interferon gamma	Mus musculus	76-85
16177113-13	2005	In conclusion, LL-37 induces keratinocyte migration via heparin-binding-EGF-mediated transactivation of EGFR, and SOCS1/Jak 2 binding and SOCS3/CIS3 negatively regulate this migration.	Heparin	56-63	cathelicidin antimicrobial peptide	Homo sapiens	15-20
16177113-13	2005	In conclusion, LL-37 induces keratinocyte migration via heparin-binding-EGF-mediated transactivation of EGFR, and SOCS1/Jak 2 binding and SOCS3/CIS3 negatively regulate this migration.	Heparin	56-63	epidermal growth factor receptor	Homo sapiens	104-108
16270635-8	2005	With decreasing levels of AT or HCII, heparin and Intimatan became less effective in thrombin inhibition, respectively.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	85-93
16126225-11	2005	A more detailed analysis of the biological behavior of stable FGF-1 mutants revealed that, compared with the wild-type, their mitogenic properties, as probed by the DNA synthesis assay, were significantly increased in the absence of heparin, and that their half-lives were extensively prolonged.	Heparin	233-240	fibroblast growth factor 1	Homo sapiens	62-67
15905187-2	2005	Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin"s ability to inhibit proliferation, migration, capillary-like tube formation, basic fibroblast growth factor (bFGF) signaling, and perlecan gene expression in bFGF-stimulated human umbilical vein endothelial cells.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	228-258
16159120-7	2005	Having a means, such as HOST, for automating the interpretation of the MSn data generated from glycosaminoglycans, provides a practical methodology for the future analysis of heparin/HS oligosaccharides of unknown structure.	Heparin	175-182	moesin	Homo sapiens	71-74
16027124-3	2005	We reported previously that heparin has an affinity for VEGF165, the major isoform of VEGF, whereas 2-O-desulfated heparin and 6-O-desulfated heparin have weak but significant affinity (Ashikari-Hada, S., Habuchi, H., Kariya, Y., Itoh, N., Reddi, A. H., and Kimata, K. (2004) J. Biol.	Heparin	28-35	vascular endothelial growth factor A	Homo sapiens	56-60
16173813-2	2005	Acid fibroblast growth factor (aFGF) in the presence of heparin was used as negatively charged polyelectrolytes, while poly(ethyleneimine) (PEI) was chosen as a positively charged counterpart.	Heparin	56-63	fibroblast growth factor 1	Homo sapiens	31-35
15905187-2	2005	Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin"s ability to inhibit proliferation, migration, capillary-like tube formation, basic fibroblast growth factor (bFGF) signaling, and perlecan gene expression in bFGF-stimulated human umbilical vein endothelial cells.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	260-264
15905187-2	2005	Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin"s ability to inhibit proliferation, migration, capillary-like tube formation, basic fibroblast growth factor (bFGF) signaling, and perlecan gene expression in bFGF-stimulated human umbilical vein endothelial cells.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	309-313
15973728-0	2005	Heparin structures in FGF-2-dependent morphological transformation of astrocytes.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	22-27
16162790-7	2005	CONCLUSION: This study shows, for the first time, that heparin causes the inhibition of TNF-alpha protein synthesis and release from the isolated ischemic rat heart within the posttranscriptional stage, and that it prevents the depression of LV function caused by ischemic-reperfusion injury.	Heparin	55-62	tumor necrosis factor	Rattus norvegicus	88-97
16158039-0	2005	Elevation of plasma von Willebrand factor and tumor necrosis factor-a in obese subjects and their reduction by the low molecular weight heparin tinzaparin.	Heparin	136-143	von Willebrand factor	Homo sapiens	20-41
15985490-1	2005	OBJECTIVE: Elevation of free fatty acids (FFAs) by the infusion of triglyceride-heparin emulsion infusion (TG-Hep) causes insulin resistance (IR).	Heparin	80-87	insulin	Homo sapiens	122-129
15973728-3	2005	Native heparin significantly promoted FGF-2-dependent astrocytic stellation, whereas heparin hexasaccharide inhibited FGF-2-dependent stellation.	Heparin	7-14	fibroblast growth factor 2	Homo sapiens	38-43
15973728-2	2005	In the current study, we used quantitative morphometric analysis to investigate the structural requirements for heparin"s enhancement of FGF-2-induced stellation of cultured cortical astrocytes.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	137-142
15973728-6	2005	These results demonstrate that the length and sulfated position of heparin are important for its enhancement of FGF-2-dependent astrocyte stellation.	Heparin	67-74	fibroblast growth factor 2	Homo sapiens	112-117
16350383-15	2005	Novel hyaluronan-based heparin-bonded circuits reduce platelet adhesion-aggregation and protein adsorption and provide better perioperative clinical parameters through platelet, albumin, and fibrinogen-sparing effects.	Heparin	23-30	fibrinogen beta chain	Homo sapiens	191-201
16350384-1	2005	Bivalirudin is a short-acting direct thrombin inhibitor that has been used in cardiac surgical patients with heparin-induced thrombocytopenia (HIT) or suspected HIT.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	37-45
16055320-6	2005	Heparin treatment significantly stimulated VIC production of TGF-beta1 at all concentrations tested (50 to 400 mug/ml).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	61-70
16116207-6	2005	Soluble heparin and heparan sulfate but not chondroitin sulfates greatly diminished cytokine induction through inhibition of capsid binding to THP-1 macrophages.	Heparin	8-15	GLI family zinc finger 2	Homo sapiens	143-148
16116207-9	2005	Finally, NF-kappaB activation by the capsid in HEK 293 cells specifically required expression of TLR2 and was compromised by soluble heparin.	Heparin	133-140	nuclear factor kappa B subunit 1	Homo sapiens	9-18
16140736-7	2005	The HSPG analog heparin completely blocked attachment of the gC ectodomain to Vero cells.	Heparin	16-23	syndecan 2	Mus musculus	4-8
16055320-7	2005	Heparin-modified substrates were found to alter cell morphology through increased adsorption of serum proteins, specifically TGF-beta1.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	125-134
16055320-8	2005	In sum, heparin produced alpha-SMA-positive myofibroblasts through both the de novo production of TGF-beta1, and its localization in the pericellular environment.	Heparin	8-15	transforming growth factor beta 1	Homo sapiens	98-107
16055320-9	2005	The addition of heparin to fibronectin-modified substrates led to a synergistic increase in VIC alpha-SMA expression, produced by the reciprocal binding of fibronectin, heparin, cell-produced TGF-beta1.	Heparin	16-23	fibronectin 1	Homo sapiens	27-38
16055320-9	2005	The addition of heparin to fibronectin-modified substrates led to a synergistic increase in VIC alpha-SMA expression, produced by the reciprocal binding of fibronectin, heparin, cell-produced TGF-beta1.	Heparin	16-23	fibronectin 1	Homo sapiens	156-167
16055320-9	2005	The addition of heparin to fibronectin-modified substrates led to a synergistic increase in VIC alpha-SMA expression, produced by the reciprocal binding of fibronectin, heparin, cell-produced TGF-beta1.	Heparin	16-23	transforming growth factor beta 1	Homo sapiens	192-201
16078853-0	2005	Mechanism of poly(acrylic acid) acceleration of antithrombin inhibition of thrombin: implications for the design of novel heparin mimics.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	52-60
16087794-2	2005	We have demonstrated that vascular effects of ECSOD require an intact heparin-binding domain.	Heparin	70-77	superoxide dismutase 3	Homo sapiens	46-51
16087794-3	2005	A common genetic variant with a substitution in the heparin-binding domain (ECSOD(R213G)) was reported recently to be associated with ischemic heart disease.	Heparin	52-59	superoxide dismutase 3	Homo sapiens	76-81
16078853-1	2005	The bridging mechanism of antithrombin inhibition of thrombin is a dominant mechanism contributing a massive approximately 2500-fold acceleration in the reaction rate and is also a key reason for the clinical usage of heparin.	Heparin	218-225	coagulation factor II, thrombin	Homo sapiens	30-38
16086844-13	2005	CONCLUSION: Endothelial cells injured by high glucose or heparinase I are protected by a combination of insulin, heparin and bFGF, although protection by heparin and/or bFGF was variable.	Heparin	57-64	insulin	Homo sapiens	104-111
16086844-13	2005	CONCLUSION: Endothelial cells injured by high glucose or heparinase I are protected by a combination of insulin, heparin and bFGF, although protection by heparin and/or bFGF was variable.	Heparin	57-64	fibroblast growth factor 2	Homo sapiens	125-129
15863840-7	2005	Moreover, there is a high level of lipoprotein lipase activity in the endothelium of the tissue, which is heparin-releasable.	Heparin	106-113	lipoprotein lipase	Rattus norvegicus	35-53
15985216-4	2005	The stimulatory effect of VEGF165 was not affected by the presence of exogenous heparin, while that of bFGF was further enhanced in the presence of up to 0.1 microg/ml heparin.	Heparin	168-175	fibroblast growth factor 2	Homo sapiens	103-107
15985216-7	2005	Although bFGF was found to bind more strongly to heparin-Sepharose than endostatin, the latter, but not the former, displaced protamine from heparin in solution, which supports the notion that endostatin can compete with bFGF for binding to heparan sulfate in vivo.	Heparin	49-56	fibroblast growth factor 2	Homo sapiens	9-13
16026400-12	2005	Administration of low-molecular-weight heparin may affect CRP production, however, further studies are still needed in order to clarify the exact immunosuppressive action of heparins.	Heparin	39-46	C-reactive protein	Homo sapiens	58-61
15845897-1	2005	Heparin-induced thrombocytopenia (HIT) is a life-threatening, thrombotic disorder associated with development of anti-platelet factor 4 (anti-PF4)/heparin autoantibodies.	Heparin	0-7	platelet factor 4	Mus musculus	142-145
15845897-5	2005	Mice injected with mPF4/heparin, but not mPF4 or heparin alone, developed heparin-dependent autoantibodies that shared serologic and functional characteristics of human HIT antibodies, including preferential binding to mPF4/heparin complexes and causing heparin- and FcRgammaIIA-dependent platelet activation.	Heparin	24-31	platelet factor 4	Mus musculus	19-23
16034135-3	2005	We have previously demonstrated that heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) decreases proinflammatory cytokine IL-8 and NO production in cytokine-stimulated intestinal epithelial cells by interfering with the NF-kappaB signaling pathway.	Heparin	37-44	C-X-C motif chemokine ligand 8	Homo sapiens	146-150
16254626-2	2005	Heparin and chondroitin sulfate produced by thrombin-activated basophils are good candidates for inductors of these processes.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	44-52
16051824-12	2005	Moderate ERK induction with soluble gB was seen only in HMVEC-d. Preincubation of gpK8.1A with heparin or anti-gpK8.1A antibodies inhibited the ERK induction.	Heparin	95-102	mitogen-activated protein kinase 1	Homo sapiens	9-12
16051824-12	2005	Moderate ERK induction with soluble gB was seen only in HMVEC-d. Preincubation of gpK8.1A with heparin or anti-gpK8.1A antibodies inhibited the ERK induction.	Heparin	95-102	mitogen-activated protein kinase 1	Homo sapiens	144-147
15878877-5	2005	On the other hand, apoA-V-dimyristoylphosphatidylcholine disc particles bound to heparin-Sepharose and were specifically eluted upon application of a linear gradient of NaCl.	Heparin	81-88	apolipoprotein A5	Homo sapiens	19-25
15878877-7	2005	ApoA-V showed strong binding to heparin-coated chips, and binding was competed by free heparin.	Heparin	32-39	apolipoprotein A5	Homo sapiens	0-6
15878877-7	2005	ApoA-V showed strong binding to heparin-coated chips, and binding was competed by free heparin.	Heparin	87-94	apolipoprotein A5	Homo sapiens	0-6
15878877-8	2005	ApoA-V enrichment enhanced binding of apoC-II-deficient chylomicrons and VLDL to heparin-coated chips.	Heparin	81-88	apolipoprotein A5	Homo sapiens	0-6
15878877-9	2005	When LPL was first bound to the heparin-coated chip, apoA-V-enriched chylomicrons showed binding.	Heparin	32-39	apolipoprotein A5	Homo sapiens	53-59
15878877-12	2005	Taken together, the results show that apoA-V lipid complexes bind heparin and, when present on TG-rich lipoprotein particles, may promote their association with cell surface heparan sulfate proteoglycans.	Heparin	66-73	apolipoprotein A5	Homo sapiens	38-44
16701826-7	2005	The binding affinity of the peptide for VEGF(165) was ascertained by surface plasmon resonance and compared with the heparin mimic suramin; the peptide binds to VEGF(165) 100-fold stronger than the sulfonated compound.	Heparin	117-124	vascular endothelial growth factor A	Homo sapiens	161-165
16701827-1	2005	Heparin was modified with methacrylate groups, copolymerized with dimethacrylated poly(ethylene glycol), and analyzed as a localized delivery vehicle for bFGF and synthetic extracellular matrix for the differentiation of hMSCs.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	154-158
16701827-5	2005	In addition, the heparin functionalized gels can deliver biologically active bFGF for up to 5 weeks.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	77-81
15936726-5	2005	Furthermore, we could demonstrate that the XT-I interacts strongly with heparin and that this glycosaminoglycan is a predominantly non-competitive inhibitor of the enzyme using the fragment bFGF (1-24) as xylose acceptor.	Heparin	72-79	fibroblast growth factor 2	Homo sapiens	190-194
15949466-1	2005	Pleiotrophin (PTN) is a heparin-binding growth/differentiation inducing cytokine that shares 50% amino acid sequence identity and striking domain homology with Midkine (MK), the only other member of the Ptn/Mk developmental gene family.	Heparin	24-31	pleiotrophin	Homo sapiens	0-12
15949466-1	2005	Pleiotrophin (PTN) is a heparin-binding growth/differentiation inducing cytokine that shares 50% amino acid sequence identity and striking domain homology with Midkine (MK), the only other member of the Ptn/Mk developmental gene family.	Heparin	24-31	pleiotrophin	Homo sapiens	14-17
16039522-3	2005	The minimum heparin binding sequence for FGF1 and FGF2 necessary to promote signaling was investigated.	Heparin	12-19	fibroblast growth factor 1	Homo sapiens	41-45
16039522-3	2005	The minimum heparin binding sequence for FGF1 and FGF2 necessary to promote signaling was investigated.	Heparin	12-19	fibroblast growth factor 2	Homo sapiens	50-54
15925240-0	2005	Capillary zone electrophoresis characterization of low molecular weight heparin binding to interleukin 2.	Heparin	72-79	interleukin 2	Homo sapiens	91-104
15925240-1	2005	A method based on capillary zone electrophoresis (CZE) was used to study the interaction between low molecular weight heparin (LMWH) and interleukin 2 (IL-2).	Heparin	118-125	interleukin 2	Homo sapiens	137-150
15925240-1	2005	A method based on capillary zone electrophoresis (CZE) was used to study the interaction between low molecular weight heparin (LMWH) and interleukin 2 (IL-2).	Heparin	118-125	interleukin 2	Homo sapiens	152-156
16127995-0	2005	[Thrombin-activated fibrinolysis inhibitor and prognosis in patients with heparines treatment unstable angina pectoris].	Heparin	74-83	coagulation factor II, thrombin	Homo sapiens	1-9
15988707-4	2005	Analysis of messenger RNA (mRNA) concentration demonstrated that pyruvate dehydrogenase kinase isoform 4 (PDK4) mRNA, a key negative regulator of glucose oxidation, was increased in all trials with a 24-fold response after Intralipid infusion, 15-fold after saline and heparin infusion, and 9-fold after saline alone.	Heparin	269-276	pyruvate dehydrogenase kinase 4	Homo sapiens	65-104
15988707-4	2005	Analysis of messenger RNA (mRNA) concentration demonstrated that pyruvate dehydrogenase kinase isoform 4 (PDK4) mRNA, a key negative regulator of glucose oxidation, was increased in all trials with a 24-fold response after Intralipid infusion, 15-fold after saline and heparin infusion, and 9-fold after saline alone.	Heparin	269-276	pyruvate dehydrogenase kinase 4	Homo sapiens	106-110
15988269-3	2005	Nevertheless, heparin (a specific thrombin inhibitor) remains the most widely used microvascular irrigant.	Heparin	14-21	coagulation factor II	Rattus norvegicus	34-42
16119279-4	2005	Upon transitioning from heparin-induced thrombocytopenia treatment with direct thrombin inhibitors, argatroban, or lepirudin, careful consideration must be taken to avoid further thrombotic complications.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	79-87
15987622-1	2005	Direct thrombin inhibitors (DTIs) are a new class of therapeutics possessing theoretic advantages over unfractionated heparin (UFH).	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	7-15
15987622-1	2005	Direct thrombin inhibitors (DTIs) are a new class of therapeutics possessing theoretic advantages over unfractionated heparin (UFH).	Heparin	127-130	coagulation factor II, thrombin	Homo sapiens	7-15
15995351-0	2005	P-Selectin-mediated acute inflammation can be blocked by chemically modified heparin, RO-heparin.	Heparin	77-84	selectin, platelet	Mus musculus	0-10
15989807-7	2005	Heparin, C5 and adenosine did not induce any histamine release at concentrations tested, but heparin enhanced histamine release induced by C5a and substance P. CONCLUSION: Trypsin, anti-IgE, CI, FMLP, C5a and substance P can induce histamine release from baosophils, but PAR-2 agonist can not.	Heparin	93-100	complement C5a receptor 1	Homo sapiens	139-142
15989807-7	2005	Heparin, C5 and adenosine did not induce any histamine release at concentrations tested, but heparin enhanced histamine release induced by C5a and substance P. CONCLUSION: Trypsin, anti-IgE, CI, FMLP, C5a and substance P can induce histamine release from baosophils, but PAR-2 agonist can not.	Heparin	93-100	formyl peptide receptor 1	Homo sapiens	195-199
15989807-7	2005	Heparin, C5 and adenosine did not induce any histamine release at concentrations tested, but heparin enhanced histamine release induced by C5a and substance P. CONCLUSION: Trypsin, anti-IgE, CI, FMLP, C5a and substance P can induce histamine release from baosophils, but PAR-2 agonist can not.	Heparin	93-100	complement C5a receptor 1	Homo sapiens	201-204
15989807-8	2005	Heparin can greatly enhance the ability of C5a and substance P to stimulate histamine release, which may be a novel mechanism of amplification of basophil activation signal.	Heparin	0-7	complement C5a receptor 1	Homo sapiens	43-46
16113788-4	2005	Heparin, however, partially relieves this protective effect and at the same time it facilitates the inhibition of the intrinsic thrombin activity by antithrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	128-136
15995351-2	2005	Heparin can bind to P-selectin, and its anti-inflammatory property is mainly due to inhibition of P-selectin.	Heparin	0-7	selectin, platelet	Mus musculus	20-30
15995351-2	2005	Heparin can bind to P-selectin, and its anti-inflammatory property is mainly due to inhibition of P-selectin.	Heparin	0-7	selectin, platelet	Mus musculus	98-108
15797857-1	2005	Heparin affin regulatory peptide (HARP) is an 18-kDa secreted growth factor that has a high affinity for heparin and a potent role on tumor growth and angiogenesis.	Heparin	105-112	pleiotrophin	Homo sapiens	0-32
15913650-0	2005	The oligomeric structure of vaccinia viral envelope protein A27L is essential for binding to heparin and heparan sulfates on cell surfaces: a structural and functional approach using site-specific mutagenesis.	Heparin	93-100	IMV surface protein	Vaccinia virus	60-64
15952792-0	2005	Identification of the heparin-binding region of snake venom vascular endothelial growth factor (VEGF-F) and its blocking of VEGF-A165.	Heparin	22-29	vascular endothelial growth factor A	Homo sapiens	60-94
15952792-0	2005	Identification of the heparin-binding region of snake venom vascular endothelial growth factor (VEGF-F) and its blocking of VEGF-A165.	Heparin	22-29	vascular endothelial growth factor A	Homo sapiens	96-100
15952792-0	2005	Identification of the heparin-binding region of snake venom vascular endothelial growth factor (VEGF-F) and its blocking of VEGF-A165.	Heparin	22-29	vascular endothelial growth factor A	Homo sapiens	124-128
15952792-3	2005	In fact, VEGF-A lacking a C-terminal heparin-binding region exhibits significantly reduced mitogenic activity.	Heparin	37-44	vascular endothelial growth factor A	Homo sapiens	9-15
15952792-4	2005	We recently found novel heparin-binding VEGFs in snake venom, designated VEGF-Fs, which specifically recognize KDR, rather than other VEGF receptors.	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	40-44
15952792-4	2005	We recently found novel heparin-binding VEGFs in snake venom, designated VEGF-Fs, which specifically recognize KDR, rather than other VEGF receptors.	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	73-77
15952792-5	2005	VEGF-Fs virtually lack the C-terminal heparin-binding region when compared with other heparin-binding VEGF subtypes, despite their heparin-binding potential.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	0-4
15952792-5	2005	VEGF-Fs virtually lack the C-terminal heparin-binding region when compared with other heparin-binding VEGF subtypes, despite their heparin-binding potential.	Heparin	86-93	vascular endothelial growth factor A	Homo sapiens	102-106
15952792-5	2005	VEGF-Fs virtually lack the C-terminal heparin-binding region when compared with other heparin-binding VEGF subtypes, despite their heparin-binding potential.	Heparin	86-93	vascular endothelial growth factor A	Homo sapiens	102-106
15952792-7	2005	In this study, we attempted to identify the heparin-binding region of VEGF-F using synthetic peptides.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	70-74
15952792-8	2005	The C-terminal peptide of vammin (one of the VEGF-Fs, 19 residues) bound to heparin with similar affinity as native vammin.	Heparin	76-83	vascular endothelial growth factor A	Homo sapiens	45-49
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	104-111	vascular endothelial growth factor A	Homo sapiens	67-71
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	67-71
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	177-181
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	177-181
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	177-181
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	67-71
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	177-181
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	177-181
15952792-11	2005	These observations demonstrate that the short C-terminal region of VEGF-F functions fully as the active heparin-binding domain and the corresponding peptide specifically blocks VEGF-A165, thus suggesting that the C-terminal heparin-binding region of VEGF-F recognizes similar heparin/heparan sulfate molecules as VEGF-A165.	Heparin	224-231	vascular endothelial growth factor A	Homo sapiens	177-181
15952792-12	2005	The present results will provide novel insight into VEGF-heparin interaction and may facilitate the design of new anti-VEGF drugs based on novel strategies.	Heparin	57-64	vascular endothelial growth factor A	Homo sapiens	52-56
15952792-12	2005	The present results will provide novel insight into VEGF-heparin interaction and may facilitate the design of new anti-VEGF drugs based on novel strategies.	Heparin	57-64	vascular endothelial growth factor A	Homo sapiens	119-123
15924430-15	2005	Tear fluid PLTP was quantitatively bound to Heparin-Sepharose and could be eluted as a single peak by 0.5 M NaCl.	Heparin	44-51	phospholipid transfer protein	Homo sapiens	11-15
15797857-1	2005	Heparin affin regulatory peptide (HARP) is an 18-kDa secreted growth factor that has a high affinity for heparin and a potent role on tumor growth and angiogenesis.	Heparin	105-112	pleiotrophin	Homo sapiens	34-38
15935280-0	2005	Interaction with heparin protects tissue transglutaminase against inactivation by heating and by proteolysis.	Heparin	17-24	transglutaminase 2	Homo sapiens	34-57
15918828-2	2005	Direct thrombin inhibitors are a novel class of drugs that have been developed as an effective alternative mode of anticoagulation in patients who suffer from heparin-induced thrombocytopaenia, and for the management of thromboembolic disorders and acute coronary syndromes.	Heparin	159-166	coagulation factor II, thrombin	Homo sapiens	7-15
15935280-1	2005	The considerable affinity of tissue transglutaminase for heparin was the basis for use of heparin-based affinity matrices for enzyme purification.	Heparin	57-64	transglutaminase 2	Homo sapiens	29-52
15935280-1	2005	The considerable affinity of tissue transglutaminase for heparin was the basis for use of heparin-based affinity matrices for enzyme purification.	Heparin	90-97	transglutaminase 2	Homo sapiens	29-52
15966988-7	2005	In hemodialysis patients, lower doses of epoetin were required for patients receiving low molecular heparin and those with lower iPTH.	Heparin	100-107	erythropoietin	Homo sapiens	41-48
15922935-2	2005	Inspired by the ternary complex formation of heparin with antithrombin III and thrombin, the active pentasaccharide fondaparinux has been succeeded by several clinical candidates, such as SR123781, that have tailor-made factor Xa and thrombin inhibitory activities combined with less aspecific binding (e.g. binding to platelet factor 4 involved in thrombocytopenia).	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	62-70
15922935-2	2005	Inspired by the ternary complex formation of heparin with antithrombin III and thrombin, the active pentasaccharide fondaparinux has been succeeded by several clinical candidates, such as SR123781, that have tailor-made factor Xa and thrombin inhibitory activities combined with less aspecific binding (e.g. binding to platelet factor 4 involved in thrombocytopenia).	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	79-87
16556013-3	2005	These include fibrin formation; binding of heparin to angiogenic growth factors, such as basic fibroblast growth factor and vascular endothelial growth factor; modulation of tissue factor; and perhaps other more important modulatory mechanisms, such as enhanced tissue factor pathway inhibitor (TFPI) release and inhibition of various matrix-degrading enzymes.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	124-158
16082605-1	2005	BACKGROUND: Heparin-induced thrombocytopenia (HIT) can lead to catastrophic thromboembolic complications and requires treatment with an alternative, rapidly active anticoagulant, such as a direct thrombin inhibitor (DTI), either to prevent or treat these complications.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	196-204
15870544-1	2005	Argatroban is a direct thrombin inhibitor used for the treatment of heparin-induced thrombocytopenia.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	23-31
15943814-6	2005	Interleukin-1beta (IL-1beta) alone, or in synergy with FGF-2/heparin strongly induced the gene in 3T3 fibroblasts.	Heparin	61-68	interleukin 1 beta	Mus musculus	0-17
15943814-6	2005	Interleukin-1beta (IL-1beta) alone, or in synergy with FGF-2/heparin strongly induced the gene in 3T3 fibroblasts.	Heparin	61-68	interleukin 1 beta	Mus musculus	19-27
17375473-2	2005	MK and PTN share receptors and biophysical characteristics, such as a heparin-binding property.	Heparin	70-77	midkine	Homo sapiens	0-2
17375473-2	2005	MK and PTN share receptors and biophysical characteristics, such as a heparin-binding property.	Heparin	70-77	pleiotrophin	Homo sapiens	7-10
15968387-6	2005	Direct binding and AT inhibition studies in the presence of heparin revealed that the affinity of heparin for interaction with exosite-2 of des-60-loop thrombin was impaired, though the reactivity of the mutant with AT and other plasma serpins was not impaired, but rather improved approximately 2-fold.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	152-160
15604198-8	2005	Coincubation of TNF-alpha with soluble HS or heparin abolished these synergistic effects.	Heparin	45-52	tumor necrosis factor	Homo sapiens	16-25
15927062-7	2005	In contrast, membrane-permeable late apoptotic neutrophils exhibited strong CRP binding, which comprised both Ca2+-dependent and heparin-inhibitable Ca2+-independent components.	Heparin	129-136	C-reactive protein	Homo sapiens	76-79
15760902-0	2005	Identification and characterization of heparin/heparan sulfate binding domains of the endoglycosidase heparanase.	Heparin	39-46	heparanase	Homo sapiens	102-112
15760902-11	2005	The two heparin/heparan sulfate recognition domains are potentially attractive targets for the development of heparanase inhibitors.	Heparin	8-15	heparanase	Homo sapiens	110-120
15778226-6	2005	Next, we incubated mitochondria with CK2 and either ATP or GTP, in the presence of heparin, a known inhibitor of CK2.	Heparin	83-90	casein kinase 2 beta	Rattus norvegicus	113-116
15778226-7	2005	Heparin inhibited CK2-induced stimulation of mtGAT activity; this inhibition resulted in decreased (32)P-labeling of mtGAT.	Heparin	0-7	casein kinase 2 beta	Rattus norvegicus	18-21
15746105-4	2005	Conversely, heparin blocked thrombin interaction with the A2 subunit and showed a marginal effect on A1 binding.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	28-36
15746105-9	2005	These data suggest the acidic region comprising residues 389-394 in factor VIII A2 domain interacts with thrombin via its heparin-binding exosite and facilitates cleavage at Arg(740) during procofactor activation.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	105-113
15851487-7	2005	Moreover, syndecan-1-positive plasma cells and proteoglycan-rich nonhematopoietic cells displayed high specific, heparin-sensitive binding to APRIL.	Heparin	113-120	TNF superfamily member 13	Homo sapiens	142-147
15705969-2	2005	Although the EGFR ligand, heparin-binding epidermal growth factor-like growth factor (HB-EGF), is known to be released as a result of this stimulation, whether compressive stress enhances expression of other EGFR ligands, and the duration of mechanical compression required to initiate this response, is not known.	Heparin	26-33	epidermal growth factor receptor	Homo sapiens	13-17
15854939-11	2005	Glial injury started after initiation of surgery and peaked at the end of cardiopulmonary bypass with significantly higher concentration of s100beta in the noncoated than in the heparin-coated group (p = 0.008).	Heparin	178-185	S100 calcium binding protein B	Homo sapiens	140-148
15705969-2	2005	Although the EGFR ligand, heparin-binding epidermal growth factor-like growth factor (HB-EGF), is known to be released as a result of this stimulation, whether compressive stress enhances expression of other EGFR ligands, and the duration of mechanical compression required to initiate this response, is not known.	Heparin	26-33	epidermal growth factor receptor	Homo sapiens	208-212
15845669-0	2005	An evaluation of the effects of a standard heparin dose on thrombin inhibition during cardiopulmonary bypass in neonates.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	59-67
15902370-5	2005	The bivalent direct thrombin inhibitor (DTI) lepirudin is used for anticoagulation of patients with heparin-induced thrombocytopenia (HIT) as is the monovalent DTI argatroban.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	20-28
15659705-8	2005	In expanded COCs and differentiated granulosa cells, FSH induced expression of ADAMTS4 and versican message and protein, whereas increased levels of ADAMTS1 protein was observed in the media of granulosa cells where it was stabilized by heparin in this in vitro system.	Heparin	237-244	a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1	Mus musculus	149-156
15785094-0	2005	Heparin regulates transcription of endothelin-1 gene in endothelial cells.	Heparin	0-7	endothelin 1	Homo sapiens	35-47
15722560-2	2005	In HepG2 cells infected with adenovirus encoding human EL, the mature EL was detectable in the cell lysates and heparin-releasable fractions.	Heparin	112-119	lipase G, endothelial type	Homo sapiens	55-57
15722560-2	2005	In HepG2 cells infected with adenovirus encoding human EL, the mature EL was detectable in the cell lysates and heparin-releasable fractions.	Heparin	112-119	lipase G, endothelial type	Homo sapiens	70-72
15860733-7	2005	In accordance with this notion, affinity chromatography showed that recombinant cathepsin E bound strongly to heparin under acidic conditions (the conditions prevailing in mast-cell granules) but not at neutral pH.	Heparin	110-117	cathepsin E	Mus musculus	80-91
15785094-6	2005	Gel mobility shift assays using oligonucleotides encoding the ET-1 AP-1 and ET-1 GATA sites confirmed that both AP-1 and GATA binding activities in BAEC nuclear extract were markedly inhibited by heparin.	Heparin	196-203	endothelin 1	Homo sapiens	62-66
15785094-6	2005	Gel mobility shift assays using oligonucleotides encoding the ET-1 AP-1 and ET-1 GATA sites confirmed that both AP-1 and GATA binding activities in BAEC nuclear extract were markedly inhibited by heparin.	Heparin	196-203	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	67-71
15785094-6	2005	Gel mobility shift assays using oligonucleotides encoding the ET-1 AP-1 and ET-1 GATA sites confirmed that both AP-1 and GATA binding activities in BAEC nuclear extract were markedly inhibited by heparin.	Heparin	196-203	endothelin 1	Homo sapiens	76-80
15785094-4	2005	ET-1 mRNA expression was significantly suppressed by heparin in a dose-dependent manner.	Heparin	53-60	endothelin 1	Homo sapiens	0-4
15785094-6	2005	Gel mobility shift assays using oligonucleotides encoding the ET-1 AP-1 and ET-1 GATA sites confirmed that both AP-1 and GATA binding activities in BAEC nuclear extract were markedly inhibited by heparin.	Heparin	196-203	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	112-116
15866045-6	2005	Heparin enhanced Sema3A"s binding to neuropilin-1-expressing cells and potentiated its growth cone collapsing activity.	Heparin	0-7	neuropilin 1	Mus musculus	37-49
15785094-7	2005	Western blot analyses indicated that heparin completely blocked extracellular signal-regulated kinase (ERK) activation, and inhibiting ERK activity resulted in loss of heparin-dependent inhibition of the ET-1 gene.	Heparin	37-44	mitogen-activated protein kinase 1	Homo sapiens	64-101
15785094-7	2005	Western blot analyses indicated that heparin completely blocked extracellular signal-regulated kinase (ERK) activation, and inhibiting ERK activity resulted in loss of heparin-dependent inhibition of the ET-1 gene.	Heparin	37-44	mitogen-activated protein kinase 1	Homo sapiens	103-106
15785094-7	2005	Western blot analyses indicated that heparin completely blocked extracellular signal-regulated kinase (ERK) activation, and inhibiting ERK activity resulted in loss of heparin-dependent inhibition of the ET-1 gene.	Heparin	168-175	mitogen-activated protein kinase 1	Homo sapiens	135-138
15785094-7	2005	Western blot analyses indicated that heparin completely blocked extracellular signal-regulated kinase (ERK) activation, and inhibiting ERK activity resulted in loss of heparin-dependent inhibition of the ET-1 gene.	Heparin	168-175	endothelin 1	Homo sapiens	204-208
15839662-1	2005	FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide.	Heparin	75-82	fibroblast growth factor 1	Homo sapiens	0-5
15718352-0	2005	Higher concentrations of heparin and hirudin are required to inhibit thrombin generation in tissue factor-activated cord plasma than in adult plasma.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	69-77
15718352-5	2005	After strong activation with high amounts of TF (30 microM), the thrombin potential was significantly more suppressed in cord plasma compared with adult plasma in the presence of 0.4 IE/mL heparin (-92 versus -75%; p &lt; 0.01) and in the presence of 2 IE/mL hirudin (-18 versus -8%; p &lt; 0.01).	Heparin	189-196	coagulation factor II, thrombin	Homo sapiens	65-73
15718352-6	2005	In contrast, after weak activation with low amounts of TF (30 pM), the thrombin potential was significantly more suppressed in adult plasma compared with neonatal plasma in the presence of 0.025 IE/mL heparin (-93 versus -8%; p &lt; 0.01) and in the presence of 2 IE/mL hirudin (-89 versus -48%; p &lt; 0.01).	Heparin	201-208	coagulation factor II, thrombin	Homo sapiens	71-79
15866365-1	2005	Midkine (MK) is a heparin binding growth factor and promotes growth, survival and migration of various cells including neurons.	Heparin	18-25	midkine	Homo sapiens	0-7
15866365-1	2005	Midkine (MK) is a heparin binding growth factor and promotes growth, survival and migration of various cells including neurons.	Heparin	18-25	midkine	Homo sapiens	9-11
15839662-2	2005	The first direct NMR determination of the conformation of a conformationally flexible heparin-like hexasaccharide bound to a key receptor, FGF-1, is described.	Heparin	86-93	fibroblast growth factor 1	Homo sapiens	139-144
15848171-0	2005	The cell surface receptor G6b, a member of the immunoglobulin superfamily, binds heparin.	Heparin	81-88	megakaryocyte and platelet inhibitory receptor G6b	Homo sapiens	26-29
15731113-0	2005	Regulation of vascular smooth muscle proliferation by heparin: inhibition of cyclin-dependent kinase 2 activity by p27(kip1).	Heparin	54-61	zinc ribbon domain containing 2	Homo sapiens	115-118
15731113-5	2005	Our results indicate that the heparin-induced block in G(1) to S phase transition is imposed by p27(kip1)-mediated inhibition of cyclin-dependent kinase 2 activity.	Heparin	30-37	zinc ribbon domain containing 2	Homo sapiens	96-99
15731113-6	2005	Further analysis of p27(kip1) mRNA levels showed that the increase in p27(kip1) protein levels in heparin-treated VSMC occurs at posttranscriptional levels.	Heparin	98-105	zinc ribbon domain containing 2	Homo sapiens	20-23
15731113-6	2005	Further analysis of p27(kip1) mRNA levels showed that the increase in p27(kip1) protein levels in heparin-treated VSMC occurs at posttranscriptional levels.	Heparin	98-105	zinc ribbon domain containing 2	Homo sapiens	70-73
15848171-2	2005	In this study, we show using a variety of techniques that the extracellular domain of the G6b protein, containing a single Ig-like domain, binds to heparin with high affinity.	Heparin	148-155	megakaryocyte and platelet inhibitory receptor G6b	Homo sapiens	90-93
15848171-5	2005	The observed interaction between G6b and heparin is strongly salt dependent suggesting a mainly electrostatic interaction.	Heparin	41-48	megakaryocyte and platelet inhibitory receptor G6b	Homo sapiens	33-36
15848171-6	2005	Heparin might modulate the interaction of G6b with its as yet unidentified protein ligand.	Heparin	0-7	megakaryocyte and platelet inhibitory receptor G6b	Homo sapiens	42-45
15695515-4	2005	Moreover, these protein-protein interactions are dependent on the ionic strength of the medium and are inhibited by heparin, and the kinetics of binding of FGF-2, FGF-4 and HGF/SF to Npn-1 are characterized by fast association rate constants (270,000-1,600,000 m(-1) s(-1)).	Heparin	116-123	fibroblast growth factor 4	Homo sapiens	163-168
15741074-5	2005	Consecutive binding of the thrombin inhibitors heparin, antithrombin III or the heparin-antithrombin III complex to the immobilized thrombin molecules, and binding of a ternary complex of heparin, anithrombin III, and thrombin to aptamers was evaluated.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	27-35
15741074-7	2005	Binding of heparin activated the formation of the inhibitory complex of antithrombin III with thrombin about 2.7-fold.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	76-84
15810091-1	2005	AIM: Human heparanase is an endo-D-glucuronidase that degrades heparan sulfate/heparin and has been implicated in a variety of biological processes.	Heparin	79-86	heparanase	Homo sapiens	11-21
15773911-7	2005	Although Abeta binds to heparin-binding sequence of VEGF, it does not bind to other heparin-binding growth factors except midkine.	Heparin	24-31	amyloid beta precursor protein	Homo sapiens	9-14
15590773-12	2005	We speculate that the template mechanism may predominate over the allosteric effect in the case of the linear sulfated fucan inactivation of thrombin in the presence of heparin cofactor II.	Heparin	169-176	coagulation factor II, thrombin	Homo sapiens	141-149
15773911-7	2005	Although Abeta binds to heparin-binding sequence of VEGF, it does not bind to other heparin-binding growth factors except midkine.	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	52-56
15764700-6	2005	The intramolecular interaction between pY783 and SH2(C) induces a rearrangement of surface charge such that PLC-gamma1 molecules phosphorylated at Y783 are retained more strongly by heparin resins than are unphosphorylated molecules.	Heparin	182-189	phospholipase C gamma 1	Homo sapiens	108-118
15644496-3	2005	Soluble glycosaminoglycans such as heparin and heparan sulfate bind gp120 via V3 and, possibly, a CD4-induced domain.	Heparin	35-42	CD4 molecule	Homo sapiens	98-101
15644496-7	2005	In vitro, and in conditions in which gp120 could bind CD4, heparin and heparan sulfate reduced PDI-mediated gp120 reduction by approximately 80%.	Heparin	59-66	CD4 molecule	Homo sapiens	54-57
15644496-7	2005	In vitro, and in conditions in which gp120 could bind CD4, heparin and heparan sulfate reduced PDI-mediated gp120 reduction by approximately 80%.	Heparin	59-66	protein disulfide isomerase family A member 2	Homo sapiens	95-98
15767480-5	2005	Tyrosine phosphorylation of FGFR1 induced by FGF was examined by immunoprecipitation after stimulation with FGF-1 in the presence or absence of heparin.	Heparin	144-151	fibroblast growth factor receptor 1	Homo sapiens	28-33
15781750-10	2005	Coagulation marker analysis at 6 and 12 hours after PCI demonstrated that fondaparinux was superior to UFH in inducing a sustained reduction in markers of thrombin generation, as measured by prothrombin fragment F1.2 (P=0.02).	Heparin	103-106	coagulation factor II, thrombin	Homo sapiens	155-163
15868907-7	2005	Studies performed with synthetic peptides derived from the TSP-1 sequence indicated that two heparin-binding peptides, Hep-I and GGWSHW, located within the NH2-terminal and type 1 repeats respectively, were strong inducers of apoptosis of HL-60 and NB4 cells, suggesting that cell surface heparan sulfate molecules might be involved in the apoptotic effect of TSP-1 on promyelocytic cells.	Heparin	93-100	thrombospondin 1	Homo sapiens	59-64
15868907-7	2005	Studies performed with synthetic peptides derived from the TSP-1 sequence indicated that two heparin-binding peptides, Hep-I and GGWSHW, located within the NH2-terminal and type 1 repeats respectively, were strong inducers of apoptosis of HL-60 and NB4 cells, suggesting that cell surface heparan sulfate molecules might be involved in the apoptotic effect of TSP-1 on promyelocytic cells.	Heparin	93-100	thrombospondin 1	Homo sapiens	360-365
15847948-11	2005	Decline of EC SOD activity was observed after administration of repeated doses of heparin both in the examined and in the control groups.	Heparin	82-89	superoxide dismutase 3	Homo sapiens	11-17
15736967-1	2005	Human tryptase-beta (HTbeta) is a serine protease with an atypical tetrameric structure and an unusual dependence on heparin binding or high salt for functional and structural stability.	Heparin	117-124	zinc finger protein 148	Homo sapiens	6-28
15736967-4	2005	Using small irreversible or competitive inhibitors of HTbeta as stabilizing ligands, we were able to examine tetramer stability under inactivating (decay) conditions in the absence of heparin and to define further the process of spontaneous inactivation.	Heparin	184-191	zinc finger protein 148	Homo sapiens	54-60
15736967-8	2005	At high concentrations of si-HTbeta (4-5 microM), the binding of inhibitor alone provided sufficient free energy for complete reactivation and tetramer stabilization, whereas at low si-HTbeta concentration (0.1 microM) where the destabilized tetramer would be mostly dissociated, reactivation required more free energy which was provided by the binding of both an inhibitor and heparin.	Heparin	378-385	zinc finger protein 148	Homo sapiens	29-35
15767480-5	2005	Tyrosine phosphorylation of FGFR1 induced by FGF was examined by immunoprecipitation after stimulation with FGF-1 in the presence or absence of heparin.	Heparin	144-151	fibroblast growth factor 1	Homo sapiens	28-31
15767480-9	2005	The FGFR1 was differentially phosphorylated in a time- and heparin-dependent manner by FGF-1.	Heparin	59-66	fibroblast growth factor receptor 1	Homo sapiens	4-9
15767480-9	2005	The FGFR1 was differentially phosphorylated in a time- and heparin-dependent manner by FGF-1.	Heparin	59-66	fibroblast growth factor 1	Homo sapiens	87-92
15534875-10	2005	The protease binds to heparin and its ability to degrade IGFBP-5 is blocked in the presence of heparin.	Heparin	22-29	insulin like growth factor binding protein 5	Homo sapiens	57-64
15876859-0	2005	Inhibition of P-glycoprotein-mediated multidrug resistance by unfractionated heparin: a new potential chemosensitizer for cancer therapy.	Heparin	77-84	ATP binding cassette subfamily B member 1	Homo sapiens	14-28
15876859-2	2005	In the present study, we investigated the ability of unfractionated heparin (UFH) to inhibit P-glycoprotein (Pgp)-mediated multidrug resistance (MDR) on human breast cancer cell line (MDA-MB231) and its doxo-resistant subline.	Heparin	68-75	ATP binding cassette subfamily B member 1	Homo sapiens	93-107
15876859-2	2005	In the present study, we investigated the ability of unfractionated heparin (UFH) to inhibit P-glycoprotein (Pgp)-mediated multidrug resistance (MDR) on human breast cancer cell line (MDA-MB231) and its doxo-resistant subline.	Heparin	68-75	ATP binding cassette subfamily B member 1	Homo sapiens	109-112
15876859-2	2005	In the present study, we investigated the ability of unfractionated heparin (UFH) to inhibit P-glycoprotein (Pgp)-mediated multidrug resistance (MDR) on human breast cancer cell line (MDA-MB231) and its doxo-resistant subline.	Heparin	77-80	ATP binding cassette subfamily B member 1	Homo sapiens	93-107
15876859-2	2005	In the present study, we investigated the ability of unfractionated heparin (UFH) to inhibit P-glycoprotein (Pgp)-mediated multidrug resistance (MDR) on human breast cancer cell line (MDA-MB231) and its doxo-resistant subline.	Heparin	77-80	ATP binding cassette subfamily B member 1	Homo sapiens	109-112
15876859-4	2005	We analysed the Pgp function by calcein acetoxymethylester (calcein-AM) uptake, a fluorescent marker substrate, before and after in vitro exposure to UFH at clinically achievable dose of 20 U/ml.	Heparin	150-153	ATP binding cassette subfamily B member 1	Homo sapiens	16-19
15769511-0	2005	Structural observation of complexes of FGF-2 and regioselectively desulfated heparin in aqueous solutions.	Heparin	77-84	fibroblast growth factor 2	Homo sapiens	39-44
15769511-2	2005	In the FGF-2-native heparin complex, the global FGF-2 molecules appeared to attach along heparin chain as strained unilaterally.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	7-12
15769511-2	2005	In the FGF-2-native heparin complex, the global FGF-2 molecules appeared to attach along heparin chain as strained unilaterally.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	48-53
15769511-2	2005	In the FGF-2-native heparin complex, the global FGF-2 molecules appeared to attach along heparin chain as strained unilaterally.	Heparin	89-96	fibroblast growth factor 2	Homo sapiens	7-12
15769511-2	2005	In the FGF-2-native heparin complex, the global FGF-2 molecules appeared to attach along heparin chain as strained unilaterally.	Heparin	89-96	fibroblast growth factor 2	Homo sapiens	48-53
15769511-4	2005	On the other hand, 2-O-desulfated heparin did not indicate the aggregation with FGF-2, indicating that the sulfate groups at O-2 of iduronate residues in heparin is most essential for association with FGF-2.	Heparin	154-161	fibroblast growth factor 2	Homo sapiens	201-206
15583000-0	2005	Two-step mechanism of binding of apolipoprotein E to heparin: implications for the kinetics of apolipoprotein E-heparan sulfate proteoglycan complex formation on cell surfaces.	Heparin	53-60	apolipoprotein E	Homo sapiens	33-49
15583000-0	2005	Two-step mechanism of binding of apolipoprotein E to heparin: implications for the kinetics of apolipoprotein E-heparan sulfate proteoglycan complex formation on cell surfaces.	Heparin	53-60	apolipoprotein E	Homo sapiens	95-111
15583000-2	2005	ApoE interacts predominantly with heparin through the N-terminal binding site spanning the residues around 136-150.	Heparin	34-41	apolipoprotein E	Homo sapiens	0-4
15583000-3	2005	In this work, surface plasmon resonance analysis was employed to investigate how amphipathic alpha-helix properties and basic residue organization in this region modulate binding of apoE to heparin.	Heparin	190-197	apolipoprotein E	Homo sapiens	182-186
15583000-4	2005	The apoE/heparin interaction involves a two-step process; apoE initially binds to heparin with fast association and dissociation rates, followed by a step exhibiting much slower kinetics.	Heparin	9-16	apolipoprotein E	Homo sapiens	4-8
15583000-4	2005	The apoE/heparin interaction involves a two-step process; apoE initially binds to heparin with fast association and dissociation rates, followed by a step exhibiting much slower kinetics.	Heparin	9-16	apolipoprotein E	Homo sapiens	58-62
15583000-4	2005	The apoE/heparin interaction involves a two-step process; apoE initially binds to heparin with fast association and dissociation rates, followed by a step exhibiting much slower kinetics.	Heparin	82-89	apolipoprotein E	Homo sapiens	4-8
15583000-4	2005	The apoE/heparin interaction involves a two-step process; apoE initially binds to heparin with fast association and dissociation rates, followed by a step exhibiting much slower kinetics.	Heparin	82-89	apolipoprotein E	Homo sapiens	58-62
15583000-9	2005	In addition, disruption of the alpha-helix structure in the apoE heparin binding region led to an increased favorable free energy of binding in the second step, suggesting that hydrophobic interactions contribute to the second binding step.	Heparin	65-72	apolipoprotein E	Homo sapiens	60-64
15699163-6	2005	The presence of clinically relevant heparin concentrations in human whole blood increased LPS-induced production of the proinflammatory cytokine IL-8.	Heparin	36-43	C-X-C motif chemokine ligand 8	Homo sapiens	145-149
15744060-0	2005	Involvement of Ca2+/calmodulin-dependent protein kinase II in heparin-stimulated release of hepatic lipase activity from rat hepatocytes.	Heparin	62-69	lipase C, hepatic type	Rattus norvegicus	92-106
15744060-1	2005	The release of hepatic lipase (HTGL), which is responsible for the hydrolysis of lipoprotein triacylglyceride, produced by heparin from the isolated rat hepatocytes in primary culture has been examined.	Heparin	123-130	lipase C, hepatic type	Rattus norvegicus	15-29
15534875-10	2005	The protease binds to heparin and its ability to degrade IGFBP-5 is blocked in the presence of heparin.	Heparin	95-102	insulin like growth factor binding protein 5	Homo sapiens	57-64
15694965-7	2005	Two isoforms of hSA-14 (pI 6.0 and 8.4) had affinity to heparin.	Heparin	56-63	albumin	Homo sapiens	16-19
15706030-8	2005	The use of a direct thrombin inhibitor in treatment should be considered early if a diagnosis of heparin-induced thrombocytopenia is possible.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	20-28
15719581-0	2005	Direct thrombin inhibitors in heparin-induced thrombocytopenia.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	7-15
15661045-4	2005	Heparin has been shown to activate DC by signalling through Toll-like receptor 4 (TLR4) and nuclear factor (NF)-kappaB.	Heparin	0-7	nuclear factor kappa B subunit 1	Homo sapiens	92-118
15668394-4	2005	In vitro, alpha1LG1-3 domains bind integrins, and alpha1LG4 binds dystroglycan, heparin, and sulfatides.	Heparin	80-87	cholinergic receptor, nicotinic, alpha polypeptide 3	Mus musculus	50-59
15670034-6	2005	However, when patients were stratified by IL-1RN genotype, LMWH was superior to UFH in reducing Delta vWF only in allele *2 carriers (0.51 iU mL(-1) vs. 1.37, P &lt; 0.01), but not in non-carriers (- 0.03 iU mL(-1) vs. 0.15, P = NS).	Heparin	80-83	von Willebrand factor	Homo sapiens	102-105
15362977-0	2005	The high concentration of Arg213--&gt;Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities.	Heparin	129-136	superoxide dismutase 3	Homo sapiens	42-76
15548541-0	2005	Crystal structure of thrombin bound to heparin.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	21-29
15548541-5	2005	Here we report the 1.85-A structure of human alpha-thrombin bound to a heparin fragment of eight monosaccharide units in length.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	51-59
15856910-3	2005	Heparin administration increased lipoprotein lipase activity, high-density lipoprotein (HDL) concentration in the blood, and haptoglobin messenger RNA content of the liver.	Heparin	0-7	haptoglobin	Rattus norvegicus	125-136
15362977-0	2005	The high concentration of Arg213--&gt;Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities.	Heparin	129-136	superoxide dismutase 3	Homo sapiens	78-84
15362977-1	2005	The C-terminal region of EC-SOD (extracellular superoxide dismutase) mediates the binding to both heparin/heparan sulphate and type I collagen.	Heparin	98-105	superoxide dismutase 3	Homo sapiens	25-31
15362977-1	2005	The C-terminal region of EC-SOD (extracellular superoxide dismutase) mediates the binding to both heparin/heparan sulphate and type I collagen.	Heparin	98-105	superoxide dismutase 3	Homo sapiens	33-67
15362977-3	2005	This relatively common mutation affects the heparin affinity, and the concentration of EC-SOD in the plasma of R213G homozygous individuals is increased 10- to 30-fold.	Heparin	44-51	superoxide dismutase 3	Homo sapiens	87-93
15362977-4	2005	In the present study we confirm, using R213G EC-SOD purified from a homozygous individual, that the heparin affinity is reduced.	Heparin	100-107	superoxide dismutase 3	Homo sapiens	45-51
15362977-7	2005	We conclude that the increased concentration of EC-SOD in the plasma of R213G carriers is caused by a reduction in both heparin and collagen affinities.	Heparin	120-127	superoxide dismutase 3	Homo sapiens	48-54
15819171-0	2005	Effect of heparins on thrombin generation in hemophilic plasma supplemented with FVIII, FVIIa, or FEIBA.	Heparin	10-18	coagulation factor II, thrombin	Homo sapiens	22-30
15620727-4	2005	Heparin also potenciated Ang II-induced activation for ERK1/2 and p38.	Heparin	0-7	mitogen-activated protein kinase 3	Homo sapiens	55-61
15620727-4	2005	Heparin also potenciated Ang II-induced activation for ERK1/2 and p38.	Heparin	0-7	mitogen-activated protein kinase 1	Homo sapiens	66-69
15671997-7	2005	In villous trophoblast, heparin increased Bcl-2 and cytokeratin 18 protein expression.	Heparin	24-31	BCL2 apoptosis regulator	Homo sapiens	42-47
15782857-13	2005	Heparin in the interstitial tissue of the wound surface blocks the conversion of fibrinogen to fibrin.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	81-91
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	37-45
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	37-45
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	37-45
15819171-5	2005	Covalent anti-thrombin-heparin may give a greater anticoagulant response in hemophilic plasma supplemented with factor VIII or factor VIIa than with factor eight inhibitor bypassing agent.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	14-22
15528194-7	2005	Pretreatment of muscle cells with chlorate that blocks all sulfation or with an siRNA that selectively blocks N-sulfation significantly reduced erbB receptor activation by neuregulin-1 but had no effect on the activity of neuregulin-1 that lacks the heparin-binding domain.	Heparin	250-257	epidermal growth factor receptor	Homo sapiens	144-148
15328075-6	2005	In contrast, AMPK activators, like perhexiline and oligomycin, produced a significant elevation in heparin-releasable LPL activity.	Heparin	99-106	protein kinase AMP-activated catalytic subunit alpha 2	Rattus norvegicus	13-17
15328075-6	2005	In contrast, AMPK activators, like perhexiline and oligomycin, produced a significant elevation in heparin-releasable LPL activity.	Heparin	99-106	lipoprotein lipase	Rattus norvegicus	118-121
15991797-8	2005	A sample stability investigation with different sample specimens revealed that intact proinsulin is stable for two days at room temperature in EDTA whole blood and heparin whole blood tubes without centrifugation, while serum samples should be centrifuged immediately and frozen to retain intact proinsulin concentrations.	Heparin	164-171	insulin	Homo sapiens	86-96
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	37-45
16305518-3	2005	This paper (a) reviews why thrombin is an ideal target for new anticoagulants, (b) describes the pharmacological profiles of the various direct thrombin inhibitors, (c) outlines the potential mechanistic advantages of parenteral direct thrombin inhibitors over heparin, (d) defines the potential benefits of ximelagatran, the first orally active direct thrombin inhibitor, over vitamin K antagonists, and (e) provides clinical perspective on the strengths and weaknesses of the various parenteral and oral direct thrombin inhibitors.	Heparin	261-268	coagulation factor II, thrombin	Homo sapiens	27-35
16305521-2	2005	Despite its limitations, such as its scarce ability to activate bound thrombin and its unpredictable pharmacological response, heparin is the most widely used drug for this purpose.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	70-78
15471966-1	2005	Local regulation of pituitary FSH secretion and many other cellular processes by follistatin (FS) can be ascribed to its potent ability to bind and bioneutralize activin, in conjunction with binding to cell surface heparan-sulfate proteoglycans through a basic heparin-binding sequence (HBS; residues 75-86) in the first of the three FS domains.	Heparin	261-268	follistatin	Homo sapiens	81-92
16305521-3	2005	Direct thrombin inhibitors are biologically superior to heparin principally because they inhibit clot-bound and circulating thrombin without interacting with other plasma proteins.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	124-132
16305522-0	2005	Direct thrombin inhibitors for treatment of heparin induced thrombocytopenia, deep vein thrombosis and atrial fibrillation.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	7-15
15471966-10	2005	Introduction of the full domain from FS conferred heparin binding to FSTL3, but activin binding was abolished.	Heparin	50-57	follistatin like 3	Homo sapiens	69-74
16114264-8	2005	The clusterisation of AChE depends upon ColQ through three sites of interactions: two different heparin binding domains in the collagen domain interact with heparan sulfate proteoglycan particularly the perlecan and the C-terminal non collagenic domain interacts with MuSK, the tyrosine kinase receptor organiser of the neuromuscular junction.	Heparin	96-103	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
15557391-0	2005	Low-molecular-weight heparin lowers the recurrence rate of preeclampsia and restores the physiological vascular changes in angiotensin-converting enzyme DD women.	Heparin	21-28	angiotensin I converting enzyme	Homo sapiens	123-152
15490481-4	2005	The soluble form of HB-EGF-AP bound to heparin and exhibited potent biological activity as measured by DNA synthesis assay.	Heparin	39-46	heparin-binding EGF-like growth factor	Rattus norvegicus	20-26
15665568-3	2005	Recent studies reported that epidermal growth factor receptor (EGFR) could be activated through heparin binding- EGF cleavage by metalloproteinases.	Heparin	96-103	epidermal growth factor receptor	Homo sapiens	29-61
16353041-17	2005	The use of TIC in UFH treated pts was associated with indirect signs of decreased thrombin activity and some inhibition of fibrinolysis while the use of CL in enoxaparin treated pts was associated with signs of activation of fibrinolysis.	Heparin	18-21	coagulation factor II, thrombin	Homo sapiens	82-90
15634279-2	2005	The protein has three heparin-binding sites, is synthesized primarily in the liver and copurifies from platelets with thrombospondin-1.	Heparin	22-29	thrombospondin 1	Homo sapiens	118-134
15665568-3	2005	Recent studies reported that epidermal growth factor receptor (EGFR) could be activated through heparin binding- EGF cleavage by metalloproteinases.	Heparin	96-103	epidermal growth factor receptor	Homo sapiens	63-67
15632895-5	2004	METHODS: The Clinical Trial of Reviparin and Metabolic Modulation in Acute Myocardial Infarction Treatment and Evaluation-Estudios Clinicos Latino America (CREATE-ECLA) study is a randomized controlled trial in ST-elevation AMI patients evaluating a 24-hour infusion of Glucose-Insulin-Potassium (GIK) intravenous vs usual care (control) on 30-day mortality in 20,000 patients from 21 countries.	Heparin	31-40	insulin	Homo sapiens	278-285
15990442-2	2005	Extracellular superoxide dismutase (EC-SOD), localized on the endothelial cell surface, plays an important role in reducing oxidative stress especially in the vessels by binding to the endothelial cell surface via the heparin-binding domain.	Heparin	218-225	superoxide dismutase 3	Homo sapiens	0-34
15990442-2	2005	Extracellular superoxide dismutase (EC-SOD), localized on the endothelial cell surface, plays an important role in reducing oxidative stress especially in the vessels by binding to the endothelial cell surface via the heparin-binding domain.	Heparin	218-225	superoxide dismutase 3	Homo sapiens	36-42
16707926-0	2005	Identification and localization of heparin-binding region of snake venom VEGF and its blocking of VEGF-A165.	Heparin	35-42	vascular endothelial growth factor A	Homo sapiens	73-77
16707926-0	2005	Identification and localization of heparin-binding region of snake venom VEGF and its blocking of VEGF-A165.	Heparin	35-42	vascular endothelial growth factor A	Homo sapiens	98-102
16707926-3	2005	Indeed, the mitogenic potency of VEGF-A165 lacking the C-terminal heparin-binding region is less than 1% compared with intact VEGF-A165.	Heparin	66-73	vascular endothelial growth factor A	Homo sapiens	33-37
16707926-4	2005	We previously found novel heparin-binding VEGFs, designated VEGF-F that specifically recognizes KDR in snake venoms.	Heparin	26-33	vascular endothelial growth factor A	Homo sapiens	42-46
16707926-5	2005	VEGF-Fs almost completely lack the C-terminal heparin-binding region compared with VEGF-A165, despite their heparin-binding potential.	Heparin	46-53	vascular endothelial growth factor A	Homo sapiens	0-4
16707926-6	2005	In this study, we attempted to identify the heparin-binding region of VEGF-F using synthetic peptides.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	70-74
16707926-7	2005	We have demonstrated that the heparin-binding site of VEGF-F is located in its C-terminal region, particularly localized on the N-terminal portion of this region.	Heparin	30-37	vascular endothelial growth factor A	Homo sapiens	54-58
15501822-7	2004	Interestingly, binding of the polyanion heparin also leads to release of the C terminus of beta-arrestin 2; however, heparin and V(2)R-pp have different binding site(s) and/or induce different conformational changes in beta-arrestin 2.	Heparin	40-47	arrestin beta 2	Homo sapiens	91-106
15501822-7	2004	Interestingly, binding of the polyanion heparin also leads to release of the C terminus of beta-arrestin 2; however, heparin and V(2)R-pp have different binding site(s) and/or induce different conformational changes in beta-arrestin 2.	Heparin	40-47	arrestin beta 2	Homo sapiens	219-234
15604266-5	2004	In contrast, inhibition of vascular endothelial growth factor-A-induced chorioallantoic membrane angiogenesis by endostatin was only dependent on the minor heparin-binding site (R193/194).	Heparin	156-163	vascular endothelial growth factor A	Homo sapiens	27-63
15381701-7	2004	Surprisingly, mammalian TSG did not bind heparin unless prebound to Chordin and/or BMP-4, although Drosophila TSG has been reported to bind heparin on its own.	Heparin	140-147	twisted gastrulation	Drosophila melanogaster	110-113
15532057-5	2004	The FGF-2 effect can be abolished by heparin, suggesting the involvement of heparan sulfate proteoglycans (HSPGs) in growth factor signaling.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	4-9
15572165-4	2004	Recent evidence support this notion: first, the presence of two heparin-binding domains in ColQ that interact with heparan sulfate proteoglycans (HSPGs) at the synaptic basal lamina; and second, a knockout mouse for perlecan, a HSPG concentrated in nerve-muscle contact, in which absence of asymmetric AChE at the NMJ is observed.	Heparin	64-71	syndecan 2	Mus musculus	146-150
15767980-0	2004	Differential regulation of thrombin activatable fibrinolytic inhibitor by low molecular weight heparins.	Heparin	95-103	coagulation factor II, thrombin	Homo sapiens	27-35
15733401-1	2004	OBJECTIVE: To investigate the clinical effect and safety of heparin in treating fetal growth restriction (FGR).	Heparin	60-67	FGR proto-oncogene, Src family tyrosine kinase	Homo sapiens	106-109
15648269-2	2004	METHODS: Insoluble lysozyme-heparin complexes were formed at pH 7.2 and the binding stoichiometry determined using a solution depletion method.	Heparin	28-35	lysozyme	Homo sapiens	19-27
15648269-5	2004	At low ionic strength (I approximately 0.01) about 11 lysozyme molecules could bind to a 17 kDa heparin chain, 3 to a 6 kDa chain, and less than 2 to a 3 kDa chain.	Heparin	96-103	lysozyme	Homo sapiens	54-62
15648269-6	2004	At higher ionic strength (I approximately 0.1), only 7 lysozyme molecules could bind to a 18 kDa heparin chain..	Heparin	97-104	lysozyme	Homo sapiens	55-63
15815878-6	2004	In a multiple logistic regression model that included inflammatory markers and clinical risk factors, antibody to PF4/heparin was a strong predictor of 30 day MI (odds ratio: 9.0; 95% confidence intervals 2.1-38.6; p &lt; 0.01), with IL-6 being the only other predictor (odds ratio: 1.1; 95% confidence intervals 1.0-1.2; p = 0.03).	Heparin	118-125	interleukin 6	Homo sapiens	234-238
15526371-6	2004	The tetrasaccharide with Mr of 1,142, produced by depolymerizing heparin with hydrogen peroxide, had the strongest inhibitory effect on the secretion of IL-4.	Heparin	65-72	interleukin 4	Homo sapiens	153-157
15471890-8	2004	Anosmin binds to the GN11 cell surface by interacting with the heparan sulphate proteoglycans, and the chemotactic effect of anosmin-1-enriched CM can be specifically blocked by heparin or by heparitinase pretreatment.	Heparin	178-185	anosmin 1	Homo sapiens	125-134
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	51-59
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	51-59
15533444-7	2004	The apparent inserted regions are shown to be associated with heparin-binding functionality; however, despite a marked reduction in heparin-binding affinity the mutant form of FGF-1 is surprisingly approximately 70 times more potent in 3T3 fibroblast mitogenic assays.	Heparin	62-69	fibroblast growth factor 1	Homo sapiens	176-181
15533444-7	2004	The apparent inserted regions are shown to be associated with heparin-binding functionality; however, despite a marked reduction in heparin-binding affinity the mutant form of FGF-1 is surprisingly approximately 70 times more potent in 3T3 fibroblast mitogenic assays.	Heparin	132-139	fibroblast growth factor 1	Homo sapiens	176-181
15535971-2	2004	As a result of the identification of FN fragment responsible for TNF-alpha secretion, a 30-kDa fragment derived from the carboxyl-terminal heparin-binding (Hep 2) domain of FN was isolated from the FN digest.	Heparin	139-146	tumor necrosis factor	Rattus norvegicus	65-74
14764524-2	2004	PF4 binds to heparin with high affinity, but its in vivo biologic role has not been defined.	Heparin	13-20	platelet factor 4	Mus musculus	0-3
14764524-6	2004	The thrombotic defect in the mPF4(+/-) and mPF4(-/-) animals was particularly sensitive to infusions of the negatively charged anticoagulant heparin.	Heparin	141-148	platelet factor 4	Mus musculus	29-33
14764524-6	2004	The thrombotic defect in the mPF4(+/-) and mPF4(-/-) animals was particularly sensitive to infusions of the negatively charged anticoagulant heparin.	Heparin	141-148	platelet factor 4	Mus musculus	43-47
15544705-6	2004	After injection of heparin, LPL mass in liver increased for at least an hour.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	28-31
15544705-13	2004	CONCLUSIONS: This study shows that there are heparin-insensitive binding sites for LPL on both hepatocytes and Kupffer cells.	Heparin	45-52	lipoprotein lipase	Rattus norvegicus	83-86
15544705-15	2004	The results support the hypothesis that turnover of endothelial LPL occurs in part by transport to and degradation in the liver, and that this transport is accelerated after injection of heparin.	Heparin	187-194	lipoprotein lipase	Rattus norvegicus	64-67
15627717-0	2004	Comparison of effects of different heparins on thrombin activatable fibrinolysis inhibitor in hemodialyzed patients.	Heparin	35-43	coagulation factor II, thrombin	Homo sapiens	47-55
15648269-10	2004	CONCLUSIONS: Heparin has multiple binding sites for lysozyme, amounting to at most one lysozyme molecule per 3 disaccharide units of heparin.	Heparin	13-20	lysozyme	Homo sapiens	52-60
15648269-10	2004	CONCLUSIONS: Heparin has multiple binding sites for lysozyme, amounting to at most one lysozyme molecule per 3 disaccharide units of heparin.	Heparin	13-20	lysozyme	Homo sapiens	87-95
15648269-10	2004	CONCLUSIONS: Heparin has multiple binding sites for lysozyme, amounting to at most one lysozyme molecule per 3 disaccharide units of heparin.	Heparin	133-140	lysozyme	Homo sapiens	52-60
15648269-10	2004	CONCLUSIONS: Heparin has multiple binding sites for lysozyme, amounting to at most one lysozyme molecule per 3 disaccharide units of heparin.	Heparin	133-140	lysozyme	Homo sapiens	87-95
15648269-11	2004	Complexation decreased lysozyme stability, suggesting that heparin has a higher affinity for the unfolded state than the native state.	Heparin	59-66	lysozyme	Homo sapiens	23-31
15247267-6	2004	Using neutralizing antibodies against the EGFR ligands EGF, heparin-binding-EGF, transforming growth factor-alpha (TGFalpha), or amphiregulin we have shown that only the anti-TGFalpha antibody significantly decreases NT-induced phosphorylation of EGFR and MAP kinases.	Heparin	60-67	epidermal growth factor receptor	Homo sapiens	42-46
15522270-10	2004	Incubation of myocytes with LPA, a phospholipase D (PLD) mediated breakdown metabolite of PLPC, significantly enhanced basal and heparin-releasable myocyte LPL activity, an effect that was duplicated by co-incubation of control myocytes with exogenous PLD and PLPC.	Heparin	129-136	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	35-50
15522270-10	2004	Incubation of myocytes with LPA, a phospholipase D (PLD) mediated breakdown metabolite of PLPC, significantly enhanced basal and heparin-releasable myocyte LPL activity, an effect that was duplicated by co-incubation of control myocytes with exogenous PLD and PLPC.	Heparin	129-136	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	52-55
15543318-3	2004	The results show that the anticoagulant effects of the latter three heparins under conditions approximating physiologic are exerted almost exclusively by acceleration of the inactivation of thrombin, factor Xa and factor IXa to near diffusion-controlled rate constants of approximately 10(6) - 10(7) M(-1).s(-1).	Heparin	68-76	coagulation factor II, thrombin	Homo sapiens	190-198
15543318-9	2004	The bridging effect due to binding of antithrombin and proteinase to the same, long heparin chain is dominating, approximately 1000-3000-fold, for thrombin inhibition and is appreciably smaller, although up to approximately 250-350-fold, for the inactivation of factors IXa and XIa.	Heparin	84-91	endogenous retrovirus group K member 25	Homo sapiens	55-65
15543318-9	2004	The bridging effect due to binding of antithrombin and proteinase to the same, long heparin chain is dominating, approximately 1000-3000-fold, for thrombin inhibition and is appreciably smaller, although up to approximately 250-350-fold, for the inactivation of factors IXa and XIa.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	42-50
15543318-10	2004	These results establish the proteinase targets of heparin derivatives currently used in or considered for thrombosis therapy and give new insights into the mechanism of heparin acceleration of antithrombin inhibition of proteinases.	Heparin	50-57	endogenous retrovirus group K member 25	Homo sapiens	28-38
15502018-5	2004	The addition of increasing concentrations of argatroban, heparin, or both to donor PPP (AT level approximately 100%) caused progressive decreases in the lag time and peak formation of thrombin generation.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	184-192
15502018-6	2004	Heparin (0.25 U/mL) at small AT concentrations had a minimal effect on lag time or peak thrombin formation; its effectiveness of inhibiting thrombin was directly correlated with the concentration of AT.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	140-148
15549170-3	2004	Current studies support a model whereby AT(1)R-dependent transactivation of EGFRs on cardiomyocytes involves stimulation of membrane-bound metalloproteases, which in turn cleave EGFR ligands such as heparin-binding EGF from a plasma membrane-associated precursor.	Heparin	199-206	epidermal growth factor receptor	Homo sapiens	76-80
15388349-0	2004	Synthesis of disaccharides derived from heparin and evaluation of effects on endothelial cell growth and on binding of heparin to FGF-2.	Heparin	119-126	fibroblast growth factor 2	Bos taurus	130-135
15292185-5	2004	This adhesion requires both the N-terminal heparin-binding domain and the RGD site of TSP.	Heparin	43-50	thrombospondin 1	Homo sapiens	86-89
15524061-3	2004	An adequate level of heparin provides satisfactory thrombin inhibition during routine angioplasty.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	51-59
15230691-0	2004	Effect of intravenous heparin on serum levels of endostatin, VEGF and HGF: author"s reply.	Heparin	22-29	vascular endothelial growth factor A	Homo sapiens	61-65
15230692-0	2004	Effect of intravenous heparin on serum levels of endostatin, VEGF and HGF.	Heparin	22-29	vascular endothelial growth factor A	Homo sapiens	61-65
15613925-9	2004	In control measurements the capability of rhAPC to suppress prothrombin fragment 1.2 generation dose-dependently increased in combination with heparin and melagatran.	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	60-71
15203110-1	2004	Heparin affin regulatory peptide (HARP) is a growth factor displaying high affinity for heparin.	Heparin	88-95	pleiotrophin	Homo sapiens	0-32
15726889-1	2004	Native Fucoidan and unfractionated heparin enhanced by 6-fold the in vitro activation of human glutamic plasminogen (Glu-Plg) by tissue plasminogen activator (t-PA) using 0.05M Tris buffer pH 7.4, while sulfated fucoidan inhibited the activation under these conditions.	Heparin	35-42	plasminogen activator, tissue type	Homo sapiens	129-163
15203110-1	2004	Heparin affin regulatory peptide (HARP) is a growth factor displaying high affinity for heparin.	Heparin	88-95	pleiotrophin	Homo sapiens	34-38
15203110-5	2004	Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation.	Heparin	0-7	pleiotrophin	Homo sapiens	58-62
15203110-5	2004	Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation.	Heparin	0-7	pleiotrophin	Homo sapiens	110-114
15203110-6	2004	The molecules with higher affinity to HARP are the more protective, heparin being the most efficient.	Heparin	68-75	pleiotrophin	Homo sapiens	38-42
15325306-5	2004	The heparanase-induced release of radioactivity was linear with respect either to time or to the amount of enzyme and was inhibited by heparin or high ionic strength.	Heparin	135-142	heparanase	Homo sapiens	4-14
15561282-0	2004	Sustained release of vascular endothelial growth factor from calcium-induced alginate hydrogels reinforced by heparin and chitosan.	Heparin	110-117	vascular endothelial growth factor A	Homo sapiens	21-55
15561282-4	2004	In this study, we evaluated sustained VEGF release with a model using hydrogels coated with chitosan and heparin in vitro.	Heparin	105-112	vascular endothelial growth factor A	Homo sapiens	38-42
15178583-1	2004	A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	79-87
15238620-1	2004	BACKGROUND: Patients with heparin-induced thrombocytopenia and thrombosis may be acutely anticoagulated with direct thrombin inhibitors (DTIs).	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	116-124
15358546-5	2004	Although soluble decorin prevented VWF binding to heparin, purified VWF-A1 domain failed to interact with the proteoglycan.	Heparin	50-57	von Willebrand factor	Homo sapiens	35-38
15379633-1	2004	Heparin affin regulatory peptide (HARP), also known as pleiotrophin or heparin-binding growth-associated molecule, is an 18-kDa growth factor that has a high affinity for heparin.	Heparin	71-78	pleiotrophin	Homo sapiens	0-32
15383472-2	2004	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	70-78
15379633-1	2004	Heparin affin regulatory peptide (HARP), also known as pleiotrophin or heparin-binding growth-associated molecule, is an 18-kDa growth factor that has a high affinity for heparin.	Heparin	71-78	pleiotrophin	Homo sapiens	34-38
15379633-1	2004	Heparin affin regulatory peptide (HARP), also known as pleiotrophin or heparin-binding growth-associated molecule, is an 18-kDa growth factor that has a high affinity for heparin.	Heparin	71-78	pleiotrophin	Homo sapiens	55-67
15177934-6	2004	The NT-induced stimulation of EGFR/ERK/Akt phosphorylation and DNA synthesis was inhibited by EGFR-tyrosine kinase inhibitors (AG1478, PD153035), metallo-endopeptidase inhibitor phosphoramidon and by heparin, but not by neutralizing anti-EGF antibody.	Heparin	200-207	epidermal growth factor receptor	Homo sapiens	30-34
15311268-1	2004	Antithrombin, the principal physiological inhibitor of the blood coagulation proteinase thrombin, requires heparin as a cofactor.	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	4-12
15311268-5	2004	The 16-mer oligosaccharide is just long enough to form the predicted bridge between the high-affinity pentasaccharide-binding site on antithrombin and the highly basic exosite 2 on thrombin, validating the design strategy for this synthetic heparin.	Heparin	241-248	coagulation factor II, thrombin	Homo sapiens	138-146
15311269-0	2004	Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	21-29
15311269-0	2004	Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	21-29
15311269-2	2004	Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	4-12
15311269-5	2004	The structure reveals a template mechanism with antithrombin and thrombin bound to the same heparin chain.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	52-60
15300904-8	2004	Heparin treatment lowered IL-6 (359.0 +/- 66 U/mL vs 288.5 +/- 58 U/mL) and hematocrit level (53 +/- 4% vs 46 +/- 3%).	Heparin	0-7	interleukin 6	Rattus norvegicus	26-30
15339877-6	2004	These include fondaparinux and idraparinux, synthetic analogs of the pentasaccharide sequence that mediates the interaction of heparin and LMWH with antithrombin, and ximelagatran, an orally active inhibitor of thrombin.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	153-161
15177934-6	2004	The NT-induced stimulation of EGFR/ERK/Akt phosphorylation and DNA synthesis was inhibited by EGFR-tyrosine kinase inhibitors (AG1478, PD153035), metallo-endopeptidase inhibitor phosphoramidon and by heparin, but not by neutralizing anti-EGF antibody.	Heparin	200-207	mitogen-activated protein kinase 1	Homo sapiens	35-38
15177934-6	2004	The NT-induced stimulation of EGFR/ERK/Akt phosphorylation and DNA synthesis was inhibited by EGFR-tyrosine kinase inhibitors (AG1478, PD153035), metallo-endopeptidase inhibitor phosphoramidon and by heparin, but not by neutralizing anti-EGF antibody.	Heparin	200-207	AKT serine/threonine kinase 1	Homo sapiens	39-42
15177934-6	2004	The NT-induced stimulation of EGFR/ERK/Akt phosphorylation and DNA synthesis was inhibited by EGFR-tyrosine kinase inhibitors (AG1478, PD153035), metallo-endopeptidase inhibitor phosphoramidon and by heparin, but not by neutralizing anti-EGF antibody.	Heparin	200-207	epidermal growth factor receptor	Homo sapiens	94-98
15177934-7	2004	Thus, transactivation of EGFR by NT involved heparin-binding EGF (HB-EGF or amphiregulin) rather than EGF.	Heparin	45-52	epidermal growth factor receptor	Homo sapiens	25-29
15262417-8	2004	Subsequently, the ability of aminoBP-heparin conjugates to enhance the mineral affinity of basic fibroblast growth factor (bFGF) and bone morphogenetic protein-2 (BMP-2) was explored.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	91-121
15262417-8	2004	Subsequently, the ability of aminoBP-heparin conjugates to enhance the mineral affinity of basic fibroblast growth factor (bFGF) and bone morphogenetic protein-2 (BMP-2) was explored.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	123-127
15194626-2	2004	Heparin has long been a mainstay choice of antithrombotic regimen in cardiac patients, but persistent thrombin generation seems to occur during heparin therapy.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	102-110
15274177-9	2004	Furthermore, laminin-dependent BG2-c6 cell spreading was inhibited by heparin.	Heparin	70-77	Laminin A	Drosophila melanogaster	13-20
15291808-4	2004	Here, we compared the effects of PF-4 on the signalling events involved in the proliferation induced by VEGF(165), which binds heparin, and by VEGF(121), which does not.	Heparin	127-134	vascular endothelial growth factor A	Homo sapiens	104-108
15246840-4	2004	In addition, heparin significantly increased the number of cells within the E14 striatum responding to a brief pulse of FGF-2.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	120-125
15246840-8	2004	Interestingly, the addition of heparin to EGF neurospheres, which had no effects on EGF stability or growth rates, increased the numbers of neurons generated to that seen for FGF-2/heparin neurospheres.	Heparin	31-38	fibroblast growth factor 2	Homo sapiens	175-180
15246840-0	2004	Heparin stabilizes FGF-2 and modulates striatal precursor cell behavior in response to EGF.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	19-24
15259000-5	2004	GPI-PLD binding to heparan sulphate proteoglycan was determined in the absence or presence of heparan sulphate or heparin.	Heparin	114-121	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	0-7
15253736-12	2004	CONCLUSION: The practice of locking newly inserted tunneled central venous catheters with gentamicin and heparin is an effective strategy to reduce line sepsis rates, and is associated with beneficial effects on epoetin requirements.	Heparin	105-112	erythropoietin	Homo sapiens	212-219
15304046-0	2004	Thrombin generation for the control of heparin treatment, comparison with the activated partial thromboplastin time.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	0-8
15282457-8	2004	RESULTS: Heparin rebound was demonstrated in every patient in the placebo group as reflected by increased thrombin clotting time, anti-factor Xa activity, and protein-bound heparin between 1 and 6 hours after surgery.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	106-114
15280800-3	2004	EC-SOD is a secretory, tetrameric glycoprotein containing copper and zinc, with a high affinity to certain glycosaminoglycans, such as heparin and heparan sulfate.	Heparin	135-142	superoxide dismutase 3	Homo sapiens	0-6
15173164-5	2004	Activation of mast cells resulted in marked increases in both the formation and subsequent degradation of Ang II, and both of these processes were strongly reduced in heparin-deficient peritoneal cells.	Heparin	167-174	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	106-112
15219850-5	2004	Inhibitors of matrix metalloproteinase and heparin bound-EGF prevented the CaR-mediated increases of pERK and PTHrP, consistent with a "triple-membrane-spanning signaling" requirement for transactivation of the EGFR by the CaR.	Heparin	43-50	epidermal growth factor receptor	Homo sapiens	211-215
15232299-0	2004	Heparin regulates survival and differentiation of mesencephalic progenitors mediated via FGF2 in vitro.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	89-93
15232299-1	2004	Heparin plays an important role in the survival and differentiation of mesencephalic progenitors mediated by FGF-2 in vitro.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	109-114
15232299-2	2004	If the heparin concentration is gradually increased, cell survival mediated by FGF-2 can be greatly enhanced, to a maximum concentration of 20 ng/ml FGF-2 from 5 microg/ml heparin.	Heparin	7-14	fibroblast growth factor 2	Homo sapiens	79-84
15232299-2	2004	If the heparin concentration is gradually increased, cell survival mediated by FGF-2 can be greatly enhanced, to a maximum concentration of 20 ng/ml FGF-2 from 5 microg/ml heparin.	Heparin	7-14	fibroblast growth factor 2	Homo sapiens	149-154
15232299-2	2004	If the heparin concentration is gradually increased, cell survival mediated by FGF-2 can be greatly enhanced, to a maximum concentration of 20 ng/ml FGF-2 from 5 microg/ml heparin.	Heparin	172-179	fibroblast growth factor 2	Homo sapiens	79-84
15232299-2	2004	If the heparin concentration is gradually increased, cell survival mediated by FGF-2 can be greatly enhanced, to a maximum concentration of 20 ng/ml FGF-2 from 5 microg/ml heparin.	Heparin	172-179	fibroblast growth factor 2	Homo sapiens	149-154
15232299-3	2004	However, differentiation of FGF-2 responsive mesencephalic progenitors is inhibited by heparin.	Heparin	87-94	fibroblast growth factor 2	Homo sapiens	28-33
15249683-9	2004	Heparin also increased the digestion of purified plasma vWF.	Heparin	0-7	von Willebrand factor	Homo sapiens	56-59
15223398-8	2004	Heparin-coated polyvinylchloride efficiently prevented synthesis of both IL-8 and MCP-1.	Heparin	0-7	C-X-C motif chemokine ligand 8	Homo sapiens	73-77
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	AKT serine/threonine kinase 1	Rattus norvegicus	240-243
14966081-7	2004	Heparin had an additive effect on the reduced [(3)H]thymidine incorporation in FGF-2-treated AT2 cells caused by inhibition of the MEK/ERK pathway by the MEK inhibitor PD-98059.	Heparin	0-7	Eph receptor B1	Rattus norvegicus	135-138
15223398-9	2004	Addition of recombinant human complement factor 5a to blood incubated in heparin-coated polyvinylchloride restored IL-8 and MCP-1 production completely and partly, respectively.	Heparin	73-80	C-X-C motif chemokine ligand 8	Homo sapiens	115-119
15223398-14	2004	The increase in IL-8 and MCP-1 was prevented by heparin-coated polyvinylchloride.	Heparin	48-55	C-X-C motif chemokine ligand 8	Homo sapiens	16-20
15320792-2	2004	The limitations of heparin, largely used in the therapy of arterial and venous thromboembolism, has prompted the development of new antithrombotic drugs, able to directly inhibit thrombin.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	179-187
15320820-7	2004	Pharmacological anticoagulants include warfarin, FVIIa inhibitors, FXa inhibitors, and thrombin inhibition by its direct inhibitors or heparins.	Heparin	135-143	coagulation factor II, thrombin	Homo sapiens	87-95
15347838-0	2004	Heparin increases prolactin and modifies the effects of fgf-2 upon prolactin accumulation in pituitary primary cultures.	Heparin	0-7	prolactin	Rattus norvegicus	18-27
15347838-0	2004	Heparin increases prolactin and modifies the effects of fgf-2 upon prolactin accumulation in pituitary primary cultures.	Heparin	0-7	prolactin	Rattus norvegicus	67-76
15347838-4	2004	However, low doses of heparin reduced the effects of FGF-2, but higher doses of heparin increased the maximal FGF-2-induced prolactin secretion and ED50.	Heparin	80-87	prolactin	Rattus norvegicus	124-133
15132978-9	2004	Surface plasmon resonance analysis indicated a Kd of 15.7 nM for the RG-1192/FGF-2 interaction (10.6 nM for the heparin/FGF-2 interaction).	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	77-82
15132978-9	2004	Surface plasmon resonance analysis indicated a Kd of 15.7 nM for the RG-1192/FGF-2 interaction (10.6 nM for the heparin/FGF-2 interaction).	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	120-125
15201252-4	2004	UFH was significantly more effective than LMWH at inhibiting P selectin expression (p = 0.001) and platelet derived growth factor release from thrombin activated platelets (p = 0.012).	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	143-151
15102889-8	2004	Heparin reduced PG production in HL-producing cells, confirming that PG production is stimulated only when HL is present as a ligand for HSPG.	Heparin	0-7	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	137-141
15205081-9	2004	The expression levels of Bcl-2 protein on lymphoblasts were lower at the first hour than at 0 and 2 h in 10- and 20-U/mL heparin concentrations (p &lt;.001).	Heparin	121-128	BCL2 apoptosis regulator	Homo sapiens	25-30
15205081-10	2004	The lowest expression of Bcl-2 protein was detected in the 20-U/mL heparin concentration at the first hour.	Heparin	67-74	BCL2 apoptosis regulator	Homo sapiens	25-30
15223860-4	2004	FGF-2 is a member of a family of heparin binding growth factors that bind to heparan sulphate proteoglycans (HSPG), an important determinant of FGF-2 activity.	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	0-5
15223860-4	2004	FGF-2 is a member of a family of heparin binding growth factors that bind to heparan sulphate proteoglycans (HSPG), an important determinant of FGF-2 activity.	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	144-149
15223860-7	2004	A novel ELISA based method was developed to detect solubilisation of FGF-2 following addition of heparin and heparitinase to bronchial tissue slices.	Heparin	97-104	fibroblast growth factor 2	Homo sapiens	69-74
15269982-5	2004	RESULT: Human recombinant IFN-gamma bound to heparin in a concentration  dependent manner, the binding of IFN-gamma to HBC was detected at the concentration of 0.25 ng, and saturated at around 2 ng.	Heparin	45-52	interferon gamma	Homo sapiens	26-35
15199558-3	2004	In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	111-119
15269982-5	2004	RESULT: Human recombinant IFN-gamma bound to heparin in a concentration  dependent manner, the binding of IFN-gamma to HBC was detected at the concentration of 0.25 ng, and saturated at around 2 ng.	Heparin	45-52	interferon gamma	Homo sapiens	106-115
15269982-6	2004	Free heparin, LMW heparin, CS,HA and carrageenans competed for the binding of IFN-gamma to HBC with significant different ability.	Heparin	5-12	interferon gamma	Homo sapiens	78-87
15196911-4	2004	This suggested that the primary effect of aptamer binding was through the heparin-binding site of thrombin, anion-binding exosite-2 (exosite-2).	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	98-106
15044445-6	2004	Heparan sulfate proteoglycans (HSPGs) and low density lipoprotein receptor-related protein (LRP) were crucial for CER-enhanced emulsion uptake, because heparin or lactoferrin inhibited the emulsion uptake.	Heparin	152-159	LDL receptor related protein 1	Homo sapiens	92-95
15069070-2	2004	The aims of the present study were to examine the affinity of fibronectin type III repeats of TN-C fragments (TNIII) for heparin, to investigate the role of the TNIII4 domains in the binding of TN-C to heparin, and to delineate a sequence of amino acids within the TNIII4 domain, which mediates cooperative heparin binding.	Heparin	121-128	fibronectin 1	Homo sapiens	62-73
15149336-9	2004	In addition, heparin, one of the major components of mast cells, inhibited the expression of TGF-beta mRNA in rat fibroblasts in culture.	Heparin	13-20	transforming growth factor, beta 1	Rattus norvegicus	93-101
15155316-0	2004	Reversal of direct thrombin inhibition after cardiopulmonary bypass in a patient with heparin-induced thrombocytopenia.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	19-27
15149315-11	2004	Differential receptor activation was also seen: Heparin-binding EGF markedly activated EGFR (&gt;EGF = TGF-alpha &gt; amphiregulin), with a greater effect seen in cystic vs. control collecting tubule cells.	Heparin	48-55	amphiregulin	Mus musculus	118-130
15149336-11	2004	Rather, they might be protective or ameliorative in this model through the inhibition of TGF-beta production by heparin, and possibly in other models and also in humans.	Heparin	112-119	transforming growth factor beta 1	Homo sapiens	89-97
15174044-0	2004	Determination of dissociation constants for a heparin-binding domain of amyloid precursor protein and heparins or heparan sulfate by affinity capillary electrophoresis.	Heparin	46-53	amyloid beta precursor protein	Homo sapiens	72-97
15282649-1	2004	Heparin-induced thrombocytopenia (HIT) is caused by heparin-dependent, platelet-activating IgG antibodies that increase thrombin generation in vivo, producing a prothrombotic phenotype.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	120-128
15282652-0	2004	Direct thrombin inhibitors in the treatment of immune-mediated heparin-induced thrombocytopenia.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	7-15
15282654-0	2004	The use of direct thrombin inhibitors in cardiovascular surgery in patients with heparin-induced thrombocytopenia.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	18-26
15282657-7	2004	In a multiple logistic regression model that included inflammatory markers and clinical risk factors, antibodies to PF4/heparin were a strong predictor of 30-day MI (odds ratio, 9.0; 95% confidence intervals, 2.1 to 38.6; p &lt; 0.01), with IL-6 being the only other predictor (odds ratio, 1.1; 95% confidence intervals, 1.0 to 1.2; p = 0.03).	Heparin	120-127	interleukin 6	Homo sapiens	241-245
15044433-7	2004	Heparanase-mediated Akt phosphorylation was independent of its enzymatic activity or the presence of cell membrane HS proteoglycans and was augmented by heparin.	Heparin	153-160	AKT serine/threonine kinase 1	Homo sapiens	20-23
15108362-0	2004	Heparin modulates the growth and adherence and augments the growth-inhibitory action of TNF-alpha on cultured human keratinocytes.	Heparin	0-7	tumor necrosis factor	Homo sapiens	88-97
15108362-9	2004	Interestingly, heparin at 2-20 microg/ml augmented or even potentiated this growth-inhibitory effect of TNF-alpha.	Heparin	15-22	tumor necrosis factor	Homo sapiens	104-113
15108362-10	2004	The association of TNF-alpha with heparin was shown by demonstrating that TNF-alpha bound tightly to heparin-Sepharose chromatographic material.	Heparin	34-41	tumor necrosis factor	Homo sapiens	19-28
15108362-10	2004	The association of TNF-alpha with heparin was shown by demonstrating that TNF-alpha bound tightly to heparin-Sepharose chromatographic material.	Heparin	34-41	tumor necrosis factor	Homo sapiens	74-83
15108362-10	2004	The association of TNF-alpha with heparin was shown by demonstrating that TNF-alpha bound tightly to heparin-Sepharose chromatographic material.	Heparin	101-108	tumor necrosis factor	Homo sapiens	19-28
15108362-10	2004	The association of TNF-alpha with heparin was shown by demonstrating that TNF-alpha bound tightly to heparin-Sepharose chromatographic material.	Heparin	101-108	tumor necrosis factor	Homo sapiens	74-83
15108362-12	2004	In the cell adherence assay, heparin at 2 microg/ml inhibited significantly by 12-13% or 33% the adherence of keratinocytes onto the plastic surface coated with fibronectin or collagen, respectively, but this inhibition was reversed back to baseline at 20 or 200 microg/ml heparin.	Heparin	29-36	fibronectin 1	Homo sapiens	161-172
15108362-14	2004	In conclusion, heparin not only inhibits or modulates keratinocyte growth and adherence but it also binds and potentiates the growth-inhibitory function of TNF-alpha.	Heparin	15-22	tumor necrosis factor	Homo sapiens	156-165
15134651-6	2004	CD spectroscopy and calorimetry show the stability of these AChE model peptides is increased by addition of heparin, confirming binding to heparin, and the lack of significant enthalpy change indicates the binding is largely electrostatic in nature.	Heparin	108-115	acetylcholinesterase (Cartwright blood group)	Homo sapiens	60-64
15134651-6	2004	CD spectroscopy and calorimetry show the stability of these AChE model peptides is increased by addition of heparin, confirming binding to heparin, and the lack of significant enthalpy change indicates the binding is largely electrostatic in nature.	Heparin	139-146	acetylcholinesterase (Cartwright blood group)	Homo sapiens	60-64
15177561-10	2004	The Kazal domain of CPAMD8 binds to heparin, and subcellular fractionation shows that CPAMD8 is membrane associated via ionic interaction.	Heparin	36-43	C3 and PZP like alpha-2-macroglobulin domain containing 8	Homo sapiens	20-26
15177561-10	2004	The Kazal domain of CPAMD8 binds to heparin, and subcellular fractionation shows that CPAMD8 is membrane associated via ionic interaction.	Heparin	36-43	C3 and PZP like alpha-2-macroglobulin domain containing 8	Homo sapiens	86-92
15144459-14	2004	CONCLUSION: Data indicate that anti-thrombin III affects eosinophil motility via the effects of its heparin-binding site on cell surface syndecan-4.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	36-44
15111489-9	2004	Intralipid/heparin infusion resulted in a 24.73% decrease in insulin sensitivity (P = 0.007) and a 47.81% increase in ceramide content (P = 0.005).	Heparin	11-18	insulin	Homo sapiens	61-68
15174044-1	2004	Dynamic affinity capillary electrophoresis (ACE) was used for determining the binding constants between heparin-like glycosaminoglycans and the (96-110) heparin-binding domain of amyloid precursor protein (APP).	Heparin	104-111	amyloid beta precursor protein	Homo sapiens	179-204
15675186-10	2004	LMWH have antitumour effects in animal models of malignancy: heparin oligosaccharides containing less than 10 saccharide residues have been found to inhibit the biological activity of basic fibroblast growth factor (bFGF), whereas heparin fragments with less than 18 saccharide residues have been reported to inhibit the binding of vascular endothelial growth factor (VEGF) to its receptors on endothelial cells.	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	184-214
14963717-8	2004	In contrast, the mitogenic effects of the platelet-derived and the heparin-binding epidermal growth factors were dependent on p44/p42 MAPK activation and independent of activation of p38 MAPK.	Heparin	67-74	mitogen-activated protein kinase 1	Homo sapiens	134-138
14963717-8	2004	In contrast, the mitogenic effects of the platelet-derived and the heparin-binding epidermal growth factors were dependent on p44/p42 MAPK activation and independent of activation of p38 MAPK.	Heparin	67-74	mitogen-activated protein kinase 1	Homo sapiens	183-186
15675186-10	2004	LMWH have antitumour effects in animal models of malignancy: heparin oligosaccharides containing less than 10 saccharide residues have been found to inhibit the biological activity of basic fibroblast growth factor (bFGF), whereas heparin fragments with less than 18 saccharide residues have been reported to inhibit the binding of vascular endothelial growth factor (VEGF) to its receptors on endothelial cells.	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	216-220
15675186-10	2004	LMWH have antitumour effects in animal models of malignancy: heparin oligosaccharides containing less than 10 saccharide residues have been found to inhibit the biological activity of basic fibroblast growth factor (bFGF), whereas heparin fragments with less than 18 saccharide residues have been reported to inhibit the binding of vascular endothelial growth factor (VEGF) to its receptors on endothelial cells.	Heparin	61-68	vascular endothelial growth factor A	Homo sapiens	332-366
15675186-10	2004	LMWH have antitumour effects in animal models of malignancy: heparin oligosaccharides containing less than 10 saccharide residues have been found to inhibit the biological activity of basic fibroblast growth factor (bFGF), whereas heparin fragments with less than 18 saccharide residues have been reported to inhibit the binding of vascular endothelial growth factor (VEGF) to its receptors on endothelial cells.	Heparin	61-68	vascular endothelial growth factor A	Homo sapiens	368-372
15675186-12	2004	In vitro heparin fragments of less than 18 saccharide residues reduce the activity of VEGF, and fragments of less than 10 saccharide residues inhibit the activity of bFGF.	Heparin	9-16	vascular endothelial growth factor A	Homo sapiens	86-90
15056378-9	2004	The trapping of chemokines by heparinoids reduced the chemotactic activity of islets supernatant from 3.05 +/- 0.27 to 1.2 +/- 0.1 with heparin or pentosan and to 1.72 +/- 0.22 with C8S, and also decreased the TNF-alpha release by human macrophages from 1205 +/- 35 to 1000 +/- 26 (C8S), 250 +/- 21 (heparin) and 320 +/- 19 (pentosan) pg/ml, and IL-1beta from 234 +/- 13 to 151 +/- 5 (C8S), 50 +/- 3 (heparin) and 57 +/- 4 (pentosan) pg/ml.	Heparin	30-37	tumor necrosis factor	Homo sapiens	210-219
15096041-6	2004	Interestingly, comparison of sensorgrams of sequential injections of FGF2 and FGFR1 and equimolar FGF2-FGFR1 injections onto a heparin neoproteoglycan surface demonstrates that FGF2 dramatically enhances the association of FGFR1 with heparin and leads us to propose a model for the stepwise assembly of a ternary FGF-FGFR-HSPG complex.	Heparin	127-134	fibroblast growth factor 2	Homo sapiens	98-102
15096041-6	2004	Interestingly, comparison of sensorgrams of sequential injections of FGF2 and FGFR1 and equimolar FGF2-FGFR1 injections onto a heparin neoproteoglycan surface demonstrates that FGF2 dramatically enhances the association of FGFR1 with heparin and leads us to propose a model for the stepwise assembly of a ternary FGF-FGFR-HSPG complex.	Heparin	127-134	fibroblast growth factor receptor 1	Homo sapiens	103-108
15096041-6	2004	Interestingly, comparison of sensorgrams of sequential injections of FGF2 and FGFR1 and equimolar FGF2-FGFR1 injections onto a heparin neoproteoglycan surface demonstrates that FGF2 dramatically enhances the association of FGFR1 with heparin and leads us to propose a model for the stepwise assembly of a ternary FGF-FGFR-HSPG complex.	Heparin	127-134	fibroblast growth factor 2	Homo sapiens	98-102
15096041-6	2004	Interestingly, comparison of sensorgrams of sequential injections of FGF2 and FGFR1 and equimolar FGF2-FGFR1 injections onto a heparin neoproteoglycan surface demonstrates that FGF2 dramatically enhances the association of FGFR1 with heparin and leads us to propose a model for the stepwise assembly of a ternary FGF-FGFR-HSPG complex.	Heparin	127-134	fibroblast growth factor receptor 1	Homo sapiens	103-108
15096041-7	2004	The weak binding affinity of the FGFR1-heparin interaction suggests that in this model, FGFR and HSPG are unbound in the absence of FGF ligand.	Heparin	39-46	fibroblast growth factor receptor 1	Homo sapiens	33-38
15087389-2	2004	At the cellular level, many of the antimetastatic effects of heparin in vivo are due to its action on P-selectin-mediated binding.	Heparin	61-68	selectin, platelet	Mus musculus	102-112
15087389-7	2004	Heparin not only inhibits P-selectin-mediated melanoma cell rolling but also attenuates melanoma metastasis formation in vivo, further supporting the concept that endothelial P-selectin expression may represent an additional target of heparin action in experimental melanoma lung metastasis.	Heparin	0-7	selectin, platelet	Mus musculus	26-36
15087389-7	2004	Heparin not only inhibits P-selectin-mediated melanoma cell rolling but also attenuates melanoma metastasis formation in vivo, further supporting the concept that endothelial P-selectin expression may represent an additional target of heparin action in experimental melanoma lung metastasis.	Heparin	0-7	selectin, platelet	Mus musculus	175-185
15087389-7	2004	Heparin not only inhibits P-selectin-mediated melanoma cell rolling but also attenuates melanoma metastasis formation in vivo, further supporting the concept that endothelial P-selectin expression may represent an additional target of heparin action in experimental melanoma lung metastasis.	Heparin	235-242	selectin, platelet	Mus musculus	175-185
15096041-2	2004	The recent FGF2-FGFR1-heparin crystal structure provides a detailed but static view of the FGF-FGFR-heparin complex.	Heparin	22-29	fibroblast growth factor 2	Homo sapiens	11-15
15096041-2	2004	The recent FGF2-FGFR1-heparin crystal structure provides a detailed but static view of the FGF-FGFR-heparin complex.	Heparin	22-29	fibroblast growth factor receptor 1	Homo sapiens	16-21
15096041-5	2004	Binding constants for binary FGF2/FGFR1 (KD = 62 nM), FGF2/heparin (KD = 39 nM), and FGFR1/heparin (KD = 3.2 microM) interactions correlate to the magnitude of binding interface observed in the FGF2-FGFR1-heparin crystal structure.	Heparin	91-98	fibroblast growth factor receptor 1	Homo sapiens	85-90
15096041-5	2004	Binding constants for binary FGF2/FGFR1 (KD = 62 nM), FGF2/heparin (KD = 39 nM), and FGFR1/heparin (KD = 3.2 microM) interactions correlate to the magnitude of binding interface observed in the FGF2-FGFR1-heparin crystal structure.	Heparin	91-98	fibroblast growth factor receptor 1	Homo sapiens	85-90
15096041-5	2004	Binding constants for binary FGF2/FGFR1 (KD = 62 nM), FGF2/heparin (KD = 39 nM), and FGFR1/heparin (KD = 3.2 microM) interactions correlate to the magnitude of binding interface observed in the FGF2-FGFR1-heparin crystal structure.	Heparin	91-98	fibroblast growth factor receptor 1	Homo sapiens	85-90
15096041-5	2004	Binding constants for binary FGF2/FGFR1 (KD = 62 nM), FGF2/heparin (KD = 39 nM), and FGFR1/heparin (KD = 3.2 microM) interactions correlate to the magnitude of binding interface observed in the FGF2-FGFR1-heparin crystal structure.	Heparin	91-98	fibroblast growth factor receptor 1	Homo sapiens	85-90
14736885-4	2004	EC-SOD contains a C-terminal heparin-binding region thought to be important for modulating its distribution in the extracellular matrix.	Heparin	29-36	superoxide dismutase 3	Homo sapiens	0-6
15066178-9	2004	The contributions of positively charged residues located in CCP4 were all minor when analyzed by heparin affinity chromatography.	Heparin	97-104	AGBL carboxypeptidase 1	Homo sapiens	60-64
15093980-0	2004	Pericardial fluid and serum VEGF in response to different types of heparin treatment.	Heparin	67-74	vascular endothelial growth factor A	Homo sapiens	28-32
15093980-2	2004	We designed an observational study to compare the effects of standard heparin (SH) with low molecular weight heparin (LMWH) on vascular endothelial growth factor (VEGF) levels in patients undergoing coronary artery bypass grafting (CABG).	Heparin	70-77	vascular endothelial growth factor A	Homo sapiens	127-161
15093980-2	2004	We designed an observational study to compare the effects of standard heparin (SH) with low molecular weight heparin (LMWH) on vascular endothelial growth factor (VEGF) levels in patients undergoing coronary artery bypass grafting (CABG).	Heparin	70-77	vascular endothelial growth factor A	Homo sapiens	163-167
15093980-2	2004	We designed an observational study to compare the effects of standard heparin (SH) with low molecular weight heparin (LMWH) on vascular endothelial growth factor (VEGF) levels in patients undergoing coronary artery bypass grafting (CABG).	Heparin	109-116	vascular endothelial growth factor A	Homo sapiens	127-161
15093980-2	2004	We designed an observational study to compare the effects of standard heparin (SH) with low molecular weight heparin (LMWH) on vascular endothelial growth factor (VEGF) levels in patients undergoing coronary artery bypass grafting (CABG).	Heparin	109-116	vascular endothelial growth factor A	Homo sapiens	163-167
15056378-9	2004	The trapping of chemokines by heparinoids reduced the chemotactic activity of islets supernatant from 3.05 +/- 0.27 to 1.2 +/- 0.1 with heparin or pentosan and to 1.72 +/- 0.22 with C8S, and also decreased the TNF-alpha release by human macrophages from 1205 +/- 35 to 1000 +/- 26 (C8S), 250 +/- 21 (heparin) and 320 +/- 19 (pentosan) pg/ml, and IL-1beta from 234 +/- 13 to 151 +/- 5 (C8S), 50 +/- 3 (heparin) and 57 +/- 4 (pentosan) pg/ml.	Heparin	30-37	interleukin 1 beta	Homo sapiens	346-354
15066025-0	2004	The ShdA adhesin binds to the cationic cradle of the fibronectin 13FnIII repeat module: evidence for molecular mimicry of heparin binding.	Heparin	122-129	fibronectin 1	Homo sapiens	53-64
15003840-7	2004	In vitro assays of binding to several different potential receptors revealed that the MIC2 A-domain binds specifically to heparin, a ubiquitous sulfated proteoglycan found in the extracellular matrix (ECM).	Heparin	122-129	CD99 molecule (Xg blood group)	Homo sapiens	86-90
15003840-9	2004	The recombinant MIC2 A-domain bound to heparin as a high molecular weight species, as did MIC2 from parasite lysate, indicating that the recombinant A-domain mimics the binding of native MIC2.	Heparin	39-46	CD99 molecule (Xg blood group)	Homo sapiens	16-20
15066025-5	2004	The (13)FnIII repeat module of fibronectin contains a cationic cradle formed by six basic residues (R6, R7, R9, R23, K25 and R54) that is a high affinity heparin-binding site conserved among fibronectin sequences from frogs to man.	Heparin	154-161	fibronectin 1	Homo sapiens	31-42
15066025-5	2004	The (13)FnIII repeat module of fibronectin contains a cationic cradle formed by six basic residues (R6, R7, R9, R23, K25 and R54) that is a high affinity heparin-binding site conserved among fibronectin sequences from frogs to man.	Heparin	154-161	fibronectin 1	Homo sapiens	191-202
15066025-6	2004	Binding of ShdA to the (13)FnIII repeat module of fibronectin and to a second extracellular matrix protein, Collagen I, could be inhibited by heparin.	Heparin	142-149	fibronectin 1	Homo sapiens	50-61
15290792-6	2004	These results demonstrate that hCox-2 directly increases breast tumor cell proliferation, stimulates invasion across a basement membrane, and induces synthesis of specific heparin binding splice variants of VEGF.	Heparin	172-179	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	31-37
15003253-5	2004	Proteins with affinity for gelatin and heparin, immunologically related to human fibronectin, are found in the cell wall of epicotyls grown under salt stress or not.	Heparin	39-46	fibronectin 1	Homo sapiens	81-92
15290792-6	2004	These results demonstrate that hCox-2 directly increases breast tumor cell proliferation, stimulates invasion across a basement membrane, and induces synthesis of specific heparin binding splice variants of VEGF.	Heparin	172-179	vascular endothelial growth factor A	Homo sapiens	207-211
14991948-1	2004	AIM: To observe the effects of low molecular weight heparin (LMWH) on platelet surface P-selectin expression and serum interleukin-8 production in rats with trinitrobenzene sulphonic acid (TNBS) induced colitis.	Heparin	52-59	selectin P	Rattus norvegicus	87-97
14702351-0	2004	C-terminal and heparin-binding domains of collagenic tail subunit are both essential for anchoring acetylcholinesterase at the synapse.	Heparin	15-22	acetylcholinesterase (Cartwright blood group)	Homo sapiens	99-119
15014132-11	2004	Blocking IP(3) receptors using heparin prevented the excitatory effect of NT.	Heparin	31-38	neurotensin	Homo sapiens	74-76
15179322-5	2004	In recent years, detailed studies of structure-function relationships have yielded new understanding of the interactions between C4BP and the activated complement factors C4b and C3b, heparin, and vitamin K-dependent anticoagulant protein S. This review describes the localization of binding sites for a number of C4BP ligands in relation to well-established and novel functions of C4BP such as complement inhibition, protection of apoptotic cells from complement, CD40-dependent stimulation of B cells, and the contribution of a number of human pathogens to pathogenesis.	Heparin	184-191	complement component 4 binding protein alpha	Homo sapiens	129-133
15253248-2	2004	The indirect thrombin inhibitor heparin has been previously shown to be effective in limiting intimal hyperplasia (IH).	Heparin	32-39	coagulation factor II	Rattus norvegicus	13-21
15076227-6	2004	All examined PARP inhibitors reduced the ADP-induced platelet aggregation in a dose-dependent manner (significant inhibition at 20 microM for HO-3089 and at 500 microM for the other agents; P &lt; 0.05), even if platelets were sensitized with heparin.	Heparin	243-250	poly(ADP-ribose) polymerase 1	Homo sapiens	13-17
15001987-1	2004	Heparin affin regulatory peptide (HARP) is an heparin-binding molecule involved in the regulation of cell proliferation and differentiation.	Heparin	46-53	pleiotrophin	Homo sapiens	0-32
15001987-1	2004	Heparin affin regulatory peptide (HARP) is an heparin-binding molecule involved in the regulation of cell proliferation and differentiation.	Heparin	46-53	pleiotrophin	Homo sapiens	34-38
14991768-8	2004	However, TSP-1(1-90) itself was poorly endocytosed and this truncated amino-terminal domain was considerably more effective than the full-length heparin-binding domain (HBD) of TSP-1 in blocking the catabolism of endogenously expressed TSP-1.	Heparin	145-152	thrombospondin 1	Homo sapiens	177-182
14991768-8	2004	However, TSP-1(1-90) itself was poorly endocytosed and this truncated amino-terminal domain was considerably more effective than the full-length heparin-binding domain (HBD) of TSP-1 in blocking the catabolism of endogenously expressed TSP-1.	Heparin	145-152	thrombospondin 1	Homo sapiens	177-182
14991768-9	2004	These results indicate that TSP-1 binding to LRP-1 does not require prior or concomitant interaction with cell surface HSPG but suggest subsequent endocytosis requires high-affinity heparin-binding.	Heparin	182-189	thrombospondin 1	Homo sapiens	28-33
15287195-11	2004	One mg/mL of heparin eluted PLA2 bound to the large-pore hemofilter.	Heparin	13-20	phospholipase A2 group IB	Homo sapiens	28-32
14751231-1	2004	Heparin/heparan sulfate-like glycosaminoglycans (HSGAGs) modulate the activity of the fibroblast growth factor (FGF) family of proteins.	Heparin	0-7	fibroblast growth factor 1	Mus musculus	112-115
14670838-12	2004	Heparin may inhibit the mitogenic effects of thrombin and FXa in human SMCs by preventing bFGF binding to FGFR-1.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	45-53
14670838-12	2004	Heparin may inhibit the mitogenic effects of thrombin and FXa in human SMCs by preventing bFGF binding to FGFR-1.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	90-94
14670838-12	2004	Heparin may inhibit the mitogenic effects of thrombin and FXa in human SMCs by preventing bFGF binding to FGFR-1.	Heparin	0-7	fibroblast growth factor receptor 1	Homo sapiens	106-112
15072225-0	2004	Heparin inhibits IFN-gamma-induced fractalkine/CX3CL1 expression in human endothelial cells.	Heparin	0-7	interferon gamma	Homo sapiens	17-26
12896874-13	2004	Some antibodies blocked a basic fibroblast growth factor-binding site of HS, and one antibody blocked a vascular endothelial growth factor-binding site of heparin.	Heparin	155-162	vascular endothelial growth factor A	Homo sapiens	104-138
14748844-0	2004	Regulation of interleukin-6 fetoplacental levels could be involved in the protective effect of low-molecular weight heparin treatment on murine spontaneous abortion.	Heparin	116-123	interleukin 6	Mus musculus	14-27
14748844-8	2004	CONCLUSION: This study suggests that regulation of IL-6 fetoplacental levels could be involved in heparin-mediated anticoagulation protection against abortion.	Heparin	98-105	interleukin 6	Mus musculus	51-55
14576044-7	2004	All high-affinity peptides reversed inhibition of thrombin-induced clot formation by UFH.	Heparin	85-88	coagulation factor II, thrombin	Homo sapiens	50-58
15003908-0	2004	Heparin based anticoagulation during peripheral blood stem cell collection may increase the CD34+ cell yield.	Heparin	0-7	CD34 molecule	Homo sapiens	92-96
15072225-0	2004	Heparin inhibits IFN-gamma-induced fractalkine/CX3CL1 expression in human endothelial cells.	Heparin	0-7	C-X3-C motif chemokine ligand 1	Homo sapiens	35-46
15072225-0	2004	Heparin inhibits IFN-gamma-induced fractalkine/CX3CL1 expression in human endothelial cells.	Heparin	0-7	C-X3-C motif chemokine ligand 1	Homo sapiens	47-53
15072225-4	2004	We have investigated the effect of heparin on the fractalkine expression in human umbilical vein endothelial cells (HUVEC) in culture.	Heparin	35-42	C-X3-C motif chemokine ligand 1	Homo sapiens	50-61
15072225-6	2004	The IFN-gamma-induced expressions of fractalkine mRNA and protein were inhibited by heparin in a concentration-dependent manner.	Heparin	84-91	interferon gamma	Homo sapiens	4-13
15072225-6	2004	The IFN-gamma-induced expressions of fractalkine mRNA and protein were inhibited by heparin in a concentration-dependent manner.	Heparin	84-91	C-X3-C motif chemokine ligand 1	Homo sapiens	37-48
15072225-7	2004	Heparin also inhibited adhesion of mononuclear cells (MNC) to HUVEC monolayers stimulated with IFN-gamma, but it did not inhibit the MNC adhesion to the monolayers stimulated with interleukin-1beta.	Heparin	0-7	interferon gamma	Homo sapiens	95-104
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	56-63	interferon gamma	Homo sapiens	67-76
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	56-63	interferon gamma	Homo sapiens	133-142
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	56-63	interferon gamma	Homo sapiens	133-142
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	56-63	interferon gamma	Homo sapiens	133-142
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	81-88	interferon gamma	Homo sapiens	133-142
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	81-88	interferon gamma	Homo sapiens	133-142
15072225-8	2004	Electrophoretic analysis demonstrated direct binding of heparin to IFN-gamma and heparin was found to partially block the binding of IFN-gamma to IFN-gamma receptor (IFN-gamma R).	Heparin	81-88	interferon gamma	Homo sapiens	133-142
15228221-3	2004	The binding activity of apoE to heparin was decreased by the oxidative modification.	Heparin	32-39	apolipoprotein E	Homo sapiens	24-28
14725788-14	2004	Anti-thrombin III alone was not inhibitory, but in the presence of heparin inhibited both MASP-1 and MASP-2.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	5-13
14742788-1	2004	BACKGROUND: Argatroban is a direct thrombin inhibitor used to treat heparin-induced thrombocytopenia (HIT).	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	35-43
14657241-4	2004	We found that FGF-2 translocation occurred in endothelial cells and fibroblasts, which express FGF receptors, and that the efficiency of translocation was increased in the presence of heparin.	Heparin	184-191	fibroblast growth factor 2	Homo sapiens	14-19
14657241-4	2004	We found that FGF-2 translocation occurred in endothelial cells and fibroblasts, which express FGF receptors, and that the efficiency of translocation was increased in the presence of heparin.	Heparin	184-191	fibroblast growth factor 1	Homo sapiens	14-17
14695513-1	2004	Six synthetic heparin-like oligosaccharides have been used to investigate the effect of the oligosaccharide sulfation pattern on the stimulation of acidic fibroblast growth factor (FGF-1) induced mitogenesis signaling and the biological significance of FGF-1 trans dimerization in the FGF-1 activation process.	Heparin	14-21	fibroblast growth factor 1	Homo sapiens	181-186
14570917-5	2004	Here we report that VEGF(165) and VEGF(121) binding to fibronectin also increased at acidic pH, and that these interactions are further enhanced by the addition of heparin.	Heparin	164-171	vascular endothelial growth factor A	Homo sapiens	20-24
14570917-5	2004	Here we report that VEGF(165) and VEGF(121) binding to fibronectin also increased at acidic pH, and that these interactions are further enhanced by the addition of heparin.	Heparin	164-171	vascular endothelial growth factor A	Homo sapiens	34-43
14570917-5	2004	Here we report that VEGF(165) and VEGF(121) binding to fibronectin also increased at acidic pH, and that these interactions are further enhanced by the addition of heparin.	Heparin	164-171	fibronectin 1	Homo sapiens	55-66
14570917-6	2004	These results reveal that the accepted non-heparin-binding isoform of VEGF (VEGF(121)) is converted into a heparin-binding growth factor under acidic conditions.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	70-74
14570917-6	2004	These results reveal that the accepted non-heparin-binding isoform of VEGF (VEGF(121)) is converted into a heparin-binding growth factor under acidic conditions.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	76-85
14706599-9	2004	RESULTS: Heparin concentrations &gt; or =20 IU/mL significantly increased LPS-induced IL-8 production.	Heparin	9-16	C-X-C motif chemokine ligand 8	Homo sapiens	86-90
14706599-11	2004	Heparin and fondaparinux sodium exhibited the expected anticoagulatory activities: heparin increased both thrombin clotting time and anti-Xa activity, fondaparinux sodium increased anti-Xa activity only.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	106-114
14742803-5	2004	Conventional anticoagulant therapies, such as warfarin, unfractionated heparin, and low-molecular-weight heparin, exert their pharmacologic action by indirect thrombin inhibition.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	159-167
14742803-5	2004	Conventional anticoagulant therapies, such as warfarin, unfractionated heparin, and low-molecular-weight heparin, exert their pharmacologic action by indirect thrombin inhibition.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	159-167
15702865-1	2004	Fibroblast growth factor-2 is a member of a large family of proteins that bind heparin and heparan sulfate and modulate the function of a wide range of cell types.	Heparin	79-86	fibroblast growth factor 2	Homo sapiens	0-26
14733594-4	2004	Significantly, the capacity of this heparin-mimic to promote an FGF-2 specific proliferative cell response was confirmed and suggests potential applications for this compound and related derivatives in areas related to therapeutic angiogenesis.	Heparin	36-43	fibroblast growth factor 2	Homo sapiens	64-69
17271049-7	2004	We have generated mutants with lower and higher affinity to heparin, which could prove valuable in controlling the therapeutic zone of an AAV vector in tissues where ECM HS hinders AAV2 diffusion.	Heparin	60-67	adeno-associated virus integration site 1	Homo sapiens	138-141
14964479-2	2004	t-PA is reasonably safe if used in a carefully defined manner that ensures close attention to blood pressure, careful patient monitoring, no use of heparin and aspirin during first 24 hours, and appropriate patient selection.	Heparin	148-155	plasminogen activator, tissue type	Homo sapiens	0-4
15387448-7	2004	Addition of heparin to serum (51 samples) caused decreased cTnT (mean ratio 0.92).	Heparin	12-19	troponin T2, cardiac type	Homo sapiens	59-63
15387448-8	2004	In 3 of 51 such samples the cTnT decrease was more marked, but in a second sample from the same subjects (1 week later) such a prominent, heparin-induced loss of cTnT no longer appeared.	Heparin	138-145	troponin T2, cardiac type	Homo sapiens	28-32
15387448-8	2004	In 3 of 51 such samples the cTnT decrease was more marked, but in a second sample from the same subjects (1 week later) such a prominent, heparin-induced loss of cTnT no longer appeared.	Heparin	138-145	troponin T2, cardiac type	Homo sapiens	162-166
15586623-6	2004	Unlike warfarin and heparin, these direct thrombin inhibitors are able to inhibit fibrin-bound thrombin and so produce more effective inhibition of coagulation.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	95-103
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	218-226
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	270-278
15035435-8	2004	Heparin and heparan sulfate fully protected bFGF from complexation and cleavage by HABP, although these glycosaminoglycans are known to enhance the proteolytic activity of HABP.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	44-48
15648575-1	2004	Dextran derivatives that mimic the action of heparin have been shown to protect heparin-binding growth factors, such as Transforming Growth Factor-beta1 (TGF-beta1) and Fibroblast Growth Factor-2 (FGF-2).	Heparin	45-52	transforming growth factor beta 1	Homo sapiens	120-152
14668575-0	2004	Role of endothelin-1 and thromboxane A2 in the pulmonary hypertension induced by heparin-protamine interaction in anesthetized dogs.	Heparin	81-88	endothelin 1	Canis lupus familiaris	8-20
23105443-16	2004	The clinical tolerability and the efficacy of low molecular weight heparins has established that inhibition of further thrombin generation, by blocking factor Xa alone can be an effective way of preventing thrombus growth without inactivating thrombin.	Heparin	67-75	coagulation factor II, thrombin	Homo sapiens	119-127
15648575-1	2004	Dextran derivatives that mimic the action of heparin have been shown to protect heparin-binding growth factors, such as Transforming Growth Factor-beta1 (TGF-beta1) and Fibroblast Growth Factor-2 (FGF-2).	Heparin	45-52	transforming growth factor beta 1	Homo sapiens	154-163
15648575-1	2004	Dextran derivatives that mimic the action of heparin have been shown to protect heparin-binding growth factors, such as Transforming Growth Factor-beta1 (TGF-beta1) and Fibroblast Growth Factor-2 (FGF-2).	Heparin	45-52	fibroblast growth factor 2	Homo sapiens	169-195
15648575-1	2004	Dextran derivatives that mimic the action of heparin have been shown to protect heparin-binding growth factors, such as Transforming Growth Factor-beta1 (TGF-beta1) and Fibroblast Growth Factor-2 (FGF-2).	Heparin	45-52	fibroblast growth factor 2	Homo sapiens	197-202
15081565-11	2004	A substantial prolongation of the thrombin clotting time was observed in the fibrinogen solution containing EDTA at 37 degrees C compared to 20 degrees C. However, the viscosity of EDTA anticoagulated purified fibrinogen and plasma samples did not differ from that of heparin anticoagulated samples.	Heparin	268-275	fibrinogen beta chain	Homo sapiens	77-87
15506032-8	2004	Thrombin generation was decreased in circuits anticoagulated with argatroban versus heparin, despite aPTTs being less prolonged.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	0-8
15163860-5	2004	This chapter focuses on studies of the binding of bovine serum albumin (BSA) to heparin using FACCE.	Heparin	80-87	albumin	Homo sapiens	57-70
15188027-2	2004	Because of the importance of VEGF in animal tumors, we purified VEGF/VPF from ascitic fluid of ovarian cancer patients with heparin sepharose column.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	64-68
15188027-2	2004	Because of the importance of VEGF in animal tumors, we purified VEGF/VPF from ascitic fluid of ovarian cancer patients with heparin sepharose column.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	69-72
12963740-5	2003	Heparin, a cell-impermeable complex carbohydrate with high affinity for Group V PLA2, blocks that association, suggesting that the granules are formed by internalization of the Group V sPLA2 previously associated with the outer cellular surface.	Heparin	0-7	phospholipase A2, group V	Mus musculus	80-84
14751391-0	2004	Protective effect of vasoactive intestinal peptide on testicular torsion-detorsion injury: association with heparin-containing mast cells.	Heparin	108-115	vasoactive intestinal peptide	Rattus norvegicus	21-50
14749535-6	2003	Endogenous CK2 in HeLa cells and the cell lysate was able to phosphorylate deoxyhypusine synthase and this modification is enhanced or decreased by the addition of CK2 effectors such as polylysine, heparin, and poly(Glu, Tyr) 4:1.	Heparin	198-205	deoxyhypusine synthase	Homo sapiens	75-97
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparin	170-177	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
14532267-3	2003	All chimeras bound heparin with a high affinity similar to wild-type, underwent heparin-induced fluorescence changes indicative of normal conformational activation, and were able to form SDS-stable complexes with thrombin, factor Xa, and factor IXa and inhibit these proteases with stoichiometries minimally altered from those of wild-type antithrombin.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	213-221
12947001-5	2003	The region of TSP-1 responsible for these activities was located within the 140-kDa antiangiogenic and FGF-2 binding fragment, whereas the 25-kDa heparin-binding fragment was inactive.	Heparin	146-153	thrombospondin 1	Homo sapiens	14-19
12907439-4	2003	However, in the presence of full-length heparin there was a 3- and 7-fold increase in stoichiometry of inhibition of factor Xa and thrombin.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	131-139
12951367-8	2003	After heparin administration in vivo, hepatic lipase activity in plasma increased nearly 100-fold with appearance of an additional 55 kDa band in postheparin plasma.	Heparin	6-13	lipase C, hepatic type	Rattus norvegicus	38-52
14623192-11	2003	The data support the concept that inter molecular coiled-coil helix formation is an essential structural feature of the apoE CT domain, which likely plays a role in clustering heparin-binding sites and/or sequestering the lipid-binding surface in lipid-free states.	Heparin	176-183	apolipoprotein E	Homo sapiens	120-124
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparin	170-177	coagulation factor II	Mus musculus	4-12
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparin	199-206	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
12963740-5	2003	Heparin, a cell-impermeable complex carbohydrate with high affinity for Group V PLA2, blocks that association, suggesting that the granules are formed by internalization of the Group V sPLA2 previously associated with the outer cellular surface.	Heparin	0-7	phospholipase A2, group V	Mus musculus	185-190
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparin	199-206	coagulation factor II	Mus musculus	4-12
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparin	71-78	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
14636878-4	2003	RESULTS: Heparin and citrate increased S100B levels (p&lt;0.001), whereas EDTA had no effect (p=0.24).	Heparin	9-16	S100 calcium binding protein B	Homo sapiens	39-44
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparin	133-140	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparin	133-140	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
14521955-8	2003	Although the proteolytic cleavage of IGFBP-rP1 decreased its heparin-binding activity, the cleaved form could bind syndecan-1 efficiently.	Heparin	61-68	insulin like growth factor binding protein 7	Homo sapiens	37-46
14642154-3	2003	The standard agent used in clinical practice, unfractionated heparin (UFH), is associated with the disadvantages of variable anticoagulant effect, inability to inhibit clot-bound thrombin, neutralization by platelet factor 4, and the propensity to cause thrombocytopenic complications.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	179-187
14642154-3	2003	The standard agent used in clinical practice, unfractionated heparin (UFH), is associated with the disadvantages of variable anticoagulant effect, inability to inhibit clot-bound thrombin, neutralization by platelet factor 4, and the propensity to cause thrombocytopenic complications.	Heparin	70-73	coagulation factor II, thrombin	Homo sapiens	179-187
14642154-7	2003	The pharmacokinetic characteristics of better availability, longer half-life, and dose-independent clearance together with the ability of inhibiting both thrombin generation and activity make the low-molecular-weight heparins (LMWHs) an attractive alternative to UFH.	Heparin	217-225	coagulation factor II, thrombin	Homo sapiens	154-162
14534780-8	2003	Semi-purified circulating VEGF proteins were obtained by heparin-sepharose and its biological activities were shown to alter gene expressions in human aortic endothelial cells.	Heparin	57-64	vascular endothelial growth factor A	Homo sapiens	26-30
14585904-9	2003	Patients homozygous for both the ACE D and PAI-1 4G alleles may benefit from the application of low molecular weight heparin as early as possible in the pregnancy in order to prevent uteroplacental microthromboses.	Heparin	117-124	angiotensin I converting enzyme	Homo sapiens	33-36
14551349-4	2003	We have now studied the influence of heparin on the Ang II-induced intracellular Ca(2+) release and activation of nuclear factor kappa B (NF-kappaB).	Heparin	37-44	angiotensinogen	Homo sapiens	52-58
14551349-4	2003	We have now studied the influence of heparin on the Ang II-induced intracellular Ca(2+) release and activation of nuclear factor kappa B (NF-kappaB).	Heparin	37-44	nuclear factor kappa B subunit 1	Homo sapiens	114-136
14551349-4	2003	We have now studied the influence of heparin on the Ang II-induced intracellular Ca(2+) release and activation of nuclear factor kappa B (NF-kappaB).	Heparin	37-44	nuclear factor kappa B subunit 1	Homo sapiens	138-147
14551349-7	2003	The addition of heparin resulted in an oscillatory pattern of Ca(2+) influxes upon Ang II stimulation.	Heparin	16-23	angiotensinogen	Homo sapiens	83-89
14551349-13	2003	Heparin inhibited NF-kappaB activation in Ang II-stimulated MCs that expressed either normal or chemically altered GAG.	Heparin	0-7	nuclear factor kappa B subunit 1	Homo sapiens	18-27
14551349-13	2003	Heparin inhibited NF-kappaB activation in Ang II-stimulated MCs that expressed either normal or chemically altered GAG.	Heparin	0-7	angiotensinogen	Homo sapiens	42-48
12917428-10	2003	This effect of IGFBP-5 was inhibited by soluble heparin and by treating cells with heparinase.	Heparin	48-55	insulin like growth factor binding protein 5	Homo sapiens	15-22
14511765-1	2003	In the blood coagulation cascade, human antithrombin III (hAT III) acts as an inhibitor of serine proteases such as thrombin and factor Xa, and this anticoagulatory glycoprotein requires the binding of heparin for its activation.	Heparin	202-209	coagulation factor II, thrombin	Homo sapiens	44-52
14530380-3	2003	We show that HS and heparin interact directly with BACE1 and inhibit in vitro processing of peptide and APP substrates.	Heparin	20-27	beta-secretase 1	Homo sapiens	51-56
14528000-2	2003	Here, we establish by deletion mutagenesis that the HGF/SF and heparin-binding sites of MET are contained within a large N-terminal domain spanning the alpha-chain (amino acids 25-307) and the first 212 amino acids of the beta-chain (amino acids 308-519).	Heparin	63-70	Fc gamma receptor and transporter	Homo sapiens	152-163
12867435-4	2003	To gain a structural insight into this interaction, we have solved the crystal structure of the presumed heparan sulfate-binding domain of follistatin, both alone and in complex with the small heparin analogs sucrose octasulfate and D-myo-inositol hexasulfate.	Heparin	193-200	follistatin	Homo sapiens	139-150
12867435-7	2003	Moreover, the crystallographic analysis of the two protein-ligand complexes mentioned above leads us to propose a potential location for the heparan sulfate-binding site on the surface of follistatin and to suggest the involvement of residues Asn80 and Arg86 in such a follistatin-heparin interaction.	Heparin	281-288	follistatin	Homo sapiens	188-199
13679071-2	2003	AT inhibits clotting factors such as thrombin and factor Xa, a reaction catalyzed by heparin.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	37-45
13679071-4	2003	In order to overcome some of heparin"s limitations, we prepared a covalent AT-heparin complex (ATH) that has increased intravenous half-life, reduced bleeding risk, and can directly inhibit clot-bound thrombin.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	201-209
13679071-7	2003	Further analysis of the rate of heparin-catalyzed inhibition of thrombin by AT isoforms prepared from ATH revealed that the beta-variant reacted approximately 2-fold faster.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	64-72
14502551-5	2003	The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology.	Heparin	17-24	fibroblast growth factor 1	Homo sapiens	57-60
12818887-6	2003	We show that altering endogenous gradients of HS sulfation with sodium chlorate or over-O-sulfated synthetic heparin in lung organ cultures dramatically decreases Fgf10 binding.	Heparin	109-116	fibroblast growth factor 10	Homo sapiens	163-168
12853245-5	2003	Information of the molecular surface structure of the heparin coatings could be derived from the ratios at different photon energies between S2p signals from sulfonate groups in heparin and disulfide groups originating from a cross-linking unit in the heparin conjugate.	Heparin	54-61	ribosomal protein S2	Homo sapiens	141-144
12853245-5	2003	Information of the molecular surface structure of the heparin coatings could be derived from the ratios at different photon energies between S2p signals from sulfonate groups in heparin and disulfide groups originating from a cross-linking unit in the heparin conjugate.	Heparin	178-185	ribosomal protein S2	Homo sapiens	141-144
12853245-5	2003	Information of the molecular surface structure of the heparin coatings could be derived from the ratios at different photon energies between S2p signals from sulfonate groups in heparin and disulfide groups originating from a cross-linking unit in the heparin conjugate.	Heparin	178-185	ribosomal protein S2	Homo sapiens	141-144
14519117-5	2003	M27 blocked the ability of antithrombin to inhibit thrombin as well as antithrombin cleavage, both in the presence and absence of heparin.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	31-39
14517862-2	2003	We developed a novel alginate gel sheet that is crosslinked with heparin (H/A gel sheet) and discovered its properties of releasing biologically active basic fibroblast growth factor (bFGF), a representative member of the heparin-binding growth factors (HBGFs), for about 1 month in vitro and of inducing angiogenesis in vivo.	Heparin	65-72	fibroblast growth factor 2	Homo sapiens	152-182
14517862-2	2003	We developed a novel alginate gel sheet that is crosslinked with heparin (H/A gel sheet) and discovered its properties of releasing biologically active basic fibroblast growth factor (bFGF), a representative member of the heparin-binding growth factors (HBGFs), for about 1 month in vitro and of inducing angiogenesis in vivo.	Heparin	65-72	fibroblast growth factor 2	Homo sapiens	184-188
14502551-7	2003	In the presence of purified anticoagulant heparin and derivative, FGF7 has the similar activity as protamine sulfate for reversal of anticoagulant effect, while FGF1 is much less potent than FGF7.	Heparin	42-49	fibroblast growth factor 7	Homo sapiens	66-70
14502551-9	2003	In addition, FGF7 and homologues may be useful in pharmaceutical neutralization of anticoagulant heparin and heparan sulfate.	Heparin	97-104	fibroblast growth factor 7	Homo sapiens	13-17
14564303-3	2003	METHODS: Direct thrombin inhibitors comprise a family of agents with promising properties that offer several potential advantages over unfractionated heparin.	Heparin	150-157	coagulation factor II, thrombin	Homo sapiens	16-24
14563444-4	2003	RESULTS: Heparin plasma and citrate increased plasma S100B levels (p &lt; 0.001), whereas EDTA had no effect (p = 0.24).	Heparin	9-16	S100 calcium binding protein B	Homo sapiens	53-58
14563444-6	2003	CONCLUSIONS: When anticoagulant is required, heparin plasma should be the primary choice for measurement of S100 B levels.	Heparin	45-52	S100 calcium binding protein B	Homo sapiens	108-114
14517862-0	2003	Action of microparticles of heparin and alginate crosslinked gel when used as injectable artificial matrices to stabilize basic fibroblast growth factor and induce angiogenesis by controlling its release.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	122-152
14568677-8	2003	Presence of the heparin binding domain in PlGF-4 suggests that this variant would remain cell membrane-associated and thus could influence trophoblast and endothelial cells in an autocrine manner.	Heparin	16-23	placental growth factor	Homo sapiens	42-46
14502551-5	2003	The diversity of heparin-binding motifs within the large FGF family of polypeptides and receptors provides a repertoire of diverse templates for capture of diverse heparin/heparan sulfate motifs in biology.	Heparin	164-171	fibroblast growth factor 1	Homo sapiens	57-60
14502551-6	2003	We show here that, similar to antithrombin, a member of the FGF family, FGF7, selectively captures anti-Factor Xa and anti-Factor IIa activity from commercially and clinically applied heparin mixtures.	Heparin	184-191	fibroblast growth factor 1	Homo sapiens	60-63
14502551-6	2003	We show here that, similar to antithrombin, a member of the FGF family, FGF7, selectively captures anti-Factor Xa and anti-Factor IIa activity from commercially and clinically applied heparin mixtures.	Heparin	184-191	fibroblast growth factor 7	Homo sapiens	72-76
13679486-12	2003	With the AN69ST heparin-coated membrane, thrombin generation was reduced then suppressed, as compared with the original AN69, primed in the same conditions.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	41-49
14578460-2	2003	We designed a novel vascular-targeting fusion construct designated as GrB/vascular endothelial growth factor (VEGF)121, which is composed of a non-heparin-binding isoform of VEGF and the proapoptotic pathway enzyme GrB fused via a short, flexible tether (G4S).	Heparin	147-154	vascular endothelial growth factor A	Homo sapiens	74-108
14578460-2	2003	We designed a novel vascular-targeting fusion construct designated as GrB/vascular endothelial growth factor (VEGF)121, which is composed of a non-heparin-binding isoform of VEGF and the proapoptotic pathway enzyme GrB fused via a short, flexible tether (G4S).	Heparin	147-154	vascular endothelial growth factor A	Homo sapiens	110-114
14572330-4	2003	After TNF-alpha or heparin treated 90 minutes, the perfusion pressure stimulated by endothelin-1 (ET-1) was detected.	Heparin	19-26	endothelin 1	Rattus norvegicus	84-96
14572330-4	2003	After TNF-alpha or heparin treated 90 minutes, the perfusion pressure stimulated by endothelin-1 (ET-1) was detected.	Heparin	19-26	endothelin 1	Rattus norvegicus	98-102
14572330-6	2003	When ET-1 was added at 2 nmol/L, the perfusion pressures increased to (47+/-9) mmHg, (97+/-36) mm Hg and (11+/-6) mm Hg in control, TNF-alpha and heparin (10mg/L) treated group, respectively, which were different among the three groups (t&gt;or=3.811, P&lt;0.01).	Heparin	146-153	endothelin 1	Rattus norvegicus	5-9
12860985-1	2003	The serpin antithrombin is a slow thrombin inhibitor that requires heparin to enhance its reaction rate.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	15-23
12957170-5	2003	By using a cartridge containing gelatin immobilized affinity membranes followed by another cartridge containing heparin immobilized membranes, fibronectin from human blood plasma could be separated.	Heparin	112-119	fibronectin 1	Homo sapiens	143-154
12948857-0	2003	Suppression of mitogen-activated protein kinase phosphatase-1 (MKP-1) by heparin in vascular smooth muscle cells.	Heparin	73-80	dual specificity phosphatase 1	Homo sapiens	15-61
12810721-5	2003	Inhibition of proteoglycan sulfation by sodium chlorate or incubation of cells with labeled lipoproteins in the presence of heparin (100 microg/ml) abolished bridging effects of EL.	Heparin	124-131	endothelial lipase	Cricetulus griseus	178-180
12935804-1	2003	A manufacturing process for the production of Anti-thrombin IIII concentrate is described, which is based primarily on Heparin Sepharose affinity chromatography.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	51-59
12948857-0	2003	Suppression of mitogen-activated protein kinase phosphatase-1 (MKP-1) by heparin in vascular smooth muscle cells.	Heparin	73-80	dual specificity phosphatase 1	Homo sapiens	63-68
12948857-4	2003	MKP-1 protein was increased by serum stimulation of quiescent cells, and this increase was diminished by heparin (1 microg/mL).	Heparin	105-112	dual specificity phosphatase 1	Homo sapiens	0-5
12948857-6	2003	Decreased Erk activity in the presence of heparin preceded, and may account for, decreased MKP-1.	Heparin	42-49	mitogen-activated protein kinase 1	Homo sapiens	10-13
12948857-6	2003	Decreased Erk activity in the presence of heparin preceded, and may account for, decreased MKP-1.	Heparin	42-49	dual specificity phosphatase 1	Homo sapiens	91-96
12948857-8	2003	However, because MKP-1 is known to cause an increase in activity of kinases upstream of Erk, that may signal through additional pathways, the decrease in MKP-1 activity may paradoxically enhance heparin"s antiproliferative effects.	Heparin	195-202	dual specificity phosphatase 1	Homo sapiens	17-22
12948857-8	2003	However, because MKP-1 is known to cause an increase in activity of kinases upstream of Erk, that may signal through additional pathways, the decrease in MKP-1 activity may paradoxically enhance heparin"s antiproliferative effects.	Heparin	195-202	mitogen-activated protein kinase 1	Homo sapiens	88-91
12948857-8	2003	However, because MKP-1 is known to cause an increase in activity of kinases upstream of Erk, that may signal through additional pathways, the decrease in MKP-1 activity may paradoxically enhance heparin"s antiproliferative effects.	Heparin	195-202	dual specificity phosphatase 1	Homo sapiens	154-159
12948857-9	2003	VSMC selected to grow in the presence of heparin express decreased levels of MKP-1 that are unresponsive to heparin, and Erk activity becomes unresponsive to heparin in one cell line.	Heparin	41-48	dual specificity phosphatase 1	Homo sapiens	77-82
14708939-6	2003	Here we use exogenous modified heparins to determine those structural features required to inhibit GDNF signalling in ex vivo assays.	Heparin	31-39	glial cell derived neurotrophic factor	Homo sapiens	99-103
13677658-4	2003	TniA was collected from the flow-through fraction and applied onto HiTrap heparin HP 5 ml in order to capture the basic TniA.	Heparin	74-81	TniA	Escherichia coli	0-4
12928380-7	2003	Finally, the binding of a murine pre-BCR to stroma cells can be blocked either with heparin or by pretreatment of stroma cells with heparitinase or a sulfation inhibitor.	Heparin	84-91	BCR activator of RhoGEF and GTPase	Mus musculus	37-40
12941035-1	2003	Rebound thrombin generation after successful thrombolysis might be related to (i) too short-term anticoagulant therapy and to (ii) the inability of heparin derivatives to inhibit clot-bound thrombin.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	8-16
12941037-4	2003	In buffer, heparin and SanOrg123781A inhibited FXa and thrombin at similar concentrations [concentration inhibiting 50% (IC50) of Xa and IIa activity were, respectively: heparin 120 +/- 7 and 3 +/- 1 ng mL-1; SanOrg123781A 77 +/- 5 and 4 +/- 1 ng mL-1].	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	55-63
12941037-4	2003	In buffer, heparin and SanOrg123781A inhibited FXa and thrombin at similar concentrations [concentration inhibiting 50% (IC50) of Xa and IIa activity were, respectively: heparin 120 +/- 7 and 3 +/- 1 ng mL-1; SanOrg123781A 77 +/- 5 and 4 +/- 1 ng mL-1].	Heparin	170-177	coagulation factor II, thrombin	Homo sapiens	55-63
12941037-8	2003	Both compounds also inhibited clot-bound thrombin activity, the IC50 values of heparin and SanOrg123781A being 1 +/- 0.01 micro g mL-1 and 0.1 +/- 0.1 micro g mL-1, respectively.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	41-49
12941037-9	2003	Moreover, both heparin and SanOrg123781A significantly inhibited fibrinopeptide A generated by the action of clot-bound thrombin on fibrinogen but also by free thrombin generated from prothrombin by clot-bound FXa with IC50 values of 4 +/- 0.6 and 1 +/- 0.1 micro g mL-1, respectively.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	120-128
12810718-7	2003	We also find no evidence for an interaction between DCC and heparin and instead demonstrate that a loop on the fifth fibronectin type III repeat of DCC previously implicated in mediating interactions with heparin is important for sNetrin binding.	Heparin	205-212	fibronectin 1	Homo sapiens	117-128
12975470-6	2003	Heparin (an antithrombin-potentiating agent that can also block P- and L-selectin recognition of ligands) ameliorated this platelet aggregation, but had no additional effect in P- or L-selectin-deficient mice.	Heparin	0-7	selectin, lymphocyte	Mus musculus	71-81
12810820-6	2003	The HepG2 PLTP could be enriched by Heparin-Sepharose affinity chromatography and eluted in size-exclusion chromatography at a position corresponding to the size of 160 kDa.	Heparin	36-43	phospholipid transfer protein	Homo sapiens	10-14
12941037-9	2003	Moreover, both heparin and SanOrg123781A significantly inhibited fibrinopeptide A generated by the action of clot-bound thrombin on fibrinogen but also by free thrombin generated from prothrombin by clot-bound FXa with IC50 values of 4 +/- 0.6 and 1 +/- 0.1 micro g mL-1, respectively.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	160-168
12924949-6	2003	Mutations of either or both VV sequences of rCBD (1037-38 and 1123-24 of TSP1) to GG had a modest effect on cell binding, a component of which was inhibited by heparin.	Heparin	160-167	thrombospondin 1	Homo sapiens	73-77
12912723-1	2003	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is an intensely prothrombotic syndrome managed by discontinuation of heparin therapy and substitution of an alternative inhibitor of thrombin.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	184-192
14567441-0	2003	An inter-subunit disulfide bond affects affinity of human lung extracellular superoxide dismutase to heparin.	Heparin	101-108	superoxide dismutase 3	Homo sapiens	63-97
14513837-6	2003	Thrombin-inducedVEGF release was blocked by anti-thrombin, heparin, a synthetic thrombin receptor inhibitor E5510, the calcium chelator BAPTA, the protein kinase C inhibitor calphostin C, and the MEK1/2 inhibitor U0126.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	0-8
12919102-1	2003	HIP is a heparin/heparan sulfate (Hp/HS) binding protein identical to ribosomal protein L29 that displays diverse biological functions.	Heparin	9-16	predicted gene 13841	Mus musculus	70-91
12960499-3	2003	Recently, heparin has been reported to diminish TNF-alpha production from macrophages in response to LPS.	Heparin	10-17	tumor necrosis factor	Rattus norvegicus	48-57
14567441-1	2003	Human extracellular superoxide dismutase (EC-SOD) was purified to homogeneity from lung tissue and the nature of the binding of heparin to EC-SOD was investigated.	Heparin	128-135	superoxide dismutase 3	Homo sapiens	6-40
14567441-1	2003	Human extracellular superoxide dismutase (EC-SOD) was purified to homogeneity from lung tissue and the nature of the binding of heparin to EC-SOD was investigated.	Heparin	128-135	superoxide dismutase 3	Homo sapiens	42-48
14567441-1	2003	Human extracellular superoxide dismutase (EC-SOD) was purified to homogeneity from lung tissue and the nature of the binding of heparin to EC-SOD was investigated.	Heparin	128-135	superoxide dismutase 3	Homo sapiens	139-145
14567441-4	2003	Western blot analysis of the heparin affinity chromatography product indicated that the presence of the inter-subunit disulfide bond affects the affinity of EC-SOD for heparin.	Heparin	29-36	superoxide dismutase 3	Homo sapiens	157-163
14567441-4	2003	Western blot analysis of the heparin affinity chromatography product indicated that the presence of the inter-subunit disulfide bond affects the affinity of EC-SOD for heparin.	Heparin	168-175	superoxide dismutase 3	Homo sapiens	157-163
14567441-5	2003	The affinity of EC-SOD for heparin is a very important feature of the enzyme because it controls the distribution of the enzyme in tissues.	Heparin	27-34	superoxide dismutase 3	Homo sapiens	16-22
12740361-7	2003	Recombinant 3-OST-5 only exhibited sulfotransferase activity toward heparan sulfate and heparin.	Heparin	88-95	heparan sulfate-glucosamine 3-sulfotransferase 5	Homo sapiens	12-19
12911595-8	2003	Both H483-K497 and G486-K502 were effective in neutralizing the accelerated inhibition by heparin of thrombin by antithrombin in the absence of Zn++.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	101-109
12695507-1	2003	Covalent antithrombin-heparin (ATH) complexes, formed spontaneously between antithrombin (AT) and unfractionated standard heparin (H), have a potent ability to catalyze the inhibition of factor Xa (or thrombin) by added AT.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	13-21
12842558-4	2003	Two patients with documented heparin-induced thrombocytopenia underwent revascularization using a new thrombin inhibitor (Bivalirudin [Angiomax, Medicines Co, Cambridge, MA]) for anticoagulation.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	102-110
12799194-4	2003	In contrast, for phospholipase Cgamma(1) (PLCgamma(1)) and the adaptor molecule Shb to be maximally tyrosine-phosphorylated, cells had to be stimulated with both FGF-2 and heparin (100 ng/ml).	Heparin	172-179	SH2 domain-containing adapter protein B	Cricetulus griseus	80-83
12821199-0	2003	Two-step purification of His-tagged Nef protein in native condition using heparin and immobilized metal ion affinity chromatographies.	Heparin	74-81	S100 calcium binding protein B	Homo sapiens	36-39
12689334-0	2003	Interaction of the 268-282 region of glycoprotein Ibalpha with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	91-99
12689334-2	2003	Full FVIII activation requires cleavage at Arg(372), a process involving the alpha-thrombin exosite-II; referred to as heparin-binding site (HBS).	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	83-91
12904260-1	2003	BACKGROUND: In spite of using heparin-coated extracorporeal circuits, cardiopulmonary bypass (CPB) is still associated with an extensive thrombin generation, which is only partially suppressed by the use of high dosages of heparin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	137-145
12904260-1	2003	BACKGROUND: In spite of using heparin-coated extracorporeal circuits, cardiopulmonary bypass (CPB) is still associated with an extensive thrombin generation, which is only partially suppressed by the use of high dosages of heparin.	Heparin	223-230	coagulation factor II, thrombin	Homo sapiens	137-145
12851529-7	2003	Our data suggest that a fragment of approximately 60 kDa that co-purified with FN, with affinity to heparin and gelatin, has the arFN that controls vWF multimer size.	Heparin	100-107	fibronectin 1	Homo sapiens	79-81
12851529-7	2003	Our data suggest that a fragment of approximately 60 kDa that co-purified with FN, with affinity to heparin and gelatin, has the arFN that controls vWF multimer size.	Heparin	100-107	von Willebrand factor	Homo sapiens	148-151
12810880-5	2003	Virus receptor binding as examined by heparin treatment of adsorbed virus was significantly reduced only if the virus had been coated with the AD-2-specific antibody.	Heparin	38-45	apolipoprotein E	Homo sapiens	143-147
14618797-3	2003	Convincing, statistically significant data have been obtained on a decline in the concentration of fibrinogen in those patients with acute viral myocarditis placed on a complex therapy, running a mild course of the disease, a mild one presenting with elevated indices for hemostasis, and moderately severe course (diclofenac, heparin, thiotriazoline) as well, in grave condition (prednisolone, heparin, thiotriazoline), that can help in choosing of patient treatment tactics.	Heparin	326-333	fibrinogen beta chain	Homo sapiens	99-109
14618797-3	2003	Convincing, statistically significant data have been obtained on a decline in the concentration of fibrinogen in those patients with acute viral myocarditis placed on a complex therapy, running a mild course of the disease, a mild one presenting with elevated indices for hemostasis, and moderately severe course (diclofenac, heparin, thiotriazoline) as well, in grave condition (prednisolone, heparin, thiotriazoline), that can help in choosing of patient treatment tactics.	Heparin	394-401	fibrinogen beta chain	Homo sapiens	99-109
12695507-10	2003	Thus, exogenous AT can compete with the AT moiety of ATH for binding to the covalently linked heparin chain, leading to catalytic inhibition of factor Xa or thrombin.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	157-165
12684504-5	2003	Hybrid apolipoprotein and apoE3-N-terminal, but not apoLp-III, bound to heparin-Sepharose.	Heparin	72-79	apolipoprotein E	Homo sapiens	7-21
12766186-4	2003	[3H]-IP3 binding was inhibited by heparin, 2-APB and xestospongin C. Microsomal Ca2+-ATPase activity was inhibited by thapsigargin.	Heparin	34-41	Sarco/endoplasmic reticulum Ca(2+)-ATPase	Drosophila melanogaster	80-91
12684504-5	2003	Hybrid apolipoprotein and apoE3-N-terminal, but not apoLp-III, bound to heparin-Sepharose.	Heparin	72-79	apolipoprotein E	Homo sapiens	26-31
12734113-8	2003	To elucidate the role of the heparin-binding domain in modulating angiogenesis, we showed that wild-type kallistatin interrupted the binding of (125)I-labeled VEGF to endothelial cells, whereas kallistatin mutant K312A/K313A did not interfere with VEGF binding.	Heparin	29-36	vascular endothelial growth factor A	Homo sapiens	159-163
12734113-8	2003	To elucidate the role of the heparin-binding domain in modulating angiogenesis, we showed that wild-type kallistatin interrupted the binding of (125)I-labeled VEGF to endothelial cells, whereas kallistatin mutant K312A/K313A did not interfere with VEGF binding.	Heparin	29-36	vascular endothelial growth factor A	Homo sapiens	248-252
12734113-10	2003	Taken together, these results indicate that the heparin-binding domain, but not the reactive site loop of kallistatin, is essential for inhibiting VEGF-induced angiogenesis.	Heparin	48-55	vascular endothelial growth factor A	Homo sapiens	147-151
12871332-5	2003	Recombinant VWF A1 domain (rVWF-A1) bound specifically and saturably to sulfatides (half-maximal concentration of approximately 12.5 microg mL(-1)), binding that was blocked by dextran sulfate (IC(50) approximately equal to 100 microg mL(-1)) but not by heparin at concentrations up to 100 U mL(-1).	Heparin	254-261	von Willebrand factor	Homo sapiens	12-15
12626395-0	2003	The binding of human glial cell line-derived neurotrophic factor to heparin and heparan sulfate: importance of 2-O-sulfate groups and effect on its interaction with its receptor, GFRalpha1.	Heparin	68-75	glial cell derived neurotrophic factor	Homo sapiens	21-64
12626395-3	2003	The binding of GDNF to heparin is particularly dependent on the presence of 2-O-sulfate groups.	Heparin	23-30	glial cell derived neurotrophic factor	Homo sapiens	15-19
12626395-5	2003	We also show that heparin at low concentrations protects GDNF from proteolytic modification by an endoprotease and also promotes the binding of GDNF to its receptor polypeptide, GFRalpha1.	Heparin	18-25	glial cell derived neurotrophic factor	Homo sapiens	57-61
12626395-5	2003	We also show that heparin at low concentrations protects GDNF from proteolytic modification by an endoprotease and also promotes the binding of GDNF to its receptor polypeptide, GFRalpha1.	Heparin	18-25	glial cell derived neurotrophic factor	Homo sapiens	144-148
12626395-7	2003	Considered overall, these findings provide strong support for a hypothesis that the bioactivity of GDNF during prenatal development is essentially dependent on the binding of this growth factor to 2-O-sulfate-rich heparin-related glycosaminoglycan.	Heparin	214-221	glial cell derived neurotrophic factor	Homo sapiens	99-103
12871328-1	2003	Antithrombin and its cofactor, heparin, target both the product of prothrombin activation by prothrombinase, thrombin, as well as the enzyme responsible for the reaction, factor (F)Xa.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	67-78
12871328-1	2003	Antithrombin and its cofactor, heparin, target both the product of prothrombin activation by prothrombinase, thrombin, as well as the enzyme responsible for the reaction, factor (F)Xa.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	4-12
12773140-4	2003	lipid fuel source (Intralipid 20%/heparin) that would incur only a modest increase in insulin.	Heparin	34-41	insulin	Homo sapiens	86-93
12773140-17	2003	CONCLUSIONS: These data showed that Intralipid/heparin: (i) are not sufficient to trigger the effect of dexamethasone on leptin, (ii) have an acute inhibitory effect on both fasting and insulin-stimulated leptin levels, and (iii) that this inhibitory effect cannot reverse the strong stimulatory effect of dexamethasone and insulin on serum leptin.	Heparin	47-54	insulin	Homo sapiens	186-193
12801846-8	2003	With long periods of incubation (24-48h), both unfractionated heparin and enoxaparin significantly increased TFPI release (control vs. unfractionated heparin, p&lt;0.05-0.001; control vs. enoxaparin, p&lt;0.01-0.001) and also reduced the release of vWF in the culture medium, though no variations in endothelial cell procoagulant activity or TF content were observed.	Heparin	62-69	von Willebrand factor	Homo sapiens	249-252
12731055-5	2003	Heparin inhibited intracellular calcium flux, respiratory burst and chemotactic responses of eosinophils to CCL11, but not to the chemoattractant C5a, and inhibited binding of CCL11 to CCR3.	Heparin	0-7	C-C motif chemokine ligand 11	Homo sapiens	108-113
12637571-7	2003	Consistent with these findings, soluble heparin competed for VEGF binding to endothelial cells under acidic conditions.	Heparin	40-47	vascular endothelial growth factor A	Homo sapiens	61-65
12637571-8	2003	However, at neutral pH (7.5) low concentrations of heparin (0.1-1.0 microg/ml) potentiated VEGF binding.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	91-95
12743035-4	2003	Moreover, AR gene silencing by siRNA or inhibition of AR biological activity by neutralizing antibodies and heparin prevents GPCR-induced EGFR tyrosine phosphorylation, downstream mitogenic signalling events, cell proliferation, migration and activation of the survival mediator Akt/PKB.	Heparin	108-115	epidermal growth factor receptor	Homo sapiens	138-142
12598527-0	2003	VEGF162, a new heparin-binding vascular endothelial growth factor splice form that is expressed in transformed human cells.	Heparin	15-22	vascular endothelial growth factor A	Homo sapiens	31-65
12701115-3	2003	Eosinophil granule proteins and purified eosinophil peroxidase markedly reduced the anticoagulant properties of the mast cell tryptase/heparin complex.	Heparin	135-142	eosinophil peroxidase	Homo sapiens	41-62
12701115-4	2003	Moreover, eosinophil peroxidase by itself functioned as a powerful procoagulant and also inhibited the anticoagulant actions of heparin in a chromogenic assay for antithrombin III/factor Xa activity.	Heparin	128-135	eosinophil peroxidase	Homo sapiens	10-31
12924614-2	2003	Through the application of heparin and lowering the pH value, lipoproteins and fibrinogen are reduced by 50-60%.	Heparin	27-34	fibrinogen beta chain	Homo sapiens	79-89
12731055-5	2003	Heparin inhibited intracellular calcium flux, respiratory burst and chemotactic responses of eosinophils to CCL11, but not to the chemoattractant C5a, and inhibited binding of CCL11 to CCR3.	Heparin	0-7	C-C motif chemokine ligand 11	Homo sapiens	176-181
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	0-7	C-C motif chemokine ligand 11	Homo sapiens	49-54
15170395-4	2003	Soon after heparin administration and the start of CPB, k(inh) increased 25-fold resulting in decreased active thrombin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	111-119
12739991-3	2003	Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	99-107
12739991-3	2003	Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases.	Heparin	50-58	coagulation factor II, thrombin	Homo sapiens	99-107
12756357-0	2003	R136K fibroblast growth factor-1 mutant induces heparin-independent migration of endothelial cells through fibrin glue.	Heparin	48-55	fibroblast growth factor 1	Homo sapiens	6-32
12756357-15	2003	CONCLUSION: Site-directed mutagenesis of FGF-1 to R136K enables induction of heparin-independent migration of EC through fibrin glue at an optimal concentration of 100 ng/mL.	Heparin	77-84	fibroblast growth factor 1	Homo sapiens	41-46
12744932-4	2003	Heparin inhibited this effect of VEGF.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	33-37
12744932-10	2003	VEGF (1, 10 and 100 ng/ml+/-1 microg/ml heparin or +/-100 microM L-NAME) and PlGF (1, 10, 100 ng/ml) were tested.	Heparin	40-47	vascular endothelial growth factor A	Homo sapiens	0-4
12588864-0	2003	Characterization of the heparin binding sites in human apolipoprotein E.	Heparin	24-31	apolipoprotein E	Homo sapiens	55-71
14577148-7	2003	Ancystron-H is used for determination of fibrinogen level in blood plasma of patients undergoing heparin treatment and blood coagulation inhibitors accumulation.	Heparin	97-104	fibrinogen beta chain	Homo sapiens	41-51
12588864-2	2003	Both the 22-kDa N-terminal domain and 10-kDa C-terminal domain of apoE contain a heparin binding site; the N-terminal site overlaps with the low density lipoprotein receptor binding region and the C-terminal site is undefined.	Heparin	81-88	apolipoprotein E	Homo sapiens	66-70
12588864-3	2003	To understand the molecular details of the apoE-heparin interaction, we defined the microenvironments of all 12 lysine residues in intact apoE3 and examined their relative contributions to heparin binding.	Heparin	48-55	apolipoprotein E	Homo sapiens	43-47
12588864-6	2003	With lipidated apoE3, it is confirmed that the Lys-233 site is completely masked and the N-terminal site mediates heparin binding.	Heparin	114-121	apolipoprotein E	Homo sapiens	15-20
12588864-7	2003	In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state.	Heparin	34-41	apolipoprotein E	Homo sapiens	66-71
12588864-7	2003	In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state.	Heparin	34-41	apolipoprotein E	Homo sapiens	66-70
12588864-7	2003	In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state.	Heparin	133-140	apolipoprotein E	Homo sapiens	66-71
12588864-7	2003	In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state.	Heparin	133-140	apolipoprotein E	Homo sapiens	66-70
12686329-11	2003	vWF is linked to inflammation and, like glycoprotein Ib/IX, is affected more favorably by the LWMHs than by UFH.	Heparin	108-111	von Willebrand factor	Homo sapiens	0-3
12591924-3	2003	The abnormal antithrombin was separated from the normal inhibitor by complexing the latter with thrombin followed by heparin-agarose affinity chromatography.	Heparin	117-124	coagulation factor II, thrombin	Homo sapiens	17-25
12591924-4	2003	The purified variant, antithrombin London, was completely inactive as a thrombin or factor Xa inhibitor even after heparin activation.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	26-34
12591924-7	2003	Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	74-82
12591924-7	2003	Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction.	Heparin	134-141	coagulation factor II, thrombin	Homo sapiens	74-82
12692004-4	2003	The FGF-1/oxLDL complex had a dramatically decreased ability to bind heparin and was nonmitogenic on cultured smooth muscle cells.	Heparin	69-76	fibroblast growth factor 1	Homo sapiens	4-9
12551943-10	2003	To further explore how LPL is distributed in the tissue, heparin (which detaches the enzyme from the endothelial surface) was injected.	Heparin	57-64	lipoprotein lipase	Rattus norvegicus	23-26
12551943-11	2003	Tissue LPL activity decreased by about 10% in 2 min and by 50% in 1 h. Heparin released mainly the active form of the lipase.	Heparin	71-78	lipoprotein lipase	Rattus norvegicus	7-10
12551943-13	2003	The fraction of extracellular LPL that heparin released and the time course were the same in fed and fasted rats, indicating that active, extracellular LPL was distributed in a similar way in the two nutritional states.	Heparin	39-46	lipoprotein lipase	Rattus norvegicus	30-33
12682461-9	2003	Heparin, despite effectively inhibiting thrombin formation, has not shown consistent benefits in reducing lung injury, and its efficacy has not yet been evaluated in a controlled study.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	40-48
12663052-11	2003	After heparin-induced rescue of tryptase activity, the major part of the tryptase activity was sensitive to inhibition by bovine pancreatic trypsin inhibitor, whereas tryptase before addition of polycationic peptide was completely resistant.	Heparin	6-13	trophoblast Kunitz domain protein 1	Bos taurus	140-157
12652502-0	2003	Thrombin injection for treatment of false aneurysms after failed compression therapy in patients on full-dose antiplatelet and heparin therapy.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	0-8
12652502-1	2003	The aim of this study was to gauge the effectiveness of thrombin injection after failed manual compression in patients with false aneurysms receiving full-dose antiplatelet and heparin therapy.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	56-64
12652502-12	2003	In patients with false aneurysms and failed compression therapy under full-dose aspirin, clopidogrel, and heparin, selective thrombin injection is highly effective and safe.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	125-133
12698397-16	2003	The UFH-based strategy and supplementation with AT III, r-hirudin, and tirofiban resulted in significantly reduced (p &lt; 0.05) thrombin generation compared with ACT management.	Heparin	4-7	coagulation factor II, thrombin	Homo sapiens	129-137
12579570-11	2003	Furthermore, addition of heparin with either FGF-1 or FGF-2 into the hydrogel resulted in a significantly enhanced and prolonged vascularization effect.	Heparin	25-32	fibroblast growth factor 1	Mus musculus	45-50
12482864-6	2003	Because heparin competed with decorin competitively, binding of decorin to fibronectin likely occurs at a heparin-binding region.	Heparin	8-15	fibronectin 1	Homo sapiens	75-86
12482864-6	2003	Because heparin competed with decorin competitively, binding of decorin to fibronectin likely occurs at a heparin-binding region.	Heparin	106-113	fibronectin 1	Homo sapiens	75-86
12818259-0	2003	Additive thrombin inhibition by fast moving heparin and dermatan sulfate explains the anticoagulant effect of sulodexide, a natural mixture of glycosaminoglycans.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	9-17
12598330-4	2003	A response was acquired, however, when myofibroblasts were incubated with FGF-2 in the presence of heparan sulfate (HS) and heparin.	Heparin	124-131	fibroblast growth factor 2	Homo sapiens	74-79
12678905-13	2003	VEGF is a 45 kDA glycoprotein, homodimeric, basic, and able to bind heparin.	Heparin	68-75	vascular endothelial growth factor A	Homo sapiens	0-4
12579570-12	2003	These results indicate that the controlled release of biologically active FGF-1 and FGF-2 with heparin is caused by biodegradation of the chitosan hydrogel, and subsequent induction of vascularization.	Heparin	95-102	fibroblast growth factor 1	Mus musculus	74-79
12644344-2	2003	Direct thrombin inhibitors are theoretically likely to be more effective than indirect thrombin inhibitors, such as unfractionated heparin or low-molecular-weight heparin, because the heparins block only circulating thrombin, whereas direct thrombin inhibitors block both circulating and clot-bound thrombin.	Heparin	184-192	coagulation factor II, thrombin	Homo sapiens	7-15
12768067-0	2003	Heparin reduces glomerular infiltration and TGF-beta protein expression by macrophages in puromycin glomerulosclerosis.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	44-52
12768067-5	2003	These effects were associated with the prevention of macrophage glomerular infiltration, and the inhibition of the TGF-beta axes in foam cells as shown by the reduction in cytoplasm immunostaining for TGF-beta and LTBP-1; heparin also reduced peri-macrophagic collagen IV deposition.	Heparin	222-229	transforming growth factor beta 1	Homo sapiens	115-123
12768067-6	2003	CONCLUSIONS: The inhibition of TGF-beta in macrophages seems to be part of heparin general activities.	Heparin	75-82	transforming growth factor beta 1	Homo sapiens	31-39
12768067-7	2003	The inhibitory effect of heparin on macrophage infiltration and TGF-beta synthesis in this renal disease model supports the notion that heparin and derived molecules constitute potentially useful therapeutic agents in nephropathies.	Heparin	25-32	transforming growth factor beta 1	Homo sapiens	64-72
12768067-7	2003	The inhibitory effect of heparin on macrophage infiltration and TGF-beta synthesis in this renal disease model supports the notion that heparin and derived molecules constitute potentially useful therapeutic agents in nephropathies.	Heparin	136-143	transforming growth factor beta 1	Homo sapiens	64-72
12640331-0	2003	Heparin stimulates production of bFGF and TGF-beta 1 by human normal, keloid, and fetal dermal fibroblasts.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	33-37
12640331-0	2003	Heparin stimulates production of bFGF and TGF-beta 1 by human normal, keloid, and fetal dermal fibroblasts.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	42-52
12640331-2	2003	Heparin may mediate these effects by altering the levels of growth factors such as basic fibroblast growth factor (bFGF) and transforming growth factor-beta 1 (TGF-b1).	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	83-113
12640331-2	2003	Heparin may mediate these effects by altering the levels of growth factors such as basic fibroblast growth factor (bFGF) and transforming growth factor-beta 1 (TGF-b1).	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	115-119
12640331-2	2003	Heparin may mediate these effects by altering the levels of growth factors such as basic fibroblast growth factor (bFGF) and transforming growth factor-beta 1 (TGF-b1).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	125-158
12640331-2	2003	Heparin may mediate these effects by altering the levels of growth factors such as basic fibroblast growth factor (bFGF) and transforming growth factor-beta 1 (TGF-b1).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	160-166
12640331-8	2003	All doses of heparin significantly stimulated production of bFGF by normal (341% to 1137% increase), keloid (237% to 1955% increase), and fetal fibroblasts (292% to 1866% increase) at all time points (p&lt;0.05).	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	60-64
12640331-9	2003	Heparin (300 microg/ml and 600 microg/ml) also stimulated production of TGF-b1 by normal (56% to 75%), keloid (105% to 269%), and fetal fibroblasts (25% to 57%), with statistical significance (p&lt;0.05) at various time points.	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	72-78
12640331-11	2003	CONCLUSIONS: Heparin inhibits proliferation by keloid and fetal fibroblasts and significantly stimulates production of bFGF and TGF-b1 by normal, keloid, and fetal dermal fibroblasts.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	119-123
12640331-11	2003	CONCLUSIONS: Heparin inhibits proliferation by keloid and fetal fibroblasts and significantly stimulates production of bFGF and TGF-b1 by normal, keloid, and fetal dermal fibroblasts.	Heparin	13-20	transforming growth factor beta 1	Homo sapiens	128-134
12603746-5	2003	Three B. burgdorferi surface proteins, Bgp, DbpA and DbpB, have been demonstrated previously to bind to GAGs or to GAG-containing molecules, and we show here that recombinant derivatives of each of these proteins were able to bind to purified heparin and dermatan sulphate.	Heparin	243-250	Y-box binding protein 1	Homo sapiens	53-57
12644344-2	2003	Direct thrombin inhibitors are theoretically likely to be more effective than indirect thrombin inhibitors, such as unfractionated heparin or low-molecular-weight heparin, because the heparins block only circulating thrombin, whereas direct thrombin inhibitors block both circulating and clot-bound thrombin.	Heparin	184-192	coagulation factor II, thrombin	Homo sapiens	87-95
12393592-1	2003	Some cases of heparin-induced thrombocytopenia (HIT) have been reported to be associated with antibodies against interleukin-8 (IL-8), a chemokine related to platelet factor 4.	Heparin	14-21	C-X-C motif chemokine ligand 8	Homo sapiens	113-126
12393592-1	2003	Some cases of heparin-induced thrombocytopenia (HIT) have been reported to be associated with antibodies against interleukin-8 (IL-8), a chemokine related to platelet factor 4.	Heparin	14-21	C-X-C motif chemokine ligand 8	Homo sapiens	128-132
12393592-3	2003	This activation occurred at IL-8 concentrations achievable in vivo and was facilitated by heparin (0.1 U/mL).	Heparin	90-97	C-X-C motif chemokine ligand 8	Homo sapiens	28-32
12644344-2	2003	Direct thrombin inhibitors are theoretically likely to be more effective than indirect thrombin inhibitors, such as unfractionated heparin or low-molecular-weight heparin, because the heparins block only circulating thrombin, whereas direct thrombin inhibitors block both circulating and clot-bound thrombin.	Heparin	184-192	coagulation factor II, thrombin	Homo sapiens	87-95
12644344-2	2003	Direct thrombin inhibitors are theoretically likely to be more effective than indirect thrombin inhibitors, such as unfractionated heparin or low-molecular-weight heparin, because the heparins block only circulating thrombin, whereas direct thrombin inhibitors block both circulating and clot-bound thrombin.	Heparin	184-192	coagulation factor II, thrombin	Homo sapiens	87-95
12644344-2	2003	Direct thrombin inhibitors are theoretically likely to be more effective than indirect thrombin inhibitors, such as unfractionated heparin or low-molecular-weight heparin, because the heparins block only circulating thrombin, whereas direct thrombin inhibitors block both circulating and clot-bound thrombin.	Heparin	184-192	coagulation factor II, thrombin	Homo sapiens	87-95
12535736-5	2003	Significantly enhanced binding (4.6-fold) and internalisation (2.6-fold) of 125I-LDL by N9 compared with D9 cells was eradicated by pre-treatment with either heparin or heparinase, confirming involvement of LPL and cell surface proteoglycans.	Heparin	158-165	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	207-210
12540482-2	2003	We previously showed that covalent antithrombin-heparin complex (ATH) is superior to noncovalent antithrombin (AT) + heparin (H) mixtures at inhibiting plasma thrombin generation on rat fetal distal lung epithelium (FDLE) in vitro.	Heparin	48-55	coagulation factor II	Rattus norvegicus	39-47
12576961-14	2003	Heparin administration further increased, in a dose-dependent manner, myeloperoxidase activity and P-selectin expression in the lung in animals with pancreatitis.	Heparin	0-7	selectin P	Rattus norvegicus	99-109
12729008-2	2003	Alpha-Toc also suppressed the decrease in the heparin-binding activity of apoE in the VLDL oxidation.	Heparin	46-53	apolipoprotein E	Homo sapiens	74-78
12871500-5	2003	It does not inhibit hydrolysis of small chromogenic thrombin substrates, nor does it influence the heparin-catalyzed inactivation of thrombin by antithrombin.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	133-141
12568929-0	2003	Inhibition of cryogelation by the novel synthetic peptide (Gly-Arg-Lys-Lys-Thr): recognition site of extra domain A containing fibronectin for heparin in cryogelation.	Heparin	143-150	fibronectin 1	Homo sapiens	127-138
14574076-2	2003	Unfractionated heparin (UFH) has been the thrombin inhibitor of choice for decades.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	42-50
14574076-2	2003	Unfractionated heparin (UFH) has been the thrombin inhibitor of choice for decades.	Heparin	24-27	coagulation factor II, thrombin	Homo sapiens	42-50
12696182-5	2003	In contrast, argatroban, heparin, and low-molecular-weight heparin (LMWH; dalteparin) inhibited thrombin-induced platelet aggregation at concentrations lower than those needed for their anticoagulant actions.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	96-104
12696182-5	2003	In contrast, argatroban, heparin, and low-molecular-weight heparin (LMWH; dalteparin) inhibited thrombin-induced platelet aggregation at concentrations lower than those needed for their anticoagulant actions.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	96-104
15041796-4	2003	Here, we have generated a novel heparin-binding form of VEGF-E by introducing the heparin-domain of the human VEGF-A(165) splice variant into the viral VEGF-E protein.	Heparin	32-39	vascular endothelial growth factor A	Homo sapiens	110-116
12475577-8	2003	CONCLUSION: Short-term low-dose heparin plus bedrest suppresses 1,25-dihydroxyvitamin D(3) and osteocalcin levels in pregnancy.	Heparin	32-39	bone gamma-carboxyglutamate protein	Homo sapiens	95-106
15041796-4	2003	Here, we have generated a novel heparin-binding form of VEGF-E by introducing the heparin-domain of the human VEGF-A(165) splice variant into the viral VEGF-E protein.	Heparin	82-89	vascular endothelial growth factor A	Homo sapiens	110-116
12493698-11	2003	As in follicular fluid, cleavage of IGFBP-2 by rhPAPP-A was dose-dependently enhanced by IGFs and inhibited by a peptide derived from the heparin-binding domain of IGFBP-5 (P5).	Heparin	138-145	insulin like growth factor binding protein 2	Bos taurus	36-43
12493698-11	2003	As in follicular fluid, cleavage of IGFBP-2 by rhPAPP-A was dose-dependently enhanced by IGFs and inhibited by a peptide derived from the heparin-binding domain of IGFBP-5 (P5).	Heparin	138-145	insulin like growth factor binding protein 5	Bos taurus	164-171
12493698-15	2003	In atretic follicles, the increase and decrease in IGFBP-2 and PAPP-A mRNA expression, respectively, as well as the inhibition of PAPP-A activity by heparin-binding domains present in IGFBP-5 or other proteins, might participate in higher IGFBP-2 levels and a decrease in IGF bioavailability.	Heparin	149-156	insulin like growth factor binding protein 5	Bos taurus	184-191
12493698-15	2003	In atretic follicles, the increase and decrease in IGFBP-2 and PAPP-A mRNA expression, respectively, as well as the inhibition of PAPP-A activity by heparin-binding domains present in IGFBP-5 or other proteins, might participate in higher IGFBP-2 levels and a decrease in IGF bioavailability.	Heparin	149-156	insulin like growth factor binding protein 2	Bos taurus	239-246
12583005-2	2003	Although the structural requirements of heparin and heparan sulfate for the high-affinity binding to bFGF have been extensively examined, studies on intact heparin proteoglycans are limited.	Heparin	40-47	fibroblast growth factor 2	Homo sapiens	101-105
12583005-7	2003	Heparin-BSA-bFGF conjugate was obtained following incubation of heparin-BSA with bFGF for 2 h at 37 degrees C. Intact heparin, heparin-BSA and heparin-BSA-bFGF conjugates were completely resolved by CZE using 50 mM phosphate, pH 3.5, as operating buffer, reversed polarity (30 kV) and detection at 232 nm.	Heparin	64-71	fibroblast growth factor 2	Homo sapiens	12-16
12583005-8	2003	Competitive solid phase assay showed that, among the glycosaminoglycans tested, heparin exhibits the highest affinity binding to bFGF (IC(50) = 6.4 nM).	Heparin	80-87	fibroblast growth factor 2	Homo sapiens	129-133
12583005-10	2003	The developed CZE method is rapid and accurate and can be easily used to identify bFGF-interacting heparin preparations of biopharmaceutical importance.	Heparin	99-106	fibroblast growth factor 2	Homo sapiens	82-86
12508198-1	2003	We evaluated a combination therapy using glycoprotein IIb/IIIa receptor antagonism and direct thrombin inhibition in nine patients with heparin-induced thrombocytopenia (HIT) undergoing 10 percutaneous coronary interventions (PCIs).	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	94-102
14651331-5	2003	In insulin resistant states, a decreased post-heparin plasma LPL activity contributes to a low HDL cholesterol, whereas an increased activity of HL reduces HDL particle size by hydrolysing its triglycerides and phospholipids.	Heparin	46-53	insulin	Homo sapiens	3-10
14515016-3	2003	Because many of heparin"s effects are mediated by suppression of thrombin generation and activity, this study assessed the influence of thrombin inhibition on PCF.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	65-73
14515016-20	2003	These results indicate that some of the antiplatelet effects of heparin are the result of thrombin inhibition and that low-level thrombin generation is essential for clot retraction.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	90-98
14593356-13	2003	CONCLUSION: Short term use of ticlopidine in patients with NSTEACS treated with aspirin and unfractionated heparin was associated with lower levels of TAT and fibrinogen (relative to control group) on day 14.	Heparin	107-114	fibrinogen beta chain	Homo sapiens	159-169
12656349-2	2003	Heparin is generally thought to play an extremely important role in regulating aFGF and bFGF bioactivities through its strong binding with them.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	79-83
12656349-2	2003	Heparin is generally thought to play an extremely important role in regulating aFGF and bFGF bioactivities through its strong binding with them.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	88-92
12527510-2	2003	METHODS: The recombinant yeast strain containing the gene sequence encoding highly soluble rhES was induced by methanol for rhES production, which was purified with heparin affinity chromatography.	Heparin	165-172	RASD family, member 2	Mus musculus	91-95
12527510-2	2003	METHODS: The recombinant yeast strain containing the gene sequence encoding highly soluble rhES was induced by methanol for rhES production, which was purified with heparin affinity chromatography.	Heparin	165-172	RASD family, member 2	Mus musculus	124-128
12634322-8	2003	Together with results of previous studies, we concluded that the multivalent trisulfated heparin-like unit is another structure involved in strong binding to MK.	Heparin	89-96	midkine	Homo sapiens	158-160
12656349-9	2003	These methods established here can be used for analysing the effect of sulfate groups in heparin on the binding with other human FGF members or other heparin-binding proteins.	Heparin	89-96	fibroblast growth factor 1	Homo sapiens	129-132
12679132-10	2003	We conclude that argatroban seems to be a more efficient and safer anticoagulant than UFH for the prevention of thrombus formation and acceleration of t-PA-induced thrombolysis.	Heparin	86-89	plasminogen activator, tissue type	Homo sapiens	151-155
12493544-4	2003	Aptamer ODN 2 is directed against the thrombin heparin binding site (exosite 2).	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	38-46
15013278-7	2003	Results of experiments on gel-filtered platelets from humans indicate that the inhibition of thrombin-induced platelet aggregation caused by UFH and LMWH in the presence of AT is more prominent than that caused by DHG with HCII.	Heparin	141-144	coagulation factor II, thrombin	Homo sapiens	93-101
14698650-0	2003	Signs of thrombin generation in pediatric cardiac catheterization with unfractionated heparin bolus or subcutaneous low molecular weight heparin for antithrombotic cover.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	9-17
14698650-0	2003	Signs of thrombin generation in pediatric cardiac catheterization with unfractionated heparin bolus or subcutaneous low molecular weight heparin for antithrombotic cover.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	9-17
15013278-3	2003	In contrast to UFH and LMWH, which exert their anticoagulant effects by inhibiting thrombin in the presence of antithrombin III (AT), DHG exerts its anticoagulant effect by inhibiting the intrinsic factor Xase complex and thrombin in the presence of heparin cofactor II (HCII).	Heparin	15-18	coagulation factor II, thrombin	Homo sapiens	83-91
12484774-7	2002	Among the 12 beta-strands constituting the beta-barrel architecture of hFGF-1, beta-strand XI, located in the heparin binding domain, exhibits the lowest average protection factor value.	Heparin	110-117	fibroblast growth factor 1	Homo sapiens	71-77
14663596-2	2003	By means of heparin and lowering the pH level, lipoproteins and fibrinogen are reduced by 50-60%.	Heparin	12-19	fibrinogen beta chain	Homo sapiens	64-74
14663601-8	2003	In a prospective pilot-study we examined whether drastic postoperative lowering of fibrinogen by H.E.L.P.-(Heparin-mediated Extracorporeal LDL-/Fibrinogen Precipitation) apheresis can prevent early graft vessel closure in patients undergoing CABG.	Heparin	107-114	fibrinogen beta chain	Homo sapiens	83-93
14663601-8	2003	In a prospective pilot-study we examined whether drastic postoperative lowering of fibrinogen by H.E.L.P.-(Heparin-mediated Extracorporeal LDL-/Fibrinogen Precipitation) apheresis can prevent early graft vessel closure in patients undergoing CABG.	Heparin	107-114	fibrinogen beta chain	Homo sapiens	144-154
12377765-0	2002	Mapping the heparin-binding site on the 13-14F3 fragment of fibronectin.	Heparin	12-19	fibronectin 1	Homo sapiens	60-71
12377765-2	2002	Various studies have revealed that the human 13th and 14th fibronectin type III domains (labeled (13)F3 and (14)F3 here) contain a heparin-binding site.	Heparin	131-138	fibronectin 1	Homo sapiens	59-70
12470644-3	2002	First, when we abolished [Ca(2+)](i) increases by injecting BAPTA or heparin into UV-treated HeLa cells, cytochrome c release was either blocked or severely delayed.	Heparin	69-76	cytochrome c, somatic	Homo sapiens	105-117
12374809-0	2002	Heparin and heparan sulfate disaccharides bind to the exchanger inhibitor peptide region of Na+/Ca2+ exchanger and reduce the cytosolic calcium of smooth muscle cell lines.	Heparin	0-7	solute carrier family 8 member A1	Homo sapiens	92-110
12392734-0	2002	Identification of novel inhibitors of fibroblast growth factor (FGF-2) binding to heparin and endothelial cell survival from a structurally diverse carbohybrid library.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	64-69
12460379-5	2002	TNF-alpha in FBS required a higher concentration of heparin (50% concentration inhibition [IC50] &gt; 20microg/ml) to inhibit adsorption to the heparin beads-column compared with IL-6, probably because of a stronger interaction between TNF-alpha and heparin-beads.	Heparin	52-59	tumor necrosis factor	Homo sapiens	0-9
12460379-5	2002	TNF-alpha in FBS required a higher concentration of heparin (50% concentration inhibition [IC50] &gt; 20microg/ml) to inhibit adsorption to the heparin beads-column compared with IL-6, probably because of a stronger interaction between TNF-alpha and heparin-beads.	Heparin	52-59	tumor necrosis factor	Homo sapiens	236-245
12460379-5	2002	TNF-alpha in FBS required a higher concentration of heparin (50% concentration inhibition [IC50] &gt; 20microg/ml) to inhibit adsorption to the heparin beads-column compared with IL-6, probably because of a stronger interaction between TNF-alpha and heparin-beads.	Heparin	144-151	tumor necrosis factor	Homo sapiens	0-9
12460379-5	2002	TNF-alpha in FBS required a higher concentration of heparin (50% concentration inhibition [IC50] &gt; 20microg/ml) to inhibit adsorption to the heparin beads-column compared with IL-6, probably because of a stronger interaction between TNF-alpha and heparin-beads.	Heparin	144-151	tumor necrosis factor	Homo sapiens	236-245
12460379-5	2002	TNF-alpha in FBS required a higher concentration of heparin (50% concentration inhibition [IC50] &gt; 20microg/ml) to inhibit adsorption to the heparin beads-column compared with IL-6, probably because of a stronger interaction between TNF-alpha and heparin-beads.	Heparin	144-151	tumor necrosis factor	Homo sapiens	0-9
12460379-5	2002	TNF-alpha in FBS required a higher concentration of heparin (50% concentration inhibition [IC50] &gt; 20microg/ml) to inhibit adsorption to the heparin beads-column compared with IL-6, probably because of a stronger interaction between TNF-alpha and heparin-beads.	Heparin	144-151	tumor necrosis factor	Homo sapiens	236-245
12460379-8	2002	Therefore, the adsorption of inflammatory cytokines, especially TNF-alpha, onto the inner heparin-coated surface of an extracorporeal circuit may partly account for a reduction in inflammatory responses.	Heparin	90-97	tumor necrosis factor	Homo sapiens	64-73
12492611-9	2002	The TFPI release rate rapidly increased to maximum of 200 +/- 45 micro g min-1 after 17.5 min heparin infusion but did not increase further although heparin concentrations further doubled.	Heparin	94-101	CD59 molecule (CD59 blood group)	Homo sapiens	73-78
12429975-6	2002	The protein levels of VEGF were markedly increased only in the VEGF189-transfectants cultured in the presence of heparin.	Heparin	113-120	vascular endothelial growth factor A	Homo sapiens	22-26
12466122-8	2002	In vitro, anti-thrombin formed complexes more readily with human kallikrein 2, particularly in the presence of heparin, and less efficiently with prostate-specific antigen.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	15-23
12643418-3	2002	We present a patient with a clinical picture of heparin-induced thrombocytopenia type II who was effectively anticoagulated with bivalirudin, a direct thrombin inhibitor, during cardiopulmonary bypass for a cardiac operation.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	151-159
12441912-6	2002	Combined with UFH, rt-PA and r-PA increased the aPTT versus UFH alone (P &lt; 0.05 for both).	Heparin	60-63	plasminogen activator, tissue type	Homo sapiens	29-33
12544717-2	2002	The aim of this study was to evaluate whether there was a relationship between IgE serum levels and plasma concentration of endogenous heparin in patients with myocardial infarction.	Heparin	135-142	immunoglobulin heavy constant epsilon	Homo sapiens	79-82
12544717-8	2002	Higher levels of IgE were strongly correlated with higher concentrations of endogenous heparin ( r= 0.80, p &lt; 0.001).	Heparin	87-94	immunoglobulin heavy constant epsilon	Homo sapiens	17-20
12544717-10	2002	CONCLUSION: The results suggest that high concentrations of endogenous heparin in association with high IgE concentrations and their negative influence on thrombinogenesis, may act as a marker for a favourable prognosis in patients with MI.	Heparin	71-78	immunoglobulin heavy constant epsilon	Homo sapiens	104-107
12384988-5	2002	In a similar manner as NH, the modified heparins were capable of inhibiting activation of ERK1 and 2 and DNA synthesis induced by FCS and hbEGF whereas the modified heparins potentiated the mitogenic effect of bFGF and no compound affected PDGF BB-induced ERK activity and SMC growth.	Heparin	40-48	heparin-binding EGF-like growth factor	Rattus norvegicus	138-143
12384988-5	2002	In a similar manner as NH, the modified heparins were capable of inhibiting activation of ERK1 and 2 and DNA synthesis induced by FCS and hbEGF whereas the modified heparins potentiated the mitogenic effect of bFGF and no compound affected PDGF BB-induced ERK activity and SMC growth.	Heparin	40-48	Eph receptor B1	Rattus norvegicus	90-93
12460766-4	2002	The recombinant mouse heparanase protein was purified to homogeneity from cell lysates by a combination of Con-A affinity chromatography, heparin affinity chromatography, and size exclusion chromatography.	Heparin	138-145	heparanase	Mus musculus	22-32
12186633-2	2002	We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin.	Heparin	133-140	prion protein	Homo sapiens	32-35
12164779-8	2002	To elucidate the mechanism responsible for the effects of THL, we analysed the abundance of heparin-releasable EDL protein from infected HepG2 cells upon incubations with THL, HDL and free (non-esterified) fatty acids (FFAs).	Heparin	92-99	lipase G, endothelial type	Homo sapiens	111-114
12526215-5	2002	Purification of rhES was performed with heparin affinity chromatography.	Heparin	40-47	RASD family, member 2	Mus musculus	16-20
12393591-6	2002	In this report we demonstrate that the flow adherence of sickle cells to thrombin-treated human vascular endothelial cells also uses P-selectin and that this component of adhesion is inhibited by unfractionated heparin.	Heparin	211-218	coagulation factor II, thrombin	Homo sapiens	73-81
12221095-9	2002	The kinetic constants k(a), k(d), and K(d) suggested that MK, PTN, FGF-16, FGF-18, and HB-EGF bound strongly to CS-E, in comparable degrees to the binding to Hep, whereas the intensity of binding of FGF-2 and FGF-10 toward CS-E was lower than that for Hep.	Heparin	158-161	heparin-binding EGF-like growth factor	Rattus norvegicus	87-93
12215437-2	2002	Like most members of the FGF family, the activity of FGF-7 is strongly influenced by binding to heparin, but this glycosaminoglycan is absent on keratinocyte cell surfaces and minimally present in the wound environment.	Heparin	96-103	fibroblast growth factor 7	Homo sapiens	25-28
12215437-2	2002	Like most members of the FGF family, the activity of FGF-7 is strongly influenced by binding to heparin, but this glycosaminoglycan is absent on keratinocyte cell surfaces and minimally present in the wound environment.	Heparin	96-103	fibroblast growth factor 7	Homo sapiens	53-58
12485860-6	2002	However, heparin-binding studies revealed that intact, full-length N-termini of TNF-alpha or its analogs were necessary for high retention on the heparin affinity column, whereas the three-lysine containing tip of LK-805 by itself was not enough for binding.	Heparin	9-16	tumor necrosis factor	Mus musculus	80-89
12414535-0	2002	Heparin inhibits phosphorylation and autonomous activity of Ca(2+)/calmodulin-dependent protein kinase II in vascular smooth muscle cells.	Heparin	0-7	calmodulin 1	Homo sapiens	67-77
12414535-4	2002	Using activity assays, radioactive labeling, and immunoprecipitation it was found that heparin inhibits the overall phosphorylation of the delta-subunit of CaM kinase II which is consistent with inhibition of autophosphorylation-dependent, Ca(2+)/calmodulin-independent CaM kinase II activity.	Heparin	87-94	calmodulin 1	Homo sapiens	247-257
12485860-6	2002	However, heparin-binding studies revealed that intact, full-length N-termini of TNF-alpha or its analogs were necessary for high retention on the heparin affinity column, whereas the three-lysine containing tip of LK-805 by itself was not enough for binding.	Heparin	146-153	tumor necrosis factor	Mus musculus	80-89
12436337-9	2002	CONCLUSION/INTERPRETATION: Increasing plasma NEFA concentrations by oral fat feeding with heparin infusion augments glucose-stimulated insulin secretion with the greatest effect for monounsaturated fatty acids and the lowest effect for saturated fatty acids.	Heparin	90-97	insulin	Homo sapiens	135-142
12381667-4	2002	Rather, changes in the extracellular localization of VEGF-A in heparin-binding mutant embryos resulted in an altered distribution of endothelial cells within the growing vasculature.	Heparin	63-70	vascular endothelial growth factor A	Homo sapiens	53-59
12391246-4	2002	Fucoidin, heparin/heparin sulfate, N-acetyl-D-glucosamine, mannose-6-phosphate, and laminarin were found to inhibit adhesion of T84 cells to CD11b/CD18.	Heparin	10-17	integrin subunit beta 2	Homo sapiens	147-151
12401853-1	2002	BACKGROUND: Recombinant hirudin (r-hirudin) is a highly selective thrombin inhibitor used for anticoagulation in heparin-induced thrombocytopenia type II.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	66-74
12391192-8	2002	Finally, biosensor-based binding kinetic analysis revealed that IFN-kappa, like IFN-beta, binds strongly to heparin (K(d): 2.1 nM), suggesting that the cytokine can be retained close to the local site of production.	Heparin	108-115	interferon kappa	Homo sapiens	64-73
12536119-2	2002	Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	22-30
12536119-3	2002	Although x-ray structures of antithrombin, free and complexed with heparin, have suggested that exposure of a reactive proteinase binding loop is a key feature of conformational activation, mutagenesis of reactive loop residues indicates that the function of this structural change is not to present an optimal loop sequence to target clotting proteinases.	Heparin	67-74	endogenous retrovirus group K member 25	Homo sapiens	119-129
12395090-1	2002	Glial cell-line neurotrophic factor (GDNF), a neurotrophic factor with heparin binding affinity, promotes the survival and differentiation of a variety of neuronal cells including dopaminergic neuron.	Heparin	71-78	glial cell derived neurotrophic factor	Homo sapiens	37-41
12395090-2	2002	The effect of heparin on GDNF signaling was investigated based on the expression of the tyrosine hydroxyrase (TH) gene in neurobalstoma cells.	Heparin	14-21	glial cell derived neurotrophic factor	Homo sapiens	25-29
12395090-3	2002	Up-regulation of TH gene mRNA by GDNF was enhanced by co-administration of heparin.	Heparin	75-82	glial cell derived neurotrophic factor	Homo sapiens	33-37
12395090-4	2002	This facilitation by heparin was particularly evident at suboptimal levels of GDNF, which was consistent with the luciferase assay using TH gene promoter.	Heparin	21-28	glial cell derived neurotrophic factor	Homo sapiens	78-82
12395090-8	2002	These results indicate that interaction with glycosaminoglycans such as heparin affects GDNF signal transduction positively.	Heparin	72-79	glial cell derived neurotrophic factor	Homo sapiens	88-92
12381667-6	2002	The disruption of the normal VEGF-A concentration gradient also impaired the directed extension of endothelial cell filopodia, suggesting that heparin-binding VEGF-A isoforms normally provide spatially restricted stimulatory cues that polarize and thereby guide sprouting endothelial cells to initiate vascular branch formation.	Heparin	143-150	vascular endothelial growth factor A	Homo sapiens	29-35
12381667-6	2002	The disruption of the normal VEGF-A concentration gradient also impaired the directed extension of endothelial cell filopodia, suggesting that heparin-binding VEGF-A isoforms normally provide spatially restricted stimulatory cues that polarize and thereby guide sprouting endothelial cells to initiate vascular branch formation.	Heparin	143-150	vascular endothelial growth factor A	Homo sapiens	159-165
12381667-7	2002	Consistent with this idea, we found opposing defects in embryos harboring only a heparin-binding isoform of VEGF-A, including excess endothelial filopodia and abnormally thin vessel branches in ectopic sites.	Heparin	81-88	vascular endothelial growth factor A	Homo sapiens	108-114
12239166-0	2002	Heparin acts synergistically with interleukin-11 to induce STAT3 activation and in vitro osteoclast formation.	Heparin	0-7	signal transducer and activator of transcription 3	Mus musculus	59-64
12357148-10	2002	CONCLUSION: Compared with heparin management with the activated clotting time, heparin concentration-based anticoagulation management during CPB leads to a significant reduction of thrombin generation, fibrinolysis, and neutrophil activation, whereas there is no difference in the effect on platelet activation.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	181-189
12357148-11	2002	The generation of fibrin even in the presence of high heparin concentrations most likely has to be attributed to the reduced antithrombin III concentrations or reduced inhibition of clot-bound thrombin.	Heparin	54-61	coagulation factor II, thrombin	Homo sapiens	129-137
12239166-7	2002	Heparin was found to enhance both IL-11-induced STAT3-DNA complex formation and transactivation without altering either STAT3 (signal transducer and activator of transcription-3) tyrosine or serine phosphorylation.	Heparin	0-7	signal transducer and activator of transcription 3	Mus musculus	48-53
12239166-8	2002	Heparin was also found to enhance IL-11"s ability to induce the expression of both receptor activator of nuclear factor-kappaB ligand (RANKL) and glycoprotein (gp) 130.	Heparin	0-7	interleukin 6 signal transducer	Mus musculus	146-167
12450065-8	2002	Interestingly, tryptase in the presence of heparin failed to induce relaxation of precontracted neuraminidase-treated rat aorta.	Heparin	43-50	tryptase alpha/beta 1	Rattus norvegicus	15-23
12359775-4	2002	In all four cell lines, AdtrEGFR markedly attenuated EGF and heparin-binding EGF-dependent cell growth, EGFR family tyrosine phosphorylation, and phosphorylation of MAPK, c-Jun NH2-terminal kinase, p38 MAPK, and activating transcription factor 2.	Heparin	61-68	epidermal growth factor receptor	Homo sapiens	28-32
12359775-4	2002	In all four cell lines, AdtrEGFR markedly attenuated EGF and heparin-binding EGF-dependent cell growth, EGFR family tyrosine phosphorylation, and phosphorylation of MAPK, c-Jun NH2-terminal kinase, p38 MAPK, and activating transcription factor 2.	Heparin	61-68	mitogen-activated protein kinase 14	Homo sapiens	198-201
12450065-9	2002	We conclude that tryptase-induced relaxation of rat aorta, most likely via PAR2, is tightly regulated by heparin and cell-surface sialic acid.	Heparin	105-112	tryptase alpha/beta 1	Rattus norvegicus	17-25
12124794-0	2002	Hyaluronate-heparin conjugate gels for the delivery of basic fibroblast growth factor (FGF-2).	Heparin	12-19	fibroblast growth factor 2	Homo sapiens	87-92
12516687-9	2002	The patient was given low-molecular-weight heparin with a dramatic reduction in previously elevated fibrinogen level and a good control of the hepatic function.	Heparin	43-50	fibrinogen beta chain	Homo sapiens	100-110
12124794-2	2002	This study describes a novel basic fibroblast growth factor-2 (FGF-2) delivery system synthesized by the conjugation of a structure-stabilizing polymer, hyaluronate (HA), with a sulfated glycosaminoglycan, heparin (HP), that has inherent specific binding sites for members of the FGF family.	Heparin	206-213	fibroblast growth factor 2	Homo sapiens	35-61
12124794-2	2002	This study describes a novel basic fibroblast growth factor-2 (FGF-2) delivery system synthesized by the conjugation of a structure-stabilizing polymer, hyaluronate (HA), with a sulfated glycosaminoglycan, heparin (HP), that has inherent specific binding sites for members of the FGF family.	Heparin	206-213	fibroblast growth factor 2	Homo sapiens	63-68
12124794-2	2002	This study describes a novel basic fibroblast growth factor-2 (FGF-2) delivery system synthesized by the conjugation of a structure-stabilizing polymer, hyaluronate (HA), with a sulfated glycosaminoglycan, heparin (HP), that has inherent specific binding sites for members of the FGF family.	Heparin	206-213	fibroblast growth factor 2	Homo sapiens	63-66
12124794-2	2002	This study describes a novel basic fibroblast growth factor-2 (FGF-2) delivery system synthesized by the conjugation of a structure-stabilizing polymer, hyaluronate (HA), with a sulfated glycosaminoglycan, heparin (HP), that has inherent specific binding sites for members of the FGF family.	Heparin	215-217	fibroblast growth factor 2	Homo sapiens	35-61
12124794-2	2002	This study describes a novel basic fibroblast growth factor-2 (FGF-2) delivery system synthesized by the conjugation of a structure-stabilizing polymer, hyaluronate (HA), with a sulfated glycosaminoglycan, heparin (HP), that has inherent specific binding sites for members of the FGF family.	Heparin	215-217	fibroblast growth factor 2	Homo sapiens	63-68
12124794-2	2002	This study describes a novel basic fibroblast growth factor-2 (FGF-2) delivery system synthesized by the conjugation of a structure-stabilizing polymer, hyaluronate (HA), with a sulfated glycosaminoglycan, heparin (HP), that has inherent specific binding sites for members of the FGF family.	Heparin	215-217	fibroblast growth factor 2	Homo sapiens	63-66
12124794-4	2002	The addition of recombinant human FGF-2 resulted in the rapid binding of FGF-2 to the heparin segment of the hyaluronate-heparin (HAHP) conjugate.	Heparin	86-93	fibroblast growth factor 2	Homo sapiens	34-39
12124794-4	2002	The addition of recombinant human FGF-2 resulted in the rapid binding of FGF-2 to the heparin segment of the hyaluronate-heparin (HAHP) conjugate.	Heparin	86-93	fibroblast growth factor 2	Homo sapiens	73-78
12124794-5	2002	The FGF-2 was released in vitro from the imine-bonded (HAHPi) gels in the form of FGF-2-heparin complexes through the hydrolysis of the imine bonds.	Heparin	88-95	fibroblast growth factor 2	Homo sapiens	4-9
12124794-5	2002	The FGF-2 was released in vitro from the imine-bonded (HAHPi) gels in the form of FGF-2-heparin complexes through the hydrolysis of the imine bonds.	Heparin	88-95	fibroblast growth factor 2	Homo sapiens	82-87
12356477-4	2002	L-AT was determined by integration of the low heparin affinity peak when analyzed by the affinity chromatography method.	Heparin	46-53	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	2-4
12423248-5	2002	Moreover, the heparin-resistant binding of [125I]bFGF in TM-BBB4 cells was significantly reduced by 50% following treatment with sodium chlorate, suggesting the loss of perlecan (a core protein of heparan sulfate proteoglycan, HSPG) from the extracellular matrix of the cells.	Heparin	14-21	syndecan 2	Mus musculus	227-231
12714831-3	2002	In a single center pilot study of patients with acute coronary syndromes (ACS) we reported that thrombin generation was evident within one (1) hour of UFH cessation, increased progressively over the subsequent 24 hours, correlated directly with factor VII activity and inversely with TFPI (concentration and activity).	Heparin	151-154	coagulation factor II, thrombin	Homo sapiens	96-104
12556751-5	2002	The direct thrombin inhibitors also have been shown to have advantages in the treatment of patients with heparin-induced thrombocytopenia.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	11-19
12121971-4	2002	Inhibition of COM crystal binding to the cells by heparin blocked the effects of COM crystals on p38 MAPK activation.	Heparin	50-57	mitogen-activated protein kinase 14	Homo sapiens	97-100
12221676-0	2002	Venous limb gangrene during overlapping therapy with warfarin and a direct thrombin inhibitor for immune heparin-induced thrombocytopenia.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	75-83
12565724-9	2002	The changes in TFPI level after administration of thioglycosides and heparin were similar in the mentioned model to those without endotoxin.	Heparin	69-76	tissue factor pathway inhibitor	Oryctolagus cuniculus	15-19
12558000-8	2002	Anticoagulant activity test using activated partial thromboplastin time (aPTT) is more sensitive in assessing heparin-immobilized surfaces, since it corresponds to Factor X and initiates the inhibition of Factor XII and thrombin.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	220-228
12145273-8	2002	S18 was found to be abundantly phosphorylated in response to serum treatment, and this effect was strongly inhibited by heparin.	Heparin	120-127	ribosomal protein S18	Homo sapiens	0-3
12221676-1	2002	We report two patients with deep-vein thrombosis complicating immune heparin-induced thrombocytopenia who developed venous limb gangrene during overlapping therapy with a direct thrombin inhibitor (lepirudin or argatroban) and warfarin.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	178-186
12236772-4	2002	In this study a series of silyl-heparins were synthesized and each of the analogues found to function similar to unmodified heparin relative to their binding of antithrombin III and also the binding of bFGF.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	202-206
12529961-5	2002	Heparin and LMWH bind to low affinity sites on KGF and produce non-specific inhibition, while KGFR2 beta (IIIb)/Fc, a soluble chimera of an extracellular KGFR fragment, is a more specific KGF inhibitor.	Heparin	0-7	fibroblast growth factor 7	Homo sapiens	47-50
12393117-1	2002	Lepirudin is a specific thrombin inhibitor that is used for anticoagulation in patients with heparin-induced thrombocytopenia who are also undergoing cardiopulmonary bypass (CPB).	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	24-32
12124773-0	2002	Structure-activity relationships of heparin-mimicking compounds in induction of bFGF release from extracellular matrix and inhibition of smooth muscle cell proliferation and heparanase activity.	Heparin	36-43	fibroblast growth factor 2	Homo sapiens	80-84
12164862-6	2002	Addition of neutralizing anti-heparin-binding EGF-like growth factor (HB-EGF) antibody, pretreatment with heparin and the metalloproteinase (MMP) inhibitor batimastat blocked FN expression.	Heparin	30-37	fibronectin 1	Homo sapiens	175-177
12164861-10	2002	Heparin, an inhibitor of GRK activity, decreased the expression of GRK2 and GRK4 and attenuated the desensitization of the D1 receptor (85 +/- 1%).	Heparin	0-7	G protein-coupled receptor kinase 2	Homo sapiens	67-71
12114192-2	2002	VLDL-triglycerides are hydrolyzed to fatty acids by lipoprotein lipase (LPL), an enzyme activated by heparin.	Heparin	101-108	lipoprotein lipase	Rattus norvegicus	52-70
12164861-10	2002	Heparin, an inhibitor of GRK activity, decreased the expression of GRK2 and GRK4 and attenuated the desensitization of the D1 receptor (85 +/- 1%).	Heparin	0-7	G protein-coupled receptor kinase 4	Homo sapiens	76-80
12218949-10	2002	Further studies are required to clarify the mechanism of increased SOD and CAT activity in red blood cells induced by heparin.	Heparin	118-125	superoxide dismutase 1	Homo sapiens	67-70
12218949-10	2002	Further studies are required to clarify the mechanism of increased SOD and CAT activity in red blood cells induced by heparin.	Heparin	118-125	catalase	Homo sapiens	75-78
12411975-4	2002	The anticoagulation effect of low-molecular-weight heparins is caused by a combination of inhibition of thrombin generation and inhibition of thrombin activity.	Heparin	51-59	coagulation factor II, thrombin	Homo sapiens	104-112
12411975-4	2002	The anticoagulation effect of low-molecular-weight heparins is caused by a combination of inhibition of thrombin generation and inhibition of thrombin activity.	Heparin	51-59	coagulation factor II, thrombin	Homo sapiens	142-150
12173939-6	2002	Since the splitting reaction also occurs at the level of the essential glucuronic acid residue of the active site for antithrombin, the heparin derivative has no anticoagulant activity.	Heparin	136-143	serpin family C member 1	Gallus gallus	118-130
12147313-0	2002	Unfractionated heparin is associated with a lower rise of serum vascular cell adhesion molecule-1 in acute ischemic stroke patients.	Heparin	15-22	vascular cell adhesion molecule 1	Homo sapiens	64-97
12034712-0	2002	Fibroblast growth factor receptors 1 and 2 interact differently with heparin/heparan sulfate.	Heparin	69-76	fibroblast growth factor receptor 1	Homo sapiens	0-42
12034712-5	2002	We show that the ectodomains of FGFR1 IIIc and FGFR2 IIIc exhibit specific interactions with different characteristics for both heparin and porcine mucosal HS.	Heparin	128-135	fibroblast growth factor receptor 1	Homo sapiens	32-37
12034712-8	2002	FGFR1 and FGFR2 bind heparin with mean association rate constants of 1.9 x 10(5) and 2.1 x 10(6) m(-1)s(-1), respectively, and dissociation rate constants of 1.2 x 10(-2) and 2.7 x 10(-2) s(-1), respectively.	Heparin	21-28	fibroblast growth factor receptor 1	Homo sapiens	0-5
12034712-10	2002	Hence, FGFR1 and FGFR2 bind to heparin chains with markedly different kinetics and affinities.	Heparin	31-38	fibroblast growth factor receptor 1	Homo sapiens	7-12
12173939-7	2002	However, it fully retains the FGF2-binding ability of the original heparin, as shown by its capacity to protect FGF2 from trypsin cleavage and to prevent the formation of heparan sulfate proteoglycan (HSPG)/FGF2/FGFR1 ternary complexes.	Heparin	67-74	fibroblast growth factor receptor 1	Gallus gallus	212-217
12114192-2	2002	VLDL-triglycerides are hydrolyzed to fatty acids by lipoprotein lipase (LPL), an enzyme activated by heparin.	Heparin	101-108	lipoprotein lipase	Rattus norvegicus	72-75
12127922-5	2002	Thrombin formation tended to increase with hirudin and decrease with heparin; by 8h into infusion, thrombin formation was significantly less for heparin (P&lt;0.01).	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	99-107
12052468-7	2002	Induced EC-SOD by lysoPC had a high affinity for heparin, and may bind to the endothelial cell surface.	Heparin	49-56	superoxide dismutase 3	Homo sapiens	8-14
12127922-5	2002	Thrombin formation tended to increase with hirudin and decrease with heparin; by 8h into infusion, thrombin formation was significantly less for heparin (P&lt;0.01).	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	0-8
12413592-2	2002	We compared the inhibition properties of PCI and HCII to ATIII using R93A/R97A/R101A thrombin, an anion-binding exosite-2 (exosite-2) mutant that has greatly reduced heparin-binding properties.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	85-93
12147593-2	2002	METHODS: A peptide corresponding to a major heparin- and cell-binding domain of the LG4 module of the laminin alpha5 chain was analyzed.	Heparin	44-51	laminin subunit alpha 5	Homo sapiens	102-122
12225805-5	2002	The FN fragments showed a weak, but not physiologically important, binding to heparin, and did not bind elastin or laminin.	Heparin	78-85	fibronectin 1	Homo sapiens	4-6
12195701-1	2002	Heparin has been proposed to enhance thrombolysis by inhibiting thrombin-dependent generation of activated TAFI (thrombin activatable fibrinolysis inhibitor), a carboxypeptidase that inhibits fibrinolysis.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	64-72
12195701-6	2002	Thrombin generation in the fluid phase was totally inhibited by heparin at concentrations &gt; 0.5 U/ml.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	0-8
12105168-2	2002	In patients with thrombosis, however, thrombin is often protected from AT-dependent, heparin-mediated inactivation.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	38-46
12413592-3	2002	Heparin-enhanced PCI inhibition of R93A/R97A/R101A thrombin was only approximately 2-fold compared to 40-fold enhancement with wild-type recombinant thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	51-59
12413592-3	2002	Heparin-enhanced PCI inhibition of R93A/R97A/R101A thrombin was only approximately 2-fold compared to 40-fold enhancement with wild-type recombinant thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	149-157
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	107-115
12413592-7	2002	These results suggest that PCI is similar to ATIII and depends upon ternary complex formation with heparin and these specific thrombin exosite-2 residues to accelerate thrombin inhibition.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	168-176
12131916-1	2002	The purpose of the present report is to demonstrate the long-term efficacy and safety of heparin-induced extracorporeal lipoprotein precipitation (HELP) of LDL-c and fibrinogen in the management of familial hypercholesterolemia.	Heparin	89-96	component of oligomeric golgi complex 2	Homo sapiens	156-161
12095635-0	2002	Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	110-118
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	14-22
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	157-165
11986311-6	2002	Heparin enhanced the binding of both 125I-VEGF165 and 125I-PlGF-2 to the b1b2 domain by 20- and 4-fold, respectively.	Heparin	0-7	placental growth factor	Homo sapiens	59-65
11986311-9	2002	It was concluded that an intact b1b2 domain serves as the VEGF165-, PlGF-2-, and heparin-binding sites in NRP1, and that heparin is a critical component for regulating VEGF165 and PlGF-2 interactions with NRP1 by physically interacting with both receptor and ligands.	Heparin	121-128	placental growth factor	Homo sapiens	180-186
12099815-5	2002	Furthermore, heparin bound strongly to the protein"s anti-thrombin III-based region.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	58-66
12131916-1	2002	The purpose of the present report is to demonstrate the long-term efficacy and safety of heparin-induced extracorporeal lipoprotein precipitation (HELP) of LDL-c and fibrinogen in the management of familial hypercholesterolemia.	Heparin	89-96	fibrinogen beta chain	Homo sapiens	166-176
12270764-1	2002	OBJECTIVES: Heparin is thought to play a crucial role in the clinical monitoring of patients with acute coronary syndrome as well as after coronary bypass surgery in that it interferes with different commercial immunoassay test systems for cardiac troponin T (cTnT) and troponin I (cTnI).	Heparin	12-19	troponin T2, cardiac type	Homo sapiens	240-258
12270764-1	2002	OBJECTIVES: Heparin is thought to play a crucial role in the clinical monitoring of patients with acute coronary syndrome as well as after coronary bypass surgery in that it interferes with different commercial immunoassay test systems for cardiac troponin T (cTnT) and troponin I (cTnI).	Heparin	12-19	troponin T2, cardiac type	Homo sapiens	260-264
12270764-2	2002	The mechanism, however, by which heparin apparently affects the cTnT and cTnI levels in plasma is not yet resolved.	Heparin	33-40	troponin T2, cardiac type	Homo sapiens	64-68
12270764-6	2002	RESULTS: The data obtained indicate that heparin produces an apparent decrease in cTnT as well as of cTnI levels, analyzed either by the Elecsys, the Opus or the ACS:Centaur immunoassay systems.	Heparin	41-48	troponin T2, cardiac type	Homo sapiens	82-86
12270764-9	2002	When serum is supplemented with increasing concentrations of heparin, and cardiac troponin levels were reanalysed, significantly lower recoveries for the cTnT than for the cTnI immunoassays were detectable.	Heparin	61-68	troponin T2, cardiac type	Homo sapiens	154-158
12270764-10	2002	Affinity chromatography with heparin Sepharose demonstrates that cTnT and cTnI interact differentially with the negatively charged ligand.	Heparin	29-36	troponin T2, cardiac type	Homo sapiens	65-69
12270764-12	2002	CONCLUSIONS: We conclude, therefore, that the apparent decrease in cTnT values by addition of heparin is a result of direct molecular interaction between the negatively charged glycosaminoglycan and clusters of basic residues within the sequence of the cardiac protein.	Heparin	94-101	troponin T2, cardiac type	Homo sapiens	67-71
12124681-2	2002	Their action is in contrast to heparin and its derivatives, which inhibit thrombin and other coagulation serine proteases via antithrombin, and to the warfarin-type drugs that interfere with synthesis of the precursors of the coagulation serine proteases.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	74-82
12093896-2	2002	Here we show that the potent anti-inflammatory property of heparin results primarily from blockade of P-selectin and L-selectin.	Heparin	59-66	selectin, platelet	Mus musculus	102-112
12093896-2	2002	Here we show that the potent anti-inflammatory property of heparin results primarily from blockade of P-selectin and L-selectin.	Heparin	59-66	selectin, lymphocyte	Mus musculus	117-127
12093896-8	2002	We conclude that (a) heparin"s anti-inflammatory effects are mainly mediated by blocking P- and L-selectin-initiated cell adhesion; (b) the sulfate groups at C6 on the glucosamine residues play a critical role in selectin inhibition; and (c) some non-anticoagulant forms of heparin retain anti-inflammatory activity.	Heparin	21-28	selectin, lymphocyte	Mus musculus	96-106
11923311-5	2002	Mechanistic studies with human cells indicated two modes of FGF-10 action: (i) translocation of rFGF-10 into urothelial cell nuclei and (ii) a signaling cascade that begins with the heparin-dependent phosphorylation of tyrosine residues of surface transmembrane receptors.	Heparin	182-189	fibroblast growth factor 10	Homo sapiens	60-66
12074579-1	2002	In vascular smooth muscle cells (VSMCs), angiotensin II (AngII) induces transactivation of the EGF receptor (EGFR) which involves a metalloprotease that stimulates processing of heparin-binding EGF from its precursor.	Heparin	178-185	angiotensinogen	Homo sapiens	41-55
12074579-1	2002	In vascular smooth muscle cells (VSMCs), angiotensin II (AngII) induces transactivation of the EGF receptor (EGFR) which involves a metalloprotease that stimulates processing of heparin-binding EGF from its precursor.	Heparin	178-185	angiotensinogen	Homo sapiens	57-62
12074579-1	2002	In vascular smooth muscle cells (VSMCs), angiotensin II (AngII) induces transactivation of the EGF receptor (EGFR) which involves a metalloprotease that stimulates processing of heparin-binding EGF from its precursor.	Heparin	178-185	epidermal growth factor receptor	Homo sapiens	95-107
12074579-1	2002	In vascular smooth muscle cells (VSMCs), angiotensin II (AngII) induces transactivation of the EGF receptor (EGFR) which involves a metalloprotease that stimulates processing of heparin-binding EGF from its precursor.	Heparin	178-185	epidermal growth factor receptor	Homo sapiens	109-113
12063122-1	2002	Rheumatoid arthritis (RA) patients, in whom cryogelation occurs in the presence of heparin, exhibit abnormally high concentrations of extra domain A containing fibronectin [EDA(+)FN] in their plasma.	Heparin	83-90	fibronectin 1	Homo sapiens	160-171
12088864-5	2002	Microinjection of heparin abolished BK-induced Ca(2+) release.	Heparin	18-25	kininogen 1	Homo sapiens	36-38
12069613-4	2002	ApoE is a heparan-sulfate binding protein, and apoE peptide neurotoxicity can be blocked by heparin and prevented by degrading heparan sulfate or inhibiting its biosynthesis.	Heparin	92-99	apolipoprotein E	Homo sapiens	0-4
12069613-4	2002	ApoE is a heparan-sulfate binding protein, and apoE peptide neurotoxicity can be blocked by heparin and prevented by degrading heparan sulfate or inhibiting its biosynthesis.	Heparin	92-99	apolipoprotein E	Homo sapiens	47-51
12069613-5	2002	The possibility that heparin inhibition of toxicity is mediated by a specific oligosaccharide sequence was investigated using a bioassay to determine the inhibition of apoE peptide toxicity by glycosaminoglycans and purified glycosaminoglycan oligosaccharides.	Heparin	21-28	apolipoprotein E	Homo sapiens	168-172
12033828-2	2002	We show the commercial enzyme corresponds to the major peak 2 PME previously separated by heparin-Sepharose chromatography (Cameron et al., J.	Heparin	90-97	pectinesterase 2	Citrus sinensis	62-65
12069854-4	2002	Glycated apoE binding to heparin and heparan sulfates (HS) was assessed by surface plasmon resonance (SPR) technology.	Heparin	25-32	apolipoprotein E	Homo sapiens	9-13
12034879-4	2002	Treating cartilage with the heparin-degrading enzyme heparitinase also caused release of bFGF, suggesting the presence of an extracellular store that is sequestered in the matrix and released upon damage.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	89-93
11920660-4	2002	The results showed that fucan, dextran derivatives, and heparin differentially (1) triggered interleukin-1alpha, tumor necrosis factor alpha, interleukin-6, and interleukin-8 production by monocytes in a dose-dependent manner, (2) modulated cytokine production by LPS-stimulated monocytes, and (3) specifically inhibited the binding of biotinylated LPS to monocyte membranes.	Heparin	56-63	interleukin 6	Homo sapiens	142-155
11920660-4	2002	The results showed that fucan, dextran derivatives, and heparin differentially (1) triggered interleukin-1alpha, tumor necrosis factor alpha, interleukin-6, and interleukin-8 production by monocytes in a dose-dependent manner, (2) modulated cytokine production by LPS-stimulated monocytes, and (3) specifically inhibited the binding of biotinylated LPS to monocyte membranes.	Heparin	56-63	C-X-C motif chemokine ligand 8	Homo sapiens	161-174
12079941-2	2002	Heparin-coated circuits with a centrifugal pump provided 2.5 to 3.5 L x min(-1) of flow to maintain good hemodynamics and enable easy access to the posterior vessels during vertical displacement of the heart.	Heparin	0-7	CD59 molecule (CD59 blood group)	Homo sapiens	72-78
11861638-0	2002	Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase.	Heparin	36-43	superoxide dismutase 3	Homo sapiens	62-96
12059036-3	2002	Acidic fibroblast growth factor (aFGF) belongs to a family of growth factors that show a high affinity for heparin sulfate proteoglycans.	Heparin	107-114	fibroblast growth factor 1	Homo sapiens	0-31
12059036-3	2002	Acidic fibroblast growth factor (aFGF) belongs to a family of growth factors that show a high affinity for heparin sulfate proteoglycans.	Heparin	107-114	fibroblast growth factor 1	Homo sapiens	33-37
11973358-8	2002	Heparin completely inhibits heparanase endocytosis but only partially inhibits its association with the cells, suggesting that cell surface heparan sulfate moieties play a specific role in its endocytosis.	Heparin	0-7	heparanase	Homo sapiens	28-38
12355033-6	2002	RESULTS: Platelet reactivity was greater in blood treated with UFH than in blood anticoagulated with bivalirudin with respect to both the capacity to bind fibrinogen (by 4 +/- 1.8%, p = 0.01) and P-selectin expression (by 7.7 +/- 0.7%, p, &lt; 0.0001) in response to 1 microM ADP.	Heparin	63-66	fibrinogen beta chain	Homo sapiens	155-165
12064568-1	2002	In a large phase III study of patients with unstable angina treated with percutaneous transluminal coronary angioplasty (PTCA), the thrombin-specific anticoagulant bivalirudin produced relative risk reductions of 22% (p = 0.039) for ischemic complications and 62% (p &lt; 0.001) for bleeding complications compared with heparin.	Heparin	320-327	coagulation factor II, thrombin	Homo sapiens	132-140
15344331-8	2002	Thapsigargin and IP3 receptor antagonist heparin induced nucleoplasmic Ca2+ free concentration decrease.	Heparin	41-48	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	17-29
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	201-208	coagulation factor II, thrombin	Homo sapiens	63-71
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	201-208	coagulation factor II, thrombin	Homo sapiens	63-71
12022870-2	2002	To probe this molecular reaction as well as the role of electrostatic forces in VWF-heparin interaction, we performed mutagenesis and molecular modeling experiments.	Heparin	84-91	von Willebrand factor	Homo sapiens	80-83
11861638-2	2002	A polybasic region in the carboxyl terminus distinguishes EC-SOD from other superoxide dismutases and determines EC-SOD"s tissue half-life and affinity for heparin.	Heparin	156-163	superoxide dismutase 3	Homo sapiens	58-64
11861638-2	2002	A polybasic region in the carboxyl terminus distinguishes EC-SOD from other superoxide dismutases and determines EC-SOD"s tissue half-life and affinity for heparin.	Heparin	156-163	superoxide dismutase 3	Homo sapiens	113-119
11861638-3	2002	There are two types of EC-SOD that differ based on the presence or absence of this heparin-binding region.	Heparin	83-90	superoxide dismutase 3	Homo sapiens	23-29
11854286-8	2002	Both LA- and HA-PLTP bind to heparin-Sepharose and can be separated by elution with 0-0.5 m NaCl gradient, with HA-PLTP displaying higher affinity for the matrix.	Heparin	29-36	phospholipid transfer protein	Homo sapiens	16-20
11854286-10	2002	HA-PLTP was subjected to a second heparin-Sepharose step and hydroxylapatite chromatography.	Heparin	34-41	phospholipid transfer protein	Homo sapiens	3-7
11964252-5	2002	The cis bFGF-heparin (2:1) complex, essential for the activation of the angiogenic process, is thus prevented.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	8-12
12108544-3	2002	Here we show that NDST-2+/+ bone marrow-derived mast cells cultured in the presence of IL-3 synthesise, in addition to highly sulphated chondroitin sulphate (CS), small amounts of equally highly sulphated heparin-like polysaccharide.	Heparin	205-212	interleukin 3	Mus musculus	87-91
11964252-10	2002	With heparin, however, wild-type bFGF forms a tighter complex with a more compact structure.	Heparin	5-12	fibroblast growth factor 2	Homo sapiens	33-37
12061718-0	2002	Refinement of the solution structure of the heparin-binding domain of vascular endothelial growth factor using residual dipolar couplings.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	70-104
12061718-1	2002	Previous NMR structural studies of the heparin-binding domain of vascular endothelial growth factor (VEGF165) revealed a novel fold comprising two subdomains, each containing two disulfide bridges and a short two-stranded antiparallel beta-sheet.	Heparin	39-46	vascular endothelial growth factor A	Homo sapiens	65-99
11978889-0	2002	Effect of heparin on tissue binding activity of fibroblast growth factor and heparin-binding epidermal growth factor in experimental colitis in rats.	Heparin	10-17	heparin-binding EGF-like growth factor	Rattus norvegicus	77-116
12029263-3	2002	Basically, it acts as the natural inhibitor of thrombin, which, in presence of heparin, blocks the thrombin action and avoids gross thrombus formation inside the extracorporeal circulation circuit.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	47-55
12029263-3	2002	Basically, it acts as the natural inhibitor of thrombin, which, in presence of heparin, blocks the thrombin action and avoids gross thrombus formation inside the extracorporeal circulation circuit.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	99-107
12115937-5	2002	Wound epithelium thickened when recombinant newt FGF-1 was provided on heparin-coated beads, demonstrating that the FGF-1 was biologically active and that the wound epithelium is a possible target tissue of FGF.	Heparin	71-78	fibroblast growth factor 1	Homo sapiens	49-54
12115937-5	2002	Wound epithelium thickened when recombinant newt FGF-1 was provided on heparin-coated beads, demonstrating that the FGF-1 was biologically active and that the wound epithelium is a possible target tissue of FGF.	Heparin	71-78	fibroblast growth factor 1	Homo sapiens	116-121
11978889-3	2002	Heparin is a potent modulator of receptor binding of growth factors such as fibroblast growth factor (FGF), vascular endothelial growth factor, and heparin-binding epidermal growth factor (HB-EGF), that play a role in wound repair.	Heparin	0-7	heparin-binding EGF-like growth factor	Rattus norvegicus	148-187
11978889-3	2002	Heparin is a potent modulator of receptor binding of growth factors such as fibroblast growth factor (FGF), vascular endothelial growth factor, and heparin-binding epidermal growth factor (HB-EGF), that play a role in wound repair.	Heparin	0-7	heparin-binding EGF-like growth factor	Rattus norvegicus	189-195
11978889-4	2002	We examined the effect of heparin on the functional levels of FGF and HB-EGF in a model of experimental colitis.	Heparin	26-33	heparin-binding EGF-like growth factor	Rattus norvegicus	70-76
11978889-12	2002	Heparin caused a significant increase in HB-EGF content in group 4 (p &lt; 0.05).	Heparin	0-7	heparin-binding EGF-like growth factor	Rattus norvegicus	41-47
22896898-1	2002	Limited proteolysis of buffalo plasma fibronectin (FN) by thermolysin yielded four gelatin-binding fragments of which, the major 59 kDa fragment, GBF1, was isolated by gelatin-Sepharose and heparin-Sepharose affinity columns.	Heparin	190-197	fibronectin 1	Homo sapiens	38-49
11971193-2	2002	We show here that mutated diphtheria toxin, a specific inhibitor of heparin-binding epidermal growth factor-like growth factor (HB-EGF), blocked the IL-6-induced growth of two myeloma cell lines (XG-1 and XG-14) and did not significantly affect that of two other cell lines (XG-6 and XG-13).	Heparin	68-75	interleukin 6	Homo sapiens	149-153
11895948-5	2002	Lactoferrin strongly inhibited the interaction of radiolabeled IL-8 to immobilized heparin, whereas a lactoferrin variant lacking the amino acid residues essential for heparin binding was not inhibitory.	Heparin	83-90	C-X-C motif chemokine ligand 8	Homo sapiens	63-67
11832488-7	2002	These results suggest the essential roles of DEXT3, its human ortholog EXTL3, and the C. elegans ortholog rib-2 in the biosynthesis of heparan sulfate and heparin, if present, in the respective organisms.	Heparin	155-162	Exostosin-2 homolog	Caenorhabditis elegans	106-111
11923794-1	2002	BACKGROUND: Because of the adverse characteristics associated with heparin, direct antagonists of thrombin have been investigated as anticoagulants during percutaneous coronary interventions.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	98-106
22896898-1	2002	Limited proteolysis of buffalo plasma fibronectin (FN) by thermolysin yielded four gelatin-binding fragments of which, the major 59 kDa fragment, GBF1, was isolated by gelatin-Sepharose and heparin-Sepharose affinity columns.	Heparin	190-197	fibronectin 1	Homo sapiens	51-53
11890696-0	2002	Minimal heparin/heparan sulfate sequences for binding to fibroblast growth factor-1.	Heparin	8-15	fibroblast growth factor 1	Homo sapiens	57-83
11904525-11	2002	The frequency of PCNA-positive vascular smooth muscle cells (%) was significantly less at the heparin-coated stent (10.8 +/- 1.0) than at the control stent site (19.1 +/- 1.7) (p &lt; 0.01).	Heparin	94-101	proliferating cell nuclear antigen	Sus scrofa	17-21
11992238-12	2002	The analysis of vWF multimers in the different fractions obtained by affinity chromatography on heparin Sepharose showed that the activity measured both with RCo assay and CBA correlated with the degree of multimerization.	Heparin	96-103	von Willebrand factor	Homo sapiens	16-19
12008942-5	2002	UFH inhibited thrombin generation to a greater extent compared to LMWH in all plasmas.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	14-22
12008942-7	2002	Lower concentrations of UFH and LMWH were required to inhibit thrombin generation in cord and child plasmas compared to adult plasma.	Heparin	24-27	coagulation factor II, thrombin	Homo sapiens	62-70
12008942-12	2002	In summary, lower doses of UFH, LMWH or ATH result in similar peak thrombin generation in newborn and child plasmas compared to adult plasma.	Heparin	27-30	coagulation factor II, thrombin	Homo sapiens	67-75
12097308-5	2002	bFGF significantly stimulated gingival fibroblast proliferation with or without heparin.	Heparin	80-87	fibroblast growth factor 2	Homo sapiens	0-4
11890696-1	2002	The glycosaminoglycans heparin and heparan sulfate (HS) bind to fibroblast growth factor FGF1 and promote its dimerization, a proposed prerequisite for binding to a cellular receptor and triggering mitogenic signals.	Heparin	23-30	fibroblast growth factor 1	Homo sapiens	89-93
11890696-5	2002	Furthermore, MALDI experiments show that, in addition to 1:1 protein:tetrasaccharide complexes, AA and BA are able to form 2:1 complexes, indicating that heparin/HS-induced dimerization of FGF1 requires only one 6-OSO(3) group per tetrasaccharide.	Heparin	154-161	fibroblast growth factor 1	Homo sapiens	189-193
11855916-12	2002	Heparin appears to block thrombin-stimulated oxidation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	25-33
11986603-1	2002	OBJECTIVE: Reports evaluating the efficacy of heparin-bonded circuits to blunt inflammation, platelet dysfunction, and thrombin generation in response to cardiopulmonary bypass have varied.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	119-127
11869846-0	2002	Rebound thrombin generation after heparin therapy in unstable angina.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	8-16
11877267-1	2002	Low-molecular-weight and unfractionated heparins are frequently used to treat venous thromboembolism, but it is not known whether they are equally effective in inhibiting in vivo generation of thrombin.	Heparin	40-48	coagulation factor II, thrombin	Homo sapiens	193-201
12009874-2	2002	Although gC from HSV-1 (gC1) and from HSV-2 (gC2) bind to heparin, gC2 is believed to play a less significant role than gC1 in attachment of virus to cells.	Heparin	58-65	solute carrier family 25 member 18	Homo sapiens	45-48
11863456-1	2002	An essential property of human extracellular superoxide dismutase (hEC-SOD) is its affinity for heparin and heparan sulfate proteoglycans located on cell surfaces and in the connective tissue matrix.	Heparin	96-103	superoxide dismutase 3	Homo sapiens	67-74
11989502-5	2002	On the 15th day after operation, an initial search for lupus anticoagulant revealed that the prothrombin time (PT) ratio and dilute activated partial thromboplastin time (aPTT) were positive under heparin treatment, without evidence of rheumatic or connective tissue disease.	Heparin	197-204	coagulation factor II, thrombin	Homo sapiens	93-104
11814358-3	2002	The binding affinities, obtained by isothermal fluorescence titration, of size-defined heparin and HS oligosaccharides to the chemokine were found to depend on the oligomerization state of IL-8: high affinity was detected for monomeric and low affinity was detected for dimeric IL-8, referring to a self-regulatory mechanism for its chemoattractant effect.	Heparin	87-94	C-X-C motif chemokine ligand 8	Homo sapiens	189-193
11830470-1	2002	Heparin-induced thrombocytopenia/thrombosis (HIT/T) is a common complication of heparin therapy that is caused by antibodies to platelet factor 4 (PF4) complexed with heparin.	Heparin	0-7	platelet factor 4	Mus musculus	147-150
11830470-1	2002	Heparin-induced thrombocytopenia/thrombosis (HIT/T) is a common complication of heparin therapy that is caused by antibodies to platelet factor 4 (PF4) complexed with heparin.	Heparin	80-87	platelet factor 4	Mus musculus	147-150
11830470-1	2002	Heparin-induced thrombocytopenia/thrombosis (HIT/T) is a common complication of heparin therapy that is caused by antibodies to platelet factor 4 (PF4) complexed with heparin.	Heparin	167-174	platelet factor 4	Mus musculus	147-150
12001541-7	2002	The ACE study (Anticoagulation in Cardioversion using Enoxaparin) is a randomized, prospective, open-label multicenter trial comparing the safety and efficacy of subcutaneous enoxaparin with intravenous heparin/oral phenprocoumon before and after cardioversion (stratified to TEE guidance or no TEE guidance).	Heparin	203-210	angiotensin I converting enzyme	Homo sapiens	4-7
11854515-11	2002	Although heparin can block both P- and L-selectin in vitro, the in vivo effect of a single heparin dose given before tumor cells seems to be completely accounted for by blockade of P-selectin function.	Heparin	9-16	selectin, lymphocyte	Mus musculus	39-49
11854515-11	2002	Although heparin can block both P- and L-selectin in vitro, the in vivo effect of a single heparin dose given before tumor cells seems to be completely accounted for by blockade of P-selectin function.	Heparin	91-98	selectin, platelet	Mus musculus	181-191
11814358-9	2002	Thermal unfolding of IL-8 yielded a single transition at 56 degrees C which was completely prevented by the presence of undigested HS or heparin, indicating structural stabilization, thereby prolonging the biological effect of the chemokine.	Heparin	137-144	C-X-C motif chemokine ligand 8	Homo sapiens	21-25
11814358-3	2002	The binding affinities, obtained by isothermal fluorescence titration, of size-defined heparin and HS oligosaccharides to the chemokine were found to depend on the oligomerization state of IL-8: high affinity was detected for monomeric and low affinity was detected for dimeric IL-8, referring to a self-regulatory mechanism for its chemoattractant effect.	Heparin	87-94	C-X-C motif chemokine ligand 8	Homo sapiens	278-282
11836169-0	2002	Reduced inhibition of activated prothrombin by heparin and venous thromboembolism: heparin resistance revisited.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	32-43
11866879-11	2002	CONCLUSION: Heparin and ADM appear to interact in a synergistic manner, which may be related to the over-expression of p53 and p21 mRNA and the elevated ratio of Bax/Bcl-2 mRNA.	Heparin	12-19	tumor protein p53	Homo sapiens	119-122
11866879-11	2002	CONCLUSION: Heparin and ADM appear to interact in a synergistic manner, which may be related to the over-expression of p53 and p21 mRNA and the elevated ratio of Bax/Bcl-2 mRNA.	Heparin	12-19	BCL2 associated X, apoptosis regulator	Homo sapiens	162-165
11866879-11	2002	CONCLUSION: Heparin and ADM appear to interact in a synergistic manner, which may be related to the over-expression of p53 and p21 mRNA and the elevated ratio of Bax/Bcl-2 mRNA.	Heparin	12-19	BCL2 apoptosis regulator	Homo sapiens	166-171
11836169-0	2002	Reduced inhibition of activated prothrombin by heparin and venous thromboembolism: heparin resistance revisited.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	32-43
11836169-10	2002	INTERPRETATION AND CONCLUSIONS: Lower than expected thrombin inhibition by endogenous antithrombin action after full activation by heparin addition was found to be a common feature in patients who suffered from previous venous thrombotic events, and may reflect a hitherto unrecognized thrombophilic alteration.	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	52-60
11842287-1	2002	Bradykinin is formed by the interaction of factor XII, prekallikrein, and high-molecular-weight kininogen on negatively charged inorganic surfaces (silicates, urate, and pyrophosphate) or macromolecular organic surfaces (heparin, other mucopolysaccharides, and sulfatides) or on assembly along the surface of cells.	Heparin	221-228	kininogen 1	Homo sapiens	0-10
11801647-9	2002	Functionally, heparin-treated DCs respond to LPS or LPS plus IFN-gamma with higher IL-10 and less IL-12 production than heparin-untreated DCs.	Heparin	14-21	interferon gamma	Homo sapiens	61-70
11807222-2	2002	The HS-binding domain of gC is composed of three discrete heparin-binding domains (HBDs), designated HBD1, -2 and -3 for their proximity to the amino terminus of gC.	Heparin	58-65	defensin beta 1	Homo sapiens	101-116
11801647-9	2002	Functionally, heparin-treated DCs respond to LPS or LPS plus IFN-gamma with higher IL-10 and less IL-12 production than heparin-untreated DCs.	Heparin	120-127	interferon gamma	Homo sapiens	61-70
11885025-3	2002	These processes might include fibrin formation, binding of heparin to angiogenic growth factors such as basic fibroblast growth factor and vascular endothelial growth factor, modulation of tissue factor, and other mechanisms.	Heparin	59-66	vascular endothelial growth factor A	Homo sapiens	139-173
11945080-6	2002	To confirm the cell surface association of PP5/TFPI-2, placental villi were incubated with heparin and resultant soluble fraction was analysed by Western blotting.	Heparin	91-98	tissue factor pathway inhibitor 2	Homo sapiens	43-46
11945080-7	2002	Heparin liberating PP5/TFPI-2 from villi suggested that PP5/TFPI-2 might be retained on the microvilli surface through the binding to membrane-anchored proteoglycans such as glypican and/or syndecan family members.	Heparin	0-7	tissue factor pathway inhibitor 2	Homo sapiens	19-22
11945080-7	2002	Heparin liberating PP5/TFPI-2 from villi suggested that PP5/TFPI-2 might be retained on the microvilli surface through the binding to membrane-anchored proteoglycans such as glypican and/or syndecan family members.	Heparin	0-7	tissue factor pathway inhibitor 2	Homo sapiens	23-29
11945080-7	2002	Heparin liberating PP5/TFPI-2 from villi suggested that PP5/TFPI-2 might be retained on the microvilli surface through the binding to membrane-anchored proteoglycans such as glypican and/or syndecan family members.	Heparin	0-7	tissue factor pathway inhibitor 2	Homo sapiens	56-59
11945080-7	2002	Heparin liberating PP5/TFPI-2 from villi suggested that PP5/TFPI-2 might be retained on the microvilli surface through the binding to membrane-anchored proteoglycans such as glypican and/or syndecan family members.	Heparin	0-7	tissue factor pathway inhibitor 2	Homo sapiens	60-66
11714710-7	2002	In addition, both 6-O- and 2-O-desulfated heparin activated FGF-1 signaling via FGFR2 IIIb, whereas neither one stimulated FGF-1 signaling via FGFR1 or FGF-7 via FGFR2 IIIb.	Heparin	42-49	fibroblast growth factor 1	Homo sapiens	60-65
11858483-0	2002	Effect of new synthetic heparin mimetics on whole blood thrombin generation in vivo and in vitro in rats.	Heparin	24-31	coagulation factor II	Rattus norvegicus	56-64
11858483-1	2002	The effect of new heparin mimetics (synthetic oligosaccharides) was studied in vitro with regard to thrombin generation (TG) in rat platelet rich plasma (PRP) and whole blood (WB) and in vivo on stasis-induced venous thrombosis in the rat.	Heparin	18-25	coagulation factor II	Rattus norvegicus	100-108
11858488-4	2002	The activated form, thrombin Perija, however, did not show any proteolytic activity towards native substrates, fibrinogen, protein C or various synthetic substrates for alpha-thrombin, but it was able to bind to antithrombin III, although the binding capacity was markedly reduced even in the presence of heparin.	Heparin	305-312	coagulation factor II, thrombin	Homo sapiens	20-28
11853892-1	2002	The ability of a soluble heparin-binding oligopeptide sequence derived from the von Willebrand factor (vWF) to modulate the adhesion and chemokinetic migration behavior of arterial smooth muscle cells was assessed using a novel glass microsphere centrifugation assay and automated time-lapse fluorescence videomicroscopy, respectively.	Heparin	25-32	von Willebrand factor	Homo sapiens	80-101
11853892-1	2002	The ability of a soluble heparin-binding oligopeptide sequence derived from the von Willebrand factor (vWF) to modulate the adhesion and chemokinetic migration behavior of arterial smooth muscle cells was assessed using a novel glass microsphere centrifugation assay and automated time-lapse fluorescence videomicroscopy, respectively.	Heparin	25-32	von Willebrand factor	Homo sapiens	103-106
11853892-4	2002	The specificity of this response to the vWF-derived heparin-binding peptide was supported by the absence of an observed effect in the presence of either a scrambled peptide or a consensus heparin-binding peptide sequence of similar heparin affinity.	Heparin	52-59	von Willebrand factor	Homo sapiens	40-43
11706028-4	2002	Using gene microarrays, we identified the tyrosine kinase receptor EphB2 as being differentially expressed in response to continuous intravenous heparin administration in the rabbit model of arterial injury.	Heparin	145-152	ephrin type-B receptor 2	Oryctolagus cuniculus	67-72
11706028-5	2002	EphB2 protein levels increased in cultured bovine vascular smooth muscle cells following serum stimulation and were decreased in a dose-dependent fashion by heparin.	Heparin	157-164	EPH receptor B2	Bos taurus	0-5
11706028-8	2002	Co-administration of EphB2/Fc chimera with heparin shifted the dose-response curve to the right.	Heparin	43-50	EPH receptor B2	Bos taurus	21-26
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	placental growth factor	Homo sapiens	91-97
11774259-1	2002	Vascular endothelial growth factor (VEGF) is a heparin-binding, dimeric polypeptide with potent mitogenic effects on endothelial cells.	Heparin	47-54	vascular endothelial growth factor A	Homo sapiens	0-34
11774259-1	2002	Vascular endothelial growth factor (VEGF) is a heparin-binding, dimeric polypeptide with potent mitogenic effects on endothelial cells.	Heparin	47-54	vascular endothelial growth factor A	Homo sapiens	36-40
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	vascular endothelial growth factor A	Homo sapiens	169-173
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	placental growth factor	Homo sapiens	156-162
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	placental growth factor	Homo sapiens	179-201
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	vascular endothelial growth factor C	Homo sapiens	167-173
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	placental growth factor	Homo sapiens	203-207
11751276-9	2002	The specificity of these inhibitors is shifted toward thrombin inhibition in the presence of heparin, suggesting that aHSPGs direct their action to control fibrin deposition in the follicle.	Heparin	93-100	coagulation factor II	Rattus norvegicus	54-62
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	vascular endothelial growth factor A	Homo sapiens	11-15
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	placental growth factor	Homo sapiens	67-89
11761163-6	2002	This study showed significant differences in adsorption patterns among the heparin-coated and the uncoated surfaces, notably for fibronectin, fibrinogen, C3 and high molecular weight kininogen (HMWK).	Heparin	75-82	fibronectin 1	Homo sapiens	129-140
11761163-6	2002	This study showed significant differences in adsorption patterns among the heparin-coated and the uncoated surfaces, notably for fibronectin, fibrinogen, C3 and high molecular weight kininogen (HMWK).	Heparin	75-82	fibrinogen beta chain	Homo sapiens	142-152
11761163-6	2002	This study showed significant differences in adsorption patterns among the heparin-coated and the uncoated surfaces, notably for fibronectin, fibrinogen, C3 and high molecular weight kininogen (HMWK).	Heparin	75-82	kininogen 1	Homo sapiens	161-192
14727968-18	2002	The clinical tolerability and the efficacy of low molecular weight heparins led to the concept that inhibition of further thrombin generation, by blocking factor Xa alone, can be an effective way of preventing thrombus growth without inactivating thrombin.	Heparin	67-75	coagulation factor II, thrombin	Homo sapiens	122-130
11761163-6	2002	This study showed significant differences in adsorption patterns among the heparin-coated and the uncoated surfaces, notably for fibronectin, fibrinogen, C3 and high molecular weight kininogen (HMWK).	Heparin	75-82	kininogen 1	Homo sapiens	194-198
11840659-0	2002	[Intraoperative management for a patient with heparin-induced thrombocytopenia (HIT) undergoing off-pump coronary bypass surgery using argatroban, a direct thrombin inhibitor].	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	156-164
11991242-8	2002	UFH induced an increase in t-PA either at 1 or 10 U/mL.	Heparin	0-3	plasminogen activator, tissue type	Homo sapiens	27-31
11805133-1	2002	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin.	Heparin	135-142	coagulation factor II	Mus musculus	61-69
12515911-4	2002	HPF-1 was recovered as a non-adsorbed fraction in blue Sepharose and heparin Sepharose columns, and had a molecular weight of 26-31 kDa as estimated by gel filtration in high salt condition.	Heparin	69-76	histone PARylation factor 1	Rattus norvegicus	0-5
12481200-3	2002	Unlike plasmapheresis, apolipoprotein B-containing lipoproteins (LDL, Lp(a), and VLDL) are selectively removed by heparin precipitation or columns containing dextran sulfate cellulose or antibodies to apolipoprotein B.	Heparin	114-121	apolipoprotein B	Homo sapiens	23-39
11848100-1	2002	Heparin-affin regulatory peptide (HARP) and Midkine (MK) belong to a family of growth/differentiation factors that have a high affinity for heparin.	Heparin	140-147	pleiotrophin	Homo sapiens	0-32
11848100-1	2002	Heparin-affin regulatory peptide (HARP) and Midkine (MK) belong to a family of growth/differentiation factors that have a high affinity for heparin.	Heparin	140-147	pleiotrophin	Homo sapiens	34-38
11848100-1	2002	Heparin-affin regulatory peptide (HARP) and Midkine (MK) belong to a family of growth/differentiation factors that have a high affinity for heparin.	Heparin	140-147	midkine	Homo sapiens	44-51
11848100-1	2002	Heparin-affin regulatory peptide (HARP) and Midkine (MK) belong to a family of growth/differentiation factors that have a high affinity for heparin.	Heparin	140-147	midkine	Homo sapiens	53-55
11898913-9	2002	Surprisingly, women with aPS receiving low molecular weight heparin prophylaxis had significantly higher (P = 0.02) levels of TAT (median 8.6; interquartile range (IQR) 6.5-20.8) between weeks 20 and 30 of gestation compared to the normal pregnant population (median 5.9; IQR 4.7-7.9), thus indicating increased thrombin generation in women with aPS in mid-pregnancy.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	312-320
11848445-8	2002	In summary, the structurally different polysaccharides, heparin, fucoidan (and fucans) have distinguishable effects on mitogenesis and ERK1/ERK2 activation, suggesting that different mechanism(s) mediate these actions.	Heparin	56-63	mitogen-activated protein kinase 3	Homo sapiens	135-139
11927149-7	2002	Intracellular injection of the IP(3) receptor blocker heparin prevented both the mAchR-mediated occurrence of IP(3)-assisted CICR and enhancement of spike-frequency adaptation with 10 microM carbachol.	Heparin	54-61	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	31-45
11848445-8	2002	In summary, the structurally different polysaccharides, heparin, fucoidan (and fucans) have distinguishable effects on mitogenesis and ERK1/ERK2 activation, suggesting that different mechanism(s) mediate these actions.	Heparin	56-63	mitogen-activated protein kinase 1	Homo sapiens	140-144
11724555-4	2001	In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin.	Heparin	96-103	fibroblast growth factor 7	Homo sapiens	122-127
11592962-7	2001	The use of a neutralizing antibody for heparin-binding EGF, one of the ligands of EGFR, blocked TPA-induced phosphorylation of ERKs.	Heparin	39-46	epidermal growth factor receptor	Homo sapiens	82-86
11592962-7	2001	The use of a neutralizing antibody for heparin-binding EGF, one of the ligands of EGFR, blocked TPA-induced phosphorylation of ERKs.	Heparin	39-46	mitogen-activated protein kinase 1	Homo sapiens	127-131
11755953-2	2001	This activation results in the thrombin generation, which is supposed to be suppressed by the low-molecular-mass heparins (LMMH), administered to the surgical patients as the prophylaxis against postoperative venous thromboembolism.	Heparin	113-121	coagulation factor II, thrombin	Homo sapiens	31-39
11724555-7	2001	Protection of FGF-7 required interaction with specifically the fraction of crude heparin retained on antithrombin affinity columns.	Heparin	81-88	fibroblast growth factor 7	Homo sapiens	14-19
11724555-8	2001	Conversely, heparin enriched by affinity for immobilized FGF-7 exhibited anti-factor Xa activity similar to that purified on an antithrombin affinity matrix.	Heparin	12-19	fibroblast growth factor 7	Homo sapiens	57-62
11724555-9	2001	In contrast, an FGF-1 affinity matrix enriched the fraction of crude heparin with low anti-factor Xa activity.	Heparin	69-76	fibroblast growth factor 1	Homo sapiens	16-21
11796239-2	2002	In addition, both neuropilins are able to bind to certain heparin-binding splice forms of vascular endothelial growth factor (VEGF), indicating that both neuropilins have roles in the cardiovascular system as well.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	90-124
11796239-2	2002	In addition, both neuropilins are able to bind to certain heparin-binding splice forms of vascular endothelial growth factor (VEGF), indicating that both neuropilins have roles in the cardiovascular system as well.	Heparin	58-65	vascular endothelial growth factor A	Homo sapiens	126-130
11755958-11	2001	Heparin alone, up to a concentration of 1 U/ml, had no effect on the activation of protein C. Small direct thrombin inhibitors thus inhibited both free and TM-bound thrombin and therefore also inhibited the activation of protein C. Whether this will influence their clinical efficacy or safety versus heparin and warfarin, which also inhibit protein activation, respectively, lowers the concentration of protein C, remains to be studied in clinical trials.	Heparin	301-308	coagulation factor II, thrombin	Homo sapiens	107-115
11724555-10	2001	The results provide a structural basis to suggest that the unique FGF-7 heparin-binding (HB) domain underlies a specific restriction in respect to composition and length of the heparan sulfate motif that may impact specificity of localization, stability, and trafficking of FGF-7 in the microenvironment, and formation and activation of the FGFR2IIIb kinase signaling complex in epithelial cells.	Heparin	72-79	fibroblast growth factor 7	Homo sapiens	66-71
11724555-10	2001	The results provide a structural basis to suggest that the unique FGF-7 heparin-binding (HB) domain underlies a specific restriction in respect to composition and length of the heparan sulfate motif that may impact specificity of localization, stability, and trafficking of FGF-7 in the microenvironment, and formation and activation of the FGFR2IIIb kinase signaling complex in epithelial cells.	Heparin	72-79	fibroblast growth factor 7	Homo sapiens	274-279
11724555-4	2001	In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin.	Heparin	96-103	fibroblast growth factor 1	Homo sapiens	159-164
11724555-4	2001	In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin.	Heparin	96-103	fibroblast growth factor 2	Homo sapiens	169-174
11724555-4	2001	In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin.	Heparin	193-200	fibroblast growth factor 7	Homo sapiens	122-127
11724555-4	2001	In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin.	Heparin	193-200	fibroblast growth factor 1	Homo sapiens	159-164
11724555-4	2001	In contrast, a decrease and dispersion of the positive surface charge density characterized the heparin-binding domain of FGF-7 defined by homology to that of FGF-1 and FGF-2 in complexes with heparin.	Heparin	193-200	fibroblast growth factor 2	Homo sapiens	169-174
11795306-6	2001	HB-EGF-dependent EGFR activation is blocked by heparin, a growth inhibitor of SMCs in vitro and in vivo.	Heparin	47-54	epidermal growth factor receptor	Homo sapiens	17-21
11748397-11	2001	TNF-alpha was below detectable concentrations in the control, KH + anti-TNF &gt; protamine + anti-TNF &gt; KH + anti-TNF, and KH + heparin &gt; protamine + heparin &gt; KH + heparin groups.	Heparin	131-138	tumor necrosis factor	Rattus norvegicus	0-9
11748397-11	2001	TNF-alpha was below detectable concentrations in the control, KH + anti-TNF &gt; protamine + anti-TNF &gt; KH + anti-TNF, and KH + heparin &gt; protamine + heparin &gt; KH + heparin groups.	Heparin	156-163	tumor necrosis factor	Rattus norvegicus	0-9
11748397-11	2001	TNF-alpha was below detectable concentrations in the control, KH + anti-TNF &gt; protamine + anti-TNF &gt; KH + anti-TNF, and KH + heparin &gt; protamine + heparin &gt; KH + heparin groups.	Heparin	156-163	tumor necrosis factor	Rattus norvegicus	0-9
11748397-13	2001	Heparin improved LV recovery and decreased protamine-induced TNF-alpha release (KH &gt; protamine &gt; KH + heparin group).	Heparin	0-7	tumor necrosis factor	Rattus norvegicus	61-70
11748397-14	2001	CONCLUSIONS: Anti-TNF-alpha antibodies and heparin prevent protamine-induced TNF-alpha release and depression of LV function.	Heparin	43-50	tumor necrosis factor	Rattus norvegicus	77-86
11742862-0	2001	Myeloperoxidase and hypochlorite, but not copper ions, oxidize heparin-bound LDL particles and release them from heparin.	Heparin	63-70	myeloperoxidase	Homo sapiens	0-15
11742862-0	2001	Myeloperoxidase and hypochlorite, but not copper ions, oxidize heparin-bound LDL particles and release them from heparin.	Heparin	113-120	myeloperoxidase	Homo sapiens	0-15
11730810-0	2001	Heparin-stimulated expression of extracellular-superoxide dismutase in human fibroblasts.	Heparin	0-7	superoxide dismutase 3	Homo sapiens	33-67
11730810-5	2001	In this study, we measured the induction of EC-SOD after treatment with heparin to understand the role of heparin in the antiatherosclerotic response of fibroblasts.	Heparin	72-79	superoxide dismutase 3	Homo sapiens	44-50
11730810-6	2001	Heparin induced EC-SOD expression at both the mRNA and protein levels.	Heparin	0-7	superoxide dismutase 3	Homo sapiens	16-22
11730810-11	2001	The enhanced expression of EC-SOD by heparin must contribute to the antiatherosclerotic effect of heparin.	Heparin	37-44	superoxide dismutase 3	Homo sapiens	27-33
11730810-11	2001	The enhanced expression of EC-SOD by heparin must contribute to the antiatherosclerotic effect of heparin.	Heparin	98-105	superoxide dismutase 3	Homo sapiens	27-33
11742862-5	2001	In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin.	Heparin	98-105	myeloperoxidase	Homo sapiens	13-28
11737589-8	2001	Addition of neutralizing anti-HB-EGF antibody, as well as pretreatment with heparin or the metalloproteinase inhibitor batimastat abolished induction of FN expression by Ang II.	Heparin	76-83	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	170-176
11742862-5	2001	In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin.	Heparin	98-105	myeloperoxidase	Homo sapiens	60-75
11742862-5	2001	In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin.	Heparin	186-193	myeloperoxidase	Homo sapiens	13-28
11742862-5	2001	In contrast, myeloperoxidase and hypochlorite, a product of myeloperoxidase, were able to oxidize heparin-bound LDL, and this oxidation led to the release of the oxidized particles from heparin.	Heparin	186-193	myeloperoxidase	Homo sapiens	60-75
11787776-5	2001	Western blot analysis showed that levels of bcl-2, bax and c-myc were significantly overexpressed by treatment with the increase of heparin concentrations.	Heparin	132-139	BCL2 apoptosis regulator	Homo sapiens	44-49
11787776-5	2001	Western blot analysis showed that levels of bcl-2, bax and c-myc were significantly overexpressed by treatment with the increase of heparin concentrations.	Heparin	132-139	BCL2 associated X, apoptosis regulator	Homo sapiens	51-54
11689276-0	2001	A patient with subcutaneous-insulin resistance treated by insulin lispro plus heparin.	Heparin	78-85	insulin	Homo sapiens	28-35
11689276-3	2001	From these results, the patient followed the insulin lispro plus heparin protocol and obtained a better glycemic control without any adverse events.	Heparin	65-72	insulin	Homo sapiens	45-52
11822782-2	2001	This study investigated the impact of low molecular weight heparin (LMWH) on tumor necrosis factor (TNF)-alpha-provoked leukocyte rolling, adhesion and extravascular accumulation.	Heparin	59-66	tumor necrosis factor	Mus musculus	77-110
11776314-1	2001	The aim of our study was to characterise heparin-binding properties of mutated von Willebrand factor (VWF) in 24 patients plasmas with type 2 von Willebrand disease (VWD).	Heparin	41-48	von Willebrand factor	Homo sapiens	79-100
12080874-10	2001	Heparin dose was guided by usual parameters of blood coagulation, and insulin dose, by serial determinations of blood glucose.	Heparin	0-7	insulin	Homo sapiens	70-77
11776314-1	2001	The aim of our study was to characterise heparin-binding properties of mutated von Willebrand factor (VWF) in 24 patients plasmas with type 2 von Willebrand disease (VWD).	Heparin	41-48	von Willebrand factor	Homo sapiens	102-105
11683636-2	2001	Recent studies have shown that the thrombin domain referred to as heparin binding site (HBS) is involved in the interaction with the platelet Gp(Ib)alpha.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	35-43
11551944-1	2001	Fibroblast growth factor 2 (FGF2)-initiated FGF receptor (FGFR)-signaling requires the assistance of heparin/heparan sulfate.	Heparin	101-108	fibroblast growth factor 2	Homo sapiens	0-26
11551944-1	2001	Fibroblast growth factor 2 (FGF2)-initiated FGF receptor (FGFR)-signaling requires the assistance of heparin/heparan sulfate.	Heparin	101-108	fibroblast growth factor 2	Homo sapiens	28-32
11584020-7	2001	In contrast, the integrity of exosite 2 is largely retained when thrombin is complexed by serpins, because interaction with heparin or an exosite 2-directed DNA aptamer was only modestly altered.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	65-73
11760675-1	2001	UNLABELLED: We report a case of renal vein thrombosis, treated with heparin and thrombolytic therapy, in a patient who was heterozygous for both factor V Leiden and prothrombin mutations.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	165-176
11694151-11	2001	Those taking dalteparin with elevated IL-6 levels experienced lower 6-month mortality than those who did not take dalteparin (3.5% absolute reduction; P =.08).	Heparin	13-23	interleukin 6	Homo sapiens	38-42
11600429-5	2001	However, a better preservation was obtained in the presence of selective PP1 inhibitors heparin (100 microg/ml) or protein phosphatase inhibitor 2 (I2; 100 nM).	Heparin	88-95	neuropeptide Y receptor Y4	Rattus norvegicus	73-76
12536495-0	2001	[Influence of low-molecular weight heparin on urine interleukin-6 in patients with proliferative glomerulonephritis].	Heparin	35-42	interleukin 6	Homo sapiens	52-65
11685164-11	2001	After both unfractionated heparin and dalteparin administration, platelet surface GP IIIa expression was significantly increased compared with baseline at both 8 to 10 and 16 to 24 hours.	Heparin	26-33	integrin subunit beta 3	Homo sapiens	82-89
11704218-0	2001	Anticoagulation with a selective thrombin inhibitor in a woman with heparin-induced thrombocytopenia.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	33-41
11514538-0	2001	Vascular endothelial growth factor 165 (VEGF(165)) activities are inhibited by carboxymethyl benzylamide dextran that competes for heparin binding to VEGF(165) and VEGF(165).KDR Complexes.	Heparin	131-138	vascular endothelial growth factor A	Homo sapiens	40-44
11514538-0	2001	Vascular endothelial growth factor 165 (VEGF(165)) activities are inhibited by carboxymethyl benzylamide dextran that competes for heparin binding to VEGF(165) and VEGF(165).KDR Complexes.	Heparin	131-138	vascular endothelial growth factor A	Homo sapiens	150-154
11514538-0	2001	Vascular endothelial growth factor 165 (VEGF(165)) activities are inhibited by carboxymethyl benzylamide dextran that competes for heparin binding to VEGF(165) and VEGF(165).KDR Complexes.	Heparin	131-138	vascular endothelial growth factor A	Homo sapiens	150-154
11514538-7	2001	Moreover, CMDB7 reduces the (125)I-VEGF(165) binding to coated heparin-albumin and prevents a heparin-induced increase in iodinated VEGF(165) binding to soluble (125)I-KDR-Fc chimera.	Heparin	94-101	vascular endothelial growth factor A	Homo sapiens	132-136
11514538-9	2001	In the presence of VEGF(165), (125)I-KDR-Fc binding to heparin is enhanced, and under these conditions, CMDB7 interferes with KDR binding.	Heparin	55-62	vascular endothelial growth factor A	Homo sapiens	19-23
11514538-10	2001	These data indicate that CMDB7 effectively inhibits the VEGF(165) activities by interfering with heparin binding to VEGF(165) and VEGF(165).KDR complexes but not by direct interactions with KDR.	Heparin	97-104	vascular endothelial growth factor A	Homo sapiens	56-60
11514538-10	2001	These data indicate that CMDB7 effectively inhibits the VEGF(165) activities by interfering with heparin binding to VEGF(165) and VEGF(165).KDR complexes but not by direct interactions with KDR.	Heparin	97-104	vascular endothelial growth factor A	Homo sapiens	116-120
11514538-10	2001	These data indicate that CMDB7 effectively inhibits the VEGF(165) activities by interfering with heparin binding to VEGF(165) and VEGF(165).KDR complexes but not by direct interactions with KDR.	Heparin	97-104	vascular endothelial growth factor A	Homo sapiens	116-120
12536495-1	2001	OBJECTIVE: To explore the influence of low-molecular weight heparin (LMWH) on interleukin-6 (IL-6) in patients with proliferative glomerulonephritis, 24 patients which had been distinctly diagnosed by renal biopsy were randomly divided into a control group (n = 12) and a treatment group (n = 12).	Heparin	60-67	interleukin 6	Homo sapiens	78-91
12536495-1	2001	OBJECTIVE: To explore the influence of low-molecular weight heparin (LMWH) on interleukin-6 (IL-6) in patients with proliferative glomerulonephritis, 24 patients which had been distinctly diagnosed by renal biopsy were randomly divided into a control group (n = 12) and a treatment group (n = 12).	Heparin	60-67	interleukin 6	Homo sapiens	93-97
11557552-4	2001	The expression and secretion of EC-SOD were upregulated by histamine, vasopressin, oxytocin, endothelin-1, angiotensin II, serotonin, heparin, and heparan sulfate and were downregulated by platelet-derived growth factors-AA and -BB, acidic and basic fibroblast growth factors, and epidermal growth factor.	Heparin	134-141	superoxide dismutase 3	Homo sapiens	32-38
11500500-3	2001	To identify which residues in the heparin-binding site of apoE and which structural elements of heparan sulfate interact, we used a variety of approaches, including glycosaminoglycan specificity assays, (13)C nuclear magnetic resonance, and heparin affinity chromatography.	Heparin	34-41	apolipoprotein E	Homo sapiens	58-62
11500500-4	2001	The formation of the high affinity complex required Arg-142, Lys-143, Arg-145, Lys-146, and Arg-147 from apoE and N- and 6-O-sulfo groups of the glucosamine units from the heparin fragment.	Heparin	172-179	apolipoprotein E	Homo sapiens	105-109
11695869-6	2001	The use of CarboPac PA1 columns for the semi-preparative scale separation of oligosaccharides in size-uniform fractions isolated from depolymerized heparin by low-pressure (gravity flow) GPC is also reported.	Heparin	148-155	PAXIP1 associated glutamate rich protein 1	Homo sapiens	20-23
11668418-3	2001	Unfractionated heparin (UFH) as well as low molecular weight heparin (LMWH) (enoxaparin) inhibited the mitogenic effects of FXa, thrombin and fetal calf serum (FCS), but did not reduce mitogenesis induced by PDGF.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	129-137
11820460-1	2001	We analyzed the influence of heparins (unfractionated heparin, UFH and low molecular weight heparin certoparin) on the generation of IL-1ra, IL-6, IL-10, and IL-12p40 and from leukocyte fractions in vitro.	Heparin	29-37	interleukin 6	Homo sapiens	141-145
11583732-2	2001	A prospective trial of familial hypercholesterolemic patients treated with Heparin-induced Extra-corporeal Low-Density Lipoprotein Precipitation (HELP, B. Braun Melsungen) therapy was undertaken to evaluate the short- and long-term effects on CRP.	Heparin	75-82	C-reactive protein	Homo sapiens	243-246
11606310-15	2001	Heparin : tryptase molar ratios of greater than 2 : 1 abrogated tryptase activation of PAR(2)T25(-).	Heparin	0-7	tryptase alpha/beta 1	Rattus norvegicus	10-18
11606310-15	2001	Heparin : tryptase molar ratios of greater than 2 : 1 abrogated tryptase activation of PAR(2)T25(-).	Heparin	0-7	tryptase alpha/beta 1	Rattus norvegicus	64-72
11606310-17	2001	Our results indicate that glycosylation of PAR(2) and heparin-inhibition of PAR(2) activation by tryptase could provide novel mechanisms for regulating receptor activation by tryptase and possibly other proteases.	Heparin	54-61	tryptase alpha/beta 1	Rattus norvegicus	97-105
11606310-17	2001	Our results indicate that glycosylation of PAR(2) and heparin-inhibition of PAR(2) activation by tryptase could provide novel mechanisms for regulating receptor activation by tryptase and possibly other proteases.	Heparin	54-61	tryptase alpha/beta 1	Rattus norvegicus	175-183
11723606-2	2001	During clot resolution, platelet-rich thrombi are relatively resistant to fibrinolytic agents, mainly due to the release of plasminogen inhibitor-1 by platelets which are activated as a result of the increase in thrombin generation induced by plasminogen activator therapy despite heparin administration.	Heparin	281-288	coagulation factor II, thrombin	Homo sapiens	212-220
11668414-9	2001	Preliminary plasma protein adhesion measurements on immobilized HE derivatives with four different fluorescence-labeled plasma proteins showed a regioselective influence with serum albumin and fibrinogen.	Heparin	64-66	fibrinogen beta chain	Homo sapiens	193-203
11668417-0	2001	Effects of sulfation on antithrombin-thrombin/factor Xa interactions in semisynthetic low molecular weight heparins.	Heparin	107-115	coagulation factor II, thrombin	Homo sapiens	28-36
11668418-3	2001	Unfractionated heparin (UFH) as well as low molecular weight heparin (LMWH) (enoxaparin) inhibited the mitogenic effects of FXa, thrombin and fetal calf serum (FCS), but did not reduce mitogenesis induced by PDGF.	Heparin	24-27	coagulation factor II, thrombin	Homo sapiens	129-137
11668418-3	2001	Unfractionated heparin (UFH) as well as low molecular weight heparin (LMWH) (enoxaparin) inhibited the mitogenic effects of FXa, thrombin and fetal calf serum (FCS), but did not reduce mitogenesis induced by PDGF.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	129-137
11668418-4	2001	Similarly, both UFH and LMWH inhibited the activation of extracellular signal-regulated kinase (ERK-1/2) by FXa, thrombin and FCS, but not by PDGF.	Heparin	16-19	mitogen-activated protein kinase 3	Homo sapiens	96-103
11668418-4	2001	Similarly, both UFH and LMWH inhibited the activation of extracellular signal-regulated kinase (ERK-1/2) by FXa, thrombin and FCS, but not by PDGF.	Heparin	16-19	coagulation factor II, thrombin	Homo sapiens	113-121
11686357-0	2001	Comparison of enoxaparin and unfractionated heparin on thrombin generation in acute coronary syndromes without ST-segment elevation.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	55-63
11686357-2	2001	No data are available concerning the in-vivo comparison of enoxaparin and unfractionated heparin on thrombin generation in patients with unstable angina or non-Q-wave myocardial infarction.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	100-108
11686357-8	2001	Both enoxaparin and unfractionated heparin produced a marked and similar reduction of thrombin generation.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	86-94
11668418-6	2001	The inhibition of ERK-1/2 correlated with the inhibition of mitogenesis by the heparins.	Heparin	79-87	mitogen-activated protein kinase 3	Homo sapiens	18-25
11668418-7	2001	Thus, the inhibition of ERK-1/2 phosphorylation by heparins might predict an antimitogenai response in this system.	Heparin	51-59	mitogen-activated protein kinase 3	Homo sapiens	24-31
11668419-4	2001	The characterization of the HBP using heparin activity assays showed that the HBP shortened the prolonged clotting times of the activated partial thromboplastin time (aPTT) and thrombin clotting time induced by high concentrations of unfractionated heparin.	Heparin	38-45	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	28-31
11668419-4	2001	The characterization of the HBP using heparin activity assays showed that the HBP shortened the prolonged clotting times of the activated partial thromboplastin time (aPTT) and thrombin clotting time induced by high concentrations of unfractionated heparin.	Heparin	38-45	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	78-81
11668419-4	2001	The characterization of the HBP using heparin activity assays showed that the HBP shortened the prolonged clotting times of the activated partial thromboplastin time (aPTT) and thrombin clotting time induced by high concentrations of unfractionated heparin.	Heparin	38-45	coagulation factor II	Mus musculus	177-185
11668419-5	2001	The chromogenic assays for antithrombin (AT), thrombin inhibition, and factor Xa inhibition demonstrated that this effect is related to heparin concentrations below 0.5 IU/ml.	Heparin	136-143	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
11668419-5	2001	The chromogenic assays for antithrombin (AT), thrombin inhibition, and factor Xa inhibition demonstrated that this effect is related to heparin concentrations below 0.5 IU/ml.	Heparin	136-143	coagulation factor II	Mus musculus	31-39
11668419-11	2001	These data suggest that the HBP isolated from mouse myeloma cells has a low affinity to heparin and interacts with the secondary binding site to AT and also perhaps to PF4.	Heparin	88-95	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	28-31
11535495-6	2001	In this study, the purification of human vWF-cleaving protease from a commercial preparation of factor VIII/vWF concentrate by means of several column chromatographic steps, including 2 steps of heparin-Sepharose column, is reported.	Heparin	195-202	von Willebrand factor	Homo sapiens	41-44
11566193-4	2001	SNAP and NOR4 also decreased the binding of EC-SOD to immobilized heparin.	Heparin	66-73	superoxide dismutase 3	Homo sapiens	44-50
11828504-6	2001	Both compounds 1 and 2 induce the mitogenic activity of acid fibroblast growth factor (FGF1), with the half-maximum activating concentration of 2 being equivalent to that of heparin.	Heparin	174-181	fibroblast growth factor 1	Homo sapiens	87-91
11571649-4	2001	Since VEGF has an extracellular matrix (ECM)-binding domain and possesses binding affinity for heparin, we sought to determine the effects of VEGF in breast cancer cells and the role of heparin and/or fibronectin in VEGF-induced signaling.	Heparin	95-102	vascular endothelial growth factor A	Homo sapiens	6-10
11571649-7	2001	After treatment with VEGF, [(3)H]thymidine incorporation, c-fos induction, and the number of migrating cells were significantly higher ( approximately twofold) in cells grown on fibronectin or in cells grown on plastic in the presence of heparin when compared to those grown on plastic only.	Heparin	238-245	vascular endothelial growth factor A	Homo sapiens	21-25
11571649-8	2001	Likewise, tyrosine phosphorylation of VEGF receptors, MAPK activity and PI3-kinase activity were all several-fold higher in cells seeded on fibronectin or in the presence of heparin as compared to cells exposed to VEGF alone.	Heparin	174-181	vascular endothelial growth factor A	Homo sapiens	38-42
11828504-7	2001	Sedimentation equilibrium analysis with compound 2 suggests that heparin-induced FGF1 dimerization is not an absolute requirement for biological activity.	Heparin	65-72	fibroblast growth factor 1	Homo sapiens	81-85
11555579-2	2001	We examined the concentration of vascular endothelial growth factor (VEGF) and basic fibroblast growth factor (bFGF), two potent heparin-binding mediators of angiogenesis in peripheral blood (PB; PB-VEGF and PB-bFGF) and bone marrow (BM; BM-VEGF and BM-bFGF), in combination with well-characterized predictors for response and survival to chemotherapy.	Heparin	129-136	fibroblast growth factor 2	Homo sapiens	111-115
11532694-0	2001	Regulation of renal proximal tubular epithelial cell fibroblast growth factor-2 generation by heparin.	Heparin	94-101	fibroblast growth factor 2	Homo sapiens	53-79
11532694-3	2001	FGF-2 is characterized by its high affinity for heparin, and numerous studies have suggested that heparin may modify the progression of renal disease.	Heparin	48-55	fibroblast growth factor 2	Homo sapiens	0-5
11555702-1	2001	We report the case of a 31-year-old woman with protein S deficiency and heterozygosity for the prothrombin 3" UTR mutation who developed an internal jugular vein thrombosis despite therapeutic anticoagulation with a low molecular weight heparin, following in-vitro fertilization.	Heparin	237-244	coagulation factor II, thrombin	Homo sapiens	95-106
11532694-3	2001	FGF-2 is characterized by its high affinity for heparin, and numerous studies have suggested that heparin may modify the progression of renal disease.	Heparin	98-105	fibroblast growth factor 2	Homo sapiens	0-5
11532694-4	2001	The current study examined how heparin influenced FGF-2 generation and bioactivity in the human renal epithelial PTC line, HK-2.	Heparin	31-38	fibroblast growth factor 2	Homo sapiens	50-55
11532694-5	2001	Incubation of HK-2 cells with heparin led to a dose- and time-dependent increase in FGF-2 concentration in the culture supernatant that was not accompanied by alterations in FGF-2 messenger RNA expression, assessed by reverse-transcriptase polymerase chain reaction and Northern analysis.	Heparin	30-37	fibroblast growth factor 2	Homo sapiens	84-89
11532694-6	2001	The heparin-induced increase in FGF-2 concentration was accompanied by a decrease in the amount of FGF-2 bound to the extracellular matrix, although this accounted for only a small proportion of the total FGF-2 generated.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	32-37
11532694-6	2001	The heparin-induced increase in FGF-2 concentration was accompanied by a decrease in the amount of FGF-2 bound to the extracellular matrix, although this accounted for only a small proportion of the total FGF-2 generated.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	99-104
11532694-6	2001	The heparin-induced increase in FGF-2 concentration was accompanied by a decrease in the amount of FGF-2 bound to the extracellular matrix, although this accounted for only a small proportion of the total FGF-2 generated.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	99-104
11532694-7	2001	Induction of FGF-2 by 2-O-desulfated heparin, together with a reduction in total cell-associated FGF-2 and anti-FGF-2 antibody binding to fixed permeabilized cells after the addition of heparin, suggested that the FGF-2 released was mainly derived from a preformed intracellular source.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	13-18
11532694-9	2001	The addition of heparin resulted in the generation of bioinactive FGF-2, judged by in vitro fibroblast proliferation.	Heparin	16-23	fibroblast growth factor 2	Homo sapiens	66-71
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	165-170
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	218-223
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	218-223
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	165-170
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	218-223
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	218-223
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	165-170
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	218-223
11532694-10	2001	Conversely, heparitinase treatment of supernatant samples from heparin-treated cells and the addition of 2-O-desulfated heparin resulted in the generation of active FGF-2, suggesting that the generation of bioinactive FGF-2 was related to binding of FGF-2 by extracellular heparin after its release from cells.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	218-223
11532694-11	2001	These data show that heparin depletes both the cell and surrounding matrix of FGF-2 and suggest that FGF-2 released from cells was mainly derived from a preformed intracellular source.	Heparin	21-28	fibroblast growth factor 2	Homo sapiens	78-83
11532694-12	2001	Furthermore, FGF-2 released from epithelial PTCs after the application of heparin was bioinactive.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	13-18
11532694-13	2001	This likely resulted from released FGF-2 binding to an excess of extracellular heparin.	Heparin	79-86	fibroblast growth factor 2	Homo sapiens	35-40
11532694-14	2001	Results presented here therefore suggest a mechanism by which heparin, through its effect on depletion of matrix and cells of FGF-2 and its generation in an inactive form, may influence progressive renal interstitial fibrosis.	Heparin	62-69	fibroblast growth factor 2	Homo sapiens	126-131
11533507-1	2001	Use of combination glycoprotein IIb/IIIa inhibitor and direct thrombin inhibitor drugs to support percutaneous coronary stent placement in a patient with renal insufficiency and heparin-induced thrombocytopenia.	Heparin	178-185	coagulation factor II, thrombin	Homo sapiens	62-70
11532088-0	2001	Low-molecular-weight heparin prevents high glucose- and phorbol ester-induced TGF-beta 1 gene activation.	Heparin	21-28	transforming growth factor beta 1	Homo sapiens	78-88
11518760-8	2001	In solid-phase assays, heparin, suramin, and chondroitin sulfates A and B efficiently inhibited the binding of apoE to heparan sulfate proteoglycans, but were unable to displace apoE from this glycosaminoglycan.	Heparin	23-30	apolipoprotein E	Homo sapiens	111-115
11800287-8	2001	Heparin-releasable lipoprotein lipase activity in perirenal and subcutaneous adipose tissues was not different among rats fed olive oil, safflower oil, palm oil or beef tallow.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-37
11532088-2	2001	Since previous in vivo studies demonstrated a renoprotective effect of low-molecular-weight (LMW) heparin in experimental animals, and recent in vitro data showed an interaction of this drug with the overactivated TGF-beta 1 cascade in high glucose- and phorbol ester-stimulated mesangial cells, we studied the molecular mechanism of these effects on TGF-beta 1 gene expression.	Heparin	98-105	transforming growth factor beta 1	Homo sapiens	214-224
11532088-10	2001	The LMW heparin effect on basal promoter activity was abolished by mutation of the regulatory AP-1 box B and by deletion of this AP-1 binding site.	Heparin	8-15	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	94-98
11532088-10	2001	The LMW heparin effect on basal promoter activity was abolished by mutation of the regulatory AP-1 box B and by deletion of this AP-1 binding site.	Heparin	8-15	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	129-133
11532088-11	2001	CONCLUSIONS: LMW heparin prevents high glucose- and PMA-mediated TGF-beta 1 expression by inhibiting the activation of the TGF-beta 1 promoter and by preventing the enhanced binding of nuclear proteins to the regulatory AP-1 site.	Heparin	17-24	transforming growth factor beta 1	Homo sapiens	65-75
11532088-11	2001	CONCLUSIONS: LMW heparin prevents high glucose- and PMA-mediated TGF-beta 1 expression by inhibiting the activation of the TGF-beta 1 promoter and by preventing the enhanced binding of nuclear proteins to the regulatory AP-1 site.	Heparin	17-24	transforming growth factor beta 1	Homo sapiens	123-133
11532088-11	2001	CONCLUSIONS: LMW heparin prevents high glucose- and PMA-mediated TGF-beta 1 expression by inhibiting the activation of the TGF-beta 1 promoter and by preventing the enhanced binding of nuclear proteins to the regulatory AP-1 site.	Heparin	17-24	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	220-224
11703814-7	2001	The mechanisms through which heparin can enhance thrombin generation are discussed and treatment alternatives for affected patients are presented in detail.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	49-57
11486033-0	2001	Identification of receptor and heparin binding sites in fibroblast growth factor 4 by structure-based mutagenesis.	Heparin	31-38	fibroblast growth factor 4	Homo sapiens	56-82
11486033-1	2001	Fibroblast growth factors (FGFs) comprise a large family of multifunctional, heparin-binding polypeptides that show diverse patterns of interaction with a family of receptors (FGFR1 to -4) that are subject to alternative splicing.	Heparin	77-84	fibroblast growth factor receptor 1	Homo sapiens	176-181
11486033-6	2001	To identify potential receptor and heparin binding sites in FGF4, a ternary FGF4-FGFR1-heparin model was constructed by superimposing the FGF4 structure onto FGF2 in the FGF2-FGFR1-heparin structure.	Heparin	35-42	fibroblast growth factor 4	Homo sapiens	60-64
11486033-7	2001	Mutation of several key residues in FGF4, observed to interact with FGFR1 or with heparin in the model, produced ligands with reduced receptor binding and concomitant low mitogenic potential.	Heparin	82-89	fibroblast growth factor 4	Homo sapiens	36-40
11486033-9	2001	Moreover, we show that FGF4 needs to interact with both the 2-O- and 6-O-sulfates in heparin to exert its optimal biological activity.	Heparin	85-92	fibroblast growth factor 4	Homo sapiens	23-27
11583326-1	2001	We compare the relative activities of surface-bound and fluid-phase thrombin and their inhibition by heparin and Intimatan, a novel heparin cofactor II (HCII) agonist.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	68-76
11583326-3	2001	In vivo, we compared the inhibitory effects of heparin and Intimatan on thrombin activity bound to injured vessel walls.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	72-80
11583326-5	2001	In vivo, injured vessel wall surface-bound thrombin activity persisted for &gt; 24 h. This activity was not inhibited by heparin, but was inhibited by Intimatan, p &lt; 0.001.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	43-51
11583326-6	2001	We conclude that surface-bound thrombin is as active as fluid-phase thrombin and remains protected from inhibition by heparin, thereby contributing to vessel wall thrombogenicity following injury.	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	31-39
11456069-5	2001	Immobilization of increasing amounts of heparin, also using EDC and NHS, to crosslinked collagen containing 14 free primary amino groups per 1000 amino acid residues (E/N14C) resulted in binding of increasing amounts of bFGF.	Heparin	40-47	fibroblast growth factor 2	Homo sapiens	220-224
11493478-0	2001	Antibodies from patients with heparin-induced thrombocytopenia stimulate monocytic cells to express tissue factor and secrete interleukin-8.	Heparin	30-37	C-X-C motif chemokine ligand 8	Homo sapiens	126-139
11479487-3	2001	UFH has been linked to a discontinuation rebound in thrombin generation, which is associated with greater ischemic end points than those with the direct thrombin inhibitor hirudin.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	52-60
11488617-0	2001	Binding of bovine serum albumin to heparin determined by turbidimetric titration and frontal analysis continuous capillary electrophoresis.	Heparin	35-42	albumin	Homo sapiens	18-31
11454595-4	2001	Wy-14643 and BM-17.0744 also reduced heparin-releasable LPL activity and mass in the culture medium.	Heparin	37-44	lipoprotein lipase	Rattus norvegicus	56-59
11454595-6	2001	A similar inhibitory effect on cellular and heparin-releasable LPL activity was observed when cardiomyocytes were cultured with 60 microM linoleic acid.	Heparin	44-51	lipoprotein lipase	Rattus norvegicus	63-66
11456069-6	2001	A plateau in bFGF binding was observed for heparinized E/N14C containing approximately 2.0-3.0 wt% of immobilized heparin which was obtained using a molar ratio of EDC to heparin-carboxylic acid groups of 0.4 during heparin immobilization (E/N14C-H(0.4)).	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	13-17
11456069-6	2001	A plateau in bFGF binding was observed for heparinized E/N14C containing approximately 2.0-3.0 wt% of immobilized heparin which was obtained using a molar ratio of EDC to heparin-carboxylic acid groups of 0.4 during heparin immobilization (E/N14C-H(0.4)).	Heparin	114-121	fibroblast growth factor 2	Homo sapiens	13-17
11457782-4	2001	Total and heparin-releasable LPL (HR-LPL) activities were decreased 38% (P &lt; 0.01) and 52% (P &lt; 0.05), respectively, in the soleus muscle of the older Fischer 344 rats.	Heparin	10-17	lipoprotein lipase	Rattus norvegicus	29-32
11457455-4	2001	We have analysed the sequences of worm and fly FGFs and FGFRs and used the recently determined crystal structure of the human FGF1-FGFR2-heparin ternary complex [Pellegrini, L., Burke, D.F., von Delft, F., Mulloy, B. and Blundell, T.L.	Heparin	137-144	fibroblast growth factor 1	Homo sapiens	126-130
12940068-4	2001	Incubations with heparinase (3 U/ml) and heparin (1 mg/ml) decreased apoE by 25.0% and 30.5% respectively indicating association through cell surface haparin sulfate proteoglycans.	Heparin	17-24	apolipoprotein E	Homo sapiens	69-73
11435305-7	2001	However, when the 2 genotypes were compared in the in vitro perfusion chamber where thrombin was inhibited by heparin, no significant differences were found in either initial single-platelet adhesion or thrombus volume.	Heparin	110-117	coagulation factor II	Mus musculus	84-92
11573243-9	2001	In adhesion assays performed on matrix-coated titer plates both cell lines adhered to types I and III collagen and cellular fibronectin, and cell adhesion was inhibited by preincubation of the matrix with heparin, heparan sulfate, chondroitin sulfate, dermatan sulfate, or chondroitin glycosaminoglycans.	Heparin	205-212	fibronectin 1	Homo sapiens	124-135
11522012-3	2001	Binding to the cell blocked acceleration of the thrombin:antithrombin interaction by heparin.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	48-56
11427638-5	2001	On bivariate regression analysis, vWF : Ag level was directly associated with the presence of CVD, age, fibrinogen and the use of enoxaparin (vs unfractionated heparin) during HD procedures, and inversely with albumin and pre-dialysis BP.	Heparin	160-167	von Willebrand factor	Homo sapiens	34-37
11350966-4	2001	Additional experiments showed that reductively methylated apoE, which is incapable of receptor binding yet retains its heparin binding capability, was equally effective as apoE in inhibiting PDGF-stimulated smooth muscle cell proliferation.	Heparin	119-126	apolipoprotein E	Homo sapiens	58-62
11451924-9	2001	Heparin as low as 0.01 mg/mL significantly downregulated expression of TGF-beta(1) and FGF-1-stimulated FGF-2 and FGFR-1.	Heparin	0-7	transforming growth factor, beta 1	Rattus norvegicus	71-82
11510916-13	2001	After switching back to UFH for hemodialysis, these biochemical indices reverted to previous values during UFH treatment with a significant higher level in TC and Apo B while serum Apo A-1 remained elevated.	Heparin	24-27	apolipoprotein B	Homo sapiens	163-168
11510916-13	2001	After switching back to UFH for hemodialysis, these biochemical indices reverted to previous values during UFH treatment with a significant higher level in TC and Apo B while serum Apo A-1 remained elevated.	Heparin	24-27	apolipoprotein A1	Homo sapiens	181-188
11510916-13	2001	After switching back to UFH for hemodialysis, these biochemical indices reverted to previous values during UFH treatment with a significant higher level in TC and Apo B while serum Apo A-1 remained elevated.	Heparin	107-110	apolipoprotein B	Homo sapiens	163-168
11436089-8	2001	Compared with the heparin group, the TFPI group had a significant reduction in intimal area (0.19 +/- 0.05 mm(2) vs 0.30 +/- 0.09 mm(2), P =.0051), in percentage of stenosis (35.7% +/- 7.7% vs 61.4% +/- 15.8%, P &lt;.0001), and in intimal/media areas ratio (0.64 +/- 0.24 vs. 1.04 +/- 0.33, P =.0051).	Heparin	18-25	tissue factor pathway inhibitor	Oryctolagus cuniculus	37-41
11692908-8	2001	To reduce thrombin generation, i.e., the mechanism by which heparin-induced thrombocytopenia induces thrombotic events, intravenous treatment with dermatan sulphate and low-dose urokinase was initiated.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	10-18
11441979-2	2001	The current mainstays of anticoagulation treatment are heparins, which are indirect thrombin inhibitors, and coumarins, such as warfarin, which modulate the synthesis of vitamin K-dependent proteins.	Heparin	55-63	coagulation factor II, thrombin	Homo sapiens	84-92
11454528-2	2001	Since enoxaparin appears to offer clinical advantages over UFH in managing ACS, markers of thrombin generation, endothelial function and acute phase response could manifest different responses to UFH or enoxaparin.	Heparin	196-199	coagulation factor II, thrombin	Homo sapiens	91-99
11454528-10	2001	INTERPRETATION AND CONCLUSIONS: Markers of thrombin generation, endothelial function and acute-phase reactants manifest a similar response to UFH and enoxaparin.	Heparin	142-145	coagulation factor II, thrombin	Homo sapiens	43-51
11454528-11	2001	An increase in thrombin generation may be a result of persistently activated inflammatory and endothelial processes, despite UFH and enoxaparin treatment.	Heparin	125-128	coagulation factor II, thrombin	Homo sapiens	15-23
11390626-0	2001	Heparin inhibits retrovirus binding to fibronectin as well as retrovirus gene transfer on fibronectin fragments.	Heparin	0-7	fibronectin 1	Homo sapiens	39-50
11390626-0	2001	Heparin inhibits retrovirus binding to fibronectin as well as retrovirus gene transfer on fibronectin fragments.	Heparin	0-7	fibronectin 1	Homo sapiens	90-101
11292822-2	2001	In the case of fibroblast growth factor-2 (FGF2) signaling, heparin/heparan sulfate-like glycosaminoglycans (HLGAGs) are involved through interaction with both FGF2 and its receptors (FGFRs) in assembling a tertiary complex and modulating FGF2 activity.	Heparin	60-67	fibroblast growth factor 2	Homo sapiens	15-41
11292822-2	2001	In the case of fibroblast growth factor-2 (FGF2) signaling, heparin/heparan sulfate-like glycosaminoglycans (HLGAGs) are involved through interaction with both FGF2 and its receptors (FGFRs) in assembling a tertiary complex and modulating FGF2 activity.	Heparin	60-67	fibroblast growth factor 2	Homo sapiens	43-47
11292822-2	2001	In the case of fibroblast growth factor-2 (FGF2) signaling, heparin/heparan sulfate-like glycosaminoglycans (HLGAGs) are involved through interaction with both FGF2 and its receptors (FGFRs) in assembling a tertiary complex and modulating FGF2 activity.	Heparin	60-67	fibroblast growth factor 2	Homo sapiens	160-164
11292822-2	2001	In the case of fibroblast growth factor-2 (FGF2) signaling, heparin/heparan sulfate-like glycosaminoglycans (HLGAGs) are involved through interaction with both FGF2 and its receptors (FGFRs) in assembling a tertiary complex and modulating FGF2 activity.	Heparin	60-67	fibroblast growth factor 2	Homo sapiens	160-164
11316800-1	2001	In vivo, the catalytic activity of APC is regulated by two serpins, alpha1-antitrypsin and the protein C inhibitor (PCI), the inhibition by the latter being stimulated by heparin.	Heparin	171-178	serpin family A member 1	Homo sapiens	68-86
11412111-1	2001	Inhibition of factor XIa by protease nexin II (K(i) approximately 450 pM) is potentiated by heparin (K(I) approximately 30 pM).	Heparin	92-99	amyloid beta precursor protein	Homo sapiens	28-45
11460008-4	2001	The kinetic studies of inhibition of thrombin by C1-INH showed an average second-order rate constant of 19/s per mol/l, which was significantly increased in the presence of heparin.	Heparin	173-180	coagulation factor II, thrombin	Homo sapiens	37-45
11373076-3	2001	With the addition of heparin to the enzyme sample, MMP-7 can be detected at a level of 30 pg in transferrin zymography and MMP-1 and -13 can be detected at a level of 0.2 ng in gelatin zymography.	Heparin	21-28	transferrin	Rattus norvegicus	96-107
11453879-0	2001	Heparin-coated extracorporeal circulation with full and low dose heparinization: comparison of thrombin related coagulatory effects.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	95-103
11453879-1	2001	Thrombin related coagulatory effects of a heparin-coated cardiopulmonary bypass system combined with full and low dose systemic heparinization were investigated in a prospective, randomized study in coronary bypass surgery patients.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	0-8
11453879-7	2001	Thrombin generation as indicated by F1/F2 was significantly elevated at an ECC duration &gt;60 min if heparin-coated ECC combined with low dose systemic heparinization was employed.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	0-8
11453879-10	2001	Signs of clinical thromboembolism, i.e., postoperative neurological deficit, occurred in 2 patients in Group A and 1 patient in Group C. We conclude that heparin-coated extracorporeal circulation combined with reduced systemic heparinization intraoperatively leads to significantly increased thrombin generation, but not to increased fibrinolysis.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	292-300
11390981-0	2001	Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode alpha 1,4- N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/ heparin biosynthesis.	Heparin	159-166	exostosin like glycosyltransferase 1	Homo sapiens	47-52
11390981-1	2001	The tumor suppressors EXT1 and EXT2 are associated with hereditary multiple exostoses and encode bifunctional glycosyltransferases essential for chain polymerization of heparan sulfate (HS) and its analog, heparin (Hep).	Heparin	206-213	exostosin glycosyltransferase 2	Homo sapiens	31-35
11390981-1	2001	The tumor suppressors EXT1 and EXT2 are associated with hereditary multiple exostoses and encode bifunctional glycosyltransferases essential for chain polymerization of heparan sulfate (HS) and its analog, heparin (Hep).	Heparin	215-218	exostosin glycosyltransferase 2	Homo sapiens	31-35
11294849-0	2001	Molecular basis for the susceptibility of fibrin-bound thrombin to inactivation by heparin cofactor ii in the presence of dermatan sulfate but not heparin.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	55-63
11294849-1	2001	Although fibrin-bound thrombin is resistant to inactivation by heparin.antithrombin and heparin.heparin cofactor II complexes, indirect studies in plasma systems suggest that the dermatan sulfate.heparin cofactor II complex can inhibit fibrin-bound thrombin.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	22-30
11294849-2	2001	Herein we demonstrate that fibrin monomer produces a 240-fold decrease in the heparin-catalyzed rate of thrombin inhibition by heparin cofactor II but reduces the dermatan sulfate-catalyzed rate only 3-fold.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	104-112
11434701-1	2001	Heparin-induced thrombocytopenia (HIT) is a hypercoagulable syndrome strongly associated with thrombosis that is usually treated with drugs that inhibit factor Xa (danaparoid) or thrombin (lepirudin).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	179-187
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	31-39
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	125-133
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	125-133
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	31-39
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	125-133
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	125-133
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	31-39
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	125-133
11294849-3	2001	The protection of fibrin-bound thrombin from inhibition by heparin.heparin cofactor II reflects heparin-mediated bridging of thrombin to fibrin that results in the formation of a ternary heparin.thrombin.fibrin complex.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	125-133
11294849-4	2001	This complex, formed as a result of three binary interactions (thrombin.fibrin, thrombin.heparin, and heparin.fibrin), limits accessibility of heparin-catalyzed inhibitors to thrombin and induces conformational changes at the active site of the enzyme.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	63-71
11294849-4	2001	This complex, formed as a result of three binary interactions (thrombin.fibrin, thrombin.heparin, and heparin.fibrin), limits accessibility of heparin-catalyzed inhibitors to thrombin and induces conformational changes at the active site of the enzyme.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	80-88
11294849-4	2001	This complex, formed as a result of three binary interactions (thrombin.fibrin, thrombin.heparin, and heparin.fibrin), limits accessibility of heparin-catalyzed inhibitors to thrombin and induces conformational changes at the active site of the enzyme.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	80-88
11294849-10	2001	This study explains why fibrin-bound thrombin is susceptible to inactivation by heparin cofactor II in the presence of dermatan sulfate but not heparin.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	37-45
12769663-1	2001	Thrombin-specific inhibitors directly diminish thrombin-induced coagulation and cellular activities without the side effects of heparin.	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	0-8
11406199-9	2001	NT-evoked current was blocked after the internal perfusion of heparin, an IP(3) receptor antagonist, or BAPTA, a fast Ca(2+) chelator.	Heparin	62-69	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	74-88
11378658-12	2001	Thus, a major mechanism of heparin action in cancer may be inhibition of P-selectin-mediated platelet coating of tumor cells during the initial phase of the metastatic process.	Heparin	27-34	selectin, platelet	Mus musculus	73-83
11278319-2	2001	In the presence of heparin-like molecules, both receptors also function as receptors for the heparin-binding 165-amino acid isoform of vascular endothelial growth factor (VEGF(165)).	Heparin	19-26	vascular endothelial growth factor A	Homo sapiens	135-169
11278319-2	2001	In the presence of heparin-like molecules, both receptors also function as receptors for the heparin-binding 165-amino acid isoform of vascular endothelial growth factor (VEGF(165)).	Heparin	19-26	vascular endothelial growth factor A	Homo sapiens	171-175
11689113-3	2001	FGF-2 (basic FGF) requires a cooperative interaction with heparin or heparan sulfate proteoglycans in order to form functional growth factor-receptor complexes that are essential for receptor binding and activation.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	0-5
11350054-2	2001	Here, using covalent affinity crosslinking of radiolabeled FGF7 to binary complexes of FGFR2IIIb and heparin, we show that two molecules of FGF7 contact each FGFR2IIIb.	Heparin	101-108	fibroblast growth factor 7	Homo sapiens	59-63
11371192-5	2001	Our results indicate that the heparin binding site, defined as the 40s loop, is only marginally involved in CCR5 binding and activation, but largely overlaps the CCR1 and CCR3 binding and activation domain in RANTES.	Heparin	30-37	C-C chemokine receptor type 3	Cricetulus griseus	171-175
11350054-2	2001	Here, using covalent affinity crosslinking of radiolabeled FGF7 to binary complexes of FGFR2IIIb and heparin, we show that two molecules of FGF7 contact each FGFR2IIIb.	Heparin	101-108	fibroblast growth factor 7	Homo sapiens	140-144
11350927-6	2001	Both GD and Snk bind to heparin-Sepharose, providing a link between the pipe-defined ventral prepattern and the protease cascade.	Heparin	24-31	snake	Drosophila melanogaster	12-15
11336503-6	2001	This factor binds heparin with high affinity and increases delta-crystallin expression in an ERK-insensitive manner, properties consistent with an FGF but not insulin or IGF.	Heparin	18-25	fibroblast growth factor 10	Gallus gallus	147-150
11278930-0	2001	Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	40-48
11389993-1	2001	The aim of this study is to develop a heparin/protamine-based prodrug system for the controlled delivery of enzyme such as tissue-type plasminogen activator (tPA).	Heparin	38-45	plasminogen activator, tissue type	Homo sapiens	123-156
11278641-0	2001	Identification and characterization of a conformational heparin-binding site involving two fibronectin type III modules of bovine tenascin-X.	Heparin	56-63	tenascin XB	Bos taurus	130-140
11278641-1	2001	Tenascin-X is known as a heparin-binding molecule, but the localization of the heparin-binding site has not been investigated until now.	Heparin	25-32	tenascin XB	Bos taurus	0-10
11278641-1	2001	Tenascin-X is known as a heparin-binding molecule, but the localization of the heparin-binding site has not been investigated until now.	Heparin	79-86	tenascin XB	Bos taurus	0-10
11278930-2	2001	Heparin activates the primary serpin inhibitor of blood clotting proteinases, antithrombin, both by an allosteric conformational change mechanism that specifically enhances factor Xa inactivation and by a ternary complex bridging mechanism that promotes the inactivation of thrombin and other target proteinases.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	82-90
11358513-7	2001	Heparin, but not other glycosaminoglycans, enhanced dramatically the ability of hK3 but not hK2 to degrade IGFBP-3 and IGFBP-4.	Heparin	0-7	keratin 3	Homo sapiens	80-83
11855056-2	2001	In the second variant of this condition, high doses of proteinase inhibitors in combination with minimum heparin doses are the most rational.	Heparin	105-112	endogenous retrovirus group K member 25	Homo sapiens	55-65
11322862-3	2001	At present there is only limited clinical use of some parenteral preparations of thrombin inhibitors in acute situations, especially when the common antithrombotic drugs heparin, warfarin and aspirin are ineffective or associated with side effects.	Heparin	170-177	coagulation factor II, thrombin	Homo sapiens	81-89
11358517-1	2001	Recombinant human procollagen C-proteinase enhancer (rPCPE) was expressed using a baculovirus system and purified to homogeneity using a three-step procedure including heparin affinity chromatography.	Heparin	168-175	procollagen C-endopeptidase enhancer	Rattus norvegicus	53-58
11975790-0	2001	Argatroban: a direct thrombin inhibitor for heparin-induced thrombocytopenia and other clinical applications.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	21-29
11925507-3	2001	MK-induced migration of peritoneal exudate macrophages was inhibited by heparin, chondroitin sulfate E and dermatan sulfate, but not by chondroitin sulfate D or chondroitin 6-sulfate.	Heparin	72-79	midkine	Homo sapiens	0-2
11465671-6	2001	The suppression of T cell proliferation and the enhancement of IL-10 secretion with soluble TSP-1 was inhibited byadding RGDS peptide or heparin.	Heparin	137-144	thrombospondin 1	Homo sapiens	92-97
11369420-1	2001	It is known that a low-molecular-weight heparin (LMWH) is more effective than unfractionated heparin in unstable angina/non-Q-wave myocardial infarction (UA/NQMI) and the platelet GPIIb/IIIa receptors play an important role in acute myocardial infarction (AMI).	Heparin	40-47	integrin subunit alpha 2b	Canis lupus familiaris	180-185
11344214-3	2001	The interaction of IGFBP-3 with FN and the 40-kDa heparin-binding carboxyl-terminal fragment of FN was confirmed using Western ligand blotting.	Heparin	50-57	fibronectin 1	Homo sapiens	96-98
11344214-6	2001	Competitive inhibition of IGFBP-3 binding to FN was observed in the presence of IGFBP-5 and heparin.	Heparin	92-99	fibronectin 1	Homo sapiens	45-47
11312151-10	2001	Finally, GC responsiveness to IGF-I and FSH, in terms of proliferation and steroidogenesis, was generally maintained when cells were grown on ECM components, RGD peptides and in the presence of heparin.	Heparin	194-201	insulin like growth factor 1	Homo sapiens	30-35
11322758-5	2001	Site-directed mutagenesis, replacing this sequence with the corresponding residues from ErbB-1, resulted in complete loss of heparin binding activity of the chimeric receptor.	Heparin	125-132	epidermal growth factor receptor	Homo sapiens	88-94
11296226-0	2001	p53 induction of heparin-binding EGF-like growth factor counteracts p53 growth suppression through activation of MAPK and PI3K/Akt signaling cascades.	Heparin	17-24	tumor protein p53	Homo sapiens	0-3
11290592-3	2001	There are conflicting results as to whether anticoagulant heparins can catalyze the antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged membrane surfaces, and calcium ion), which is the physiologically relevant form of the proteinase responsible for the activation of prothrombin to thrombin during the blood coagulation process.	Heparin	58-66	coagulation factor II, thrombin	Homo sapiens	128-139
11296226-0	2001	p53 induction of heparin-binding EGF-like growth factor counteracts p53 growth suppression through activation of MAPK and PI3K/Akt signaling cascades.	Heparin	17-24	tumor protein p53	Homo sapiens	68-71
11290592-3	2001	There are conflicting results as to whether anticoagulant heparins can catalyze the antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged membrane surfaces, and calcium ion), which is the physiologically relevant form of the proteinase responsible for the activation of prothrombin to thrombin during the blood coagulation process.	Heparin	58-66	coagulation factor II, thrombin	Homo sapiens	88-96
11296226-0	2001	p53 induction of heparin-binding EGF-like growth factor counteracts p53 growth suppression through activation of MAPK and PI3K/Akt signaling cascades.	Heparin	17-24	AKT serine/threonine kinase 1	Homo sapiens	127-130
11290592-4	2001	In this study, a novel assay system was developed to compare the catalytic effect of different molecular-weight heparins in the antithrombin inhibition of factor Xa, either in free form or assembled into the prothrombinase complex during the process of prothrombin activation.	Heparin	112-120	coagulation factor II, thrombin	Homo sapiens	208-219
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	3-11
11290592-5	2001	This assay takes advantage of the unique property of a recombinant mutant antithrombin, which, similar to the wild-type antithrombin, rapidly inhibits factor Xa, but not thrombin, in the presence of heparin.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	78-86
11134040-12	2001	In addition, FGFR3DeltaAB responds to FGF1 at lower concentrations of heparin than FGFR3 does.	Heparin	70-77	fibroblast growth factor 1	Mus musculus	38-42
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	von Willebrand factor	Homo sapiens	250-271
11154699-0	2001	Glucose and insulin stimulate heparin-releasable lipoprotein lipase activity in mouse islets and INS-1 cells.	Heparin	30-37	lipoprotein lipase	Rattus norvegicus	49-67
11154699-5	2001	Acute exposure of beta-cells to physiological concentrations of glucose stimulated both total cellular LpL activity and heparin-releasable LpL activity.	Heparin	120-127	lipoprotein lipase	Rattus norvegicus	139-142
11154699-7	2001	The induction of heparin-releasable LpL activity was unaffected by treatment with diazoxide, an inhibitor of insulin exocytosis that does not alter glucose metabolism but was blocked by conditions that inhibit glucose metabolism.	Heparin	17-24	lipoprotein lipase	Rattus norvegicus	36-39
11154699-10	2001	LpL was also detected at the cell surface and was displaced from this site by heparin in dispersed islets and INS-1 cells.	Heparin	78-85	lipoprotein lipase	Rattus norvegicus	0-3
11118430-5	2001	To determine the mechanism by which hVPLA(2) interacts with cell membranes to induce leukotriene formation, we mutated surface cationic residues and a catalytic residue of hVPLA(2) and measured the interactions of mutants with model membranes, immobilized heparin, and human neutrophils.	Heparin	256-263	phospholipase A2 group V	Homo sapiens	36-44
11118430-7	2001	Additionally, hVPLA(2) binds heparin with high affinity and has a well defined heparin-binding site.	Heparin	29-36	phospholipase A2 group V	Homo sapiens	14-22
11118430-7	2001	Additionally, hVPLA(2) binds heparin with high affinity and has a well defined heparin-binding site.	Heparin	79-86	phospholipase A2 group V	Homo sapiens	14-22
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	von Willebrand factor	Homo sapiens	273-276
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	coagulation factor II, thrombin	Homo sapiens	3-11
11259264-1	2001	Using a variety of approaches, we have examined the expression of the heparin/heparan sulfate (Hp/HS) interacting protein/ribosomal protein L29 (HIP/RPL29) in mouse uteri during the estrous cycle and early pregnancy.	Heparin	70-77	predicted gene 13841	Mus musculus	122-143
11298735-0	2001	The oxidative mechanism of heparin interferes with radical production by glucose and reduces the degree of glycooxidative modifications on human serum albumin.	Heparin	27-34	albumin	Homo sapiens	145-158
11285600-0	2001	From confusion to clarity: Direct thrombin inhibitors for patients with heparin-induced thrombocytopenia.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	34-42
11298735-6	2001	The effects of heparin were dependent on its specific binding to HSA, which triggered an oxidative mechanism strikingly different from that caused by glucose.	Heparin	15-22	albumin	Homo sapiens	65-68
11298735-7	2001	In the presence of heparin, only the radical species catalyzed by heparin was detected across all samples of glycated HSA, irrespective of glucose concentration.	Heparin	19-26	albumin	Homo sapiens	118-121
11298735-7	2001	In the presence of heparin, only the radical species catalyzed by heparin was detected across all samples of glycated HSA, irrespective of glucose concentration.	Heparin	66-73	albumin	Homo sapiens	118-121
11298735-9	2001	The results demonstrate that the oxidative mechanism sustained by heparin mediates biological effects that may be beneficial in reducing the extent of glycooxidative damage on HSA.	Heparin	66-73	albumin	Homo sapiens	176-179
11024046-10	2001	Finally, we demonstrated that low molecular weight heparin (which binds to thrombin exosite II) but not hirugen (residues 54-65 of hirudin, which binds to exosite I of thrombin) inhibited thrombin binding to GPIb alpha.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	75-83
11599124-10	2001	These results indicate that heparin and HS inhibited ET-1-induced ERK activation, resulting in suppression of Elk-1 phosphorylation, and lead to inhibition of c-fos gene expression through SRF-independent manner.	Heparin	28-35	endothelin 1	Rattus norvegicus	53-57
11599124-10	2001	These results indicate that heparin and HS inhibited ET-1-induced ERK activation, resulting in suppression of Elk-1 phosphorylation, and lead to inhibition of c-fos gene expression through SRF-independent manner.	Heparin	28-35	Eph receptor B1	Rattus norvegicus	66-69
11599124-11	2001	Moreover, heparin and HS inhibited ET-1-induced [3H] leucine incorporation.	Heparin	10-17	endothelin 1	Rattus norvegicus	35-39
11599124-12	2001	These results suggest that heparin and HS inhibit ET-1 induced myocardial cell hypertrophy through the inhibition of gene expression and protein synthesis.	Heparin	27-34	endothelin 1	Rattus norvegicus	50-54
11599124-0	2001	Heparin and heparan sulfate inhibit extracellular signal-regulated kinase activation and myocardial cell hypertrophy induced by endothelin-1.	Heparin	0-7	Eph receptor B1	Rattus norvegicus	36-73
11599124-0	2001	Heparin and heparan sulfate inhibit extracellular signal-regulated kinase activation and myocardial cell hypertrophy induced by endothelin-1.	Heparin	0-7	endothelin 1	Rattus norvegicus	128-140
11599124-3	2001	We examined the intracellular signal mechanisms linking to the inhibitory effects of heparin and HS on endothelin-1 (ET-1)-induced hypertrophy in cultured rat neonatal myocardial cells (MCs).	Heparin	85-92	endothelin 1	Rattus norvegicus	103-115
11599124-3	2001	We examined the intracellular signal mechanisms linking to the inhibitory effects of heparin and HS on endothelin-1 (ET-1)-induced hypertrophy in cultured rat neonatal myocardial cells (MCs).	Heparin	85-92	endothelin 1	Rattus norvegicus	117-121
11599124-4	2001	Heparin inhibited ET-1-induced c-fos mRNA expression.	Heparin	0-7	endothelin 1	Rattus norvegicus	18-22
11599124-5	2001	Heparin and HS inhibited ET-1-induced activation of c-fos promoter/enhancer in MCs.	Heparin	0-7	endothelin 1	Rattus norvegicus	25-29
11599124-6	2001	Although heparin and HS inhibited ET-1-induced activation of the wild-type c-fos serum response element (SRE), the activation of a mutated c-fos SRE that contains an intact binding site for the serum response factor (SRF) but lacks the ternary complex factor (TCF) binding site, was not inhibited.	Heparin	9-16	endothelin 1	Rattus norvegicus	34-38
11599124-9	2001	Furthermore, heparin and HS inhibited ET-1-induced activation of extracellular signal-regulated kinase (ERK) and phosphorylation of Elk-1, which is one of the TCFs.	Heparin	13-20	endothelin 1	Rattus norvegicus	38-42
11599124-9	2001	Furthermore, heparin and HS inhibited ET-1-induced activation of extracellular signal-regulated kinase (ERK) and phosphorylation of Elk-1, which is one of the TCFs.	Heparin	13-20	Eph receptor B1	Rattus norvegicus	65-102
11599124-9	2001	Furthermore, heparin and HS inhibited ET-1-induced activation of extracellular signal-regulated kinase (ERK) and phosphorylation of Elk-1, which is one of the TCFs.	Heparin	13-20	Eph receptor B1	Rattus norvegicus	104-107
12577350-4	2001	In the heparin group, level of PT and APTT prolonged, FIB decreased, t-PA activity elevated and PAI activity lowered, and APC unchanged.	Heparin	7-14	fibrinogen beta chain	Homo sapiens	54-57
12577350-4	2001	In the heparin group, level of PT and APTT prolonged, FIB decreased, t-PA activity elevated and PAI activity lowered, and APC unchanged.	Heparin	7-14	plasminogen activator, tissue type	Homo sapiens	69-73
11264008-1	2001	HARP (heparin affin regulatory peptide) is a growth factor displaying high affinity for heparin.	Heparin	6-13	pleiotrophin	Homo sapiens	0-4
11248082-4	2001	Here, we bring together all these unexplained and seemingly disparate observations, showing that heparin treatment attenuates tumor metastasis in mice by inhibiting P-selectin-mediated interactions of platelets with carcinoma cell-surface mucin ligands.	Heparin	97-104	selectin, platelet	Mus musculus	165-175
11258893-0	2001	Interaction of the N-terminal domain of apolipoprotein E4 with heparin.	Heparin	63-70	apolipoprotein E	Homo sapiens	40-57
11258893-5	2001	Here we report our studies of the interaction of the N-terminal domain of apoE4 (residues 1-191), which contains the major heparin-binding site, with an enzymatically prepared heparin oligosaccharide.	Heparin	123-130	apolipoprotein E	Homo sapiens	74-79
11258893-7	2001	Kinetic analysis of the interaction between the N-terminal apoE4 fragment and immobilized heparin by surface plasmon resonance yielded a K(d) of 150 nM.	Heparin	90-97	apolipoprotein E	Homo sapiens	59-64
11223430-0	2001	Chymase bound to heparin is resistant to its natural inhibitors and capable of proteolyzing high density lipoproteins in aortic intimal fluid.	Heparin	17-24	chymase 1	Homo sapiens	0-7
11255277-0	2001	Low molecular weight heparins prevent thrombin-induced thrombo-embolism in mice despite low anti-thrombin activity.	Heparin	21-29	coagulation factor II	Mus musculus	38-46
11269422-4	2001	Thrombocytopenia and a femoral artery thrombosis after 9 days of heparin exposure marked the development of heparin-induced thrombocytopenia and thrombosis that was successfully managed with argatroban, a direct thrombin inhibitor anticoagulant.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	212-220
11269422-4	2001	Thrombocytopenia and a femoral artery thrombosis after 9 days of heparin exposure marked the development of heparin-induced thrombocytopenia and thrombosis that was successfully managed with argatroban, a direct thrombin inhibitor anticoagulant.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	212-220
11255277-11	2001	At comparable antithrombotic dosages, the anti IIa activity generated in plasma (assessed by TcT) was highest with UFH, intermediate with tinzaparin and very low with reviparin.	Heparin	115-118	ATPase, class II, type 9A	Mus musculus	47-50
11255277-12	2001	Accordingly, the fibrinogen drop, which is caused mainly by the injected thrombin, was prevented by the heparins to an extent that was fairly well related to their anti IIa activity.	Heparin	104-112	coagulation factor II	Mus musculus	73-81
11255277-12	2001	Accordingly, the fibrinogen drop, which is caused mainly by the injected thrombin, was prevented by the heparins to an extent that was fairly well related to their anti IIa activity.	Heparin	104-112	ATPase, class II, type 9A	Mus musculus	169-172
11241131-4	2001	Heparin"s effect on fibrinogen binding to platelets was measured with a radioligand-binding assay.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	20-30
11181800-4	2001	Recessive type III HLP is caused by apoE2 (Arg(158) Cys), a mutant with diminished low-density lipoprotein (LDL) receptor binding but halfnormal heparin binding.	Heparin	145-152	apolipoprotein E	Homo sapiens	36-41
11181800-9	2001	Heparin-binding activities were 53%, 23%, and 66%, respectively, of apoE3.	Heparin	0-7	apolipoprotein E	Homo sapiens	68-73
11181800-11	2001	ApoE2 Sendai (Arg(145) Pro) represents the only known mutation within the heparin-binding domain of apoE (residues 142 through 147), revealing diminished receptor binding and almost normal heparin binding.	Heparin	74-81	apolipoprotein E	Homo sapiens	0-5
11181800-11	2001	ApoE2 Sendai (Arg(145) Pro) represents the only known mutation within the heparin-binding domain of apoE (residues 142 through 147), revealing diminished receptor binding and almost normal heparin binding.	Heparin	74-81	apolipoprotein E	Homo sapiens	100-104
11181800-11	2001	ApoE2 Sendai (Arg(145) Pro) represents the only known mutation within the heparin-binding domain of apoE (residues 142 through 147), revealing diminished receptor binding and almost normal heparin binding.	Heparin	189-196	apolipoprotein E	Homo sapiens	0-5
11241127-1	2001	OBJECTIVE: Cardiovascular tissue engineering approaches to vessel wall restoration have focused on the potent but relatively nonspecific and heparin-dependent mesenchymal cell mitogen fibroblast growth factor 1 (FGF-1).	Heparin	141-148	fibroblast growth factor 1	Homo sapiens	184-210
11241131-8	2001	Low concentrations of unfractionated porcine mucosal heparin (2-5 U/mL) significantly increased fibrinogen I 125 binding to activated platelets, whereas higher doses did not.	Heparin	53-60	fibrinogen beta chain	Homo sapiens	96-106
11241127-1	2001	OBJECTIVE: Cardiovascular tissue engineering approaches to vessel wall restoration have focused on the potent but relatively nonspecific and heparin-dependent mesenchymal cell mitogen fibroblast growth factor 1 (FGF-1).	Heparin	141-148	fibroblast growth factor 1	Homo sapiens	212-217
11241131-9	2001	Heparin-mediated platelet aggregation was completely blocked by GRGDS peptide (5 mmol/L), a competitive inhibitor of fibrinogen binding, and was blocked by EDTA (2 mmol/L), which dissociates the functional integrin complex.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	117-127
11241127-7	2001	RESULTS: In the presence of heparin the HB-GAM/FGF-1 chimera stimulated less SMC proliferation than did the wild-type FGF-1 with a median effective dose of approximately 0.3 nmol versus approximately 0.1 nmol (P &lt;.001).	Heparin	28-35	pleiotrophin	Homo sapiens	40-46
11087757-2	2001	We report the cloning and partial characterization of the fourth member of the vertebrate heparan sulfate/heparin: GlcNAc N-deacetylase/GlcN N-sulfotransferase family, which we designate NDST4.	Heparin	106-113	N-deacetylase/N-sulfotransferase (heparin glucosaminyl) 4	Mus musculus	187-192
11241127-7	2001	RESULTS: In the presence of heparin the HB-GAM/FGF-1 chimera stimulated less SMC proliferation than did the wild-type FGF-1 with a median effective dose of approximately 0.3 nmol versus approximately 0.1 nmol (P &lt;.001).	Heparin	28-35	fibroblast growth factor 1	Homo sapiens	47-52
11241127-11	2001	CONCLUSIONS: The HB-GAM/FGF-1 chimera displays significantly greater and uniquely heparin-independent mitogenic activity for both cell types, and in the presence of heparin it displays a significantly greater EC specificity.	Heparin	82-89	pleiotrophin	Homo sapiens	17-23
11241127-11	2001	CONCLUSIONS: The HB-GAM/FGF-1 chimera displays significantly greater and uniquely heparin-independent mitogenic activity for both cell types, and in the presence of heparin it displays a significantly greater EC specificity.	Heparin	82-89	fibroblast growth factor 1	Homo sapiens	24-29
11241127-11	2001	CONCLUSIONS: The HB-GAM/FGF-1 chimera displays significantly greater and uniquely heparin-independent mitogenic activity for both cell types, and in the presence of heparin it displays a significantly greater EC specificity.	Heparin	165-172	pleiotrophin	Homo sapiens	17-23
11157673-9	2001	In cells microinjected with a low dose of heparin, VP-induced CCE was more susceptible than IICR to mild inhibition of both IP(3)R(1) and IP(3)R(3).	Heparin	42-49	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	138-146
11094060-4	2001	Soluble TSP bound to and induced aggregation of Fg-coated beads dose-dependently, which could be blocked by the amino-terminal heparin-binding domain of TSP, TSP18.	Heparin	127-134	thrombospondin 1	Homo sapiens	8-11
11094060-4	2001	Soluble TSP bound to and induced aggregation of Fg-coated beads dose-dependently, which could be blocked by the amino-terminal heparin-binding domain of TSP, TSP18.	Heparin	127-134	thrombospondin 1	Homo sapiens	153-156
11084032-9	2001	3) An oligonucleotide DNA aptamer, HD22, which binds to the thrombin heparin-binding site (HBS) and inhibits thrombin interaction with GpIbalpha, reduced the apparent k(cat)/K(m) value by about 5-fold.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	60-68
11084032-9	2001	3) An oligonucleotide DNA aptamer, HD22, which binds to the thrombin heparin-binding site (HBS) and inhibits thrombin interaction with GpIbalpha, reduced the apparent k(cat)/K(m) value by about 5-fold.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	109-117
11058594-6	2001	VEGF lacking the heparin binding domain was also able to potentiate TF expression, indicating that heparin-sulfate proteoglycan or neuropilin binding is not required for TF up-regulation.	Heparin	17-24	vascular endothelial growth factor A	Homo sapiens	0-4
11171786-5	2001	EC-SOD activity was determined after release from endothelium by heparin bolus injection.	Heparin	65-72	superoxide dismutase 3	Homo sapiens	0-6
11217091-0	2001	Heparin-Affinity of human extracellular-superoxide dismutase in the brain.	Heparin	0-7	superoxide dismutase 3	Homo sapiens	26-60
11217091-2	2001	The C-terminal portion of EC-SOD is responsible for the heparin-affinity of this enzyme, but this portion should be a target of proteinases.	Heparin	56-63	superoxide dismutase 3	Homo sapiens	26-32
11217091-5	2001	It has been speculated that the heparin-binding domain of EC-SOD in the brain is sensitive to proteolysis, which may result in a loss of extracellular immunoreactivity.	Heparin	32-39	superoxide dismutase 3	Homo sapiens	58-64
11217091-6	2001	This study was performed to investigate the heparin-affinity of EC-SOD in the human brain.	Heparin	44-51	superoxide dismutase 3	Homo sapiens	64-70
11217091-7	2001	We found that human EC-SOD in brain tissue has high heparin-affinity similar to that in the umbilical cord.	Heparin	52-59	superoxide dismutase 3	Homo sapiens	20-26
11217091-8	2001	Moreover, heparin-affinity of EC-SOD in brain homogenate was not decreased by incubation at 37 degrees C for 72 h. The proteolytic activity in brain homogenate might be less than that in umbilical cord homogenates.	Heparin	10-17	superoxide dismutase 3	Homo sapiens	30-36
11159885-0	2001	Disaccharides derived from heparin or heparan sulfate regulate IL-8 and IL-1 beta secretion by intestinal epithelial cells.	Heparin	27-34	C-X-C motif chemokine ligand 8	Homo sapiens	63-67
11159885-0	2001	Disaccharides derived from heparin or heparan sulfate regulate IL-8 and IL-1 beta secretion by intestinal epithelial cells.	Heparin	27-34	interleukin 1 beta	Homo sapiens	72-81
11159885-5	2001	METHODS: Spontaneous and tumor necrosis factor (TNF)-alpha-stimulated interleukin (IL)-8 and IL-1 beta secretion and mRNA expression were assessed in HT-29 and Caco-2 intestinal epithelial cell lines in the presence of a panel of heparin and heparan sulfate disaccharides.	Heparin	230-237	tumor necrosis factor	Homo sapiens	25-58
11160850-7	2001	In C2C12 myocytes, LG268 suppresses the level of cell surface (i.e., heparin-releasable) LPL activity without altering LPL mRNA.	Heparin	69-76	lipoprotein lipase	Rattus norvegicus	89-92
11246004-0	2001	Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants.	Heparin	26-33	fibronectin 1	Homo sapiens	92-103
11246004-0	2001	Identification of a novel heparin-binding site in the alternatively spliced IIICS region of fibronectin: roles of integrins and proteoglycans in cell adhesion to fibronectin splice variants.	Heparin	26-33	fibronectin 1	Homo sapiens	162-173
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	19-27
11244311-0	2001	Low molecular weight heparin reduces proteinuria and modulates glomerular TNF-alpha production in the early phase of adriamycin nephropathy.	Heparin	21-28	tumor necrosis factor	Rattus norvegicus	74-83
11806242-4	2001	While small amounts of VEGF183 were secreted into the conditioned media (CM) of 293 cells expressing VEGF183 (293-VEGF183 cells), most of the VEGF183 remained cell surface-bound and could be released into the CM following treatment with plasmin or heparin.	Heparin	248-255	vascular endothelial growth factor A	Homo sapiens	23-27
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	46-54
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	19-27
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	46-54
11936877-1	2001	Heparin affin regulatory peptide (HARP) also named pleiotrophin (PTN) is a polypeptide that belongs to a family of heparin-binding molecules.	Heparin	115-122	pleiotrophin	Homo sapiens	0-32
11288878-2	2001	To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics, which structurally are very similar to the genuine polysaccharide.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	38-46
11936877-1	2001	Heparin affin regulatory peptide (HARP) also named pleiotrophin (PTN) is a polypeptide that belongs to a family of heparin-binding molecules.	Heparin	115-122	pleiotrophin	Homo sapiens	34-38
11936877-1	2001	Heparin affin regulatory peptide (HARP) also named pleiotrophin (PTN) is a polypeptide that belongs to a family of heparin-binding molecules.	Heparin	115-122	pleiotrophin	Homo sapiens	51-63
11135081-17	2001	The binding of pIgA1 to HMCs was decreased by preincubation with heparin.	Heparin	65-72	MKKS centrosomal shuttling protein	Homo sapiens	24-28
11936877-1	2001	Heparin affin regulatory peptide (HARP) also named pleiotrophin (PTN) is a polypeptide that belongs to a family of heparin-binding molecules.	Heparin	115-122	pleiotrophin	Homo sapiens	65-68
11455580-1	2001	Using recombinant fibronectin proteins containing the V region and two point mutations in the high-affinity heparin-binding domain, we previously showed that these domains modulate tumor cell invasion as well as proteinase expression and apoptosis in human fibroblasts.	Heparin	108-115	fibronectin 1	Homo sapiens	18-29
11455580-7	2001	These models suggest that the two point mutations in the heparin-binding domain of fibronectin III-13 alter cell function probably through changes in charge and not through changes in the conformational structure of the cationic cradle.	Heparin	57-64	fibronectin 1	Homo sapiens	83-94
11436205-4	2001	To demonstrate that the comparative kinetic RT/PCR strategy-which uses a housekeeping gene as internal standard-is a quantitative method to detect significant differences in mRNA levels between different samples, the inhibitory effect of heparin on phorbol 12-myristate 13-acetate (PMA)-induced-TGF-beta1 mRNA expression was evaluated by RT/PCR and RPA, the standard method of mRNA quantification, and the results were compared.	Heparin	238-245	transforming growth factor beta 1	Homo sapiens	295-304
11150552-6	2001	As vitronectin and fibronectin each bind to heparin, these molecules are removed first and the heparin-Sepharose depletion occurs last in the sequence.	Heparin	44-51	fibronectin 1	Homo sapiens	19-30
11150552-6	2001	As vitronectin and fibronectin each bind to heparin, these molecules are removed first and the heparin-Sepharose depletion occurs last in the sequence.	Heparin	95-102	fibronectin 1	Homo sapiens	19-30
11135070-2	2001	While the heparin-releasable lipoprotein lipase (LpL) pool in NAR and in NS is similar, TG levels are significantly greater in NS, suggesting that factors other than reduced LpL alone act in NS but not in NARs.	Heparin	10-17	lipoprotein lipase	Rattus norvegicus	49-52
11770031-10	2001	Using heparin-coated circuits in group 3 led to IL-10 upregulation (P &lt; 0.05) and IL-6 suppression (P &lt; 0.05).	Heparin	6-13	interleukin 6	Homo sapiens	85-89
11192304-12	2001	As thrombin generation decreases, the ACT-heparin dose response curve is warped, resulting in a dose response curve resembling a PTT-heparin dose response curve.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	3-11
11192304-12	2001	As thrombin generation decreases, the ACT-heparin dose response curve is warped, resulting in a dose response curve resembling a PTT-heparin dose response curve.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	3-11
11680695-5	2001	To evaluate the effect of ChM-I on ectopic bone formation, guanidine extracts of demineralized bone matrix were mixed with the ChM-I-bound heparin-Sepharose beads and were implanted onto the fasciae of back muscle of 6-week old nude mice.	Heparin	139-146	chondromodulin	Mus musculus	127-132
11124973-7	2000	Ruthenium red (50 microm) and, to a lesser extent, heparin (3 mg/ml) antagonized IL-1beta-induced Ca(2+) release, and both compounds administered together completely abolished this response.	Heparin	51-58	interleukin 1 beta	Homo sapiens	81-89
11113458-4	2000	Furthermore, binding of EC-SOD to heparin immobilized on plates was decreased with homocysteine.	Heparin	34-41	superoxide dismutase 3	Homo sapiens	24-30
11215510-3	2000	SeP binds to heparin and cell membranes, and is associated with endothelial cells.	Heparin	13-20	selenoprotein P	Homo sapiens	0-3
11101304-1	2000	The effect of heparin on the conformation and stability of triple-helical peptide models of the collagen tail of asymmetric acetylcholinesterase expands our understanding of heparin interactions with proteins and presents an opportunity for clarifying the nature of binding of ligands to collagen triple-helix domains.	Heparin	14-21	acetylcholinesterase (Cartwright blood group)	Homo sapiens	124-144
11101304-1	2000	The effect of heparin on the conformation and stability of triple-helical peptide models of the collagen tail of asymmetric acetylcholinesterase expands our understanding of heparin interactions with proteins and presents an opportunity for clarifying the nature of binding of ligands to collagen triple-helix domains.	Heparin	174-181	acetylcholinesterase (Cartwright blood group)	Homo sapiens	124-144
11101304-2	2000	Within the collagen tail of AChE, there are two consensus sequences for heparin binding of the form BBXB, surrounded by additional basic residues.	Heparin	72-79	acetylcholinesterase (Cartwright blood group)	Homo sapiens	28-32
11095655-2	2000	In a rat model of diabetes mellitus-induced glomerulosclerosis, daily administration of a modified heparin (mH) glycosaminoglycan (GAG) preparation with low anticoagulant activity prevented glomerular and tubular matrix accumulation, as well as overexpression of TGF-beta1 mRNA and albuminuria, without obvious side effects.	Heparin	99-106	transforming growth factor, beta 1	Rattus norvegicus	263-272
11067924-1	2000	We establish, using an ELISA approach, that recombinant human and murine IL-6 bind to an immobilized heparin-BSA complex.	Heparin	101-108	interleukin 6	Mus musculus	73-77
11156731-5	2000	Direct thrombin inhibitors, such as bivalirudin and hirudin, overcome many of the limitations of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	7-15
11067924-2	2000	In the case of human IL-6, this binding is displaceable by soluble heparin, IC(50) approximately 2 microg/ml, corresponding to approximately 200 nM.	Heparin	67-74	interleukin 6	Homo sapiens	21-25
11067924-5	2000	The epitopes of five IL-6-specific mAbs were still accessible in heparin-bound IL-6, and the dimer formed from the association of rIL-6 with its truncated soluble receptor polypeptide, srIL-6alpha, still bound to heparin.	Heparin	65-72	interleukin 6	Homo sapiens	21-25
11067924-5	2000	The epitopes of five IL-6-specific mAbs were still accessible in heparin-bound IL-6, and the dimer formed from the association of rIL-6 with its truncated soluble receptor polypeptide, srIL-6alpha, still bound to heparin.	Heparin	65-72	interleukin 6	Homo sapiens	79-83
11067924-5	2000	The epitopes of five IL-6-specific mAbs were still accessible in heparin-bound IL-6, and the dimer formed from the association of rIL-6 with its truncated soluble receptor polypeptide, srIL-6alpha, still bound to heparin.	Heparin	213-220	interleukin 6	Homo sapiens	21-25
11067924-5	2000	The epitopes of five IL-6-specific mAbs were still accessible in heparin-bound IL-6, and the dimer formed from the association of rIL-6 with its truncated soluble receptor polypeptide, srIL-6alpha, still bound to heparin.	Heparin	213-220	interleukin 6	Rattus norvegicus	130-135
11067924-6	2000	Further analysis showed that heparin competed partially and weakly with the binding of srIL-6 to IL-6; however, it competed strongly for the binding of the rIL-6/srIL-6Ralpha dimer, to soluble glycoprotein 130.	Heparin	29-36	interleukin 6	Homo sapiens	89-93
11067924-6	2000	Further analysis showed that heparin competed partially and weakly with the binding of srIL-6 to IL-6; however, it competed strongly for the binding of the rIL-6/srIL-6Ralpha dimer, to soluble glycoprotein 130.	Heparin	29-36	interleukin 6	Rattus norvegicus	88-93
11067924-8	2000	By contrast, heparin was able to protect IL-6 from digestion by the bacterial endoproteinase Lys-C.	Heparin	13-20	interleukin 6	Homo sapiens	41-45
11067924-10	2000	This interaction will tend to retain IL-6 close to its sites of secretion in the tissues by binding to heparin-like glycosaminoglycans, thus favoring a paracrine mode of activity.	Heparin	103-110	interleukin 6	Homo sapiens	37-41
11054819-4	2000	As with secretory rh-chymase, efficient purification was possible by heparin affinity chromatography.	Heparin	69-76	chymase 1	Homo sapiens	21-28
11085545-3	2000	Both UFH and LMWH inhibited bFGF-induced proliferation of human microvascular endothelial cells (hMVECs) to the same the extent (36-60%).	Heparin	5-8	fibroblast growth factor 2	Homo sapiens	28-32
11060016-6	2000	In contrast to hirudin, however, the markedly acidic C-terminal peptide of haemadin does not bind the fibrinogen-recognition exosite, but interacts with the heparin-binding exosite of thrombin.	Heparin	157-164	coagulation factor II, thrombin	Homo sapiens	184-192
11029577-9	2000	Interaction of the substituted peptides with heparin and chondroitin sulfate glycosaminoglycans demonstrate that although electrostatic interactions contribute to binding, nonionic interactions such as hydrogen bonding and van der Waals packing play a role in glycosaminoglycan-induced Abeta folding and aggregation.	Heparin	45-52	amyloid beta precursor protein	Homo sapiens	286-291
11369259-2	2000	Binding of a full-length heparin chain to this site of factor Xa in the presence of calcium makes a significant contribution to acceleration of the proteinase inhibition by antithrombin through a ternary complex bridging or template mechanism.	Heparin	25-32	endogenous retrovirus group K member 25	Homo sapiens	148-158
11087710-1	2000	The interaction of heparan sulfate (HS) (and the closely related molecule heparin) with FGF-1 is a requirement for enabling the growth factor to activate its cell surface tyrosine kinase receptor.	Heparin	74-81	fibroblast growth factor 1	Homo sapiens	88-93
11958287-3	2000	During routine HD with a cuprophane membrane and high molecular weight (HMW) heparin, plasma MPO was rapidly upregulated to maximal levels within 15 min after starting extracorporeal circulation.	Heparin	77-84	myeloperoxidase	Homo sapiens	93-96
11080685-3	2000	The heparin-binding signaling sPLA(2)-IIA, IID and V bind the glycosylphosphatidylinositol-anchored heparan sulfate proteoglycan glypican, which plays a role in sorting of these isozymes into caveolae and perinuclear compartments.	Heparin	4-11	phospholipase A2 group X	Homo sapiens	30-37
11215206-3	2000	The biological functions of this enzyme in vivo were as follows: 1) this enzyme accelerates cancer cell invasion and metastasis though the degradation of vascular basement membrane and extracellular matrix by cancer cells; 2) this enzyme releases and activates heparin-binding growth factors such as bFGF and VEGF from heparan sulfate proteoglycans, and induces angiogenesis; 3) the degradative products of heparan sulfate proteoglycans by this enzyme suppress the biological function of activated T-lymphocytes.	Heparin	261-268	fibroblast growth factor 2	Homo sapiens	300-304
11080685-7	2000	sPLA(2)-X, a heparin-non-binding sPLA(2) isozyme, is capable of releasing AA from intact cells in the absence of cofactors.	Heparin	13-20	phospholipase A2 group X	Homo sapiens	0-9
11080685-7	2000	sPLA(2)-X, a heparin-non-binding sPLA(2) isozyme, is capable of releasing AA from intact cells in the absence of cofactors.	Heparin	13-20	phospholipase A2 group X	Homo sapiens	0-7
10944532-8	2000	However, in chlorate-treated cells, the addition of heparin or purified HSPGs simultaneously with FGF-2 restored DNA synthesis, the sustained phosphorylation of p42/44(MAPK) and p90(RSK), and the degradation of IkappaBalpha and IkappaBbeta.	Heparin	52-59	NFKB inhibitor beta	Rattus norvegicus	228-239
11798537-9	2000	CONCLUSION: TGF-beta1, EGF and bFGF may play an important role in the airway wall and pulmonary arteriole structure remodeling in COPD, the intervention against TGF-beta1 and long term inhalation of heparin mat be helpful for the inhibition of airway wall remodeling in human COPD and worth of further observation.	Heparin	199-206	transforming growth factor beta 1	Homo sapiens	12-21
11798537-9	2000	CONCLUSION: TGF-beta1, EGF and bFGF may play an important role in the airway wall and pulmonary arteriole structure remodeling in COPD, the intervention against TGF-beta1 and long term inhalation of heparin mat be helpful for the inhibition of airway wall remodeling in human COPD and worth of further observation.	Heparin	199-206	fibroblast growth factor 2	Homo sapiens	31-35
11069186-6	2000	The complex is assembled around a central heparin molecule linking two FGF1 ligands into a dimer that bridges between two receptor chains.	Heparin	42-49	fibroblast growth factor 1	Homo sapiens	71-75
11069186-7	2000	The asymmetric heparin binding involves contacts with both FGF1 molecules but only one receptor chain.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	59-63
11069186-8	2000	The structure of the FGF1-FGFR2-heparin ternary complex provides a structural basis for the essential role of heparan sulphate in FGF signalling.	Heparin	32-39	fibroblast growth factor 1	Homo sapiens	21-25
10922378-8	2000	Binding experiments done in the presence of heparin and with altered forms of TFPI suggest that the basic C-terminal region of TFPI is required for TSP-1 binding.	Heparin	44-51	thrombospondin 1	Homo sapiens	148-153
11018553-2	2000	Although beta-NGF does not bind heparin with high affinity, we postulated that a basic domain found at the surface of native beta-NGF could interact with heparin and slow its diffusion from a heparin-containing delivery system.	Heparin	154-161	nerve growth factor	Homo sapiens	125-133
11018553-2	2000	Although beta-NGF does not bind heparin with high affinity, we postulated that a basic domain found at the surface of native beta-NGF could interact with heparin and slow its diffusion from a heparin-containing delivery system.	Heparin	154-161	nerve growth factor	Homo sapiens	125-133
11018553-6	2000	The ability of heparin-containing fibrin matrices, with a high excess of heparin-binding sites, to slow the diffusion-based release of beta-NGF from fibrin matrices was measured in the absence of cells.	Heparin	15-22	nerve growth factor	Homo sapiens	135-143
11018553-6	2000	The ability of heparin-containing fibrin matrices, with a high excess of heparin-binding sites, to slow the diffusion-based release of beta-NGF from fibrin matrices was measured in the absence of cells.	Heparin	73-80	nerve growth factor	Homo sapiens	135-143
11001899-6	2000	Both heparin and low molecular weight heparin block thrombin-induced platelet procoagulant activity, which may account for part of their clinical efficacy.	Heparin	5-12	coagulation factor II, thrombin	Homo sapiens	52-60
11001899-6	2000	Both heparin and low molecular weight heparin block thrombin-induced platelet procoagulant activity, which may account for part of their clinical efficacy.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	52-60
11075902-0	2000	Heparin-free DALI LDL-apheresis in hyperlipidemic patients: efficacy, safety and biocompatibility.	Heparin	0-7	DNMT1-associated long intergenic non-coding RNA	Homo sapiens	13-17
11075902-17	2000	CONCLUSION: In this pilot study, heparin-free DALI apheresis was safe and effective and may thus be performed in LDL-apheresis dependent patients who suffer from heparin intolerance.	Heparin	33-40	DNMT1-associated long intergenic non-coding RNA	Homo sapiens	46-50
11075902-17	2000	CONCLUSION: In this pilot study, heparin-free DALI apheresis was safe and effective and may thus be performed in LDL-apheresis dependent patients who suffer from heparin intolerance.	Heparin	162-169	DNMT1-associated long intergenic non-coding RNA	Homo sapiens	46-50
10992473-4	2000	Fimbrial binding to Fn, HB-GAM, and the 30K and the 40K fragments was inhibited by high concentrations of heparin.	Heparin	106-113	pleiotrophin	Homo sapiens	24-30
11215206-3	2000	The biological functions of this enzyme in vivo were as follows: 1) this enzyme accelerates cancer cell invasion and metastasis though the degradation of vascular basement membrane and extracellular matrix by cancer cells; 2) this enzyme releases and activates heparin-binding growth factors such as bFGF and VEGF from heparan sulfate proteoglycans, and induces angiogenesis; 3) the degradative products of heparan sulfate proteoglycans by this enzyme suppress the biological function of activated T-lymphocytes.	Heparin	261-268	vascular endothelial growth factor A	Homo sapiens	309-313
11039850-3	2000	Synthetic peptides containing a heparin-binding motif and encompassing residues F16-G33 or A74-S95 of TSP1 competed quantitatively with iodine 125-labeled TSP1 for binding to heparinagarose beads.	Heparin	32-39	thrombospondin 1	Homo sapiens	155-159
11129958-9	2000	In the presence of heparin, apo E depleted HDL overcame the testosterone production induced by pravastatin, indicating that uptake of HDL without apo E via a secretion of apo E by the cells themselves was not involved.	Heparin	19-26	apolipoprotein E	Rattus norvegicus	28-33
10896681-7	2000	LpL-mediated LDL selective uptake was not affected by the LpL inhibitor tetrahydrolipstatin but was nearly abolished by heparin, monoclonal anti-LpL antibodies, or chlorate treatment of cells and was not found using proteoglycan-deficient Chinese hamster ovary cells.	Heparin	120-127	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	0-3
10862775-0	2000	Unraveling the amino acid sequence crucial for heparin binding to collagen V. We have previously shown that a recombinant 12-kDa fragment of the collagen alpha1(V) chain (Ile(824)-Pro(950)), referred to as HepV, binds to heparin and heparan sulfate (Delacoux, F., Fichard, A., Geourjon, C., Garrone, R., and Ruggiero, F. (1998) J. Biol.	Heparin	47-54	collagen type V alpha 1 chain	Homo sapiens	154-163
10862775-5	2000	Further evidence for the precise localization of the heparin-binding site was provided by experiments based on the fact that heparin can protect the alpha1(V) chain heparin-binding site from trypsin digestion.	Heparin	125-132	collagen type V alpha 1 chain	Homo sapiens	149-158
10862775-5	2000	Further evidence for the precise localization of the heparin-binding site was provided by experiments based on the fact that heparin can protect the alpha1(V) chain heparin-binding site from trypsin digestion.	Heparin	125-132	collagen type V alpha 1 chain	Homo sapiens	149-158
10862775-5	2000	Further evidence for the precise localization of the heparin-binding site was provided by experiments based on the fact that heparin can protect the alpha1(V) chain heparin-binding site from trypsin digestion.	Heparin	53-60	collagen type V alpha 1 chain	Homo sapiens	149-158
10973863-0	2000	Lower cardiac troponin T and I results in heparin-plasma than in serum.	Heparin	42-49	troponin T2, cardiac type	Homo sapiens	6-24
10893232-0	2000	High and low affinity heparin-binding sites in the G domain of the mouse laminin alpha 4 chain.	Heparin	22-29	laminin, alpha 4	Mus musculus	73-88
10978264-0	2000	In vivo thrombin generation and activity during and after intravenous infusion of heparin or recombinant hirudin in patients with unstable angina pectoris.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	8-16
10978264-1	2000	In patients with unstable angina, intravenous heparin reduces thrombin activity but does not influence thrombin generation.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	62-70
10862775-6	2000	The results parallel the alanine scanning mutagenesis data, i.e. heparin binding to the alpha1(V) chain involved Arg(912), Arg(918), and Arg(921) and two additional neighboring basic residues, Lys(905) and Arg(909).	Heparin	65-72	collagen type V alpha 1 chain	Homo sapiens	88-97
10982508-16	2000	CONCLUSIONS: Children undergoing CPB with heparin dosing adjusted to optimize the ACT manifest inadequate anticoagulation (ongoing thrombin formation).	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	131-139
10816596-2	2000	We show that FGF-induced angiogenesis can be modulated using selectively desulfated heparin.	Heparin	84-91	fibroblast growth factor 10	Gallus gallus	13-16
10980906-4	2000	The low molecular weight heparins have yielded encouraging results in large-scale clinical trials, but it remains unclear whether their benefit stems from a superior pharmacologic profile to unfractionated heparin or is determined by an enhanced ability to suppress thrombin generation (by virtue of a direct anti-Xa effect).	Heparin	25-33	coagulation factor II, thrombin	Homo sapiens	266-274
10980906-4	2000	The low molecular weight heparins have yielded encouraging results in large-scale clinical trials, but it remains unclear whether their benefit stems from a superior pharmacologic profile to unfractionated heparin or is determined by an enhanced ability to suppress thrombin generation (by virtue of a direct anti-Xa effect).	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	266-274
11030473-4	2000	A significant reduction with desirudin compared with heparin in the incidence of death or non-fatal (re)infarction at 24 hours in patients with acute myocardial infarction (MI) was reported in the GUSTO (Global Use of Strategies to Open Occluded Coronary Arteries) IIb trial but not in the TIMI (Thrombolysis and Thrombin Inhibition in Myocardial Infarction) 9B trial.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	313-321
11043400-3	2000	CECs grown in the presence of ECGF and its cofactor heparin exhibit an epithelial-like morphology (type I CECs).	Heparin	52-59	fibroblast growth factor 1	Homo sapiens	30-34
11026623-6	2000	Isolated livers, perfused with heparin-free medium, secreted fully active hepatic lipase to the perfusate.	Heparin	31-38	lipase C, hepatic type	Rattus norvegicus	74-88
11026623-7	2000	The addition of heparin resulted in a rapid and larger release of hepatic lipase to the perfusate.	Heparin	16-23	lipase C, hepatic type	Rattus norvegicus	66-80
10926855-1	2000	The collagen-like tail of asymmetric acetylcholinesterase (AChE) contains two heparin-binding domains (HBDs) that interact with heparan sulphate proteoglycans, determining the anchoring of the enzyme at the basal lamina and its specific localization at the neuromuscular junction.	Heparin	78-85	acetylcholinesterase (Cartwright blood group)	Homo sapiens	59-63
11251332-5	2000	Induction of small platelet aggregates by heparin was inhibited by preincubation with nafamostat mesilate, a synthetic protease inhibitor, and cilostazol, a platelet phosphodiesterase inhibitor, but not by the therapeutic doses of aspirin or argatroban, a selective thrombin inhibitor.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	266-274
10816596-5	2000	The length of the heparin oligomer, minimally an 8/10-mer, was critical for the ability to enhance FGFR-1 kinase activity.	Heparin	18-25	fibroblast growth factor receptor 1	Gallus gallus	99-105
10816596-7	2000	Sulfation at 2-O- and 6-O-positions was moreover a prerequisite for binding of heparin to a lysine-rich peptide corresponding to amino acids 160-177 in the extracellular domain of FGFR-1.	Heparin	79-86	fibroblast growth factor receptor 1	Gallus gallus	180-186
10942794-3	2000	In this study, prothrombin (6.7 mg) was purified from the ascites fluid (1130 mL) of a patient with liver cirrhosis by barium citrate adsorption, ammonium sulfate elution, DEAE Sephacel and Heparin Sepharose CL-6B column chromatography steps.	Heparin	190-197	coagulation factor II, thrombin	Homo sapiens	15-26
10992840-12	2000	Serum S100 protein levels are reduced after using arterial line filtration and covalent-bonded heparin to coat the inner surface of the CPB circuit.	Heparin	95-102	S100 calcium binding protein A1	Homo sapiens	6-10
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	75-82	fibroblast growth factor 2	Homo sapiens	0-26
10959695-8	2000	Incubation of plasma with heparin and protamine in vitro generated complement-CRP complexes, which was blocked by phosphorylcholine and stimulated by exogenous CRP.	Heparin	26-33	C-reactive protein	Homo sapiens	78-81
10959695-8	2000	Incubation of plasma with heparin and protamine in vitro generated complement-CRP complexes, which was blocked by phosphorylcholine and stimulated by exogenous CRP.	Heparin	26-33	C-reactive protein	Homo sapiens	160-163
10959702-5	2000	The antithrombotic activity of argatroban was accompanied by increases in the thrombin and ecarin clotting times but not the aPTT, whereas heparin increased the thrombin time and aPTT but not the ecarin clotting times.	Heparin	139-146	coagulation factor II	Rattus norvegicus	161-169
11951105-6	2000	(3) Contraction of antral muscle cells induced by motilin and gastrin was inhibited by the phospholipase C (PLC) inhibitor U  73122 and the IP(3) receptor antagonist heparin.	Heparin	166-173	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	140-154
10770945-10	2000	Although fractalkine can bind to heparin in vitro, as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivo is not well understood.	Heparin	33-40	C-X3-C motif chemokine ligand 1	Homo sapiens	9-20
10913257-9	2000	The rate constants for inhibition of thrombin and factor Xa by the complexes between antithrombin and full-length heparin or pentasaccharide were unaffected by both mutations, indicating that neither Lys136 nor Lys139 is involved in heparin activation of the inhibitor.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	37-45
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	75-82	fibroblast growth factor 2	Homo sapiens	28-33
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	75-82	fibroblast growth factor 2	Homo sapiens	170-175
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	0-26
10903991-4	2000	In rat SMCs, EGFR phosphorylation and extracellular signal-regulated kinase (ERK) activation in response to thrombin are inhibited not only by the EGFR inhibitor AG1478 and by EGFR blocking antibody but also by heparin and by neutralizing HB-EGF antibody.	Heparin	211-218	Eph receptor B1	Rattus norvegicus	77-80
10903991-3	2000	Because thrombin stimulation of vascular smooth muscle cell migration is blocked by heparin and because heparin can displace HB-EGF, we investigated the possibility that thrombin stimulation of smooth muscle cells (SMCs) depends on EGFR activation by HB-EGF.	Heparin	104-111	heparin-binding EGF-like growth factor	Rattus norvegicus	125-131
10903925-1	2000	HARP (Heparin Affin Regulatory Peptide) is a 18-kDa secreted protein displaying high affinity for heparin.	Heparin	98-105	pleiotrophin	Homo sapiens	0-4
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	28-33
10903925-1	2000	HARP (Heparin Affin Regulatory Peptide) is a 18-kDa secreted protein displaying high affinity for heparin.	Heparin	98-105	pleiotrophin	Homo sapiens	6-38
10903991-0	2000	Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor.	Heparin	0-7	coagulation factor II	Rattus norvegicus	20-28
10903991-0	2000	Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor.	Heparin	0-7	heparin-binding EGF-like growth factor	Rattus norvegicus	147-185
10903991-4	2000	In rat SMCs, EGFR phosphorylation and extracellular signal-regulated kinase (ERK) activation in response to thrombin are inhibited not only by the EGFR inhibitor AG1478 and by EGFR blocking antibody but also by heparin and by neutralizing HB-EGF antibody.	Heparin	211-218	Eph receptor B1	Rattus norvegicus	38-75
10903991-4	2000	In rat SMCs, EGFR phosphorylation and extracellular signal-regulated kinase (ERK) activation in response to thrombin are inhibited not only by the EGFR inhibitor AG1478 and by EGFR blocking antibody but also by heparin and by neutralizing HB-EGF antibody.	Heparin	211-218	coagulation factor II	Rattus norvegicus	108-116
10903991-7	2000	We conclude from these data that the inhibitory effect of heparin on SMC migration induced by thrombin relies, at least in part, on a blockade of HB-EGF-mediated EGFR transactivation.	Heparin	58-65	coagulation factor II	Rattus norvegicus	94-102
10903991-7	2000	We conclude from these data that the inhibitory effect of heparin on SMC migration induced by thrombin relies, at least in part, on a blockade of HB-EGF-mediated EGFR transactivation.	Heparin	58-65	heparin-binding EGF-like growth factor	Rattus norvegicus	146-152
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	170-175
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	0-26
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	28-33
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	fibroblast growth factor 2	Homo sapiens	170-175
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	114-121	fibroblast growth factor 2	Homo sapiens	229-234
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	114-121	fibroblast growth factor 2	Homo sapiens	295-300
10913474-12	2000	These data indicate a significant in vivo effect of abciximab plus heparin in increasing ACT and decreasing F1.2, results that are consistent with an effect on reducing thrombin generation.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	169-177
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	114-121	fibroblast growth factor 2	Homo sapiens	295-300
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	114-121	fibroblast growth factor 2	Homo sapiens	295-300
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	177-184	fibroblast growth factor 2	Homo sapiens	229-234
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	177-184	fibroblast growth factor 2	Homo sapiens	295-300
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	177-184	fibroblast growth factor 2	Homo sapiens	295-300
10873433-4	2000	We demonstrate that the experimentally observed receptor binding phenomena can be reproduced if cells (1) express heparin-binding cell surface molecules and if either (2) these heparin binding sites are FGFR and bind heparin and FGF-2-heparin complexes or (3) are surface molecules able to bind FGF-2 and couple with FGF-2 receptors to form high-affinity FGF-2-bound surface complexes.	Heparin	177-184	fibroblast growth factor 2	Homo sapiens	295-300
10873433-5	2000	The ability of heparin to directly interact with the FGFR and bind FGF-2 in the absence of this coupling function was not sufficient to explain heparin activity.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	67-72
10921707-6	2000	RESULTS: In the pilot study, heparin-bonded circuit patients had less complement 3a (p &lt; 0.001) and interleukin-8 (p &lt; 0.05) compared with uncoated cardiopulmonary bypass circuit patients.	Heparin	29-36	C-X-C motif chemokine ligand 8	Homo sapiens	103-116
10921707-8	2000	Multiple variable analysis revealed that the following postoperative variables were increased with bypass time (p = 0.01) and diminished with heparin-bonded circuits: interleukins (p = 0.01), peak airway pressures (p = 0.05), and prothrombin time (p = 0.03).	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	230-241
10949727-6	2000	Mean finger blood flow recovery time improved, and serum levels of circulating ICAM-1, VCAM-1 and E-selectin were lower at completion of heparin therapy, but changes did not reach statistical significance.	Heparin	137-144	vascular cell adhesion molecule 1	Homo sapiens	87-93
10937807-4	2000	A study of patient pooled plasma showed that incubation with a protease increased the thrombin time from 23 s to &gt; 300 s, suggesting that the anticoagulant activity of heparin could be neutralized by plasma proteins and released with proteolytic digestion.	Heparin	171-178	coagulation factor II, thrombin	Homo sapiens	86-94
10937807-6	2000	In addition, patients who received prior heparin injections had different responses to similar dosages of heparin, as indicated by differences in thrombin times.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	146-154
10937807-6	2000	In addition, patients who received prior heparin injections had different responses to similar dosages of heparin, as indicated by differences in thrombin times.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	146-154
11028764-12	2000	Heparin drastically inhibited the binding of IGF-1 by BP-3.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	45-50
11028764-12	2000	Heparin drastically inhibited the binding of IGF-1 by BP-3.	Heparin	0-7	BP3	Homo sapiens	54-58
10764763-5	2000	Consistent with these findings, the mutant antithrombin was normally activated by heparin for accelerated inhibition of factor Xa and thrombin.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	47-55
11060763-3	2000	Fractionated, or low-molecular weight, heparins (LMWHs) are more selective for coagulation Factor Xa (FXa) over thrombin (FIIa).	Heparin	39-47	coagulation factor II, thrombin	Homo sapiens	112-120
10902786-4	2000	A rapid and robust release of activin A and follistatin occurred in the circulation of patients undergoing abdominal aortic aneurysm repair or carotid endarterectomy at the time of vessel clamping and administration of heparin (5000 IU).	Heparin	219-226	follistatin	Homo sapiens	44-55
10902786-6	2000	However, administering heparin (2500 IU) to coronary angiography patients produced a similar activin and follistatin response, whereas placebo-treated angiography patients had no response.	Heparin	23-30	follistatin	Homo sapiens	105-116
10902786-7	2000	These findings illustrate that the routine use of heparin in surgical procedures elicits a rapid and robust release of activin and follistatin.	Heparin	50-57	follistatin	Homo sapiens	131-142
10958307-1	2000	We previously showed that rat thyroglobulin (Tg) is a heparin-binding protein and that heparin inhibits Tg binding to megalin (gp330), an endocytic Tg receptor found on the apical surface of thyrocytes.	Heparin	54-61	thyroglobulin	Rattus norvegicus	30-43
10867020-11	2000	These studies are the first to document a role for heparins in the catabolism of SERPIN-protease complexes at a point further in the pathway than cell surface binding, and this role may extend to other heparin-binding LRP-internalized ligands.	Heparin	51-59	LDL receptor related protein 1	Homo sapiens	218-221
10867020-11	2000	These studies are the first to document a role for heparins in the catabolism of SERPIN-protease complexes at a point further in the pathway than cell surface binding, and this role may extend to other heparin-binding LRP-internalized ligands.	Heparin	51-58	LDL receptor related protein 1	Homo sapiens	218-221
10861269-0	2000	Heparin attenuates TNF-alpha induced inflammatory response through a CD11b dependent mechanism.	Heparin	0-7	tumor necrosis factor	Rattus norvegicus	19-28
10861269-0	2000	Heparin attenuates TNF-alpha induced inflammatory response through a CD11b dependent mechanism.	Heparin	0-7	integrin subunit alpha M	Rattus norvegicus	69-74
10861269-3	2000	METHODS: The effects of heparin on tumour necrosis factor alpha (TNF-alpha) induced leucocyte rolling, adhesion, and migration as well as vascular permeability were assessed in rat mesenteric venules using intravital microscopy.	Heparin	24-31	tumor necrosis factor	Rattus norvegicus	65-74
10861269-9	2000	Binding of heparin was significantly increased on blood neutrophils obtained five hours after TNF-alpha administration.	Heparin	11-18	tumor necrosis factor	Rattus norvegicus	94-103
10861269-10	2000	Preincubation with an anti-CD11b mAb but not with an anti-CD11a or anti-L-selectin antibody significantly diminished heparin binding ex vivo.	Heparin	117-124	integrin subunit alpha M	Rattus norvegicus	27-32
10861269-11	2000	CONCLUSIONS: Our results support the concept that the anti-inflammatory effects of heparin involve attenuation of a CD11b dependent adherent mechanism.	Heparin	83-90	integrin subunit alpha M	Rattus norvegicus	116-121
10902786-0	2000	Release of activin and follistatin during cardiovascular procedures is largely due to heparin administration.	Heparin	86-93	follistatin	Homo sapiens	23-34
10902786-2	2000	As heparin is used routinely in many cardiovascular procedures for its anticoagulation properties, it may also cause the release of heparin-binding growth factors, including activin and follistatin, from the vascular endothelium.	Heparin	3-10	follistatin	Homo sapiens	186-197
10902786-3	2000	We examined the effect of two cardiovascular procedures and the use of heparin directly on the circulating concentrations of activin A and follistatin.	Heparin	71-78	follistatin	Homo sapiens	139-150
10849447-11	2000	Recombinant ADAM 12-S partially purified from conditioned medium on a heparin-Sepharose column also proteolyzed IGFBP-3.	Heparin	70-77	ADAM metallopeptidase domain 12	Homo sapiens	12-19
10748121-2	2000	np-1 also binds to the 165-amino acid heparin-binding form of VEGF (VEGF(165)) but not to the shorter VEGF(121) form, which lacks a heparin binding ability.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	62-66
10748121-2	2000	np-1 also binds to the 165-amino acid heparin-binding form of VEGF (VEGF(165)) but not to the shorter VEGF(121) form, which lacks a heparin binding ability.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	68-77
10748121-2	2000	np-1 also binds to the 165-amino acid heparin-binding form of VEGF (VEGF(165)) but not to the shorter VEGF(121) form, which lacks a heparin binding ability.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	68-72
10748121-4	2000	Both np-2 forms bind VEGF(165) with high affinity in the presence of heparin (K(D) 1.3 x 10(-10) m) but not VEGF(121).	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	21-30
10748121-4	2000	Both np-2 forms bind VEGF(165) with high affinity in the presence of heparin (K(D) 1.3 x 10(-10) m) but not VEGF(121).	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	21-25
10748121-7	2000	VEGF(145) is a secreted heparin binding VEGF form that contains the peptide encoded by exon 6 of VEGF but not the peptide encoded by exon 7, which is present in VEGF(165).	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	0-4
10748121-7	2000	VEGF(145) is a secreted heparin binding VEGF form that contains the peptide encoded by exon 6 of VEGF but not the peptide encoded by exon 7, which is present in VEGF(165).	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	40-44
10748121-7	2000	VEGF(145) is a secreted heparin binding VEGF form that contains the peptide encoded by exon 6 of VEGF but not the peptide encoded by exon 7, which is present in VEGF(165).	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	40-44
10748121-7	2000	VEGF(145) is a secreted heparin binding VEGF form that contains the peptide encoded by exon 6 of VEGF but not the peptide encoded by exon 7, which is present in VEGF(165).	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	40-44
10852713-4	2000	Mutant forms of FGF-1 that substitute a serine residue at these cysteine positions have been reported to increase the protein"s half-life and specific activity as well as decrease the dependence upon heparin for full activity.	Heparin	200-207	fibroblast growth factor 1	Homo sapiens	16-21
10860838-3	2000	Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity.	Heparin	129-136	fibroblast growth factor 1	Homo sapiens	190-195
10860838-3	2000	Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity.	Heparin	129-136	fibroblast growth factor 2	Homo sapiens	197-202
10860838-3	2000	Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity.	Heparin	129-136	fibroblast growth factor 7	Homo sapiens	208-213
10837139-7	2000	Using specific CK2 inhibitors such as heparin and 5, 6-dichloro-1-beta-d-ribofuranosylbenzimidazole, endogenous CK2 was confirmed as the main enzyme phosphorylating E-cadherin.	Heparin	38-45	cadherin 1	Homo sapiens	165-175
10819795-9	2000	The pattern of cellular calmodulin binding was highly decreased when spermatozoa were incubated under capacitating conditions, in the presence of heparin, in agreement with the published effect of capacitation on calmodulin binding proteins.	Heparin	146-153	calmodulin 1	Homo sapiens	24-34
10843884-1	2000	In streptozotocin (STZ)-induced diabetic rats, we previously showed an increased heparin-releasable (luminal) lipoprotein lipase (LPL) activity from perfused hearts.	Heparin	81-88	lipoprotein lipase	Rattus norvegicus	110-128
10843884-1	2000	In streptozotocin (STZ)-induced diabetic rats, we previously showed an increased heparin-releasable (luminal) lipoprotein lipase (LPL) activity from perfused hearts.	Heparin	81-88	lipoprotein lipase	Rattus norvegicus	130-133
10843884-9	2000	This increased VLDL-TG hydrolysis was essentially abolished by prior perfusion of the diabetic heart with heparin, implicating LPL in this process.	Heparin	106-113	lipoprotein lipase	Rattus norvegicus	127-130
10806335-0	2000	Inhibition of binding of lactoferrin to the human promonocyte cell line THP-1 by heparin: the role of cell surface sulphated molecules.	Heparin	81-88	GLI family zinc finger 2	Homo sapiens	72-77
10806335-3	2000	In the present work we found that heparin caused a dose-dependent inhibition of specific binding of both human and bovine lactoferrin to human monocytic THP-1 cells.	Heparin	34-41	GLI family zinc finger 2	Homo sapiens	153-158
10834640-5	2000	Thrombin activation is indirectly blocked by heparin and its analogs.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	0-8
10839770-5	2000	RESULTS: Mean cTnT was 15% lower in heparin sampling tubes than in serum.	Heparin	36-43	troponin T2, cardiac type	Homo sapiens	14-18
10839770-8	2000	Addition of heparin ( approximately 100 IU/mL) to serial samples from nine acute myocardial infarction patients produced mean cTnT losses of 33% at 1-12 h after onset of chest pain, 17% at 13-48 h, and 7% after 48 h. The changing heparin effects were seen for both cTnT and cTnI during time courses of individual patients with myocardial infarction.	Heparin	12-19	troponin T2, cardiac type	Homo sapiens	126-130
10839770-8	2000	Addition of heparin ( approximately 100 IU/mL) to serial samples from nine acute myocardial infarction patients produced mean cTnT losses of 33% at 1-12 h after onset of chest pain, 17% at 13-48 h, and 7% after 48 h. The changing heparin effects were seen for both cTnT and cTnI during time courses of individual patients with myocardial infarction.	Heparin	12-19	troponin T2, cardiac type	Homo sapiens	265-269
10848900-8	2000	Partial purification of a putative sheep tryptase from lung and gut extracts was achieved using heparin-Sepharose affinity chromatography.	Heparin	96-103	tryptase beta-2	Ovis aries	41-49
10844618-18	2000	Actin expression was blunted with the addition of insulin or heparin in the culture medium.	Heparin	61-68	Actin 79B	Drosophila melanogaster	0-5
10835602-8	2000	By constructing a biologically active proteoglycan-FGF-1 fusion protein, we have demonstrated an approach that may prove effective for engineering not only FGF family members, but other HP-binding molecules as well.	Heparin	186-188	fibroblast growth factor 1	Homo sapiens	51-56
10834640-6	2000	However, after thrombin is clot-bound (with fibrin), it is relatively protected from heparin and is effectively blocked only by direct thrombin inhibitors (hirudin and its analogs).	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	15-23
10799535-0	2000	Identification of a major heparin and cell binding site in the LG4 module of the laminin alpha 5 chain.	Heparin	26-33	laminin subunit alpha 5	Homo sapiens	81-102
10891598-1	2000	Using recombinant human tau protein phosphorylated by a brain extract and the glycogen synthase kinase-3beta in the absence or the presence of heparin, we showed that phosphorylation-dependent antibody AD2 recognition only requires phosphorylated Ser-396.	Heparin	143-150	apolipoprotein E	Homo sapiens	202-205
11032250-1	2000	Acid fibroblast growth factor (aFGF) binds to its cell-surface receptors in a heparin-dependent manner.	Heparin	78-85	fibroblast growth factor 1	Homo sapiens	31-35
11032250-3	2000	To retain the natural conformation of aFGF during screening, we used biotinylated heparin to immobilize aFGF on a streptavidin-coated dish.	Heparin	82-89	fibroblast growth factor 1	Homo sapiens	104-108
10822071-8	2000	PATIENTS: Before CPB, heparin effectively abolished platelet macroaggregation induced by collagen (20.5 to 1.4 Ohms) or fMLP (3.9 to 0 Ohms (p&lt;0.0001).	Heparin	22-29	formyl peptide receptor 1	Homo sapiens	120-124
10822071-13	2000	In vitro heparin promoted fMLP macroaggregation (2.9 to 8.6 Omega).	Heparin	9-16	formyl peptide receptor 1	Homo sapiens	26-30
10788475-7	2000	The peptides bind to VEGF and inhibit binding of both VEGF(165) and VEGF(121), suggesting that the peptides interact with the main body of VEGF but not the heparin-binding domain that is absent in VEGF(121).	Heparin	156-163	vascular endothelial growth factor A	Homo sapiens	54-58
10788475-7	2000	The peptides bind to VEGF and inhibit binding of both VEGF(165) and VEGF(121), suggesting that the peptides interact with the main body of VEGF but not the heparin-binding domain that is absent in VEGF(121).	Heparin	156-163	vascular endothelial growth factor A	Homo sapiens	54-58
10788472-7	2000	Studies using CD and NMR spectroscopy suggest that HB-GAM undergoes a conformational change upon binding to heparin, and that the binding occurs primarily to the beta-sheet domains of the protein.	Heparin	108-115	pleiotrophin	Homo sapiens	51-57
10788475-7	2000	The peptides bind to VEGF and inhibit binding of both VEGF(165) and VEGF(121), suggesting that the peptides interact with the main body of VEGF but not the heparin-binding domain that is absent in VEGF(121).	Heparin	156-163	vascular endothelial growth factor A	Homo sapiens	54-58
10788475-7	2000	The peptides bind to VEGF and inhibit binding of both VEGF(165) and VEGF(121), suggesting that the peptides interact with the main body of VEGF but not the heparin-binding domain that is absent in VEGF(121).	Heparin	156-163	vascular endothelial growth factor A	Homo sapiens	54-58
10808153-8	2000	Heparin suppressed thrombin activation, whereas aspirin or dipyridamole did not.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	19-27
10821379-4	2000	Heparin stimulates the activity of antithrombin, a serine-protease inhibitor.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	35-47
10780935-6	2000	Lipoprotein lipase (LPL) activity was increased in endotoxin-pretreated hearts, and after perfusion with "endotoxic" VLDL, there was a tendency for translocation of LPL from tissue-residual to heparin-releasable compartments, but these changes were modest.	Heparin	193-200	lipoprotein lipase	Rattus norvegicus	0-18
10780935-6	2000	Lipoprotein lipase (LPL) activity was increased in endotoxin-pretreated hearts, and after perfusion with "endotoxic" VLDL, there was a tendency for translocation of LPL from tissue-residual to heparin-releasable compartments, but these changes were modest.	Heparin	193-200	lipoprotein lipase	Rattus norvegicus	20-23
10780935-6	2000	Lipoprotein lipase (LPL) activity was increased in endotoxin-pretreated hearts, and after perfusion with "endotoxic" VLDL, there was a tendency for translocation of LPL from tissue-residual to heparin-releasable compartments, but these changes were modest.	Heparin	193-200	lipoprotein lipase	Rattus norvegicus	165-168
10769176-8	2000	These findings suggested that the mutated site, i.e. the main heparin-binding site of FN, was also the principal site for binding to alpha-Ag.	Heparin	62-69	fibronectin 1	Homo sapiens	86-88
10792372-0	2000	The antagonism of interferon-gamma (IFN-gamma) by heparin: examination of the blockade of class II MHC antigen and heat shock protein-70 expression.	Heparin	50-57	interferon gamma	Homo sapiens	18-34
10792372-0	2000	The antagonism of interferon-gamma (IFN-gamma) by heparin: examination of the blockade of class II MHC antigen and heat shock protein-70 expression.	Heparin	50-57	interferon gamma	Homo sapiens	36-45
10792372-6	2000	In this study it is shown that heparin can prevent normal induction of the class II transactivator and heat shock cognate protein-70 in an IFN-gamma-treated endothelial cell line.	Heparin	31-38	interferon gamma	Homo sapiens	139-148
10792372-8	2000	This provides further evidence for the blockade by heparin of ligand activation of the specific IFN-gamma receptor.	Heparin	51-58	interferon gamma	Homo sapiens	96-105
10809899-12	2000	Heparin drastically decreased the binding of IGF-I by BP-3.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	45-50
10857760-2	2000	Here, circular dichroism and fluorescence spectroscopic techniques are used to demonstrate that low molecular weight heparin and chondroitin sulfate cause significant changes in secondary and tertiary structure of IFN-gamma.	Heparin	117-124	interferon gamma	Homo sapiens	214-223
10857760-3	2000	The results suggest that heparin and chondroitin sulfate modulate IFN-gamma activity by causing structural changes in the IFN-gamma dimer.	Heparin	25-32	interferon gamma	Homo sapiens	66-75
10857760-3	2000	The results suggest that heparin and chondroitin sulfate modulate IFN-gamma activity by causing structural changes in the IFN-gamma dimer.	Heparin	25-32	interferon gamma	Homo sapiens	122-131
10764593-3	2000	Furthermore, NAP-1 and NAP-2 phosphorylation in crude HeLa cell extracts is abolished by heparin, a specific inhibitor of CKII.	Heparin	89-96	nucleosome assembly protein 1 like 1	Homo sapiens	13-18
10756332-1	2000	Previously we proposed a heparin/protamine-based system for delivery of protease drugs such as tissue-specific plasminogen activator (tPA).	Heparin	25-32	plasminogen activator, tissue type	Homo sapiens	95-132
10756332-1	2000	Previously we proposed a heparin/protamine-based system for delivery of protease drugs such as tissue-specific plasminogen activator (tPA).	Heparin	25-32	plasminogen activator, tissue type	Homo sapiens	134-137
10756332-3	2000	This cation-modified tPA showed much stronger heparin affinity than the parent tPA.	Heparin	46-53	plasminogen activator, tissue type	Homo sapiens	21-24
10756332-3	2000	This cation-modified tPA showed much stronger heparin affinity than the parent tPA.	Heparin	46-53	plasminogen activator, tissue type	Homo sapiens	79-82
10756332-4	2000	The complex formed by mtPA and heparin was stable in human plasma, and the activity of mtPA in such a complex was inhibited by the appended heparin.	Heparin	31-38	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	87-91
10756332-4	2000	The complex formed by mtPA and heparin was stable in human plasma, and the activity of mtPA in such a complex was inhibited by the appended heparin.	Heparin	140-147	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	22-26
10756332-4	2000	The complex formed by mtPA and heparin was stable in human plasma, and the activity of mtPA in such a complex was inhibited by the appended heparin.	Heparin	140-147	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	87-91
10756332-7	2000	These findings suggest the applicability of the heparin/protamine delivery system to abort the potential bleeding risks associated with clinical use of tPA.	Heparin	48-55	plasminogen activator, tissue type	Homo sapiens	152-155
10756332-9	2000	The expressed modified tPA (EmtPA) thus prepared retained the full catalytic activity of the parent tPA, and this activity could also be inhibited by heparin, and the heparin-induced inhibition could be reversed following the addition of protamine.	Heparin	150-157	plasminogen activator, tissue type	Homo sapiens	23-26
10756332-9	2000	The expressed modified tPA (EmtPA) thus prepared retained the full catalytic activity of the parent tPA, and this activity could also be inhibited by heparin, and the heparin-induced inhibition could be reversed following the addition of protamine.	Heparin	150-157	plasminogen activator, tissue type	Homo sapiens	30-33
10756332-9	2000	The expressed modified tPA (EmtPA) thus prepared retained the full catalytic activity of the parent tPA, and this activity could also be inhibited by heparin, and the heparin-induced inhibition could be reversed following the addition of protamine.	Heparin	167-174	plasminogen activator, tissue type	Homo sapiens	23-26
10756332-9	2000	The expressed modified tPA (EmtPA) thus prepared retained the full catalytic activity of the parent tPA, and this activity could also be inhibited by heparin, and the heparin-induced inhibition could be reversed following the addition of protamine.	Heparin	167-174	plasminogen activator, tissue type	Homo sapiens	30-33
10944959-11	2000	The cationic peroxidases, such as major basic protein and eosinophil peroxidase, are neutralized by the highly anionic heparin; thus heparin inhibits the epithelial damage induced by some of these cationic proteins.	Heparin	119-126	eosinophil peroxidase	Homo sapiens	58-79
10944959-11	2000	The cationic peroxidases, such as major basic protein and eosinophil peroxidase, are neutralized by the highly anionic heparin; thus heparin inhibits the epithelial damage induced by some of these cationic proteins.	Heparin	133-140	eosinophil peroxidase	Homo sapiens	58-79
11200464-0	2000	[Cytokine profile and fibrinogen level in blood plasma in diabetic foot under the action of heparin].	Heparin	92-99	fibrinogen beta chain	Homo sapiens	22-32
10782678-3	2000	Like the heparin from which they were prepared, they inhibit thrombin-induced blood coagulation.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	61-69
10736217-0	2000	Consequences of the non-specific binding of a protein to a linear polymer: reconciliation of stoichiometric and equilibrium titration data for the thrombin-heparin interaction.	Heparin	156-163	coagulation factor II, thrombin	Homo sapiens	147-155
10736217-5	2000	Consideration of published results for spectrofluorometric titrations of the thrombin-heparin system under stoichiometric conditions in such terms has permitted their reconciliation with results of a later publication on the interaction under equilibrium conditions.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	77-85
10749676-7	2000	Heparin was a potent inhibitor of binding with a K(i) of 50 nM, suggesting that the heparin-binding domain of TSP1 may be involved in this interaction.	Heparin	0-7	thrombospondin 1	Homo sapiens	110-114
10749676-7	2000	Heparin was a potent inhibitor of binding with a K(i) of 50 nM, suggesting that the heparin-binding domain of TSP1 may be involved in this interaction.	Heparin	84-91	thrombospondin 1	Homo sapiens	110-114
10749676-8	2000	This was confirmed by the ability of a recombinant heparin-binding domain of TSP1 to directly compete for TSP1 binding to polyhistidine-containing proteins.	Heparin	51-58	thrombospondin 1	Homo sapiens	77-81
10749676-8	2000	This was confirmed by the ability of a recombinant heparin-binding domain of TSP1 to directly compete for TSP1 binding to polyhistidine-containing proteins.	Heparin	51-58	thrombospondin 1	Homo sapiens	106-110
10725457-5	2000	We report here that hsp40, hsp60, hsc70, hsp70, hsp84, hsp86, and gp96 (grp94) but not BiP (grp78) and calreticulin can be separated from a single tumor sample in one step using heparin-agarose chromatography.	Heparin	178-185	DnaJ heat shock protein family (Hsp40) member B1 pseudogene 1	Homo sapiens	20-25
10699297-7	2000	The results demonstrated that bFGF, immobilized within fibrin containing a 500-fold molar excess of immobilized heparin relative to bFGF, enhanced neurite extension by up to about 100% relative to unmodified fibrin.	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	30-34
10727210-0	2000	Imaging and mapping heparin-binding sites on single fibronectin molecules with atomic force microscopy.	Heparin	20-27	fibronectin 1	Homo sapiens	52-63
10832659-8	2000	RESULTS: IL 6 and IL 10 release was significantly less (p&lt;0.05) in the heparin-coated group.	Heparin	74-81	interleukin 6	Homo sapiens	9-13
10832659-10	2000	CONCLUSIONS: These results suggest that with the use of heparin-coated circuits there is a lower production of IL 6 and IL 10 from isolated PBMC than with uncoated circuits.	Heparin	56-63	interleukin 6	Homo sapiens	111-115
10734175-4	2000	The rapid internalization of hDOR was totally blocked in the presence of heparin, known as an inhibitor of G protein-coupled receptor kinases (Benovic et al., 1989), a result indicating that phosphorylation by these kinases is a critical step in desensitization (Hasbi et al, 1998) and internalization of hDOR (present study) in SK-N-BE cell line.	Heparin	73-80	tumor protein p53 inducible nuclear protein 2	Homo sapiens	29-33
10734175-4	2000	The rapid internalization of hDOR was totally blocked in the presence of heparin, known as an inhibitor of G protein-coupled receptor kinases (Benovic et al., 1989), a result indicating that phosphorylation by these kinases is a critical step in desensitization (Hasbi et al, 1998) and internalization of hDOR (present study) in SK-N-BE cell line.	Heparin	73-80	tumor protein p53 inducible nuclear protein 2	Homo sapiens	305-309
10977903-1	2000	In vivo experiments on the model of wound healing showed that thrombin and thrombin receptor agonist TRAP-6 stimulated heparin secretion by mast cells in rat subcutaneous fat: the saturation of mast cells with heparin decreased, while degranulation and granulolysis increased.	Heparin	119-126	coagulation factor II	Rattus norvegicus	62-70
10977903-1	2000	In vivo experiments on the model of wound healing showed that thrombin and thrombin receptor agonist TRAP-6 stimulated heparin secretion by mast cells in rat subcutaneous fat: the saturation of mast cells with heparin decreased, while degranulation and granulolysis increased.	Heparin	210-217	coagulation factor II	Rattus norvegicus	62-70
10727210-3	2000	The Hep II site has been considered the high-affinity heparin-binding site based on studies of fibronectin fragments.	Heparin	54-61	fibronectin 1	Homo sapiens	95-106
10727210-4	2000	However, few studies have been carried out on heparin binding by intact fibronectin.	Heparin	46-53	fibronectin 1	Homo sapiens	72-83
10727210-5	2000	We imaged single fibronectin molecules as well as heparin-coated gold particles bound to whole dimeric plasma fibronectin molecules with tapping mode atomic force microscopy.	Heparin	50-57	fibronectin 1	Homo sapiens	110-121
10727210-7	2000	Quantitative analysis of images of individual fibronectin-heparin-gold complexes showed that almost twice as many heparin-gold particles bound to the N-terminal Hep I site compared to the Hep II site.	Heparin	58-65	fibronectin 1	Homo sapiens	46-57
10727210-7	2000	Quantitative analysis of images of individual fibronectin-heparin-gold complexes showed that almost twice as many heparin-gold particles bound to the N-terminal Hep I site compared to the Hep II site.	Heparin	114-121	fibronectin 1	Homo sapiens	46-57
10782998-0	2000	Binding of selenoprotein P to heparin: characterization with surface plasmon resonance.	Heparin	30-37	selenoprotein P	Homo sapiens	11-26
10722716-1	2000	Antithrombin requires heparin for efficient inhibition of the final two proteinases of the blood coagulation cascade, factor Xa and thrombin.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	4-12
10669869-2	2000	Recombinant human heart chymase (rh-chymase) was purified from the culture medium via a single one-step heparin-agarose column chromatography tracing, using succinyl-Ala-Ala-Pro-Phe-para-nitroanilide (Suc-AAPF-pNA) hydrolysing activity.	Heparin	104-111	chymase 1	Homo sapiens	24-31
10669869-2	2000	Recombinant human heart chymase (rh-chymase) was purified from the culture medium via a single one-step heparin-agarose column chromatography tracing, using succinyl-Ala-Ala-Pro-Phe-para-nitroanilide (Suc-AAPF-pNA) hydrolysing activity.	Heparin	104-111	chymase 1	Homo sapiens	36-43
10782998-1	2000	The binding of selenoprotein P to glycosaminoglycans using heparin as a model compound was studied by surface plasmon resonance.	Heparin	59-66	selenoprotein P	Homo sapiens	15-30
10782998-2	2000	It was found that heparin contains two binding sites for selenoprotein P, a high-affinity, low-capacity site (Kd approximately 1 nM) and a low-affinity, high-capacity site (Kd approximately 140 nM).	Heparin	18-25	selenoprotein P	Homo sapiens	57-72
10720891-8	2000	CONCLUSION: These results suggest that the presence of a substitution in the EC-SOD gene at the heparin-binding domain could be a prognostic marker of dialysis patients.	Heparin	96-103	superoxide dismutase 3	Homo sapiens	77-83
10759005-8	2000	The thrombin-based assays also overestimated antithrombin activity in patients under high-dose heparin.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	4-12
10818267-11	2000	Also, acidic polysaccharides such as heparin were much more efficacious in the inhibition of hIFN-gamma binding to hemolymph relative to protocerebral particulates.	Heparin	37-44	interferon gamma	Homo sapiens	93-103
10698186-3	2000	As TSP-1 binds avidly to heparin, as does IGFBP-5, the effect of glycosaminoglycans on the TSP-1/IGFBP-5 interaction was analyzed.	Heparin	25-32	thrombospondin 1	Homo sapiens	3-8
10698186-6	2000	In contrast, both heparin and heparan sulfate significantly inhibited the OPN-IGFBP-5 interaction and chondroitin sulfate A, B, and C had no effect.	Heparin	18-25	insulin like growth factor binding protein 5	Homo sapiens	78-85
12501620-2	2000	The results showed that there were basic production of interleukin-6(IL-6) and tumor necrosis factor-alpha (TNF-alpha) on MC in the control group without LPS, that high-concentration heparin(500 U/ml) increased the effects of LPS on MC, and that low-concentration heparin (5 U/ml) conversely inhibited the effects of LPS on MC.	Heparin	183-190	tumor necrosis factor	Homo sapiens	79-106
12501620-2	2000	The results showed that there were basic production of interleukin-6(IL-6) and tumor necrosis factor-alpha (TNF-alpha) on MC in the control group without LPS, that high-concentration heparin(500 U/ml) increased the effects of LPS on MC, and that low-concentration heparin (5 U/ml) conversely inhibited the effects of LPS on MC.	Heparin	183-190	tumor necrosis factor	Homo sapiens	108-117
12501620-3	2000	These data indicate that the low-concentration heparin could inhibit the proliferation of MC and the secrection of IL-6 and TNF-alpha induced by LPS, and hence provide an experimental evidence for administration of heparin in the treatment glomerular disease.	Heparin	47-54	interleukin 6	Homo sapiens	115-119
12501620-3	2000	These data indicate that the low-concentration heparin could inhibit the proliferation of MC and the secrection of IL-6 and TNF-alpha induced by LPS, and hence provide an experimental evidence for administration of heparin in the treatment glomerular disease.	Heparin	47-54	tumor necrosis factor	Homo sapiens	124-133
12501620-3	2000	These data indicate that the low-concentration heparin could inhibit the proliferation of MC and the secrection of IL-6 and TNF-alpha induced by LPS, and hence provide an experimental evidence for administration of heparin in the treatment glomerular disease.	Heparin	215-222	interleukin 6	Homo sapiens	115-119
12501620-3	2000	These data indicate that the low-concentration heparin could inhibit the proliferation of MC and the secrection of IL-6 and TNF-alpha induced by LPS, and hence provide an experimental evidence for administration of heparin in the treatment glomerular disease.	Heparin	215-222	tumor necrosis factor	Homo sapiens	124-133
10867212-3	2000	The effect of heparin-induced extracorporeal LDL/fibrinogen precipitation (HELP), a method for safe and immediate reduction of parameters relevant to hemorheology, such as plasma fibrinogen and the lipoproteins, was investigated in 141 patients with MID.	Heparin	14-21	fibrinogen beta chain	Homo sapiens	49-59
10867212-3	2000	The effect of heparin-induced extracorporeal LDL/fibrinogen precipitation (HELP), a method for safe and immediate reduction of parameters relevant to hemorheology, such as plasma fibrinogen and the lipoproteins, was investigated in 141 patients with MID.	Heparin	14-21	fibrinogen beta chain	Homo sapiens	179-189
12501620-2	2000	The results showed that there were basic production of interleukin-6(IL-6) and tumor necrosis factor-alpha (TNF-alpha) on MC in the control group without LPS, that high-concentration heparin(500 U/ml) increased the effects of LPS on MC, and that low-concentration heparin (5 U/ml) conversely inhibited the effects of LPS on MC.	Heparin	183-190	interleukin 6	Homo sapiens	55-68
12501620-2	2000	The results showed that there were basic production of interleukin-6(IL-6) and tumor necrosis factor-alpha (TNF-alpha) on MC in the control group without LPS, that high-concentration heparin(500 U/ml) increased the effects of LPS on MC, and that low-concentration heparin (5 U/ml) conversely inhibited the effects of LPS on MC.	Heparin	183-190	interleukin 6	Homo sapiens	69-73
10660541-0	2000	The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	111-119
10709911-5	2000	Unlike heparin-induced stimulation of antithrombin-thrombin interaction, the heparin-induced stimulation of tissue plasminogen activator did not seem to follow a template model.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	42-50
10885035-1	2000	The chronic heparin deficiency achieved by long-term treatment (for 3 weeks) with protamine-sulfate is accompanied by the development of stable hyperglycemia, decreased glucose tolerance, and the appearance of insulin resistance.	Heparin	12-19	insulin	Homo sapiens	210-217
10660568-2	2000	It has been proposed that residues P15 and P14 are expelled from beta-sheet A of antithrombin by heparin binding, permitting better interaction of the reactive center loop with factor Xa.	Heparin	97-104	cyclin dependent kinase inhibitor 2B	Homo sapiens	35-38
10686395-0	2000	Heparin specifically inhibits binding of apolipoprotein E to amyloid beta-peptide.	Heparin	0-7	apolipoprotein E	Homo sapiens	41-57
10686395-2	2000	We find here that heparin specifically inhibits apoE-amyloid beta-peptide (1-40) interaction.	Heparin	18-25	apolipoprotein E	Homo sapiens	48-52
10686395-4	2000	The binding is not affected by high salt concentration, which prevents heparin-induced changes of apoE conformation.	Heparin	71-78	apolipoprotein E	Homo sapiens	98-102
10686395-5	2000	We propose that rigid protein conformation, induced by high affinity heparin binding to apoE, is unfavorable for its interaction to amyloid beta-peptide.	Heparin	69-76	apolipoprotein E	Homo sapiens	88-92
10640649-3	2000	In this study, the influence of immobilization of heparin to collagen, crosslinked using N-(3-dimethylaminopropyl)-N"-ethylcarbodiimide (EDC) in combination with N-hydroxysuccinimide (NHS), on the binding and release of bFGF was determined.	Heparin	50-57	fibroblast growth factor 2	Homo sapiens	220-224
10640649-6	2000	Immobilization of increasing amounts of heparin to EDC/NHS-crosslinked collagen (containing 14 free epsilon-amino groups per 1000 amino acid residues, E/N14C) resulted in binding of increasing amounts of bFGF to the material.	Heparin	40-47	fibroblast growth factor 2	Homo sapiens	204-208
10640649-7	2000	Maximal bFGF binding was observed for E/N14C containing 20-30 mg heparin immobilized per gram of collagen which was obtained using a molar ratio of EDC to heparin-carboxylic acid groups of 0.4 for heparin immobilization (E/N14C-H(0.4)).	Heparin	65-72	fibroblast growth factor 2	Homo sapiens	8-12
10640649-7	2000	Maximal bFGF binding was observed for E/N14C containing 20-30 mg heparin immobilized per gram of collagen which was obtained using a molar ratio of EDC to heparin-carboxylic acid groups of 0.4 for heparin immobilization (E/N14C-H(0.4)).	Heparin	155-162	fibroblast growth factor 2	Homo sapiens	8-12
10640649-7	2000	Maximal bFGF binding was observed for E/N14C containing 20-30 mg heparin immobilized per gram of collagen which was obtained using a molar ratio of EDC to heparin-carboxylic acid groups of 0.4 for heparin immobilization (E/N14C-H(0.4)).	Heparin	155-162	fibroblast growth factor 2	Homo sapiens	8-12
10660568-9	2000	In contrast, the basal rate of inhibition of thrombin is similar to that of control antithrombin but is increased 300-fold by heparin.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	45-53
10660541-0	2000	The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	111-119
10660541-2	2000	Thrombin binds to GpIb via its heparin-binding site (HBS) (De Candia, E., De Cristofaro, R., De Marco, L., Mazzucato, M., Picozzi, M., and Landolfi, R. (1997) Thromb.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	0-8
10660541-6	2000	To identify the thrombin-binding domain on GpIbalpha, we examined the effect of GpIbalpha(1-282), a GpIbalpha fragment released by the cobra venom mocarhagin on the heparin-catalyzed rate of thrombin inhibition by antithrombin III (AT).	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	16-24
10660541-14	2000	It was also demonstrated that intact platelets may dose-dependently inhibit the heparin-catalyzed thrombin inhibition by AT at enzyme concentrations &lt;5 nM.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	98-106
10660541-15	2000	Altogether, these findings show that thrombin HBS binds to the region of GpIbalpha involving the Asp(272)-Glu(282) segment, protecting the enzyme from the inactivation by the heparin-AT system.	Heparin	175-182	coagulation factor II, thrombin	Homo sapiens	37-45
10662704-1	2000	Several laboratories have shown that when rats are fasted, the amount of lipoprotein lipase (LPL) at the vascular endothelium in heart (monitored as the amount released by heparin) increases severalfold without corresponding changes in the production of LPL.	Heparin	172-179	lipoprotein lipase	Rattus norvegicus	73-91
10652320-2	2000	Structural data indicate that 7 of the 11 basic residues of the heparin-binding exosite of thrombin are conserved at similar three-dimensional locations in FXa.	Heparin	64-71	coagulation factor II, thrombin	Homo sapiens	91-99
10662704-1	2000	Several laboratories have shown that when rats are fasted, the amount of lipoprotein lipase (LPL) at the vascular endothelium in heart (monitored as the amount released by heparin) increases severalfold without corresponding changes in the production of LPL.	Heparin	172-179	lipoprotein lipase	Rattus norvegicus	93-96
10657692-3	2000	We studied the effect of fasting on the distribution of hepatic lipase between extracellular (heparin-releasable) and intracellular (liver-retained or residual) compartments in perfused livers, and on the secretion of hepatic lipase by isolated hepatocytes.	Heparin	94-101	lipase C, hepatic type	Rattus norvegicus	56-70
10669638-7	2000	A 50% increase in FGF-2 content versus control (P&lt;0.01) was found in the pericellular fraction (extracted by heparin treatment).	Heparin	112-119	fibroblast growth factor 2	Homo sapiens	18-23
10640391-0	2000	Specificities of heparin-binding sites from the amino-terminus and type 1 repeats of thrombospondin-1.	Heparin	17-24	thrombospondin 1	Homo sapiens	85-101
10640391-1	2000	Interactions of heparin with intact human thrombospondin-1 (TSP1) and with two heparin-binding fragments of TSP1 were characterized using chemically modified heparins, a vascular heparan sulfate proteoglycan, and a series of heparin oligosaccharides prepared by partial deaminative cleavage.	Heparin	16-23	thrombospondin 1	Homo sapiens	42-58
10640391-1	2000	Interactions of heparin with intact human thrombospondin-1 (TSP1) and with two heparin-binding fragments of TSP1 were characterized using chemically modified heparins, a vascular heparan sulfate proteoglycan, and a series of heparin oligosaccharides prepared by partial deaminative cleavage.	Heparin	16-23	thrombospondin 1	Homo sapiens	60-64
10640391-1	2000	Interactions of heparin with intact human thrombospondin-1 (TSP1) and with two heparin-binding fragments of TSP1 were characterized using chemically modified heparins, a vascular heparan sulfate proteoglycan, and a series of heparin oligosaccharides prepared by partial deaminative cleavage.	Heparin	16-23	thrombospondin 1	Homo sapiens	108-112
10640391-1	2000	Interactions of heparin with intact human thrombospondin-1 (TSP1) and with two heparin-binding fragments of TSP1 were characterized using chemically modified heparins, a vascular heparan sulfate proteoglycan, and a series of heparin oligosaccharides prepared by partial deaminative cleavage.	Heparin	79-86	thrombospondin 1	Homo sapiens	108-112
10640391-3	2000	The dependence on oligosaccharide size for binding to the recombinant amino-terminal heparin-binding domain of TSP1 was the same as that of the intact TSP1 molecule but differed from that of a synthetic heparin-binding peptide from the type 1 repeats, suggesting that the interaction between intact TSP1 and heparin is primarily mediated by the amino-terminal domain.	Heparin	85-92	thrombospondin 1	Homo sapiens	111-115
10640391-3	2000	The dependence on oligosaccharide size for binding to the recombinant amino-terminal heparin-binding domain of TSP1 was the same as that of the intact TSP1 molecule but differed from that of a synthetic heparin-binding peptide from the type 1 repeats, suggesting that the interaction between intact TSP1 and heparin is primarily mediated by the amino-terminal domain.	Heparin	203-210	thrombospondin 1	Homo sapiens	111-115
10640391-4	2000	Based on activities of chemically modified heparins, binding to TSP1 depended primarily on 2-N- and 6-O-sulfation of glucosamine and to a lesser degree on 2,3-O-sulfation and the carboxyl residues of the uronic acids.	Heparin	43-51	thrombospondin 1	Homo sapiens	64-68
10640391-8	2000	These data demonstrate that the heparin-binding specificities of intact TSP1 and peptides from the type 1 repeats overlap with that of basic fibroblast growth factor (FGF2) and are consistent with the ability of these TSP1-derived molecules to inhibit FGF2-stimulated angiogenesis.	Heparin	32-39	thrombospondin 1	Homo sapiens	72-76
10640391-8	2000	These data demonstrate that the heparin-binding specificities of intact TSP1 and peptides from the type 1 repeats overlap with that of basic fibroblast growth factor (FGF2) and are consistent with the ability of these TSP1-derived molecules to inhibit FGF2-stimulated angiogenesis.	Heparin	32-39	thrombospondin 1	Homo sapiens	218-222
10640391-8	2000	These data demonstrate that the heparin-binding specificities of intact TSP1 and peptides from the type 1 repeats overlap with that of basic fibroblast growth factor (FGF2) and are consistent with the ability of these TSP1-derived molecules to inhibit FGF2-stimulated angiogenesis.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	252-256
11096650-1	2000	For more than 25 years, basic experiments using cell culture and animal experimental techniques have predicted superior thrombin inhibition with use of low molecular weight heparin (LMWH) rather than unfractionated heparin (UFH).	Heparin	173-180	coagulation factor II, thrombin	Homo sapiens	120-128
10687947-1	2000	Fibroblast growth factor-2 (FGF-2) is a member of a large family of proteins that bind heparin and heparan sulfate and modulate the function of a wide range of cell types.	Heparin	87-94	fibroblast growth factor 2	Homo sapiens	0-26
10687947-1	2000	Fibroblast growth factor-2 (FGF-2) is a member of a large family of proteins that bind heparin and heparan sulfate and modulate the function of a wide range of cell types.	Heparin	87-94	fibroblast growth factor 2	Homo sapiens	28-33
10681410-3	2000	The primary amino acid sequence of HL was compared to that of lipoprotein lipase (LPL), a related enzyme that possesses several putative heparin-binding domains.	Heparin	137-144	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	62-80
10665930-13	2000	Treatment of rats with heparin blunted glomerular proliferation as well as ERK activation and restored p38 MAP kinase activity.	Heparin	23-30	Eph receptor B1	Rattus norvegicus	75-78
10681410-3	2000	The primary amino acid sequence of HL was compared to that of lipoprotein lipase (LPL), a related enzyme that possesses several putative heparin-binding domains.	Heparin	137-144	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	82-85
10681410-4	2000	Of the three putative heparin-binding clusters of LPL (J. Biol.	Heparin	22-29	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	50-53
10681410-18	2000	This is different for LPL: mutations in the C-terminal binding domain (Cluster 4) cause a more significant shift in the salt required for elution from heparin-Sepharose than mutations in the N-terminal domain (Cluster 1).	Heparin	151-158	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	22-25
10664506-2	2000	S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site.	Heparin	95-102	fibroblast growth factor 1	Homo sapiens	23-49
10664506-2	2000	S130K is a mutation of fibroblast growth factor-1 (FGF-1), with lysine replacing serine in the heparin-binding site.	Heparin	95-102	fibroblast growth factor 1	Homo sapiens	51-56
10664506-9	2000	S130K is also significantly more potent than FGF-1 in the presence of heparin.	Heparin	70-77	fibroblast growth factor 1	Homo sapiens	45-50
10664506-16	2000	CONCLUSIONS: Site-directed mutagenesis changed the potency and the heparin dependency on cellular proliferation of FGF-1 in vitro.	Heparin	67-74	fibroblast growth factor 1	Homo sapiens	115-120
10739395-7	2000	When protamine sulphate was added to PRP containing heparin, even at clinically relevant neutralizing doses the GPIb-vWF activity was reduced by 20-30% (p &lt; 0.001).	Heparin	52-59	von Willebrand factor	Homo sapiens	117-120
10636879-6	2000	Intracellular heparin inhibited responses to carbachol and PTH, and pretreatment with ATP and carbachol abolished responses to PTH, suggesting that the effects of PTH involve inositol trisphosphate (IP(3)) receptors.	Heparin	14-21	parathyroid hormone	Homo sapiens	59-62
10623810-3	2000	Vanadate-induced Ca2+ signaling was blocked by heparin, a competitive inhibitor of the 1,4, 5-inositol trisphosphate (IP3) receptor, suggesting that Ca2+ influx is secondary to depletion of IP3-sensitive Ca2+ stores.	Heparin	47-54	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	118-131
10667601-3	2000	Adhesion of SCLC cells on TSP1 was inhibited by heparin, function-blocking antibodies recognizing alpha3 or beta1 integrin subunits, and by soluble alpha3beta1 integrin ligands.	Heparin	48-55	thrombospondin 1	Homo sapiens	26-30
10625611-4	2000	Regardless of the amino acids, Hir(52-65) decreased, and heparin increased the k(cat)/K(m) value of hydrolysis by thrombin.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	114-122
10728372-10	2000	Although induction of c-fos by serum is thought to signal through the Erk mitogen activated protein kinase family, Erk activity was decreased more by 1 microgram/ml heparin in A10 cells than in PAC-1 or ASMC.	Heparin	165-172	Eph receptor B1	Rattus norvegicus	115-118
10728372-14	2000	Although Erk is implicated in c-fos induction, cells comparatively resistant to heparin still show heparin-dependent inhibition of Erk activation, suggesting that other pathways may be more important for heparin resistance.	Heparin	80-87	Eph receptor B1	Rattus norvegicus	131-134
10625498-1	2000	The C-terminal domain of human extracellular superoxide dismutase (hEC-SOD) plays a crucial role in the protein"s interaction with heparin.	Heparin	131-138	superoxide dismutase 3	Homo sapiens	67-74
10625498-2	2000	Here we investigated this interaction in more detail by comparing the heparin-binding characteristics of two variants of hEC-SOD: the two fusion proteins containing the hEC-SOD C-terminal domain and a synthetic peptide homologous to the C-terminal.	Heparin	70-77	superoxide dismutase 3	Homo sapiens	121-128
10728372-14	2000	Although Erk is implicated in c-fos induction, cells comparatively resistant to heparin still show heparin-dependent inhibition of Erk activation, suggesting that other pathways may be more important for heparin resistance.	Heparin	99-106	Eph receptor B1	Rattus norvegicus	131-134
10728372-14	2000	Although Erk is implicated in c-fos induction, cells comparatively resistant to heparin still show heparin-dependent inhibition of Erk activation, suggesting that other pathways may be more important for heparin resistance.	Heparin	99-106	Eph receptor B1	Rattus norvegicus	131-134
10625498-6	2000	Comparison of affinities for size-fractionated heparins revealed that octa- or decasaccharides are the smallest heparin fragments that can efficiently interact with the C-terminal domain of hEC-SOD.	Heparin	47-55	superoxide dismutase 3	Homo sapiens	190-197
10681038-8	2000	Optimal binding and elution conditions were developed with knowledge of the dependence of rh-bFGF adsorption isotherms on the salt concentration to allow direct application of eluates onto Heparin HyperD.	Heparin	189-196	fibroblast growth factor 2	Homo sapiens	93-97
10625498-6	2000	Comparison of affinities for size-fractionated heparins revealed that octa- or decasaccharides are the smallest heparin fragments that can efficiently interact with the C-terminal domain of hEC-SOD.	Heparin	47-54	superoxide dismutase 3	Homo sapiens	190-197
10625498-7	2000	At physiological salt concentration, and pH 7.4, the hEC-SOD/heparin interaction was found to be of a high-affinity type, with an equilibrium dissociation constant, K(d), of 0.12 microM, which is 700 and 10-20 times lower than the K(d) values for the synthetic peptide and the fusion proteins, respectively.	Heparin	61-68	superoxide dismutase 3	Homo sapiens	53-60
10625498-10	2000	The hEC-SOD/heparin interaction itself was found to have a fairly high dissociation rate constant (0.1 s(-)(1)), and a very high association rate constant (8 x 10(5) M(-)(1) s(-)(1)), suggesting that the interaction is mainly controlled by the association.	Heparin	12-19	superoxide dismutase 3	Homo sapiens	4-11
10625498-11	2000	These results together with circular dichroism spectra of the synthetic peptide suggest that an alpha-helical structure in the C-terminal is essential for optimal binding to heparin and that other parts of hEC-SOD moderate the affinity.	Heparin	174-181	superoxide dismutase 3	Homo sapiens	206-213
11741223-5	2000	Compared with tPA, mtPA showed much stronger heparin affinity, and the heparin/mtPA complex was stable in human plasma.	Heparin	45-52	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	19-23
11741223-5	2000	Compared with tPA, mtPA showed much stronger heparin affinity, and the heparin/mtPA complex was stable in human plasma.	Heparin	71-78	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	19-23
11741223-5	2000	Compared with tPA, mtPA showed much stronger heparin affinity, and the heparin/mtPA complex was stable in human plasma.	Heparin	71-78	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	79-83
11741223-6	2000	The activity of mtPA in such a complex was inhibited by heparin, and, unlike tPA, the heparin/mtPA complex did not cause statistically meaningful depletion of plasminogen, fibrinogen, and alpha2-antiplasmin in plasma.	Heparin	56-63	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	16-20
11741223-6	2000	The activity of mtPA in such a complex was inhibited by heparin, and, unlike tPA, the heparin/mtPA complex did not cause statistically meaningful depletion of plasminogen, fibrinogen, and alpha2-antiplasmin in plasma.	Heparin	86-93	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	16-20
11741223-7	2000	Using the chromogenic and the in vitro clot lysis assay, it was demonstrated that the heparin-induced inhibition of the mtPA activity was easily reversed following the addition of an adequate amount of protamine.	Heparin	86-93	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	120-124
11741223-8	2000	To enhance the clot-targeting efficiency of the heparin/mtPA complex further, anti-fibrin immunoglobulin (IgG) was conjugated to heparin via an end-point attachment of heparin to the sugar moieties in the Fc region of the IgG.	Heparin	48-55	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	56-60
11741223-8	2000	To enhance the clot-targeting efficiency of the heparin/mtPA complex further, anti-fibrin immunoglobulin (IgG) was conjugated to heparin via an end-point attachment of heparin to the sugar moieties in the Fc region of the IgG.	Heparin	129-136	hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha	Homo sapiens	56-60
10645795-2	2000	Many growth factors, notably the fibroblast growth family (FGF) which now numbers 19 members, bind to heparin and heparan sulfate proteoglycans and this binding has been shown to have a significant impact on the availability and activity of these growth factors.	Heparin	102-109	fibroblast growth factor 2	Bos taurus	59-62
10949652-4	2000	FGF2 is a Mr 18,000 heparin-binding cationic polypeptide that induces proliferation, migration, and protease production in endothelial cells in culture and neovascularization in vivo.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	0-4
10677157-6	2000	The thrombin-antithrombin III (TAT) content just after CPB in both MHT and DHT was significantly lower in the heparin group than in the ACT group.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	4-12
10634807-1	2000	Apolipoprotein E (apoE) and lipoprotein lipase (LPL), key proteins in the regulation of lipoprotein metabolism, bind with high affinity to heparin and cell-surface heparan sulfate proteoglycan (HSPG).	Heparin	139-146	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	28-46
10634807-1	2000	Apolipoprotein E (apoE) and lipoprotein lipase (LPL), key proteins in the regulation of lipoprotein metabolism, bind with high affinity to heparin and cell-surface heparan sulfate proteoglycan (HSPG).	Heparin	139-146	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	48-51
10634807-1	2000	Apolipoprotein E (apoE) and lipoprotein lipase (LPL), key proteins in the regulation of lipoprotein metabolism, bind with high affinity to heparin and cell-surface heparan sulfate proteoglycan (HSPG).	Heparin	139-146	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	194-198
10677157-8	2000	Furthermore, maintenance of the higher heparin concentration during hypothermic CPB may suppress the activation of the coagulation system via thrombin inhibition.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	142-150
10632394-3	2000	Insulin and heparin co-immobilized PET (PET-I-H) was prepared by the grafting of poly(ethylene oxide) (PEO) on to PET-AA, followed by reaction first with insulin and then heparin.	Heparin	12-19	insulin	Homo sapiens	154-161
10600645-2	2000	Heparin induced FGF dimerization has been suggested to mediate receptor dimerization and activation.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	16-19
10600645-4	2000	These heparin-induced dimers of FGF2 acquire high affinity for receptor binding and are biologically active.	Heparin	6-13	fibroblast growth factor 2	Homo sapiens	32-36
10600645-6	2000	Streptavidin induced FGF2 dimers bind and activate FGF receptors only in the presence of heparin.	Heparin	89-96	fibroblast growth factor 2	Homo sapiens	21-25
10600645-6	2000	Streptavidin induced FGF2 dimers bind and activate FGF receptors only in the presence of heparin.	Heparin	89-96	fibroblast growth factor 2	Homo sapiens	21-24
10600645-8	2000	All these suggest predominant receptor binding and activation by heparin associated FGF2 oligomers.	Heparin	65-72	fibroblast growth factor 2	Homo sapiens	84-88
10600645-10	2000	Direct binding of soluble FGF receptors (FGFRs) to either monomers or dimers of FGF2, immobilized on heparin, confirm the preferred association of FGFRs with dimers of FGF2.	Heparin	101-108	fibroblast growth factor 2	Homo sapiens	26-29
10600645-10	2000	Direct binding of soluble FGF receptors (FGFRs) to either monomers or dimers of FGF2, immobilized on heparin, confirm the preferred association of FGFRs with dimers of FGF2.	Heparin	101-108	fibroblast growth factor 2	Homo sapiens	80-84
10600645-11	2000	Computerized molecular docking predicts a cis-oriented FGF2 dimer, stabilized by heparin, which complies with all the experimental data.	Heparin	81-88	fibroblast growth factor 2	Homo sapiens	55-59
10691099-0	2000	Pharmacologic modulation of thrombin generation associated with human clots by human purified antithrombin alone or in the presence of low molecular weight heparin or unfractionated heparin.	Heparin	156-163	coagulation factor II, thrombin	Homo sapiens	28-36
10691099-0	2000	Pharmacologic modulation of thrombin generation associated with human clots by human purified antithrombin alone or in the presence of low molecular weight heparin or unfractionated heparin.	Heparin	182-189	coagulation factor II, thrombin	Homo sapiens	28-36
10691099-2	2000	We investigate the inhibition of clot-associated factor Xa and thrombin activities by purified human antithrombin either alone or as combination with a low molecular weight heparin (enoxaparin) as compared with unfractionated heparin (UFH).	Heparin	173-180	coagulation factor II, thrombin	Homo sapiens	63-71
10632394-3	2000	Insulin and heparin co-immobilized PET (PET-I-H) was prepared by the grafting of poly(ethylene oxide) (PEO) on to PET-AA, followed by reaction first with insulin and then heparin.	Heparin	171-178	insulin	Homo sapiens	0-7
10632394-5	2000	The concentration of the heparin (1.23 microg/cm2) bound to the PEO-grafted PET (PET-PEO) was higher than that (0.77 microg/cm2) on the insulin-immobilized PET (PET-In).	Heparin	25-32	insulin	Homo sapiens	136-143
10600521-1	1999	Heparin affin regulatory peptide (HARP), also called pleiotrophin (PTN), is a secreted polypeptide which binds to heparin and plays a key role in cellular growth and differentiation.	Heparin	114-121	pleiotrophin	Homo sapiens	0-32
11920189-0	2000	von Willebrand factor binding to heparin in various types of von Willebrand disease.	Heparin	33-40	von Willebrand factor	Homo sapiens	0-21
11920189-1	2000	INTRODUCTION: The purpose was to study von Willebrand factor (vWF) binding to heparin in different types of von Willebrand disease (vWD).	Heparin	78-85	von Willebrand factor	Homo sapiens	39-60
11920189-1	2000	INTRODUCTION: The purpose was to study von Willebrand factor (vWF) binding to heparin in different types of von Willebrand disease (vWD).	Heparin	78-85	von Willebrand factor	Homo sapiens	62-65
11920189-4	2000	We determined the range of vWF concentrations in plasma where the percentage of (125)I-MAb/vWF complexes bound to heparin-agarose beads was constant.	Heparin	114-121	von Willebrand factor	Homo sapiens	27-30
11920189-4	2000	We determined the range of vWF concentrations in plasma where the percentage of (125)I-MAb/vWF complexes bound to heparin-agarose beads was constant.	Heparin	114-121	von Willebrand factor	Homo sapiens	91-94
11920189-6	2000	RESULTS: The multimeric composition of vWF had hardly any influence on the ability of vWF to bind to heparin.	Heparin	101-108	von Willebrand factor	Homo sapiens	86-89
11920189-10	2000	Furthermore, when comparing the mean values of plasma vWF-heparin binding ratios by ANOVA F-test in the six groups (one normal and five vWD), we found significant differences between them (P&lt;0.0001).	Heparin	58-65	von Willebrand factor	Homo sapiens	54-57
11920189-12	2000	CONCLUSION: Our data suggest a relationship between the ability of vWF to bind to heparin and to the platelet GPIb receptor, since type 2B and 2N patients have an increased or normal ability to bind to GPIb whereas type 2A and 2M patients have an impaired interaction with that receptor.	Heparin	82-89	von Willebrand factor	Homo sapiens	67-70
16232878-6	2000	The renatured midkine was recovered using a SP-Sepharose column, and purified further by Heparin-Sepharose column chromatography.	Heparin	89-96	midkine	Homo sapiens	14-21
10714610-8	2000	Furthermore, glycosaminoglycans with a sulfate residue, chondroitin sulfate B and C (each 10 microg/mL) also inhibited the binding of 125I-bFGF The in vivo transcytosis of 125I-bFGF from the luminal side to the brain was also inhibited by the presence of heparin (10 microg/mL) and poly-L-lysine (300 microM), whereas neither hyaruronic acid (10 microg/mL) nor insulin (10 microM) had any effect.	Heparin	255-262	fibroblast growth factor 2	Bos taurus	139-143
10816058-0	2000	Heparin-coated cardiopulmonary bypass circuits reduce circulating complement factors and interleukin-6 in paediatric heart surgery.	Heparin	0-7	interleukin 6	Homo sapiens	89-102
10593896-1	1999	The keratinocyte growth factor (KGF or FGF-7) is unique among its family members both in its target cell specificity and its inhibition by the addition of heparin and the native heparan-sulfate proteoglycan (HSPG), glypican-1 in cells expressing endogenous HSPGs.	Heparin	155-162	fibroblast growth factor 7	Homo sapiens	32-35
10593896-1	1999	The keratinocyte growth factor (KGF or FGF-7) is unique among its family members both in its target cell specificity and its inhibition by the addition of heparin and the native heparan-sulfate proteoglycan (HSPG), glypican-1 in cells expressing endogenous HSPGs.	Heparin	155-162	fibroblast growth factor 7	Homo sapiens	39-44
10593896-3	1999	In the present study, we investigated the modulation of FGF-7 activities by heparin and glypican-1 in HS-free background utilizing either HS-deficient cells expressing the FGF-7 receptor (designated BaF/KGFR cells) or soluble extracellular domain of the receptor.	Heparin	76-83	fibroblast growth factor 7	Homo sapiens	56-61
10593896-4	1999	At physiological concentrations of FGF-7, heparin was required for high affinity receptor binding and for signaling in BaF/KGFR cells.	Heparin	42-49	fibroblast growth factor 7	Homo sapiens	35-40
10593896-4	1999	At physiological concentrations of FGF-7, heparin was required for high affinity receptor binding and for signaling in BaF/KGFR cells.	Heparin	42-49	BAF nuclear assembly factor 1	Homo sapiens	119-122
10593896-6	1999	However, high concentrations of heparin inhibited the binding of FGF-7 to both the cell surface and the soluble receptor, similar to the reported effect of heparin in cells expressing endogenous HSPGs.	Heparin	32-39	fibroblast growth factor 7	Homo sapiens	65-70
10593896-6	1999	However, high concentrations of heparin inhibited the binding of FGF-7 to both the cell surface and the soluble receptor, similar to the reported effect of heparin in cells expressing endogenous HSPGs.	Heparin	156-163	fibroblast growth factor 7	Homo sapiens	65-70
12044223-9	2000	Heparin, even in concentrations as low as 2.0 microg/mL, significantly inhibited transduction of CFU on FN-fragments.	Heparin	0-7	fibronectin 1	Homo sapiens	104-106
10765057-6	2000	Two-dimensional gel electrophoretic analysis of the heparin-Mn(2+)-precipitable lipoprotein fraction in CSFs showed that the ratio between the level of CSF apoA-I and that of CSF apoE of controls was significantly higher than those of all AD and LOAD subjects (p < 0.01, p < 0.05), while the CSF apoA-I-to-apoE ratios of the two AD groups were not significantly different.	Heparin	52-59	apolipoprotein A1	Homo sapiens	156-162
10765057-6	2000	Two-dimensional gel electrophoretic analysis of the heparin-Mn(2+)-precipitable lipoprotein fraction in CSFs showed that the ratio between the level of CSF apoA-I and that of CSF apoE of controls was significantly higher than those of all AD and LOAD subjects (p < 0.01, p < 0.05), while the CSF apoA-I-to-apoE ratios of the two AD groups were not significantly different.	Heparin	52-59	apolipoprotein E	Homo sapiens	179-183
10765057-6	2000	Two-dimensional gel electrophoretic analysis of the heparin-Mn(2+)-precipitable lipoprotein fraction in CSFs showed that the ratio between the level of CSF apoA-I and that of CSF apoE of controls was significantly higher than those of all AD and LOAD subjects (p < 0.01, p < 0.05), while the CSF apoA-I-to-apoE ratios of the two AD groups were not significantly different.	Heparin	52-59	apolipoprotein A1	Homo sapiens	296-302
10765057-6	2000	Two-dimensional gel electrophoretic analysis of the heparin-Mn(2+)-precipitable lipoprotein fraction in CSFs showed that the ratio between the level of CSF apoA-I and that of CSF apoE of controls was significantly higher than those of all AD and LOAD subjects (p < 0.01, p < 0.05), while the CSF apoA-I-to-apoE ratios of the two AD groups were not significantly different.	Heparin	52-59	apolipoprotein E	Homo sapiens	306-310
10965219-4	2000	In experiment 1, total cholesterol, triglyceride, adipose tissue weight, and LPL activity of post-heparin plasma were measured in ovariectomized female rats with and without tamoxifen treatment.	Heparin	98-105	lipoprotein lipase	Rattus norvegicus	77-80
10651945-1	2000	We have found previously that disaccharides (DS) enzymatically generated from heparin or heparan sulphate can modulate tumour necrosis factor-alpha (TNF-alpha) secretion from immune cells in vitro and cell-mediated immune reactions in vivo.	Heparin	78-85	tumor necrosis factor	Homo sapiens	149-158
10651945-3	2000	We found that certain heparin- and heparan sulphate-derived DS induced, in a dose-dependent manner, the adhesion of human T cells to both extracellular matrix (ECM) and immobilized fibronectin (FN); maximal T-cell adhesion occurred with 1 ng/ml of DS.	Heparin	22-29	fibronectin 1	Homo sapiens	181-192
10651945-3	2000	We found that certain heparin- and heparan sulphate-derived DS induced, in a dose-dependent manner, the adhesion of human T cells to both extracellular matrix (ECM) and immobilized fibronectin (FN); maximal T-cell adhesion occurred with 1 ng/ml of DS.	Heparin	22-29	fibronectin 1	Homo sapiens	194-196
10793628-7	2000	The presence of heparin reduced the uptake of cholesteryl ester from apolipoprotein E vesicles but not with apolipoprotein A-I vesicles, indicating that uptake of apolipoprotein A-I vesicles via a secretion of apolipoprotein E by the cells themselves was not involved.	Heparin	16-23	apolipoprotein E	Rattus norvegicus	69-85
10793628-7	2000	The presence of heparin reduced the uptake of cholesteryl ester from apolipoprotein E vesicles but not with apolipoprotein A-I vesicles, indicating that uptake of apolipoprotein A-I vesicles via a secretion of apolipoprotein E by the cells themselves was not involved.	Heparin	16-23	apolipoprotein E	Rattus norvegicus	210-226
10593896-9	1999	Glypican-1 abrogated the stimulatory effect of heparin, and heparin reversed the inhibitory effect of glypican-1, indicating that this HSPG inhibits FGF-7 activities by acting, most likely, as a competitive inhibitor of stimulatory HSPG species for FGF-7.	Heparin	47-54	fibroblast growth factor 7	Homo sapiens	149-154
10593896-9	1999	Glypican-1 abrogated the stimulatory effect of heparin, and heparin reversed the inhibitory effect of glypican-1, indicating that this HSPG inhibits FGF-7 activities by acting, most likely, as a competitive inhibitor of stimulatory HSPG species for FGF-7.	Heparin	60-67	fibroblast growth factor 7	Homo sapiens	149-154
10593896-11	1999	The effect of heparin and glypican-1 on FGF-1 and FGF-7 oligomerization was studied employing high and physiological concentrations of growth factors.	Heparin	14-21	fibroblast growth factor 7	Homo sapiens	50-55
10600606-5	1999	Heparin and mannan also inhibit SDF-1alpha binding to intact CD4(+) CXCR4(+/-) cells, and electroblotted soluble CD4.	Heparin	0-7	CD4 molecule	Homo sapiens	61-64
10590063-0	1999	Modulation by heparin of the interaction of the A1 domain of Von Willebrand factor with glycoprotein Ib.	Heparin	14-21	von Willebrand factor	Homo sapiens	61-82
10590063-6	1999	Using monoclonal antibodies blocking vWF interaction with GPIb/V/IX or mocarhagin, a venom metalloproteinase that removes the amino-terminal fragment of GPIbalpha extending from aa 1 to 282, we demonstrated that both ristocetin- and heparin-induced aggregations involved an interaction between the A1 domain of vWF and the GPIbalpha subunit of the GPIb/V/IX complex.	Heparin	233-240	von Willebrand factor	Homo sapiens	37-40
10600521-1	1999	Heparin affin regulatory peptide (HARP), also called pleiotrophin (PTN), is a secreted polypeptide which binds to heparin and plays a key role in cellular growth and differentiation.	Heparin	114-121	pleiotrophin	Homo sapiens	34-38
10590063-8	1999	These results indicated that heparin was able to induce vWF-dependent CHO-GPIbalphabeta/IX cell aggregation.	Heparin	29-36	von Willebrand factor	Homo sapiens	56-59
10590063-9	1999	In conclusion, we demonstrated that heparin is capable of positively modulating the vWF interaction with the GPIb/V/IX complex.	Heparin	36-43	von Willebrand factor	Homo sapiens	84-87
10600521-1	1999	Heparin affin regulatory peptide (HARP), also called pleiotrophin (PTN), is a secreted polypeptide which binds to heparin and plays a key role in cellular growth and differentiation.	Heparin	114-121	pleiotrophin	Homo sapiens	53-65
10600521-1	1999	Heparin affin regulatory peptide (HARP), also called pleiotrophin (PTN), is a secreted polypeptide which binds to heparin and plays a key role in cellular growth and differentiation.	Heparin	114-121	pleiotrophin	Homo sapiens	67-70
10577460-0	1999	Effectiveness of heparin in preventing thrombin generation and thrombin activity in patients undergoing coronary intervention.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	39-47
10574913-7	1999	Ser(670) is located in a peptide sequence that conforms to an ERK consensus phosphorylation sequence, and in vitro, in the presence of heparin, ERK1 phosphorylates GRK2.	Heparin	135-142	mitogen-activated protein kinase 1	Homo sapiens	62-65
10574913-7	1999	Ser(670) is located in a peptide sequence that conforms to an ERK consensus phosphorylation sequence, and in vitro, in the presence of heparin, ERK1 phosphorylates GRK2.	Heparin	135-142	mitogen-activated protein kinase 3	Homo sapiens	144-148
10574913-7	1999	Ser(670) is located in a peptide sequence that conforms to an ERK consensus phosphorylation sequence, and in vitro, in the presence of heparin, ERK1 phosphorylates GRK2.	Heparin	135-142	G protein-coupled receptor kinase 2	Homo sapiens	164-168
10574918-3	1999	Thrombin inhibition by rHCII-CHis(6) was increased &gt;2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	0-8
10574918-3	1999	Thrombin inhibition by rHCII-CHis(6) was increased &gt;2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	0-8
10577460-0	1999	Effectiveness of heparin in preventing thrombin generation and thrombin activity in patients undergoing coronary intervention.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	63-71
10577463-2	1999	Antithrombin therapy with unfractionated heparin has several important disadvantages, such as a variable anticoagulant effect, sensitivity to platelet factor 4, an inability to inhibit clot-bound thrombin, and the potential to cause thrombocytopenia.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	4-12
10607857-10	1999	HepArrest binds low molecular weight heparins and causes reversal of anticoagulation by low molecular weight heparins, as determined by activated partial thromboplastin time, thrombin time, or factor Xa neutralization assays.	Heparin	37-45	coagulation factor II, thrombin	Homo sapiens	175-183
10607857-10	1999	HepArrest binds low molecular weight heparins and causes reversal of anticoagulation by low molecular weight heparins, as determined by activated partial thromboplastin time, thrombin time, or factor Xa neutralization assays.	Heparin	109-117	coagulation factor II, thrombin	Homo sapiens	175-183
10570098-1	1999	BACKGROUND: After introducing the specific thrombin inhibitor recombinant hirudin (r-hirudin) into clinical practice in cases of heparin-induced thrombocytopenia (HIT, type II) the possibility of its use as an anticoagulant during haemodialysis treatment in HIT II patients is being discussed more frequently.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	43-51
11096641-1	1999	Inhibition of thrombin and platelets during percutaneous coronary intervention (PCI), using a combination of unfractionated heparin and aspirin, is designed primarily to minimize the rare but devastating potential acute thrombotic complications of the procedure.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	14-22
10569765-7	1999	Stimulation with a mixture of HlpA and heparin resulted in reduced cytokine production (50% less IL-1 and 76% less TNF-alpha) compared to that by cells incubated with HlpA alone.	Heparin	39-46	tumor necrosis factor	Mus musculus	115-124
10658376-8	1999	Lower interleukin-6 and tumor necrosis factor-alpha were found immediately after cardiopulmonary bypass (p &lt; 0.05) and a higher mean postbypass oxygenation index was also seen (p &lt; 0.05) in the heparin-bonded group.	Heparin	200-207	interleukin 6	Homo sapiens	6-51
10669049-1	1999	Chymase is a chymotrypsin-like protease localized in mast cells in complexes with heparin.	Heparin	82-89	chymase 1	Homo sapiens	0-7
10669049-4	1999	It was observed that suramin competed with heparin-Sepharose gel for binding to chymase and the inhibition of chymase activity by suramin was partially impaired by heparin.	Heparin	43-50	chymase 1	Homo sapiens	80-87
10669049-4	1999	It was observed that suramin competed with heparin-Sepharose gel for binding to chymase and the inhibition of chymase activity by suramin was partially impaired by heparin.	Heparin	43-50	chymase 1	Homo sapiens	110-117
10669049-4	1999	It was observed that suramin competed with heparin-Sepharose gel for binding to chymase and the inhibition of chymase activity by suramin was partially impaired by heparin.	Heparin	164-171	chymase 1	Homo sapiens	80-87
10669049-4	1999	It was observed that suramin competed with heparin-Sepharose gel for binding to chymase and the inhibition of chymase activity by suramin was partially impaired by heparin.	Heparin	164-171	chymase 1	Homo sapiens	110-117
10600487-4	1999	Heparin, an inhibitor of VSMC proliferation, inhibited the serum-induced loss of caveolin-1 and caveolin-2.	Heparin	0-7	caveolin 1	Homo sapiens	81-91
10605952-0	1999	The binding of unfractionated heparin and low molecular weight heparin to thrombin-activated human endothelial cells.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	74-82
10605952-0	1999	The binding of unfractionated heparin and low molecular weight heparin to thrombin-activated human endothelial cells.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	74-82
10605952-2	1999	Thrombin can induce endothelial cells to express and/or secrete a number of heparin binding proteins that have the potential to increase the binding of unfractionated heparin and to a lesser extent the binding of low molecular weight heparin.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	0-8
10605952-2	1999	Thrombin can induce endothelial cells to express and/or secrete a number of heparin binding proteins that have the potential to increase the binding of unfractionated heparin and to a lesser extent the binding of low molecular weight heparin.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	0-8
10605952-3	1999	To explore this possibility, we examined the binding of unfractionated heparin and low molecular weight heparin to thrombin-activated endothelial cells.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	115-123
10605952-3	1999	To explore this possibility, we examined the binding of unfractionated heparin and low molecular weight heparin to thrombin-activated endothelial cells.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	115-123
10605952-4	1999	Cultured human umbilical vein endothelial cells were used to determine the binding of 125I-labeled unfractionated heparin and low molecular weight heparin to untreated and to thrombin-activated cells.	Heparin	147-154	coagulation factor II, thrombin	Homo sapiens	175-183
10605952-5	1999	After thrombin treatment, we obtained a time-dependent increase in the binding of radio-labeled unfractionated heparin.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	6-14
10605952-7	1999	After 30, 45, and 60 minutes of thrombin treatment, the binding of unfractionated heparin was significantly higher than that of low molecular weight heparin.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	32-40
10605952-7	1999	After 30, 45, and 60 minutes of thrombin treatment, the binding of unfractionated heparin was significantly higher than that of low molecular weight heparin.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	32-40
10605952-8	1999	The increase in binding of unfractionated heparin to thrombin-activated cells also was demonstrated using fluorescently labeled unfractionated heparin followed by fluorescence microscopy.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	53-61
10605952-8	1999	The increase in binding of unfractionated heparin to thrombin-activated cells also was demonstrated using fluorescently labeled unfractionated heparin followed by fluorescence microscopy.	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	53-61
10605952-10	1999	The present results indicate that thrombin can increase the binding of unfractionated heparin to human umbilical vein endothelial cells.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	34-42
10600487-5	1999	In addition, heparin caused an increase in both caveolin-1 and caveolin-2 localization to caveolae-enriched sucrose gradient membrane fractions when compared to serum alone.	Heparin	13-20	caveolin 1	Homo sapiens	48-58
10545430-2	1999	METHODS AND RESULTS: We conducted a randomized, double-blind, placebo-controlled study of basic fibroblast growth factor (bFGF; 10 or 100 microg versus placebo) delivered via sustained-release heparin-alginate microcapsules implanted in ischemic and viable but ungraftable myocardial territories in patients undergoing CABG.	Heparin	193-200	fibroblast growth factor 2	Homo sapiens	90-120
10630893-3	1999	By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P.	Heparin	67-74	selenoprotein P	Homo sapiens	166-181
10544000-0	1999	The fourth immunoglobulin-like loop in the extracellular domain of FLT-1, a VEGF receptor, includes a major heparin-binding site.	Heparin	108-115	fms related receptor tyrosine kinase 1	Homo sapiens	67-72
10544000-0	1999	The fourth immunoglobulin-like loop in the extracellular domain of FLT-1, a VEGF receptor, includes a major heparin-binding site.	Heparin	108-115	vascular endothelial growth factor A	Homo sapiens	76-80
10544000-1	1999	We found that heparin at low concentrations increases the vascular endothelial growth factor (VEGF)-induced proliferation of human umbilical vein endothelial cells (HUVECs) but at high concentrations decreases it.	Heparin	14-21	vascular endothelial growth factor A	Homo sapiens	58-92
10544000-1	1999	We found that heparin at low concentrations increases the vascular endothelial growth factor (VEGF)-induced proliferation of human umbilical vein endothelial cells (HUVECs) but at high concentrations decreases it.	Heparin	14-21	vascular endothelial growth factor A	Homo sapiens	94-98
10544000-6	1999	We thus concluded that the fourth Ig-like loop of FLT-1 is a major heparin-binding site and divalent cations are not involved in the interaction of FLT-1 and heparin.	Heparin	67-74	fms related receptor tyrosine kinase 1	Homo sapiens	50-55
10545182-4	1999	Heparin and VN accelerated the second-order association rate constant [k(2) = (7.9 +/- 0.5) x 10(2) M(-)(1) s(-)(1)] of alpha-thrombin with PAI-1 approximately 200- and approximately 240-fold, respectively.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	126-134
10545182-5	1999	The k(2) value for gamma-thrombin [(7.9 +/- 0.7) x 10(1) M(-)(1) s(-)(1)] was impaired 10-fold, but was enhanced by heparin and VN approximately 280- and approximately 75-fold, respectively.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	25-33
10545182-9	1999	Continuous kinetic analysis as well as competition kinetic studies in the presence of S195A thrombin suggested that the accelerating effect of VN or heparin occurs primarily by lowering the dissociation constant (K(d)) for formation of a noncovalent, Michaelis-type complex.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	92-100
10527629-13	1999	Interestingly enough, RGTA and heparin, which both strongly increased differentiation, reduced the expression of the mu- and m-calpains and slightly increased that of calpain 3 in differentiating cultures.	Heparin	31-38	calpain 3	Rattus norvegicus	167-176
10583162-5	1999	The bFGF binding to normal or transformed keratinocytes in vivo and in vitro was dependent on HS modification, as it was completely eliminated by pretreatment with heparitinase or by blocking with free heparin, whereas chondroitinase had no effect.	Heparin	202-209	fibroblast growth factor 2	Homo sapiens	4-8
10583162-8	1999	This bFGF effect was again completely abolished by heparitinase or free heparin, but not by chondroitinase.	Heparin	72-79	fibroblast growth factor 2	Homo sapiens	5-9
10551684-6	1999	For the thrombin component, several recent trials have shown that lower doses of heparin improve the safety profile of the thrombolytic-antithrombotic regimen.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	8-16
10844403-0	1999	Comparative inhibition of LPS-activated human monocyte-induced thrombin generation by unfractionated heparin and low molecular weight heparins.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	63-71
10844403-0	1999	Comparative inhibition of LPS-activated human monocyte-induced thrombin generation by unfractionated heparin and low molecular weight heparins.	Heparin	134-142	coagulation factor II, thrombin	Homo sapiens	63-71
10844403-2	1999	It is well known that unfractionated heparin and low molecular weight heparins inhibit extrinsic thrombin generation.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	97-105
10844403-2	1999	It is well known that unfractionated heparin and low molecular weight heparins inhibit extrinsic thrombin generation.	Heparin	70-78	coagulation factor II, thrombin	Homo sapiens	97-105
10844403-9	1999	Our results show that unfractionated and low molecular weight heparins potently inhibit monocytic tissue factor induced thrombin generation.	Heparin	62-70	coagulation factor II, thrombin	Homo sapiens	120-128
10521484-9	1999	These results demonstrate that the V and heparin binding domains of FN modulate pp125(FAK) levels and regulate apoptosis through a chondroitin sulfate proteoglycan- and possibly alpha4 integrin-mediated pathway, which triggers a caspase cascade.	Heparin	41-48	fibronectin 1	Homo sapiens	68-70
10531345-5	1999	Both types IIA and V sPLA(2), the AA released by which was efficiently converted to prostaglandin E(2), markedly augmented IL-1-induced expression of cyclooxygenase (COX)-2 in a heparin-sensitive fashion, whereas type X sPLA(2) lacked the ability to augment COX-2 expression, thereby exhibiting the poor prostaglandin E(2)-biosynthetic response unless either of the COX isozymes was forcibly introduced into type X sPLA(2)-expressing cells.	Heparin	178-185	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	150-172
10545950-5	1999	The CACP protein, which has previously been identified as both "megakaryocyte stimulating factor precursor" and "superficial zone protein", contains domains that have homology to somatomedin B, heparin-binding proteins, mucins and haemopexins.	Heparin	194-201	proteoglycan 4	Homo sapiens	4-8
10527820-14	1999	The addition of VEGF increased the motility of the SGHPL-4 cells (P&lt; 0.002); the addition of heparin prevented this VEGF-induced increase in motility.	Heparin	96-103	vascular endothelial growth factor A	Homo sapiens	119-123
10521414-1	1999	We recently showed that thyroglobulin (Tg) is a heparin-binding protein and that heparin inhibits binding of Tg to its endocytic receptor megalin (gp330).	Heparin	48-55	thyroglobulin	Rattus norvegicus	24-37
10510057-0	1999	Heparin inhibits ligand binding to the leukocyte integrin Mac-1 (CD11b/CD18).	Heparin	0-7	integrin subunit beta 2	Homo sapiens	71-75
10510057-2	1999	Recently, it has been described that leukocytes adhere on immobilized heparin mediated by the integrin Mac-1 (CD11b/CD18, alphaMbeta2, or CR3).	Heparin	70-77	integrin subunit beta 2	Homo sapiens	116-120
10512728-0	1999	Heparin differentially regulates the interaction of fibroblast growth factor-4 with FGF receptors 1 and 2.	Heparin	0-7	fibroblast growth factor 4	Homo sapiens	52-78
10512728-1	1999	Fibroblast growth factor-4 (FGF4), like other FGFs, shares a high affinity for the anionic glycosaminoglycans heparin and heparan sulfate (HS), which in turn enhance FGF-receptor (FGFR) binding and activation.	Heparin	110-117	fibroblast growth factor 4	Homo sapiens	0-26
10512728-1	1999	Fibroblast growth factor-4 (FGF4), like other FGFs, shares a high affinity for the anionic glycosaminoglycans heparin and heparan sulfate (HS), which in turn enhance FGF-receptor (FGFR) binding and activation.	Heparin	110-117	fibroblast growth factor 4	Homo sapiens	28-32
10512728-2	1999	Here we demonstrate using a cell free system that, at low concentrations of heparin, FGF4 binds only to FGFR-2, while much higher heparin levels are required for binding to FGFR-1.	Heparin	76-83	fibroblast growth factor 4	Homo sapiens	85-89
10512728-2	1999	Here we demonstrate using a cell free system that, at low concentrations of heparin, FGF4 binds only to FGFR-2, while much higher heparin levels are required for binding to FGFR-1.	Heparin	130-137	fibroblast growth factor receptor 1	Homo sapiens	173-179
10512728-3	1999	Chemical crosslinking of radiolabeled FGF4 to the soluble FGF receptors confirms the preferential formation of FGF4-FGFR-2 complexes under restricted heparin availability, with maximal ligand-receptor interactions at almost 20-fold lower heparin concentrations then those required for the affinity labeling of FGFR-1.	Heparin	150-157	fibroblast growth factor 4	Homo sapiens	38-42
10512728-3	1999	Chemical crosslinking of radiolabeled FGF4 to the soluble FGF receptors confirms the preferential formation of FGF4-FGFR-2 complexes under restricted heparin availability, with maximal ligand-receptor interactions at almost 20-fold lower heparin concentrations then those required for the affinity labeling of FGFR-1.	Heparin	150-157	fibroblast growth factor 4	Homo sapiens	111-115
10512728-3	1999	Chemical crosslinking of radiolabeled FGF4 to the soluble FGF receptors confirms the preferential formation of FGF4-FGFR-2 complexes under restricted heparin availability, with maximal ligand-receptor interactions at almost 20-fold lower heparin concentrations then those required for the affinity labeling of FGFR-1.	Heparin	238-245	fibroblast growth factor 4	Homo sapiens	38-42
10512728-3	1999	Chemical crosslinking of radiolabeled FGF4 to the soluble FGF receptors confirms the preferential formation of FGF4-FGFR-2 complexes under restricted heparin availability, with maximal ligand-receptor interactions at almost 20-fold lower heparin concentrations then those required for the affinity labeling of FGFR-1.	Heparin	238-245	fibroblast growth factor 4	Homo sapiens	111-115
10510057-5	1999	Unfractionated heparin inhibited binding of the soluble ligands fibrinogen, factor X, and iC3b to Mac-1.	Heparin	15-22	fibrinogen beta chain	Homo sapiens	64-74
10510057-6	1999	Adhesion of the monocytic cell line THP-1 and of peripheral monocytes and granulocytes to immobilized ICAM-1 was impaired by unfractionated heparin, to the same extent as with inhibition of Mac-1 by monoclonal antibodies such as c7E3.	Heparin	140-147	GLI family zinc finger 2	Homo sapiens	36-41
10510057-7	1999	Low-molecular-weight heparin also inhibits binding of fibrinogen to Mac-1.	Heparin	21-28	fibrinogen beta chain	Homo sapiens	54-64
10510057-8	1999	Additionally, flow cytometry of whole blood preparations of patients treated with unfractionated heparin revealed an inhibitory effect of heparin on the binding of fibrinogen to Mac-1 that correlates (n= 48, r=0.63, P&lt;0.001) to the extent of prolongation of the activated partial thromboplastin time.	Heparin	97-104	fibrinogen beta chain	Homo sapiens	164-174
10510057-8	1999	Additionally, flow cytometry of whole blood preparations of patients treated with unfractionated heparin revealed an inhibitory effect of heparin on the binding of fibrinogen to Mac-1 that correlates (n= 48, r=0.63, P&lt;0.001) to the extent of prolongation of the activated partial thromboplastin time.	Heparin	138-145	fibrinogen beta chain	Homo sapiens	164-174
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Heparin	166-173	tissue factor pathway inhibitor 2	Homo sapiens	23-56
10496984-11	1999	To determine whether heparin modulates the activity of TFPI-2/MSPI, we determined the rate of inhibition of plasmin by the inhibitor with and without heparin and found that TFPI-2/MSPI is more active in the presence of heparin.	Heparin	150-157	tissue factor pathway inhibitor 2	Homo sapiens	173-179
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Heparin	166-173	tissue factor pathway inhibitor 2	Homo sapiens	102-108
10496984-12	1999	Collectively, our results demonstrate that conformation-dependent arginine-mediated ionic interactions are responsible for the TFPI-2/MSPI triplet binding to fibroblast ECM, heparin, and dermatan sulfate and that heparin augmented the rate of inhibition of plasmin by TFPI-2/MSPI.	Heparin	174-181	tissue factor pathway inhibitor 2	Homo sapiens	127-133
10552212-4	1999	The stimulatory activity was comparable to that of heparin, with affinity to VEGF(165), and decreased on heparin-induced stimulation.	Heparin	51-58	vascular endothelial growth factor A	Homo sapiens	77-81
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Heparin	196-203	tissue factor pathway inhibitor 2	Homo sapiens	23-56
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Heparin	196-203	tissue factor pathway inhibitor 2	Homo sapiens	102-108
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Heparin	196-203	tissue factor pathway inhibitor 2	Homo sapiens	232-238
10496984-5	1999	We found that TFPI-2/MSPI bound specifically to heparin and dermatan sulfate.	Heparin	48-55	tissue factor pathway inhibitor 2	Homo sapiens	14-20
10496984-7	1999	However, binding affinity for TFPI-2/MSPI with heparin was 250-300 times greater than that for TFPI-2/MSPI with dermatan sulfate.	Heparin	47-54	tissue factor pathway inhibitor 2	Homo sapiens	30-36
10496984-11	1999	To determine whether heparin modulates the activity of TFPI-2/MSPI, we determined the rate of inhibition of plasmin by the inhibitor with and without heparin and found that TFPI-2/MSPI is more active in the presence of heparin.	Heparin	21-28	tissue factor pathway inhibitor 2	Homo sapiens	55-61
10496984-11	1999	To determine whether heparin modulates the activity of TFPI-2/MSPI, we determined the rate of inhibition of plasmin by the inhibitor with and without heparin and found that TFPI-2/MSPI is more active in the presence of heparin.	Heparin	21-28	tissue factor pathway inhibitor 2	Homo sapiens	173-179
10493910-11	1999	In addition, heparin, a competitive antagonist of InsP(3)Rs, blocked Ca(2+)-mobilization in permeabilized SH-SY5Y cells in response to MCh or exogenously added Ins(1,4,5)P(3), but failed to inhibit Ca(2+)-release induced by LPA.	Heparin	13-20	pro-melanin concentrating hormone	Homo sapiens	135-138
10496984-11	1999	To determine whether heparin modulates the activity of TFPI-2/MSPI, we determined the rate of inhibition of plasmin by the inhibitor with and without heparin and found that TFPI-2/MSPI is more active in the presence of heparin.	Heparin	150-157	tissue factor pathway inhibitor 2	Homo sapiens	173-179
10726023-1	1999	Argatroban is a peptidomimetic inhibitor of thrombin that is currently undergoing extensive clinical trials as a heparin substitute for thrombotic complications.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	44-52
10726035-7	1999	This study reports on the circulating levels of various adhesion molecules in patients with heparin-induced thrombocytopenia and their modulation after therapeutic interventions by the use of direct thrombin inhibitors.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	199-207
10726037-7	1999	However, a chemical structure that is different from heparin (e.g., a heparinoid or a thrombin inhibitor) will also be nonreactive to platelet activation by heparin-induced thrombocytopenia antibodies.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	86-94
10506571-7	1999	Analysis of the mutant FGF-2 molecules show that reduction in heparin binding interactions and primary receptor site binding interactions can also be compensated for in the same manner.	Heparin	62-69	fibroblast growth factor 2	Homo sapiens	23-28
10504408-6	1999	The phosphodiesterase/pyrophosphatase activity of PC-1 was competitively inhibited by glycosaminoglycans, such as heparin and heparan sulfate, which are the major components of the extracellular matrix.	Heparin	114-121	ectonucleotide pyrophosphatase/phosphodiesterase 1	Homo sapiens	50-54
10504408-7	1999	PC-1 was capable of binding to heparin-Sepharose and the binding was inhibited in the presence of the enzyme substrate, ATP or its nonhydrolyzable analog.	Heparin	31-38	ectonucleotide pyrophosphatase/phosphodiesterase 1	Homo sapiens	0-4
10497166-1	1999	A sequence-specific heparin pentasaccharide activates the serpin, antithrombin, to inhibit factor Xa through an allosteric mechanism, whereas full-length heparin chains containing this sequence further activate the serpin to inhibit thrombin by an alternative bridging mechanism.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	70-78
10520784-0	1999	Thrombin generation after the abrupt cessation of intravenous unfractionated heparin among patients with acute coronary syndromes: potential mechanisms for heightened prothrombotic potential.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	0-8
10520784-7	1999	weaning over 12 h or 3) subcutaneous weaning over 12 h. RESULTS: Thrombin generation (prothrombin fragment 1.2) was evident within 1 h of UFH cessation, increased progressively (by nearly two-fold) at 24 h (p = 0.002) and correlated inversely with tissue factor pathway inhibitor concentration (r = -0.61).	Heparin	138-141	coagulation factor II, thrombin	Homo sapiens	65-73
10521538-3	1999	Heparin bound to type V collagen, type IX collagen, fibronectin, laminin, and vitronectin; and chondroitin sulfate E bound to type II, type V, and type VII collagen.	Heparin	0-7	fibronectin 1	Homo sapiens	52-63
10561907-7	1999	The addition of heparin to cultures stimulated by FGF-1 or FGF-2 resulted in a 2-fold increase in the number of megakaryocyte colonies compared to the culture containing FGF alone.	Heparin	16-23	fibroblast growth factor 1	Homo sapiens	50-55
10561907-7	1999	The addition of heparin to cultures stimulated by FGF-1 or FGF-2 resulted in a 2-fold increase in the number of megakaryocyte colonies compared to the culture containing FGF alone.	Heparin	16-23	fibroblast growth factor 2	Homo sapiens	59-64
10561907-10	1999	The combination of FGF and heparin induced a maximal growth of megakaryocyte colonies from CD34+ cells.	Heparin	27-34	CD34 molecule	Homo sapiens	91-95
10497166-4	1999	Surprisingly, the enhanced thrombin specificity of the mutant antithrombin was attenuated when a full-length bridging heparin was the activator, due both to a reduced rate of covalent reaction of the mutant serpin and thrombin and preferred reaction of the mutant serpin as a substrate.	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	27-35
10497166-4	1999	Surprisingly, the enhanced thrombin specificity of the mutant antithrombin was attenuated when a full-length bridging heparin was the activator, due both to a reduced rate of covalent reaction of the mutant serpin and thrombin and preferred reaction of the mutant serpin as a substrate.	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	66-74
10497166-5	1999	These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex.	Heparin	282-289	coagulation factor II, thrombin	Homo sapiens	124-132
10497195-7	1999	Larger doses of EGF or heparin-binding EGF induced only weak tyrosine phosphorylation of mt25, whereas the response to transforming growth factor-alpha was undetectable.	Heparin	23-30	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	39-42
10589445-2	1999	In this model, chylomicrons and very low density lipoprotein (VLDL) accumulation was known to occur as a result of reduction in lipoprotein lipase (LPL) activity in the heart and heparin-releasable heart LPL.	Heparin	179-186	lipoprotein lipase	Rattus norvegicus	204-207
10511129-6	1999	The phospholipase C inhibitors, D-609, NCDC, or U73122, and the IP3 receptor blocker, heparin, abolished the [Ca2+]i response to AVP.	Heparin	86-93	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	64-76
10511129-6	1999	The phospholipase C inhibitors, D-609, NCDC, or U73122, and the IP3 receptor blocker, heparin, abolished the [Ca2+]i response to AVP.	Heparin	86-93	arginine vasopressin	Rattus norvegicus	129-132
10490955-9	1999	This TSP1 peptide-dependent activation of AP-1 was inhibited by both heparin and the MAP/ERK kinase inhibitor PD98059, providing a functional link between adhesion molecule interaction and nuclear transactivation events via the MAP kinase pathways.	Heparin	69-76	thrombospondin 1	Homo sapiens	5-9
10497080-1	1999	Large amounts of soluble fibronectin were easily purified from cryoprecipitated or fresh citrated human blood plasma by a three-step combination of gelatin and heparin-cellufine affinity chromatography.	Heparin	160-167	fibronectin 1	Homo sapiens	25-36
10480945-8	1999	The interaction of cells with the heparin-binding domain of vitronectin resulted in changes in actin microfilament organization and the subcellular distribution of the actin-associated proteins alpha-actinin and talin.	Heparin	34-41	actinin alpha 1	Homo sapiens	194-217
10544908-3	1999	Our aim was to explore the effect of inhibiting both plasmin action with tranexamic acid (TA) and thrombin production with low molecular weight heparin (LMWH), on the bleeding time (BT) and platelet function in patients with CRF.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	98-106
10488098-0	1999	Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	66-74
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	153-161
10581995-4	1999	Thrombotic complications of heparin-induced thrombocytopenia are prevented and treated by direct thrombin inhibitors or danaparoid.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	97-105
10504268-8	1999	Isothermal titration calorimetry data confirm these results; IL-8 binds heparin fragments with a K(d) of 0.39-2.63 microM, and requires five saccharide units to bind each monomer of chemokine.	Heparin	72-79	C-X-C motif chemokine ligand 8	Homo sapiens	61-65
10504268-10	1999	Consistent with this, heparin and heparin sulfate could inhibit IL-8-induced neutrophil calcium flux.	Heparin	22-29	C-X-C motif chemokine ligand 8	Homo sapiens	64-68
10480945-9	1999	These data suggest a mechanism whereby the heparin-binding domain of vitronectin regulates the deposition of fibronectin into the extracellular matrix through alterations in the organization of the actin cytoskeleton.	Heparin	43-50	fibronectin 1	Homo sapiens	109-120
10478144-6	1999	Because syndecan-1 interacts with heparin-binding growth factors such as FGF-2, accumulation of syndecan-1 within the tumor stroma may contribute to the extensive angiogenesis and stromal proliferation characteristic of infiltrating breast carcinoma.	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	73-78
10505536-7	1999	The principal biophysical limitation of heparins, however, is that they cannot inactivate clot-bound thrombin, which probably contributes to morbidity and mortality in acute coronary syndromes.	Heparin	40-48	coagulation factor II, thrombin	Homo sapiens	101-109
10505540-1	1999	Although unfractionated heparin is widely used for thrombin inhibition in the management of unstable coronary artery disease, clinical and experimental evidence suggests that it is suboptimal.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	51-59
10508424-3	1999	The tight binding of chymase to heparin PG results in increased activity of the protease toward certain substrates, e.g., thrombin and MeO-Suc-Arg-Pro-Tyr-pNA (S-2586).	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	122-130
10508424-4	1999	In this study, the mechanism by which heparin PG modulates chymase activity was investigated, using thrombin and various chromogenic peptide substrates as model substrates.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	100-108
10508424-5	1999	Incubation of thrombin with oligonucleotides that block the heparin-binding site of thrombin abolished the stimulatory effect of heparin PG on thrombin inactivation.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	14-22
10508424-5	1999	Incubation of thrombin with oligonucleotides that block the heparin-binding site of thrombin abolished the stimulatory effect of heparin PG on thrombin inactivation.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	84-92
10508424-5	1999	Incubation of thrombin with oligonucleotides that block the heparin-binding site of thrombin abolished the stimulatory effect of heparin PG on thrombin inactivation.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	84-92
10508424-5	1999	Incubation of thrombin with oligonucleotides that block the heparin-binding site of thrombin abolished the stimulatory effect of heparin PG on thrombin inactivation.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	14-22
10508424-5	1999	Incubation of thrombin with oligonucleotides that block the heparin-binding site of thrombin abolished the stimulatory effect of heparin PG on thrombin inactivation.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	84-92
10508424-5	1999	Incubation of thrombin with oligonucleotides that block the heparin-binding site of thrombin abolished the stimulatory effect of heparin PG on thrombin inactivation.	Heparin	129-136	coagulation factor II, thrombin	Homo sapiens	84-92
10475283-8	1999	The adsorption of platelet adhesive proteins such as fibrinogen and von Willebrand factor was not altered, whereas that of fibronectin was increased by heparin coating.	Heparin	152-159	fibronectin 1	Homo sapiens	123-134
10484460-2	1999	Three peaks of PLA2 activity were identified by heparin-Sepharose chromatography.	Heparin	48-55	phospholipase A2	Ovis aries	15-19
10484460-3	1999	The heparin-nonbinding PLA2 activity was twofold higher in the extracts from lungs exposed to smoke than in normal lungs.	Heparin	4-11	phospholipase A2	Ovis aries	23-27
10484460-5	1999	The activities of the forms of PLA2 that bound to heparin did not change after smoke exposure.	Heparin	50-57	phospholipase A2	Ovis aries	31-35
10484460-8	1999	The other form of lung PLA2 that bound heparin was a group II PLA2.	Heparin	39-46	phospholipase A2	Ovis aries	23-27
10484460-8	1999	The other form of lung PLA2 that bound heparin was a group II PLA2.	Heparin	39-46	phospholipase A2	Ovis aries	62-66
10475283-10	1999	Surface heparin coating is associated with an increased fibronectin adsorption on the fibers.	Heparin	8-15	fibronectin 1	Homo sapiens	56-67
10628351-4	1999	These results show that the heparin-binding domain of bFGF provides an inefficient epitope for in vivo neutralization of anti-bFGF mAb, and anti-bFGF neutralizing mAbs without competition against heparin have the potential to show in vivo antitumor effects.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	54-58
10462449-4	1999	A minor component, TrxR2, the mitochondrial form of TrxR, was detected in the heparin-bound enzyme fraction.	Heparin	78-85	thioredoxin reductase 2	Homo sapiens	19-24
10628351-4	1999	These results show that the heparin-binding domain of bFGF provides an inefficient epitope for in vivo neutralization of anti-bFGF mAb, and anti-bFGF neutralizing mAbs without competition against heparin have the potential to show in vivo antitumor effects.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	126-130
10628351-4	1999	These results show that the heparin-binding domain of bFGF provides an inefficient epitope for in vivo neutralization of anti-bFGF mAb, and anti-bFGF neutralizing mAbs without competition against heparin have the potential to show in vivo antitumor effects.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	126-130
10628351-4	1999	These results show that the heparin-binding domain of bFGF provides an inefficient epitope for in vivo neutralization of anti-bFGF mAb, and anti-bFGF neutralizing mAbs without competition against heparin have the potential to show in vivo antitumor effects.	Heparin	196-203	fibroblast growth factor 2	Homo sapiens	54-58
10493215-5	1999	Plasma levels of bradykinin increased 12-fold during LDL apheresis with heparin, but did not increase during LDL apheresis with nafamostat mesilate.	Heparin	72-79	kininogen 1	Homo sapiens	17-27
10530949-0	1999	Oligosaccharides corresponding to the regular sequence of heparin: chemical synthesis and interaction with FGF-2.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	107-112
10530949-1	1999	It has been proposed that oligosaccharides corresponding to the so-called regular region of heparin/heparan sulfate (HS) bind to fibroblast growth factor-2 (FGF-2).	Heparin	92-99	fibroblast growth factor 2	Homo sapiens	129-155
10530949-1	1999	It has been proposed that oligosaccharides corresponding to the so-called regular region of heparin/heparan sulfate (HS) bind to fibroblast growth factor-2 (FGF-2).	Heparin	92-99	fibroblast growth factor 2	Homo sapiens	157-162
10530949-2	1999	In order to explore the molecular basis of FGF/HS interaction, we describe here the chemical synthesis of a tetra and a hexasaccharide, prepared as methyl glycosides, corresponding to the regular sequence of heparin.	Heparin	208-215	fibroblast growth factor 2	Homo sapiens	43-46
10530949-4	1999	The hexasaccharide inhibited the binding of FGF-2 on its receptor on human aorta vascular smooth muscle cells with an IC50 value (16+/-1.2 microg/mL) close to that of standard heparin (14.8+/-0.5 microg/mL) whereas the tetrasaccharide was much less potent (IC50 = 127+/-10.5 microg/mL).	Heparin	176-183	fibroblast growth factor 2	Homo sapiens	44-49
10530949-5	1999	The hexasaccharide and heparin, inhibited in a dose-dependent manner FGF-2 (30 nM) induced proliferation (IC50 = 23.7+/-1.6 and 30.1+/-1.3 microg/mL, respectively).	Heparin	23-30	fibroblast growth factor 2	Homo sapiens	69-74
10456843-8	1999	The apo E peptide acetyl-Y(141-155)(2)C bound to heparin, a property of LDL receptor ligands, and in this complex the peptide had no effect on androstenedione production.	Heparin	49-56	apolipoprotein E	Rattus norvegicus	4-9
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	54-62
10456887-3	1999	The mechanism involves specific bacterial recruitment of heparin, glycosaminoglycans, or related sulfated polysaccharides, which in turn serve as universal binding sites for a diverse array of mammalian heparin binding proteins, including adhesive glycoproteins (vitronectin and fibronectin), inflammatory (MCP-3, PF-4, and MIP-1alpha) and immunomodulatory (gamma interferon) intermediates, and fibroblast growth factor.	Heparin	57-64	fibronectin 1	Homo sapiens	279-290
10467078-0	1999	Effects of local heparin administration on coronary thrombin activity during percutaneous transluminal coronary angioplasty.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	52-60
10494034-8	1999	All antithrombotics, be it anticoagulants (e.g. OAC, all heparins or hirudin) or antiplatelet drugs (aspirin, GPIIb/IIIa blockers) diminish thrombin generation.	Heparin	57-65	coagulation factor II, thrombin	Homo sapiens	140-148
10596847-0	1999	Increased adsorption of high molecular weight kininogen to heparin-coated artificial surfaces and correlation to hemocompatibility.	Heparin	59-66	kininogen 1	Homo sapiens	24-55
10596847-5	1999	High concentrations of fibrinogen were detected after very short blood material contact, both on uncoated as well as heparin-coated tubes.	Heparin	117-124	fibrinogen beta chain	Homo sapiens	23-33
10596847-6	1999	However, high amounts of HMWK were only found on the heparin-bonded surfaces.	Heparin	53-60	kininogen 1	Homo sapiens	25-29
10596847-8	1999	We presume that adsorption of HMWK to heparin-coated surfaces contributes to the improved hemocompatibility of these bondings.	Heparin	38-45	kininogen 1	Homo sapiens	30-34
10496308-6	1999	Heparin induced IL-12 and interferon-gamma production but did not promote the release of other cytokines.	Heparin	0-7	interferon gamma	Homo sapiens	26-42
10517123-4	1999	A case of congenital afibrinogenemia is described in a patient who suffered from severe bleeding episodes in the absence of replacement therapy but developed a deep vein thrombosis with multiple pulmonary emboli after fibrinogen replacement and surgical treatment of a hip fracture, despite conventional heparin prophylaxis.	Heparin	304-311	fibrinogen beta chain	Homo sapiens	22-32
11721408-0	1999	[Heparin enhances the stimulating effect of thrombopoietin on megakaryocytopoiesis].	Heparin	1-8	thrombopoietin	Homo sapiens	44-58
11721408-4	1999	RESULTS: Heparin could enhance the stimulating effect of Tpo on stimulating the proliferation of M-07e, the growth of CFU-MK from human cord blood CD34+ cells and in vivo megakaryocytopoiesis in mice.	Heparin	9-16	CD34 molecule	Homo sapiens	147-151
10452964-0	1999	Glycation of apolipoprotein E impairs its binding to heparin: identification of the major glycation site.	Heparin	53-60	apolipoprotein E	Homo sapiens	13-29
10452964-5	1999	ApoE from diabetic plasma showed decreased binding to heparin compared to normal plasma apoE.	Heparin	54-61	apolipoprotein E	Homo sapiens	0-4
10432310-1	1999	The ability to separate the isoforms of human tumour suppressor protein p53 expressed in insect cells using heparin-Sepharose correlates with differences in the isoelectric point of p53, demonstrating that p53 can be heterogeneously modified and providing support for the use of insect cells as a model system for identifying novel signalling pathways that target p53.	Heparin	108-115	tumor protein p53	Homo sapiens	72-75
10452964-7	1999	The glycation of apoE in vitro significantly decreased its ability to bind to heparin, a critical process in the sequestration and uptake of apoE-containing lipoproteins by cells.	Heparin	78-85	apolipoprotein E	Homo sapiens	17-21
10452964-7	1999	The glycation of apoE in vitro significantly decreased its ability to bind to heparin, a critical process in the sequestration and uptake of apoE-containing lipoproteins by cells.	Heparin	78-85	apolipoprotein E	Homo sapiens	141-145
10452964-13	1999	These findings suggest that apoE is glycated in an isoform-specific manner and that the glycation, in turn, significantly decreases apoE heparin-binding activity.	Heparin	137-144	apolipoprotein E	Homo sapiens	28-32
10452964-13	1999	These findings suggest that apoE is glycated in an isoform-specific manner and that the glycation, in turn, significantly decreases apoE heparin-binding activity.	Heparin	137-144	apolipoprotein E	Homo sapiens	132-136
10432310-1	1999	The ability to separate the isoforms of human tumour suppressor protein p53 expressed in insect cells using heparin-Sepharose correlates with differences in the isoelectric point of p53, demonstrating that p53 can be heterogeneously modified and providing support for the use of insect cells as a model system for identifying novel signalling pathways that target p53.	Heparin	108-115	tumor protein p53	Homo sapiens	182-185
10432310-1	1999	The ability to separate the isoforms of human tumour suppressor protein p53 expressed in insect cells using heparin-Sepharose correlates with differences in the isoelectric point of p53, demonstrating that p53 can be heterogeneously modified and providing support for the use of insect cells as a model system for identifying novel signalling pathways that target p53.	Heparin	108-115	tumor protein p53	Homo sapiens	182-185
10432310-1	1999	The ability to separate the isoforms of human tumour suppressor protein p53 expressed in insect cells using heparin-Sepharose correlates with differences in the isoelectric point of p53, demonstrating that p53 can be heterogeneously modified and providing support for the use of insect cells as a model system for identifying novel signalling pathways that target p53.	Heparin	108-115	tumor protein p53	Homo sapiens	182-185
10485423-16	1999	However, significantly lower interleukin 8 release and complement activation can be achieved by heparin coating.	Heparin	96-103	C-X-C motif chemokine ligand 8	Homo sapiens	29-42
10441104-2	1999	We studied whether chymase bound to heparin, resembling an in vivo form, could contribute to Ang II formation in the presence of natural protease inhibitors.	Heparin	36-43	chymase 1	Homo sapiens	19-26
10441104-15	1999	CONCLUSIONS: These findings suggest that human chymase bound to heparin plays a functional role in Ang II formation in the presence of natural protease inhibitors such as alpha-antitrypsin.	Heparin	64-71	chymase 1	Homo sapiens	47-54
10413640-18	1999	The level of thrombin inhibition by efegatran, as measured by activated partial thromboplastin time, appeared to be more stable than with heparin.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	13-21
10441378-7	1999	The k(ass) value for inhibition was decreased approximately 10-fold by addition of heparin, a glycosaminoglycan produced by mast cells that binds to chymase.	Heparin	83-90	chymase 1	Homo sapiens	149-156
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	53-61
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	53-61
10480261-6	1999	One of the exceptions was heparin which had an IC50 of 9.6 microg/ml in SupT1 cells and &gt;250 microg/ml in CD4+ T lymphocytes.	Heparin	26-33	CD4 molecule	Homo sapiens	109-112
10543720-4	1999	Diabetes also resulted in lower heparin-releasable (HR) LPL activity compared with control cells (111+/-25 vs. 432+/-63 nmol x h(-1) x mg(-1) cell protein).	Heparin	32-39	lipoprotein lipase	Rattus norvegicus	56-59
10393815-6	1999	In contrast, K27, 30Q/R31Q-FGF2, K128Q/K138Q-FGF2 and R118,129Q/K119,128Q-FGF2 exerted a significant uPA-inducing and morphogenic activity in an ERK1/2-dependent manner only in the presence of heparin.	Heparin	193-200	fibroblast growth factor 2	Bos taurus	27-31
10468245-6	1999	Heparin can reduce the generation of and mediate neutralization of excessive and CPB-associated thrombin activity.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	96-104
10468245-11	1999	Administration of heparin doses higher than those generally recommended, as guided by predetermined, patient-specific whole blood heparin concentration measurements during bypass, can reduce excessive thrombin-mediated consumption of platelets and coagulation factors as well as post-CPB blood loss and blood component transfusions.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	201-209
10468245-11	1999	Administration of heparin doses higher than those generally recommended, as guided by predetermined, patient-specific whole blood heparin concentration measurements during bypass, can reduce excessive thrombin-mediated consumption of platelets and coagulation factors as well as post-CPB blood loss and blood component transfusions.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	201-209
10400721-6	1999	Presence of PE2 was associated with an increase in HS-dependent attachment to cells and efficient attachment to heparin-agarose beads, presumably because the furin recognition site for PE2 cleavage also represents a candidate HS binding sequence.	Heparin	112-119	ETS2 repressor factor	Homo sapiens	12-15
10397725-8	1999	On Western blot analysis, a protein consistent with full-length TFPI (42 kD) was identified in the conditioned media of PASMC, and the levels of the protein were much higher in the conditioned media of serum and bFGF/heparin-treated cells.	Heparin	217-224	fibroblast growth factor 2	Homo sapiens	212-216
10389767-7	1999	These findings were associated with a reduced biological response to bFGF in the carcinoma cells that could be partially reversed by the addition of exogenous heparin, suggesting that both the proteoglycan and signal transducing receptor control the cells" response to bFGF.	Heparin	159-166	fibroblast growth factor 2	Homo sapiens	69-73
10389767-7	1999	These findings were associated with a reduced biological response to bFGF in the carcinoma cells that could be partially reversed by the addition of exogenous heparin, suggesting that both the proteoglycan and signal transducing receptor control the cells" response to bFGF.	Heparin	159-166	fibroblast growth factor 2	Homo sapiens	269-273
10400621-8	1999	Formation of the complex was dependent on cell interaction with the heparin binding region in fibronectin and required IL-1/type I IL-1 receptor binding.	Heparin	68-75	fibronectin 1	Homo sapiens	94-105
10393102-3	1999	This release was Ca2+-dependent and was blocked by antibodies against the RyR or CE, by the RyR inhibitor dantrolene, and by a seven-amino-acid peptide fragment corresponding to positions 4689-4697 of the RyR, but not by heparin, an Ins(1,4,5)P3-receptor antagonist.	Heparin	221-228	ryanodine receptor 2	Homo sapiens	74-77
10413500-0	1999	Site-directed mutagenesis and molecular modeling identify a crucial amino acid in specifying the heparin affinity of FGF-1.	Heparin	97-104	fibroblast growth factor 1	Homo sapiens	117-122
10413500-1	1999	Heparin potentiates the mitogenic activity of FGF-1 by increasing the affinity for its receptor and by extending its biological half-life.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	46-51
10413500-2	1999	During the course of labeling human FGF-1 with Na(125)I and chloramine T, it was observed that the protein lost its ability to bind to heparin.	Heparin	135-142	fibroblast growth factor 1	Homo sapiens	36-41
10413500-5	1999	The results showed that the C-terminal region of human FGF-1 was responsible for the loss of heparin affinity.	Heparin	93-100	fibroblast growth factor 1	Homo sapiens	55-60
10413500-9	1999	In contrast, a mutant human FGF-1 that has cysteine-131 replaced with serine (C131S) was able to bind to heparin even after iodination while bovine FGF-1 (S131C) lost its binding affinity to heparin upon iodination.	Heparin	105-112	fibroblast growth factor 1	Homo sapiens	28-33
10413500-9	1999	In contrast, a mutant human FGF-1 that has cysteine-131 replaced with serine (C131S) was able to bind to heparin even after iodination while bovine FGF-1 (S131C) lost its binding affinity to heparin upon iodination.	Heparin	191-198	fibroblast growth factor 1	Homo sapiens	28-33
10413500-11	1999	Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132.	Heparin	35-42	fibroblast growth factor 1	Homo sapiens	61-66
10397725-11	1999	Cycloheximide, but not actinomycin-D, treatment inhibited the serum and bFGF/heparin-induced increase in TFPI activity in PASMC.	Heparin	77-84	fibroblast growth factor 2	Homo sapiens	72-76
10397733-6	1999	At the same time, the Tat basic sequence retrieves into a soluble form extracellular basic fibroblast growth factor (bFGF) bound to heparan sulfate proteoglycans by competing for heparin-binding sites.	Heparin	179-186	fibroblast growth factor 2	Homo sapiens	117-121
10402474-4	1999	We report here that IP-10 inhibited EGF- and heparin-binding EGF-like growth factor-induced Hs68 human dermal fibroblast motility in a dose-dependent manner (to 52% and 44%, respectively, at 50 ng/ml IP-10), whereas IP-10 had no effect on either basal or EGFR-mediated mitogenesis (96 +/- 15% at 50 ng/ml).	Heparin	45-52	epidermal growth factor receptor	Homo sapiens	255-259
10385763-13	1999	CONCLUSION: Addition of abciximab to heparin plus aspirin during PCI was associated with a significant decrease in thrombin generation and a borderline decrease in thrombin activity.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	115-123
10413105-1	1999	The interaction of heparin with heparin binding growth-associated molecule (HB-GAM) was studied using isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR).	Heparin	19-26	pleiotrophin	Homo sapiens	32-74
10413105-1	1999	The interaction of heparin with heparin binding growth-associated molecule (HB-GAM) was studied using isothermal titration calorimetry (ITC) and surface plasmon resonance (SPR).	Heparin	19-26	pleiotrophin	Homo sapiens	76-82
10413105-2	1999	ITC studies showed that, in solution, heparin bound HB-GAM with a deltaH of -30 kcal/mole corresponding to a dissociation constant (Kd) of 460 nM.	Heparin	38-45	pleiotrophin	Homo sapiens	52-58
10413105-3	1999	The stoichiometry of interaction was 3 moles of HB-GAM per mole of heparin, corresponding to a minimum heparin binding site for HB-GAM of 12-16 saccharide residues.	Heparin	67-74	pleiotrophin	Homo sapiens	48-54
10413105-3	1999	The stoichiometry of interaction was 3 moles of HB-GAM per mole of heparin, corresponding to a minimum heparin binding site for HB-GAM of 12-16 saccharide residues.	Heparin	67-74	pleiotrophin	Homo sapiens	128-134
10413105-3	1999	The stoichiometry of interaction was 3 moles of HB-GAM per mole of heparin, corresponding to a minimum heparin binding site for HB-GAM of 12-16 saccharide residues.	Heparin	103-110	pleiotrophin	Homo sapiens	48-54
10413105-3	1999	The stoichiometry of interaction was 3 moles of HB-GAM per mole of heparin, corresponding to a minimum heparin binding site for HB-GAM of 12-16 saccharide residues.	Heparin	103-110	pleiotrophin	Homo sapiens	128-134
10413105-4	1999	Kinetic measurements of heparin interaction with HB-GAM made by SPR afforded a Kd of 4 nM, suggesting considerably tighter binding when HB-GAM was immobilized on a surface.	Heparin	24-31	pleiotrophin	Homo sapiens	49-55
10413105-4	1999	Kinetic measurements of heparin interaction with HB-GAM made by SPR afforded a Kd of 4 nM, suggesting considerably tighter binding when HB-GAM was immobilized on a surface.	Heparin	24-31	pleiotrophin	Homo sapiens	136-142
10385763-13	1999	CONCLUSION: Addition of abciximab to heparin plus aspirin during PCI was associated with a significant decrease in thrombin generation and a borderline decrease in thrombin activity.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	164-172
10375392-3	1999	The modified apoE lost heparin-binding activity.	Heparin	23-30	apolipoprotein E	Homo sapiens	13-17
10573618-8	1999	Comparing fibrinogen levels between Groups A and B, we observed lower values in heparin-treated group than in the other one (p &lt; 0.0001), while in laparoscopic surgery there was not a significant difference between two groups of treatment.	Heparin	80-87	fibrinogen beta chain	Homo sapiens	10-20
10375392-5	1999	The lipid peroxidation and oxidative modification of apoE in VLDL mediated by Cu2+ and an aqueous radical generator were suppressed by GAG, heparan sulfate, heparin, and chondroitin sulfate A, even though GAGs demonstrated no ability to scavenge alpha,alpha-diphenyl-beta-picrylhydrazyl radical.	Heparin	157-164	apolipoprotein E	Homo sapiens	53-57
10412773-5	1999	Plasma LPL activity was measured as free fatty acid (FFA) generation after intravenous administration of heparin.	Heparin	105-112	lipoprotein lipase	Rattus norvegicus	7-10
10726009-9	1999	Platelet induced thrombin generation time was slightly prolonged and platelet adhesion was slightly diminished up to 2 hours using 0.5 mg/kg aprosulate, and up to 4 hours using 1.0 mg/kg aprosulate while the platelet induced thrombin generation time system was not influenced by the subcutaneous injection (7,500 IU) of unfractionated heparin.	Heparin	335-342	coagulation factor II, thrombin	Homo sapiens	17-25
10726009-9	1999	Platelet induced thrombin generation time was slightly prolonged and platelet adhesion was slightly diminished up to 2 hours using 0.5 mg/kg aprosulate, and up to 4 hours using 1.0 mg/kg aprosulate while the platelet induced thrombin generation time system was not influenced by the subcutaneous injection (7,500 IU) of unfractionated heparin.	Heparin	335-342	coagulation factor II, thrombin	Homo sapiens	225-233
10484747-2	1999	They can cleave the human fibrinogen to release the fibrinopeptide A and fibrinopeptide B with specific activity of 120 and 370 NIH units/mg, respectively; the fibrinogen-clotting activity can be inhibited distinctly by PMSF or DFP or EDTA, but not by heparin.	Heparin	252-259	fibrinogen beta chain	Homo sapiens	26-36
10385702-7	1999	Accordingly, molecular modeling, based on the crystal structure of the interaction of FGF-2 with a heparin hexamer, showed the feasibility of docking PAMPS into the heparin-binding domain of FGF-2.	Heparin	99-106	fibroblast growth factor 2	Bos taurus	86-91
10385702-7	1999	Accordingly, molecular modeling, based on the crystal structure of the interaction of FGF-2 with a heparin hexamer, showed the feasibility of docking PAMPS into the heparin-binding domain of FGF-2.	Heparin	99-106	fibroblast growth factor 2	Bos taurus	191-196
10385702-7	1999	Accordingly, molecular modeling, based on the crystal structure of the interaction of FGF-2 with a heparin hexamer, showed the feasibility of docking PAMPS into the heparin-binding domain of FGF-2.	Heparin	165-172	fibroblast growth factor 2	Bos taurus	86-91
10385702-7	1999	Accordingly, molecular modeling, based on the crystal structure of the interaction of FGF-2 with a heparin hexamer, showed the feasibility of docking PAMPS into the heparin-binding domain of FGF-2.	Heparin	165-172	fibroblast growth factor 2	Bos taurus	191-196
10385702-11	1999	In conclusion, sulfonic acid polymers bind FGF-2 by mimicking heparin interaction.	Heparin	62-69	fibroblast growth factor 2	Bos taurus	43-48
10493153-11	1999	This fraction is positively correlated to the activity of hepatic lipase (HL) and negatively to the activity of lipoprotein lipase (LPL), released by heparin.	Heparin	150-157	lipoprotein lipase	Rattus norvegicus	112-130
10493153-11	1999	This fraction is positively correlated to the activity of hepatic lipase (HL) and negatively to the activity of lipoprotein lipase (LPL), released by heparin.	Heparin	150-157	lipoprotein lipase	Rattus norvegicus	132-135
10456457-1	1999	Inhibition of activated protein C (APC) by protein C inhibitor (PCI) is stimulated by heparin, whereas inhibition by alpha1-antitrypsin (AAT) is heparin-independent.	Heparin	145-152	serpin family A member 1	Homo sapiens	117-135
10456457-1	1999	Inhibition of activated protein C (APC) by protein C inhibitor (PCI) is stimulated by heparin, whereas inhibition by alpha1-antitrypsin (AAT) is heparin-independent.	Heparin	145-152	serpin family A member 1	Homo sapiens	137-140
10484747-2	1999	They can cleave the human fibrinogen to release the fibrinopeptide A and fibrinopeptide B with specific activity of 120 and 370 NIH units/mg, respectively; the fibrinogen-clotting activity can be inhibited distinctly by PMSF or DFP or EDTA, but not by heparin.	Heparin	252-259	fibrinogen beta chain	Homo sapiens	160-170
10385507-0	1999	Thrombin-induced platelet activation is inhibited by high- and low-molecular-weight heparin.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	0-8
10385507-2	1999	Thrombin ligation to Gp Ib was recently shown to be inhibited by heparin, thus raising the hypothesis, investigated in this article, that heparin might inhibit thrombin-induced platelet activation.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	0-8
10385507-2	1999	Thrombin ligation to Gp Ib was recently shown to be inhibited by heparin, thus raising the hypothesis, investigated in this article, that heparin might inhibit thrombin-induced platelet activation.	Heparin	65-72	coagulation factor II, thrombin	Homo sapiens	160-168
10385507-9	1999	Moreover, platelet stimulation by heparin binding site phosphopyridoxylated thrombin, which has a severe impairment of Gp Ib ligation, was not affected by heparin.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	76-84
10385507-11	1999	CONCLUSIONS: These results demonstrated that heparin, by inhibiting the thrombin-Gp Ib interaction, is able to interfere with thrombin-induced platelet activation.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	72-80
10385507-2	1999	Thrombin ligation to Gp Ib was recently shown to be inhibited by heparin, thus raising the hypothesis, investigated in this article, that heparin might inhibit thrombin-induced platelet activation.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	0-8
10385507-11	1999	CONCLUSIONS: These results demonstrated that heparin, by inhibiting the thrombin-Gp Ib interaction, is able to interfere with thrombin-induced platelet activation.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	126-134
10385507-2	1999	Thrombin ligation to Gp Ib was recently shown to be inhibited by heparin, thus raising the hypothesis, investigated in this article, that heparin might inhibit thrombin-induced platelet activation.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	160-168
10387076-1	1999	Multiple sites within the N-terminal domain (1-5F1) of fibronectin have been implicated previously in fibronectin matrix assembly, heparin binding, and binding to cell surface proteins of pathogenic bacteria.	Heparin	131-138	fibronectin 1	Homo sapiens	55-66
10387091-8	1999	Heparin, which accelerates the inhibition of the three proteinases by native MPI, also favors their interaction with oxidized MPI.	Heparin	0-7	secretory leukocyte peptidase inhibitor	Homo sapiens	77-80
10387091-8	1999	Heparin, which accelerates the inhibition of the three proteinases by native MPI, also favors their interaction with oxidized MPI.	Heparin	0-7	secretory leukocyte peptidase inhibitor	Homo sapiens	126-129
10387091-9	1999	Flow calorimetry shows that heparin binds oxidized MPI with Kd, Delta H degrees, and Delta S degrees values close to those reported for native MPI.	Heparin	28-35	secretory leukocyte peptidase inhibitor	Homo sapiens	51-54
10387091-9	1999	Flow calorimetry shows that heparin binds oxidized MPI with Kd, Delta H degrees, and Delta S degrees values close to those reported for native MPI.	Heparin	28-35	secretory leukocyte peptidase inhibitor	Homo sapiens	143-146
10387091-10	1999	In the presence of heparin, oxidized MPI inhibits cathepsin G via a two-step reaction characterized by Ki = 0.22 microM, k2 = 0.1 s-1, k-2 = 0.023 s-1, and Ki = 42 nM.	Heparin	19-26	secretory leukocyte peptidase inhibitor	Homo sapiens	37-40
10387091-12	1999	Heparin also improves the inhibition of chymotrypsin and elastase by oxidized MPI by increasing their kass or k2/Ki and decreasing their Ki.	Heparin	0-7	secretory leukocyte peptidase inhibitor	Homo sapiens	78-81
10385507-3	1999	METHODS AND RESULTS: Aggregation of gel-filtered platelets by 1 nmol/L thrombin was reduced by both high-molecular-weight (MW) (14 500-Da) and low-MW (4500-Da) heparin, with IC50 values of 1.65+/-0.26 and 5.13+/-0.8 micromol/L, respectively.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	71-79
10385507-4	1999	Homogeneous-MW fractions (16 000- to 13 000-Da range) were used to evaluate the heparin effect on intracytoplasmic calcium release by thrombin.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	134-142
10385507-5	1999	Calcium mobilization by 1 nmol/L thrombin was reduced as a function of heparin concentration, and the inhibitory effect was correlated to the MW of heparin fractions (IC50 values were 1.9+/-0.39, 6.07+/-0.83, and 14.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	33-41
10385507-5	1999	Calcium mobilization by 1 nmol/L thrombin was reduced as a function of heparin concentration, and the inhibitory effect was correlated to the MW of heparin fractions (IC50 values were 1.9+/-0.39, 6.07+/-0.83, and 14.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	33-41
10364085-2	1999	In streptozotocin (STZ)-diabetic rats, we have previously demonstrated an increased heparin-releasable LPL activity from perfused hearts.	Heparin	84-91	lipoprotein lipase	Rattus norvegicus	103-106
10353261-12	1999	Heparin, however, competes with CMDB and their fragments for binding to FGF-2.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	72-77
10353261-13	1999	The carboxymethyl and benzylamide groups of these molecules likely interact directly with a heparin-binding region of FGF-2.	Heparin	92-99	fibroblast growth factor 2	Homo sapiens	118-123
10334872-5	1999	Heparin, at high concentrations, can prevent the inhibition of tryptase by MPO.	Heparin	0-7	myeloperoxidase	Homo sapiens	75-78
10334872-7	1999	These data suggest that MPO inhibits tryptase by interfering with the heparin stabilization of tryptase tetramer.	Heparin	70-77	myeloperoxidase	Homo sapiens	24-27
10383842-1	1999	BACKGROUND: We have previously reported that very low doses of low molecular weight heparin compounds (LMWH) inhibit a variety of T-cell-mediated reactions by down-regulation of TNF-alpha production.	Heparin	84-91	tumor necrosis factor	Rattus norvegicus	178-187
10383842-1	1999	BACKGROUND: We have previously reported that very low doses of low molecular weight heparin compounds (LMWH) inhibit a variety of T-cell-mediated reactions by down-regulation of TNF-alpha production.	Heparin	103-107	tumor necrosis factor	Rattus norvegicus	178-187
10383842-11	1999	CONCLUSIONS: Treatment with very low doses of nonanticoagulant LMWH preparations having anti-TNF-alpha activity significantly prolongs rat skin and cardiac allograft survival in a dose- and schedule-dependent manner.	Heparin	63-67	tumor necrosis factor	Rattus norvegicus	93-102
10404599-0	1999	A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding.	Heparin	57-64	fibroblast growth factor receptor 1	Homo sapiens	29-33
10404599-0	1999	A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding.	Heparin	122-129	fibroblast growth factor receptor 1	Homo sapiens	29-33
10404599-0	1999	A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding.	Heparin	122-129	fibroblast growth factor receptor 1	Homo sapiens	49-54
10404599-0	1999	A dimeric ternary complex of FGFR [correction of FGFR1], heparin and FGF-1 leads to an "electrostatic sandwich" model for heparin binding.	Heparin	122-129	fibroblast growth factor 1	Homo sapiens	69-74
10364085-3	1999	Because heparin can traverse the endothelial barrier, conventional Langendorff retrograde perfusion of the heart with heparin could release LPL from both the capillary luminal and abluminal surfaces.	Heparin	8-15	lipoprotein lipase	Rattus norvegicus	140-143
10364085-3	1999	Because heparin can traverse the endothelial barrier, conventional Langendorff retrograde perfusion of the heart with heparin could release LPL from both the capillary luminal and abluminal surfaces.	Heparin	118-125	lipoprotein lipase	Rattus norvegicus	140-143
10364085-5	1999	In response to heparin, a 4-fold increase in LPL activity and protein mass was observed in the coronary perfusate after 2 weeks of STZ diabetes.	Heparin	15-22	lipoprotein lipase	Rattus norvegicus	45-48
10364085-9	1999	An increased heparin-releasable LPL activity in diabetic rats was demonstrated shortly (6 to 24 hours) after STZ injection or after withdrawal from exogenous insulin.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	32-35
10364085-10	1999	Heparin-releasable coronary LPL activity was also increased after an overnight fast.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	28-31
10333493-3	1999	In contrast, cytochalasin D (2 microM) completely abolished the stimulatory effect of insulin and dexamethasone on both heparin-releasable LPL and total cellular LPL activities.	Heparin	120-127	lipoprotein lipase	Rattus norvegicus	139-142
10364085-11	1999	These studies indicate that the intravascular heparin-releasable fraction of cardiac LPL activity is acutely regulated by short-term changes in insulin rather than glucose.	Heparin	46-53	lipoprotein lipase	Rattus norvegicus	85-88
10340997-4	1999	A time-course analysis of PCI-uPA complex formation showed that &gt;80% of the complex had been formed within 15 min in normal seminal plasma in the presence of heparin, compared with the total complex formed after 150 min incubation, whereas no response to heparin stimulation was observed in the assays with the two patient samples.	Heparin	161-168	plasminogen activator, urokinase	Homo sapiens	30-33
16602995-4	1999	Preoperative heparin therapy affected most coagulation tests (e.g. international normalised ratio, activated partial thromboplastin time, thrombin clotting time, prothrombin time, activated clotting time and coagulation time of thrombelastography) before anaesthesia.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	138-146
10362188-3	1999	In vitro and in vivo studies have shown that argatroban has advantages over heparin for the inhibition of clot-bound thrombin and for the enhancement of thrombolysis with TPA.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	117-125
10383000-0	1999	Enhanced interstitial expression of caldesmon in IgA nephropathy and its suppression by glucocorticoid-heparin therapy.	Heparin	103-110	caldesmon 1	Homo sapiens	36-45
10346980-3	1999	The suppression of heparin-releasable LPL activity produced by combinations of LPS and interleukin 1 (IL-1), IL-11 or tumour necrosis factor alpha(TNF-alpha) was substantially less than that expected from the simple additive action of the corresponding two effectors.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	38-41
10346980-3	1999	The suppression of heparin-releasable LPL activity produced by combinations of LPS and interleukin 1 (IL-1), IL-11 or tumour necrosis factor alpha(TNF-alpha) was substantially less than that expected from the simple additive action of the corresponding two effectors.	Heparin	19-26	toll-like receptor 4	Mus musculus	79-82
10346980-3	1999	The suppression of heparin-releasable LPL activity produced by combinations of LPS and interleukin 1 (IL-1), IL-11 or tumour necrosis factor alpha(TNF-alpha) was substantially less than that expected from the simple additive action of the corresponding two effectors.	Heparin	19-26	tumor necrosis factor	Rattus norvegicus	147-156
10404636-2	1999	Upon activation by at least five genetically distinct ligands (including EGF, transforming growth factor-alpha (TGF alpha) and heparin-binding EGF (HB-EGF)), the intrinsic kinase is activated and EGFR tyrosyl-phosphorylates itself and numerous intermediary effector molecules, including closely-related c-erbB receptor family members.	Heparin	127-134	epidermal growth factor receptor	Homo sapiens	196-200
10340997-4	1999	A time-course analysis of PCI-uPA complex formation showed that &gt;80% of the complex had been formed within 15 min in normal seminal plasma in the presence of heparin, compared with the total complex formed after 150 min incubation, whereas no response to heparin stimulation was observed in the assays with the two patient samples.	Heparin	258-265	plasminogen activator, urokinase	Homo sapiens	30-33
10340997-5	1999	Similarly, &gt;90% of PCI-tPA complex was formed after 30 min of heparin stimulation in normal seminal plasma but no response was observed in the two patient samples.	Heparin	65-72	plasminogen activator, tissue type	Homo sapiens	26-29
10404775-4	1999	Under the same experimental conditions, heparin (100 microg/ml) inhibited thrombin generation mostly by delaying and by reducing the burst of thrombin.	Heparin	40-47	coagulation factor II	Rattus norvegicus	74-82
10404775-4	1999	Under the same experimental conditions, heparin (100 microg/ml) inhibited thrombin generation mostly by delaying and by reducing the burst of thrombin.	Heparin	40-47	coagulation factor II	Rattus norvegicus	142-150
10226073-14	1999	These findings demonstrate that FGF-1, mostly in the presence of heparin, upregulates collagenase and downregulates type I collagen expression that might have a protective role in avoiding collagen accumulation during lung ECM remodeling.	Heparin	65-72	fibroblast growth factor 1	Homo sapiens	32-37
10340746-6	1999	These results indicate that the neurotrophic substance in 0.5 M NaCl-eluate from heparin-affinity chromatography is IGF-II and that mechanisms may exist in vivo for the activation of latent IGF-II, whose biological effects may be blocked by its specific binding proteins.	Heparin	81-88	insulin like growth factor 2	Gallus gallus	116-122
10340746-6	1999	These results indicate that the neurotrophic substance in 0.5 M NaCl-eluate from heparin-affinity chromatography is IGF-II and that mechanisms may exist in vivo for the activation of latent IGF-II, whose biological effects may be blocked by its specific binding proteins.	Heparin	81-88	insulin like growth factor 2	Gallus gallus	190-196
10224111-1	1999	The interaction of basic fibroblast growth factor (bFGF) with heparan sulfate (HS)/heparin has been shown to strongly enhance the activity of the growth factor although the mechanism of activation is unclear.	Heparin	83-90	fibroblast growth factor 2	Homo sapiens	19-49
10224111-1	1999	The interaction of basic fibroblast growth factor (bFGF) with heparan sulfate (HS)/heparin has been shown to strongly enhance the activity of the growth factor although the mechanism of activation is unclear.	Heparin	83-90	fibroblast growth factor 2	Homo sapiens	51-55
10226073-4	1999	Heparin was used because it enhances the biologic activities of FGF-1.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	64-69
10226073-8	1999	Our results show that FGF-1 induced collagenase mRNA expression, which was strongly enhanced when FGF-1 was used with heparin.	Heparin	118-125	fibroblast growth factor 1	Homo sapiens	22-27
10226073-8	1999	Our results show that FGF-1 induced collagenase mRNA expression, which was strongly enhanced when FGF-1 was used with heparin.	Heparin	118-125	fibroblast growth factor 1	Homo sapiens	98-103
10336501-4	1999	Cell-free complexes of heparin and recombinant FGFR4 bound FGF-1 and FGF-2 equally.	Heparin	23-30	fibroblast growth factor 1	Homo sapiens	59-64
10336501-4	1999	Cell-free complexes of heparin and recombinant FGFR4 bound FGF-1 and FGF-2 equally.	Heparin	23-30	fibroblast growth factor 2	Homo sapiens	69-74
10328953-4	1999	Furthermore, agrin"s heparan sulfate side chains encode a specificity in interactions with heparin-binding molecules since fibronectin and the cell adhesion molecule L1 do not bind agrin.	Heparin	91-98	agrin	Gallus gallus	13-18
10328761-9	1999	Thrombin-stimulated clot formation was completely inhibited by heparin.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	0-8
10318803-8	1999	These results altogether indicate that EXTL2/EXTR2 encodes the alpha1,4-N-acetylhexosaminyltransferase that transfers GalNAc/GlcNAc to the tetrasaccharide representing the common glycosaminoglycan-protein linkage region and that is most likely the critical enzyme that determines and initiates the heparin/heparan sulfate synthesis, separating it from the chondroitin sulfate/dermatan sulfate synthesis.	Heparin	298-305	exostosin like glycosyltransferase 2	Homo sapiens	39-44
10318803-8	1999	These results altogether indicate that EXTL2/EXTR2 encodes the alpha1,4-N-acetylhexosaminyltransferase that transfers GalNAc/GlcNAc to the tetrasaccharide representing the common glycosaminoglycan-protein linkage region and that is most likely the critical enzyme that determines and initiates the heparin/heparan sulfate synthesis, separating it from the chondroitin sulfate/dermatan sulfate synthesis.	Heparin	298-305	exostosin like glycosyltransferase 2	Homo sapiens	45-50
10427858-3	1999	In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	66-74
10408373-7	1999	Protein modeling together with site directed mutagenesis indicate that R39, R64 and R66 from the C4BP alpha-chain form a key binding site for heparin, suggesting that this region could be of major importance for interaction with C4b.	Heparin	142-149	complement component 4 binding protein alpha	Homo sapiens	97-107
10323780-0	1999	Lipolytic modification of LDL by phospholipase A2 induces particle aggregation in the absence and fusion in the presence of heparin.	Heparin	124-131	phospholipase A2 group IB	Homo sapiens	33-49
10346888-1	1999	We analyzed the binding of heparinoid or heparin with fibrinogen by real-time measurement using surface plasmon resonance technology.	Heparin	27-34	fibrinogen beta chain	Homo sapiens	54-64
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	84-91	thrombospondin 1	Homo sapiens	218-223
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	255-262	thrombospondin 1	Homo sapiens	60-65
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	255-262	fibronectin 1	Homo sapiens	69-80
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	255-262	thrombospondin 1	Homo sapiens	218-223
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	255-262	thrombospondin 1	Homo sapiens	218-223
10222136-7	1999	Addition of heparin blocked the effect of full-length syndecan-2, suggesting that heparan sulfate chains in the extracellular domain are necessary to induce filopodia.	Heparin	12-19	syndecan 2	Mus musculus	54-64
10194419-8	1999	The adhesive properties of thrombospondin-1 for thyroid cells were shown to be mediated by both the amino-terminal heparin-binding domain and the RGD domain of thrombospondin-1.	Heparin	115-122	thrombospondin 1	Homo sapiens	27-43
10323780-5	1999	Here we studied the effect of heparin GAG on the lipolytic modification of LDL by PLA2.	Heparin	30-37	phospholipase A2 group IB	Homo sapiens	82-86
10323780-6	1999	Untreated LDL, heparin-treated LDL, and heparin-bound LDL were lipolyzed with bee venom PLA2.	Heparin	40-47	phospholipase A2 group IB	Homo sapiens	88-92
10323780-11	1999	In summary, lipolysis of LDL PC by PLA2 under physiological conditions, which allow transfer of the lipolytic degradation products to albumin, leads to fusion of LDL particles in the presence, but not in the absence, of heparin.	Heparin	220-227	phospholipase A2 group IB	Homo sapiens	35-39
10346888-7	1999	These results suggest that the interaction mechanism of heparinoids with fibrinogen was different from that of heparin.	Heparin	56-63	fibrinogen beta chain	Homo sapiens	73-83
10222132-1	1999	Thrombospondin-1 (TSP-1) interacts specifically with heparin and fibronectin in vitro and colocalizes with fibronectin and heparan sulfate in the extracellular matrix (ECM).	Heparin	53-60	thrombospondin 1	Homo sapiens	0-16
10222132-1	1999	Thrombospondin-1 (TSP-1) interacts specifically with heparin and fibronectin in vitro and colocalizes with fibronectin and heparan sulfate in the extracellular matrix (ECM).	Heparin	53-60	thrombospondin 1	Homo sapiens	18-23
10222132-7	1999	We found that while trypsin cleavage of free TSP-1 resulted in the inactivation of ligand binding, TSP-1 bound to either fibronectin or heparin remained stably associated with these ligands.	Heparin	136-143	thrombospondin 1	Homo sapiens	99-104
10222132-8	1999	Cleavage by thrombin or tissue plasminogen activator (tPA) showed that Ca2+-depleted TSP-1, when bound to fibronectin or to heparin, yielded proteolytic cleavage patterns typical of the Ca2+-containing form.	Heparin	124-131	thrombospondin 1	Homo sapiens	85-90
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	84-91	thrombospondin 1	Homo sapiens	60-65
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	84-91	fibronectin 1	Homo sapiens	69-80
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	84-91	thrombospondin 1	Homo sapiens	218-223
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	84-91	fibronectin 1	Homo sapiens	240-251
10233160-0	1999	Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13.	Heparin	95-102	fibronectin 1	Homo sapiens	0-11
10233160-2	1999	This process is known to involve both the central alpha5beta1 integrin-binding and the C-terminal heparin-binding regions of FN.	Heparin	98-105	fibronectin 1	Homo sapiens	125-127
10411247-7	1999	Differential evaluation of the TT and heparin neutralized thrombin time (HNTT) was shown in laboratory studies to be more sensitive to small amounts of residual heparin than the ACT.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	58-66
10212279-2	1999	Megalin-bound Tg was releasable by heparin.	Heparin	35-42	thyroglobulin	Rattus norvegicus	14-16
10212279-6	1999	To investigate cell binding further, we developed an assay in which cells were incubated with unlabeled Tg at 4 degrees C, followed by incubation with heparin, which released almost all of the cell-bound Tg into the medium.	Heparin	151-158	thyroglobulin	Rattus norvegicus	204-206
10212279-10	1999	Tg endocytosis by FRTL-5 and IRPT cells was demonstrated in experiments in which cells were incubated with unlabeled Tg at 37 degrees C, followed by heparin to remove cell-bound Tg.	Heparin	149-156	thyroglobulin	Rattus norvegicus	0-2
10212279-7	1999	In solid phase experiments designed to illuminate the mechanism of heparin release, we demonstrated that Tg is a heparin-binding protein, as are several megalin ligands.	Heparin	67-74	thyroglobulin	Rattus norvegicus	105-107
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	thyroglobulin	Rattus norvegicus	14-16
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	thyroglobulin	Rattus norvegicus	278-280
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	293-300	thyroglobulin	Rattus norvegicus	14-16
10196157-3	1999	Heparin binds to VEGF165 and enhances its binding to VEGF receptors.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	17-21
10466208-0	1999	Assessment through chemical synthesis of the size of the heparin sequence involved in thrombin inhibition.	Heparin	57-64	coagulation factor II, thrombin	Homo sapiens	86-94
10466208-4	1999	These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	70-78
10338119-0	1999	Heparin down-regulates the phorbol ester-induced protein kinase C gene expression in human endothelial cells: enzyme-mediated autoregulation of protein kinase C-alpha and -delta genes.	Heparin	0-7	protein kinase C alpha	Homo sapiens	144-177
10338119-3	1999	Heparin, markedly but not completely, inhibited the serum-stimulated protein kinase C-alpha and -delta mRNA expression.	Heparin	0-7	protein kinase C alpha	Homo sapiens	69-102
10328304-0	1999	New synthetic heparin mimetics able to inhibit thrombin and factor Xa.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	47-55
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	107-115
10365287-0	1999	The effect of a low molecular mass thrombin inhibitor, inogatran, and heparin on thrombin generation and fibrin turnover in patients with unstable coronary artery disease.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	81-89
10203088-0	1999	Heparin and enoxaparin enhance endotoxin-induced tumor necrosis factor-alpha production in human monocytes.	Heparin	0-7	tumor necrosis factor	Homo sapiens	49-76
10203088-10	1999	RESULTS: Heparin (10 to 1000 microg/ml) and enoxaparin (1000 microg/ml) significantly enhanced LPS-induced TNF-alpha release.	Heparin	9-16	tumor necrosis factor	Homo sapiens	107-116
10203088-12	1999	Blockade of CD14 abrogated both LPS-induced TNF-alpha release and the effect of heparin or enoxaparin to enhance LPS-induced TNF-alpha release.	Heparin	80-87	tumor necrosis factor	Homo sapiens	125-134
10203088-13	1999	CONCLUSIONS: The effect of heparin to enhance LPS-induced TNF-alpha release is a biologic phenomenon that reveals a novel and potentially important host defense mechanism during endotoxemia and sepsis.	Heparin	27-34	tumor necrosis factor	Homo sapiens	58-67
10365287-3	1999	Prothrombin fragment 1 + 2, indicating thrombin generation, decreased in the low, medium and high dose inogatran groups and in the heparin group during the first 6 h of treatment by 12%, 15%, 21% and 26%, respectively.	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	3-11
10365287-12	1999	CONCLUSION: The more pronounced decrease in thrombin generation and fibrin turnover during the first 6 h of infusion, and the later increase in thrombin generation and fibrin turnover, in the heparin group, as compared to the inogatran groups, may be related to the lower clinical event rate during infusion with heparin compared with inogatran and the recurrence of ischaemic events, early after cessation of heparin infusion.	Heparin	192-199	coagulation factor II, thrombin	Homo sapiens	44-52
10365287-12	1999	CONCLUSION: The more pronounced decrease in thrombin generation and fibrin turnover during the first 6 h of infusion, and the later increase in thrombin generation and fibrin turnover, in the heparin group, as compared to the inogatran groups, may be related to the lower clinical event rate during infusion with heparin compared with inogatran and the recurrence of ischaemic events, early after cessation of heparin infusion.	Heparin	192-199	coagulation factor II, thrombin	Homo sapiens	144-152
10213181-3	1999	An examination of the mechanism of heparin neutralization and protamine toxicity suggests that the reversal of heparin anticoagulation may only require a small arginine-rich fragment of protamine to electrostatically dissociate antithrombin III from its binding to a specific pentasaccharide sequence in heparin.	Heparin	111-118	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	228-244
10323280-2	1999	The antithrombin III-stimulated release of big endothelin-1 and endothelin-1 (1.7-fold and 1.3-fold over baseline) was abolished by nicardipine (L-type Ca2+ channel blocker), heparin, and N-acetyl heparin (a derivative devoid of antithrombin affinity), whereas staurosporine and genistein (inhibitors of protein kinase C and tyrosine kinase, respectively) were ineffective.	Heparin	175-182	endothelin 1	Rattus norvegicus	47-59
10323280-2	1999	The antithrombin III-stimulated release of big endothelin-1 and endothelin-1 (1.7-fold and 1.3-fold over baseline) was abolished by nicardipine (L-type Ca2+ channel blocker), heparin, and N-acetyl heparin (a derivative devoid of antithrombin affinity), whereas staurosporine and genistein (inhibitors of protein kinase C and tyrosine kinase, respectively) were ineffective.	Heparin	175-182	endothelin 1	Rattus norvegicus	64-76
10235427-0	1999	Differential inhibition of thrombin activity and thrombin generation by a synthetic direct thrombin inhibitor (napsagatran, Ro 46-6240) and unfractionated heparin in patients with deep vein thrombosis.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	49-57
10235427-0	1999	Differential inhibition of thrombin activity and thrombin generation by a synthetic direct thrombin inhibitor (napsagatran, Ro 46-6240) and unfractionated heparin in patients with deep vein thrombosis.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	49-57
10235427-10	1999	CONCLUSIONS: The data presented suggest that direct thrombin inhibition with napsagatran at 9 mg/h is more potent than UFH in attenuating thrombin activity, but is less potent than UFH in inhibiting thrombin generation.	Heparin	119-122	coagulation factor II, thrombin	Homo sapiens	138-146
10235427-10	1999	CONCLUSIONS: The data presented suggest that direct thrombin inhibition with napsagatran at 9 mg/h is more potent than UFH in attenuating thrombin activity, but is less potent than UFH in inhibiting thrombin generation.	Heparin	119-122	coagulation factor II, thrombin	Homo sapiens	138-146
10085407-4	1999	Several experimental strategies have recently documented the involvement of the thrombin domain referred to as "heparin binding site" in the binding to GpIb.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	80-88
10082128-8	1999	These results suggest that peptide LG-6 plays a functional role as a heparin binding site in the G-domain of the laminin alpha1 chain, and this sequence was thus concluded to play a crucial role in regulating cell adhesion and spreading and neurite out-growth which is related to integrin alpha2.	Heparin	69-76	integrin subunit alpha 2	Rattus norvegicus	280-295
10363587-1	1999	We have examined the expression of midkine (MK), a neurotrophic factor with heparin-binding activity, in human esophageal cancer cells.	Heparin	76-83	midkine	Homo sapiens	35-42
10201371-0	1999	Synthesis of thrombin-inhibiting heparin mimetics without side effects.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	13-21
10201371-6	1999	To obtain more potent and well-tolerated antithrombotic drugs, we wished to synthesize heparin mimetics able to inhibit thrombin, that is, longer oligosaccharides.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	120-128
10363611-13	1999	Using heparin-coated circuits (group C) also led to a significant (p&lt;0.05) IL-10 upregulation (C: peak at 2 h, 1380 pg/ml) and IL-6 suppression (C: peak at 4 h, 290 pg/ml).	Heparin	6-13	interleukin 6	Homo sapiens	130-134
10363611-16	1999	Heparin coating reduces IL-6 and increases IL-10 release, whereas IL-8 is not affected.	Heparin	0-7	interleukin 6	Homo sapiens	24-70
10213181-3	1999	An examination of the mechanism of heparin neutralization and protamine toxicity suggests that the reversal of heparin anticoagulation may only require a small arginine-rich fragment of protamine to electrostatically dissociate antithrombin III from its binding to a specific pentasaccharide sequence in heparin.	Heparin	111-118	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	228-244
10051433-0	1999	Heparin and heparan sulphate protect basic fibroblast growth factor from non-enzymic glycosylation.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	37-67
10051433-8	1999	If heparin was added to bFGF prior to non-enzymic glycosylation, the mitogenic activity and heparin affinity of bFGF were nearly completely preserved.	Heparin	3-10	fibroblast growth factor 2	Homo sapiens	24-28
10051433-8	1999	If heparin was added to bFGF prior to non-enzymic glycosylation, the mitogenic activity and heparin affinity of bFGF were nearly completely preserved.	Heparin	3-10	fibroblast growth factor 2	Homo sapiens	112-116
10051433-5	1999	To investigate this, we measured the effect of non-enzymic glycosylation on bFGF bound to heparin, heparan sulphate and related compounds.	Heparin	90-97	fibroblast growth factor 2	Homo sapiens	76-80
10051433-10	1999	Whereas non-enzymic glycosylation of bFGF with G3P impaired its ability to stimulate c-myc mRNA expression in fibroblasts, no such impairment was noticeable when bFGF was glycosylated in the presence of heparin.	Heparin	203-210	fibroblast growth factor 2	Homo sapiens	37-41
10051565-0	1999	Fibroblast growth factors 1 and 2 are distinct in oligomerization in the presence of heparin-like glycosaminoglycans.	Heparin	85-92	fibroblast growth factor 1	Homo sapiens	0-33
10082988-1	1999	Human chymase from vascular tissues was purified to homogeneity by heparin affinity and gel filtration chromatography.	Heparin	67-74	chymase 1	Homo sapiens	6-13
10037709-0	1999	Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	62-70
10075919-1	1999	The crystal structure of human fibronectin (FN) type III repeats 12-14 reveals the primary heparin-binding site, a clump of positively charged residues in FN13, and a putative minor site approximately 60 A away in FN14.	Heparin	91-98	fibronectin 1	Homo sapiens	31-42
10037709-1	1999	Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	20-28
10037709-1	1999	Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	96-104
10037709-1	1999	Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	96-104
10037709-1	1999	Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	20-28
10037709-4	1999	Likewise, the rate of thrombin inhibition by the heparin-independent inhibitor, alpha1-antitrypsin Met358 --&gt; Arg, is decreased less than 2-fold in the presence of soluble fibrin and heparin.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	22-30
10397936-0	1999	Proliferation of endothelial cells on surface-immobilized albumin-heparin conjugate loaded with basic fibroblast growth factor.	Heparin	66-73	fibroblast growth factor 2	Homo sapiens	96-126
10037709-4	1999	Likewise, the rate of thrombin inhibition by the heparin-independent inhibitor, alpha1-antitrypsin Met358 --&gt; Arg, is decreased less than 2-fold in the presence of soluble fibrin and heparin.	Heparin	49-56	serpin family A member 1	Homo sapiens	80-98
10037709-4	1999	Likewise, the rate of thrombin inhibition by the heparin-independent inhibitor, alpha1-antitrypsin Met358 --&gt; Arg, is decreased less than 2-fold in the presence of soluble fibrin and heparin.	Heparin	186-193	coagulation factor II, thrombin	Homo sapiens	22-30
10037709-4	1999	Likewise, the rate of thrombin inhibition by the heparin-independent inhibitor, alpha1-antitrypsin Met358 --&gt; Arg, is decreased less than 2-fold in the presence of soluble fibrin and heparin.	Heparin	186-193	serpin family A member 1	Homo sapiens	80-98
10037709-5	1999	In contrast, thrombin is protected from inhibition by a covalent antithrombin-heparin complex, suggesting that access of heparin to exosite 2 of thrombin is hampered when ternary complex formation occurs.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	13-21
10037709-5	1999	In contrast, thrombin is protected from inhibition by a covalent antithrombin-heparin complex, suggesting that access of heparin to exosite 2 of thrombin is hampered when ternary complex formation occurs.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	69-77
10037709-6	1999	These results reveal the importance of exosites 1 and 2 of thrombin in assembly of the ternary complex and the subsequent protection of thrombin from inhibition by heparin-catalyzed inhibitors.	Heparin	164-171	coagulation factor II, thrombin	Homo sapiens	59-67
10037709-6	1999	These results reveal the importance of exosites 1 and 2 of thrombin in assembly of the ternary complex and the subsequent protection of thrombin from inhibition by heparin-catalyzed inhibitors.	Heparin	164-171	coagulation factor II, thrombin	Homo sapiens	136-144
10397936-8	1999	However, only a minor part of the bFGF used in this study displayed heparin affinity.	Heparin	68-75	fibroblast growth factor 2	Homo sapiens	34-38
10397936-10	1999	In conclusion, bFGF loading of vascular graft surfaces through complexation of bFGF with a heparin-containing matrix probably will lead to more rapid formation of a confluent monolayer of ECs on graft surfaces upon seeding of the cells.	Heparin	91-98	fibroblast growth factor 2	Homo sapiens	15-19
10397936-10	1999	In conclusion, bFGF loading of vascular graft surfaces through complexation of bFGF with a heparin-containing matrix probably will lead to more rapid formation of a confluent monolayer of ECs on graft surfaces upon seeding of the cells.	Heparin	91-98	fibroblast growth factor 2	Homo sapiens	79-83
10397936-3	1999	Human umbilical vein endothelial cells (HUVECs) were grown on bFGF-loaded albumin-heparin conjugate bound to CO2 gas-plasma-treated polystyrene.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	62-66
10397936-7	1999	Binding of bFGF to heparin and the biological activity of bFGF towards ECs were not influenced by the (radio-)labeling of bFGF with iodine.	Heparin	19-26	fibroblast growth factor 2	Homo sapiens	11-15
10205000-21	1999	Intracellular Ang II induced contraction was not affected by pre-treatment with heparin filled liposomes, but completely abolished in Ca2+-free external medium.	Heparin	80-87	angiotensinogen	Rattus norvegicus	14-20
10372444-3	1999	RESULTS: N-formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated NO production was significantly decreased by heparin at doses of 0.5 and 5 micrograms/mL, while LMWH was only effective at doses of 50 and 200 micrograms/mL by means of a mechanism not related to NO synthase (NOS) activity.	Heparin	112-119	formyl peptide receptor 1	Homo sapiens	50-54
10372444-3	1999	RESULTS: N-formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated NO production was significantly decreased by heparin at doses of 0.5 and 5 micrograms/mL, while LMWH was only effective at doses of 50 and 200 micrograms/mL by means of a mechanism not related to NO synthase (NOS) activity.	Heparin	112-119	nitric oxide synthase 2	Homo sapiens	263-274
10372444-3	1999	RESULTS: N-formyl-methionyl-leucyl-phenylalanine (fMLP)-stimulated NO production was significantly decreased by heparin at doses of 0.5 and 5 micrograms/mL, while LMWH was only effective at doses of 50 and 200 micrograms/mL by means of a mechanism not related to NO synthase (NOS) activity.	Heparin	163-167	formyl peptide receptor 1	Homo sapiens	50-54
10064733-5	1999	Epitope mapping revealed positive amino acid clusters as common epitopes of Abeta (13 through 17; HHQKL) and apoE (residues 144 through 148; LRKRL), both regions known to be heparin binding domains.	Heparin	174-181	amyloid beta precursor protein	Homo sapiens	76-81
10089894-0	1999	Selectivity of von Willebrand factor triplet bands towards heparin binding supports structural model.	Heparin	59-66	von Willebrand factor	Homo sapiens	15-36
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	52-55
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105
10089894-2	1999	Because heparin binding sites are contained in each vWF subunit, high molecular weight multimers of r-vWF and hp-vWF, respectively, were eluted with higher salt concentration, in comparison to r-vWF and hp-vWF molecules with a low degree of multimerization.	Heparin	8-15	von Willebrand factor	Homo sapiens	102-105
10089894-4	1999	By contrast, faster migrating satellite bands and slower migrating satellite bands of hp-vWF exhibited reduced and increased heparin affinity, respectively, compared to the intermediate band of the same triplet.	Heparin	125-132	von Willebrand factor	Homo sapiens	89-92
10089894-5	1999	Because heparin binding sites are localised in the N-terminal domain of the hp-vWF subunit, this result confirms a structural model of hp-vWF (Fischer et al., Biochem.	Heparin	8-15	von Willebrand factor	Homo sapiens	79-82
10037469-7	1999	The results are consistent with a mechanism by which astrocytoma cells clear thrombin in a sequential manner: thrombin is first complexed with PN1, then bound to cell-surface heparins, and finally internalized by LRP.	Heparin	175-183	coagulation factor II, thrombin	Homo sapiens	110-118
10064745-8	1999	Fasting and heparin injection, two factors that increase LpL activity in skeletal muscle, increased uptake of chylomicron [3H] retinoid by rat skeletal muscle.	Heparin	12-19	lipoprotein lipase	Rattus norvegicus	57-60
10064733-5	1999	Epitope mapping revealed positive amino acid clusters as common epitopes of Abeta (13 through 17; HHQKL) and apoE (residues 144 through 148; LRKRL), both regions known to be heparin binding domains.	Heparin	174-181	apolipoprotein E	Homo sapiens	109-113
10026256-1	1999	Keratinocyte growth factor (KGF) is an unusual fibroblast growth factor (FGF) family member in that its activity is largely restricted to epithelial cells, and added heparin/heparan sulfate inhibits its activity in most cell types.	Heparin	166-173	fibroblast growth factor 7	Cricetulus griseus	0-26
10406064-6	1999	Heparin may counteract the thrombolysis-induced thrombin generation, but has an unpredictable effect.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	48-56
10022829-5	1999	In the alpha1 chain, however, strong heparin binding was found on alpha1LG4 and not on alpha1LG5.	Heparin	37-44	cholinergic receptor, nicotinic, alpha polypeptide 3	Mus musculus	66-75
10368283-9	1999	In this model, the heparin-binding residues of IL-8 are exposed, thereby allowing presentation of the chemokine from endothelial cell-surface glycosaminoglycans.	Heparin	19-26	C-X-C motif chemokine ligand 8	Homo sapiens	47-51
10026256-1	1999	Keratinocyte growth factor (KGF) is an unusual fibroblast growth factor (FGF) family member in that its activity is largely restricted to epithelial cells, and added heparin/heparan sulfate inhibits its activity in most cell types.	Heparin	166-173	fibroblast growth factor 7	Cricetulus griseus	28-31
10093889-2	1999	The use of the current antithrombotic drugs, namely heparin + chronic aspirin (ASA) +/- oral anticoagulants, is based upon the assumptions that: i) heparin blocks thrombin generation and/or accelerates thrombin inhibition by antithrombin III (ATIII); ii) aspirin acetylates platelet cyclooxygenase, thereby preventing thromboxane A2 (TxA2) synthesis; and iii) oral anticoagulants reduce the availability of vitamin K-dependent procoagulants, thereby reducing the risk of thrombus formation.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	163-171
10093889-2	1999	The use of the current antithrombotic drugs, namely heparin + chronic aspirin (ASA) +/- oral anticoagulants, is based upon the assumptions that: i) heparin blocks thrombin generation and/or accelerates thrombin inhibition by antithrombin III (ATIII); ii) aspirin acetylates platelet cyclooxygenase, thereby preventing thromboxane A2 (TxA2) synthesis; and iii) oral anticoagulants reduce the availability of vitamin K-dependent procoagulants, thereby reducing the risk of thrombus formation.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	202-210
10026256-4	1999	Higher heparin concentrations inhibited KGF, but not aFGF, binding and signaling.	Heparin	7-14	fibroblast growth factor 7	Cricetulus griseus	40-43
10026256-5	1999	In addition to the known interaction between HSPG and KGF, we found that the KGFR also bound heparin.	Heparin	93-100	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	45-49
10026256-6	1999	The biphasic effect of heparin on KGF, but not aFGF, binding and signaling suggests that occupancy of the HSPG binding site on the KGFR may specifically inhibit KGF signaling.	Heparin	23-30	fibroblast growth factor 7	Cricetulus griseus	34-37
10026256-6	1999	The biphasic effect of heparin on KGF, but not aFGF, binding and signaling suggests that occupancy of the HSPG binding site on the KGFR may specifically inhibit KGF signaling.	Heparin	23-30	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	106-110
10026256-6	1999	The biphasic effect of heparin on KGF, but not aFGF, binding and signaling suggests that occupancy of the HSPG binding site on the KGFR may specifically inhibit KGF signaling.	Heparin	23-30	fibroblast growth factor 7	Cricetulus griseus	131-134
9924158-0	1999	Effectiveness of heparin in preventing thrombin generation and thrombin activity in patients undergoing coronary intervention.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	39-47
10082659-5	1999	Furthermore, compared with the serum collected before heparin administration, the serum collected after heparin administration had more prominent growth-promoting and vascular tube-inducing properties on endothelial cells, and these increased activities were completely inhibited by neutralization of HGF, whereas neutralization of bFGF and VEGF had no effect.	Heparin	104-111	fibroblast growth factor 2	Homo sapiens	332-336
10082659-5	1999	Furthermore, compared with the serum collected before heparin administration, the serum collected after heparin administration had more prominent growth-promoting and vascular tube-inducing properties on endothelial cells, and these increased activities were completely inhibited by neutralization of HGF, whereas neutralization of bFGF and VEGF had no effect.	Heparin	104-111	vascular endothelial growth factor A	Homo sapiens	341-345
9924158-0	1999	Effectiveness of heparin in preventing thrombin generation and thrombin activity in patients undergoing coronary intervention.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	63-71
9924158-9	1999	CONCLUSIONS: Angioplasty performed in the presence of adequate heparin inhibited thrombin even when there was complex lesion morphology or dissection.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	81-89
9924158-10	1999	These data suggest that heparin provides satisfactory thrombin inhibition during routine angioplasty.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	54-62
10327605-4	1999	About one-half of [125I]hIFN-gamma binding could be displaced by heparin.	Heparin	65-72	interferon gamma	Homo sapiens	24-34
9927340-0	1999	Heparin-binding property of human prolactin: a novel aspect of prolactin biology.	Heparin	0-7	prolactin	Homo sapiens	34-43
9927298-4	1999	Autonomous and 1,25-(OH)2D3-stimulated proliferations were inhibited by a specific inhibitor of EGF receptor (EGFR) tyrosine kinase, an EGFR-neutralizing antibody, heparin, the heparin antagonist hexadimethrine, and the proteoglycan sulfation inhibitor chlorate.	Heparin	177-184	epidermal growth factor receptor	Homo sapiens	96-108
9927298-4	1999	Autonomous and 1,25-(OH)2D3-stimulated proliferations were inhibited by a specific inhibitor of EGF receptor (EGFR) tyrosine kinase, an EGFR-neutralizing antibody, heparin, the heparin antagonist hexadimethrine, and the proteoglycan sulfation inhibitor chlorate.	Heparin	177-184	epidermal growth factor receptor	Homo sapiens	110-114
9927298-4	1999	Autonomous and 1,25-(OH)2D3-stimulated proliferations were inhibited by a specific inhibitor of EGF receptor (EGFR) tyrosine kinase, an EGFR-neutralizing antibody, heparin, the heparin antagonist hexadimethrine, and the proteoglycan sulfation inhibitor chlorate.	Heparin	177-184	epidermal growth factor receptor	Homo sapiens	136-140
9927340-0	1999	Heparin-binding property of human prolactin: a novel aspect of prolactin biology.	Heparin	0-7	prolactin	Homo sapiens	63-72
9927340-2	1999	In this study we examined the heparin-binding properties of selected members of the PRL/GH family, using heparin affinity columns followed by gel electrophoresis/Western blotting.	Heparin	30-37	prolactin	Homo sapiens	84-87
9927340-2	1999	In this study we examined the heparin-binding properties of selected members of the PRL/GH family, using heparin affinity columns followed by gel electrophoresis/Western blotting.	Heparin	105-112	prolactin	Homo sapiens	84-87
9927340-3	1999	Purified human PRL and its cleaved 16K fragment, but not human GH or placental lactogen, were retained on the heparin column and were displaced by 0.5 M NaCl.	Heparin	110-117	prolactin	Homo sapiens	15-18
9927340-4	1999	Native PRL in human pituitary extracts and amniotic fluid showed a similar binding affinity to heparin as the purified hormone.	Heparin	95-102	prolactin	Homo sapiens	7-10
9927340-6	1999	Two consensus heparin-binding sequences are present in human PRL but not in the other hormones included in this study.	Heparin	14-21	prolactin	Homo sapiens	61-64
9927340-7	1999	We postulate that the heparin-binding capability of PRL affects its biological activity as a growth factor and the angiostatic actions of its 16K fragment.	Heparin	22-29	prolactin	Homo sapiens	52-55
10023691-5	1999	Heparin prevents the formation of thrombin and neutralizes its activity.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	34-42
9950679-11	1999	Conversely, the soluble receptor and free heparin inhibit the interaction of fluorochrome-labeled GM1 to immobilized FGF-2.	Heparin	42-49	fibroblast growth factor 2	Homo sapiens	117-122
9882449-2	1999	The studies reported here examined the mechanism whereby heparin enhances C1 esterase inhibitor (C1INH) activity on C1 esterase (C1).	Heparin	57-64	complement C1s	Homo sapiens	74-85
9916734-3	1999	By interpolation with our previous findings, this indicates an affinity for heparin greater than that of antithrombin III and comparable with that of FGF-2, two high-affinity heparin-binding proteins.	Heparin	175-182	fibroblast growth factor 2	Homo sapiens	150-155
9927280-8	1999	This cell-associated IGFBP was deduced to be IGFBP-5 based on its molecular size, detection of IGFBP-5 messenger RNA only in slow growing clones, and competition of its binding by heparin.	Heparin	180-187	insulin like growth factor binding protein 5	Homo sapiens	45-52
10226805-3	1999	This proteolysis was less pronounced for IGFBP-3 containing a mutated heparin binding domain, and was prevented by purifying IGFBP-3 on an IGF-I affinity column in the presence of 2 M sodium chloride, suggesting that the responsible protease(s) binds the IGFBP-3 heparin binding domain.	Heparin	70-77	insulin like growth factor 1	Homo sapiens	139-144
9924194-9	1999	In separate experiments, LPL activity in post-heparin plasma was measured.	Heparin	46-53	lipoprotein lipase	Rattus norvegicus	25-28
9882436-10	1999	Heparin accelerated the reaction largely by enhancing formation of thrombin-AT complexes and had little effect on TSP.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	67-75
9989246-4	1999	Our data showed that (i) monoclonal antibodies (MoAbs) against cell surface heparan sulfate (HS) or the heparin-binding domain of TSP, or cleavage of HS on HUVEC by heparitinase reduced TSP binding by 28-40%, (ii) the RGD peptide or MoAbs against integrin alpha v beta 3 or the calcium binding region of TSP inhibited binding by 18-28%, and (iii) a MoAb against the cell-binding domain of TSP inhibited binding by 36%.	Heparin	104-111	thrombospondin 1	Homo sapiens	130-133
9989246-5	1999	Unmodified heparin inhibited the binding of TSP to endothelial cells by 70% and did so far more effectively than selectively desulfated heparins, HS or chondroitin sulfate.	Heparin	11-18	thrombospondin 1	Homo sapiens	44-47
9989246-6	1999	Heparin inhibited TSP binding to HUVEC at much lower concentrations than were required to inhibit TSP binding to sickle erythrocytes.	Heparin	0-7	thrombospondin 1	Homo sapiens	18-21
9989246-6	1999	Heparin inhibited TSP binding to HUVEC at much lower concentrations than were required to inhibit TSP binding to sickle erythrocytes.	Heparin	0-7	thrombospondin 1	Homo sapiens	98-101
9989246-7	1999	Unmodified heparin effectively inhibited the TSP-mediated adhesion of sickle erythrocytes to HUVEC.	Heparin	11-18	thrombospondin 1	Homo sapiens	45-48
10494346-0	1999	Heparin-mediated extracorporeal LDL/fibrinogen precipitation--H.E.L.P.--in coronary and cerebral ischemia.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	36-46
10494346-3	1999	To maintain this supply, H.E.L.P.-apheresis (Heparin-mediated Extracorporeal LDL/Fibrinogen Precipitation) has already proven beneficial in the prevention and therapy of myocardial infarction.	Heparin	45-52	fibrinogen beta chain	Homo sapiens	81-91
14517433-0	1999	Dual effects of heparin on VEGF binding to VEGF receptor-1 and transduction of biological responses.	Heparin	16-23	vascular endothelial growth factor A	Homo sapiens	43-47
14517433-2	1999	As exon 7-containing isoforms of VEGF bind to heparin, angiogenesis may be modulated by heparin/heparan sulfate.	Heparin	46-53	vascular endothelial growth factor A	Homo sapiens	33-37
14517433-2	1999	As exon 7-containing isoforms of VEGF bind to heparin, angiogenesis may be modulated by heparin/heparan sulfate.	Heparin	88-95	vascular endothelial growth factor A	Homo sapiens	33-37
14517433-3	1999	We analyzed the effect of heparin on VEGF(165)-binding and activation of VEGF receptor-1 in porcine aortic endothelial cells, which lack expression of VEGF receptor-2 and neuropilins.	Heparin	26-33	vascular endothelial growth factor A	Homo sapiens	37-41
14517433-4	1999	Heparin decreased binding of (125)I-VEGF to 50% at 5 microg/ml and cross-linking of (125)I-VEGF to VEGF receptor-1 on intact cells was similarly decreased.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	36-40
14517433-5	1999	Schatchard analyses showed that the affinity for binding of (125)I-VEGF to VEGF receptor-1 was decreased in the presence of heparin.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	67-71
14517433-5	1999	Schatchard analyses showed that the affinity for binding of (125)I-VEGF to VEGF receptor-1 was decreased in the presence of heparin.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	75-79
14517433-6	1999	In contrast, VEGF receptor-1 kinase activity was elevated when cells were treated simultaneously with VEGF and heparin.	Heparin	111-118	vascular endothelial growth factor A	Homo sapiens	13-17
14517433-7	1999	In accordance, VEGF-induced tyrosine phosphorylation of phospholipase Cgamma (PLCgamma) and DNA synthesis were augmented by heparin.	Heparin	124-131	vascular endothelial growth factor A	Homo sapiens	15-19
14517433-9	1999	We conclude that although heparin decreases binding of VEGF to VEGF receptor-1, the remaining binding results in more efficient kinase activation.	Heparin	26-33	vascular endothelial growth factor A	Homo sapiens	55-59
14517433-9	1999	We conclude that although heparin decreases binding of VEGF to VEGF receptor-1, the remaining binding results in more efficient kinase activation.	Heparin	26-33	vascular endothelial growth factor A	Homo sapiens	63-67
10470442-7	1999	Heparin had a beneficial effect on the microcirculatory values, serum IL-6 activity, and morphologic changes.	Heparin	0-7	interleukin 6	Rattus norvegicus	70-74
14517424-1	1999	On the surface of smooth muscle cells there are two types of receptors for the mitogenic and angiogenic growth factor fibroblast growth factor-2 (FGF-2); a high affinity tyrosine kinase FGF receptor (FGFR1) and low affinity heparin./heparan-like glycosaminoglycan (HLGAG) component of surface expressed proteoglycans.	Heparin	224-231	fibroblast growth factor 2	Bos taurus	118-144
14517424-1	1999	On the surface of smooth muscle cells there are two types of receptors for the mitogenic and angiogenic growth factor fibroblast growth factor-2 (FGF-2); a high affinity tyrosine kinase FGF receptor (FGFR1) and low affinity heparin./heparan-like glycosaminoglycan (HLGAG) component of surface expressed proteoglycans.	Heparin	224-231	fibroblast growth factor 2	Bos taurus	146-151
14517432-4	1999	Although both VEGF(165) and TSP are heparin binding proteins, TSP had a higher affinity for (125)I-heparin than VEGF(165) (K(d1) 4 nM and K(d2) 14 nM for TSP; K(d) 91 nM for VEGF(165)).	Heparin	36-43	vascular endothelial growth factor A	Homo sapiens	14-18
14517432-4	1999	Although both VEGF(165) and TSP are heparin binding proteins, TSP had a higher affinity for (125)I-heparin than VEGF(165) (K(d1) 4 nM and K(d2) 14 nM for TSP; K(d) 91 nM for VEGF(165)).	Heparin	36-43	thrombospondin 1	Homo sapiens	28-31
14517432-6	1999	About 35% of the mitogenic activity of VEGF(165) was attributable to its heparin binding region.	Heparin	73-80	vascular endothelial growth factor A	Homo sapiens	39-43
14517432-8	1999	Further, (125)I-VEGF(165) bound directly to TSP in a saturable, concentration dependent manner, and heparin modulated this binding.	Heparin	100-107	vascular endothelial growth factor A	Homo sapiens	16-20
14517432-8	1999	Further, (125)I-VEGF(165) bound directly to TSP in a saturable, concentration dependent manner, and heparin modulated this binding.	Heparin	100-107	thrombospondin 1	Homo sapiens	44-47
14517432-9	1999	The mAbs to the heparin binding domain to the type 1 and type 3 repeats of TSP inhibited the binding of VEGF(165) to TSP, and also blocked the inhibitory effect of TSP on VEGF(165) induced HDMEC proliferation.	Heparin	16-23	thrombospondin 1	Homo sapiens	75-78
14517432-9	1999	The mAbs to the heparin binding domain to the type 1 and type 3 repeats of TSP inhibited the binding of VEGF(165) to TSP, and also blocked the inhibitory effect of TSP on VEGF(165) induced HDMEC proliferation.	Heparin	16-23	vascular endothelial growth factor A	Homo sapiens	104-108
14517432-9	1999	The mAbs to the heparin binding domain to the type 1 and type 3 repeats of TSP inhibited the binding of VEGF(165) to TSP, and also blocked the inhibitory effect of TSP on VEGF(165) induced HDMEC proliferation.	Heparin	16-23	thrombospondin 1	Homo sapiens	117-120
14517432-9	1999	The mAbs to the heparin binding domain to the type 1 and type 3 repeats of TSP inhibited the binding of VEGF(165) to TSP, and also blocked the inhibitory effect of TSP on VEGF(165) induced HDMEC proliferation.	Heparin	16-23	thrombospondin 1	Homo sapiens	117-120
14517432-9	1999	The mAbs to the heparin binding domain to the type 1 and type 3 repeats of TSP inhibited the binding of VEGF(165) to TSP, and also blocked the inhibitory effect of TSP on VEGF(165) induced HDMEC proliferation.	Heparin	16-23	vascular endothelial growth factor A	Homo sapiens	171-175
14517432-10	1999	We conclude that (i) the anti-angiogenic activity of TSP is localized in its heparin binding domain and type 1 and type 3 repeats (ii) TSP inhibits angiogenesis by at least two separate mechanisms, (a) displacement of VEGF(165) from endothelial cell HS and (b) direct binding to VEGF(165).	Heparin	77-84	thrombospondin 1	Homo sapiens	53-56
14517433-0	1999	Dual effects of heparin on VEGF binding to VEGF receptor-1 and transduction of biological responses.	Heparin	16-23	vascular endothelial growth factor A	Homo sapiens	27-31
10473982-2	1999	In a vignette describing a hemispheric TIA 1 day prior with ipsilateral bruit, 53% chose admission, 47% elected an outpatient work-up, 28% treated with intravenous heparin and 70% chose aspirin, reflecting the disagreement about medical management of carotid stenosis in the literature.	Heparin	164-171	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	39-44
10228733-3	1999	The adhesion of cells to thrombospondin-1 was mediated by the N-terminal heparin binding domain of thrombospondin-1 as shown by the use of a recombinant fragment, N18.	Heparin	73-80	thrombospondin 1	Homo sapiens	25-41
10228733-3	1999	The adhesion of cells to thrombospondin-1 was mediated by the N-terminal heparin binding domain of thrombospondin-1 as shown by the use of a recombinant fragment, N18.	Heparin	73-80	thrombospondin 1	Homo sapiens	99-115
10092985-6	1999	Total integrated GIP (P &lt; 0.05) and glucose (P &lt; 0.01) responses were higher post heparin than after acipimox in obese subjects only.	Heparin	88-95	gastric inhibitory polypeptide	Homo sapiens	17-20
10725984-0	1999	Heparin-induced thrombocytopenia: clinical considerations of alternative anticoagulation with various glycosaminoglycans and thrombin inhibitors.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	125-133
10473982-3	1999	There was more agreement in the second case, a posterior circulation TIA 1 day prior with atrial fibrillation, in which 84% chose hospital admission, 74% chose intravenous heparin and 90% treated with some form of anticoagulation.	Heparin	172-179	TIA1 cytotoxic granule associated RNA binding protein	Homo sapiens	69-74
10094397-9	1999	Calreticulin and grp94/endoplasmin could be partially resolved from CK2 by chromatography on heparin-agarose and almost completely on ConA-Sepharose.	Heparin	93-100	heat shock protein 90 beta family member 1	Rattus norvegicus	17-22
10466952-5	1999	RESULTS: Compared to control patients, retransfusion of unprocessed CBP blood significantly increased heparin, free plasma hemoglobin and D-Dimers.	Heparin	102-109	CREB binding protein	Homo sapiens	68-71
10070748-5	1999	From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21.	Heparin	63-70	fibroblast growth factor 1	Homo sapiens	58-62
10070748-5	1999	From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	49-53
10070748-5	1999	From the chemical shift differences between free aFGF and aFGF-heparin complex, we concluded that the major heparin binding site was located on the regions 110-131 and 17-21.	Heparin	108-115	fibroblast growth factor 1	Homo sapiens	58-62
10071484-0	1999	Coagulation protein function: the influence of acetaldehyde-modified heparin on thrombin activity.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	80-88
10071484-1	1999	BACKGROUND: The affect of acetaldehyde-treated heparin on thrombin activity has been investigated using factor II-deficient human plasma.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	58-66
10071484-2	1999	METHODS: It was observed that 0.021 units of heparin exerts a marked inhibition of thrombin activity (1.03 units) as measured by clotting times, prolonging the clotting times from 9.6 +/- 0.1 seconds to 24.8 +/- 0.1 seconds.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	83-91
10071484-3	1999	However, when the heparin is preincubated with 447 mmol/L acetaldehyde at RT for 30 minutes prior to mixing with thrombin, a clotting time in excess of 200 seconds is observed.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	113-121
10071484-7	1999	They further indicate that thrombin is targeted by the acetaldehyde-treated heparin.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	27-35
10071484-8	1999	Heparin-acetaldehyde mixtures also reacted with plasma prior to the addition of thrombin to modestly prolong coagulation time.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	80-88
10071484-10	1999	These data further suggest the possibility that reactions of acetaldehyde and heparin are not restricted to those with thrombin, and that they may extend to other blood factors/proteins.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	119-127
10071484-11	1999	CONCLUSIONS: The amount of heparin (0.021 units) required to substantially affect clotting time of thrombin (1.03 units) is substantially lower than that required to prolong clotting of 0.1 mL of whole plasma (0.36 units), by an order of magnitude.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	99-107
10447213-3	1999	By inhibiting thrombin we have previously shown that heparin, a highly negatively-charged glycosaminoglycan (GAG), suppresses the production of ET-1 by cultured human umbilical vein endothelial cells (HUVEC).	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	14-22
10447213-3	1999	By inhibiting thrombin we have previously shown that heparin, a highly negatively-charged glycosaminoglycan (GAG), suppresses the production of ET-1 by cultured human umbilical vein endothelial cells (HUVEC).	Heparin	53-60	endothelin 1	Homo sapiens	144-148
10447213-8	1999	GAGs and related molecules with higher sulfate content, heparin, chondroitin sulfate B, low and high molecular weight dextran sulfates significantly suppressed ET-1 production by HUVEC.	Heparin	56-63	endothelin 1	Homo sapiens	160-164
9882700-8	1999	All FGF2 catabolic fragments bound heparin, demonstrating the preservation of their HSPG-binding site during the in vivo intracellular catabolism of FGF2.	Heparin	35-42	syndecan 2	Rattus norvegicus	84-88
10629396-2	1999	Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin.	Heparin	21-29	coagulation factor II, thrombin	Homo sapiens	147-155
10629396-2	1999	Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	147-155
10629396-2	1999	Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin.	Heparin	68-71	coagulation factor II, thrombin	Homo sapiens	147-155
10702706-7	1999	Despite normal thrombin times in all samples, the amounts of endogenous heparin/heparan sulfate identified in protease-digested samples by radiometric assay were of sufficient concentrations to produce inordinately prolonged thrombin times when compared with the same concentrations of unfractionated heparin.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	225-233
21340993-8	1999	The A1 domain is involved in binding of vWF to platelet glycoprotein 1b (GpIb), binding to fibrillar collagen, sulfatides, and heparin.	Heparin	127-134	von Willebrand factor	Homo sapiens	40-43
21341006-4	1999	Thus, the last update of the antithrombin database listed 11 distinct molecular defects causing heparin binding abnormalities and nine defects having pleiotropic effects interfering with both thrombin inhibitory activity and heparin binding.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	33-41
21341006-4	1999	Thus, the last update of the antithrombin database listed 11 distinct molecular defects causing heparin binding abnormalities and nine defects having pleiotropic effects interfering with both thrombin inhibitory activity and heparin binding.	Heparin	225-232	coagulation factor II, thrombin	Homo sapiens	33-41
10094397-9	1999	Calreticulin and grp94/endoplasmin could be partially resolved from CK2 by chromatography on heparin-agarose and almost completely on ConA-Sepharose.	Heparin	93-100	heat shock protein 90 beta family member 1	Rattus norvegicus	23-34
10094397-9	1999	Calreticulin and grp94/endoplasmin could be partially resolved from CK2 by chromatography on heparin-agarose and almost completely on ConA-Sepharose.	Heparin	93-100	casein kinase 2 beta	Rattus norvegicus	68-71
16801109-1	1999	Heparin-induced thrombocytopenia (HIT) is a relatively common, immunoglobulin-mediated adverse drug reaction associated with in vivo thrombin generation and both venous and arterial thrombosis.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	133-141
10506830-11	1999	Moreover, it implies a novel transcriptional link that creates an FGF action-controlling autoregulatory loop between the heparan sulfate proteoglycans and the heparin-binding FGFs.	Heparin	159-166	fibroblast growth factor 2	Homo sapiens	66-69
9857078-7	1998	Despite the lack of the carboxyl-terminal 52% of apoB, the apoB48-LDL bound to heparin-affinity gel as well as did apoB100-LDL.	Heparin	79-86	apolipoprotein B	Homo sapiens	59-65
10926265-14	1999	The anticoagulant effect of heparin is usually monitored by the APTT, a test that is sensitive to the inhibitory effects of heparin on thrombin, factor Xa.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	135-143
10926265-14	1999	The anticoagulant effect of heparin is usually monitored by the APTT, a test that is sensitive to the inhibitory effects of heparin on thrombin, factor Xa.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	135-143
9930558-1	1999	Heparin-induced thrombocytopenia (HIT) occurs in 1% to 3% of patients receiving heparin and results from the development of antibodies that recognize heparin-platelet factor 4 (H-PF4) complexes that form on the surface of activated platelets and on the vascular endothelium.	Heparin	0-7	platelet factor 4	Mus musculus	179-182
9930558-1	1999	Heparin-induced thrombocytopenia (HIT) occurs in 1% to 3% of patients receiving heparin and results from the development of antibodies that recognize heparin-platelet factor 4 (H-PF4) complexes that form on the surface of activated platelets and on the vascular endothelium.	Heparin	80-87	platelet factor 4	Mus musculus	179-182
9930560-1	1999	A multicenter clinical trial of the thrombin inhibitor argatroban (Novastan; Texas Biotechnology, Houston, TX; Smith-Kline Beecham Pharmaceuticals, Philadelphia, PA) was recently conducted in patients with heparin-induced thrombocytopenia (HIT) and HIT that had progressed to thrombosis (HITTS).	Heparin	206-213	coagulation factor II, thrombin	Homo sapiens	36-44
9930564-8	1999	The increased interest in thrombin inhibitors is also prompted by reports of heparin-induced thrombocytopenia (HIT) with heparin and the need to anticoagulate patients with alternate drugs.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	26-34
9930564-8	1999	The increased interest in thrombin inhibitors is also prompted by reports of heparin-induced thrombocytopenia (HIT) with heparin and the need to anticoagulate patients with alternate drugs.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	26-34
10348708-10	1999	SMCs proliferation, late activation of the extracellular signal-regulated kinases (ERK1/2), and PKC activity were inhibited by heparin (IC 50: 30-50 microg/ml) in SMCs stimulated by FCS but not in SMCs treated by PDGF or EGF.	Heparin	127-134	mitogen-activated protein kinase 3	Homo sapiens	83-89
9856996-6	1998	Fluorescein-labeled heparin was displaced from either thrombin or active site blocked thrombin by ATH, indicating that thrombin must bind to the conjugate"s heparin moiety.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	54-62
9856996-6	1998	Fluorescein-labeled heparin was displaced from either thrombin or active site blocked thrombin by ATH, indicating that thrombin must bind to the conjugate"s heparin moiety.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	86-94
9856996-6	1998	Fluorescein-labeled heparin was displaced from either thrombin or active site blocked thrombin by ATH, indicating that thrombin must bind to the conjugate"s heparin moiety.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	86-94
9856996-6	1998	Fluorescein-labeled heparin was displaced from either thrombin or active site blocked thrombin by ATH, indicating that thrombin must bind to the conjugate"s heparin moiety.	Heparin	157-164	coagulation factor II, thrombin	Homo sapiens	86-94
9856996-6	1998	Fluorescein-labeled heparin was displaced from either thrombin or active site blocked thrombin by ATH, indicating that thrombin must bind to the conjugate"s heparin moiety.	Heparin	157-164	coagulation factor II, thrombin	Homo sapiens	86-94
9856996-7	1998	Interaction of thrombin with ATH"s heparin component was confirmed by a slow reaction rate of conjugate with a thrombin mutant that has weak heparin binding.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	15-23
9857078-9	1998	Monoclonal antibodies against the NH2-terminal region of apoB decreased apoB100 LDL binding to heparin, whereas antibodies against the LDL receptor-binding region did not alter LDL-heparin interaction.	Heparin	95-102	apolipoprotein B	Homo sapiens	57-61
9856996-7	1998	Interaction of thrombin with ATH"s heparin component was confirmed by a slow reaction rate of conjugate with a thrombin mutant that has weak heparin binding.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	111-119
9856996-7	1998	Interaction of thrombin with ATH"s heparin component was confirmed by a slow reaction rate of conjugate with a thrombin mutant that has weak heparin binding.	Heparin	141-148	coagulation factor II, thrombin	Homo sapiens	15-23
9857078-9	1998	Monoclonal antibodies against the NH2-terminal region of apoB decreased apoB100 LDL binding to heparin, whereas antibodies against the LDL receptor-binding region did not alter LDL-heparin interaction.	Heparin	95-102	apolipoprotein B	Homo sapiens	72-79
9856996-7	1998	Interaction of thrombin with ATH"s heparin component was confirmed by a slow reaction rate of conjugate with a thrombin mutant that has weak heparin binding.	Heparin	141-148	coagulation factor II, thrombin	Homo sapiens	111-119
9856996-9	1998	Thus, ATH reacts directly with thrombin through a bridge mechanism and probably catalyzes the reaction of thrombin with antithrombin by a second binding sequence on its heparin chain.	Heparin	169-176	coagulation factor II, thrombin	Homo sapiens	31-39
9842027-0	1998	Effect of intravenous heparin infusion on thrombin-antithrombin complex and fibrinopeptide A in unstable angina.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	42-50
9856996-9	1998	Thus, ATH reacts directly with thrombin through a bridge mechanism and probably catalyzes the reaction of thrombin with antithrombin by a second binding sequence on its heparin chain.	Heparin	169-176	coagulation factor II, thrombin	Homo sapiens	106-114
9845530-11	1998	Significantly more CD34(+) cells adhered directly to immobilized O-sulfated heparin than to N-sulfated or desulfated heparin.	Heparin	76-83	CD34 molecule	Homo sapiens	19-23
9843744-3	1998	Training also increased total and heparin-releasable LPL enzyme activity in white hindlimb muscles and in postheparin plasma (P &lt; 0.05).	Heparin	34-41	lipoprotein lipase	Rattus norvegicus	53-56
9837885-5	1998	SRIF-induced desensitization of N-type calcium channel currents was not reduced in cells stably overexpressing a dominant negative mutant of GRK2 or following intracellular dialysis with GRK2- and GRK3-blocking peptides or with heparin.	Heparin	228-235	somatostatin	Mus musculus	0-4
9842027-6	1998	CONCLUSIONS: The results confirm ongoing fibrin formation in the active phase of unstable angina, indicate incomplete and variable inhibition of thrombin by heparin during continuous infusion, and suggest a risk of re-emergence of thrombosis (in spite of initiating aspirin) 24 hours after withdrawal of heparin.	Heparin	157-164	coagulation factor II, thrombin	Homo sapiens	145-153
9842027-7	1998	Data demonstrate a better control of thrombin activity when heparin is infused at rates that maintain aPTT at &gt;1.5 times baseline, as currently recommended in unstable angina.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	37-45
9848889-7	1998	Certain polyanions, eg, heparin, pentosan polysulfate, dextran sulfate, and suramin, bind to adsorbed fibrin(ogen) and prevent thrombin-dependent adhesion of fibrinogen-coated surfaces.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	127-135
9848889-7	1998	Certain polyanions, eg, heparin, pentosan polysulfate, dextran sulfate, and suramin, bind to adsorbed fibrin(ogen) and prevent thrombin-dependent adhesion of fibrinogen-coated surfaces.	Heparin	24-31	fibrinogen beta chain	Homo sapiens	158-168
9922933-5	1998	In patients having orthopedic surgery, inactivating bound thrombin with direct antithrombins markedly reduces venous thromboembolism as compared with heparin or its derivatives, without significant impairment of hemostasis.	Heparin	150-157	coagulation factor II, thrombin	Homo sapiens	58-66
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	matrix metallopeptidase 3	Homo sapiens	154-202
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	TIMP metallopeptidase inhibitor 1	Homo sapiens	208-254
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	TIMP metallopeptidase inhibitor 1	Homo sapiens	256-262
9827576-3	1998	Addition of heparin to cell culture medium 1 hour following IL-1beta decreased MMP and TIMP-1 expression in a dose-dependent manner.	Heparin	12-19	interleukin 1 beta	Homo sapiens	60-68
9827576-3	1998	Addition of heparin to cell culture medium 1 hour following IL-1beta decreased MMP and TIMP-1 expression in a dose-dependent manner.	Heparin	12-19	TIMP metallopeptidase inhibitor 1	Homo sapiens	87-93
18020612-4	1998	However, hirudin is not as effective as heparin in blocking thrombin generation, but is more effective than heparin in inhibiting thrombin activity.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	130-138
9930660-6	1998	In contrast, fucoidan and heparin inhibited HUVEC proliferation induced by FGF-2, but did not influence the mitogenic activity of vascular endothelial growth factor (VEGF).	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	75-80
10743240-5	1998	In 16 patients with stable COPD and F1 + 2 greater than 1.65 nmol/L (mean +2s of control), intra-venose heparin therapy (100 mg qd for 10 days) significantly reduced F1 + 2(P &lt; 0.005), vWF (P &lt; 0.05), GMP-140 (P &lt; 0.05), and PaCO2 (P &lt; 0.05).	Heparin	104-111	von Willebrand factor	Homo sapiens	188-191
9827576-0	1998	Influence of heparin(s) on the interleukin-1-beta-induced expression of collagenase, stromelysin-1, and tissue inhibitor of metalloproteinase-1 in human gingival fibroblasts.	Heparin	13-20	interleukin 1 beta	Homo sapiens	31-49
9827576-0	1998	Influence of heparin(s) on the interleukin-1-beta-induced expression of collagenase, stromelysin-1, and tissue inhibitor of metalloproteinase-1 in human gingival fibroblasts.	Heparin	13-20	matrix metallopeptidase 3	Homo sapiens	85-98
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	interleukin 1 beta	Homo sapiens	53-71
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	interleukin 1 beta	Homo sapiens	73-81
9884078-7	1998	Co-injection of histamine or heparin significantly reduced the chymase induced neutrophil accumulation, whereas neither histamine nor heparin by themselves had any effect on the accumulation of nucleated cells.	Heparin	29-36	chymase 1	Homo sapiens	63-70
9870465-7	1998	At concentrations of 300 and 1000 microg/ml, heparin inhibited fibronectin mRNA levels in TGF-beta1 (6 ng/ml) stimulated cells.	Heparin	45-52	transforming growth factor, beta 1	Rattus norvegicus	90-99
9836771-5	1998	We also examined heparin"s effect on thrombin-induced gray matter edema.	Heparin	17-24	coagulation factor II	Rattus norvegicus	37-45
9836771-13	1998	As with whole blood, thrombin-induced gray matter edema at 24 hours was significantly reduced by coinjection of heparin.	Heparin	112-119	coagulation factor II	Rattus norvegicus	21-29
9838220-4	1998	Serine protease inhibitors aprotinin and heparin effectively inhibited the breakdown of IGFBP-5.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	0-15
9838220-4	1998	Serine protease inhibitors aprotinin and heparin effectively inhibited the breakdown of IGFBP-5.	Heparin	41-48	insulin like growth factor binding protein 5	Homo sapiens	88-95
9828107-9	1998	The effect of ECM on erb-B2 expression was mediated by the heparin chains of heparin proteoglycan.	Heparin	59-66	erb-b2 receptor tyrosine kinase 2	Homo sapiens	21-27
9813026-9	1998	PN1 bound to heparin uses exosite-I to some extent, possibly by utilizing the positive electrostatic field of exosite-I to enhance orientation and thrombin complex formation.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	147-155
9813026-10	1998	The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	26-34
29711149-2	1998	Thus, there is evidence that heparin fragments with at least 15 saccharide units are required for thrombin inhibition.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	98-106
9880200-4	1998	Serum VEGF level was significantly reduced after heparin administration (P&lt;0.001).	Heparin	49-56	vascular endothelial growth factor A	Homo sapiens	6-10
9843417-2	1998	In the presence of heparin, FGF-1 binds and activates in vitro all FGFR subtypes, while FGF-7 exhibits absolute specificity for the IIIb splice variant of FGFR2.	Heparin	19-26	fibroblast growth factor 1	Homo sapiens	28-33
9813035-0	1998	A novel type of vascular endothelial growth factor, VEGF-E (NZ-7 VEGF), preferentially utilizes KDR/Flk-1 receptor and carries a potent mitotic activity without heparin-binding domain.	Heparin	161-168	vascular endothelial growth factor A	Homo sapiens	16-50
9813035-0	1998	A novel type of vascular endothelial growth factor, VEGF-E (NZ-7 VEGF), preferentially utilizes KDR/Flk-1 receptor and carries a potent mitotic activity without heparin-binding domain.	Heparin	161-168	vascular endothelial growth factor A	Homo sapiens	52-58
9813035-0	1998	A novel type of vascular endothelial growth factor, VEGF-E (NZ-7 VEGF), preferentially utilizes KDR/Flk-1 receptor and carries a potent mitotic activity without heparin-binding domain.	Heparin	161-168	vascular endothelial growth factor A	Homo sapiens	52-56
9813035-8	1998	These results indicate that VEGF-E is a novel type of endothelial growth factor, utilizing only one of the VEGF receptors, and carrying a potent mitogenic activity without affinity to heparin.	Heparin	184-191	vascular endothelial growth factor A	Homo sapiens	28-34
9813035-8	1998	These results indicate that VEGF-E is a novel type of endothelial growth factor, utilizing only one of the VEGF receptors, and carrying a potent mitogenic activity without affinity to heparin.	Heparin	184-191	vascular endothelial growth factor A	Homo sapiens	28-32
9825824-1	1998	BACKGROUND: Previously, it has been demonstrated that heparin inhibits major histocompatibility complex (MHC) class II and intercellular adhesion molecule-1 (ICAM-1) expression on interferon-gamma (IFN-gamma)-stimulated human umbilical vein endothelial cells (HUVECs).	Heparin	54-61	interferon gamma	Homo sapiens	180-196
9825824-1	1998	BACKGROUND: Previously, it has been demonstrated that heparin inhibits major histocompatibility complex (MHC) class II and intercellular adhesion molecule-1 (ICAM-1) expression on interferon-gamma (IFN-gamma)-stimulated human umbilical vein endothelial cells (HUVECs).	Heparin	54-61	interferon gamma	Homo sapiens	198-207
9825824-3	1998	We also studied whether the degree of sulfation of heparin is of relevance for the binding to IFN-gamma and inhibition of MHC and ICAM-1 expression after IFN-gamma stimulation.	Heparin	51-58	interferon gamma	Homo sapiens	94-103
9825824-6	1998	RESULTS: Heparin was able to inhibit the up-regulation of MHC and ICAM-1 in a dose-dependent fashion on both IFN-gamma-stimulated HUVECs and PTECs.	Heparin	9-16	interferon gamma	Homo sapiens	109-118
9825824-8	1998	Heparin and supersulfated glycosaminoglycans (GAGs) were able to bind to IFN-gamma, whereas N-desulfated N-acetylated GAGs with a low amount of sulfate were not.	Heparin	0-7	interferon gamma	Homo sapiens	73-82
9811480-5	1998	Alginate/heparin-Sepharose microspheres and films were designed as drug carriers to control release the bFGF-SAP conjugate or bFGF alone in small doses.	Heparin	9-16	fibroblast growth factor 2	Bos taurus	104-108
9806669-3	1998	We hypothesized that the therapeutic combination of PGE1 and heparin increases the degree of anticoagulation as measured by reduced thrombin generation during CPB.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	132-140
9806669-13	1998	The addition of prostaglandin E1 to heparin enhances the degree of anticoagulation as measured by reduced thrombin formation during cardiopulmonary bypass.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	106-114
9855818-5	1998	Furthermore, alpha-thrombin-induced DNA synthesis could be inhibited by antithrombin III (2 units/ml) with heparin (2 units/ml) or D-Phe-Pro-ArgCH2Cl (50 micrograms/ml).	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	19-27
9799799-7	1998	Preincubation of 1.17 cells with an anti-rat LPL antiserum reduced the heparin-releasable lipolytic activity to &lt;10% of that measured in untreated cells.	Heparin	71-78	lipoprotein lipase	Rattus norvegicus	45-48
9811480-5	1998	Alginate/heparin-Sepharose microspheres and films were designed as drug carriers to control release the bFGF-SAP conjugate or bFGF alone in small doses.	Heparin	9-16	fibroblast growth factor 2	Bos taurus	126-130
9786878-10	1998	The glycosaminoglycans heparin and heparan sulfate bind to IGFBP-5 through its basic carboxyl-terminal domain.	Heparin	23-30	insulin like growth factor binding protein 5	Homo sapiens	59-66
9988527-3	1998	The peptide containing the sequence Phe-Ser-Trp-Ser-Asp-Trp-Trp-Ser (residues 388-395 in lipoprotein lipase, which include the consensus TSP type I sequence) showed strong binding to heparin.	Heparin	183-190	thrombospondin 1	Homo sapiens	137-140
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	53-61
9765230-6	1998	A specific NCAM-heparan sulfate interaction in this adhesion was further indicated by its inhibition with monoclonal anti-NCAM Fab antibodies that recognize the known heparin-binding domain of NCAM and with the HBD-2 peptide derived from this region, but not with antibodies directed against other regions of the protein including the homophilic binding region.	Heparin	167-174	neural cell adhesion molecule 1	Mus musculus	11-15
9809887-3	1998	These limitations reflect the inability of heparin to inactivate thrombin bound to fibrin, a major stimulus for thrombus growth.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	65-73
9809887-6	1998	Direct thrombin inhibitors, such as hirudin and bivalirudin, overcome the limitations of heparin.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	7-15
9761736-3	1998	We show here that sulphated polysaccharides (heparin, keratan and chondroitin) inhibit the neurotoxicity of these amyloid fibrils and this appears to be mediated via inhibition of the polymerization of the PrP peptide into fibrils.	Heparin	45-52	prion protein	Homo sapiens	206-209
9765230-6	1998	A specific NCAM-heparan sulfate interaction in this adhesion was further indicated by its inhibition with monoclonal anti-NCAM Fab antibodies that recognize the known heparin-binding domain of NCAM and with the HBD-2 peptide derived from this region, but not with antibodies directed against other regions of the protein including the homophilic binding region.	Heparin	167-174	neural cell adhesion molecule 1	Mus musculus	122-126
9765230-6	1998	A specific NCAM-heparan sulfate interaction in this adhesion was further indicated by its inhibition with monoclonal anti-NCAM Fab antibodies that recognize the known heparin-binding domain of NCAM and with the HBD-2 peptide derived from this region, but not with antibodies directed against other regions of the protein including the homophilic binding region.	Heparin	167-174	neural cell adhesion molecule 1	Mus musculus	122-126
9755102-4	1998	Desulfated heparin significantly elevated FGF-1- and FGF-2-stimulated DNA synthesis, whereas desulfated CS and N-desulfated heparin elevated FGF-7-stimulated DNA synthesis by type II cells on laminin substrata.	Heparin	124-131	fibroblast growth factor 7	Homo sapiens	141-146
9809799-2	1998	Using different agents which inhibit or stimulate PP1 and PP2A we found that in membrane and nuclear fractions phosphatase activity was inhibited by okadaic acid (OA), protamine, heparin, and inhibitor-2 in a concentration-dependent manner.	Heparin	179-186	neuropeptide Y receptor Y4	Rattus norvegicus	50-53
9755102-4	1998	Desulfated heparin significantly elevated FGF-1- and FGF-2-stimulated DNA synthesis, whereas desulfated CS and N-desulfated heparin elevated FGF-7-stimulated DNA synthesis by type II cells on laminin substrata.	Heparin	11-18	fibroblast growth factor 1	Homo sapiens	42-47
9755102-4	1998	Desulfated heparin significantly elevated FGF-1- and FGF-2-stimulated DNA synthesis, whereas desulfated CS and N-desulfated heparin elevated FGF-7-stimulated DNA synthesis by type II cells on laminin substrata.	Heparin	11-18	fibroblast growth factor 2	Homo sapiens	53-58
9821816-5	1998	It has been suggested that EC-SOD form V is the primary form synthesized in the body and that EC-SOD forms with reduced heparin affinity are the result of proteolytic truncation of the C-terminal end of EC-SOD form V which is responsible for the binding with heparin.	Heparin	259-266	superoxide dismutase 3	Homo sapiens	94-100
9821816-5	1998	It has been suggested that EC-SOD form V is the primary form synthesized in the body and that EC-SOD forms with reduced heparin affinity are the result of proteolytic truncation of the C-terminal end of EC-SOD form V which is responsible for the binding with heparin.	Heparin	259-266	superoxide dismutase 3	Homo sapiens	94-100
9821816-1	1998	Extracellular-superoxide dismutase [EC 1.15.1.1] (EC-SOD) is a secretory glycoprotein with high affinity for heparin.	Heparin	109-116	superoxide dismutase 3	Homo sapiens	50-56
9821816-6	1998	Recently, we reported that only plasma EC-SOD form V, with the highest heparin affinity, was increased by intravenous injection of heparin.	Heparin	71-78	superoxide dismutase 3	Homo sapiens	39-45
9821816-4	1998	Plasma EC-SOD is heterogeneous in heparin affinity and can be divided into five fractions, I to V, by heparin-HPLC.	Heparin	34-41	superoxide dismutase 3	Homo sapiens	7-13
9821816-6	1998	Recently, we reported that only plasma EC-SOD form V, with the highest heparin affinity, was increased by intravenous injection of heparin.	Heparin	131-138	superoxide dismutase 3	Homo sapiens	39-45
9821816-4	1998	Plasma EC-SOD is heterogeneous in heparin affinity and can be divided into five fractions, I to V, by heparin-HPLC.	Heparin	102-109	superoxide dismutase 3	Homo sapiens	7-13
9821816-7	1998	The heparin affinity of plasma EC-SOD in patients with coronary atherosclerosis (CA+ patients) was compared in this study.	Heparin	4-11	superoxide dismutase 3	Homo sapiens	31-37
9821816-5	1998	It has been suggested that EC-SOD form V is the primary form synthesized in the body and that EC-SOD forms with reduced heparin affinity are the result of proteolytic truncation of the C-terminal end of EC-SOD form V which is responsible for the binding with heparin.	Heparin	120-127	superoxide dismutase 3	Homo sapiens	94-100
9821816-5	1998	It has been suggested that EC-SOD form V is the primary form synthesized in the body and that EC-SOD forms with reduced heparin affinity are the result of proteolytic truncation of the C-terminal end of EC-SOD form V which is responsible for the binding with heparin.	Heparin	120-127	superoxide dismutase 3	Homo sapiens	94-100
9821816-8	1998	The increase of plasma EC-SOD form V after heparin injection in CA+ patients was significantly less than that in subjects without evidence of stenosis in their major coronary arteries (CA- subjects).	Heparin	43-50	superoxide dismutase 3	Homo sapiens	23-29
9821816-9	1998	On the other hand, in CA+ patients, EC-SOD forms I to III, with low heparin affinity, were significantly increased compared to those in CA- subjects.	Heparin	68-75	superoxide dismutase 3	Homo sapiens	36-42
9739080-5	1998	The HB-GAM-induced mRNA localization is specifically inhibited by low concentrations of heparin and by heparitinase treatment of cells, showing that cell-surface heparin-type glycans are required for the effect.	Heparin	88-95	pleiotrophin	Homo sapiens	4-10
9884466-10	1998	There was a time-dependent reduction of the arterial response to vasopressin after incubation with heparin.	Heparin	99-106	arginine vasopressin	Homo sapiens	65-76
9831891-20	1998	An anti-mitogenic effect of heparin was also observed against responses to combined exposure to TGF-beta1 and EGF.	Heparin	28-35	LOC521832	Bos taurus	110-113
9824581-5	1998	METHODS: bFGF was isolated by heparin affinity chromatography and characterised by western blotting and endothelial cell bioassay.	Heparin	30-37	fibroblast growth factor 2	Homo sapiens	9-13
9824581-7	1998	Binding of bFGF by heparan sulphate proteoglycans was investigated by sodium chloride and heparin extraction.	Heparin	90-97	fibroblast growth factor 2	Homo sapiens	11-15
9733854-6	1998	After partial purification using three different columns (DEAE-Sepharose, Econo S, and heparin-agarose), LRP was primarily associated with cdk2-cyclin E complexes, an enzyme which is necessary for G1-to-S-phase cell cycle progression.	Heparin	87-94	ribosomal protein SA	Homo sapiens	105-108
9753626-6	1998	Lastly, we established that this proteoglycan, but not the collagenous proteins, interacted with at least one heparin binding domain of the collagenic tail of AChE.	Heparin	110-117	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-163
9855181-1	1998	A rapidly acting anticoagulant that can either inhibit thrombin generation or inhibit thrombin itself is the optimum therapy for acute thrombosis associated with heparin-induced thrombocytopenia (HIT).	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	55-63
9855181-1	1998	A rapidly acting anticoagulant that can either inhibit thrombin generation or inhibit thrombin itself is the optimum therapy for acute thrombosis associated with heparin-induced thrombocytopenia (HIT).	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	86-94
9798991-4	1998	Thrombin is protected on cell and fibrin surfaces from antithrombin, even in the presence of high doses of heparin (approximately 5 U/ml).	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	0-8
9798991-12	1998	These results indicated that addition of this novel thrombin (and kallikrein) inhibitor to heparin preserved platelet counts, decreased platelet secretion, and provided the additional benefit of partially blocking neutrophil activation during simulated extracorporeal circulation.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	52-60
9751678-0	1998	Effect of high- and low-molecular-weight heparins on thrombin-thrombomodulin interaction and protein C activation.	Heparin	41-49	coagulation factor II, thrombin	Homo sapiens	53-61
9751678-1	1998	BACKGROUND: Thrombin-thrombomodulin (TM) interaction, which is critical for accelerating the protein C anticoagulant pathway, involves the heparin-like domain of TM.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	12-20
9751678-2	1998	This study was aimed at investigating the possible effect of heparin on thrombin-TM binding and protein C activation.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	72-80
9751678-4	1998	Both experimental approaches showed that the affinity of thrombin-TM interaction was decreased by micromolar heparin concentrations.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	57-65
9751678-6	1998	Furthermore, it was also shown that the inhibitory effect of heparin was directly proportional to the heparin molecular mass (molecular weight range, 3 to 16 kDa), which suggests that the effect was mediated by formation of electrostatic bonds between heparin and thrombin.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	264-272
9751678-6	1998	Furthermore, it was also shown that the inhibitory effect of heparin was directly proportional to the heparin molecular mass (molecular weight range, 3 to 16 kDa), which suggests that the effect was mediated by formation of electrostatic bonds between heparin and thrombin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	264-272
9751678-6	1998	Furthermore, it was also shown that the inhibitory effect of heparin was directly proportional to the heparin molecular mass (molecular weight range, 3 to 16 kDa), which suggests that the effect was mediated by formation of electrostatic bonds between heparin and thrombin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	264-272
9751678-7	1998	CONCLUSIONS: These results indicate that heparin at therapeutic concentrations reduces the affinity of thrombin for TM and the rate of protein C activation.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	103-111
9740653-4	1998	We maintained localized high levels of FGF-10 in cultured lungs using FGF-10-soaked heparin beads.	Heparin	84-91	branchless	Drosophila melanogaster	39-42
9740653-4	1998	We maintained localized high levels of FGF-10 in cultured lungs using FGF-10-soaked heparin beads.	Heparin	84-91	branchless	Drosophila melanogaster	70-73
9748565-4	1998	Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	57-65
9774158-5	1998	Heparin in a dose-dependent manner attenuated the increase in iNOS expression and NO release after cytokine activation.	Heparin	0-7	nitric oxide synthase 2	Rattus norvegicus	62-66
10420071-1	1998	Unfractionated heparin (UFH) exerts its anticoagulant properties by increasing the inactivation of thrombin and activated factor X by antithrombin III.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	99-107
9760188-0	1998	Two distinct forms of human mast cell chymase--differences in affinity for heparin and in distribution in skin, heart, and other tissues.	Heparin	75-82	chymase 1	Homo sapiens	38-45
9760188-8	1998	Chymase C required higher concentrations of NaCl to overcome the stimulatory effects of heparin than did chymase B, but had a similar pH profile.	Heparin	88-95	chymase 1	Homo sapiens	0-7
9760188-9	1998	Thus, human chymase exists in at least two distinct but similar forms, and the differences in heparin binding and tissue distribution could have important consequences for enzyme function.	Heparin	94-101	chymase 1	Homo sapiens	12-19
9716571-6	1998	Mast cell-conditioned medium added to stromal cell culture medium in vitro along with added heparin (which stabilizes tryptase activity) resulted in the appearance of molecular weight forms indicative of active MMP-3 and MMP-1.	Heparin	92-99	matrix metallopeptidase 3	Homo sapiens	211-216
10420071-1	1998	Unfractionated heparin (UFH) exerts its anticoagulant properties by increasing the inactivation of thrombin and activated factor X by antithrombin III.	Heparin	24-27	coagulation factor II, thrombin	Homo sapiens	99-107
9693112-3	1998	Ligand blots demonstrated that vitronectin bound specifically to the heparin-binding outer-membrane protein OpaA, but that coating OpaA with the sulphated polysaccharide heparin was required for the interaction to occur.	Heparin	69-76	vitronectin	Cricetulus griseus	31-42
9741698-3	1998	We made the unexpected observation that apoE-deficient mice were resistant to heparin-induced lipolysis; this study aims at examining the underlying mechanism for this observation.	Heparin	78-85	apolipoprotein E	Mus musculus	40-44
9741698-5	1998	Unlike in wild-type mice where the injection of heparin reduced total plasma triglycerides by 50% and VLDL/CMR triglycerides by over 95%, the injection of heparin into apoE-deficient mice did not significantly affect plasma lipids.	Heparin	155-162	CD320 antigen	Mus musculus	102-106
9741698-5	1998	Unlike in wild-type mice where the injection of heparin reduced total plasma triglycerides by 50% and VLDL/CMR triglycerides by over 95%, the injection of heparin into apoE-deficient mice did not significantly affect plasma lipids.	Heparin	155-162	apolipoprotein E	Mus musculus	168-172
9778119-8	1998	These results raise two possibilities: that exogenous PlGF-1 (in spite of having a low affinity for heparin) was sequestered away from its receptor because of binding to heparan sulphate proteoglycans on the EVT cell surface or the ECM, or that HSPGs could modify the interaction between Flt-1 and PlGF.	Heparin	100-107	placental growth factor	Homo sapiens	54-58
9759611-3	1998	Heparin infusion, well known to inhibit thrombin generation by fostering antithrombin activity, inhibits the formation of platelet-derived procoagulant microparticles, probably by decreasing the formation of free thrombin, which, under our circumstances, is the main platelet activator.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	40-48
9759611-3	1998	Heparin infusion, well known to inhibit thrombin generation by fostering antithrombin activity, inhibits the formation of platelet-derived procoagulant microparticles, probably by decreasing the formation of free thrombin, which, under our circumstances, is the main platelet activator.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	77-85
9712843-4	1998	PlGF-1 and PlGF-3 differ from PlGF-2 since they lack the exon 6 encoded peptide which bestows upon PlGF-2 its heparin binding properties.	Heparin	110-117	placental growth factor	Homo sapiens	0-4
9712843-4	1998	PlGF-1 and PlGF-3 differ from PlGF-2 since they lack the exon 6 encoded peptide which bestows upon PlGF-2 its heparin binding properties.	Heparin	110-117	placental growth factor	Homo sapiens	11-15
9712843-4	1998	PlGF-1 and PlGF-3 differ from PlGF-2 since they lack the exon 6 encoded peptide which bestows upon PlGF-2 its heparin binding properties.	Heparin	110-117	placental growth factor	Homo sapiens	99-105
9712843-5	1998	Cross-linking experiments revealed that 125I-PlGF-2 binds to two endothelial cell surface receptors in a heparin dependent fashion.	Heparin	105-112	placental growth factor	Homo sapiens	45-51
9712843-11	1998	We have also determined, using chemically modified heparin species, that the presence of sulfate moieties on the glucosamine-O-6 and on the iduronic acid-O-2 groups of heparin was required for the potentiation of 125I-PlGF-2 binding to these receptors.	Heparin	168-175	placental growth factor	Homo sapiens	218-224
9693112-4	1998	Bound vitronectin could be dissociated from OpaA-heparin-vitronectin complexes by the addition of excess heparin, indicating that sulphated polysaccharides provided the main linkage between the two proteins.	Heparin	49-56	vitronectin	Cricetulus griseus	57-68
9693112-5	1998	Binding assays with intact micro-organisms substantiated the requirement of sulphated polysaccharides such as heparin and dextran sulphate for the efficient binding of vitronectin to OpaA+ gonococci.	Heparin	110-117	vitronectin	Cricetulus griseus	168-179
9698365-3	1998	Mutation of K64 and R68 caused the largest decrease in affinity for a heparin Sepharose matrix, with smaller effects seen with mutations of K20, R60, and K67.	Heparin	70-77	keratin 20	Homo sapiens	140-143
9698365-6	1998	These data identify a heparin-binding surface on IL-8 that includes the C-terminal alpha-helix and the proximal loop around residues 18-23.	Heparin	22-29	C-X-C motif chemokine ligand 8	Homo sapiens	49-53
9765911-0	1998	The role of heparin in the complex formation between fibroblast growth factor 2 and its high affinity receptor: comparative modelling and biochemical studies.	Heparin	12-19	fibroblast growth factor 2	Homo sapiens	53-79
9743246-1	1998	Heparin-selenocystamine conjugate, which was intended to mimic the heparin-selenoprotein P complex, was prepared.	Heparin	0-7	selenoprotein P	Homo sapiens	75-90
9688646-6	1998	The contraction induced by CCK was inhibited by the phospholipase C (PLC) inhibitor U-73122, anti-PLC-beta3 antibody, and the IP3 receptor antagonist heparin but was not inhibited by the the phospholipase D inhibitor propranolol or antibodies against PLC-beta1 or PLC-beta2.	Heparin	150-157	cholecystokinin	Homo sapiens	27-30
9792455-4	1998	Conversely, in a selenoprotein P-enriched plasma preparation obtained via heparin-Sepharose chromatography, protection against benzoate hydroxylation was above controls.	Heparin	74-81	selenoprotein P	Homo sapiens	17-32
9650567-10	1998	Expression of erb-B2 was also differently modulated by heparin in weakly metastatic vs. highly metastatic cells.	Heparin	55-62	erb-b2 receptor tyrosine kinase 2	Homo sapiens	14-20
9727607-8	1998	We also examined in vitro lipolysis using immobilized lipoprotein lipase (LPL) in a heparin affinity column.	Heparin	84-91	lipoprotein lipase	Rattus norvegicus	74-77
9700949-1	1998	The fibroblast growth factor (FGF) family is a group of homologous heparin-binding polypeptides that has been implicated in a variety of human neoplasms and presently includes 14 members.	Heparin	67-74	fibroblast growth factor 1	Homo sapiens	30-33
9716158-5	1998	By chemical cross-linking, we observed the formation of a complex between 125I-Ibalpha 269-287 and alpha-thrombin that was inhibited by hirudin, the C-terminal peptide of hirudin, sodium pyrophosphate but not by heparin.	Heparin	212-219	coagulation factor II, thrombin	Homo sapiens	105-113
9740346-9	1998	In vitro, both unfractionated and low molecular weight heparin inhibited thrombin-induced platelet activation, but stimulation of adenosine diphosphate responses was more marked with unfractionated than low molecular weight heparin.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	73-81
15992034-2	1998	Heparins inhibit thrombin and factor X and therefore may have useful effects on arterial and venous thrombosis; they are effective in the prevention and treatment of deep vein thrombosis (DVT) and pulmonary embolism (PE) and in the prevention of myocardial infarction (MI) in patients with unstable angina.	Heparin	0-8	coagulation factor II, thrombin	Homo sapiens	17-25
9703306-4	1998	We report a case of reversal of PLE with resolution of clinical symptoms and normalization of serum albumin, total protein, and fecal alpha1-antitrypsin values after several months of heparin treatment.	Heparin	184-191	serpin family A member 1	Homo sapiens	134-152
9711933-9	1998	Moreover the early increase of von Willebrand factor was more frequent and more severe with unfractionated heparin than with enoxaparin (mean change was +8.7+/-8.8% with enoxaparin versus +93.9+/-11.7% with unfractionated heparin, P&lt;0.0001).	Heparin	107-114	von Willebrand factor	Homo sapiens	31-52
9711933-9	1998	Moreover the early increase of von Willebrand factor was more frequent and more severe with unfractionated heparin than with enoxaparin (mean change was +8.7+/-8.8% with enoxaparin versus +93.9+/-11.7% with unfractionated heparin, P&lt;0.0001).	Heparin	222-229	von Willebrand factor	Homo sapiens	31-52
9650567-11	1998	In weakly metastatic cells, heparin reduced erb-B2 levels when cells were on plastic and fibronectin, while in strongly metastatic cells, erb-B2 was induced by heparin.	Heparin	28-35	erb-b2 receptor tyrosine kinase 2	Homo sapiens	44-50
9650567-11	1998	In weakly metastatic cells, heparin reduced erb-B2 levels when cells were on plastic and fibronectin, while in strongly metastatic cells, erb-B2 was induced by heparin.	Heparin	28-35	fibronectin 1	Homo sapiens	89-100
9650567-11	1998	In weakly metastatic cells, heparin reduced erb-B2 levels when cells were on plastic and fibronectin, while in strongly metastatic cells, erb-B2 was induced by heparin.	Heparin	160-167	erb-b2 receptor tyrosine kinase 2	Homo sapiens	138-144
9650567-13	1998	In KM12SM cells, amphiregulin was induced by heparin in cells on fibronectin and collagen IV.	Heparin	45-52	fibronectin 1	Homo sapiens	65-76
9647672-2	1998	The work described here provides further evidence that the PCI H helix, but not the D helix, has a major role in heparin-accelerated inhibition of APC and thrombin.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	155-163
9657752-5	1998	Combined treatment with an antibody to P-selectin or with low molecular weight heparin, a P-selectin antagonist, blocked the P-selectin, significantly reduced the arrest of PMNs, and delayed their removal in the liver.	Heparin	79-86	selectin P	Rattus norvegicus	90-100
9657752-5	1998	Combined treatment with an antibody to P-selectin or with low molecular weight heparin, a P-selectin antagonist, blocked the P-selectin, significantly reduced the arrest of PMNs, and delayed their removal in the liver.	Heparin	79-86	selectin P	Rattus norvegicus	90-100
9712292-0	1998	Heparin coating of tantalum coronary stents reduces surface thrombin generation but not factor IXa generation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	60-68
9712292-6	1998	However, the heparin coating drastically delayed the onset of thrombin generation and largely reduced the steady-state production of thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	62-70
9712292-6	1998	However, the heparin coating drastically delayed the onset of thrombin generation and largely reduced the steady-state production of thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	133-141
9712292-8	1998	The mode of action of immobilized heparin is thought to abrogate thrombin generation by inhibiting thrombin-dependent positive feedback reactions at the surface of the coronary stent.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	65-73
9676792-0	1998	Determinants of rebound thrombin activity after cessation of heparin in patients undergoing coronary interventions.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	24-32
9755294-7	1998	Heparin had a beneficial effect on the microcirculatory values, serum IL-6 concentration, and morphologic changes.	Heparin	0-7	interleukin 6	Rattus norvegicus	70-74
9688542-3	1998	Fragment alpha1VI/V, but not fragment alpha1V, bound to purified alpha1beta1 and alpha2beta1 integrins, to heparin, and to heparan sulfate-substituted domains I and V of perlecan.	Heparin	107-114	collagen type V alpha 1 chain	Homo sapiens	9-16
9662260-7	1998	In addition, we showed that CMDB7 inhibits specifically the mitogenic effects of the growth factors that bind to heparin such as FGF-2, FGF-4, platelet-derived growth factor (PDGF-BB) and transforming growth factor (TGF-beta1), but not those of epidermal growth factor (EGF) and insulin-like growth factor (IGF-1).	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	129-134
9662260-7	1998	In addition, we showed that CMDB7 inhibits specifically the mitogenic effects of the growth factors that bind to heparin such as FGF-2, FGF-4, platelet-derived growth factor (PDGF-BB) and transforming growth factor (TGF-beta1), but not those of epidermal growth factor (EGF) and insulin-like growth factor (IGF-1).	Heparin	113-120	fibroblast growth factor 4	Homo sapiens	136-141
9662260-7	1998	In addition, we showed that CMDB7 inhibits specifically the mitogenic effects of the growth factors that bind to heparin such as FGF-2, FGF-4, platelet-derived growth factor (PDGF-BB) and transforming growth factor (TGF-beta1), but not those of epidermal growth factor (EGF) and insulin-like growth factor (IGF-1).	Heparin	113-120	transforming growth factor beta 1	Homo sapiens	216-225
9662260-7	1998	In addition, we showed that CMDB7 inhibits specifically the mitogenic effects of the growth factors that bind to heparin such as FGF-2, FGF-4, platelet-derived growth factor (PDGF-BB) and transforming growth factor (TGF-beta1), but not those of epidermal growth factor (EGF) and insulin-like growth factor (IGF-1).	Heparin	113-120	insulin like growth factor 1	Homo sapiens	307-312
9712292-8	1998	The mode of action of immobilized heparin is thought to abrogate thrombin generation by inhibiting thrombin-dependent positive feedback reactions at the surface of the coronary stent.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	99-107
9676792-2	1998	Heparin administered during PCI is known to nonuniformly suppress thrombin activity in the coronary.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	66-74
9676792-4	1998	As a related consideration, rebound thrombin activity has been demonstrated in peripheral blood samples several hours after cessation of heparin therapy in patients with acute coronary syndromes.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	36-44
9676792-5	1998	Accordingly, we hypothesized that increased thrombin activity occurs in the coronary circulation after PCI and is induced by cessation of intravenous heparin to facilitate vascular sheath removal.	Heparin	150-157	coagulation factor II, thrombin	Homo sapiens	44-52
9676792-16	1998	An increase in thrombin activity occurs in the coronary circulation after PCI following discontinuation of heparin.	Heparin	107-114	coagulation factor II, thrombin	Homo sapiens	15-23
9664197-8	1998	The Global Utilization of Streptokinase and t-PA for Occluded Coronary Arteries (GUSTO-1) study demonstrated a further mortality reduction by early combination therapy of aspirin, intravenous heparin and alteplase vs aspirin, heparin (either intravenous or subcutaneous) plus streptokinase (from 7.3 to 6.3%).	Heparin	192-199	plasminogen activator, tissue type	Homo sapiens	44-48
9641623-3	1998	We studied both their anticoagulant activity and the catalysis of thrombin (T) inhibition by heparin cofactor II (HCII) and antithrombin (AT) in the presence of these dextran derivatives relative to heparin and dextran sulfate (DXSu).	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	66-74
9636026-8	1998	These three peptides were also selectively recognized by a neutralizing monoclonal antibody against KGF, though only in the presence of heparin.	Heparin	136-143	fibroblast growth factor 7	Homo sapiens	100-103
9733593-12	1998	Addition of zymosan-activated serum did not alter the permeability and addition of heparin inhibited the ZAP-induced changes in permeability, suggesting that these changes were mediated via thrombin and not complement.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	190-198
9620865-5	1998	Furthermore functional experiments demonstrated that GC binding to thrombin competes with heparin for thrombin inactivation by the antithrombin III-heparin complex as well.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	102-110
9616153-6	1998	In EDTA, heparin enhanced thrombin activation of GDPC by reducing the Km, but it inhibited PC activation by increasing the Km.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	26-34
9624135-3	1998	By using selectively modified heparin and heparan sulfate fragments in a nitrocellulose filter trapping system, we have analyzed sequence requirements for interleukin-8 binding to heparin/heparan sulfate.	Heparin	180-187	C-X-C motif chemokine ligand 8	Homo sapiens	155-168
9624135-4	1998	We demonstrate that the affinity of a monomeric interleukin-8 molecule for heparin/heparan sulfate is too weak to allow binding at physiological ionic strength, whereas the dimeric form of the protein mediates binding to two sulfated domains of heparan sulfate.	Heparin	75-82	C-X-C motif chemokine ligand 8	Homo sapiens	48-61
9616153-1	1998	A recent study indicated that negatively charged substances such as heparin and dextran sulfate accelerate thrombin activation of coagulation factor XI by a template mechanism.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	107-115
9616153-2	1998	Because the serine proteinase of the natural anticoagulant pathway, activated protein C, can bind heparin, it was reasonable to think that these compounds may also bind protein C (PC) and accelerate its activation by thrombin or other heparin binding plasma serine proteinases by a similar mechanism.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	217-225
9614116-1	1998	A heparin binding region is known to be present within the triple helical part of the alpha1(V) chain.	Heparin	2-9	collagen type V alpha 1 chain	Homo sapiens	86-95
9614116-2	1998	Here we show that a recombinant alpha1(V) fragment (Ile824 to Pro950), referred to as HepV, is sufficient for heparin binding at physiological ionic strength.	Heparin	110-117	collagen type V alpha 1 chain	Homo sapiens	32-41
9614116-3	1998	Both native individual alpha1(V) chains and HepV are eluted at identical NaCl concentrations (0.35 M) from a heparin-Sepharose column, and this binding can be inhibited specifically by the addition of free heparin or heparan sulfate.	Heparin	109-116	collagen type V alpha 1 chain	Homo sapiens	23-32
9614116-3	1998	Both native individual alpha1(V) chains and HepV are eluted at identical NaCl concentrations (0.35 M) from a heparin-Sepharose column, and this binding can be inhibited specifically by the addition of free heparin or heparan sulfate.	Heparin	206-213	collagen type V alpha 1 chain	Homo sapiens	23-32
9614116-7	1998	However, the affinities for heparin of each of the collagen V molecular forms tested are different and increase with the number of alpha1(V) chains incorporated in the molecules.	Heparin	28-35	collagen type V alpha 1 chain	Homo sapiens	131-140
9609730-7	1998	To regulate thrombin within this procoagulant environment, we have developed a novel anticoagulant, antithrombin-heparin covalent complex (ATH) that can be retained within the lung after intrapulmonary instillation.	Heparin	113-120	coagulation factor II	Rattus norvegicus	12-20
9618554-5	1998	The bradykinin pathway was suppressed by the phospholipase C inhibitor U-73122, by blocking the IP3 receptor with pentosan polysulfate or heparin, and by buffering intracellular calcium, and it was occluded by allowing IP3 to diffuse into the cytoplasm via a patch pipette.	Heparin	138-145	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	96-108
9659371-7	1998	The pICln-associated kinase displayed broad substrate specificity and was inhibited in a concentration-dependent manner by heparin, zinc and 5,6-dichloro-1-beta-D-ribofuranosylbenose (DRB).	Heparin	123-130	chloride nucleotide-sensitive channel 1A	Homo sapiens	4-9
9622482-1	1998	The solution structure of murine macrophage inflammatory protein-2 (MIP-2), a heparin-binding chemokine that is secreted in response to inflammatory stimuli, has been determined using two-dimensional homonuclear and heteronuclear NMR spectroscopy.	Heparin	78-85	chemokine (C-X-C motif) ligand 2	Mus musculus	33-66
9622482-1	1998	The solution structure of murine macrophage inflammatory protein-2 (MIP-2), a heparin-binding chemokine that is secreted in response to inflammatory stimuli, has been determined using two-dimensional homonuclear and heteronuclear NMR spectroscopy.	Heparin	78-85	chemokine (C-X-C motif) ligand 2	Mus musculus	68-73
9603953-6	1998	Both sPLA2s-IIA and -V, but not sPLA2-IIC, were heparin-binding PLA2s that exhibited significant affinity for cell-surface proteoglycans, and site-directed mutations in residues responsible for their membrane association or catalytic activity markedly reduced their ability to release AA from activated cells.	Heparin	48-55	phospholipase A2 group IB	Homo sapiens	6-10
9611131-3	1998	cADPR (10 nM-10 microM) induced a dose-dependent increase in [Ca2+]i, which was blocked by the cADPR receptor antagonist 8-amino-cADPR (20 microM) and by the RyR blockers ruthenium red (10 microM) and ryanodine (10 microM), but not by the inositol 1,4,5-trisphosphate receptor blocker heparin (0.5 mg/ml).	Heparin	285-292	ryanodine receptor 1, skeletal muscle	Mus musculus	158-161
9626825-9	1998	Among t-PA-treated patients, the rates were 10.9% with heparin and 10.3% with hirudin (OR 1.06, 95% CI 0.81 to 1.38, p = 0.68; for treatment heterogeneity: chi-square 4.20, degrees of freedom [df] 1, p = 0.04).	Heparin	55-62	plasminogen activator, tissue type	Homo sapiens	6-10
15992009-9	1998	At present, thrombin inhibitors are the most promising class of drugs for the initial therapy of patients with heparin-induced thrombocytopaenia (HIT) or the heparin-induced thrombocytopaenia and thrombosis syndrome (HITTS).	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	12-20
15992009-9	1998	At present, thrombin inhibitors are the most promising class of drugs for the initial therapy of patients with heparin-induced thrombocytopaenia (HIT) or the heparin-induced thrombocytopaenia and thrombosis syndrome (HITTS).	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	12-20
9669548-3	1998	We have used molecular modeling method to study the modes of binding of heparin or heparan sulfate proteoglycans (HSPGs) to bFGF that leads to the dimerization of FGF receptor 1 (FGFR1) and activation of receptor tyrosine kinase.	Heparin	72-79	fibroblast growth factor 2	Homo sapiens	124-128
9669548-3	1998	We have used molecular modeling method to study the modes of binding of heparin or heparan sulfate proteoglycans (HSPGs) to bFGF that leads to the dimerization of FGF receptor 1 (FGFR1) and activation of receptor tyrosine kinase.	Heparin	72-79	fibroblast growth factor receptor 1	Homo sapiens	163-177
9669548-3	1998	We have used molecular modeling method to study the modes of binding of heparin or heparan sulfate proteoglycans (HSPGs) to bFGF that leads to the dimerization of FGF receptor 1 (FGFR1) and activation of receptor tyrosine kinase.	Heparin	72-79	fibroblast growth factor receptor 1	Homo sapiens	179-184
9669548-4	1998	Homology model of FGFR1 Ig D(II)-D(III) domains was built to investigate the interactions between heparin, bFGF and FGFR1.	Heparin	98-105	fibroblast growth factor receptor 1	Homo sapiens	18-23
9669548-5	1998	The structural requirements to bridge the two monomeric bFGF molecules by heparin or HSPGs and to simulate the dimerization and activation of FGFR1 have been examined.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	56-60
9669548-6	1998	A structural model of the biologically functional dimeric bFGF-heparin complex is proposed based on: (a) the stability of dimeric complex, (b) the favorable binding energies between heparin and bFGF molecules, and (c) its accessibility to FGFR1.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	58-62
9669548-6	1998	A structural model of the biologically functional dimeric bFGF-heparin complex is proposed based on: (a) the stability of dimeric complex, (b) the favorable binding energies between heparin and bFGF molecules, and (c) its accessibility to FGFR1.	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	194-198
9669548-6	1998	A structural model of the biologically functional dimeric bFGF-heparin complex is proposed based on: (a) the stability of dimeric complex, (b) the favorable binding energies between heparin and bFGF molecules, and (c) its accessibility to FGFR1.	Heparin	63-70	fibroblast growth factor receptor 1	Homo sapiens	239-244
9669548-6	1998	A structural model of the biologically functional dimeric bFGF-heparin complex is proposed based on: (a) the stability of dimeric complex, (b) the favorable binding energies between heparin and bFGF molecules, and (c) its accessibility to FGFR1.	Heparin	182-189	fibroblast growth factor 2	Homo sapiens	58-62
9669548-7	1998	The modeled complex between heparin, bFGF and FGFR1 has a stoichiometry of 1 heparin: 2 bFGF: 2 FGFR1.	Heparin	28-35	fibroblast growth factor receptor 1	Homo sapiens	46-51
9669548-7	1998	The modeled complex between heparin, bFGF and FGFR1 has a stoichiometry of 1 heparin: 2 bFGF: 2 FGFR1.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	88-92
9669548-7	1998	The modeled complex between heparin, bFGF and FGFR1 has a stoichiometry of 1 heparin: 2 bFGF: 2 FGFR1.	Heparin	28-35	fibroblast growth factor receptor 1	Homo sapiens	96-101
9669548-7	1998	The modeled complex between heparin, bFGF and FGFR1 has a stoichiometry of 1 heparin: 2 bFGF: 2 FGFR1.	Heparin	77-84	fibroblast growth factor 2	Homo sapiens	37-41
9669548-7	1998	The modeled complex between heparin, bFGF and FGFR1 has a stoichiometry of 1 heparin: 2 bFGF: 2 FGFR1.	Heparin	77-84	fibroblast growth factor receptor 1	Homo sapiens	46-51
9669548-9	1998	In the proposed model heparin bridges the two bFGF monomers in a specific orientation and the resulting complex induces FGF receptor dimerization, suggesting that in the oligosaccharide induced recognition process sugars orient the molecules in a way that brings about specific protein-protein or protein-carbohydrate interactions.	Heparin	22-29	fibroblast growth factor 2	Homo sapiens	46-50
9643364-7	1998	Mutation of previously identified heparin-binding regions of LPL results in a relatively small decrease in heparin-binding affinity, as compared with mutations in this carboxyl-terminal region, indicating that Lys 321, Arg 405, Arg 407, Lys 409, and Lys 416 constitute the major heparin-binding domain in LPL.	Heparin	34-41	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	61-64
9643364-7	1998	Mutation of previously identified heparin-binding regions of LPL results in a relatively small decrease in heparin-binding affinity, as compared with mutations in this carboxyl-terminal region, indicating that Lys 321, Arg 405, Arg 407, Lys 409, and Lys 416 constitute the major heparin-binding domain in LPL.	Heparin	34-41	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	305-308
9643364-7	1998	Mutation of previously identified heparin-binding regions of LPL results in a relatively small decrease in heparin-binding affinity, as compared with mutations in this carboxyl-terminal region, indicating that Lys 321, Arg 405, Arg 407, Lys 409, and Lys 416 constitute the major heparin-binding domain in LPL.	Heparin	107-114	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	61-64
9654873-5	1998	Fibrinogen levels in the standard dacron group were significantly less than that of the PTFE and heparin-bound dacron groups (P &lt; 0.05).	Heparin	97-104	fibrinogen beta chain	Homo sapiens	0-10
9654873-7	1998	These findings suggest that heparin binding significantly reduces fibrinogen consumption and hence may reduce graft thrombogenicity.	Heparin	28-35	fibrinogen beta chain	Homo sapiens	66-76
9623978-4	1998	The ectodomain potently inhibits heparin-mediated FGF-2 mitogenicity because of the poorly sulfated domains in its heparin sulfate chains.	Heparin	33-40	fibroblast growth factor 2	Homo sapiens	50-55
9623978-5	1998	Degradation of these regions by platelet heparanase produces heparin-like heparin sulfate fragments that markedly activate FGF-2 mitogenicity and are found in wound fluids.	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	123-128
9626699-3	1998	C4BP is known to interact with heparin, C4b, complement factor I, serum amyloid P component, streptococcal Arp and Sir proteins, and factor VIII/VIIIa via its alpha-chains and with protein S through its beta-chain.	Heparin	31-38	complement component 4 binding protein alpha	Homo sapiens	0-4
9626699-7	1998	Analysis of the alpha-chain model, together with monoclonal antibody studies and heparin binding experiments, suggests that a patch of positively charged residues, at the interface between the first and second CCP modules, plays an important role in the interaction between C4BP and C4b/Arp/Sir/heparin.	Heparin	81-88	complement component 4 binding protein alpha	Homo sapiens	274-278
9631524-5	1998	The GST-Bax fusion protein was bound to glutathione-Sepharose, and Bax was released by thrombin cleavage and further purified by sequential chromatography on heparin-Sepharose and DEAE-Sepharose.	Heparin	158-165	BCL2 associated X, apoptosis regulator	Homo sapiens	8-11
9631524-5	1998	The GST-Bax fusion protein was bound to glutathione-Sepharose, and Bax was released by thrombin cleavage and further purified by sequential chromatography on heparin-Sepharose and DEAE-Sepharose.	Heparin	158-165	BCL2 associated X, apoptosis regulator	Homo sapiens	67-70
9626053-9	1998	In these cells, MMP-13 expression at the mRNA and protein level was potently enhanced (up to sixfold) by tumor necrosis factor-alpha, transforming growth factor-beta(1), and transforming growth factor-alpha and by keratinocyte growth factor in the presence of heparin.	Heparin	260-267	matrix metallopeptidase 13	Homo sapiens	16-22
9603780-4	1998	The heparin-rich secretory granules in HMCs were also labeled.	Heparin	4-11	MKKS centrosomal shuttling protein	Homo sapiens	39-43
9643364-7	1998	Mutation of previously identified heparin-binding regions of LPL results in a relatively small decrease in heparin-binding affinity, as compared with mutations in this carboxyl-terminal region, indicating that Lys 321, Arg 405, Arg 407, Lys 409, and Lys 416 constitute the major heparin-binding domain in LPL.	Heparin	107-114	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	61-64
9655178-0	1998	Association of myeloperoxidase with heparin: oxidative inactivation of proteins on the surface of endothelial cells by the bound enzyme.	Heparin	36-43	myeloperoxidase	Homo sapiens	15-30
9655178-1	1998	Chromatography of human myeloperoxidase (MPO) on a heparin-agarose column demonstrated a tight association of the protein with the resin.	Heparin	51-58	myeloperoxidase	Homo sapiens	24-39
9655178-1	1998	Chromatography of human myeloperoxidase (MPO) on a heparin-agarose column demonstrated a tight association of the protein with the resin.	Heparin	51-58	myeloperoxidase	Homo sapiens	41-44
9655178-6	1998	The oxidative modification of FIXBP was only partially dependent on the addition of hydrogen peroxide and was abolished by exogenous heparin which displaced MPO from the cell surface, emphasizing the functional differences between cell-bound and free enzyme.	Heparin	133-140	myeloperoxidase	Homo sapiens	157-160
9765662-11	1998	ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	97-105
9765662-11	1998	ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	97-105
9765662-13	1998	In addition, the inhibitory effect of the AT-heparin complex is limited for thrombin bound to the thrombus.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	76-84
9657442-0	1998	Aging and venous thromboembolism influence the pharmacodynamics of the anti-factor Xa and anti-thrombin activities of a low molecular weight heparin (nadroparin).	Heparin	141-148	coagulation factor II, thrombin	Homo sapiens	95-103
9657442-10	1998	These results suggest that the mechanisms involved in the clearance of polysaccharide chains which support the anti-thrombin activity are different from those of the anti-factor Xa activity and that the enhanced binding properties of plasma proteins to unfractionated heparin reported in patients presenting an acute venous thromboembolism also exists for LMWH, predominantly for the anti-thrombin activity.	Heparin	268-275	coagulation factor II, thrombin	Homo sapiens	389-397
9626825-10	1998	After adjustment for baseline differences between thrombolytic groups, the rates were 9.1% for SK with hirudin, 10.3% for t-PA with hirudin, 10.5% for t-PA with heparin and 14.9% for SK with heparin (for treatment heterogeneity: chi-square 4.5, df 1, p = 0.03), suggesting that the beneficial treatment effect of hirudin was limited to the SK-treated patients.	Heparin	161-168	plasminogen activator, tissue type	Homo sapiens	151-155
9871735-0	1998	In vitro evaluation of synthetic heparin-like conjugates comprising different thrombin binding domains.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	78-86
9633524-6	1998	Taken together these results show that the two soluble VEGF receptor proteins, sFLT-1 and sKDR, despite binding the same ligand, behave very differently when immobilized with regard to their dependence on heparin for VEGF binding.	Heparin	205-212	vascular endothelial growth factor A	Homo sapiens	55-59
9633524-6	1998	Taken together these results show that the two soluble VEGF receptor proteins, sFLT-1 and sKDR, despite binding the same ligand, behave very differently when immobilized with regard to their dependence on heparin for VEGF binding.	Heparin	205-212	vascular endothelial growth factor A	Homo sapiens	217-221
9633525-1	1998	The heparin-binding growth-associated molecule HB-GAM (also named pleiotrophin) and the retinoic acid-induced heparin-binding protein RIHB (chicken midkine) are developmentally regulated proteins forming a new family of heparin-binding molecules with putative functions during cell growth and differentiation.	Heparin	4-11	midkine (neurite growth-promoting factor 2)	Gallus gallus	134-138
9582367-8	1998	The mitogenic activity of FGF-10 could be distinguished from that of KGF by its different sensitivity to heparin and lack of neutralization by a KGF monoclonal antibody.	Heparin	105-112	fibroblast growth factor 10	Homo sapiens	26-32
9634701-0	1998	Solution structure of the heparin-binding domain of vascular endothelial growth factor.	Heparin	26-33	vascular endothelial growth factor A	Homo sapiens	52-86
9634701-3	1998	The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate.	Heparin	103-110	vascular endothelial growth factor A	Homo sapiens	15-19
9634701-3	1998	The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate.	Heparin	103-110	fms related receptor tyrosine kinase 1	Homo sapiens	56-61
9634701-3	1998	The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate.	Heparin	149-156	vascular endothelial growth factor A	Homo sapiens	15-19
9634701-3	1998	The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate.	Heparin	149-156	fms related receptor tyrosine kinase 1	Homo sapiens	56-61
9634701-4	1998	Heparin binding to VEGF165, the most abundantly expressed isoform of VEGF, has been localized to the carboxy-terminal 55 residues; plasmin cleavage of VEGF165 yields a homodimeric 110-residue amino-terminal receptor-binding domain (VEGF110) and two 55-residue carboxy-terminal heparin-binding fragments.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	19-23
9634701-4	1998	Heparin binding to VEGF165, the most abundantly expressed isoform of VEGF, has been localized to the carboxy-terminal 55 residues; plasmin cleavage of VEGF165 yields a homodimeric 110-residue amino-terminal receptor-binding domain (VEGF110) and two 55-residue carboxy-terminal heparin-binding fragments.	Heparin	277-284	vascular endothelial growth factor A	Homo sapiens	19-23
9634701-9	1998	CONCLUSIONS: The heparin-binding domain of VEGF has no significant sequence or structural similarity to any known proteins and thus represents a novel heparin-binding domain.	Heparin	17-24	vascular endothelial growth factor A	Homo sapiens	43-47
9634701-9	1998	CONCLUSIONS: The heparin-binding domain of VEGF has no significant sequence or structural similarity to any known proteins and thus represents a novel heparin-binding domain.	Heparin	151-158	vascular endothelial growth factor A	Homo sapiens	43-47
9600090-8	1998	In the presence of exogenous heparin, the mitogenic activity of ovine FGF-1 is potentiated slightly.	Heparin	29-36	fibroblast growth factor 1	Homo sapiens	70-75
9648240-0	1998	Interaction between the carboxyl-terminal heparin-binding domain of fibronectin and (-)-epigallocatechin gallate.	Heparin	42-49	fibronectin 1	Homo sapiens	68-79
9558385-9	1998	In the presence of heparin, PF-4 abolished totally the stimulatory effect of heparin.	Heparin	19-26	platelet factor 4	Mus musculus	28-32
9558385-9	1998	In the presence of heparin, PF-4 abolished totally the stimulatory effect of heparin.	Heparin	77-84	platelet factor 4	Mus musculus	28-32
9558385-10	1998	Furthermore, PF-4 complexed to FGF-2 and inhibited endogenous or heparin-induced FGF-2 dimerization.	Heparin	65-72	platelet factor 4	Mus musculus	13-17
9597549-0	1998	Further characterization of the binding of human recombinant interleukin 2 to heparin and identification of putative binding sites.	Heparin	78-85	interleukin 2	Homo sapiens	61-74
9645599-4	1998	OBJECTIVE: The purpose of this study was to investigate the effect of heparin, heparan sulphate and alpha2-macroglobulin on IL-8 binding to neutrophils and subsequent functional effects in vitro.	Heparin	70-77	C-X-C motif chemokine ligand 8	Homo sapiens	124-128
9645599-7	1998	RESULTS: Heparin, but not heparan sulphate, inhibited the binding of 125I-IL-8 to neutrophils (IC50=26 microg/mL) and IL-8 induced neutrophil chemotactic responses (IC50=4 microg/mL).	Heparin	9-16	C-X-C motif chemokine ligand 8	Homo sapiens	74-78
9645599-7	1998	RESULTS: Heparin, but not heparan sulphate, inhibited the binding of 125I-IL-8 to neutrophils (IC50=26 microg/mL) and IL-8 induced neutrophil chemotactic responses (IC50=4 microg/mL).	Heparin	9-16	C-X-C motif chemokine ligand 8	Homo sapiens	118-122
9645599-8	1998	The specific inhibitory effect of heparin was apparently due to an interaction with IL-8 which was charge-dependent, since dextran sulphate had a greater inhibitory effect on chemotactic responses (IC50=2 microg/mL) and FITC-heparin did not bind to neutrophils.	Heparin	34-41	C-X-C motif chemokine ligand 8	Homo sapiens	84-88
9645599-9	1998	The heparin-induced inhibition of IL-8 binding and chemotactic responses was reversed in a dose-dependent manner in the presence of alpha2-macroglobulin.	Heparin	4-11	C-X-C motif chemokine ligand 8	Homo sapiens	34-38
9564830-7	1998	Both GDP-beta-S and heparin inhibit the AVP response.	Heparin	20-27	arginine vasopressin	Rattus norvegicus	40-43
9597549-1	1998	We have previously provided compelling evidence that human recombinant interleukin 2 (IL-2) binds to the sulfated polysaccharides heparin, highly sulfated heparan sulfate and fucoidan.	Heparin	130-137	interleukin 2	Homo sapiens	71-84
9597549-1	1998	We have previously provided compelling evidence that human recombinant interleukin 2 (IL-2) binds to the sulfated polysaccharides heparin, highly sulfated heparan sulfate and fucoidan.	Heparin	130-137	interleukin 2	Homo sapiens	86-90
9597549-2	1998	Here we show that IL-2 binding is dependent on heparin chain length, but with fragments as small as 15-mers retaining binding activity.	Heparin	47-54	interleukin 2	Homo sapiens	18-22
9597549-5	1998	IL-2 bound by heparin is still recognized by two IL-2 specific monoclonal antibodies, 3H9 and H2-8, whose epitopes lie in the amino terminal region.	Heparin	14-21	interleukin 2	Homo sapiens	0-4
9597549-5	1998	IL-2 bound by heparin is still recognized by two IL-2 specific monoclonal antibodies, 3H9 and H2-8, whose epitopes lie in the amino terminal region.	Heparin	14-21	interleukin 2	Homo sapiens	49-53
9597549-7	1998	Human IL-2 analogs with single amino acid substitutions at positions Lys43, Thr51, and Gln126 analogs no longer bind to heparin.	Heparin	120-127	interleukin 2	Homo sapiens	6-10
9597549-9	1998	These experimental findings together with molecular modeling studies suggest two putative heparin binding sites on human IL-2, one involving four basic residues, Lys48, Lys49, Lys54, and His55, and the other being a discontinuous site comprising Lys43, Lys64, Arg81, and Arg83.	Heparin	90-97	interleukin 2	Homo sapiens	121-125
9597549-11	1998	Overall our data suggest that the binding of human IL-2 to heparin and heparan sulfate does not interfere with IL-2/IL-2 receptor interactions.	Heparin	59-66	interleukin 2	Homo sapiens	51-55
9562618-0	1998	Increased serum midkine levels during hemodialysis using heparin in chronic renal failure.	Heparin	57-64	midkine	Homo sapiens	16-23
9556569-1	1998	Interferon-gamma (IFNgamma), in common with a number of growth factors, binds both to heparan sulfate or heparin-related molecules and to a specific high affinity receptor (IFNgammaR).	Heparin	105-112	interferon gamma	Homo sapiens	0-16
9556569-1	1998	Interferon-gamma (IFNgamma), in common with a number of growth factors, binds both to heparan sulfate or heparin-related molecules and to a specific high affinity receptor (IFNgammaR).	Heparin	105-112	interferon gamma	Homo sapiens	18-26
9556569-6	1998	This binding assay was used to investigate a possible role of heparin in the IFNgamma.IFNgammaR complex formation.	Heparin	62-69	interferon gamma	Homo sapiens	77-85
9556569-7	1998	In contrast to growth factors for which binding to heparin is usually required for high affinity receptor interaction, we found in this study that IFNgamma bound to heparin displayed a strongly reduced affinity for its receptor.	Heparin	51-58	interferon gamma	Homo sapiens	147-155
9556569-7	1998	In contrast to growth factors for which binding to heparin is usually required for high affinity receptor interaction, we found in this study that IFNgamma bound to heparin displayed a strongly reduced affinity for its receptor.	Heparin	165-172	interferon gamma	Homo sapiens	147-155
9556569-9	1998	To understand how a single domain of IFNgamma could be implicated in two discrete functions (i.e. binding to heparin and to IFNgammaR), we also analyzed in a detailed manner the role of the IFNgamma carboxyl-terminal sequence in receptor binding.	Heparin	109-116	interferon gamma	Homo sapiens	37-45
9556569-10	1998	Using forms of IFNgamma, with carboxyl terminus truncations of defined regions of the heparin binding sequence, we found that the C1 domain functioned by increasing the on rate of the IFNgamma.IFNgammaR binding reaction but was not otherwise required for the stability of the complex.	Heparin	86-93	interferon gamma	Homo sapiens	15-23
9556569-10	1998	Using forms of IFNgamma, with carboxyl terminus truncations of defined regions of the heparin binding sequence, we found that the C1 domain functioned by increasing the on rate of the IFNgamma.IFNgammaR binding reaction but was not otherwise required for the stability of the complex.	Heparin	86-93	interferon gamma	Homo sapiens	184-192
9562618-3	1998	Although no significant difference was found between control serum and serum before dialysis in HD patients, serum MK levels increased significantly at the early stage of HD sessions using heparin and gradually decreased after dialysis.	Heparin	189-196	midkine	Homo sapiens	115-117
9562618-4	1998	In normal controls, intravenous administration of heparin induced a similar sudden increase of MK, but the subsequent decrease was also rapid.	Heparin	50-57	midkine	Homo sapiens	95-97
9562618-5	1998	In an in vitro study, MK was released in time- and heparin-dose dependent manner from cultured vessels, but not from peripheral leukocytes.	Heparin	51-58	midkine	Homo sapiens	22-24
9562618-6	1998	These results indicate that, in HD patients, MK is released mainly from endothelial cells immediately after administration of heparin during HD and disappears gradually from blood due to renal impairment.	Heparin	126-133	midkine	Homo sapiens	45-47
9609229-0	1998	Cytokine gene expression in human LPS- and IFNgamma-stimulated mononuclear cells is inhibited by heparin.	Heparin	97-104	interferon gamma	Homo sapiens	43-51
9623549-12	1998	DISCUSSION: These results suggest that the expression of caldesmon in glomeruli is associated with the progression of IgA nephropathy, and that glucocorticoid heparin therapy may reverse the phenotype of mesangial cells during the disease process of glomerulonephritis.	Heparin	159-166	caldesmon 1	Homo sapiens	57-66
9848182-2	1998	Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	27-35
9848182-2	1998	Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated.	Heparin	252-259	coagulation factor II, thrombin	Homo sapiens	27-35
9609229-3	1998	we studied the effect of heparin on IL-1beta, IL-6 and TNFalpha mRNAs in human lipopolysaccharide-(LPS)- or interferon-gamma(IFN-gamma)-stimulated mononuclear cells.	Heparin	25-32	interferon gamma	Homo sapiens	108-134
9653887-7	1998	Heparin exerted both anti-FXa and anti-thrombin activity in a dose-dependent manner.	Heparin	0-7	coagulation factor II	Rattus norvegicus	39-47
9535876-9	1998	F2 and sF2-(63-116) bind to exosite II on thrombin because both reduce the heparin-catalyzed rate of thrombin inhibition by antithrombin approximately 4-fold.	Heparin	75-82	coagulation factor II	Rattus norvegicus	0-2
9531587-9	1998	The p34-58, unlike PF4, lacked affinity for heparin and its inhibitory activity could not be abrogated by the addition of heparin.	Heparin	44-51	alpha- and gamma-adaptin binding protein	Mus musculus	4-7
17029698-10	1998	261 (1986) 3214-3221] for the stoichiometric titration of heparin with thrombin.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	71-79
9535876-9	1998	F2 and sF2-(63-116) bind to exosite II on thrombin because both reduce the heparin-catalyzed rate of thrombin inhibition by antithrombin approximately 4-fold.	Heparin	75-82	coagulation factor II, thrombin	Homo sapiens	42-50
9535876-9	1998	F2 and sF2-(63-116) bind to exosite II on thrombin because both reduce the heparin-catalyzed rate of thrombin inhibition by antithrombin approximately 4-fold.	Heparin	75-82	coagulation factor II, thrombin	Homo sapiens	101-109
9683928-0	1998	Heparin inhibits mesenteric vascular hypertrophy in angiotensin II-infusion hypertension in rats.	Heparin	0-7	angiotensinogen	Rattus norvegicus	52-66
9539494-2	1998	The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	79-87
9683928-2	1998	In order to better understand mechanisms of angiotensin II induced vascular hypertrophy, this study aimed to determine whether heparin, a potent inhibitor of smooth muscle proliferation mechanisms, was able to inhibit vascular hypertrophy.	Heparin	127-134	angiotensinogen	Rattus norvegicus	44-58
9597517-2	1998	The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	79-87
9568695-5	1998	The binding of human amylin to perlecan was similarly observed using perlecan heparan sulfate glycosaminoglycans (GAGs), and was completely abolished by 10 micromol/l heparin.	Heparin	167-174	heparan sulfate proteoglycan 2	Rattus norvegicus	31-39
9578489-0	1998	The conversion of recombinant human mast cell prochymase to enzymatically active chymase by dipeptidyl peptidase I is inhibited by heparin and histamine.	Heparin	131-138	chymase 1	Homo sapiens	49-56
9578489-3	1998	The gene for human chymase was cloned in a baculovirus vector and expressed in High Five insect cells, and the recombinant protein purified by heparin-agarose and gel-filtration chromatography.	Heparin	143-150	chymase 1	Homo sapiens	19-26
9490688-2	1998	The A1, A2, and A3 domains in vWF mediate binding to glycoprotein Ib, ristocetin, botrocetin, collagen, sulphatides, and heparin and provide a protease cleavage site.	Heparin	121-128	von Willebrand factor	Homo sapiens	30-33
9613830-0	1998	Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides.	Heparin	25-32	fibroblast growth factor receptor 1	Homo sapiens	101-107
9613830-0	1998	Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides.	Heparin	114-121	fibroblast growth factor receptor 1	Homo sapiens	101-107
9613830-1	1998	We have examined structure-function relationships that have been proposed to account for the heparin-binding properties of basic fibroblast growth factor and its receptor, FGFR-1, using synthetic peptides, DNA synthesis assays and binding assays in a resonant mirror biosensor.	Heparin	93-100	fibroblast growth factor receptor 1	Homo sapiens	172-178
9613830-2	1998	The results suggest that the interaction of FGFR-1 with heparin may not be physiologically relevant and that the site of interaction of the polysaccharide on bFGF is more complex than has been anticipated.	Heparin	56-63	fibroblast growth factor receptor 1	Homo sapiens	44-50
9529385-11	1998	Furthermore, this study contributes to the understanding of the physiological role of the strongly heparin-binding VEGF isoforms, since these were found for the first time to be expressed in an activation-dependent manner in HMC-1 cells.	Heparin	99-106	vascular endothelial growth factor A	Homo sapiens	115-119
9501097-4	1998	CRP can be removed from the malT ternary complex by a moderate concentration of heparin.	Heparin	80-87	C-reactive protein	Homo sapiens	0-3
9501097-7	1998	A very high concentration of heparin is able to dissociate CRP from the galP1 ternary complex without changing the properties of the complex.	Heparin	29-36	C-reactive protein	Homo sapiens	59-62
9730255-6	1998	Furthermore, the enhancement of phagocytosis by aFGF(1-29) was suppressed by heparin (100 microg/ml).	Heparin	77-84	fibroblast growth factor 1	Mus musculus	48-52
9521691-11	1998	Since lysine and arginine residues in apoB are known to interact with the LDL receptors and heparin, we studied the effect of different glycosaminoglycans on apoB-MTP interactions.	Heparin	92-99	apolipoprotein B	Homo sapiens	38-42
9490688-12	1998	Because heparin binding inhibits the interaction with GpIb, this provides an explanation of vWF upregulation.	Heparin	8-15	von Willebrand factor	Homo sapiens	92-95
9521646-1	1998	Regulation of the inhibitory activity of antithrombin, the principal inhibitor of the blood-clotting proteinases factor Xa and thrombin, is accomplished by binding to heparin.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	45-53
9497365-6	1998	Finally, mutagenesis of PAI-1 results in loss of LRP binding, confirming that the high affinity binding site is located on PAI-1 and suggesting that the LRP binding site lays within a region of PAI-1 previously shown to contain the heparin binding domain.	Heparin	232-239	LDL receptor related protein 1	Homo sapiens	153-156
9485475-14	1998	These results suggest that binding of heparin to thrombin induces an allosteric effect causing destabilization of the thrombin-HCII(L444R) complex and that the allosteric effect may be mediated by the 60-loop.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	118-126
10087435-0	1998	Increase in thrombin generation after coronary thrombolysis with rt-PA or streptokinase with simultaneous heparin versus heparin alone.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	12-20
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	72-79	coagulation factor II, thrombin	Homo sapiens	36-44
9485475-3	1998	We recently observed that heparin induces dissociation of complexes containing thrombin and the reactive site mutant HCII(L444R) to yield active thrombin and cleaved inhibitor (Han, J.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	79-87
9485475-3	1998	We recently observed that heparin induces dissociation of complexes containing thrombin and the reactive site mutant HCII(L444R) to yield active thrombin and cleaved inhibitor (Han, J.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	145-153
9485475-7	1998	In the current study, we have investigated the mechanism by which heparin induces dissociation of the thrombin-HCII(L444R) complex.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	102-110
9485475-10	1998	By contrast, binding of heparin to thrombin appears to be necessary and sufficient to induce dissociation.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	35-43
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	73-81
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	143-151
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	73-81
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	143-151
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	41-49
9485475-14	1998	These results suggest that binding of heparin to thrombin induces an allosteric effect causing destabilization of the thrombin-HCII(L444R) complex and that the allosteric effect may be mediated by the 60-loop.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	49-57
9495276-4	1998	Heparin perfusion of the isolated Langendorff heart induced the release of LPL activity.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	75-78
9495276-6	1998	However, induction of streptozotocin-induced diabetes in SHR, as in Wistar rats, increased peak heparin-releasable LPL activity in perfused hearts.	Heparin	96-103	lipoprotein lipase	Rattus norvegicus	115-118
9495276-7	1998	The elevated heparin-releasable LPL peak could not be accounted for by enhanced LPL synthesis in that both cellular and surface-bound LPL activities in myocytes from SHR-diabetic rats were low relative to control.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	32-35
9495276-8	1998	Chronic (12-day) insulin treatment of SHR-diabetic rats reduced the augmented heparin-releasable LPL activity and increased cell-associated LPL activity.	Heparin	78-85	lipoprotein lipase	Rattus norvegicus	97-100
9495276-9	1998	Moreover, acute (90-minute) treatment of SHR-diabetic rats with rapid-acting insulin also reduced the heparin-releasable LPL activity to normal, although it had no effect on the low cellular LPL activity.	Heparin	102-109	lipoprotein lipase	Rattus norvegicus	121-124
9659449-9	1998	P-selectin mediated platelet-neutrophil rosettes formation was also tested in vitro in the presence of HEP and ENOX.	Heparin	103-106	selectin P	Canis lupus familiaris	0-10
9551799-1	1998	Affinity capillary electrophoresis (CE) was used for a detailed characterization of the binding between heparin and a peptide isolated from the heparin-binding serum protein amyloid P component (SAP).	Heparin	104-111	SH2 domain containing 1A	Homo sapiens	195-198
10087435-0	1998	Increase in thrombin generation after coronary thrombolysis with rt-PA or streptokinase with simultaneous heparin versus heparin alone.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	12-20
10087435-1	1998	This study compares the extent of inhibition of thrombin generation and activity achieved in patients with acute myocardial infarction receiving fibrinolytic treatment (streptokinase SK, or rt-PA) and concomitant intravenous heparin treatment adjusted to the patients" weight with that achieved with the same heparin regimen but without fibrinolytic therapy.	Heparin	225-232	coagulation factor II, thrombin	Homo sapiens	48-56
10087435-1	1998	This study compares the extent of inhibition of thrombin generation and activity achieved in patients with acute myocardial infarction receiving fibrinolytic treatment (streptokinase SK, or rt-PA) and concomitant intravenous heparin treatment adjusted to the patients" weight with that achieved with the same heparin regimen but without fibrinolytic therapy.	Heparin	309-316	coagulation factor II, thrombin	Homo sapiens	48-56
10087435-6	1998	After thrombolytic therapy with both SK and rt-PA, there was an increase in thrombin generation, although high-dose intravenous heparin inhibited the different increases in thrombin associated with the thrombolytic agents to the same extent.	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	173-181
9548597-9	1998	Both apoE2 (Arg136 --&gt; Cys) and apoE2 (Arg158 --&gt; Cys) displayed substantial heparin binding (61 and 53% of apoE3, respectively).	Heparin	83-90	apolipoprotein E	Homo sapiens	5-10
9502626-0	1998	Thrombin generation, inhibition and clinical outcomes in patients with acute myocardial infarction treated with thrombolytic therapy and heparin: results from the GUSTO-I Trial.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	0-8
9502626-11	1998	Thrombin activity, measured by FPA, was as closely related to aPTT as to the heparin level.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	0-8
9502626-13	1998	CONCLUSIONS: Although intravenous heparin partly suppresses the increased thrombin activity associated with thrombolysis, it does not inhibit thrombin generation.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	74-82
9462701-4	1998	Intracellular pre-loading of the InsP3 receptor antagonist heparin or the Ca2+ chelator EGTA clearly prevented both inward and outward currents, indicating that activation of Ca2+-dependent Cl- and K+ currents underlies the inward and the outward currents.	Heparin	59-66	carbonic anhydrase 2	Rattus norvegicus	175-178
9548597-9	1998	Both apoE2 (Arg136 --&gt; Cys) and apoE2 (Arg158 --&gt; Cys) displayed substantial heparin binding (61 and 53% of apoE3, respectively).	Heparin	83-90	apolipoprotein E	Homo sapiens	35-40
9548597-9	1998	Both apoE2 (Arg136 --&gt; Cys) and apoE2 (Arg158 --&gt; Cys) displayed substantial heparin binding (61 and 53% of apoE3, respectively).	Heparin	83-90	apolipoprotein E	Homo sapiens	114-119
9548597-11	1998	These findings lend support to the concept that apoE variants predisposing to dominant type III hyperlipoproteinemia differ from recessive mutations by a more severe defect in heparin binding.	Heparin	176-183	apolipoprotein E	Homo sapiens	48-52
9531028-0	1998	Low-molecular weight heparin reduces the generation and activity of thrombin in unstable coronary artery disease.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	68-76
9541411-1	1998	The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	61-69
9541411-1	1998	The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	61-69
9577163-6	1998	Although aspirin and heparin have been the conventionally used agents for inhibiting thrombin and platelet function, newer agents such as hirudin or hirulog and inhibitors of the platelet glycoprotein IIb-IIIa receptors are becoming available, and their clinical application will increase in the future.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	85-93
9634715-1	1998	The inhibitory effects of sulfated polysaccharides-fucoidan and heparin on P-selectin-ligand interaction in vitro and on the ability of fucoidan to inhibit the leukocyte extravasation in rat peritonitis were studied.	Heparin	64-71	selectin P	Rattus norvegicus	75-85
9468491-2	1998	We investigated the effect of VEGF on heparin-binding epidermal growth factor-like growth factor (HB-EGF) expression in human umbilical vein endothelial cells.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	30-34
9634715-3	1998	Fucoidan and heparin inhibited binding of labeled ligand to both purified P-selectin and the activated platelets expressing P-selectin on their surface.	Heparin	13-20	selectin P	Rattus norvegicus	74-84
9634715-3	1998	Fucoidan and heparin inhibited binding of labeled ligand to both purified P-selectin and the activated platelets expressing P-selectin on their surface.	Heparin	13-20	selectin P	Rattus norvegicus	124-134
9485375-7	1998	Tryptase competed with thrombin in clotting assays using pure fibrinogen with heparin or blood plasma in the absence of heparin.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	23-31
9453569-0	1998	Heparin oligosaccharides that pass the blood-brain barrier inhibit beta-amyloid precursor protein secretion and heparin binding to beta-amyloid peptide.	Heparin	112-119	amyloid beta precursor protein	Homo sapiens	131-151
9494024-6	1998	Heparin inhibits thrombin bound to fibrin degradation products less effectively than free thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	17-25
9494024-9	1998	Like clot-bound thrombin, thrombin bound to fibrin derivatives is protected from inhibition by heparin but susceptible to inactivation by direct thrombin inhibitors.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	16-24
9494024-9	1998	Like clot-bound thrombin, thrombin bound to fibrin derivatives is protected from inhibition by heparin but susceptible to inactivation by direct thrombin inhibitors.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	26-34
9494024-9	1998	Like clot-bound thrombin, thrombin bound to fibrin derivatives is protected from inhibition by heparin but susceptible to inactivation by direct thrombin inhibitors.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	26-34
9543101-4	1998	Mac-1 (CD11b/CD18), a monocytic counter-receptor for intercellular adhesion molecule-1 (ICAM-1), that also binds to heparin, is present on Mono Mac 6 but not on U937 cells, and may thus explain these differences in adhesion.	Heparin	116-123	integrin subunit beta 2	Homo sapiens	13-17
9451022-3	1998	Under identical experimental conditions the binding of3H-heparin to a recombinant soluble form of the cellular receptor for gp120, CD4, is negligible.	Heparin	56-64	CD4 molecule	Homo sapiens	131-134
9452495-1	1998	The G401 cell line derived from a rhabdoid tumor of the kidney secretes the heparin-binding growth factors midkine and pleiotrophin.	Heparin	76-83	midkine	Homo sapiens	107-114
9452495-1	1998	The G401 cell line derived from a rhabdoid tumor of the kidney secretes the heparin-binding growth factors midkine and pleiotrophin.	Heparin	76-83	pleiotrophin	Homo sapiens	119-131
9524068-5	1998	Treatment of the chymase-fusion protein with enterokinase or the tryptase-fusion protein with enterokinase in the presence of a highly charged polysaccharide (dextran sulfate or heparin) produced enzymatically active proteases with properties of the native enzymes.	Heparin	178-185	chymase 1	Homo sapiens	17-24
9635164-0	1998	Heparin-releasable lipoprotein lipase activity is increased in cardiomyocytes after culture.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-37
9635164-4	1998	The heparin-induced release of LPL activity into the medium of cultured cardiomyocytes (198 nmol.h-1.mg-1) was much greater than heparin-releasable LPL (HR-LPL) activity (59 nmol.h-1.mg-1) from freshly isolated cells.	Heparin	4-11	lipoprotein lipase	Rattus norvegicus	31-34
9635164-4	1998	The heparin-induced release of LPL activity into the medium of cultured cardiomyocytes (198 nmol.h-1.mg-1) was much greater than heparin-releasable LPL (HR-LPL) activity (59 nmol.h-1.mg-1) from freshly isolated cells.	Heparin	129-136	lipoprotein lipase	Rattus norvegicus	148-151
9635164-4	1998	The heparin-induced release of LPL activity into the medium of cultured cardiomyocytes (198 nmol.h-1.mg-1) was much greater than heparin-releasable LPL (HR-LPL) activity (59 nmol.h-1.mg-1) from freshly isolated cells.	Heparin	129-136	lipoprotein lipase	Rattus norvegicus	148-151
9462649-5	1998	Reduction in the extent of hemostasis by the treatment with heparin (thrombin inhibitor) or cyproheptadine (serotonin inhibitor) decreased hepatic injury.	Heparin	60-67	coagulation factor II	Mus musculus	69-77
9453569-1	1998	We have previously demonstrated that full-length heparin stimulates the synthesis and secretion of beta-amyloid precursor protein (APP) through an amyloidogenic pathway in neuroblastoma cells.	Heparin	49-56	amyloid beta precursor protein	Homo sapiens	99-129
9507993-1	1998	The acute effects of intravenous heparin administration (50 U/kg body weight) on apolipoprotein (apo)B-48 and apoB-100-containing lipoproteins in relation to postheparin lipase activities were studied in ten healthy normolipidemic volunteers.	Heparin	33-40	apolipoprotein B	Homo sapiens	110-118
9453569-5	1998	LMW heparin derivatives also inhibit the binding of heparin to the beta-amyloid peptide (1-28).	Heparin	4-11	amyloid beta precursor protein	Homo sapiens	67-87
9507993-6	1998	Heparin administration released lipoprotein lipase (LPL) and hepatic lipase (HL) activities after 20 min, and significantly reduced apoB-48 concentrations in d &lt; 1.006 g/mL fractions only.	Heparin	0-7	apolipoprotein B	Homo sapiens	132-139
9507993-9	1998	When little LPL was released (LPL activity &lt; 120 mU/mL) by heparin, apoB-48 was preferentially eliminated over apoB-100.	Heparin	62-69	apolipoprotein B	Homo sapiens	71-78
9521111-0	1998	Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin-induced conformers of antithrombin.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	50-58
9507993-9	1998	When little LPL was released (LPL activity &lt; 120 mU/mL) by heparin, apoB-48 was preferentially eliminated over apoB-100.	Heparin	62-69	apolipoprotein B	Homo sapiens	114-122
9445060-12	1998	In addition, we demonstrated that the recombinant A27L gene product binds to the heparin beads in vitro.	Heparin	81-88	IMV surface protein	Vaccinia virus	50-54
9542727-4	1998	Furthermore, the responses were inhibited by the IP3 receptor antagonist heparin.	Heparin	73-80	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	49-61
9521111-1	1998	A pentasaccharide (PS) fragment of heparin capable of activating antithrombin (AT) markedly accelerates the inhibition of factor Xa by AT, but has insignificant effect on inhibition of thrombin.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	69-77
9493603-7	1998	All the direct thrombin inhibitors were effective on both arterial and venous thrombosis at markedly lower fold aPTT increases than heparin.	Heparin	132-139	coagulation factor II	Rattus norvegicus	15-23
9521111-10	1998	In the activated conformation, other residues are made accessible for interaction with the protease, and the similar reactivity of thrombin with the native and heparin-activated conformers of AT may be coincidental.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	131-139
9422744-5	1998	Residues 568-631 of the progelatinase A C-terminal domain are important in formation of the heparin binding site, since replacement of this region with the corresponding stromelysin-1 sequence abolished binding to heparin and the potentiation of activation.	Heparin	92-99	matrix metallopeptidase 3	Homo sapiens	170-183
9422744-5	1998	Residues 568-631 of the progelatinase A C-terminal domain are important in formation of the heparin binding site, since replacement of this region with the corresponding stromelysin-1 sequence abolished binding to heparin and the potentiation of activation.	Heparin	214-221	matrix metallopeptidase 3	Homo sapiens	170-183
9468329-5	1998	SLPI inhibited rMCP-1 very efficiently in the absence of heparin, with a low dissociation constant, Ki = 3 x 10(-10) M and high second order association constant, kass = 8.0 x 10(6) M(-1) s(-1), and inhibition was enhanced when heparin was present.	Heparin	228-235	secretory leukocyte peptidase inhibitor	Homo sapiens	0-4
9468329-8	1998	However, in the presence of heparin, the Ki for inhibition of sMCP-1 by SLPI was reduced to the nanomolar range.	Heparin	28-35	secretory leukocyte peptidase inhibitor	Homo sapiens	72-76
9453518-1	1998	Current protocols for use of tissue-type plasminogen activator in acute myocardial infarction include heparin estimated by the activated partial thromboplastin time (aPTT).	Heparin	102-109	plasminogen activator, tissue type	Homo sapiens	29-62
9681155-10	1998	To sum up, administration of heparin but not of saline affected the plasma concentrations of motilin and substance P.	Heparin	29-36	tachykinin precursor 1	Homo sapiens	105-116
14517472-6	1998	Heparinase treatment of the sections decreases the staining intensity of VEGF bound to endothelial cells, suggesting that VEGF also binds to heparin-like molecules on the cell surface.	Heparin	141-148	vascular endothelial growth factor A	Homo sapiens	73-77
14517472-6	1998	Heparinase treatment of the sections decreases the staining intensity of VEGF bound to endothelial cells, suggesting that VEGF also binds to heparin-like molecules on the cell surface.	Heparin	141-148	vascular endothelial growth factor A	Homo sapiens	122-126
9456225-1	1998	Heparin induced extracorporeal lipoprotein fibrinogen precipitation (HELP) is an established procedure for removal of low-density lipoprotein (LDL) cholesterol, lipoprotein (a), and fibrinogen in patients with severe hypercholesterolemia.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	43-53
9456225-1	1998	Heparin induced extracorporeal lipoprotein fibrinogen precipitation (HELP) is an established procedure for removal of low-density lipoprotein (LDL) cholesterol, lipoprotein (a), and fibrinogen in patients with severe hypercholesterolemia.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	182-192
9456225-5	1998	Heparin was omitted from the precipitating buffer to avoid fibrinogen depletion in patients at risk (low fibrinogen, postoperative).	Heparin	0-7	fibrinogen beta chain	Homo sapiens	59-69
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	tumor necrosis factor	Mus musculus	104-113
9871804-7	1998	Recently, it has been shown that a peptide of PF4, 34-58 which does not contain the site of heparin binding, is able to inhibit the growth of hematopoietic progenitors in vitro, providing evidence for a model of heparin dependent and independent pathways of PF4 action on hematopoiesis.	Heparin	92-99	platelet factor 4	Mus musculus	46-49
9691438-10	1998	This value is considerably lower than the activities reported for various low-molecular-weight heparins, consistent with the critical importance of an antithrombin III pentasaccharide binding site for anti-factor Xa activity.	Heparin	95-103	serpin family C member 1	Bos taurus	151-167
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	tumor necrosis factor	Mus musculus	125-134
27420332-3	1998	In this study we evaluate whether heparin can also induce a naturally occurring programmed cell death in lymphocytes from B-chronic lymphocytic leukemia (B-CLL), a neoplastic lineage where apoptosis is blocked by the expression of the proto-oncogene bc1-2.	Heparin	34-41	charged multivesicular body protein 2A	Homo sapiens	250-255
27420332-10	1998	In these cases bcl-2 expression was found to be significantly reduced after heparin incubation when comparing to bcl-2 level before incubation.	Heparin	76-83	BCL2 apoptosis regulator	Homo sapiens	15-20
9429100-8	1998	The amount of the adsorption of albumin and fibrinogen decreased with increasing graft amount and heparin content.	Heparin	98-105	fibrinogen beta chain	Homo sapiens	44-54
9801927-0	1998	Effect of low-dose heparin on fibrinogen levels in patients with chronic ischemic heart disease.	Heparin	19-26	fibrinogen beta chain	Homo sapiens	30-40
9801927-6	1998	At the end of the treatment period with low-dose heparin significant decreases in the plasma fibrinogen (2.5 +/- 0.6 g/l vs. 3.3 +/- 0.5 g/l, P &lt; 0.001), prothrombin fragment 1 + 2 (1.4 +/- 0.5 nmol/l vs. 1.9 +/- 0.7 nmol/l, P &lt; 0.001), thrombinantithrombin (4.5 +/- 2.4 ng/ml vs. 9.7 +/- 3.6 ng/ml, P &lt; 0.001), and fibrinopeptide A (2.1 +/- 1.1 ng/ml vs. 3.5 +/- 2.1 ng/ml, P &lt; 0.001) were observed compared with the period without heparin.	Heparin	49-56	fibrinogen beta chain	Homo sapiens	93-103
9801927-7	1998	The present results indicate that low-dose heparin can effectively control the increased abnormal thrombin generation and elevated fibrinogen levels in patients with ischemic heart disease, possibly decreasing the risk of cardiovascular death.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	98-106
9801927-7	1998	The present results indicate that low-dose heparin can effectively control the increased abnormal thrombin generation and elevated fibrinogen levels in patients with ischemic heart disease, possibly decreasing the risk of cardiovascular death.	Heparin	43-50	fibrinogen beta chain	Homo sapiens	131-141
9646165-2	1998	The patient was given heparin intravenously after an erroneous intravenous injection of thrombin and died from lobar pneumonia 3 months afterwards without any apparently ill effects on the circulation of the body except for the brain.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	88-96
9648027-1	1998	Polyion complexation between basic fibroblast growth factor (bFGF) and gelatin was studied by the turbidity change of mixed solution, heparin high performance liquid affinity chromatography (HPLAC), and isoelectric electrophoresis.	Heparin	134-141	fibroblast growth factor 2	Homo sapiens	29-59
9595512-5	1998	Heparin (1-20 U/ml) suppressed cyclosporine-induced ET-1 mRNA expression in a dose-dependent manner.	Heparin	0-7	endothelin 1	Rattus norvegicus	52-56
9595512-7	1998	These results suggest that heparin suppresses cyclosporine-induced ET-1 mRNA expression via both NO- and calmodulin-dependent pathways.	Heparin	27-34	endothelin 1	Rattus norvegicus	67-71
9595512-0	1998	Heparin suppresses cyclosporine-induced endothelin-1 synthesis in rat endothelial cells.	Heparin	0-7	endothelin 1	Rattus norvegicus	40-52
9595512-2	1998	This study examined the effect of heparin on cyclosporine-induced ET-1 synthesis in Wistar rat aortic endothelial cells in culture.	Heparin	34-41	endothelin 1	Rattus norvegicus	66-70
9648027-1	1998	Polyion complexation between basic fibroblast growth factor (bFGF) and gelatin was studied by the turbidity change of mixed solution, heparin high performance liquid affinity chromatography (HPLAC), and isoelectric electrophoresis.	Heparin	134-141	fibroblast growth factor 2	Homo sapiens	61-65
9648027-6	1998	HPLAC study revealed that complexation of bFGF with the acidic gelatin reduced the affinity of bFGF for heparin, in contrast to the basic gelatin, although the extent became smaller with the increasing ionic strength of the solution.	Heparin	104-111	fibroblast growth factor 2	Homo sapiens	42-46
9648027-6	1998	HPLAC study revealed that complexation of bFGF with the acidic gelatin reduced the affinity of bFGF for heparin, in contrast to the basic gelatin, although the extent became smaller with the increasing ionic strength of the solution.	Heparin	104-111	fibroblast growth factor 2	Homo sapiens	95-99
9466731-6	1998	The stimulatory effects of thrombin (10 U/ml) can be inhibited by antithrombin III (2 U/ml) (a natural thrombin inhibitor) with heparin (2 U/ml), PPACK (D-Phe-Pro-ArgCH2Cl) (20-50 microg/ml) (a serine protease inhibitor), and PGE2 (0.5-1.0 microg/ml).	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	27-35
9443108-7	1998	The gp120 and gp160 specifically recognize the C-terminal heparin-binding domain of Fn (Fn-CTHBD) with a calculated KD of 2.8 x 10(-7) M for gp160.	Heparin	58-65	fibronectin 1	Homo sapiens	84-86
9443108-7	1998	The gp120 and gp160 specifically recognize the C-terminal heparin-binding domain of Fn (Fn-CTHBD) with a calculated KD of 2.8 x 10(-7) M for gp160.	Heparin	58-65	fibronectin 1	Homo sapiens	88-96
9443108-8	1998	Binding of gp160 to Fn-CTHBD is a saturable and specific process that is blocked by antibodies to Fn-CTHBD and by heparin and is inhibited to a minor extent by heparan sulfate and dextran sulfate.	Heparin	114-121	fibronectin 1	Homo sapiens	20-28
9466731-6	1998	The stimulatory effects of thrombin (10 U/ml) can be inhibited by antithrombin III (2 U/ml) (a natural thrombin inhibitor) with heparin (2 U/ml), PPACK (D-Phe-Pro-ArgCH2Cl) (20-50 microg/ml) (a serine protease inhibitor), and PGE2 (0.5-1.0 microg/ml).	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	70-78
9484897-0	1998	Heparin interferes with translocation of Yop proteins into HeLa cells and binds to LcrG, a regulatory component of the Yersinia Yop apparatus.	Heparin	0-7	control of Yop release	Yersinia enterocolitica	83-87
9808060-5	1998	When thrombin was incubated on the EC surface in the presence of AT the efficiency of the thrombomodulin(TM)-protein C(PC)-system was markedly reduced, while in the presence of exogenous heparin (0.5 IU/l) the activity of this pathway was nearly abolished.	Heparin	187-194	coagulation factor II, thrombin	Homo sapiens	5-13
10608050-6	1998	In thrombolysis with tissue plasminogen activator (t-PA), heparin seems to play an important role.	Heparin	58-65	plasminogen activator, tissue type	Homo sapiens	21-55
9484897-7	1998	LcrG could bind directly to heparin-agarose beads and, in agreement with these results, analysis of the protein sequence of Yersinia enterocolitica LcrG revealed heparin-binding motifs.	Heparin	28-35	control of Yop release	Yersinia enterocolitica	0-4
9484897-7	1998	LcrG could bind directly to heparin-agarose beads and, in agreement with these results, analysis of the protein sequence of Yersinia enterocolitica LcrG revealed heparin-binding motifs.	Heparin	162-169	control of Yop release	Yersinia enterocolitica	0-4
9484897-7	1998	LcrG could bind directly to heparin-agarose beads and, in agreement with these results, analysis of the protein sequence of Yersinia enterocolitica LcrG revealed heparin-binding motifs.	Heparin	162-169	control of Yop release	Yersinia enterocolitica	148-152
9704387-5	1998	After 2 h, mRNAs for IL-1 beta and IL-6 were highly upregulated in noncoated compared to heparin-coated circuits.	Heparin	89-96	interleukin 1 beta	Homo sapiens	21-30
9437731-1	1998	Recently we have shown an evidence that a peptide, corresponding to residues Gln1892 to Gly1910, from the C-terminal heparin-binding domain of fibronectin promotes adhesion of phorbol-12-myristate 13-acetate (PMA)-treated U937 cells and binds to both integrin alpha 4 beta 1 and glycosaminoglycans on U937 cells surface.	Heparin	117-124	fibronectin 1	Homo sapiens	143-154
9437731-2	1998	We present additional adhesion-promoting sites to PMA-treated U937 cells present in the C-terminal heparin-binding domain of fibronectin.	Heparin	99-106	fibronectin 1	Homo sapiens	125-136
9704387-5	1998	After 2 h, mRNAs for IL-1 beta and IL-6 were highly upregulated in noncoated compared to heparin-coated circuits.	Heparin	89-96	interleukin 6	Homo sapiens	35-39
9796071-4	1998	Maximal heparin-induced venorelaxation correlated with the maximal insulin effect within individuals (r = 0.8, p &lt; 0.01) and was unchanged by the addition of insulin.	Heparin	8-15	insulin	Homo sapiens	67-74
9388253-1	1997	To understand whether expression of membrane-anchored heparin binding epidermal growth factor (proHB-EGF) is involved in renal epithelial cell survival, rat membrane-bound HB-EGF precursor was stably transfected into a renal epithelial cell line, NRK 52E cells (NRKproHB-EGF).	Heparin	54-61	heparin-binding EGF-like growth factor	Rattus norvegicus	98-104
9796071-4	1998	Maximal heparin-induced venorelaxation correlated with the maximal insulin effect within individuals (r = 0.8, p &lt; 0.01) and was unchanged by the addition of insulin.	Heparin	8-15	insulin	Homo sapiens	161-168
9395501-0	1997	Heparin-binding properties of the amyloidogenic peptides Abeta and amylin.	Heparin	0-7	amyloid beta precursor protein	Homo sapiens	57-62
9395501-7	1997	We used affinity co-electrophoresis to study the interaction between Abeta and the glycosaminoglycan heparin and found that the aggregation state of Abeta governs its heparin-binding properties: heparin binds to fibrillar but not nonfibrillar Abeta.	Heparin	101-108	amyloid beta precursor protein	Homo sapiens	69-74
9395501-7	1997	We used affinity co-electrophoresis to study the interaction between Abeta and the glycosaminoglycan heparin and found that the aggregation state of Abeta governs its heparin-binding properties: heparin binds to fibrillar but not nonfibrillar Abeta.	Heparin	101-108	amyloid beta precursor protein	Homo sapiens	149-154
9395501-7	1997	We used affinity co-electrophoresis to study the interaction between Abeta and the glycosaminoglycan heparin and found that the aggregation state of Abeta governs its heparin-binding properties: heparin binds to fibrillar but not nonfibrillar Abeta.	Heparin	101-108	amyloid beta precursor protein	Homo sapiens	149-154
9395501-7	1997	We used affinity co-electrophoresis to study the interaction between Abeta and the glycosaminoglycan heparin and found that the aggregation state of Abeta governs its heparin-binding properties: heparin binds to fibrillar but not nonfibrillar Abeta.	Heparin	167-174	amyloid beta precursor protein	Homo sapiens	69-74
9395501-7	1997	We used affinity co-electrophoresis to study the interaction between Abeta and the glycosaminoglycan heparin and found that the aggregation state of Abeta governs its heparin-binding properties: heparin binds to fibrillar but not nonfibrillar Abeta.	Heparin	167-174	amyloid beta precursor protein	Homo sapiens	149-154
9395501-7	1997	We used affinity co-electrophoresis to study the interaction between Abeta and the glycosaminoglycan heparin and found that the aggregation state of Abeta governs its heparin-binding properties: heparin binds to fibrillar but not nonfibrillar Abeta.	Heparin	167-174	amyloid beta precursor protein	Homo sapiens	149-154
9395501-9	1997	The "Dutch" mutant AbetaE22Q peptide formed fibrils more readily than wild type Abeta and it also attained a heparin-binding state more readily, but, once formed, mutant and wild type fibrils bound heparin with similar affinities.	Heparin	109-116	amyloid beta precursor protein	Homo sapiens	19-24
9395501-9	1997	The "Dutch" mutant AbetaE22Q peptide formed fibrils more readily than wild type Abeta and it also attained a heparin-binding state more readily, but, once formed, mutant and wild type fibrils bound heparin with similar affinities.	Heparin	198-205	amyloid beta precursor protein	Homo sapiens	19-24
9395501-12	1997	These results demonstrate the dependence of the Abeta-heparin interaction on the conformation and aggregation state of Abeta rather than primary sequence alone, and suggest methods of interfering with this association.	Heparin	54-61	amyloid beta precursor protein	Homo sapiens	48-53
9395501-12	1997	These results demonstrate the dependence of the Abeta-heparin interaction on the conformation and aggregation state of Abeta rather than primary sequence alone, and suggest methods of interfering with this association.	Heparin	54-61	amyloid beta precursor protein	Homo sapiens	119-124
9447247-2	1997	Heparin affinity chromatography yielded r-vWF polymers of different degrees of multimerization.	Heparin	0-7	von Willebrand factor	Homo sapiens	42-45
9423940-9	1997	Heparin-coating diminished myeloperoxidase and lactoferrin release.	Heparin	0-7	myeloperoxidase	Homo sapiens	27-42
9417813-0	1997	Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach.	Heparin	63-70	interleukin 2	Homo sapiens	38-51
9417813-4	1997	Using this ELISA method, we have established that human recombinant interleukin (IL-2) binds to heparin in a concentration-dependent manner.	Heparin	96-103	interleukin 2	Homo sapiens	81-85
9417813-5	1997	Soluble heparin competes for the binding of IL-2 to the complex with 50% inhibition at 5 microg/ml.	Heparin	8-15	interleukin 2	Homo sapiens	44-48
9417813-10	1997	The interaction between IL-2 and heparin-like glycosaminoglycans is likely to be an important mechanism for retaining IL-2 close to its sites of secretion, thus giving rise to localized concentration gradients in the tissues.	Heparin	33-40	interleukin 2	Homo sapiens	24-28
9384573-10	1997	The dimer has a fused heparin-binding site at the dimer interface of the C-terminal domain, and the heparin-binding sites on MK fit the sulfate group clusters on heparin.	Heparin	100-107	midkine	Homo sapiens	125-127
9417813-10	1997	The interaction between IL-2 and heparin-like glycosaminoglycans is likely to be an important mechanism for retaining IL-2 close to its sites of secretion, thus giving rise to localized concentration gradients in the tissues.	Heparin	33-40	interleukin 2	Homo sapiens	118-122
9384573-10	1997	The dimer has a fused heparin-binding site at the dimer interface of the C-terminal domain, and the heparin-binding sites on MK fit the sulfate group clusters on heparin.	Heparin	100-107	midkine	Homo sapiens	125-127
9360977-0	1997	The efficient catabolism of thrombin-protease nexin 1 complexes is a synergistic mechanism that requires both the LDL receptor-related protein and cell surface heparins.	Heparin	160-168	coagulation factor II, thrombin	Homo sapiens	28-36
9464851-8	1997	While native EC-SOD shows high affinity for heparin and heparan sulphate, 90% of the EC-SOD in seminal plasma lacks the high affinity at ejaculation.	Heparin	44-51	superoxide dismutase 3	Homo sapiens	13-19
9412881-13	1997	Thrombin time increased from 28 +/- 6 to 48 +/- 29 seconds and did not correlate with H. CONCLUSIONS: The plasma concentration of heparin increased after veno-venous modified UF of the patient.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	0-8
9477462-13	1997	MPO was also affected by heparin-coating.	Heparin	25-32	myeloperoxidase	Homo sapiens	0-3
9360988-1	1997	The CD11c/CD18 integrin binds lipopolysaccharide, fibrinogen, and heparin, and mediates leukocyte adhesion, spreading, and migration.	Heparin	66-73	integrin subunit beta 2	Homo sapiens	10-14
9360977-9	1997	These data demonstrate the sizable contribution of cell surface heparins to Thrombin-PN1 complex binding and support a model in which these heparins act to concentrate the complexes at the cell surface facilitating their subsequent LRP-dependent endocytosis.	Heparin	64-72	coagulation factor II, thrombin	Homo sapiens	76-84
9360977-9	1997	These data demonstrate the sizable contribution of cell surface heparins to Thrombin-PN1 complex binding and support a model in which these heparins act to concentrate the complexes at the cell surface facilitating their subsequent LRP-dependent endocytosis.	Heparin	140-148	LDL receptor related protein 1	Homo sapiens	232-235
9386091-1	1997	BACKGROUND: A combined treatment of statins and extracorporeal H.E.L.P.-apheresis (Heparin-mediated Extracorporeal LDL/fibrinogen Precipitation) has already been shown to be beneficial for coronary artery disease (CAD).	Heparin	83-90	fibrinogen beta chain	Homo sapiens	119-129
9354625-9	1997	The endothelial cell binding sites for IL-8, RANTES, and MCP-1 were deduced to be glycosaminoglycans since competition assays showed the biphasic curves and micromolar IC50 values seen in studies with immobilized heparin, and mRNA for known chemokine receptors was not detected.	Heparin	213-220	C-X-C motif chemokine ligand 8	Homo sapiens	39-43
9344460-12	1997	The possibility is discussed that, while heparin and glucose binding occurs at different sites on alpha1AT, glucose favors heparin binding by inducing a partially relaxed form in the inhibitor.	Heparin	41-48	serpin family A member 1	Homo sapiens	98-106
9374687-1	1997	Using the major bone insulin-like growth factor-binding protein (IGFBP) IGFBP-5, we took a mechanistic approach in evaluating the role of the heparin-binding domain of IGFBP-5 in regulating plasmin (Pm) proteolysis of IGFBP-5.	Heparin	142-149	insulin like growth factor binding protein 5	Homo sapiens	168-175
9374687-1	1997	Using the major bone insulin-like growth factor-binding protein (IGFBP) IGFBP-5, we took a mechanistic approach in evaluating the role of the heparin-binding domain of IGFBP-5 in regulating plasmin (Pm) proteolysis of IGFBP-5.	Heparin	142-149	insulin like growth factor binding protein 5	Homo sapiens	168-175
9374687-2	1997	Using synthetic IGFBP-5 peptide fragments, we determined that the heparin-binding domain, IGFBP-5-(208-218), inhibits Pm proteolysis of intact IGFBP-5.	Heparin	66-73	insulin like growth factor binding protein 5	Homo sapiens	16-23
9374687-2	1997	Using synthetic IGFBP-5 peptide fragments, we determined that the heparin-binding domain, IGFBP-5-(208-218), inhibits Pm proteolysis of intact IGFBP-5.	Heparin	66-73	insulin like growth factor binding protein 5	Homo sapiens	90-97
9374687-2	1997	Using synthetic IGFBP-5 peptide fragments, we determined that the heparin-binding domain, IGFBP-5-(208-218), inhibits Pm proteolysis of intact IGFBP-5.	Heparin	66-73	insulin like growth factor binding protein 5	Homo sapiens	90-97
9374687-6	1997	These data indicate that the heparin-binding domain contains the serine protease (Pg-to-Pm) binding site region of IGFBP-5, and that this region, which is presumed to represent a Pm-induced proteolytic product of IGFBP-5, is capable of regulating Pm action.	Heparin	29-36	insulin like growth factor binding protein 5	Homo sapiens	115-122
9374687-6	1997	These data indicate that the heparin-binding domain contains the serine protease (Pg-to-Pm) binding site region of IGFBP-5, and that this region, which is presumed to represent a Pm-induced proteolytic product of IGFBP-5, is capable of regulating Pm action.	Heparin	29-36	insulin like growth factor binding protein 5	Homo sapiens	213-220
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	33-40
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	256-261
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor binding protein 5	Homo sapiens	33-40
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor binding protein 5	Homo sapiens	78-85
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor 1	Homo sapiens	256-261
9374688-6	1997	Heparin inhibited the binding of IGFBP-5 to HA and blocked the interaction of IGFBP-5 with IGFBP-5-(201-218) in the fluid phase, suggesting that the primary heparin-binding domain of IGFBP-5 specifically enhances the binding of IGFBP-5 to HA and increases IGF-I binding to IGFBP-5.	Heparin	157-164	insulin like growth factor binding protein 5	Homo sapiens	78-85
9344460-0	1997	Differential effects of heparin and glucose on structural conformation of human alpha1 antitrypsin: evidence for a heparin-induced cleaved form of the inhibitor.	Heparin	24-31	serpin family A member 1	Homo sapiens	80-98
9344460-0	1997	Differential effects of heparin and glucose on structural conformation of human alpha1 antitrypsin: evidence for a heparin-induced cleaved form of the inhibitor.	Heparin	115-122	serpin family A member 1	Homo sapiens	80-98
9344460-3	1997	Since previous results have shown that an apparently altered alpha1AT form may be purified from the plasma of insulin-dependent diabetics by means of heparin-affinity chromatography, in the present work the possibility was tested that heparin at various concentrations modifies the structural conformation and function of human alpha1AT in the absence and presence of glucose, used at concentrations of 15 mM to mimick mild hyperglycemic conditions.	Heparin	150-157	serpin family A member 1	Homo sapiens	61-69
9344460-3	1997	Since previous results have shown that an apparently altered alpha1AT form may be purified from the plasma of insulin-dependent diabetics by means of heparin-affinity chromatography, in the present work the possibility was tested that heparin at various concentrations modifies the structural conformation and function of human alpha1AT in the absence and presence of glucose, used at concentrations of 15 mM to mimick mild hyperglycemic conditions.	Heparin	235-242	serpin family A member 1	Homo sapiens	61-69
9344460-3	1997	Since previous results have shown that an apparently altered alpha1AT form may be purified from the plasma of insulin-dependent diabetics by means of heparin-affinity chromatography, in the present work the possibility was tested that heparin at various concentrations modifies the structural conformation and function of human alpha1AT in the absence and presence of glucose, used at concentrations of 15 mM to mimick mild hyperglycemic conditions.	Heparin	235-242	serpin family A member 1	Homo sapiens	328-336
9344460-4	1997	Heparin was observed to bind strongly to alpha1AT, causing maximal enhancement of tryptophan fluorescence emission at 50 microg/ml, mostly in the presence of glucose.	Heparin	0-7	serpin family A member 1	Homo sapiens	41-49
9344460-7	1997	However, despite inactivation, in the presence of heparin-both with and without glucose-alpha1AT was still able to bind trypsin, as revealed by inhibitor-to-proteinase complexes visible in both SDS- and nondenaturing electrophoreses.	Heparin	50-57	endogenous retrovirus group K member 25	Homo sapiens	157-167
9344460-9	1997	Even in the absence of trypsin, cleavage of alpha1AT was also observed to occur at both Val321- and Glu344- in the primary sequence of the inhibitor in the presence of 50 microg/ml heparin, with and without glucose.	Heparin	181-188	serpin family A member 1	Homo sapiens	44-52
9344460-10	1997	These results suggest that heparin binding to alpha1AT causes profound structural changes in the molecule, involving both the expulsion of the reactive site out of the molecule plane and a relaxed, heat-stable form of the inhibitor, rendered a substrate for the proteinase.	Heparin	27-34	serpin family A member 1	Homo sapiens	46-54
9344460-10	1997	These results suggest that heparin binding to alpha1AT causes profound structural changes in the molecule, involving both the expulsion of the reactive site out of the molecule plane and a relaxed, heat-stable form of the inhibitor, rendered a substrate for the proteinase.	Heparin	27-34	endogenous retrovirus group K member 25	Homo sapiens	262-272
9344460-11	1997	Although glucose apparently does not affect alpha1AT functioning, it does enhance the effects of heparin on the alpha1AT structure.	Heparin	97-104	serpin family A member 1	Homo sapiens	112-120
9382401-12	1997	CONCLUSIONS: Warfarin treatment of deep venous thrombosis associated with heparin-induced thrombocytopenia is a possible cause of venous limb gangrene, perhaps because of acquired failure of the protein C anticoagulant pathway to regulate thrombin generation.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	239-247
9344460-12	1997	The possibility is discussed that, while heparin and glucose binding occurs at different sites on alpha1AT, glucose favors heparin binding by inducing a partially relaxed form in the inhibitor.	Heparin	123-130	serpin family A member 1	Homo sapiens	98-106
9406449-3	1997	Metallic ions, NaCl and protamine sulfate reduced, and heparin increased, both LPL activities.	Heparin	55-62	lipoprotein lipase	Rattus norvegicus	79-82
9356420-10	1997	Postsynaptic injections of heparin and dantrolene (inhibitors of IP3 and ryanodine receptors at intracellular Ca2+ stores) prevented tetanus-LTP induction and PPF attenuation.	Heparin	27-34	carbonic anhydrase 2	Rattus norvegicus	110-113
9348216-8	1997	IGFBP-2 bound in vitro to the glycosaminoglycans chondroitin-4 and -6-sulfate, keratan sulfate, and heparin.	Heparin	100-107	insulin-like growth factor binding protein 2	Rattus norvegicus	0-7
9426344-1	1997	Tissue factor pathway inhibitor, a natural anticoagulant in the extrinsic pathway of blood coagulation, is associated with the endothelial membrane and presumed to be released by heparin.	Heparin	179-186	tissue factor pathway inhibitor	Oryctolagus cuniculus	0-31
9426344-11	1997	After heparin incubation an increased tissue factor pathway inhibitor concentration was determined in the cell culture medium by a chromogenic substrate assay.	Heparin	6-13	tissue factor pathway inhibitor	Oryctolagus cuniculus	38-69
9426344-14	1997	Therefore, the effect of heparin appears to be mediated by secretion of tissue factor pathway inhibitor from intracellular stores.	Heparin	25-32	tissue factor pathway inhibitor	Oryctolagus cuniculus	72-103
9466688-2	1997	Different effects of the manipulation of cellular heparan sulfates and heparin on activities of FGF-7 relative to FGF-1 in epithelial cells suggest that pericellular heparan sulfates may regulate the activity of FGF-7 by a different mechanism than other FGFs.	Heparin	71-78	fibroblast growth factor 7	Homo sapiens	96-101
9466688-2	1997	Different effects of the manipulation of cellular heparan sulfates and heparin on activities of FGF-7 relative to FGF-1 in epithelial cells suggest that pericellular heparan sulfates may regulate the activity of FGF-7 by a different mechanism than other FGFs.	Heparin	71-78	fibroblast growth factor 7	Homo sapiens	212-217
9466688-6	1997	Heparin was essential for binding of FGF-7 to recombinant FGFR2IIIb expressed in insect cells or FGFR2IIIb purified away from cell products.	Heparin	0-7	fibroblast growth factor 7	Homo sapiens	37-42
9466688-8	1997	Differences in response to heparin and alterations in the BULK heparan sulfate content of cells likely reflect FGF-specific differences in the cellular repertoire of multivalent heparan sulfate chains required for assembly and activation of the FGF signal transduction complex.	Heparin	27-34	fibroblast growth factor 1	Homo sapiens	111-114
9441796-5	1997	The decrease in heparin-releasable (HR) LPL activity in adipocytes from the septic rats was evident at the time of isolation and maintained in a 20-h culture.	Heparin	16-23	lipoprotein lipase	Rattus norvegicus	40-43
10225731-5	1997	During apheresis using heparin, the marked increase in bradykinin levels (before apheresis, 18 +/- 3 (mean +/- SE, n = 5) pg/ml; after apheresis 470 +/- 140, p &lt; 0.01) was associated with the increase in NOx (before apheresis 50 +/- 11 pg/ml; after apheresis 66 +/- 15).	Heparin	23-30	kininogen 1	Homo sapiens	55-65
9341129-0	1997	Deleted in colorectal carcinoma (DCC) binds heparin via its fifth fibronectin type III domain.	Heparin	44-51	fibronectin 1	Homo sapiens	66-77
9345296-1	1997	Hematopoietic cells differentially bind to the C-terminal heparin-binding domain of fibronectin depending on the activation state of integrin alpha 4 beta 1.	Heparin	58-65	fibronectin 1	Homo sapiens	84-95
9359413-2	1997	Insulin in combination with dexamethasone (INS/DEX) increased heparin-releasable LPL activity by 71% over the control level (566+/-85 versus 331+/-48 nmol/h.mg cell protein).	Heparin	62-69	lipoprotein lipase	Rattus norvegicus	81-84
9345296-3	1997	A peptide (FN-C/H-V; residues Gln1892 to Gly1910) was active to inhibit adhesion of PMA-treated U937 cells to the 29-kDa fragment comprising the C-terminal heparin-binding domain of fibronectin.	Heparin	156-163	fibronectin 1	Homo sapiens	182-193
9312081-1	1997	The region of fibronectin encompassing type III repeats 4-6 contains a low affinity heparin binding domain, but its physiological significance is not clear.	Heparin	84-91	fibronectin 1	Homo sapiens	14-25
9368651-2	1997	The substrate specificity of thrombin involves two electropositive surfaces, the fibrinogen-recognition and heparin-binding exosites.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	29-37
9342064-9	1997	Binding to heparin is competed out by heparin-binding factors such as basic fibroblast growth factor (bFGF), and it is mediated by the Tat basic region which forms a specific complex with heparin which blocks HIV-1 rescue by exogenous Tat and allows purification of a highly biologically active protein.	Heparin	11-18	fibroblast growth factor 2	Homo sapiens	102-106
9342064-9	1997	Binding to heparin is competed out by heparin-binding factors such as basic fibroblast growth factor (bFGF), and it is mediated by the Tat basic region which forms a specific complex with heparin which blocks HIV-1 rescue by exogenous Tat and allows purification of a highly biologically active protein.	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	102-106
9357806-0	1997	Fatty acids reduce heparin-releasable LPL activity in cultured cardiomyocytes from rat heart.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	38-41
9357806-7	1997	Immunodetectable LPL on the cell surface of oleate-treated cultured cardiomyocytes was increased compared with control cells, but heparin treatment released the same amount of LPL mass that had reduced catalytic activity.	Heparin	130-137	lipoprotein lipase	Rattus norvegicus	176-179
9326226-4	1997	Although +/+ CMCs were berberine sulfate-negative when cultured with IL-3, +/+ CMCs became berberine sulfate-positive when cultured in the presence of both IL-3 and NGF, which suggested increased heparin content.	Heparin	196-203	interleukin 3	Mus musculus	156-168
9402691-0	1997	Antigen presentation by endothelium: heparin reduces the immunogenicity of interferon-gamma-treated endothelial cells.	Heparin	37-44	interferon gamma	Homo sapiens	75-91
9310258-5	1997	Growth of MK expressing cells was inhibited by a heparin-binding blocking agent, pentosan polysulfate (PPS).	Heparin	49-56	midkine	Homo sapiens	10-12
9407722-4	1997	METHODS: Studies were carried out following a well-established perfusion model, employing either citrated blood, where fibrin formation is blocked, or blood anticoagulated with low molecular weight heparin, which allows thrombin and fibrin formation.	Heparin	198-205	coagulation factor II, thrombin	Homo sapiens	220-228
10322925-6	1997	Heparin (100 mg.L-1) inhibited rat PASMC proliferation (28% +/- 6%) and thymidine incorporation (27% +/- 7%) induced by FBS (10%), and also significantly inhibited cell proliferation 25% +/- 6%, 27% +/- 7%, and 20% +/- 4%, and [methyl-3H] TdR incorporation 23% +/- 7%, 26% +/- 6%, 20% +/- 6% induced by FBS (1%) in combination with PDGF (50 micrograms.L-1), FGF (50 micrograms.L-1), or IL-1 alpha (100 ng.L-1) respectively.	Heparin	0-7	interleukin 1 alpha	Rattus norvegicus	386-396
9352356-3	1997	We now report that the cleavage of heparin by the enzyme heparinase I generates sulfated disaccharide (DS) molecules that can inhibit the production of TNF-alpha.	Heparin	35-42	tumor necrosis factor	Homo sapiens	152-161
9328841-5	1997	In addition, heparan sulfate drastically inhibited [125I]DCN binding to solid-phase adsorbed TSP (80% inhibition), suggesting that DCN could bind to the N-terminal domain of TSP through interaction with heparin-binding sequences.	Heparin	203-210	thrombospondin 1	Homo sapiens	93-96
9328841-5	1997	In addition, heparan sulfate drastically inhibited [125I]DCN binding to solid-phase adsorbed TSP (80% inhibition), suggesting that DCN could bind to the N-terminal domain of TSP through interaction with heparin-binding sequences.	Heparin	203-210	thrombospondin 1	Homo sapiens	174-177
9307014-0	1997	Heparin inhibits the binding of basic fibroblast growth factor to cultured human aortic smooth-muscle cells.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	32-62
9307014-12	1997	Consistent with these results, heparin, suramin, protamine sulphate and platelet factor 4 inhibited bFGF-induced proliferation of human aortic smooth-muscle cells.	Heparin	31-38	fibroblast growth factor 2	Homo sapiens	100-104
9307014-13	1997	Heparin abrogated bFGF-induced release of tissue-type plasminogen activator by these cells.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	18-22
9307014-13	1997	Heparin abrogated bFGF-induced release of tissue-type plasminogen activator by these cells.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	42-75
9307014-14	1997	These observations suggest that the interaction of bFGF with human aortic smooth-muscle cells is different from that described for other cells such as endothelial cells, in which heparin acts as a potentiating factor of the mitogenic activity of bFGF.	Heparin	179-186	fibroblast growth factor 2	Homo sapiens	51-55
9307014-14	1997	These observations suggest that the interaction of bFGF with human aortic smooth-muscle cells is different from that described for other cells such as endothelial cells, in which heparin acts as a potentiating factor of the mitogenic activity of bFGF.	Heparin	179-186	fibroblast growth factor 2	Homo sapiens	246-250
9300180-8	1997	The cell adhesion to G2, alpha 3G2A, G4, and G5 was strongly inhibited by heparin, but that to native laminin-5 was inhibited less effectively.	Heparin	74-81	chromosome 6 open reading frame 47	Homo sapiens	25-47
9339389-3	1997	MATERIAL AND METHODS: TNF alpha was measured by a WEHI 164 bioassay in the plasma of 16 septic patients anticoagulated with heparin, citrate, or EDTA.	Heparin	124-131	tumor necrosis factor	Homo sapiens	22-31
9339389-11	1997	Only heparin at a concentration of 20 I.U./ml or more was found to produce falsely low values by interaction with the TNF alpha bioassay, but also with the ELISA test.	Heparin	5-12	tumor necrosis factor	Homo sapiens	118-127
9339389-12	1997	In monocyte culture experiments, heparin significantly attenuated the stimulatory effect of endotoxin on TNF alpha release already at the lowest concentration tested (25 I.U./ml).	Heparin	33-40	tumor necrosis factor	Homo sapiens	105-114
9339389-13	1997	CONCLUSIONS: Heparin and EDTA may have significant adverse effects on TNF alpha measurement when used for blood sampling.	Heparin	13-20	tumor necrosis factor	Homo sapiens	70-79
9323593-4	1997	LPL greatly increased the binding of 125I-labeled beta-VLDL to VSMCs at 4 degrees C. Binding was almost entirely inhibited by heparin, but essentially unaffected by the potent LRF-antagonist, receptor-associated protein (RAP), indicating that LRFs do not contribute significantly to the VSMC binding capacity for LPL-associated beta-VLDL.	Heparin	126-133	lipoprotein lipase	Rattus norvegicus	0-3
9323595-0	1997	Isolation of subpopulations of high density lipoproteins: three particle species containing apoE and two species devoid of apoE that have affinity for heparin.	Heparin	151-158	apolipoprotein E	Homo sapiens	123-127
9306616-4	1997	4) Fucoidan enhanced the interaction of thrombin with both AT-III and heparin cofactor II (HC-II) and it was more effective than unfractionated heparin of LMwt-heparin in enhancing the interaction of HC-II with thrombin.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	40-48
9606832-1	1997	Heparin was studied for its effect on the hydrolysis time of clots from desAA fibrin (FB), desAABB fibrin (F0) and fibrinogen (Fg) of a bull and a man by gly-or lys-plasminogen which is activated by the tissue activator.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	115-125
9606832-1	1997	Heparin was studied for its effect on the hydrolysis time of clots from desAA fibrin (FB), desAABB fibrin (F0) and fibrinogen (Fg) of a bull and a man by gly-or lys-plasminogen which is activated by the tissue activator.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	127-129
9606832-5	1997	In concentration 4.6 microM heparin increases the hydrolysis time of clots from human fibrinogen by fibrinolytic systems.	Heparin	28-35	fibrinogen beta chain	Homo sapiens	86-96
9244387-0	1997	Disulfide structure of the heparin binding domain in vascular endothelial growth factor: characterization of posttranslational modifications in VEGF.	Heparin	27-34	vascular endothelial growth factor A	Homo sapiens	53-87
9254627-4	1997	The binding of HGF to heparin or heparin-like molecules may induce oligomerization of HGF and facilitate c-Met-dependent mitogenesis [Zioncheck et al.	Heparin	22-29	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	105-110
9254627-4	1997	The binding of HGF to heparin or heparin-like molecules may induce oligomerization of HGF and facilitate c-Met-dependent mitogenesis [Zioncheck et al.	Heparin	33-40	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	105-110
9242708-9	1997	10-kDa CTGF-mediated fibroblast DNA synthesis was modulated by exogenous heparin, and CTGF-immunoreactive proteins of 10, 16, and 20 kDa were present in unfractionated uterine luminal flushings.	Heparin	73-80	cellular communication network factor 2	Sus scrofa	7-11
9244377-9	1997	This protein kinase possessed the properties (substrate specificity and inhibition by heparin) that are characteristic of the protein kinase CK2 enzymes.	Heparin	86-93	casein kinase 2 beta	Rattus norvegicus	141-144
9279212-2	1997	Enzymatically active tryptase is comprised of four subunits, and heparin stabilizes the associated tetramer.	Heparin	65-72	tryptase beta-2	Ovis aries	21-29
9279212-3	1997	Lactoferrin, a cationic protein released from activated neutrophils, binds tightly to heparin, therefore we investigated lactoferrin as an inhibitor of tryptase and found that it is both a potent (Ki" is 24 nM) and selective inhibitor.	Heparin	86-93	lactotransferrin	Ovis aries	0-11
9279212-3	1997	Lactoferrin, a cationic protein released from activated neutrophils, binds tightly to heparin, therefore we investigated lactoferrin as an inhibitor of tryptase and found that it is both a potent (Ki" is 24 nM) and selective inhibitor.	Heparin	86-93	lactotransferrin	Ovis aries	121-132
9667850-2	1997	Deficiencies in available therapies, heparin and coumadin, have recently led to an intense effort in several pharmaceutical companies to develop potent, selective, and preferably orally bioavailable direct thrombin inhibitors.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	206-214
9231661-3	1997	To examine the contribution of the severity and duration of diabetes on cellular and heparin-releasable cardiac LPL activity, Wistar rats were administered a high (100 mg/kg; D100) or moderate (55 mg/kg; D55) dose of STZ, and LPL activity was examined at various times after diabetes induction.	Heparin	85-92	lipoprotein lipase	Rattus norvegicus	112-115
9231661-4	1997	Heparin perfusion of the isolated Langendorff control heart induced the release of LPL activity as an initial fast phase followed by a slow phase of release.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	83-86
9231661-6	1997	Severe STZ-induced diabetes reduced heparin-releasable LPL activity by 1 week in the D100 rats.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	55-58
9231661-8	1997	The elevated heparin-releasable LPL peak could not be explained by an enhanced LPL synthesis because both cellular and surface-bound LPL activities in myocytes from D55 rats were low, relative to control.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	32-35
9231661-10	1997	Moreover, acute (90-min) treatment of D55 rats with rapid-acting insulin also reduced the heparin-releasable LPL activity to normal levels, although it had no effect on the low cellular LPL activity.	Heparin	90-97	lipoprotein lipase	Rattus norvegicus	109-112
9231661-12	1997	These studies demonstrate that in moderate but not severe diabetes, there is an augmented peak heparin-releasable LPL activity.	Heparin	95-102	lipoprotein lipase	Rattus norvegicus	114-117
9231661-13	1997	Whether or not this enhanced heparin-releasable LPL activity has a pathological role in the diabetic heart has yet to be determined.	Heparin	29-36	lipoprotein lipase	Rattus norvegicus	48-51
9285058-1	1997	Gene transfer into hematopoietic progenitor cells is increased when these cells are adherent to the carboxy-terminal chymotryptic fragment of human plasma fibronectin (FN30/35) containing the heparin binding domain (HBD) and the alternatively spliced type three connecting segment (IIICS) region.	Heparin	192-199	fibronectin 1	Homo sapiens	155-166
9288925-0	1997	Heparin-induced structural modifications and oxidative cleavage of human serum albumin in the absence and presence of glucose--implications for transcapillary leakage of albumin in hyperglycaemia.	Heparin	0-7	albumin	Homo sapiens	79-86
9288518-0	1997	Cell activation and thrombin generation in heparin bonded cardiopulmonary bypass circuits using a novel in vitro model.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	20-28
9270876-15	1997	In competition assays using various sulfated polysaccharides, heparin potently inhibited binding of perlecan to TSP1 immobilized on nitrocellulose.	Heparin	62-69	thrombospondin 1	Homo sapiens	112-116
9288925-0	1997	Heparin-induced structural modifications and oxidative cleavage of human serum albumin in the absence and presence of glucose--implications for transcapillary leakage of albumin in hyperglycaemia.	Heparin	0-7	albumin	Homo sapiens	170-177
9221767-4	1997	Effective inhibitors of neurotoxicity of both the apoE peptides and the apoE fragment include heparin, heparan sulfate, sodium chlorate and heparinase, the low-density lipoprotein (LDL) receptor-related protein receptor-associated protein, and a polyclonal anti-LDL receptor-related protein antibody.	Heparin	94-101	apolipoprotein E	Homo sapiens	72-76
9288925-1	1997	Both unfractionated and fractionated, low-molecular-mass heparins were tested on human serum albumin in the absence and presence of glucose at concentrations similar to those frequently found in diabetic hyperglycaemic patients, to ascertain whether heparin and glucose interfered with each other in affecting the conformation of albumin.	Heparin	57-65	albumin	Homo sapiens	93-100
9288925-1	1997	Both unfractionated and fractionated, low-molecular-mass heparins were tested on human serum albumin in the absence and presence of glucose at concentrations similar to those frequently found in diabetic hyperglycaemic patients, to ascertain whether heparin and glucose interfered with each other in affecting the conformation of albumin.	Heparin	57-64	albumin	Homo sapiens	93-100
9288925-3	1997	Spectroscopic studies showed that the binding sites of glucose and heparin on albumin do not overlap and that changes in protein structure depend on complex and mutual interference of glucose and heparin with the protein, although the effects of heparin in modifying the chromophore environment and increasing the ordered structure of the protein also prevailed in the presence of glucose.	Heparin	67-74	albumin	Homo sapiens	78-85
9288925-3	1997	Spectroscopic studies showed that the binding sites of glucose and heparin on albumin do not overlap and that changes in protein structure depend on complex and mutual interference of glucose and heparin with the protein, although the effects of heparin in modifying the chromophore environment and increasing the ordered structure of the protein also prevailed in the presence of glucose.	Heparin	196-203	albumin	Homo sapiens	78-85
9288925-3	1997	Spectroscopic studies showed that the binding sites of glucose and heparin on albumin do not overlap and that changes in protein structure depend on complex and mutual interference of glucose and heparin with the protein, although the effects of heparin in modifying the chromophore environment and increasing the ordered structure of the protein also prevailed in the presence of glucose.	Heparin	196-203	albumin	Homo sapiens	78-85
9288925-4	1997	Heparin binding to albumin rapidly gave rise to oxidative reactions, which were responsible for the increase in the carbonyl content of the protein together with its higher susceptibility to tryptic digestion.	Heparin	0-7	albumin	Homo sapiens	19-26
9288925-8	1997	While only a small percentage of albumin molecules underwent fragmentation in the presence of heparin with glucose, albumin turned out to display in an even higher proportion structural modifications consistent with a higher degree of ordered structure.	Heparin	94-101	albumin	Homo sapiens	33-40
9258342-2	1997	Binding of bFGF to heparin or heparan sulfate has been demonstrated to both stimulate and inhibit growth factor activity.	Heparin	19-26	fibroblast growth factor 2	Homo sapiens	11-15
9223379-0	1997	Fibroblast growth factor-1 induction of delayed-early mRNA expression in NIH 3T3 cells is prolonged by heparin addition.	Heparin	103-110	fibroblast growth factor 1	Mus musculus	0-26
9257695-3	1997	Monkey chymase was purified from cheek pouch vascular tissue using heparin affinity and gel filtration columns.	Heparin	67-74	chymase 1	Homo sapiens	7-14
9218427-1	1997	We have undertaken a comparative study of the interaction of the three mammalian transforming growth factor-betas (TGF-beta) with heparin and heparan sulfate.	Heparin	130-137	transforming growth factor beta 1	Homo sapiens	115-123
9218427-2	1997	TGF-beta1 and -beta2, but not -beta3, bind to heparin and the highly sulfated liver heparan sulfate.	Heparin	46-53	transforming growth factor beta 1	Homo sapiens	0-20
9223379-3	1997	FGF-1-stimulated mitogenesis is potentiated by heparin, a sulfated glycosaminoglycan.	Heparin	47-54	fibroblast growth factor 1	Mus musculus	0-5
9223379-4	1997	In this study, we examined the effect of exogenous heparin on FGF-1-inducible gene expression in murine NIH 3T3 cells using both wild-type FGF-1 and FGF-1/glu132, an FGF-1 mutant with a reduced apparent affinity for heparin.	Heparin	51-58	fibroblast growth factor 1	Mus musculus	62-67
9202024-0	1997	Interaction of the NH2-terminal domain of fibronectin with heparin.	Heparin	59-66	fibronectin 1	Homo sapiens	42-53
9202024-2	1997	Determinants of the interaction of the 29-kDa NH2-terminal domain of fibronectin with heparin were explored by analysis of normal and mutant recombinant NH2-terminal fibronectin fragments produced in an insect cell Baculovirus host vector system.	Heparin	86-93	fibronectin 1	Homo sapiens	69-80
9202024-7	1997	The wild type fragment was capable of promoting matrix-driven translocation, a morphogenetic effect in artificial extracellular matrices that depends on the interaction of the fibronectin NH2 terminus with heparin-like molecules on the surfaces of particles.	Heparin	206-213	fibronectin 1	Homo sapiens	176-187
9202024-12	1997	The results indicate that multiple residues in the Omega-loops of the fibronectin NH2-terminal domain participate in its interactions with heparin.	Heparin	139-146	fibronectin 1	Homo sapiens	70-81
9202024-13	1997	In addition, the conformation of one of the nonbinding mutants may mimic the heparin-induced structural alteration in this fibronectin domain required for certain morphogenetic events.	Heparin	77-84	fibronectin 1	Homo sapiens	123-134
9223379-7	1997	This heparin effect occurs when cells are stimulated with wild-type FGF-1 but not with FGF-1/glu132.	Heparin	5-12	fibroblast growth factor 1	Mus musculus	68-73
9223379-9	1997	These findings are consistent with the proposal that heparin promotes a long-term FGF-1:FGFR interaction which is required for sustained delayed-early gene expression and a full mitogenic response.	Heparin	53-60	fibroblast growth factor 1	Mus musculus	82-87
9223427-0	1997	Identification of heparin-binding sites in midkine and their role in neurite-promotion.	Heparin	18-25	midkine	Homo sapiens	43-50
9223427-2	1997	The three dimensional structure of MK clarified by NMR spectroscopy indicates that several basic amino acids are exposed on the surface of the C-terminal half domain, which retains heparin-binding and neurite-promoting activity.	Heparin	181-188	midkine	Homo sapiens	35-37
9223427-6	1997	Thus, the present result verifies the occurrence of two distinct heparin-binding sites involved in neurite-promoting activity of MK molecule.	Heparin	65-72	midkine	Homo sapiens	129-131
9261263-0	1997	Persistent thrombin generation during heparin therapy in patients with acute coronary syndromes.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	11-19
9288226-4	1997	Both aFGF and bFGF, each with a molecular weight of 18 kDa, were identified in PA using heparin-sepharose chromatography and Western blot analysis.	Heparin	88-95	fibroblast growth factor 1	Homo sapiens	5-9
9288226-4	1997	Both aFGF and bFGF, each with a molecular weight of 18 kDa, were identified in PA using heparin-sepharose chromatography and Western blot analysis.	Heparin	88-95	fibroblast growth factor 2	Homo sapiens	14-18
9212969-7	1997	These data demonstrated that in pediatric CPB, heparin-coated CPB circuits reduced the activation of complements and the production of PMN elastase and IL-6, suggesting the superior biocompatibility of the heparin-coated circuits.	Heparin	47-54	interleukin 6	Homo sapiens	152-156
9261263-1	1997	Intravenous heparin, a fundamental therapy in the treatment of patients with acute coronary syndromes, acts by inhibiting thrombin and activated factors X, IX, XI, and XII.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	122-130
9261263-2	1997	It has also been demonstrated that heparin reduces plasma fibrinopeptide A, a marker of thrombin activity, but it is unknown whether it decreases prothrombin fragment 1+2, an indirect marker of thrombin generation.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	88-96
9261263-7	1997	Hence, in patients with acute coronary syndromes, intravenous heparin at a dose reaching an activated partial thromboplastin time that adequately suppresses thrombin activity does not suppress increased thrombin generation.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	157-165
9262116-4	1997	Thrombin inhibitors, such as hirudin and argatroban, are a practical anticoagulant substitute where heparin cannot be used.	Heparin	100-107	coagulation factor II, thrombin	Homo sapiens	0-8
9340230-3	1997	The overlapping effect of coumarin and heparin therapy requires a close daily monitoring of the clotting inhibition (partial thromboplastin time, thromboplastin time, thrombin time).	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	167-175
9198248-5	1997	In patients having orthopedic surgery, inactivating bound thrombin with direct antithrombins markedly reduces venous thromboembolic events, compared with heparin or its derivatives, without significant impairment of hemostasis.	Heparin	154-161	coagulation factor II, thrombin	Homo sapiens	58-66
9245569-9	1997	IN CONCLUSION: (1) MAPK is activated in a time-dependent manner in response to injury; (2) the antiproliferative effect of heparin in vivo is not mediated through the inhibition of MAPK activity induced 30 min after injury; (3) the activation of MAPK after 30 min is not dependent on PDGF, bFGF, or thrombin following vessel injury in the rat.	Heparin	123-130	coagulation factor II	Rattus norvegicus	299-307
9202242-12	1997	Heparin and heparan sulfate inhibited the IGFBP-5/PAI-1 interaction; however, several other glycosaminoglycans had no effect.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	42-49
9282310-9	1997	Stromal cells grown in the presence of aFGF and heparin grow actively and maintain a fibroblast-like morphology for a number of passages, transduce efficiently with a human growth hormone (hGH) expression vector, and express and secrete high levels of hGH.	Heparin	48-55	growth hormone 1	Homo sapiens	173-187
9268229-2	1997	We assessed cardiac heparin-releasable LPL activity in an acquired model of hypertension, the fructose-hypertensive rat.	Heparin	20-27	lipoprotein lipase	Rattus norvegicus	39-42
9268229-4	1997	After short- and long-term fructose treatment, LPL activity in coronary perfusates was determined by retrogradely perfusing the hearts with heparin.	Heparin	140-147	lipoprotein lipase	Rattus norvegicus	47-50
9268229-6	1997	Discontinuation of fructose treatment for 2 weeks from the long-term group normalized blood pressure and cardiac heparin-releasable LPL activity.	Heparin	113-120	lipoprotein lipase	Rattus norvegicus	132-135
9268229-7	1997	Interestingly, acute vasodilation by in vitro perfusion of coronary vasodilators like nifedipine and CGS-21680 increased cardiac heparin-releasable LPL activity in the long-term group to control levels.	Heparin	129-136	lipoprotein lipase	Rattus norvegicus	148-151
9260561-9	1997	All but one were found to carry the same mutation, Arg213Gly, affecting the heparin-binding domain of EC-SOD.	Heparin	76-83	superoxide dismutase 3	Homo sapiens	102-108
9240301-8	1997	The heparin coating is not accompanied by similar reductions in coagulation or fibrinolysis, suggesting that thrombin and plasmin formation during cardiopulmonary bypass occurs mainly independently of the contact system activation.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	109-117
9207183-9	1997	Thus, alternative splicing of PlGF RNA produces at least three polypeptides with different secretion pattern, heparin-binding affinity and dimerization properties.	Heparin	110-117	placental growth factor	Homo sapiens	30-34
9195945-0	1997	Heparin-induced self-association of fibroblast growth factor-2.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	36-62
9195945-2	1997	Fibroblast growth factor-2 (FGF-2), a potent angiogenic factor, requires heparin for dimerization and activation of the FGF receptor tyrosine kinase.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	0-26
9195945-2	1997	Fibroblast growth factor-2 (FGF-2), a potent angiogenic factor, requires heparin for dimerization and activation of the FGF receptor tyrosine kinase.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	28-33
9195945-2	1997	Fibroblast growth factor-2 (FGF-2), a potent angiogenic factor, requires heparin for dimerization and activation of the FGF receptor tyrosine kinase.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	28-31
9195945-4	1997	Analytical ultracentrifugation of FGF-2 in the presence of heparin-derived saccharides shows that both an active heparin octasaccharide and an inactive heparin-like disaccharide induce fibroblast growth factor-2 self-association.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	34-39
9195945-4	1997	Analytical ultracentrifugation of FGF-2 in the presence of heparin-derived saccharides shows that both an active heparin octasaccharide and an inactive heparin-like disaccharide induce fibroblast growth factor-2 self-association.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	185-211
9195945-4	1997	Analytical ultracentrifugation of FGF-2 in the presence of heparin-derived saccharides shows that both an active heparin octasaccharide and an inactive heparin-like disaccharide induce fibroblast growth factor-2 self-association.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	34-39
9195945-4	1997	Analytical ultracentrifugation of FGF-2 in the presence of heparin-derived saccharides shows that both an active heparin octasaccharide and an inactive heparin-like disaccharide induce fibroblast growth factor-2 self-association.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	185-211
9195945-6	1997	Evidence is presented indicating that the dimer conformation induced by the heparin octasaccharide is a side by side dimer with the FGF-2 molecules cis to the heparin, while the disaccharide-induced dimer is a head to head dimer in which FGF-2 molecules are trans to the ligand.	Heparin	76-83	fibroblast growth factor 2	Homo sapiens	132-137
9195945-6	1997	Evidence is presented indicating that the dimer conformation induced by the heparin octasaccharide is a side by side dimer with the FGF-2 molecules cis to the heparin, while the disaccharide-induced dimer is a head to head dimer in which FGF-2 molecules are trans to the ligand.	Heparin	76-83	fibroblast growth factor 2	Homo sapiens	238-243
9195945-7	1997	These results, combined with previous studies, support the model that formation of a specific side by side heparin-induced FGF-2 dimer is required for activation of the FGF receptor.	Heparin	107-114	fibroblast growth factor 2	Homo sapiens	123-128
9188488-4	1997	In the present study, heparanase activity was examined on RL95 cell surface HS subpopulations in the presence of a synthetic peptide (CRPKAKAKAKAKDQTK) of heparin/heparan sulfate-interacting protein (HIP; Liu, S., Smith, S. E., Julian, J., Rohde, L. H., Karin, N. J., and Carson, D. D. (1996) J. Biol.	Heparin	155-162	heparanase	Homo sapiens	22-32
9217011-1	1997	The C-terminal, heparin-binding domain of human extracellular superoxide dismutase (hEC-SOD) has been studied as a fusion to human carbonic anhydrase II (HCAII).	Heparin	16-23	superoxide dismutase 3	Homo sapiens	84-91
9199199-2	1997	The binding site in heparin and heparan sulfate for fibroblast growth factor-2 (basic fibroblast growth factor) has been described as rich in glucosamine-2-sulfate 1--&gt;4 linked to iduronic acid-2-sulfate.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	52-78
9199199-7	1997	Acharan sulfate inhibits heparin"s enhancement of fibroblast growth factor-2 mitogenic activity, without affecting cell viability, while N-sulfoacharan sulfate shows heparin-like activity but at a greatly reduced level.	Heparin	25-32	fibroblast growth factor 2	Homo sapiens	50-76
9217011-4	1997	The fusion of the 27 C-terminal amino acids of hEC-SOD to the C-terminal of HCAII (FusCC) resulted in the formation of a monomeric protein, which binds to heparin-Sepharose with approximately the same affinity as the tetrameric hEC-SOD.	Heparin	155-162	superoxide dismutase 3	Homo sapiens	47-54
9217011-7	1997	The NOESY spectra demonstrate that the C-terminal in both FusCC and hEC-SOD binds to heparin, and that arginine side chains take part in the binding.	Heparin	85-92	superoxide dismutase 3	Homo sapiens	68-75
9184147-7	1997	These results demonstrate that recognition of thrombomodulin by thrombin is steered electrostatically by the highly charged regions of the fibrinogen recognition site and the heparin binding site, to which the chondroitin sulfate moiety binds and enhances the affinity of the interaction.	Heparin	175-182	coagulation factor II, thrombin	Homo sapiens	64-72
9169521-6	1997	Synaptic potentiation induced by FK-506 was significantly attenuated by co-injecting BAPTA, heparin/dantrolene (inhibitors of intracellular Ca2+ release), a CaM-binding peptide, or CaM-KII/PKC pseudosubstrate peptides.	Heparin	92-99	carbonic anhydrase 2	Rattus norvegicus	140-143
9200692-3	1997	Kinetic analysis indicated that antithrombin (AT with P2 Gly) inhibited thrombin L99Y, 14.1- and 5.5-fold slower than thrombin in the absence and presence of heparin, respectively.	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	36-44
9223678-9	1997	Heparin (5 mg/ml in the pipette solution) inhibited both [Ca2+]i responses and membrane currents induced by ANG II and ATP, but not by caffeine.	Heparin	0-7	angiotensinogen	Rattus norvegicus	108-114
9184748-8	1997	The alb-hep immobilized surface was able to bind much more thrombin than ATIII, which is probably due to the less specific heparin-thrombin interaction as compared to the heparin-ATIII interaction.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	131-139
9208230-4	1997	Addition of heparin, or treatment with chlorate, an inhibitor of proteoglycan sulfation, resulted in enhanced or reduced growth factor response, respectively, and eliminated the differences between FGF-1 and FGF-2.	Heparin	12-19	fibroblast growth factor 1	Mus musculus	198-203
9208230-7	1997	Addition of HSPG ectodomains, isolated from cultured 3T3 cells or produced as recombinant molecules, to chlorate-treated cultures of 3T3 cells inhibited the mitogenic activity of FGF-2 and eliminated the effect of heparin as a potentiator of either growth factor.	Heparin	214-221	syndecan 2	Mus musculus	12-16
9169495-8	1997	These mechanisms include: first, heparin enhancement of antithrombin III-dependent inhibition of factor V activation by thrombin; second, the inactivation of membrane-bound FVa by APC; and third, the proteolytic inactivation of membrane-bound factor V by APC, which is enhanced by heparin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	60-68
9169746-6	1997	In contrast, heparin inhibited the ability of CAP18(106-138) and CAP18(106-138)-IgG to suppress LPS-induced TNF production.	Heparin	13-20	cathelicidin antimicrobial peptide	Homo sapiens	46-51
9169746-6	1997	In contrast, heparin inhibited the ability of CAP18(106-138) and CAP18(106-138)-IgG to suppress LPS-induced TNF production.	Heparin	13-20	cathelicidin antimicrobial peptide	Homo sapiens	65-70
9169746-6	1997	In contrast, heparin inhibited the ability of CAP18(106-138) and CAP18(106-138)-IgG to suppress LPS-induced TNF production.	Heparin	13-20	tumor necrosis factor	Homo sapiens	108-111
9290261-1	1997	Extracellular superoxide dismutase (EC-SOD) with amino acid substitution R213G generated by the nucleotide substitution 760C--&gt;G in the heparin binding domain is responsible for the high EC-SOD level in serum.	Heparin	139-146	superoxide dismutase 3	Homo sapiens	0-34
9151824-6	1997	Although M-T7 retains binding to a number of interleukin-8 N-terminal (ELR) deletion mutants, binding to mutants containing deletions in the C-terminal heparin-binding domain of interleukin-8 is abrogated.	Heparin	152-159	C-X-C motif chemokine ligand 8	Homo sapiens	178-191
9290261-1	1997	Extracellular superoxide dismutase (EC-SOD) with amino acid substitution R213G generated by the nucleotide substitution 760C--&gt;G in the heparin binding domain is responsible for the high EC-SOD level in serum.	Heparin	139-146	superoxide dismutase 3	Homo sapiens	36-42
9290261-1	1997	Extracellular superoxide dismutase (EC-SOD) with amino acid substitution R213G generated by the nucleotide substitution 760C--&gt;G in the heparin binding domain is responsible for the high EC-SOD level in serum.	Heparin	139-146	superoxide dismutase 3	Homo sapiens	190-196
9153200-8	1997	The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	49-57
9152995-0	1997	Heparin promotes beta-secretase cleavage of the Alzheimer"s amyloid precursor protein.	Heparin	0-7	amyloid beta precursor protein	Homo sapiens	60-85
9241751-1	1997	Previous investigations suggested that heparin administration to humans enhances the tissue type plasminogen activator (tPA) levels in blood, but it remains uncertain whether this effect induces fibrinolysis.	Heparin	39-46	plasminogen activator, tissue type	Homo sapiens	85-118
9441286-5	1997	In comparison, the heparin from Polfa, which was found to be not toxic at standard concentrations (20 U/ml), inhibited almost completely the growth of CD34+ cells if used at higher concentrations (2000 U/ml).	Heparin	19-26	CD34 molecule	Homo sapiens	151-155
9441286-7	1997	Therefore, the heparin from Gibco, being well tolerated by clonogenic CD34+ cells, should be recommended as an anticoagulant for harvesting viable haematopoietic cells for transplantation purposes, or for in vitro diagnostic tests.	Heparin	15-22	CD34 molecule	Homo sapiens	70-74
9214693-9	1997	When mucosal preparations were subjected to heparin-Sepharose chromatography, it bound tightly and eluted in the same position on a salt gradient as authentic human group II PLA2.	Heparin	44-51	phospholipase A2 group IB	Homo sapiens	174-178
9187018-9	1997	The results suggest fibrin B beta 15-25 interaction with thrombin, possibly by blocking the heparin-binding site.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	57-65
9187023-2	1997	Heparin augments the inhibitory activity of antithrombin (AT) towards thrombin, factor Xa (FXa) and other activated clotting enzymes.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	48-56
9168236-0	1997	The in vitro anti-HIV efficacy of negatively charged human serum albumin is antagonized by heparin.	Heparin	91-98	albumin	Homo sapiens	59-72
9139874-3	1997	When extracts of the cells were fractionated on columns of heparin-Sepharose, bFGF-like activity was found in extracts from each cell line.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	78-82
9115268-0	1997	Functional requirements for inhibition of thrombin by antithrombin III in the presence and absence of heparin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	42-50
9146328-0	1997	Endothelin-1 and neutrophil activation during heparin-coated cardiopulmonary bypass.	Heparin	46-53	endothelin 1	Homo sapiens	0-12
9115268-2	1997	Mutations that decreased the susceptibility of thrombin to inhibition by antithrombin III in the presence and absence of heparin (W50A, E229A, and R233A) also decreased hydrolysis of a small tripeptidyl substrate.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	47-55
9115268-6	1997	These residues were clustered among a patch of basic residues on a surface of thrombin perpendicular to the face containing the active site cleft and were predicted to interact directly with heparin.	Heparin	191-198	coagulation factor II, thrombin	Homo sapiens	78-86
9146328-2	1997	The present study compares two different heparin coatings in terms of the release of endothelin-1 and neutrophil glycoproteins.	Heparin	41-48	endothelin 1	Homo sapiens	85-97
9191238-0	1997	Heparin modulates endothelial production of monocyte chemotactic peptide-1 following interferon-gamma stimulation.	Heparin	0-7	interferon gamma	Homo sapiens	85-101
9191239-0	1997	Endothelial cells: heparin modulates the induction of functional antigen presentation by IFN-gamma.	Heparin	19-26	interferon gamma	Homo sapiens	89-98
9141532-5	1997	FGF-2 was extracted by heparin-Sepharose affinity chromatography and quantified by specific RIA.	Heparin	23-30	fibroblast growth factor 2	Homo sapiens	0-5
9183014-5	1997	Drosophila laminin also bound to the mouse heparan sulfate proteoglycan perlecan and the formation of this complex was inhibited by heparin, but not by chondroitin sulfate.	Heparin	132-139	Laminin A	Drosophila melanogaster	11-18
9183014-7	1997	Elastase and other proteases degraded Drosophila laminin to a restricted number of larger fragments (40-300 kDa), almost all of which were bound to a heparin affinity column.	Heparin	150-157	Laminin A	Drosophila melanogaster	49-56
9183014-10	1997	Therefore, Drosophila laminin and mouse laminin-1 differ in certain aspects of protease stability and heparin-binding sites that, in part, can be attributed to their different alpha chains.	Heparin	102-109	Laminin A	Drosophila melanogaster	22-29
9183014-10	1997	Therefore, Drosophila laminin and mouse laminin-1 differ in certain aspects of protease stability and heparin-binding sites that, in part, can be attributed to their different alpha chains.	Heparin	102-109	Laminin A	Drosophila melanogaster	40-47
9092495-8	1997	The finding that several cobra CTXs and phospholipase A2 bind to heparin with different affinity may provide information on the synergistic action of the two venom proteins.	Heparin	65-72	phospholipase A2 group IB	Homo sapiens	40-56
9227345-11	1997	The high in vitro TSA-IL6 cell growth rate is attributable to the IL6-induced production of growth factors, some of which possess heparin-binding properties, such as amphiregulin.	Heparin	130-137	interleukin 6	Mus musculus	22-25
9227345-11	1997	The high in vitro TSA-IL6 cell growth rate is attributable to the IL6-induced production of growth factors, some of which possess heparin-binding properties, such as amphiregulin.	Heparin	130-137	interleukin 6	Mus musculus	66-69
9125499-1	1997	Interaction of basic fibroblast growth factor (FGF-2) with heparin or heparan sulfate proteoglycans (HSPGs) is required for receptor activation and initiation of biological responses.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	47-52
9125499-7	1997	The interaction of these heparin species with FGF-2 does not induce a significant conformational change in the overall structure of FGF-2, but small chemical shift changes are observed in both heparin and receptor binding sites.	Heparin	25-32	fibroblast growth factor 2	Homo sapiens	46-51
9154655-3	1997	Heparin inhibits vascular smooth muscle cell proliferation and lowers blood pressure by regulating endogenous endothelin 1 production.	Heparin	0-7	endothelin 1	Rattus norvegicus	110-122
9125499-10	1997	These data allow us to propose a novel mechanism to explain the functional interaction of FGF-2 with heparin and its transmembrane receptor.	Heparin	101-108	fibroblast growth factor 2	Homo sapiens	90-95
9133522-6	1997	The decrease in NO production by heparin was accompanied by a 72% decrease in steady-state Nos 3 mRNA as well as a 49% decrease in immunodetectable endothelial NO synthase (eNOS) protein.	Heparin	33-40	nitric oxide synthase 3	Bos taurus	91-96
9133522-6	1997	The decrease in NO production by heparin was accompanied by a 72% decrease in steady-state Nos 3 mRNA as well as a 49% decrease in immunodetectable endothelial NO synthase (eNOS) protein.	Heparin	33-40	nitric oxide synthase 3	Bos taurus	173-177
9133522-7	1997	CONCLUSIONS: These data show that high-dose heparin at concentrations achieved in some acute cardiovascular settings increases in vitro platelet aggregation in media conditioned by endothelial cells by decreasing endothelial NO production through a mechanism that involves a decrease in steady-state Nos 3 mRNA and eNOS protein.	Heparin	44-51	nitric oxide synthase 3	Bos taurus	300-305
9133522-7	1997	CONCLUSIONS: These data show that high-dose heparin at concentrations achieved in some acute cardiovascular settings increases in vitro platelet aggregation in media conditioned by endothelial cells by decreasing endothelial NO production through a mechanism that involves a decrease in steady-state Nos 3 mRNA and eNOS protein.	Heparin	44-51	nitric oxide synthase 3	Bos taurus	315-319
9101093-8	1997	Heparin completely blocked bFGF binding to TSP and to the 140-kDa fragment.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	27-31
9142932-8	1997	Treatment with bisindolylmaleimide, a specific protein kinase C (PKC) inhibitor, and heparin attenuated polycation-mediated PLD activation.	Heparin	85-92	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	124-127
9101093-8	1997	Heparin completely blocked bFGF binding to TSP and to the 140-kDa fragment.	Heparin	0-7	thrombospondin 1	Homo sapiens	43-46
9135573-15	1997	Our results with heparin also suggest that the binding sites on IGFBP-3 for IGF-I and IGF-II are not completely identical.	Heparin	17-24	insulin like growth factor 1	Homo sapiens	76-81
9129989-4	1997	Mb 28C3-1 was previously demonstrated to inhibit the heparin-accelerated formation of antithrombin III-thrombin complexes.	Heparin	53-60	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	86-102
9129989-4	1997	Mb 28C3-1 was previously demonstrated to inhibit the heparin-accelerated formation of antithrombin III-thrombin complexes.	Heparin	53-60	coagulation factor II	Mus musculus	90-98
9119887-5	1997	Heparin inhibited FGF2-stimulated epithelial cell growth but also basal myoepithelial cell proliferation and this inhibition could be overcome by the addition of EGF.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	18-22
9140688-6	1997	These trials are too small to draw reliable conclusions, although several trials have suggested that intravenous heparin is beneficial for maintaining patency after t-PA therapy.	Heparin	113-120	plasminogen activator, tissue type	Homo sapiens	165-169
9107173-0	1997	Endogenous basic fibroblast growth factor displaced by heparin from the lumenal surface of human blood vessels is preferentially sequestered by injured regions of the vessel wall.	Heparin	55-62	fibroblast growth factor 2	Homo sapiens	11-41
9107173-2	1997	Among the growth factors that promote SMC proliferation is basic fibroblast growth factor (bFGF), which is characterized by a high affinity for heparin and is associated with heparan sulfate on cell surfaces and extracellular matrices.	Heparin	144-151	fibroblast growth factor 2	Homo sapiens	59-89
9107173-2	1997	Among the growth factors that promote SMC proliferation is basic fibroblast growth factor (bFGF), which is characterized by a high affinity for heparin and is associated with heparan sulfate on cell surfaces and extracellular matrices.	Heparin	144-151	fibroblast growth factor 2	Homo sapiens	91-95
9107173-5	1997	Heparin displaced bFGF from the lumenal surface of the vein, and the released bFGF stimulated proliferation of SMCs.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	18-22
9107173-6	1997	Likewise, systemic administration of heparin during open heart surgery resulted in a marked increase in plasma bFGF levels.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	111-115
9107173-9	1997	CONCLUSIONS: Despite its beneficial effects, heparin may displace active bFGF, which subsequently may be preferentially deposited on injured vessel walls, thus contributing to the pathogenesis of restenosis.	Heparin	45-52	fibroblast growth factor 2	Homo sapiens	73-77
9151047-11	1997	Studying the platelet function, a statistically significant (P &lt; 0.01) better preserved ADP- and collagen-induced platelet aggregation was seen in the r-hirudin/aprotinin-treated animals when compared with heparin/aprotinin-treated animals.	Heparin	209-216	pancreatic trypsin inhibitor-like	Sus scrofa	164-173
9143230-12	1997	Heparin (50 U/ml) and dextran sulfate (200 mg/ml) restored endothelium-dependent relaxations to bradykinin (10(-10)-10(-6) M) in arteries exposed to poly-L-arginine (10(-6) M) or poly-L-lysine (10(-6) M).	Heparin	0-7	kininogen 1	Canis lupus familiaris	96-106
9134652-4	1997	These studies showed that a) thrombin binding to GC could be competitively inhibited by heparin and b) the equilibrium association constant for thrombin-GC interaction was reduced up to ten-fold by chemical modifications at the HBS.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	29-37
9121441-7	1997	Both the binding and mitogenic response of antisense-perlecan-expressing clones to bFGF can be rescued by exogenous heparin or perlecan.	Heparin	116-123	fibroblast growth factor 2	Homo sapiens	83-87
9134652-4	1997	These studies showed that a) thrombin binding to GC could be competitively inhibited by heparin and b) the equilibrium association constant for thrombin-GC interaction was reduced up to ten-fold by chemical modifications at the HBS.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	144-152
9134652-6	1997	Altogether these results demonstrated that GC interaction with thrombin involves the enzyme heparin binding site, whereas the fibrinogen recognition site does not play a significant role.	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	63-71
9086298-2	1997	We separated the LDLs containing apoB-48 (apoB-48 LDL) and apoB-100 (apoB-100 LDL) from the plasma of this patient using heparin-sepharose column chromatography.	Heparin	121-128	apolipoprotein B	Homo sapiens	33-40
9079643-0	1997	Heparin facilitates dissociation of complexes between thrombin and a reactive site mutant (L444R) of heparin cofactor II.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	54-62
9079643-6	1997	We now report that heparin facilitates dissociation of the thrombin-rHCII(L444R) complex.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	59-67
9079643-7	1997	In the presence of heparin, thrombin is inhibited rapidly and completely by a 35-fold molar excess of rHCII(L444R), but subsequently approximately 50% of the thrombin activity reappears with a t1/2 of approximately 20 min.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	28-36
9079643-7	1997	In the presence of heparin, thrombin is inhibited rapidly and completely by a 35-fold molar excess of rHCII(L444R), but subsequently approximately 50% of the thrombin activity reappears with a t1/2 of approximately 20 min.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	158-166
9079643-10	1997	Addition of heparin at longer intervals after formation of the thrombin-rHCII(L444R) complex causes a progressive decrease in the thrombin plateau, suggesting that in the absence of heparin the complex is slowly converted to a non-dissociable form.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	63-71
9079643-10	1997	Addition of heparin at longer intervals after formation of the thrombin-rHCII(L444R) complex causes a progressive decrease in the thrombin plateau, suggesting that in the absence of heparin the complex is slowly converted to a non-dissociable form.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	130-138
9086298-2	1997	We separated the LDLs containing apoB-48 (apoB-48 LDL) and apoB-100 (apoB-100 LDL) from the plasma of this patient using heparin-sepharose column chromatography.	Heparin	121-128	apolipoprotein B	Homo sapiens	59-67
9086298-2	1997	We separated the LDLs containing apoB-48 (apoB-48 LDL) and apoB-100 (apoB-100 LDL) from the plasma of this patient using heparin-sepharose column chromatography.	Heparin	121-128	apolipoprotein B	Homo sapiens	69-77
9056686-10	1997	EPO (12 to 200 U/mL) stimulated ET release time- and dose-dependently by up to 83.2% (P &lt; .01) within 12 h in the absence of fetal calf serum and heparin.	Heparin	149-156	erythropoietin	Homo sapiens	0-3
9054425-4	1997	Like other FGF-2 proteins, bacterially produced rainbow trout FGF-2 protein binds tightly to heparin-Sepharose and also promotes the proliferation of fibroblast cells.	Heparin	93-100	fibroblast growth factor 2	Homo sapiens	62-67
9047009-2	1997	Previously, dPRP was shown to associate with heparin-containing molecules and was found to reside, at least in part, within the decidual extracellular matrix, where it was postulated to influence decidual cells and other cell types.	Heparin	45-52	prp	Drosophila melanogaster	12-16
9124611-4	1997	The diminished activity of oxidized SLPI could be almost completely restored when an iduronate-containing glycosaminoglycan, such as heparin, heparan sulfate, or dermatan sulfate, was added to the reaction medium.	Heparin	133-140	secretory leukocyte peptidase inhibitor	Homo sapiens	36-40
9066381-3	1997	This work tested the hypothesis that heparin-bonded circuits per se are effective in preserving cells and reducing thrombin generation when a reduced dose of heparin is used in vitro.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	115-123
9066381-3	1997	This work tested the hypothesis that heparin-bonded circuits per se are effective in preserving cells and reducing thrombin generation when a reduced dose of heparin is used in vitro.	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	115-123
9066381-9	1997	CONCLUSIONS: Cell activation and thrombin generation were significantly reduced as a result of the presence of immobilized heparin in a system of cardiopulmonary bypass with reduced plasma heparin.	Heparin	123-130	coagulation factor II, thrombin	Homo sapiens	33-41
9062361-3	1997	This conclusion is based on demonstration of HB-EGF synthesis and secretion by primary culture HUC, identification of HER1 as an activatable HB-EGF receptor on HUC surfaces, stimulation of HUC clonal growth by HB-EGF, inhibition of HB-EGF-stimulated growth by heparin and of log-phase growth by CRM 197, a specific inhibitor of HB-EGF/HER1 interaction, and identification of human urothelium as a site of HB-EGF precursor (proHB-EGF) synthesis in vivo.	Heparin	260-267	epidermal growth factor receptor	Homo sapiens	118-122
9138592-4	1997	Supplementing gels with heparin or fibronectin produced a significant decrease in mu, even at the lowest concentrations studied (1 microgram/ml fibronectin or 0.4 microgram/ml heparin).	Heparin	24-31	fibronectin 1	Homo sapiens	144-155
9138592-4	1997	Supplementing gels with heparin or fibronectin produced a significant decrease in mu, even at the lowest concentrations studied (1 microgram/ml fibronectin or 0.4 microgram/ml heparin).	Heparin	176-183	fibronectin 1	Homo sapiens	35-46
9110152-1	1997	In the last few years, three new heparin binding growth factors that interact with the Epidermal Growth Factor receptor (EGFR) and/or the related p185erbB-2 tyrosine kinase have been identified.	Heparin	33-40	epidermal growth factor receptor	Homo sapiens	87-119
9110152-1	1997	In the last few years, three new heparin binding growth factors that interact with the Epidermal Growth Factor receptor (EGFR) and/or the related p185erbB-2 tyrosine kinase have been identified.	Heparin	33-40	epidermal growth factor receptor	Homo sapiens	121-125
9110152-1	1997	In the last few years, three new heparin binding growth factors that interact with the Epidermal Growth Factor receptor (EGFR) and/or the related p185erbB-2 tyrosine kinase have been identified.	Heparin	33-40	erb-b2 receptor tyrosine kinase 2	Homo sapiens	146-156
9151155-6	1997	During apheresis using heparin, the plasma levels of prostaglandin E2 (PGE2) increased significantly (5.6 +/- 1.2 (mean +/- SE, n = 4) pg/ml before apheresis and 33.4 +/- 13.2 after apheresis, p &lt; 0.05) in association with an increase in bradykinin levels (17.9 +/- 2.6 pg/ml before apheresis and 470 +/- 135 after apheresis, p &lt; 0.01).	Heparin	23-30	kininogen 1	Homo sapiens	241-251
9087872-3	1997	With the heparin-induced-low-density lipoprotein-precipitation (HELP), low-density lipoprotein (LDL), fibrinogen, and lipoprotein(a) can be reduced about 55%, 50%, and 60%, respectively.	Heparin	9-16	fibrinogen beta chain	Homo sapiens	102-112
9098798-9	1997	Therefore, neutralization of the activity that stimulates cell growth by antibasic fibroblast growth factor antibody suggests that the third peak, which was eluted at approximately 1.5 to 2 M NaCl in heparin affinity chromatography, might be a basic fibroblast growth factor-like growth factor.	Heparin	200-207	fibroblast growth factor 2	Bos taurus	77-107
9067536-0	1997	Examination of the mechanism by which heparin antagonizes activation of a model endothelium by interferon-gamma (IFN-gamma).	Heparin	38-45	interferon gamma	Homo sapiens	95-111
9067536-0	1997	Examination of the mechanism by which heparin antagonizes activation of a model endothelium by interferon-gamma (IFN-gamma).	Heparin	38-45	interferon gamma	Homo sapiens	113-122
9067536-3	1997	Radioligand binding assays demonstrated that total binding of 125I-IFN-gamma to the EAhy.926 endothelial hybridoma cell line was reduced in the presence of heparin or heparan sulphate (HS); the structurally dissimilar GAG chondroitin sulphate had no effect.	Heparin	156-163	interferon gamma	Homo sapiens	67-76
9105824-18	1997	CONCLUSIONS: The findings suggest that in elective cardiac surgery heparin cannot prevent generation of both thrombin and fibrin, born throughout CPB and postoperatively.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	109-117
9062364-8	1997	Heparin at the concentration that neutralized the function of amphiregulin, or antibodies against TGFalpha or HB-EGF also reduced the release of PGE2 from IFN-gamma-stimulated NHBECs.	Heparin	0-7	interferon gamma	Homo sapiens	155-164
9033392-3	1997	AT-Denver in the presence of heparin inhibited K60fA thrombin with a second-order association rate constant [k = 4.2 +/- 0.1) x 10(5) M-1 s-1] that was 3.2-fold faster than thrombin [k = (1.3 +/- 0.1) x 10(5) M-1 s-1].	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	53-61
9042823-5	1997	In the epoetin beta group the coagulation time (K) of thromboelastogram (TEG) showed an increase from 4.8 to 5.4 minutes by the seventh study day and after the initiation of heparin therapy a further increase to 7.5 minutes.	Heparin	174-181	erythropoietin	Homo sapiens	7-14
9131716-8	1997	The increases in plasma myeloperoxidase, lactoferrin, C3bc and TCC were lower in the heparin-coated group compared to the control group.	Heparin	85-92	myeloperoxidase	Homo sapiens	24-39
9038197-5	1997	Moreover, LpL-(313-448) displayed heparin sensitive binding to normal, but not to HSPG deficient Chinese hamster ovary cells.	Heparin	34-41	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	10-13
9038197-10	1997	Two segments of the domain are necessary for efficient binding to alpha2MR/LRP, one comprising residues 380-384 and another overlapping the segment important for binding to heparin.	Heparin	173-180	LDL receptor related protein 1	Homo sapiens	66-78
9012354-3	1997	The Ca2+ waves persisted in the absence of extracellular Ca2+ but were largely abolished by thapsigargin and intracellular heparin, indicating that Ca2+ was released from intracellular stores.	Heparin	123-130	carbonic anhydrase 2	Rattus norvegicus	4-7
9030584-10	1997	Two types of FGF binding sites were identified: an ionic strength and heparin-independent site that represents FGF binding to CFR290-740 and an additional FGF binding site that is heparan sulfate-dependent and sensitive to high ionic strength.	Heparin	70-77	fibroblast growth factor 10	Gallus gallus	13-16
9030584-10	1997	Two types of FGF binding sites were identified: an ionic strength and heparin-independent site that represents FGF binding to CFR290-740 and an additional FGF binding site that is heparan sulfate-dependent and sensitive to high ionic strength.	Heparin	70-77	fibroblast growth factor 10	Gallus gallus	111-114
9030584-10	1997	Two types of FGF binding sites were identified: an ionic strength and heparin-independent site that represents FGF binding to CFR290-740 and an additional FGF binding site that is heparan sulfate-dependent and sensitive to high ionic strength.	Heparin	70-77	fibroblast growth factor 10	Gallus gallus	111-114
9098971-0	1997	Characterisation of silica-based heparin affinity sorbents from equilibrium binding studies on plasma fractions containing thrombin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	123-131
9098971-4	1997	Of the two types of heparin-silica evaluated, heparin-Fractosil 1000, with a pore size of 1000 A, displayed a capacity of 2.4 mol of thrombin/mol of heparin (mol T-mol H).	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	133-141
9098971-4	1997	Of the two types of heparin-silica evaluated, heparin-Fractosil 1000, with a pore size of 1000 A, displayed a capacity of 2.4 mol of thrombin/mol of heparin (mol T-mol H).	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	133-141
9098971-4	1997	Of the two types of heparin-silica evaluated, heparin-Fractosil 1000, with a pore size of 1000 A, displayed a capacity of 2.4 mol of thrombin/mol of heparin (mol T-mol H).	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	133-141
9098971-10	1997	Binding stoichiometries and affinities in the high concentration range were similar to values reported for a largely non-specific electrostatic thrombin-heparin interaction.	Heparin	153-160	coagulation factor II, thrombin	Homo sapiens	144-152
9098971-13	1997	Thus, the results indicated that heparin-thrombin interactions with these systems involve both a weak electrostatic and a strong biospecific interaction component.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	41-49
9070209-3	1997	The endogenous 78Se peak was the most abundant plasma Se-containing protein, and it showed the affinity to heparin, indicating it to be selenoprotein P (Sel P).	Heparin	107-114	selenoprotein P	Homo sapiens	136-151
9070209-3	1997	The endogenous 78Se peak was the most abundant plasma Se-containing protein, and it showed the affinity to heparin, indicating it to be selenoprotein P (Sel P).	Heparin	107-114	selenoprotein P	Homo sapiens	153-158
9033392-3	1997	AT-Denver in the presence of heparin inhibited K60fA thrombin with a second-order association rate constant [k = 4.2 +/- 0.1) x 10(5) M-1 s-1] that was 3.2-fold faster than thrombin [k = (1.3 +/- 0.1) x 10(5) M-1 s-1].	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	173-181
9033324-0	1997	Effect of heparin loading during congenital heart operation on thrombin generation and blood loss.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	63-71
9031720-0	1997	Mechanism of thrombin inhibition by antithrombin and heparin cofactor II in the presence of heparin.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	13-21
9031720-2	1997	The experimental data indicate that the reaction of thrombin inhibition was second-order both in the absence and in the presence of heparin, and that the apparent rate constant increased at heparin concentrations ranging from 10(-9) to 10(-6) M and decreased at higher concentrations.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	52-60
9056901-0	1997	The binding of interleukin 2 to heparin revealed by a novel ELISA method.	Heparin	32-39	interleukin 2	Homo sapiens	15-28
9031720-2	1997	The experimental data indicate that the reaction of thrombin inhibition was second-order both in the absence and in the presence of heparin, and that the apparent rate constant increased at heparin concentrations ranging from 10(-9) to 10(-6) M and decreased at higher concentrations.	Heparin	190-197	coagulation factor II, thrombin	Homo sapiens	52-60
9031720-7	1997	In this model, heparin (H) binds quickly to the inhibitor (I) and forms a heparin-inhibitor complex (HI), which is more reactive than the free inhibitor towards thrombin, leading to the formation of an inactive inhibitor-thrombin complex (I*E) and the release of free heparin, in a second step which is rate limiting.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	161-169
9031720-7	1997	In this model, heparin (H) binds quickly to the inhibitor (I) and forms a heparin-inhibitor complex (HI), which is more reactive than the free inhibitor towards thrombin, leading to the formation of an inactive inhibitor-thrombin complex (I*E) and the release of free heparin, in a second step which is rate limiting.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	221-229
9031720-7	1997	In this model, heparin (H) binds quickly to the inhibitor (I) and forms a heparin-inhibitor complex (HI), which is more reactive than the free inhibitor towards thrombin, leading to the formation of an inactive inhibitor-thrombin complex (I*E) and the release of free heparin, in a second step which is rate limiting.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	161-169
9068899-0	1997	Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	13-21
9031720-7	1997	In this model, heparin (H) binds quickly to the inhibitor (I) and forms a heparin-inhibitor complex (HI), which is more reactive than the free inhibitor towards thrombin, leading to the formation of an inactive inhibitor-thrombin complex (I*E) and the release of free heparin, in a second step which is rate limiting.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	221-229
9031720-9	1997	These data indicate that heparin-HC II complex reactivity is greater than that of the heparin-AT complex towards thrombin, whereas heparin affinity is stronger for AT.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	113-121
9031720-9	1997	These data indicate that heparin-HC II complex reactivity is greater than that of the heparin-AT complex towards thrombin, whereas heparin affinity is stronger for AT.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	113-121
9031720-9	1997	These data indicate that heparin-HC II complex reactivity is greater than that of the heparin-AT complex towards thrombin, whereas heparin affinity is stronger for AT.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	113-121
9031720-10	1997	At heparin concentrations higher than 10(-6) M, the decrease in the reaction rate was in keeping with the formation of a heparin-thrombin complex (HE), whose inactivation by the heparin-inhibitor complex (HI) is slower than that of the free protease.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	129-137
9074711-1	1997	OBJECTIVE: The objectives of the present study were to determine functional (i.e., heparin-releasable) and intracellular (i.e., heparin-non-releasable) cardiac lipoprotein lipase (LPL) activity during the development of hypertension in spontaneously hypertensive (SHR) rats.	Heparin	128-135	lipoprotein lipase	Rattus norvegicus	160-178
9074711-3	1997	LPL activity in coronary perfusates was determined by retrogradely perfusing the hearts with heparin (5 U/ml).	Heparin	93-100	lipoprotein lipase	Rattus norvegicus	0-3
9074711-5	1997	RESULTS: With the development of hypertension in SHR rats, there was a concomitant and progressive reduction in the heparin-releasable coronary endothelial LPL activity.	Heparin	116-123	lipoprotein lipase	Rattus norvegicus	156-159
9074711-7	1997	However, acute vasodilation with nifedipine (a Ca2+ influx blocker) or CGS-21680 (A2-purinergic receptor agonist) increased the peak heparin-releasable LPL activity in hearts isolated from SHR rats.	Heparin	133-140	lipoprotein lipase	Rattus norvegicus	152-155
9068929-13	1997	New therapeutic approaches, such as direct thrombin inhibitors and thrombolytic agents, could overcome some limitations of the standard heparin plus oral anticoagulation therapy.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	43-51
8995378-0	1997	Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	45-53
9211051-1	1997	Heparin, the most widely used antithrombin, suffers several limitations, including high inter-individual variability of anticoagulant response, a nonlinear dose-response curve, inability to inactivate clot-bound thrombin, a requirement for endogenous cofactors and inactivation by platelet factor 4 and heparinase.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	34-42
9211051-3	1997	Heparin"s drawbacks may be overcome by direct thrombin inhibitors.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	46-54
9089410-0	1997	Importance of 2-O-sulfate groups of uronate residues in heparin for activation of FGF-1 and FGF-2.	Heparin	56-63	fibroblast growth factor 1	Mus musculus	82-87
9089410-5	1997	These results suggest that a high content of 2-O-sulfate groups in uronate residues of heparin is required for activation of both FGF-1 and FGF-2.	Heparin	87-94	fibroblast growth factor 1	Mus musculus	130-135
9162742-6	1997	Treatment of macrophages with heparin (10 micrograms/ml and 5 mg/ml) and heparinase I (1 U/ml), which releases substantial amounts of apoE from HepG2 cells, results in no additional release of apoE from macrophages.	Heparin	30-37	apolipoprotein E	Homo sapiens	134-138
9162742-6	1997	Treatment of macrophages with heparin (10 micrograms/ml and 5 mg/ml) and heparinase I (1 U/ml), which releases substantial amounts of apoE from HepG2 cells, results in no additional release of apoE from macrophages.	Heparin	30-37	apolipoprotein E	Homo sapiens	193-197
9021749-9	1997	The intracellular Ca2+ channels/receptors through which the sperm factor-mediated Ca2+ release was investigated by using heparin, a competitive inhibitor of the inositol 1,4,5 trisphosphate receptor (InsP3R), and ryanodine, which binds the ryanodine receptor (RyR).	Heparin	121-128	ryanodine receptor 1, skeletal muscle	Mus musculus	240-258
9021749-9	1997	The intracellular Ca2+ channels/receptors through which the sperm factor-mediated Ca2+ release was investigated by using heparin, a competitive inhibitor of the inositol 1,4,5 trisphosphate receptor (InsP3R), and ryanodine, which binds the ryanodine receptor (RyR).	Heparin	121-128	ryanodine receptor 1, skeletal muscle	Mus musculus	260-263
8994426-10	1997	In contrast, with UFH or DS, the rate of thrombin inhibition is twofold slower in plasma than in buffer.	Heparin	18-21	coagulation factor II, thrombin	Homo sapiens	41-49
8995378-5	1997	Heparin increased the stoichiometry of inhibition of L444R-rHCII with alpha-thrombin (compared with minus glycosaminoglycan) but decreased it with R93A,R97A,R101A-thrombin, a mutant thrombin that does not bind glycosaminoglycans.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	76-84
8995378-5	1997	Heparin increased the stoichiometry of inhibition of L444R-rHCII with alpha-thrombin (compared with minus glycosaminoglycan) but decreased it with R93A,R97A,R101A-thrombin, a mutant thrombin that does not bind glycosaminoglycans.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	163-171
8995378-5	1997	Heparin increased the stoichiometry of inhibition of L444R-rHCII with alpha-thrombin (compared with minus glycosaminoglycan) but decreased it with R93A,R97A,R101A-thrombin, a mutant thrombin that does not bind glycosaminoglycans.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	163-171
8995378-9	1997	A time course of alpha-thrombin inhibition by L444R-rHCII/heparin showed a rapid but transient inhibition with approximately 80% of the alpha-thrombin activity being regained after 6 h of incubation.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	23-31
8995378-9	1997	A time course of alpha-thrombin inhibition by L444R-rHCII/heparin showed a rapid but transient inhibition with approximately 80% of the alpha-thrombin activity being regained after 6 h of incubation.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	142-150
8995378-11	1997	Heparin fragments of 8-20 polysaccharides in length rapidly accelerated L444R-rHCII inhibition of both alpha-thrombin and R93A,R97A,R101A-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	109-117
8995378-11	1997	Heparin fragments of 8-20 polysaccharides in length rapidly accelerated L444R-rHCII inhibition of both alpha-thrombin and R93A,R97A,R101A-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	138-146
8995378-13	1997	These results collectively indicate that ternary complex formation, mediated by heparin, increases L444R-rHCII inactivation by alpha-thrombin.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	133-141
14517394-4	1997	Remarkably, FGF-1 is sequestered as a latent form in the conditioned medium, as assessed by a lack of mitogenic activity and heparin affinity.	Heparin	125-132	fibroblast growth factor 1	Mus musculus	12-17
8988995-6	1997	Ecteola cellulose effectively reversed the effect of heparin on the thrombin time and the addition of PRP significantly increased the MAWB (P &lt; 0.0001) and MAWP-PPP (P &lt; 0.0001).	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	68-76
8995297-8	1997	We demonstrated that the TSP homologous domain containing the TSP type I motif of ADAMTS-1 is functional for binding to heparin.	Heparin	120-127	a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 1	Mus musculus	82-90
14517394-5	1997	High salt treatment of conditioned medium unveils the sequestered FGF-1 as novel high molecular weight forms with reduced heparin affinity and a molecular mass of approximately 30-40kDa; we refer to these as exported forms of FGF-1 (XP-FGF-1).	Heparin	122-129	fibroblast growth factor 1	Mus musculus	66-71
14517394-5	1997	High salt treatment of conditioned medium unveils the sequestered FGF-1 as novel high molecular weight forms with reduced heparin affinity and a molecular mass of approximately 30-40kDa; we refer to these as exported forms of FGF-1 (XP-FGF-1).	Heparin	122-129	fibroblast growth factor 1	Mus musculus	226-231
9013799-7	1997	In a reconstituted system with heparin and phosphatidylcholine, 15-HPETE decreased the ability of heparin to inactivate thrombin activity.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	120-128
9192073-7	1997	Recombinant apoE3(1-183) was isolated by a combination of heparin-Sepharose chromatography and reverse-phase HPLC.	Heparin	58-65	apolipoprotein E	Homo sapiens	12-17
9013799-7	1997	In a reconstituted system with heparin and phosphatidylcholine, 15-HPETE decreased the ability of heparin to inactivate thrombin activity.	Heparin	98-105	coagulation factor II, thrombin	Homo sapiens	120-128
8978319-7	1997	Strain following pretreatment with heparin released 12.6 +/- 1.6% of the total FGF-2 (versus 15.8 +/- 0.9% for strain alone, P &lt; .05), indicating that most FGF-2 was liberated from the nuclear or cytoplasmic pools and not from low-affinity extracellular receptors.	Heparin	35-42	fibroblast growth factor 2	Homo sapiens	79-84
8978319-7	1997	Strain following pretreatment with heparin released 12.6 +/- 1.6% of the total FGF-2 (versus 15.8 +/- 0.9% for strain alone, P &lt; .05), indicating that most FGF-2 was liberated from the nuclear or cytoplasmic pools and not from low-affinity extracellular receptors.	Heparin	35-42	fibroblast growth factor 2	Homo sapiens	159-164
8978319-8	1997	Conversely, strain in the presence of heparin released 25.2 +/- 3.5% of the total FGF-2 (versus 15.6 +/- 2.6% for strain alone, P &lt; .05).	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	82-87
9610889-8	1997	The IGF-I did not bind to heparin-sepharose, while CGF bound to it and was eluted with 0.6M NaCl from heparin-sepharose columns.	Heparin	102-109	insulin like growth factor 1	Homo sapiens	4-9
8978319-10	1997	In addition, larger mechanical strains lead to transfer of intracellular FGF-2 to the extracellular low-affinity receptors, where FGF-2 may be displaced by heparin.	Heparin	156-163	fibroblast growth factor 2	Homo sapiens	73-78
9610889-9	1997	Heparin-sepharose 0.2M NaCl fractions of cementum extracts contained IGF-I migrating with Mr 7,500, but its mobility was not affected by N-glycosidase treatment.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	69-74
9144032-6	1997	Low molecular weight heparin, administered to 7 patients on dietary treatment, caused a marked drop in the F1 + 2 plasma level, providing evidence that the elevation in F1 + 2 indicates an accelerated in vivo thrombin generation rather than impaired renal catabolism.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	209-217
9028720-5	1997	We also observed that protamine effects on chemotaxis, proliferation and c-fos expression are inhibited by heparin that human insulin stimulates cell proliferation and 3H-thymidine incorporation (ANOVA, p &lt; 0.0001) at concentrations equal to or greater than 480 pmol/l and that these effects of insulin persist in the presence of protamine.	Heparin	107-114	insulin	Homo sapiens	126-133
9028720-5	1997	We also observed that protamine effects on chemotaxis, proliferation and c-fos expression are inhibited by heparin that human insulin stimulates cell proliferation and 3H-thymidine incorporation (ANOVA, p &lt; 0.0001) at concentrations equal to or greater than 480 pmol/l and that these effects of insulin persist in the presence of protamine.	Heparin	107-114	insulin	Homo sapiens	298-305
9034837-1	1997	BACKGROUND: Heparin-induced extracorporeal LDL/fibrinogen precipitation (HELP) eliminates selectively fibrinogen, LDL, cholesterol, triglycerides and LP(a) from blood plasma using extracorporeal circulation.	Heparin	12-19	fibrinogen beta chain	Homo sapiens	47-57
9034837-1	1997	BACKGROUND: Heparin-induced extracorporeal LDL/fibrinogen precipitation (HELP) eliminates selectively fibrinogen, LDL, cholesterol, triglycerides and LP(a) from blood plasma using extracorporeal circulation.	Heparin	12-19	fibrinogen beta chain	Homo sapiens	102-112
9283907-2	1997	All haematopoietic progenitor cells including primitive LTC-IC, multilineage CFU-mix, myeloid CFU-GM and erythroid BFU-E adhere to the heparin-binding domains of the extracellular matrix component fibronectin.	Heparin	135-142	fibronectin 1	Homo sapiens	197-208
9040053-4	1997	To examine whether heparin and cholesterol induce MMP and tissue inhibitor of metalloproteinase (TIMP) in human heart fibroblast (HHF) cells, confluent HHF cells were treated with cholesterol (100 microM) or heparin (20 microM).	Heparin	19-26	TIMP metallopeptidase inhibitor 1	Homo sapiens	58-95
9034202-7	1997	LDL binding to LPL containing heparin-agarose was also disrupted by the amino-terminal antibodies to apoB.	Heparin	30-37	apolipoprotein B	Homo sapiens	101-105
9040053-4	1997	To examine whether heparin and cholesterol induce MMP and tissue inhibitor of metalloproteinase (TIMP) in human heart fibroblast (HHF) cells, confluent HHF cells were treated with cholesterol (100 microM) or heparin (20 microM).	Heparin	19-26	TIMP metallopeptidase inhibitor 1	Homo sapiens	97-101
10639632-2	1997	The results suggest that these agents are comparable to heparin in terms of efficacy, and can be safely administered; however, like that of heparin, the therapeutic index of direct thrombin inhibitors is narrow.	Heparin	140-147	coagulation factor II, thrombin	Homo sapiens	181-189
9127328-2	1997	MPO levels were markedly elevated during the entire HD procedure with heparin.	Heparin	70-77	myeloperoxidase	Homo sapiens	0-3
9470339-11	1997	Finally, cTnT was reported to be able to predict which patients will benefit from treatment with regimens of low molecular weight heparin.	Heparin	130-137	troponin T2, cardiac type	Homo sapiens	9-13
9069450-13	1997	ApoB, apoC-III, apoC-III in heparin-manganese precipitate (reflecting apoC-III in VLDL and LDL) and apoE decreased significantly by 21, 18, 26 and 49%, respectively.	Heparin	28-35	apolipoprotein B	Homo sapiens	0-4
9127328-9	1997	MPO levels with heparin alone were shown to markedly rise in the closed system.	Heparin	16-23	myeloperoxidase	Homo sapiens	0-3
9469625-2	1997	Unlike heparin, it manifests its anticoagulant effect by binding directly to the active site of thrombin.	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	96-104
9489431-12	1997	Preincubation of Rantes or FMLP with heparin did not induce any significant changes in eosinophil chemotaxis.	Heparin	37-44	formyl peptide receptor 1	Homo sapiens	27-31
9346390-0	1997	Influence of heparin and type-IV collagen on IL-6 synthesis by rat glomerular mesangial cells.	Heparin	13-20	interleukin 6	Rattus norvegicus	45-49
9346390-5	1997	The action of heparin on IL-6 synthesis by MCs is presently unknown.	Heparin	14-21	interleukin 6	Rattus norvegicus	25-29
9346390-6	1997	We investigated the effect of heparin on IL-6 production when MCs were cultured with or without type-IV collagen, a major constituent of ECM.	Heparin	30-37	interleukin 6	Rattus norvegicus	41-45
9346390-7	1997	When MCs were cultured without coating, heparin significantly decreased their IL-6 production; on type-IV collagen, heparin had no significant effect.	Heparin	40-47	interleukin 6	Rattus norvegicus	78-82
9346390-8	1997	When tumor necrosis factor alpha (TNF-alpha) was used to stimulate the cells to produce IL-6, heparin was able to decrease the stimulatory effect of TNF-alpha when the cells were cultured on plastic but not when in contact with type-IV collagen.	Heparin	94-101	tumor necrosis factor	Rattus norvegicus	5-32
9346390-8	1997	When tumor necrosis factor alpha (TNF-alpha) was used to stimulate the cells to produce IL-6, heparin was able to decrease the stimulatory effect of TNF-alpha when the cells were cultured on plastic but not when in contact with type-IV collagen.	Heparin	94-101	tumor necrosis factor	Rattus norvegicus	34-43
9346390-8	1997	When tumor necrosis factor alpha (TNF-alpha) was used to stimulate the cells to produce IL-6, heparin was able to decrease the stimulatory effect of TNF-alpha when the cells were cultured on plastic but not when in contact with type-IV collagen.	Heparin	94-101	interleukin 6	Rattus norvegicus	88-92
9346390-8	1997	When tumor necrosis factor alpha (TNF-alpha) was used to stimulate the cells to produce IL-6, heparin was able to decrease the stimulatory effect of TNF-alpha when the cells were cultured on plastic but not when in contact with type-IV collagen.	Heparin	94-101	tumor necrosis factor	Rattus norvegicus	149-158
9346390-9	1997	Thus we conclude that heparin has an inhibitory effect on IL-6 secretion by MCs that is prevented by type-IV collagen.	Heparin	22-29	interleukin 6	Rattus norvegicus	58-62
9156415-15	1997	The highest correlation was found for the improvement of Marder score and thrombin inhibition in the heparin group with r = 0.42.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	74-82
9469633-3	1997	The direct thrombin inhibitors hirudin and bivalirudin are potentially superior agents to heparin and have been tested in several clinical trials.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	11-19
8952537-7	1996	Only one bFGF isoform (17.8 kd) was found in idiopathic pulmonary fibrosis and chronic beryllium disease lung tissues and interacted with heparin-like molecules in the lung.	Heparin	138-145	fibroblast growth factor 2	Homo sapiens	9-13
9200336-9	1997	Moreover, a significant inverse correlation was found between the heparin-stimulated TFPI antigen plasma levels and both BMI and basal plasma insulin concentrations.	Heparin	66-73	insulin	Homo sapiens	142-149
12215771-6	1997	In addition it could bind on the heparin-Sepharose affinity chromatography column as Apo-E.	Heparin	33-40	apolipoprotein E	Homo sapiens	85-90
9424855-8	1997	Heparin had a beneficial effect on the microcirculatory values, serum IL-6 concentration, and morphologic changes.	Heparin	0-7	interleukin 6	Rattus norvegicus	70-74
9003378-2	1996	We have previously shown that heparin activates RMCP-1 and that RMCP-1, when bound to heparin PG, is largely resistant to inhibition by a variety of macromolecular protease inhibitors.	Heparin	30-37	mast cell protease 1-like 1	Rattus norvegicus	48-54
9003378-2	1996	We have previously shown that heparin activates RMCP-1 and that RMCP-1, when bound to heparin PG, is largely resistant to inhibition by a variety of macromolecular protease inhibitors.	Heparin	86-93	mast cell protease 1-like 1	Rattus norvegicus	64-70
9003378-3	1996	In the search for alternative mechanisms in the regulation of RMCP-1 activity, we hypothesized that heparin antagonists, by interfering with the RMCP-1/heparin PG interaction, might influence the activity of heparin-bound mast cell chymase.	Heparin	100-107	mast cell protease 1-like 1	Rattus norvegicus	62-68
9003378-3	1996	In the search for alternative mechanisms in the regulation of RMCP-1 activity, we hypothesized that heparin antagonists, by interfering with the RMCP-1/heparin PG interaction, might influence the activity of heparin-bound mast cell chymase.	Heparin	100-107	mast cell protease 1-like 1	Rattus norvegicus	145-151
9003378-3	1996	In the search for alternative mechanisms in the regulation of RMCP-1 activity, we hypothesized that heparin antagonists, by interfering with the RMCP-1/heparin PG interaction, might influence the activity of heparin-bound mast cell chymase.	Heparin	152-159	mast cell protease 1-like 1	Rattus norvegicus	62-68
9003378-3	1996	In the search for alternative mechanisms in the regulation of RMCP-1 activity, we hypothesized that heparin antagonists, by interfering with the RMCP-1/heparin PG interaction, might influence the activity of heparin-bound mast cell chymase.	Heparin	152-159	mast cell protease 1-like 1	Rattus norvegicus	145-151
9003378-5	1996	LF proved to decrease the activity of heparin PG-associated RMCP-1, although a portion of the enzyme activity was resistant to regulation.	Heparin	38-45	mast cell protease 1-like 1	Rattus norvegicus	60-66
8941092-0	1996	Effects of low-dose heparin infusion on arterial endothelin-1 release in humans.	Heparin	20-27	endothelin 1	Homo sapiens	49-61
8973550-8	1996	LPL was decreased by 40% after 1 h. At that time, the LPL activity that could be released from isolated hearts by single-pass perfusion with heparin for 2 min ("functional LPL") was decreased by 75%.	Heparin	141-148	lipoprotein lipase	Rattus norvegicus	0-3
8973550-8	1996	LPL was decreased by 40% after 1 h. At that time, the LPL activity that could be released from isolated hearts by single-pass perfusion with heparin for 2 min ("functional LPL") was decreased by 75%.	Heparin	141-148	lipoprotein lipase	Rattus norvegicus	54-57
8973550-8	1996	LPL was decreased by 40% after 1 h. At that time, the LPL activity that could be released from isolated hearts by single-pass perfusion with heparin for 2 min ("functional LPL") was decreased by 75%.	Heparin	141-148	lipoprotein lipase	Rattus norvegicus	172-176
8941092-1	1996	BACKGROUND: The aim of this study was to evaluate the effect of low-dose heparin infusion on arterialized endothelin-1 (ET-1) release in the presence of fasting or high insulin levels in healthy humans.	Heparin	73-80	endothelin 1	Homo sapiens	106-118
8941092-1	1996	BACKGROUND: The aim of this study was to evaluate the effect of low-dose heparin infusion on arterialized endothelin-1 (ET-1) release in the presence of fasting or high insulin levels in healthy humans.	Heparin	73-80	endothelin 1	Homo sapiens	120-124
8941092-5	1996	Two hours after heparin infusion (test 1), ET-1 levels decreased by 32% (3.52 +/- 0.60 to 3.02 +/- 0.73 pg/mL), while nitric oxide (NO) and forearm blood flow increased by 29% and 14%, respectively.	Heparin	16-23	endothelin 1	Homo sapiens	43-47
8941092-7	1996	There was a significant interaction between the effect of decreasing ET-1 levels and the heparin treatment (F, 4.06; df, 3.30; P &lt; .01).	Heparin	89-96	endothelin 1	Homo sapiens	69-73
8940380-4	1996	The heparin Sepharose purified material degraded IGFBP-5 into 22-, 17-, and 16-kDa fragments.	Heparin	4-11	insulin like growth factor binding protein 5	Homo sapiens	49-56
8940384-7	1996	dPRP is capable of binding heparin, and a significant fraction of synthesized dPRP resides within the decidual extracellular matrix.	Heparin	27-34	prp	Drosophila melanogaster	0-4
21153086-12	1996	Heparin also specifically blocked the induction of both cell-cell adhesion and prolactin gene expression.	Heparin	0-7	prolactin	Rattus norvegicus	79-88
8977530-10	1996	The release of GM-CSF was not inhibited by catalase but was inhibited by cyclohexamide and by mixing of EPO with heparin, suggesting that the action is due to the cationic property of EPO.	Heparin	113-120	eosinophil peroxidase	Homo sapiens	184-187
8941092-9	1996	During the heparin/insulin period, ET-1 increased by 25%, returning to fasting values; nitric oxide levels increased by 12%; and forearm blood flow remained unchanged.	Heparin	11-18	endothelin 1	Homo sapiens	35-39
8941092-10	1996	CONCLUSIONS: The present study showed that it is possible to decrease ET-1 levels by use of low-dose heparin infusion in humans.	Heparin	101-108	endothelin 1	Homo sapiens	70-74
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	15-22	plasminogen activator, urokinase	Homo sapiens	75-78
9092406-5	1996	Heparin, which limits the paradoxial increase of thrombin after thrombolysis significantly decreases this risk.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	49-57
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	60-68
8910598-1	1996	The binding of heparin to antithrombin greatly accelerates the rate of inhibition of the target proteinases thrombin and factor Xa.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	30-38
8972008-7	1996	High TNF alpha levels, due to leakage during perfusion, were associated with activation of coagulation in all patients, that became obvious after the end of perfusion, when heparin treatment had been antagonized.	Heparin	173-180	tumor necrosis factor	Homo sapiens	5-14
8982859-0	1996	Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V).	Heparin	164-171	collagen type V alpha 1 chain	Homo sapiens	58-68
8901772-1	1996	BACKGROUND: Even when large doses of heparin are administered during cardiopulmonary bypass, thrombin is produced.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	93-101
9028578-1	1996	The possibility that diabetes reduces functional, heparin-releasable lipoprotein lipase (HR-LPL) activity on the coronary vasculature of perfused hearts by altering endothelial binding sites for the enzyme was examined by measuring the binding and subsequent heparin-induced release of exogenous lipoprotein lipase purified from bovine milk (mLPL).	Heparin	50-57	lipoprotein lipase	Rattus norvegicus	69-87
9028578-2	1996	Rat hearts were first perfused with heparin (5 U/mL) for 5 min to displace endogenous HR-LPL into the perfusate.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	89-92
8895319-0	1996	Binding of insulin-like growth factor (IGF) I or II to IGF-binding protein-2 enables it to bind to heparin and extracellular matrix.	Heparin	99-106	insulin like growth factor 1	Homo sapiens	11-45
8895319-6	1996	In this study we report that IGFBP-2 binds to heparin if IGF-I or IGF-II is also included in the incubation buffer.	Heparin	46-53	insulin like growth factor 1	Homo sapiens	57-62
8895319-8	1996	The binding of IGFBP-2 to heparin was detectable using an IGF-I to IGFBP-2 molar ratio of 2:1.	Heparin	26-33	insulin like growth factor 1	Homo sapiens	58-63
8895319-10	1996	Binding was also inhibited by a synthetic IGFBP-5 peptide that contained a heparin-binding domain, but not by a peptide with an identical charge to mass ratio that does not bind to heparin.	Heparin	75-82	insulin like growth factor binding protein 5	Homo sapiens	42-49
25851791-3	1996	The inhibitor is currently undergoing clinical trials as a potential replacement for the extensively used thrombin inhibitor heparin.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	106-114
8901652-9	1996	CONCLUSIONS: Heparin administration suppresses thrombin activity in most but not all patients undergoing coronary interventions.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	47-55
8982859-3	1996	Thus, the heparin affinity of alpha 1(V) may be approximately two-fold higher than those of the other alpha (V)-chains.	Heparin	10-17	collagen type V alpha 1 chain	Homo sapiens	30-40
8982859-8	1996	A possible explanation for difference in heparin affinity among the subtypes of molecules and the separated alpha-chains is that the heparin affinity of type V collagen molecule is governed by the number of alpha 1(V) chains contained in the molecule and that steric restraint in a triple-helical conformation weakens the binding of alpha 1(V) chain to heparin.	Heparin	133-140	collagen type V alpha 1 chain	Homo sapiens	207-217
8982859-8	1996	A possible explanation for difference in heparin affinity among the subtypes of molecules and the separated alpha-chains is that the heparin affinity of type V collagen molecule is governed by the number of alpha 1(V) chains contained in the molecule and that steric restraint in a triple-helical conformation weakens the binding of alpha 1(V) chain to heparin.	Heparin	133-140	collagen type V alpha 1 chain	Homo sapiens	333-343
8982859-8	1996	A possible explanation for difference in heparin affinity among the subtypes of molecules and the separated alpha-chains is that the heparin affinity of type V collagen molecule is governed by the number of alpha 1(V) chains contained in the molecule and that steric restraint in a triple-helical conformation weakens the binding of alpha 1(V) chain to heparin.	Heparin	133-140	collagen type V alpha 1 chain	Homo sapiens	207-217
8982859-8	1996	A possible explanation for difference in heparin affinity among the subtypes of molecules and the separated alpha-chains is that the heparin affinity of type V collagen molecule is governed by the number of alpha 1(V) chains contained in the molecule and that steric restraint in a triple-helical conformation weakens the binding of alpha 1(V) chain to heparin.	Heparin	133-140	collagen type V alpha 1 chain	Homo sapiens	333-343
8982859-0	1996	Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V).	Heparin	164-171	collagen type V alpha 1 chain	Homo sapiens	86-96
8982859-0	1996	Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V).	Heparin	164-171	collagen type V alpha 1 chain	Homo sapiens	86-96
8982859-0	1996	Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V).	Heparin	164-171	collagen type V alpha 1 chain	Homo sapiens	86-96
8982859-0	1996	Separation of the subtypes of type V collagen molecules, [alpha 1(V)]2 alpha 2(V) and alpha 1(V) alpha 2(V) alpha 3(V), by chain composition-dependent affinity for heparin: single alpha 1(V) chain shows intermediate heparin affinity between those of the type V collagen subtypes composed of [alpha 1(V)]2 alpha 2(V) and of alpha 1(V) alpha 2(V) alpha 3(V).	Heparin	164-171	collagen type V alpha 1 chain	Homo sapiens	86-96
8914022-0	1996	Heparin and heparinoids prevent the binding of immune complexes containing nucleosomal antigens to the GBM and delay nephritis in MRL/lpr mice.	Heparin	0-7	Fas (TNF receptor superfamily member 6)	Mus musculus	134-137
8914022-11	1996	We conclude that interaction of heparin or heparin analogs with HS reactive immune complexes containing nucleosomal antigens prevents the binding of these immune complexes to the GBM and delays nephritis in MRL/lpr mice.	Heparin	32-39	Fas (TNF receptor superfamily member 6)	Mus musculus	211-214
8981329-7	1996	Treatment of growth-arrested adult SMC cultures with heparin caused a further accumulation in perlecan mRNA levels.	Heparin	53-60	heparan sulfate proteoglycan 2	Rattus norvegicus	94-102
8914022-11	1996	We conclude that interaction of heparin or heparin analogs with HS reactive immune complexes containing nucleosomal antigens prevents the binding of these immune complexes to the GBM and delays nephritis in MRL/lpr mice.	Heparin	43-50	Fas (TNF receptor superfamily member 6)	Mus musculus	211-214
9045943-4	1996	The VHP-inducing activity was detected in the 0.5 M NaCl fraction from the heparin affinity column and was blocked by anti-VEGF neutralizing antibody.	Heparin	75-82	vascular endothelial growth factor A	Homo sapiens	123-127
8950791-8	1996	Antiplatelet profiles of aprosulate were largely similar to those of heparin, although heparin inhibited both thrombin- and collagen-induced aggregation.	Heparin	87-94	coagulation factor II, thrombin	Homo sapiens	110-118
8981663-10	1996	Heparin administration reduced the IL-6 values and also had a positive impact on the microscopic alterations within the rectal wall.	Heparin	0-7	interleukin 6	Rattus norvegicus	35-39
8885834-7	1996	The discovery of the helix-like region in the primary heparin binding site instead of the beta-strand conformation described in the X-ray structures may have important implications in understanding the nature of heparin--FGF-2 interactions.	Heparin	54-61	fibroblast growth factor 2	Homo sapiens	221-226
8885834-8	1996	A total of seven tightly bound water molecules were found in the FGF-2 structure, two of which are located in the heparin binding site.	Heparin	114-121	fibroblast growth factor 2	Homo sapiens	65-70
8824228-4	1996	We now report that BALB/cJ BMMC stimulated with KL + IL-10 + IL-1beta also exhibit the biphasic release of [3H]arachidonic acid with an immediate phase over the first 10 min followed by a delayed phase from 2 to 7 h. The delayed phase of arachidonic acid release and of PGD2 generation was inhibited by heparin, which concomitantly released a phospholipase (PL) A2 from the cells into the supernatant.	Heparin	303-310	interleukin 10	Mus musculus	53-58
8900171-3	1996	Concurrent with a marked increase in dependence on exogenous heparin for optimal activity, sequential deletion of residues in the NYKKPKL sequence in FGF-1 resulted in a progressive loss of thermal stability, resistance to protease, mitogenic activity, and affinity for the transmembrane receptor.	Heparin	61-68	fibroblast growth factor 1	Homo sapiens	150-155
8900171-5	1996	In the presence of sufficiently high concentrations of heparin, the deletion mutants exhibited mitogenic activity equal to wild-type FGF-1.	Heparin	55-62	fibroblast growth factor 1	Homo sapiens	133-138
8824283-10	1996	Heparin and chondroitin 6-sulfate increased phospholipase A2 activity on low density lipoproteins up to 4-fold at 100 microM, whereas heparan sulfate had no effect.	Heparin	0-7	phospholipase A2 group IB	Homo sapiens	44-60
8824251-0	1996	Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	41-49
8824251-0	1996	Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	101-109
8824251-0	1996	Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen.	Heparin	30-37	fibrinogen beta chain	Homo sapiens	181-191
8824251-1	1996	Interaction of the blood clotting proteinase, thrombin, with fibrin monomer and heparin to form a thrombin.fibrin monomer.heparin ternary complex is accompanied by a change in thrombin catalytic specificity.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	46-54
8824251-1	1996	Interaction of the blood clotting proteinase, thrombin, with fibrin monomer and heparin to form a thrombin.fibrin monomer.heparin ternary complex is accompanied by a change in thrombin catalytic specificity.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	98-106
8824251-1	1996	Interaction of the blood clotting proteinase, thrombin, with fibrin monomer and heparin to form a thrombin.fibrin monomer.heparin ternary complex is accompanied by a change in thrombin catalytic specificity.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	98-106
8824251-1	1996	Interaction of the blood clotting proteinase, thrombin, with fibrin monomer and heparin to form a thrombin.fibrin monomer.heparin ternary complex is accompanied by a change in thrombin catalytic specificity.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	46-54
8824251-1	1996	Interaction of the blood clotting proteinase, thrombin, with fibrin monomer and heparin to form a thrombin.fibrin monomer.heparin ternary complex is accompanied by a change in thrombin catalytic specificity.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	98-106
8824251-1	1996	Interaction of the blood clotting proteinase, thrombin, with fibrin monomer and heparin to form a thrombin.fibrin monomer.heparin ternary complex is accompanied by a change in thrombin catalytic specificity.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	98-106
8824251-4	1996	Quantitative analysis of the interactions supports a preferentially ordered path of ternary complex assembly, in which initial binding of heparin to thrombin facilitates binding of fibrin monomer with an approximately 40-fold increased affinity.	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	149-157
8824251-6	1996	These results support a ternary complex model in which heparin binding through exosite II of thrombin facilitates fibrin monomer binding via exosite I, with accompanying changes in thrombin catalytic specificity resulting from perturbations in the active site and reduced accessibility of exosite I to hirudin and fibrinogen.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	93-101
8824228-4	1996	We now report that BALB/cJ BMMC stimulated with KL + IL-10 + IL-1beta also exhibit the biphasic release of [3H]arachidonic acid with an immediate phase over the first 10 min followed by a delayed phase from 2 to 7 h. The delayed phase of arachidonic acid release and of PGD2 generation was inhibited by heparin, which concomitantly released a phospholipase (PL) A2 from the cells into the supernatant.	Heparin	303-310	interleukin 1 beta	Mus musculus	61-69
8824251-6	1996	These results support a ternary complex model in which heparin binding through exosite II of thrombin facilitates fibrin monomer binding via exosite I, with accompanying changes in thrombin catalytic specificity resulting from perturbations in the active site and reduced accessibility of exosite I to hirudin and fibrinogen.	Heparin	55-62	fibrinogen beta chain	Homo sapiens	314-324
8909909-12	1996	CONCLUSIONS: Weight-adjusted duteplase infusion, together with oral aspirin and intravenous heparin, in acute myocardial infarction resulted in patency of the infarct-related coronary artery and a safety profile comparable to those reported for the other form of tissue-type plasminogen activator, alteplase.	Heparin	92-99	plasminogen activator, tissue type	Homo sapiens	263-296
8873615-10	1996	The interaction of vWF with heparin was significantly reduced by substitution of Lys residues 642-645, indicating that these residues may form part of a heparin-binding domain in the carboxy-terminal half of the Cys509-Cys695 loop.	Heparin	28-35	von Willebrand factor	Homo sapiens	19-22
8873615-10	1996	The interaction of vWF with heparin was significantly reduced by substitution of Lys residues 642-645, indicating that these residues may form part of a heparin-binding domain in the carboxy-terminal half of the Cys509-Cys695 loop.	Heparin	153-160	von Willebrand factor	Homo sapiens	19-22
8909666-1	1996	The efficacy of prophylactic administration of H1 and H2 receptor blockers to prevent adverse haemodynamic responses to heparin and protamine was studied.	Heparin	120-127	fibroblast growth factor receptor 1	Homo sapiens	47-56
8808643-1	1996	Heparin and heparan sulfate are related glycosaminoglycans which demonstrate high-affinity interactions with a number of proteins, including antithrombin III.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-157
8899638-17	1996	Heparin, an IP3 receptor antagonist that reduces Ca2+ mobilization, attenuated the inhibitory action 10 microM ACPD from almost 100% to 39 +/- 5% (n = 5).	Heparin	0-7	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	12-24
8915986-2	1996	In addition, heparin has been shown to inhibit thrombin-stimulated smooth muscle cell proliferation.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	47-55
8903003-3	1996	Thrombin activity was dose-dependently reduced by an anti-human tissue factor antibody (76 +/- 3% at 10 micrograms/ml) and by inhibitors like heparin, rec-hirudin, hirulog 1, Napap and hirunorm, a novel hirudin-like thrombin inhibitor (IC50 = 2 +/- 0.4, 8 +/- 1, 130 +/- 22, 199 +/- 29 and 68 +/- 8 nM, respectively).	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	0-8
8845035-7	1996	Altogether the results indicate that firm binding of C1q and C4bp to SAP requires that SAP is presented on a solid phase, that C1q and C4bp react with sites distinct from the heparin binding site, and that C1q and collagen I share binding sites on SAP.	Heparin	175-182	complement component 4 binding protein alpha	Homo sapiens	61-65
8845035-7	1996	Altogether the results indicate that firm binding of C1q and C4bp to SAP requires that SAP is presented on a solid phase, that C1q and C4bp react with sites distinct from the heparin binding site, and that C1q and collagen I share binding sites on SAP.	Heparin	175-182	complement component 4 binding protein alpha	Homo sapiens	135-139
8903462-2	1996	experience hepatocellular necrosis that begins within 4 hr and that prior treatment with anticoagulants (e.g., heparin) which target thrombin prevents the liver injury.	Heparin	111-118	coagulation factor II	Rattus norvegicus	133-141
8885147-1	1996	The smallest circulating von Willebrand factor (vWF) molecule is a dimer composed of two identical subunits containing binding sites for heparin, collagen, platelet glycoproteins and coagulation factor VIII (FVIII).	Heparin	137-144	von Willebrand factor	Homo sapiens	25-46
8885147-1	1996	The smallest circulating von Willebrand factor (vWF) molecule is a dimer composed of two identical subunits containing binding sites for heparin, collagen, platelet glycoproteins and coagulation factor VIII (FVIII).	Heparin	137-144	von Willebrand factor	Homo sapiens	48-51
8885147-5	1996	Heparin affinity chromatography was used to isolate vWF polymers of different degree of multimerization.	Heparin	0-7	von Willebrand factor	Homo sapiens	52-55
8843739-5	1996	Thrombin generated three and serum five easily identified fragments; the dominant fragments, beginning at midportions of IGFBP-3, retained IGF and heparin affinity, whereas the remaining fragments had differential affinities for IGF and heparin.	Heparin	147-154	coagulation factor II, thrombin	Homo sapiens	0-8
8836144-0	1996	Binding and degradation of thrombospondin-1 mediated through heparan sulphate proteoglycans and low-density-lipoprotein receptor-related protein: localization of the functional activity to the trimeric N-terminal heparin-binding region of thrombospondin-1.	Heparin	213-220	thrombospondin-1	Cricetulus griseus	27-43
8836144-0	1996	Binding and degradation of thrombospondin-1 mediated through heparan sulphate proteoglycans and low-density-lipoprotein receptor-related protein: localization of the functional activity to the trimeric N-terminal heparin-binding region of thrombospondin-1.	Heparin	213-220	low-density lipoprotein receptor	Cricetulus griseus	96-128
8836144-0	1996	Binding and degradation of thrombospondin-1 mediated through heparan sulphate proteoglycans and low-density-lipoprotein receptor-related protein: localization of the functional activity to the trimeric N-terminal heparin-binding region of thrombospondin-1.	Heparin	213-220	thrombospondin-1	Cricetulus griseus	239-255
8836144-7	1996	These results indicate that the N-terminal heparin-binding domain in a trivalent configuration is sufficient to mediate binding and degradation of TSP-1 via the proteoglycan-LDLR family pathway.	Heparin	43-50	thrombospondin-1	Cricetulus griseus	147-152
8836144-7	1996	These results indicate that the N-terminal heparin-binding domain in a trivalent configuration is sufficient to mediate binding and degradation of TSP-1 via the proteoglycan-LDLR family pathway.	Heparin	43-50	low-density lipoprotein receptor	Cricetulus griseus	174-178
8702993-5	1996	Heparin pretreatment and a monoclonal antibody ID7 that blocks LDL receptor-binding domain of apoE both inhibited binding, and apoE2/E2 VLDL from a Type III hyperlipidemic subject did not bind.	Heparin	0-7	apolipoprotein E	Homo sapiens	94-98
8702993-5	1996	Heparin pretreatment and a monoclonal antibody ID7 that blocks LDL receptor-binding domain of apoE both inhibited binding, and apoE2/E2 VLDL from a Type III hyperlipidemic subject did not bind.	Heparin	0-7	apolipoprotein E	Homo sapiens	127-132
8884243-0	1996	IP3 receptor antagonist heparin uncompetitively inhibits [3H](+)-SKF-10047 binding to sigma receptors.	Heparin	24-31	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	0-12
8884243-3	1996	However, the IP3 receptor antagonist heparin inhibited [3H](+)-SKF-10047 to sigma receptors in an uncompetitive manner with a Ki of 93 microM.	Heparin	37-44	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	13-25
8780385-9	1996	Although heparin in solution potently inhibited the binding of SF to TSP-1-coated surfaces, even very high concentrations of heparin could not elute SF already bound to TSP-1.	Heparin	9-16	thrombospondin 1	Homo sapiens	69-74
8843739-5	1996	Thrombin generated three and serum five easily identified fragments; the dominant fragments, beginning at midportions of IGFBP-3, retained IGF and heparin affinity, whereas the remaining fragments had differential affinities for IGF and heparin.	Heparin	237-244	coagulation factor II, thrombin	Homo sapiens	0-8
8960401-12	1996	These data demonstrate that early passage cultures of endometrial Fb and Ep cells produce heparin-binding endothelial mitogens that appear to be immunologically related to FGF-2.	Heparin	90-97	fibroblast growth factor 2	Bos taurus	172-177
8864022-11	1996	Release of MPO at CPB end and of LF 45 min after start of CPB and at CPB end were significantly lower in the heparin-coated CPB circuits.	Heparin	109-116	myeloperoxidase	Homo sapiens	11-14
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Heparin	77-84	coagulation factor II, thrombin	Homo sapiens	39-47
8862928-5	1996	Addition of bFGF blocked serum-induced alpha-SM actin expression, whereas addition of TGF beta 1 enhanced alpha-SM actin expression (100%), which in combination with heparin (10 U/ml), led to a pulling apart of the fibroblastic sheet, simulating contraction.	Heparin	166-173	LOW QUALITY PROTEIN: transforming growth factor beta-1	Oryctolagus cuniculus	86-96
8816920-1	1996	The interaction of basic FGF (bFGF) with heparin, heparan sulfate and related sugars can potentiate or antagonize bFGF activity, depending on the size of the saccharide used.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	19-28
8816920-1	1996	The interaction of basic FGF (bFGF) with heparin, heparan sulfate and related sugars can potentiate or antagonize bFGF activity, depending on the size of the saccharide used.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	30-34
8816920-1	1996	The interaction of basic FGF (bFGF) with heparin, heparan sulfate and related sugars can potentiate or antagonize bFGF activity, depending on the size of the saccharide used.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	114-118
8816920-2	1996	Oligosaccharides based on heparin structures, as small as six sugar residues, have been demonstrated to bind to bFGF and block its activity, while larger structures (&gt; 10 sugar residues) tend to potentiate bFGF.	Heparin	26-33	fibroblast growth factor 2	Homo sapiens	112-116
9239682-6	1996	Heparanase (endo-beta-glucuronidase) was isolated and purified by ammonium sulphate precipitation followed by sequential chromatographies on carboxymethyl-, heparin- and ConA-Sepharose columns.	Heparin	157-164	heparanase	Homo sapiens	0-10
8757349-2	1996	Blocking studies performed with heparin or peptides containing the RGD sequence demonstrated that the heparin-binding basic domain of Tat plays a predominant role in CD4+ T cell activation.	Heparin	102-109	CD4 molecule	Homo sapiens	166-169
8800182-0	1996	Thrombin generation with heparin-bonded cardiopulmonary bypass circuits.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	0-8
9239682-7	1996	The placental enzyme was further characterized for its molecular weight and specific inhibition by heparin, and was shown to resemble heparanase expressed by highly metastatic tumor cells and activated cells of the immune system.	Heparin	99-106	heparanase	Homo sapiens	134-144
8702852-8	1996	Based on these data, Lys114 and Lys139, which are outside of the putative pentasaccharide binding site, play pivotal roles in the high affinity binding of heparin to ATIII and the activation of thrombin inhibitory activity.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	194-202
8883267-2	1996	In a recent study we found that concentrations of fibrinopeptide A, a marker of thrombin-mediated fibrin formation, were lower in the first 3 h in patients treated with intravenous heparin (5000 U bolus followed by a fixed-dose 1000 U/h infusion, n = 14) compared with subcutaneous (12,500 U every 12 h, started 4 h after streptokinse, n = 14) administration, but were increased in both groups of patients, consistent with persistent thrombin activity.	Heparin	181-188	coagulation factor II, thrombin	Homo sapiens	80-88
8883267-2	1996	In a recent study we found that concentrations of fibrinopeptide A, a marker of thrombin-mediated fibrin formation, were lower in the first 3 h in patients treated with intravenous heparin (5000 U bolus followed by a fixed-dose 1000 U/h infusion, n = 14) compared with subcutaneous (12,500 U every 12 h, started 4 h after streptokinse, n = 14) administration, but were increased in both groups of patients, consistent with persistent thrombin activity.	Heparin	181-188	coagulation factor II, thrombin	Homo sapiens	434-442
8883269-0	1996	Effect of heparin on the activation of factor XI by fibrin-bound thrombin.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	65-73
8883269-2	1996	In the presence of heparin, ternary complexes between thrombin, fibrin and heparin are formed.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	54-62
8883269-7	1996	We studied the effect of heparin on the activation of factor XI by fibrin-bound thrombin.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	80-88
8883269-14	1996	UFH enhanced thrombin-mediated factor XI activation 68-fold, LMWH (low molecular weight heparin, Fragmin) 12-fold, danaparoid (Orgaran) 3-fold, while the pentasaccharide ORG 31540 did not result in an enhancement.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	13-21
8718884-6	1996	The acid protease cathepsin D generated fragments of 31-33.5 kDa from the COOH-terminal heparin-binding domain of Fn which possessed high immunoreactivity with anti-CS-1.	Heparin	88-95	fibronectin 1	Homo sapiens	114-116
8817878-0	1996	Characterisation of silica-based heparin-affinity adsorbents through column chromatography of plasma fractions containing thrombin.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	122-130
8878902-0	1996	Potentiation of the growth-stimulatory effects of aFGF by heparin in Rama 27 fibroblasts.	Heparin	58-65	fibroblast growth factor 1	Homo sapiens	50-54
8710880-9	1996	The capillary tube formation in vitro was prevented by heparin, which inhibited the binding of TAF to the endothelial cells.	Heparin	55-62	insulin like growth factor binding protein 7	Homo sapiens	95-98
8696947-0	1996	Heparin-induced overexpression of basic fibroblast growth factor, basic fibroblast growth factor receptor, and cell-associated proteoheparan sulfate in cultured coronary smooth muscle cells.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	34-64
8696947-0	1996	Heparin-induced overexpression of basic fibroblast growth factor, basic fibroblast growth factor receptor, and cell-associated proteoheparan sulfate in cultured coronary smooth muscle cells.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	66-96
8696947-2	1996	Heparin in nanogram quantities may promote or even be required for binding of bFGF to its cognate receptor.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	78-82
8696947-11	1996	The heparin-induced increase in cellular protein content includes a 60% to 100% increase in the expression of pericellular bFGF, FGF-R1, and cell membrane-integrated HSPG.	Heparin	4-11	fibroblast growth factor 2	Bos taurus	123-127
8696947-14	1996	These results indicate that heparin, despite its anti-proliferative potency, stimulates the expression of all components of the bFGF system even in coronary SMCs in which growth is inhibited.	Heparin	28-35	fibroblast growth factor 2	Bos taurus	128-132
8806707-0	1996	Characterization of keratinocyte growth factor binding to heparin and dextran sulfate.	Heparin	58-65	fibroblast growth factor 7	Homo sapiens	20-46
8806707-1	1996	Binding of keratinocyte growth factor (KGF) with heparin (molecular weight of 5000) and dextran sulfate (molecular weight of 8000) was studied using an online monitoring of size-exclusion chromatography with light scattering, refractive index, and uv absorbance detectors.	Heparin	49-56	fibroblast growth factor 7	Homo sapiens	11-37
8806707-1	1996	Binding of keratinocyte growth factor (KGF) with heparin (molecular weight of 5000) and dextran sulfate (molecular weight of 8000) was studied using an online monitoring of size-exclusion chromatography with light scattering, refractive index, and uv absorbance detectors.	Heparin	49-56	fibroblast growth factor 7	Homo sapiens	39-42
8806707-3	1996	When mixtures of KGF with heparin were injected into the column, two peaks of heparin/KGF complexes were observed.	Heparin	26-33	fibroblast growth factor 7	Homo sapiens	86-89
8806707-3	1996	When mixtures of KGF with heparin were injected into the column, two peaks of heparin/KGF complexes were observed.	Heparin	78-85	fibroblast growth factor 7	Homo sapiens	17-20
8806707-3	1996	When mixtures of KGF with heparin were injected into the column, two peaks of heparin/KGF complexes were observed.	Heparin	78-85	fibroblast growth factor 7	Homo sapiens	86-89
8806707-5	1996	These results suggest that the heparin/ KGF complex is heterogeneous, consisting of 1,2,3, and 4 KGF molecules per complex.	Heparin	31-38	fibroblast growth factor 7	Homo sapiens	40-43
8806707-5	1996	These results suggest that the heparin/ KGF complex is heterogeneous, consisting of 1,2,3, and 4 KGF molecules per complex.	Heparin	31-38	fibroblast growth factor 7	Homo sapiens	97-100
8806707-6	1996	To calculate the number of heparin molecules in these complexes, the rate of disappearance of free KGF was determined as heparin was added.	Heparin	121-128	fibroblast growth factor 7	Homo sapiens	99-102
8806707-7	1996	The average number of KGF bound to 1 mol of heparin was calculated to be about 2 mol, suggesting that only one heparin molecule is present in these complexes.	Heparin	44-51	fibroblast growth factor 7	Homo sapiens	22-25
8806707-7	1996	The average number of KGF bound to 1 mol of heparin was calculated to be about 2 mol, suggesting that only one heparin molecule is present in these complexes.	Heparin	111-118	fibroblast growth factor 7	Homo sapiens	22-25
8806707-8	1996	The heparin binding of two KGF mutants, i.e., (C1, 15S)KGF (with substitutions of serine for cysteines 1 and 15) and d28KGF (lacking 28 N-terminal amino acid residues), was essentially identical to that of the native sequence KGF.	Heparin	4-11	fibroblast growth factor 7	Homo sapiens	27-30
8921259-5	1996	The 1,4,5-inositol triphosphate (IP3) receptor antagonist heparin as well as the protein kinase C inhibitor NPC 15437 suppressed the uncoupling action of 5-HT, suggesting that the serotonergic effect involved IP3 receptor-mediated release of calcium ions from intracellular stores.	Heparin	58-65	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	33-46
8963700-4	1996	The adjuvant therapy by means of heparin in thrombolysis seems to be necessary especially when alteplase (t-PA) is used.	Heparin	33-40	plasminogen activator, tissue type	Homo sapiens	106-110
24194252-3	1996	Western blot analysis of these heparin-binding fractions was carried out using monoclonal antibodies against human acidic and basic fibroblast growth factors (FGF-1 and-2).	Heparin	31-38	fibroblast growth factor 1	Homo sapiens	159-170
8864947-7	1996	The region of the apoE molecule surrounding residue 212 contains a heparin binding domain.	Heparin	67-74	apolipoprotein E	Homo sapiens	18-22
8836853-0	1996	Photoreactive analog of peptide FN-C/H-V from the carboxy-terminal heparin-binding domains of fibronectin supports endothelial cell adhesion and spreading on biomaterial surfaces.	Heparin	67-74	fibronectin 1	Homo sapiens	94-105
8836853-3	1996	Recently, a peptide sequence (FN-C/H-V) from the 33/66 kD carboxy-terminal heparin-binding domains of fibronectin was shown to promote the adhesion and spreading of vascular endothelial cells in vitro.	Heparin	75-82	fibronectin 1	Homo sapiens	102-113
8864964-12	1996	Finally, VLDL from HuCIITg and MoCIIITg mice showed decreased binding to heparin-Sepharose.	Heparin	73-80	CD320 antigen	Mus musculus	9-13
8864947-11	1996	These data may provide evidence for a functionally important heparin binding site around amino acid residue 212 of the apoE molecule in vivo.	Heparin	61-68	apolipoprotein E	Homo sapiens	119-123
8865534-10	1996	The concentration of TFPI was significantly increased following the incubation with thrombin and heparin, including low molecular weight heparin, in a dose- and time-dependent manner.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	84-92
8751615-8	1996	The addition of 50 units/ml heparin to VEGF significantly increased HAEC proliferation to greater than FG with VEGF alone at day 1.	Heparin	28-35	vascular endothelial growth factor A	Homo sapiens	39-43
8751615-8	1996	The addition of 50 units/ml heparin to VEGF significantly increased HAEC proliferation to greater than FG with VEGF alone at day 1.	Heparin	28-35	vascular endothelial growth factor A	Homo sapiens	111-115
8751516-5	1996	This study evaluated the effect of a heparin-coated cardiopulmonary bypass system (Duraflo II, Baxter Bentley Healthcare Systems, Irvine, Calif.) on thrombin formation, platelet stimulation, and leukocyte activation in patients undergoing reoperative coronary artery bypass grafting or valve operation.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	149-157
8751516-12	1996	In both circuits, thrombin values increased markedly 30 minutes into cardiopulmonary bypass compared with baseline values (p &lt; 0.001) (heparin-coated, 7 +/- 5 to 96 +/- 115 ng/ml; noncoated, 10 +/- 9 to 115 +/- 125 ng/ml).	Heparin	138-145	coagulation factor II, thrombin	Homo sapiens	18-26
8865534-13	1996	It is possible that thrombin-induced enhancement of TFPI synthesis may be caused by the autoregulatory system of blood coagulation and that with heparin it may represent another anticoagulatory effect of heparin.	Heparin	204-211	coagulation factor II, thrombin	Homo sapiens	20-28
8695787-0	1996	Presence of autoantibodies to interleukin-8 or neutrophil-activating peptide-2 in patients with heparin-associated thrombocytopenia.	Heparin	96-103	C-X-C motif chemokine ligand 8	Homo sapiens	30-43
8695787-5	1996	Five of these nine patients with anti-IL-8 or anti-NAP-2 developed thrombosis during heparin treatment, which is not statistically different from the patients with H-PF4 antibodies.	Heparin	85-92	C-X-C motif chemokine ligand 8	Homo sapiens	38-42
8663206-0	1996	Heparin decreases the blood clearance of interferon-gamma and increases its activity by limiting the processing of its carboxyl-terminal sequence.	Heparin	0-7	interferon gamma	Homo sapiens	41-57
8752940-2	1996	In this study, dextran sulfate, a synthetic heparin analogue, was shown to selectively inhibit IFN-gamma-induced surface expression of HLA-DR molecules by human umbilical cord vascular endothelial cells, but not other cytokine-induced molecules such as ELAM-1 or ICAM-1.	Heparin	44-51	interferon gamma	Homo sapiens	95-104
8663289-9	1996	This was documented by demonstrating incorporation of [3H]ethanolamine into anti-hepatic lipase immunoprecipitable material; in addition, hepatic lipase was released from the cells by phosphatidylinositol-specific phospholipase C but not by heparin.	Heparin	241-248	lipase C, hepatic type	Rattus norvegicus	138-152
8663206-1	1996	Interferon-gamma (IFN-gamma) binds with high affinity to heparan sulfate and heparin molecules through its carboxyl-terminal domain.	Heparin	77-84	interferon gamma	Homo sapiens	0-16
8663206-1	1996	Interferon-gamma (IFN-gamma) binds with high affinity to heparan sulfate and heparin molecules through its carboxyl-terminal domain.	Heparin	77-84	interferon gamma	Homo sapiens	18-27
8663206-4	1996	When bound to heparin, the plasma clearance of IFN-gamma is decreased greatly (t1/2 = 99 min), and the area under the curve obtained with IFN-gamma alone represented only 15% of that obtained with injected IFN-gamma bound to heparin.	Heparin	14-21	interferon gamma	Homo sapiens	47-56
8663206-4	1996	When bound to heparin, the plasma clearance of IFN-gamma is decreased greatly (t1/2 = 99 min), and the area under the curve obtained with IFN-gamma alone represented only 15% of that obtained with injected IFN-gamma bound to heparin.	Heparin	14-21	interferon gamma	Homo sapiens	138-147
8663206-4	1996	When bound to heparin, the plasma clearance of IFN-gamma is decreased greatly (t1/2 = 99 min), and the area under the curve obtained with IFN-gamma alone represented only 15% of that obtained with injected IFN-gamma bound to heparin.	Heparin	14-21	interferon gamma	Homo sapiens	138-147
8663206-4	1996	When bound to heparin, the plasma clearance of IFN-gamma is decreased greatly (t1/2 = 99 min), and the area under the curve obtained with IFN-gamma alone represented only 15% of that obtained with injected IFN-gamma bound to heparin.	Heparin	225-232	interferon gamma	Homo sapiens	47-56
8663206-5	1996	Furthermore, the binding of heparin to IFN-gamma limits the extent of its carboxyl-terminal domain degradation to less than 10 amino acids.	Heparin	28-35	interferon gamma	Homo sapiens	39-48
8663206-7	1996	These data demonstrate that the blood clearance of the cytokine is a non-receptor-mediated process and that in vivo the local concentration of heparan sulfate/heparin-like molecules regulates IFN-gamma activity by a unique mechanism involving a controlled processing of its carboxyl-terminal sequence.	Heparin	159-166	interferon gamma	Homo sapiens	192-201
8874867-7	1996	However, reteplase required five times more heparin for maximal stimulation than alteplase.	Heparin	44-51	plasminogen activator, tissue type	Homo sapiens	9-18
8694786-4	1996	In the first step, the high affinity of EC SOD for heparin is utilized to obtain a fraction in which EC SOD constitutes roughly 13% of the total protein compared with only 0.3% of that of the starting material.	Heparin	51-58	superoxide dismutase 3	Homo sapiens	40-46
8694786-4	1996	In the first step, the high affinity of EC SOD for heparin is utilized to obtain a fraction in which EC SOD constitutes roughly 13% of the total protein compared with only 0.3% of that of the starting material.	Heparin	51-58	superoxide dismutase 3	Homo sapiens	101-107
8874861-0	1996	A proposed model to monitor heparin therapy using the concentrated thrombin time which allows standardisation of reagents and improved estimation of heparin concentrations.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	67-75
8874861-0	1996	A proposed model to monitor heparin therapy using the concentrated thrombin time which allows standardisation of reagents and improved estimation of heparin concentrations.	Heparin	149-156	coagulation factor II, thrombin	Homo sapiens	67-75
8758154-5	1996	Interleukin-1 beta was increased by heparin (p &lt; 0.05), whereas interleukin-1 receptor antagonist was increased by fentanyl (p &lt; 0.05).	Heparin	36-43	interleukin 1 beta	Homo sapiens	0-18
8758154-6	1996	Protamine blocked the heparin-induced increase in tumour necrosis factor alpha and interleukin-1 beta.	Heparin	22-29	interleukin 1 beta	Homo sapiens	83-101
8776565-0	1996	Synergistic action of heparin and serum on basic fibroblast growth factor-modulated DNA synthesis and mitochondrial activity of cultured bovine corneal endothelial cells.	Heparin	22-29	fibroblast growth factor 2	Bos taurus	43-73
8776565-6	1996	Supplementation of bFGF with heparin resulted in an additional response for the mitochondrial activity, but not for the DNA synthesis.	Heparin	29-36	fibroblast growth factor 2	Bos taurus	19-23
8776565-8	1996	These processes were further enhanced by the addition of heparin to bFGF.	Heparin	57-64	fibroblast growth factor 2	Bos taurus	68-72
8891437-7	1996	Heparin bound to [125I]-IFN-gamma was also used to block the heparan sulfate binding site of the cytokine.	Heparin	0-7	interferon gamma	Homo sapiens	24-33
8891437-8	1996	In this case, blood clearance and tissue accumulation in the liver and spleen were strongly inhibited, while in the kidney the distribution, but not the accumulation, of [125I]-IFN-gamma was affected by the presence of heparin.	Heparin	219-226	interferon gamma	Homo sapiens	177-186
8874867-0	1996	Interaction of reteplase with heparin.	Heparin	30-37	plasminogen activator, tissue type	Homo sapiens	15-24
8874867-4	1996	Reteplase and alteplase bound completely to a heparin-agarose column and eluted respectively at 0.39 M and 0.60 M in a NaCl gradient.	Heparin	46-53	plasminogen activator, tissue type	Homo sapiens	0-9
8874867-6	1996	Plasminogen activation by the two-chain derivatives of reteplase and alteplase in a purified system at low ionic strength were stimulated by heparin up to 13- and 22-fold, respectively.	Heparin	141-148	plasminogen activator, tissue type	Homo sapiens	55-64
8874867-8	1996	In addition, the heparin stimulation of reteplase was more salt sensitive than that of alteplase.	Heparin	17-24	plasminogen activator, tissue type	Homo sapiens	40-49
8874867-9	1996	In conclusion, both heparin binding and heparin stimulation experiments showed that heparin interacts with reteplase, but the interaction is weaker than with alteplase.	Heparin	20-27	plasminogen activator, tissue type	Homo sapiens	107-116
8874867-9	1996	In conclusion, both heparin binding and heparin stimulation experiments showed that heparin interacts with reteplase, but the interaction is weaker than with alteplase.	Heparin	40-47	plasminogen activator, tissue type	Homo sapiens	107-116
8874867-9	1996	In conclusion, both heparin binding and heparin stimulation experiments showed that heparin interacts with reteplase, but the interaction is weaker than with alteplase.	Heparin	40-47	plasminogen activator, tissue type	Homo sapiens	107-116
8806053-3	1996	RGTA11 was deemed efficient to protect the heparin-binding growth factors FGF2 against trypsin digestion.	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	74-78
8925311-7	1996	Intravenous administration of heparin is unambiguously justified only in thrombolysis with t-PA.	Heparin	30-37	plasminogen activator, tissue type	Homo sapiens	91-95
8832397-10	1996	Since heparin treatment of cell membrane fractions from cerebellum and tectum resulted in the release of the protein, we suggest that one or several heparan-sulfate proteoglycans are involved in the binding of anosmin-1 to the membranes in vivo.	Heparin	6-13	anosmin 1	Homo sapiens	210-219
8864862-1	1996	Molecular genetic studies of extracellular-superoxide dismutase (EC-SOD) have shown that individuals with high serum EC-SOD content have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of this enzyme [Sandstrom, J. et al.	Heparin	231-238	superoxide dismutase 3	Homo sapiens	29-63
9070372-3	1996	The potentiating activity of heparin upon FGF-1 has shown to be dependent on the oligosaccharide size, degree of sulfation and carboxylation.	Heparin	29-36	fibroblast growth factor 1	Homo sapiens	42-47
8864862-1	1996	Molecular genetic studies of extracellular-superoxide dismutase (EC-SOD) have shown that individuals with high serum EC-SOD content have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of this enzyme [Sandstrom, J. et al.	Heparin	231-238	superoxide dismutase 3	Homo sapiens	65-71
8864862-1	1996	Molecular genetic studies of extracellular-superoxide dismutase (EC-SOD) have shown that individuals with high serum EC-SOD content have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of this enzyme [Sandstrom, J. et al.	Heparin	231-238	superoxide dismutase 3	Homo sapiens	117-123
8864862-8	1996	Serum EC-SOD in healthy individuals without the above mutation is heterogeneous with regard to heparin affinity and consists of five fractions, forms (I) to (V), of which (IV) and (V) are the main fractions with high affinity for heparin [Adachi, T. et al.	Heparin	95-102	superoxide dismutase 3	Homo sapiens	6-12
8864862-8	1996	Serum EC-SOD in healthy individuals without the above mutation is heterogeneous with regard to heparin affinity and consists of five fractions, forms (I) to (V), of which (IV) and (V) are the main fractions with high affinity for heparin [Adachi, T. et al.	Heparin	230-237	superoxide dismutase 3	Homo sapiens	6-12
8864862-11	1996	On the other hand, serum EC-SOD in both healthy individuals and hemodialysis patients with the R213G mutation consisted mainly of the high heparin-affinity type.	Heparin	139-146	superoxide dismutase 3	Homo sapiens	25-31
8864862-13	1996	The affinity of normal EC-SOD (n-EC-SOD) for heparin decreased by the treatment with trypsin, accompanied by a reduction in the molecular mass.	Heparin	45-52	superoxide dismutase 3	Homo sapiens	23-29
8836919-4	1996	We have shown recently that IFN-gamma-mediated effects can be blocked by heparin and that this inhibitory effect can be abrogated by the addition of protamine.	Heparin	73-80	interferon gamma	Homo sapiens	28-37
8864862-13	1996	The affinity of normal EC-SOD (n-EC-SOD) for heparin decreased by the treatment with trypsin, accompanied by a reduction in the molecular mass.	Heparin	45-52	superoxide dismutase 3	Homo sapiens	33-39
8864862-14	1996	The IC50 of trypsin for the heparin affinity of R213G mutant EC-SOD (m-EC-SOD) was 0.15 microgram/ml, fivefold that for n-EC-SOD.	Heparin	28-35	superoxide dismutase 3	Homo sapiens	61-67
8864862-14	1996	The IC50 of trypsin for the heparin affinity of R213G mutant EC-SOD (m-EC-SOD) was 0.15 microgram/ml, fivefold that for n-EC-SOD.	Heparin	28-35	superoxide dismutase 3	Homo sapiens	71-77
8864862-14	1996	The IC50 of trypsin for the heparin affinity of R213G mutant EC-SOD (m-EC-SOD) was 0.15 microgram/ml, fivefold that for n-EC-SOD.	Heparin	28-35	superoxide dismutase 3	Homo sapiens	71-77
8864862-15	1996	Heparin affinity of n-EC-SOD was again more susceptible to neutrophils than that of m-EC-SOD.	Heparin	0-7	superoxide dismutase 3	Homo sapiens	22-28
8864862-16	1996	These results suggested that m-EC-SOD is more resistant to trypsin and neutrophil-release trypsin-like proteinases than n-EC-SOD, which causes the heparin affinity of serum EC-SOD to differ in individuals with and without the R213G mutation.	Heparin	147-154	superoxide dismutase 3	Homo sapiens	31-37
8864862-16	1996	These results suggested that m-EC-SOD is more resistant to trypsin and neutrophil-release trypsin-like proteinases than n-EC-SOD, which causes the heparin affinity of serum EC-SOD to differ in individuals with and without the R213G mutation.	Heparin	147-154	superoxide dismutase 3	Homo sapiens	122-128
8864862-16	1996	These results suggested that m-EC-SOD is more resistant to trypsin and neutrophil-release trypsin-like proteinases than n-EC-SOD, which causes the heparin affinity of serum EC-SOD to differ in individuals with and without the R213G mutation.	Heparin	147-154	superoxide dismutase 3	Homo sapiens	122-128
8836919-5	1996	In this report, we show that the antagonistic effect of protamine on heparin-mediated inhibition of IFN-gamma activity is mainly due to the capacity of protamine to enhance IFN-gamma activity.	Heparin	69-76	interferon gamma	Homo sapiens	100-109
8836919-5	1996	In this report, we show that the antagonistic effect of protamine on heparin-mediated inhibition of IFN-gamma activity is mainly due to the capacity of protamine to enhance IFN-gamma activity.	Heparin	69-76	interferon gamma	Homo sapiens	173-182
8663002-0	1996	Identification of a novel binding site to the integrin alphaIIbbeta3 located in the C-terminal heparin-binding domain of human plasma fibronectin.	Heparin	95-102	fibronectin 1	Homo sapiens	134-145
8663002-2	1996	A recent study has indicated that a 29-kDa dispase-digestive fragment from the C-terminal heparin-binding domain of human plasma fibronectin (lacking RGD sequence) inhibits binding of fibronectin to thrombin-stimulated platelets and ADP-induced aggregation (Tanabe, J. , Fujita, H., Iwamatsu, A., Mohri, H., and Ohkubo, T.(1993) J. Biol.	Heparin	90-97	fibronectin 1	Homo sapiens	129-140
8663002-2	1996	A recent study has indicated that a 29-kDa dispase-digestive fragment from the C-terminal heparin-binding domain of human plasma fibronectin (lacking RGD sequence) inhibits binding of fibronectin to thrombin-stimulated platelets and ADP-induced aggregation (Tanabe, J. , Fujita, H., Iwamatsu, A., Mohri, H., and Ohkubo, T.(1993) J. Biol.	Heparin	90-97	fibronectin 1	Homo sapiens	184-195
8663002-2	1996	A recent study has indicated that a 29-kDa dispase-digestive fragment from the C-terminal heparin-binding domain of human plasma fibronectin (lacking RGD sequence) inhibits binding of fibronectin to thrombin-stimulated platelets and ADP-induced aggregation (Tanabe, J. , Fujita, H., Iwamatsu, A., Mohri, H., and Ohkubo, T.(1993) J. Biol.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	199-207
8663002-7	1996	These results indicate that a novel binding site in the C-terminal heparin-binding region of fibronectin is localized within the residues from Ala1704 to Glu1718.	Heparin	67-74	fibronectin 1	Homo sapiens	93-104
8682648-5	1996	Heparin-releasable binding of 125I-labelled lipoprotein lipase was lower to either of the mutant cells than to the wild-type cells.	Heparin	0-7	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	44-62
8664327-7	1996	Recombinant apo E2 Fukuoka showed the same heparin binding ability than recombinant apo E3.	Heparin	43-50	apolipoprotein E	Homo sapiens	12-18
8660375-7	1996	In addition, a synthetic peptide corresponding to the heparin-binding domain of HB-EGF inhibits the DNA synthesis of RGM1 cells in serum-free medium in a dose-dependent manner.	Heparin	54-61	heparin-binding EGF-like growth factor	Rattus norvegicus	80-86
8794518-7	1996	In conclusion, in every third patient thrombin generation occurs after successful elective PTCA, implying a need for a tighter control than heparin provides.	Heparin	140-147	coagulation factor II, thrombin	Homo sapiens	38-46
8839997-3	1996	In patients treated with unfractionated heparin for recent deep vein thrombosis (n = 47), plasma levels of aPTT, PT and thrombin clotting time (TCT) returned to the normal range in 100%, 97% and 91% after treatment with heparinase, respectively.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	120-128
8718936-0	1996	Heparin-like functionalized polymer surfaces: discrimination between catalytic and adsorption processes during the course of thrombin inhibition.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	125-133
8666820-9	1996	They were, however, at least partially charge mediated, since heparin abolished the effects of MBP on IL-1-stimulated cells, and the surrogate cationic molecule poly-L-arginine mimicked the stimulatory effects of MBP on fibroblast IL-6-type cytokine elaboration.	Heparin	62-69	interleukin 1 beta	Homo sapiens	102-106
8795010-9	1996	The recombinant Nef-protein obtained by one-step heparin-based purification shares immunological properties with native Nef and should prove useful for further studies of Nef function and immunogenicity.	Heparin	49-56	S100 calcium binding protein B	Homo sapiens	16-19
8827835-2	1996	FGF-1 or FGF-2 in the presence of heparin resulted in a significantly greater cell viability for exudate cells at 24 hours of culture relative to heparin alone or medium controls.	Heparin	34-41	fibroblast growth factor 1	Mus musculus	0-5
8827835-2	1996	FGF-1 or FGF-2 in the presence of heparin resulted in a significantly greater cell viability for exudate cells at 24 hours of culture relative to heparin alone or medium controls.	Heparin	146-153	fibroblast growth factor 1	Mus musculus	0-5
8827835-3	1996	Cultures supplemented with FGF-1 or FGF-2 plus heparin showed a slight increase in tritiated[3H] thymidine uptake over heparin or medium alone.	Heparin	119-126	fibroblast growth factor 1	Mus musculus	27-32
8662638-1	1996	Inositol 1,3,4-trisphosphate 5/6-kinase was purified 12,900-fold from calf brain using chromatography on heparin-agarose and affinity elution with inositol hexakisphosphate.	Heparin	105-112	inositol-tetrakisphosphate 1-kinase	Bos taurus	0-39
8636395-9	1996	Infusion of heparin to the in vitro hepatic perfusion system increased the activity of hepatic lipase in the effluent in all groups of rat except in CRF animals.	Heparin	12-19	lipase C, hepatic type	Rattus norvegicus	87-101
8635609-4	1996	In contrast, TSP-1 was extensively proteolyzed on aggregated platelets releasing in the milieu a fragment with Mr approximately 28 000, corresponding to the amino-terminal heparin-binding domain (HBD).	Heparin	172-179	thrombospondin 1	Homo sapiens	13-18
8791279-8	1996	Now, the presence of dithiothreitol (5 mM) or heparin (20 ug/ml) caused a remarkable elevation of the plasma membrane (Ca(2+)-Mg2+)-ATPase activity in the liver obtained from CCl4-administered rats.	Heparin	46-53	C-C motif chemokine ligand 4	Rattus norvegicus	175-179
29206581-1	1996	Preview Heparin has been in use for more than 40 years and is still an important agent for inhibiting plasma- and surface-bound thrombin.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	128-136
9594175-6	1996	The early administration of heparin and aprotinin after the supplement of fibrinogen has shown a great potential benifit to stop the cascade of hypercoagulation and hyperplasminogenemia by enhancing the level of AT-III and fibrinogen in plasma.	Heparin	28-35	fibrinogen beta chain	Homo sapiens	74-84
9594175-6	1996	The early administration of heparin and aprotinin after the supplement of fibrinogen has shown a great potential benifit to stop the cascade of hypercoagulation and hyperplasminogenemia by enhancing the level of AT-III and fibrinogen in plasma.	Heparin	28-35	fibrinogen beta chain	Homo sapiens	223-233
8733958-0	1996	Platelet deposition and fibrinogen binding on surfaces coated with heparin or friction-reducing polymers.	Heparin	67-74	fibrinogen beta chain	Homo sapiens	24-34
8718936-3	1996	In addition to their capacity to adsorb thrombin, such surfaces were shown to be able to catalyse its inhibition by antithrombin III (AT), i.e. they are endowed with heparin-like activity.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	40-48
9033809-4	1996	PP1 activity was inhibited by protamine, heparin, okadaic acid (IC50 50 nM) and mammalian inhibitor-1 (IC50 2 nM).	Heparin	41-48	inorganic pyrophosphatase 1	Homo sapiens	0-3
8613463-2	1996	Acidic fibroblast growth factor (aFGF) in the presence of heparin has effects opposite to IL-1 on cultured human umbilical vein endothelial cells (HUVEC); therefore, we have investigated the modulation of IL-1-induced effects by the c combination of aFGF and heparin (aFGF/heparin).	Heparin	58-65	fibroblast growth factor 1	Homo sapiens	0-31
8738586-9	1996	A laboratory artefact, i.e. the absence of Ca2+ in the anti-factor Xa tests, makes that heparin mixtures that lack extra large heparin molecules show a (spuriously) high ratio of anti-factor Xa activity over anti-thrombin activity.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	213-221
8613463-2	1996	Acidic fibroblast growth factor (aFGF) in the presence of heparin has effects opposite to IL-1 on cultured human umbilical vein endothelial cells (HUVEC); therefore, we have investigated the modulation of IL-1-induced effects by the c combination of aFGF and heparin (aFGF/heparin).	Heparin	58-65	fibroblast growth factor 1	Homo sapiens	33-37
8636243-16	1996	In BaF3 cells transfected with a plasmid encoding human c-Met, heparin and NK1 synergized to stimulate DNA synthesis and cell proliferation.	Heparin	63-70	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	56-61
8630041-2	1996	The purified molecule was identified as an FGF-1 on the basis of its biological activities, its affinity for heparin and its N-terminal amino-acid sequence.	Heparin	109-116	fibroblast growth factor 1	Mus musculus	43-48
9377378-3	1996	A possibility is shown of forecasting of the heparin therapy efficacy in the above patient populations in respect of a decline in the urinary excretion of products of the fibrinogen/fibrin cleavage more than two-fold a week after the start of treatment.	Heparin	45-52	fibrinogen beta chain	Homo sapiens	171-181
8633059-2	1996	The PLD enzyme associated with particulate fractions was solubilized by deoxycholate and partially purified by chromatography on a heparin-Sepharose column.	Heparin	131-138	glycosylphosphatidylinositol specific phospholipase D1	Homo sapiens	4-7
8901081-1	1996	Keratinocyte growth factor (KGF) has limited stability in aqueous media, as it undergoes denaturation followed by aggregation at 37 degrees C. Heparin and anionic polymers have been shown to increase the denaturation temperatures and extend the half-life of the monomeric, native form of KGF during storage.	Heparin	143-150	fibroblast growth factor 7	Homo sapiens	0-26
8603535-4	1996	In this study it is shown that the effects of interferon-gamma (IFN-gamma), but not of tumour necrosis factor-alpha (TNF-alpha), are inhibited by treatment with soluble heparin.	Heparin	169-176	interferon gamma	Homo sapiens	46-62
8603535-4	1996	In this study it is shown that the effects of interferon-gamma (IFN-gamma), but not of tumour necrosis factor-alpha (TNF-alpha), are inhibited by treatment with soluble heparin.	Heparin	169-176	interferon gamma	Homo sapiens	64-73
8603535-5	1996	Specifically, heparin was shown to inhibit the induction of class II MHC antigens and the up-regulation of intercellular adhesion molecule-1 (ICAM-1) produced by treatment of cultured human endothelial cells with IFN-gamma.	Heparin	14-21	interferon gamma	Homo sapiens	213-222
8603535-6	1996	Furthermore, it was shown that heparin blocked the enhanced adhesion of T lymphocytes to IFN-gamma-treated endothelial cells.	Heparin	31-38	interferon gamma	Homo sapiens	89-98
8603535-8	1996	These results may explain reported immunosuppressive properties of heparin, and are consistent with the model that heparin may compete with cell surface GAGs to bind IFN-gamma, thereby reducing effective biological activity.	Heparin	67-74	interferon gamma	Homo sapiens	166-175
8603535-8	1996	These results may explain reported immunosuppressive properties of heparin, and are consistent with the model that heparin may compete with cell surface GAGs to bind IFN-gamma, thereby reducing effective biological activity.	Heparin	115-122	interferon gamma	Homo sapiens	166-175
8743558-7	1996	The cell adhesion of C279 was inhibited by GRGDSP peptide but that of the fusion protein with the heparin-binding domain of fibronectin was not completely inhibited by the peptide.	Heparin	98-105	fibronectin 1	Homo sapiens	124-135
8847350-0	1996	Mechanism of thrombin inactivation by immobilized heparin.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	13-21
8847350-1	1996	The ability of heparin to interact with plasma proteins, in particular antithrombin III (ATIII) and thrombin, is its primary mechanism as an anticoagulant drug.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	75-83
8847350-4	1996	In this report, insights into binding interaction of direct versus polyethylene oxide space immobilized heparin with ATIII, thrombin, and the generation of the thrombin-antithrombin complex will be presented.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	124-132
8847350-4	1996	In this report, insights into binding interaction of direct versus polyethylene oxide space immobilized heparin with ATIII, thrombin, and the generation of the thrombin-antithrombin complex will be presented.	Heparin	104-111	coagulation factor II, thrombin	Homo sapiens	160-168
8623729-11	1996	Thus, this trial demonstrated trends favoring front-loaded t-PA with weight-adjusted heparin over APSAC without heparin in the treatment of AMI.	Heparin	85-92	plasminogen activator, tissue type	Homo sapiens	59-63
8860711-2	1996	In collaboration with B. Braun Melsungen AG, Germany, we were able to develop the heparin-mediated extracorporeal low-density lipoprotein (LDL) fibrinogen precipitation (H.E.L.P.)	Heparin	82-89	fibrinogen beta chain	Homo sapiens	144-154
8741221-0	1996	Retinoic acid-induced heparin binding (RIHB, chicken midkine) factor expression by cultured chondrocytes is strongly enhanced by ascorbic acid.	Heparin	22-29	midkine (neurite growth-promoting factor 2)	Gallus gallus	39-43
8609172-7	1996	Exogenous heparin enhanced the specific binding and affinity cross-linking of 125I-bFGF to FGFR1 in receptor transfectants that were not cotransfected with proteoglycan, but had no effect on this binding and decreased the yield of bFGFR cross-links in cells that were cotransfected with proteoglycan.	Heparin	10-17	fibroblast growth factor 2	Homo sapiens	83-87
8609172-7	1996	Exogenous heparin enhanced the specific binding and affinity cross-linking of 125I-bFGF to FGFR1 in receptor transfectants that were not cotransfected with proteoglycan, but had no effect on this binding and decreased the yield of bFGFR cross-links in cells that were cotransfected with proteoglycan.	Heparin	10-17	fibroblast growth factor receptor 1	Homo sapiens	91-96
8609172-7	1996	Exogenous heparin enhanced the specific binding and affinity cross-linking of 125I-bFGF to FGFR1 in receptor transfectants that were not cotransfected with proteoglycan, but had no effect on this binding and decreased the yield of bFGFR cross-links in cells that were cotransfected with proteoglycan.	Heparin	10-17	fibroblast growth factor receptor 1	Homo sapiens	231-236
8901081-1	1996	Keratinocyte growth factor (KGF) has limited stability in aqueous media, as it undergoes denaturation followed by aggregation at 37 degrees C. Heparin and anionic polymers have been shown to increase the denaturation temperatures and extend the half-life of the monomeric, native form of KGF during storage.	Heparin	143-150	fibroblast growth factor 7	Homo sapiens	28-31
8901081-1	1996	Keratinocyte growth factor (KGF) has limited stability in aqueous media, as it undergoes denaturation followed by aggregation at 37 degrees C. Heparin and anionic polymers have been shown to increase the denaturation temperatures and extend the half-life of the monomeric, native form of KGF during storage.	Heparin	143-150	fibroblast growth factor 7	Homo sapiens	288-291
8743172-5	1996	Thus, when heparin is given in conjunction with plasminogen activators only modest increases in FPA levels are found, and our data suggest that this is due, at least in part, to the activity of enzymes other than thrombin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	213-221
8783184-0	1996	Stimulation of collagenase (matrix metalloproteinase-1) synthesis in histiotypic epithelial cell culture by heparin is enhanced by keratinocyte growth factor.	Heparin	108-115	fibroblast growth factor 7	Homo sapiens	131-157
8783184-4	1996	The increase in collagenase secretion by heparin was further enhanced by the addition of KGF.	Heparin	41-48	fibroblast growth factor 7	Homo sapiens	89-92
8668917-0	1996	Heparin in clinical doses "primes" granulocytes to subsequent activation as measured by myeloperoxidase release.	Heparin	0-7	myeloperoxidase	Homo sapiens	88-103
8901022-6	1996	An IP3 receptor antagonist, heparin, reduced both the substance P-induced O2- production and the transient increase in [Ca2+]i without any significant effects on the sustained increase in [Ca2+]i.	Heparin	28-35	tachykinin precursor 1	Homo sapiens	54-65
8631822-4	1996	VEGF121 is a soluble mitogen that does not bind heparin; the longer forms of VEGF bind heparin with progressively higher affinity.	Heparin	87-94	vascular endothelial growth factor A	Homo sapiens	0-4
8631822-9	1996	Plasmin yields two fragments of VEGF as indicated by reverse phase high performance liquid chromatography and SDS-polyacrylamide gel electrophoresis: an amino-terminal homodimeric protein containing receptor binding determinants and a carboxyl-terminal polypeptide which bound heparin.	Heparin	277-284	vascular endothelial growth factor A	Homo sapiens	32-36
8743198-12	1996	To test whether heparin"s effect could be due to suppression of thrombin activity, the effects of the antithrombin hirudin on force development were measured.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	64-72
8743198-14	1996	Thus, heparin"s reduction of platelet force development may be due, at least in part, to suppression of thrombin activity.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	104-112
8619608-0	1996	Suppression of endothelin-1 production in cultured human umbilical vein endothelial cells by heparin fractions separated by strong anion exchange chromatography.	Heparin	93-100	endothelin 1	Homo sapiens	15-27
8619608-1	1996	Heparin has been shown to lower the production/secretion of the vasoconstrictive peptide endothelin-1.	Heparin	0-7	endothelin 1	Homo sapiens	89-101
8619608-2	1996	Endothelin-1 production is stimulated by thrombin, and it has been proposed that heparin binds to the anion-binding exosite of thrombin, preventing it from stimulating endothelin-1 production.	Heparin	81-88	endothelin 1	Homo sapiens	0-12
8619608-2	1996	Endothelin-1 production is stimulated by thrombin, and it has been proposed that heparin binds to the anion-binding exosite of thrombin, preventing it from stimulating endothelin-1 production.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	127-135
8619608-2	1996	Endothelin-1 production is stimulated by thrombin, and it has been proposed that heparin binds to the anion-binding exosite of thrombin, preventing it from stimulating endothelin-1 production.	Heparin	81-88	endothelin 1	Homo sapiens	168-180
8665923-2	1996	The OZF protein produced in Escherichia coli binds zinc ions, DNA and heparin.	Heparin	70-77	zinc finger protein 146	Homo sapiens	4-7
8619608-9	1996	These data show that charge interactions between heparin and thrombin may be important in regulating the production of endothelin-1 and in regulating other thrombin-dependent functions.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	61-69
8619608-9	1996	These data show that charge interactions between heparin and thrombin may be important in regulating the production of endothelin-1 and in regulating other thrombin-dependent functions.	Heparin	49-56	endothelin 1	Homo sapiens	119-131
8619608-9	1996	These data show that charge interactions between heparin and thrombin may be important in regulating the production of endothelin-1 and in regulating other thrombin-dependent functions.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	156-164
8721461-0	1996	Heparin-coated circuits reduce the formation of TNF alpha during cardiopulmonary bypass.	Heparin	0-7	tumor necrosis factor	Homo sapiens	48-57
8626396-0	1996	Substitution of specific amino acids in insulin-like growth factor (IGF) binding protein 5 alters heparin binding and its change in affinity for IGF-I response to heparin.	Heparin	98-105	insulin like growth factor binding protein 5	Homo sapiens	40-90
8626396-0	1996	Substitution of specific amino acids in insulin-like growth factor (IGF) binding protein 5 alters heparin binding and its change in affinity for IGF-I response to heparin.	Heparin	163-170	insulin like growth factor binding protein 5	Homo sapiens	40-90
8626396-0	1996	Substitution of specific amino acids in insulin-like growth factor (IGF) binding protein 5 alters heparin binding and its change in affinity for IGF-I response to heparin.	Heparin	163-170	insulin like growth factor 1	Homo sapiens	145-150
8626396-1	1996	Heparin binding to insulin-like growth factor (IGF)-binding protein 5 (IGFBP-5) leads to a 17-fold decrease in its affinity for IGF-I, and a region that contains several basic amino acids (Arg201-Arg218) may be involved in this affinity shift.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	19-69
8626396-1	1996	Heparin binding to insulin-like growth factor (IGF)-binding protein 5 (IGFBP-5) leads to a 17-fold decrease in its affinity for IGF-I, and a region that contains several basic amino acids (Arg201-Arg218) may be involved in this affinity shift.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	71-78
8626396-1	1996	Heparin binding to insulin-like growth factor (IGF)-binding protein 5 (IGFBP-5) leads to a 17-fold decrease in its affinity for IGF-I, and a region that contains several basic amino acids (Arg201-Arg218) may be involved in this affinity shift.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	128-133
8602827-2	1996	We examined inhibitory activities of various heparin derivatives toward interaction of midkine with neurons and elucidated the structural requirements of the heparin-like domain necessary for the interaction.	Heparin	45-52	midkine	Homo sapiens	87-94
8602827-2	1996	We examined inhibitory activities of various heparin derivatives toward interaction of midkine with neurons and elucidated the structural requirements of the heparin-like domain necessary for the interaction.	Heparin	158-165	midkine	Homo sapiens	87-94
8626396-2	1996	In the present study, mutagenesis was used to analyze the effect of substitutions for basic amino acids in the Arg201-Arg218 region of IGFBP-5 on heparin-binding and the heparin-induced affinity shift.	Heparin	146-153	insulin like growth factor binding protein 5	Homo sapiens	135-142
8626396-2	1996	In the present study, mutagenesis was used to analyze the effect of substitutions for basic amino acids in the Arg201-Arg218 region of IGFBP-5 on heparin-binding and the heparin-induced affinity shift.	Heparin	170-177	insulin like growth factor binding protein 5	Homo sapiens	135-142
8626396-5	1996	When 10 microg/ml of heparin was added, the Ka of native IGFBP-5 decreased 17-fold, and the Ka of the K134A/R136A mutant decreased 16-fold.	Heparin	21-28	insulin like growth factor binding protein 5	Homo sapiens	57-64
8626396-8	1996	When a mutant containing that single substitution was tested, heparin caused only a 2.5-fold reduction in IGF-I affinity.	Heparin	62-69	insulin like growth factor 1	Homo sapiens	106-111
8626396-9	1996	Affinity cross-linking studies showed that heparin was equipotent in inhibiting the formation of 125I-IGF-I-K134A/Rl36A mutant complexes compared to native IGFBP-5.	Heparin	43-50	insulin like growth factor 1	Homo sapiens	102-107
8626396-9	1996	Affinity cross-linking studies showed that heparin was equipotent in inhibiting the formation of 125I-IGF-I-K134A/Rl36A mutant complexes compared to native IGFBP-5.	Heparin	43-50	insulin like growth factor binding protein 5	Homo sapiens	156-163
8621443-11	1996	The GST-VEGF-exon 7 fusion protein bound to heparin-Sepharose with a similar affinity as VEGF165 and inhibited the binding of 125I-VEGF165 to 231 cells.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	8-12
8721461-3	1996	Although previous studies have shown that heparin coating of the extracorporeal circuits reduces complement and granulocyte activation, and the inflammatory response, the possible effect of heparin coating on TNF alpha formation and the inflammatory response has not been fully investigated.	Heparin	190-197	tumor necrosis factor	Homo sapiens	209-218
8721461-15	1996	CONCLUSION: From these observations, we conclude that heparin coating of the extracorporeal circuits reduces the TNF alpha formation during CPB, which may reduce neutrophil activation.	Heparin	54-61	tumor necrosis factor	Homo sapiens	113-122
8857192-9	1996	As the TAT complex dissociates from immobilized heparin, this "recovered" heparin is available for subsequent binding of more ATIII and thrombin.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	136-144
8615699-0	1996	Inhibition of human mast cell chymase by secretory leukocyte proteinase inhibitor: enhancement of the interaction by heparin.	Heparin	117-124	chymase 1	Homo sapiens	30-37
8615699-6	1996	Addition of heparin to the low-salt reaction decreased the Ki approximately 10-fold to a value of 3 x 10(-9) M, making SLPI a more effective inhibitor of human chymase.	Heparin	12-19	secretory leukocyte peptidase inhibitor	Homo sapiens	119-123
8615699-6	1996	Addition of heparin to the low-salt reaction decreased the Ki approximately 10-fold to a value of 3 x 10(-9) M, making SLPI a more effective inhibitor of human chymase.	Heparin	12-19	chymase 1	Homo sapiens	160-167
8615699-9	1996	The enhanced interaction in the presence of heparin supports the importance of this glycosaminoglycan to the inhibitory function of SLPI.	Heparin	44-51	secretory leukocyte peptidase inhibitor	Homo sapiens	132-136
8670081-8	1996	Both the native and binary complexed forms of anti-thrombin showed a greatly increased proteolytic sensitivity in the presence of heparin, indicating that heparin either induces a conformational change in the local structure of the helical reactive loop or facilitates the approximation of enzyme and inhibitor.	Heparin	130-137	coagulation factor II, thrombin	Homo sapiens	51-59
8670081-8	1996	Both the native and binary complexed forms of anti-thrombin showed a greatly increased proteolytic sensitivity in the presence of heparin, indicating that heparin either induces a conformational change in the local structure of the helical reactive loop or facilitates the approximation of enzyme and inhibitor.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	51-59
8634431-4	1996	If factor Xa is preincubated with calcium ions and thrombin-activated platelets or factor Va and phospholipids to permit formation of prothrombinase before the addition of prothrombin and physiologic concentrations of TFPI (&lt; 8 nmol/L), minimal inhibition of thrombin generation occurs, even in the presence of heparin.	Heparin	314-321	coagulation factor II, thrombin	Homo sapiens	51-59
8857192-0	1996	Binding of antithrombin III and thrombin to immobilized heparin under flow conditions.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	15-23
8857192-3	1996	However, few studies have been performed to investigate the binding kinetics of spacer-immobilized heparin under flow (shear stress) with antithrombin III (ATIII) and thrombin.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	142-150
8857192-9	1996	As the TAT complex dissociates from immobilized heparin, this "recovered" heparin is available for subsequent binding of more ATIII and thrombin.	Heparin	74-81	coagulation factor II, thrombin	Homo sapiens	136-144
8617759-1	1996	The growth promoting activity of the subendothelial extracellular matrix (ECM) is attributed to sequestration of basic fibroblast growth factor (bFGF) by heparan sulfate proteoglycans and its regulated release by heparin-like molecules and heparan sulfate (HS) degrading enzymes.	Heparin	213-220	fibroblast growth factor 2	Homo sapiens	145-149
8598091-0	1996	Heparins designed to specifically inhibit platelet interactions with von Willebrand factor.	Heparin	0-8	von Willebrand factor	Homo sapiens	69-90
8598091-2	1996	Previously, we demonstrated that heparin interfered with platelet/vWF hemostatic mechanisms by binding to vWF within the proteins"s domain responsible for binding the platelet vWF receptor, glycoprotein Ib.	Heparin	33-40	von Willebrand factor	Homo sapiens	66-69
8598091-2	1996	Previously, we demonstrated that heparin interfered with platelet/vWF hemostatic mechanisms by binding to vWF within the proteins"s domain responsible for binding the platelet vWF receptor, glycoprotein Ib.	Heparin	33-40	von Willebrand factor	Homo sapiens	106-109
8598091-2	1996	Previously, we demonstrated that heparin interfered with platelet/vWF hemostatic mechanisms by binding to vWF within the proteins"s domain responsible for binding the platelet vWF receptor, glycoprotein Ib.	Heparin	33-40	von Willebrand factor	Homo sapiens	106-109
8598091-3	1996	The purpose of the present study was to develop and refine heparins with greater potency to inhibit platelet/vWF interactions.	Heparin	59-67	von Willebrand factor	Homo sapiens	109-112
8598091-4	1996	METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding.	Heparin	69-76	von Willebrand factor	Homo sapiens	95-98
8598091-4	1996	METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding.	Heparin	146-153	von Willebrand factor	Homo sapiens	95-98
8598091-4	1996	METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding.	Heparin	146-153	von Willebrand factor	Homo sapiens	221-224
8598091-4	1996	METHODS AND RESULTS: Immobilized synthetic peptides based on a known heparin-binding domain of vWF were used to yield novel fractions of standard heparin that demonstrated a sevenfold increase in their ability to inhibit vWF-dependent platelet agglutination and vWF/platelet binding.	Heparin	146-153	von Willebrand factor	Homo sapiens	221-224
8598091-5	1996	The high vWF affinity heparin showed enhanced anti-factor Xa activity but comparable activated partial thromboplastin time activity.	Heparin	22-29	von Willebrand factor	Homo sapiens	9-12
8598091-6	1996	Chemical modification of a standard heparin by periodate oxidation and borohydride reduction enhanced its ability to inhibit platelet/vWF interactions by threefold, while eliminating more than 90% of its activated partial thromboplastin time and anti-factor Xa activity.	Heparin	36-43	von Willebrand factor	Homo sapiens	134-137
8598091-8	1996	CONCLUSIONS: Subspecies of heparin can be developed with significantly enhanced potency to inhibit vWF/platelet interactions.	Heparin	27-34	von Willebrand factor	Homo sapiens	99-102
8598091-9	1996	The vWF-inhibiting property of heparin can be dissociated from its antithrombin-binding activity.	Heparin	31-38	von Willebrand factor	Homo sapiens	4-7
8598091-10	1996	Based on a growing understanding of heparin/vWF interactions, combinations of affinity separations and chemical modifications could be designed to yield heparins uniquely suitable for prevention of arterial thrombosis.	Heparin	153-161	von Willebrand factor	Homo sapiens	44-47
8739535-4	1996	Heparin produced a marked release of TFPI and t-PA after i.v.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	46-50
8617807-4	1996	Employing different truncation fragments of agrin, we determined regions of the protein involved in binding to alpha-dystroglycan and to heparin, an inhibitor of alpha-dystroglycan binding.	Heparin	137-144	agrin	Oryctolagus cuniculus	44-49
8617759-6	1996	Binding of 125I-bFGF to sulfate-depleted ECM was reduced by 50-60% and only about 10% of the ECM-bound bFGF was accessible to release by heparin.	Heparin	137-144	fibroblast growth factor 2	Homo sapiens	16-20
8617759-10	1996	Exogenous heparin stimulated the proliferation of chlorate-treated EC seeded on native ECM, suggesting its interaction with ECM-bound bFGF and subsequent presentation to high affinity cell surface receptors.	Heparin	10-17	fibroblast growth factor 2	Homo sapiens	134-138
8596790-8	1996	The higher concentrations of tissue factor pathway inhibitor led to significantly higher patency rates than heparin, hirudin, or control solutions.	Heparin	108-115	tissue factor pathway inhibitor	Oryctolagus cuniculus	29-60
8740352-3	1996	The heparin coating significantly reduced the concentrations of C3bc, TCC, fibrinopeptide A, lactoferrin, myeloperoxidase and beta-thromboglobulin.	Heparin	4-11	myeloperoxidase	Homo sapiens	106-121
8641011-0	1996	Heparin and heparan sulfate block angiotensin II-induced hypertrophy in cultured neonatal rat cardiomyocytes.	Heparin	0-7	angiotensinogen	Rattus norvegicus	34-48
8631970-9	1996	We also analyzed the heparin binding properties of the precursor and mature forms of HGFA.	Heparin	21-28	HGF activator	Homo sapiens	85-89
8631970-10	1996	HGFA had a weak affinity for heparin near the physiological salt concentration in its precursor form but acquired a strong affinity for heparin upon activation that is linked to blood coagulation.	Heparin	29-36	HGF activator	Homo sapiens	0-4
8631970-10	1996	HGFA had a weak affinity for heparin near the physiological salt concentration in its precursor form but acquired a strong affinity for heparin upon activation that is linked to blood coagulation.	Heparin	136-143	HGF activator	Homo sapiens	0-4
8631930-4	1996	This latter interaction appears unique since the binding of copper to FGFR-1 mediates the binding of the receptor to immobilized heparin.	Heparin	129-136	fibroblast growth factor receptor 1	Homo sapiens	70-76
8849037-3	1996	Selenoprotein-P is retained on a heparin-Sepharose column, and subsequently eluted with an excess of heparin, while glutathione peroxidase is separated by a blue-Sepharose column.	Heparin	33-40	selenoprotein P	Homo sapiens	0-15
8619817-1	1996	Midkine (MK) is a heparin binding growth/differentiation factor different from fibroblast growth factors (FGFs), and is largely composed of two domains which are found by a folded polypeptide chain interconnected by disulfide bridges.	Heparin	18-25	midkine	Homo sapiens	0-7
8619817-1	1996	Midkine (MK) is a heparin binding growth/differentiation factor different from fibroblast growth factors (FGFs), and is largely composed of two domains which are found by a folded polypeptide chain interconnected by disulfide bridges.	Heparin	18-25	midkine	Homo sapiens	9-11
8779995-8	1996	Heparin did not block the Na+/H+ exchanger directly, as it still restored pHi in response to an acid load.	Heparin	0-7	glucose-6-phosphate isomerase	Bos taurus	74-77
8907299-4	1996	Heparins exert their anticoagulant effect by enhancing ATIII inhibitory action on factor Xa and thrombin, which results in decreased factor X activation, prothrombinase formation, prothrombin activation and thrombin generation.	Heparin	0-8	coagulation factor II, thrombin	Homo sapiens	96-104
8907299-4	1996	Heparins exert their anticoagulant effect by enhancing ATIII inhibitory action on factor Xa and thrombin, which results in decreased factor X activation, prothrombinase formation, prothrombin activation and thrombin generation.	Heparin	0-8	coagulation factor II, thrombin	Homo sapiens	157-165
8579370-7	1996	alpha 2M* and RAP can inhibit the binding of LDL to macrophages completely (96 and 100% inhibition, respectively), after cell surface heparin has been removed by treatment with heparinase.	Heparin	134-141	PZP, alpha-2-macroglobulin like	Mus musculus	0-8
8849037-3	1996	Selenoprotein-P is retained on a heparin-Sepharose column, and subsequently eluted with an excess of heparin, while glutathione peroxidase is separated by a blue-Sepharose column.	Heparin	101-108	selenoprotein P	Homo sapiens	0-15
8611172-6	1996	When tissue extracts were applied to columns of heparin-agarose and eluted by a gradient of NaCl, a peak of active LPL was eluted at 1.0 M NaCl, but there was also a peak of inactive LPL protein, which was eluted at 0.6 M NaCl.	Heparin	48-55	lipoprotein lipase	Rattus norvegicus	115-118
8611172-8	1996	The mass ratio between inactive and active LPL, as separated by heparin-agarose chromatography, increased from 0.5 to over 2 during the fast.	Heparin	64-71	lipoprotein lipase	Rattus norvegicus	43-46
8603018-4	1996	Using recently developed sensitive assays for FXIa-inhibitor complexes we found thrombin-mediated and FXII-dependent activation of endogenous FXI in plasma in the presence of heparan sulphate, heparin, dermatan sulphate or dextran sulphate.	Heparin	193-200	coagulation factor II, thrombin	Homo sapiens	80-88
8634855-4	1996	Blood loss from heparin neutralization to 12h after surgery was correlated with platelet count, fibrinogen and ADP aggregation rate.	Heparin	16-23	fibrinogen beta chain	Homo sapiens	96-106
8838445-0	1996	A low molecular weight heparin, nadroparin (Fraxiparine), inhibits thrombin-induced platelet shape change and does not enhance spontaneous platelet aggregation.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	67-75
8838445-1	1996	Therapeutic concentrations, added in vitro, of a low molecular weight heparin (LMWH), nadroparin (Fraxiparine), inhibit thrombin-induced platelet shape change (PSC), an early stage of human platelet activation.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	120-128
8598221-2	1996	The C-terminal heparin-binding domain of FN (Hep II) has recently been demonstrated to support adhesion of alpha 4 beta 1-dependent melanoma cells [A. P. Mould and M. J. Humphries (1991) EMBO J.	Heparin	15-22	fibronectin 1	Homo sapiens	41-43
8652906-7	1996	The sulphated glycosaminoglycans which were critical in FGF-2-induced proliferation were strictly HSPG, as an addition of heparin in cell culture medium can restore FGF-2 mitogenic activity.	Heparin	122-129	fibroblast growth factor 2	Homo sapiens	56-61
8652906-7	1996	The sulphated glycosaminoglycans which were critical in FGF-2-induced proliferation were strictly HSPG, as an addition of heparin in cell culture medium can restore FGF-2 mitogenic activity.	Heparin	122-129	fibroblast growth factor 2	Homo sapiens	165-170
8777274-0	1996	LPS induced release of IL-1 beta, IL-6, IL-8 and TNF-alpha in EDTA or heparin anticoagulated whole blood from persons with high or low levels of serum HDL.	Heparin	70-77	tumor necrosis factor	Homo sapiens	49-58
8598221-0	1996	The novel recognition site in the C-terminal heparin-binding domain of fibronectin by integrin alpha 4 beta 1 receptor on HL-60 cells.	Heparin	45-52	fibronectin 1	Homo sapiens	71-82
8555184-12	1996	Heparin markedly enhanced the ability of TFPI-2/PP5 to inhibit factor VIIa-tissue factor both in the solution phase and on cell surfaces.	Heparin	0-7	tissue factor pathway inhibitor 2	Homo sapiens	41-47
8591858-1	1996	Although fibroblast growth factor 1 (FGF-1) (formerly known as acidic FGF) but not FGF-2 (or basic FGF), has been suggested to play a pathophysiological role in liver regeneration, its clinical application has been restricted by its limited mitogenecity and heparin dependence.	Heparin	258-265	fibroblast growth factor 1	Homo sapiens	37-42
8838671-9	1996	Fibroblasts responded to the addition of dermatan sulfate, heparan sulfate and heparin with a decrease in fibronectin, collagenase and interleukin-6 mRNA.	Heparin	79-86	fibronectin 1	Homo sapiens	106-117
8838671-9	1996	Fibroblasts responded to the addition of dermatan sulfate, heparan sulfate and heparin with a decrease in fibronectin, collagenase and interleukin-6 mRNA.	Heparin	79-86	interleukin 6	Homo sapiens	135-148
8869034-1	1996	Human recombinant basic fibroblast growth factor (bFGF) is a potent mitogen for normal human dermal fibroblasts in the presence of heparin which binds to and stabilizes it.	Heparin	131-138	fibroblast growth factor 2	Homo sapiens	18-48
8869034-1	1996	Human recombinant basic fibroblast growth factor (bFGF) is a potent mitogen for normal human dermal fibroblasts in the presence of heparin which binds to and stabilizes it.	Heparin	131-138	fibroblast growth factor 2	Homo sapiens	50-54
8570646-2	1996	It has been proposed that the binding of heparin-like polysaccharides to FGF induces a conformational change in FGF, resulting in the formation of FGF dimers or oligomers, and this biologically active form is "presented" to the FGF receptor for signal transduction.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	73-76
8570646-2	1996	It has been proposed that the binding of heparin-like polysaccharides to FGF induces a conformational change in FGF, resulting in the formation of FGF dimers or oligomers, and this biologically active form is "presented" to the FGF receptor for signal transduction.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	112-115
8570646-2	1996	It has been proposed that the binding of heparin-like polysaccharides to FGF induces a conformational change in FGF, resulting in the formation of FGF dimers or oligomers, and this biologically active form is "presented" to the FGF receptor for signal transduction.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	112-115
8570646-2	1996	It has been proposed that the binding of heparin-like polysaccharides to FGF induces a conformational change in FGF, resulting in the formation of FGF dimers or oligomers, and this biologically active form is "presented" to the FGF receptor for signal transduction.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	112-115
8570646-4	1996	As a consequence, FGF-2 monomers are oriented for binding to heparin-like polysaccharides.	Heparin	61-68	fibroblast growth factor 2	Homo sapiens	18-23
8570646-8	1996	Thus, we propose that preferential FGF-2 self-association, further stabilized by heparin, like "beads on a string," mediates FGF-2-induced receptor dimerization and activation.	Heparin	81-88	fibroblast growth factor 2	Homo sapiens	35-40
8570646-8	1996	Thus, we propose that preferential FGF-2 self-association, further stabilized by heparin, like "beads on a string," mediates FGF-2-induced receptor dimerization and activation.	Heparin	81-88	fibroblast growth factor 2	Homo sapiens	125-130
8570646-9	1996	The observed FGF-2 self-association, modulated by heparin, not only provides a mechanism of growth factor activation but also represents a regulatory mechanism governing FGF-2 biological activity.	Heparin	50-57	fibroblast growth factor 2	Homo sapiens	13-18
8570646-9	1996	The observed FGF-2 self-association, modulated by heparin, not only provides a mechanism of growth factor activation but also represents a regulatory mechanism governing FGF-2 biological activity.	Heparin	50-57	fibroblast growth factor 2	Homo sapiens	170-175
8591858-1	1996	Although fibroblast growth factor 1 (FGF-1) (formerly known as acidic FGF) but not FGF-2 (or basic FGF), has been suggested to play a pathophysiological role in liver regeneration, its clinical application has been restricted by its limited mitogenecity and heparin dependence.	Heparin	258-265	fibroblast growth factor 1	Homo sapiens	9-35
8822270-5	1996	In the presence of heparin the release of LPL activity in the medium was linear until 3 h and was always significantly increased vs. without heparin.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	42-45
8822270-5	1996	In the presence of heparin the release of LPL activity in the medium was linear until 3 h and was always significantly increased vs. without heparin.	Heparin	141-148	lipoprotein lipase	Rattus norvegicus	42-45
8555184-12	1996	Heparin markedly enhanced the ability of TFPI-2/PP5 to inhibit factor VIIa-tissue factor both in the solution phase and on cell surfaces.	Heparin	0-7	tissue factor pathway inhibitor 2	Homo sapiens	48-51
8904267-1	1996	BACKGROUND: Treatment with heparin has been reported to interfere with lipid metabolism by release of Lipoprotein Lipase (LPL) into the circulation.	Heparin	27-34	lipoprotein lipase	Rattus norvegicus	102-120
8904267-1	1996	BACKGROUND: Treatment with heparin has been reported to interfere with lipid metabolism by release of Lipoprotein Lipase (LPL) into the circulation.	Heparin	27-34	lipoprotein lipase	Rattus norvegicus	122-125
8904267-12	1996	Heparin treatment in combination with continuous TPN administration was followed by increased levels of triglycerides in blood and HDL particles, suggesting that treatment with heparin might have impaired the capacity for LPL up-regulation, resulting in the development of hyperlipidemia.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	222-225
8555184-13	1996	In addition, heparin augmented the inhibition of human factor Xa amidolytic activity at relatively high levels (10-100 nM) of TFPI-2/PP5.	Heparin	13-20	tissue factor pathway inhibitor 2	Homo sapiens	126-132
8904267-12	1996	Heparin treatment in combination with continuous TPN administration was followed by increased levels of triglycerides in blood and HDL particles, suggesting that treatment with heparin might have impaired the capacity for LPL up-regulation, resulting in the development of hyperlipidemia.	Heparin	177-184	lipoprotein lipase	Rattus norvegicus	222-225
8555184-13	1996	In addition, heparin augmented the inhibition of human factor Xa amidolytic activity at relatively high levels (10-100 nM) of TFPI-2/PP5.	Heparin	13-20	tissue factor pathway inhibitor 2	Homo sapiens	133-136
8546689-0	1996	Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface.	Heparin	100-107	superoxide dismutase 3	Bos taurus	44-78
8546689-4	1996	Molecular genetic studies have shown that the donors in the high-level group have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of EC-SOD [Sandstrom, Nilsson, Karlsson and Marklund (1994) J. Biol.	Heparin	176-183	superoxide dismutase 3	Bos taurus	202-208
8546689-11	1996	Serum EC-SOD from heterozygotes and homozygotes had equally decreased affinity for heparin, as judged by heparin-HPLC, as compared with that from normal donors.	Heparin	83-90	superoxide dismutase 3	Bos taurus	6-12
8546689-12	1996	This result suggests that the serum EC-SOD in heterozygotes was mainly composed of the mutant form which has reduced heparin affinity.	Heparin	117-124	superoxide dismutase 3	Bos taurus	36-42
8546689-15	1996	The enzyme form consisting of only mutant subunits, the form with the weakest heparin affinity, can be preferentially driven out to the plasma phase, because EC-SOD in the vasculature exists in equilibrium between plasma and the endothelial cell surface.	Heparin	78-85	superoxide dismutase 3	Bos taurus	158-164
8562407-7	1996	Moreover, such an inhibitory activity of PF4-related peptides is abrogated by heparin (5 IU/dish).	Heparin	78-85	platelet factor 4	Mus musculus	41-44
8547648-5	1996	Binding of 125I-bFGF to K562 cell surfaces was reduced in a dose-dependent manner by unlabeled bFGF or by heparin.	Heparin	106-113	fibroblast growth factor 2	Homo sapiens	16-20
8845459-0	1996	Inhibition of thrombin generation by heparin and LMW heparins: a comparison of chromogenic and clotting methods.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	14-22
8845459-1	1996	Inhibition of thrombin generation by heparin and low-molecular-weight (LMW) heparins is an important parameter which relates to their anticoagulant actions in vivo.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	14-22
8845459-1	1996	Inhibition of thrombin generation by heparin and low-molecular-weight (LMW) heparins is an important parameter which relates to their anticoagulant actions in vivo.	Heparin	76-84	coagulation factor II, thrombin	Homo sapiens	14-22
8845459-3	1996	We have therefore measured the inhibition of thrombin generation by unfractionated heparin (UFH) and LMW heparins by a modified chromogenic method using microtitre plates and compared the results with the clotting method.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	45-53
8845459-3	1996	We have therefore measured the inhibition of thrombin generation by unfractionated heparin (UFH) and LMW heparins by a modified chromogenic method using microtitre plates and compared the results with the clotting method.	Heparin	92-95	coagulation factor II, thrombin	Homo sapiens	45-53
8698272-0	1996	Influence of heparin, protamine and polybrene on the time integral of thrombin generation (endogenous thrombin potential).	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	70-78
8616919-0	1996	The protective dose of the potent GPIIb/IIIa antagonist SC-54701A is reduced when used in combination with aspirin and heparin in a canine model of coronary artery thrombosis.	Heparin	119-126	integrin subunit alpha 2b	Canis lupus familiaris	34-39
9074719-6	1996	By in vitro and ex vivo experiments in mice, heparin and other glycosaminoglycans were shown to stimulate megakaryocytopoiesis by acting synergistically with thrombopoietin and interleukin 6, and in the other hand by neutralizing inhibitors of megakaryocytopoiesis such as platelet factor 4 and transforming growth factor beta.	Heparin	45-52	interleukin 6	Mus musculus	177-190
8565823-7	1996	Epidermal growth factor (EGF) and fibroblast growth factor-4 (FGF-4) inhibited apoptosis in the dental mesenchyme when applied locally using agarose or heparin-coated acrylic beads, suggesting involvement of these or related growth factors in the prevention of apoptosis in dental tissues in vivo.	Heparin	152-159	fibroblast growth factor 4	Mus musculus	34-60
8565823-7	1996	Epidermal growth factor (EGF) and fibroblast growth factor-4 (FGF-4) inhibited apoptosis in the dental mesenchyme when applied locally using agarose or heparin-coated acrylic beads, suggesting involvement of these or related growth factors in the prevention of apoptosis in dental tissues in vivo.	Heparin	152-159	fibroblast growth factor 4	Mus musculus	62-67
8698272-0	1996	Influence of heparin, protamine and polybrene on the time integral of thrombin generation (endogenous thrombin potential).	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	102-110
8664906-1	1996	Human antithrombin is the major plasma inhibitor of thrombin both in the presence and absence of heparin.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	10-18
8707164-5	1996	Most of the saccharide chains of low-molecular-weight heparins are composed of less than 18 saccharides and have reduced ability to inhibit thrombin relative to their ability to inhibit factor Xa.	Heparin	54-62	coagulation factor II, thrombin	Homo sapiens	140-148
8788110-9	1996	The results of this study demonstrate that the displacement of ATIII from immobilized heparin was proportional to the fibronectin concentration, and was reversible.	Heparin	86-93	fibronectin 1	Homo sapiens	118-129
8788110-0	1996	Effect of fibronectin on the binding of antithrombin III to immobilized heparin.	Heparin	72-79	fibronectin 1	Homo sapiens	10-21
8788110-2	1996	The competition and binding interaction between immobilized heparin and antithrombin III (ATIII)/thrombin have been described in vitro.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	76-84
8666421-7	1996	The fraction passed through the heparin column sustained the growth of IL-6-dependent MH60.BSF-2 cells.	Heparin	32-39	interleukin 6	Mus musculus	71-75
8666421-9	1996	The thymocyte proliferative activity of the fraction firmly bound to the heparin column was neutralized with an anti-IL-7 antibody.	Heparin	73-80	interleukin 7	Mus musculus	117-121
8788110-6	1996	The binding interaction of immobilized heparin with ATIII was then determined in the presence of different fibronectin concentrations.	Heparin	39-46	fibronectin 1	Homo sapiens	107-118
8639481-2	1996	Exposure of albumin-heparin modified surfaces (alb-hep surfaces) to plasma dilutions resulted in surfaces with a lower anticoagulant activity than surfaces which were not exposed to plasma dilutions.	Heparin	20-27	albumin	Homo sapiens	12-15
10602554-3	1996	Aspirin is already useful in this regard as well as heparin with recombinant tissue-type plasminogen activator.	Heparin	52-59	plasminogen activator, tissue type	Homo sapiens	77-110
8639481-4	1996	Alb-hep surfaces incubated in plasma which was preexposed to heparin-Sepharose retained 30% of their initial activity.	Heparin	61-68	albumin	Homo sapiens	0-3
8907176-1	1996	Plasma fibronectin incubated with a low concentration of SH reagent under physiological conditions without cells formed a multimer which retained the ability of heparin-binding and cell-binding but lost gelatin affinity [Sakai, K., Fujii, T., and Hayashi, T. (1994) J. Biochem.	Heparin	161-168	fibronectin 1	Homo sapiens	7-18
8938284-5	1996	In addition, heparin cannot completely inhibit thrombin formation and action and may play a central role in the coagulation disorders associated with CPB.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	47-55
8592414-6	1996	Conversely, the concentration of heparin routinely used in intraoperative vessel irrigation solutions (50 U/ml) was able to completely block thrombin activity at both sites.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	141-149
8592414-10	1996	Furthermore, vessel-associated thrombin is resistant to a standard systemic concentration of heparin but is susceptible to the much higher heparin concentration that can be delivered locally by the surgeon during vessel irrigation.	Heparin	93-100	coagulation factor II, thrombin	Homo sapiens	31-39
8592414-10	1996	Furthermore, vessel-associated thrombin is resistant to a standard systemic concentration of heparin but is susceptible to the much higher heparin concentration that can be delivered locally by the surgeon during vessel irrigation.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	31-39
8858487-0	1996	The interactions between antithrombin III, thrombin and surface immobilized heparin.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	29-37
8551753-1	1996	The hypothesis that heparin-coated perfusion circuits reduce thrombin formation and activity; fibrinolysis; and platelet, complement, and neutrophil activation was tested in 20 consecutive, randomized adults who had cardiopulmonary bypass.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	61-69
18475729-4	1996	PMN infiltration evoked by various PMN chemoattractants (FMLP, C5a desArg, LTB(4) and IL-8) was significantly inhibited after intravenous injection of dextran sulphate (25 mg/kg), heparin (2 x 90 mg/kg) or fucoidan (1 mg/kg).	Heparin	180-187	interleukin-8	Oryctolagus cuniculus	86-90
8856244-4	1996	Heparins prevent the release of endothelin-1 and potentiate the action of constitutive nitric oxide.	Heparin	0-8	endothelin 1	Homo sapiens	32-44
8844772-11	1996	VIP inhibited proliferation and degranulation of mast cells, increased heparin content of the cells, and protected Leydig cells.	Heparin	71-78	vasoactive intestinal peptide	Rattus norvegicus	0-3
8807711-1	1996	It has been suggested that mast cells contain receptors for thrombin because binding of thrombin to peritoneal mast cells (PMCs) results in heparin release.	Heparin	140-147	coagulation factor II, thrombin	Homo sapiens	60-68
8899830-0	1996	Novel synthetic peptides from the C-terminal heparin binding domain of fibronectin with heparin binding activity.	Heparin	45-52	fibronectin 1	Homo sapiens	71-82
8899830-0	1996	Novel synthetic peptides from the C-terminal heparin binding domain of fibronectin with heparin binding activity.	Heparin	88-95	fibronectin 1	Homo sapiens	71-82
8899830-1	1996	To identify a minimal peptide ligand that participates in recognition of heparin, we synthesized peptides extending a 29-kDa fragment in the C-terminal heparin binding domain of fibronectin.	Heparin	73-80	fibronectin 1	Homo sapiens	178-189
8899830-4	1996	A new heparin binding site in the C-terminal heparin binding domain of fibronectin is demonstrated and provides a rationale for understanding the mechanism of cell adhesion and spreading.	Heparin	6-13	fibronectin 1	Homo sapiens	71-82
8899830-4	1996	A new heparin binding site in the C-terminal heparin binding domain of fibronectin is demonstrated and provides a rationale for understanding the mechanism of cell adhesion and spreading.	Heparin	45-52	fibronectin 1	Homo sapiens	71-82
8807725-4	1996	The generation of thrombin seems to be a pivotal event in thrombogenesis, and inactivation of this enzyme has been attempted for many years with heparin, low-molecular-weight heparin, and other glycosaminoglycans.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	18-26
8807725-4	1996	The generation of thrombin seems to be a pivotal event in thrombogenesis, and inactivation of this enzyme has been attempted for many years with heparin, low-molecular-weight heparin, and other glycosaminoglycans.	Heparin	175-182	coagulation factor II, thrombin	Homo sapiens	18-26
8961380-4	1996	Substance P (30 microM) also induced a transient increase in the intracellular Ca2+ concentration ([Ca2+]i) in both synovial A and B cells as measured by a Ca2+ indicator, fura 2, BAPTA-AM and an inositol-1,4-5-triphosphate (IP3) receptor antagonist, heparin, inhibited the substance P induced increase in [Ca2+]i, but they had no effects on oxyradical production.	Heparin	251-258	tachykinin precursor 1	Homo sapiens	0-11
8807711-1	1996	It has been suggested that mast cells contain receptors for thrombin because binding of thrombin to peritoneal mast cells (PMCs) results in heparin release.	Heparin	140-147	coagulation factor II, thrombin	Homo sapiens	88-96
8807720-1	1996	Tissue factor pathway inhibitor (TFPI) is a Kunitz-type serine protease inhibitor found within the vascular system that is known to be released upon heparin administration.	Heparin	149-156	tissue factor pathway inhibitor	Oryctolagus cuniculus	0-31
8713780-3	1996	In the heparin tube, APC reacts completely and irreversibly with its major plasma inhibitors, protein C inhibitor (PCI) and alpha 1-antitrypsin (alpha 1AT), and the complexes formed are measured by ELISAs.	Heparin	7-14	serpin family A member 1	Homo sapiens	124-143
8713801-4	1996	Fragment PAD-1 bound to heparin and botrocetin in a specific and dose dependent manner as did the native vWF.	Heparin	24-31	von Willebrand factor	Bos taurus	105-108
8713780-3	1996	In the heparin tube, APC reacts completely and irreversibly with its major plasma inhibitors, protein C inhibitor (PCI) and alpha 1-antitrypsin (alpha 1AT), and the complexes formed are measured by ELISAs.	Heparin	7-14	serpin family A member 1	Homo sapiens	145-154
8807720-1	1996	Tissue factor pathway inhibitor (TFPI) is a Kunitz-type serine protease inhibitor found within the vascular system that is known to be released upon heparin administration.	Heparin	149-156	tissue factor pathway inhibitor	Oryctolagus cuniculus	33-37
8713801-6	1996	The studies presented in this paper demonstrated that the A1 domain of bovine vWF contained the GPIb, heparin, botrocetin as well as collagen binding sites and that integrity of the disulfide bond (Cys 509-Cys 695), did not seem to be essential for binding of bovine vWF fragment to GPIb.	Heparin	102-109	von Willebrand factor	Bos taurus	78-81
8530367-4	1995	In addition, heparin decreased monocyte binding to fibronectin, a known SEM protein, by 60%.	Heparin	13-20	fibronectin 1	Homo sapiens	51-62
8747526-3	1996	VCL inhibited 50% of vWf binding to heparin, but it did not inhibit vWf binding to type I collagen.	Heparin	36-43	von Willebrand factor	Homo sapiens	21-24
8713795-1	1996	Clot-associated thrombin retains amidolytic activity, and is resistant to inhibition by heparin, but not to low molecular weight thrombin inhibitors.	Heparin	88-95	coagulation factor II, thrombin	Homo sapiens	16-24
8713795-2	1996	We show that clot-associated thrombin induces platelet aggregation, is resistant to heparin:antithrombin III, less so to recombinant hirudin (rHV2Lys47) but not to argatroban, an active-site directed thrombin inhibitor.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	29-37
8713795-9	1996	Heparin had an IC50 of 0.02 mU/ml against aggregation induced by fluid-phase thrombin, but much greater concentrations are required to inhibit clot-induced aggregation (IC50 = 48 mU/ml).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	77-85
8530382-13	1995	PI9 was purified to homogeneity from the yeast cell lysate by a combination of heparin-agarose chromatography and Mono Q fast protein liquid chromatography and migrated as a single band in SDS-polyacrylamide gel electrophoresis with an apparent molecular mass of 42 kDa.	Heparin	79-86	serpin family B member 9	Homo sapiens	0-3
8720143-0	1995	Importance of 6-O-sulfate groups of glucosamine residues in heparin for activation of FGF-1 and FGF-2.	Heparin	60-67	fibroblast growth factor 1	Mus musculus	86-91
8787476-11	1995	Also for myeloperoxidase a higher level was observed in the high heparin dose group.	Heparin	65-72	myeloperoxidase	Homo sapiens	9-24
8747094-4	1995	The addition of basic fibroblast growth factor (bFGF) increased proliferation alone and in combination with heparin.	Heparin	108-115	fibroblast growth factor 2	Homo sapiens	48-52
8847261-4	1995	Intradermal injection of tryptase-heparin (n = 7), however, resulted in 50 (1 ng) and 82% (10 ng) of the ICR to histamine (both, P &lt; 0.05 vs. tryptase alone).	Heparin	34-41	tryptase beta-2	Ovis aries	25-33
8847261-4	1995	Intradermal injection of tryptase-heparin (n = 7), however, resulted in 50 (1 ng) and 82% (10 ng) of the ICR to histamine (both, P &lt; 0.05 vs. tryptase alone).	Heparin	34-41	tryptase beta-2	Ovis aries	145-153
7493920-7	1995	Heparin inhibits the association between FGF-1 and PS, and synthetic peptide competition assays suggest that the PS-binding domain of FGF-1 lies between residues 114 and 137.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	41-46
7493920-7	1995	Heparin inhibits the association between FGF-1 and PS, and synthetic peptide competition assays suggest that the PS-binding domain of FGF-1 lies between residues 114 and 137.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	134-139
8847261-5	1995	APC-366 inhibited (P &lt; 0.05) the ICR to 1 and 10 ng tryptase-heparin by &gt; or = 70% at all times (n = 8) but had no effect on the histamine-induced ICR (n = 3).	Heparin	64-71	tryptase beta-2	Ovis aries	55-63
7490920-4	1995	Although aspirin, heparin, and warfarin sodium have been the conventionally used agents for inhibiting thrombin and platelet function, newer agents such as hirudin and inhibitors of the platelet glycoprotein IIb-IIIa receptor are becoming available, and their clinical application will increase in the future.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	103-111
8643109-8	1995	Both heparin and sulfated dextrans also inhibit agglutination, suggesting that charged residues on rCD4 played an important role in agglutination mediated by rCD4 or CD4 peptide.	Heparin	5-12	CD4 molecule	Homo sapiens	100-103
7592941-10	1995	EDTA, heparin, and phosphorylethanolamine as well as a peptide comprising amino acids 27-39 of SAP were found to completely displace C4BP from the SAP matrix.	Heparin	6-13	complement component 4 binding protein alpha	Homo sapiens	133-137
8786730-4	1995	Tissue LPL was measured as the heparin-released (HR) and cellular-extracted (EXT) fractions 16 hours following the last bout of exercise, during which time some animals were fasted and others were allowed free access to food.	Heparin	31-38	lipoprotein lipase	Rattus norvegicus	7-10
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	51-59
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Heparin	148-155	CD59 molecule (CD59 blood group)	Homo sapiens	93-98
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Heparin	257-264	coagulation factor II, thrombin	Homo sapiens	51-59
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Heparin	257-264	CD59 molecule (CD59 blood group)	Homo sapiens	93-98
7499327-0	1995	Heparin modulates the binding of insulin-like growth factor (IGF) binding protein-5 to a membrane protein in osteoblastic cells.	Heparin	0-7	insulin-like growth factor binding protein 5	Mus musculus	33-83
7499327-5	1995	Osteoblast binding of intact 125I-IGFBP-5 was inhibited by low heparin concentrations, while 125I-IGFBP-5(1-169) binding was stimulated by heparin.	Heparin	139-146	insulin-like growth factor binding protein 5	Mus musculus	98-105
7499327-10	1995	While the membrane protein internalized both forms of IGFBP-5, heparin treatment inhibited the internalization of intact 125I-IGFBP-5 but stimulated 125I-IGFBP-5(1-169) internalization.	Heparin	63-70	insulin-like growth factor binding protein 5	Mus musculus	126-133
7499327-10	1995	While the membrane protein internalized both forms of IGFBP-5, heparin treatment inhibited the internalization of intact 125I-IGFBP-5 but stimulated 125I-IGFBP-5(1-169) internalization.	Heparin	63-70	insulin-like growth factor binding protein 5	Mus musculus	126-133
8595612-10	1995	Up-regulation of CD11b, down-regulation of L-s and release of IL8 were inversely related to heparin concentration (r = 0.87, P &lt; 0.05).	Heparin	92-99	C-X-C motif chemokine ligand 8	Homo sapiens	62-65
8526620-6	1995	RESULTS: Heparin coating by either method reduced the formation of terminal SC5b-9 complement complex and the release of lactoferrin and myeloperoxidase compared with uncoated systems.	Heparin	9-16	myeloperoxidase	Homo sapiens	137-152
8594987-1	1995	Basic fibroblast growth factor (bFGF) is a member of the heparin-binding growth factor family that interacts with cell surface heparan sulfate (HS) proteoglycans and extracellular matrix heparin.	Heparin	57-64	fibroblast growth factor 2	Homo sapiens	0-30
8594987-1	1995	Basic fibroblast growth factor (bFGF) is a member of the heparin-binding growth factor family that interacts with cell surface heparan sulfate (HS) proteoglycans and extracellular matrix heparin.	Heparin	57-64	fibroblast growth factor 2	Homo sapiens	32-36
8594987-2	1995	Here we report the development of a simple and sensitive assay that used biotinylated HS or heparin to bind to bFGF coated onto 96-well microtiter plates.	Heparin	92-99	fibroblast growth factor 2	Homo sapiens	111-115
8594987-5	1995	Glycosaminoglycans and modified heparins were assayed for their ability to compete with biotinylated HS for binding to bFGF.	Heparin	32-40	fibroblast growth factor 2	Homo sapiens	119-123
8595612-3	1995	DESIGN: In a series of experiments, we examined the effect of heparin (4 U/ml) comparing it with ethylenediamine tetra-acetate (EDTA, 1.5 mg/ml) and citrate mixture (100 microliters/ml), heparin dose-response, IL8 (human recombinant IL8) dose-response and protamine (80 micrograms/ml) neutralisation of heparin (4 U/ml) using donor blood (total of 38).	Heparin	62-69	C-X-C motif chemokine ligand 8	Homo sapiens	210-213
8595612-3	1995	DESIGN: In a series of experiments, we examined the effect of heparin (4 U/ml) comparing it with ethylenediamine tetra-acetate (EDTA, 1.5 mg/ml) and citrate mixture (100 microliters/ml), heparin dose-response, IL8 (human recombinant IL8) dose-response and protamine (80 micrograms/ml) neutralisation of heparin (4 U/ml) using donor blood (total of 38).	Heparin	62-69	C-X-C motif chemokine ligand 8	Homo sapiens	233-236
8749310-7	1995	Thus, type-II PLA2 bound to cell-surface heparin-like molecules may exert its activity and participate in eicosanoid generation only in the presence of TNF alpha.	Heparin	41-48	tumor necrosis factor	Rattus norvegicus	152-161
8608685-8	1995	After heparin therapy a significant reduction vs. basal value was observed in levels of serum osteocalcin (ng/ml;mean + SEM): 3.32 &amp; 0.19 vs. 2.05 + 0.21; p &lt; 0.001.	Heparin	6-13	bone gamma-carboxyglutamate protein	Homo sapiens	94-105
7586360-7	1995	The plasma level of thrombin-antithrombin complex and prothrombin fragment 1.2 increased in all groups during bypass, and somewhat more in both the heparin-coated groups toward the end of CPB, compared with the control group (P &lt; .01).	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	20-28
7589259-6	1995	Immunoblotting with specific monoclonal antibodies revealed initial degradation of soluble fibronectin within 1 h. Further degradation occurred over a period of 20 h. Degradation of soluble fibronectin resulted in one fragment of 58 kDa containing the gelatin-binding domain, two fragments of 37 and 38 kDa, which were part of the cell attachment domain, and three fragments of 36, 33, and 30 kDa recognized by an antibody raised against the C-terminal heparin-binding domain.	Heparin	453-460	fibronectin 1	Homo sapiens	190-201
7591632-4	1995	Because FGF2 binds to heparin, FGF2-saporin was incubated with HSM PMMA IOLs; excess toxin was washed off, and the BEL cells were grown on the FGF2-saporin-treated IOLs (HSM and non-HSM) for 4 days.	Heparin	22-29	fibroblast growth factor 2	Bos taurus	8-12
7591632-9	1995	The ability of FGF2-saporin to prevent the growth of cells on the IOL surface was strictly dependent on the presence of heparin on the IOL.	Heparin	120-127	fibroblast growth factor 2	Bos taurus	15-19
7591634-6	1995	Basic fibroblast growth factor was not chemoattractive on its own but stimulated migration when combined with heparin.	Heparin	110-117	fibroblast growth factor 2	Bos taurus	0-30
8520218-11	1995	The discovery of the helix-like region in the primary heparin-binding site (residues 128-138) instead of the beta-strand conformation described in the X-ray structures may have important implications in understanding the nature of heparin-FGF-2 interactions.	Heparin	54-61	fibroblast growth factor 2	Homo sapiens	239-244
8544408-14	1995	Labeling with the cell cycle marker MIB-1 (monoclonal antibody Ki-67), showed a progressive reduction in the observed intensity in heparin treated cells with substantially fewer cells being positive.	Heparin	131-138	MIB E3 ubiquitin protein ligase 1	Rattus norvegicus	36-41
8568518-7	1995	Adhesion to s-laminin and plastic appears to be mediated by different cell surface components, as adhesion to recombinant s-laminin is inhibited by the tripeptide, LRE, and by Ca2+ ions, but not by heparin, whereas adhesion to plastic is LRE and Ca2+ insensitive but heparin sensitive.	Heparin	267-274	laminin, beta 2 (laminin S)	Gallus gallus	124-131
8583947-17	1995	Hydrocortisone alone or in combination with heparin led to a significant inhibition of bFGF-stimulated angiogenesis.	Heparin	44-51	fibroblast growth factor 2	Bos taurus	87-91
7592764-8	1995	The heparin-binding peptide could antagonize the mitogenic activity of FGF-1, probably because of the heparin dependence of this activity.	Heparin	4-11	fibroblast growth factor 1	Homo sapiens	71-76
8578545-1	1995	Antithrombin from bony fish (Teleostei), represented by an ancient salmonid, Atlantic salmon (Salmo salar L.), and a more evolved species from the same family, rainbow trout (Oncorhynchus mykiss Walbaum), functions in vitro as does its human counterpart: it inactivates thrombin almost instantaneously in the presence of heparin and only slowly when heparin is absent.	Heparin	321-328	coagulation factor II, thrombin	Homo sapiens	4-12
8578545-1	1995	Antithrombin from bony fish (Teleostei), represented by an ancient salmonid, Atlantic salmon (Salmo salar L.), and a more evolved species from the same family, rainbow trout (Oncorhynchus mykiss Walbaum), functions in vitro as does its human counterpart: it inactivates thrombin almost instantaneously in the presence of heparin and only slowly when heparin is absent.	Heparin	350-357	coagulation factor II, thrombin	Homo sapiens	4-12
8578545-6	1995	And the thrombin inactivating capacity of purified antithrombin and diluted plasma in the presence of heparin was indeed present at temperatures down to 3 degrees C, a capacity that human antithrombin also has retained.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	8-16
10172669-1	1995	Alteplase (recombinant tissue plasminogen activator; rt-PA) is a thrombolytic agent that when given in an accelerated regimen with intravenous heparin has survival advantages compared with streptokinase in the treatment of acute myocardial infarction, as shown by the results of the Global Utilisation of Streptokinase and Tissue Plasminogen Activator for Occluded Coronary Arteries (GUSTO) trial.	Heparin	143-150	plasminogen activator, tissue type	Homo sapiens	0-9
7592764-9	1995	Together these data demonstrate that the heparin binding properties of fibroblast growth factor-1 are dictated by structural features more complex than clusters of basic amino acids.	Heparin	41-48	fibroblast growth factor 1	Homo sapiens	71-97
7574046-15	1995	CONCLUSIONS: Aprotinin treatment in combination with heparin leads to less thrombin generation during CPB.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	75-83
7575607-1	1995	Keratinocyte growth factor (KGF) is a member of the fibroblast growth factor (FGF) group of heparin-binding polypeptides.	Heparin	92-99	fibroblast growth factor 7	Homo sapiens	0-26
7575607-1	1995	Keratinocyte growth factor (KGF) is a member of the fibroblast growth factor (FGF) group of heparin-binding polypeptides.	Heparin	92-99	fibroblast growth factor 7	Homo sapiens	28-31
7575607-1	1995	Keratinocyte growth factor (KGF) is a member of the fibroblast growth factor (FGF) group of heparin-binding polypeptides.	Heparin	92-99	fibroblast growth factor 7	Homo sapiens	78-81
8674845-8	1995	Removal of extracellular bFGF with heparin resulted in a rapid, cycloheximide-sensitive increase in high-affinity bFGF binding sites.	Heparin	35-42	fibroblast growth factor 2	Homo sapiens	25-29
8674845-8	1995	Removal of extracellular bFGF with heparin resulted in a rapid, cycloheximide-sensitive increase in high-affinity bFGF binding sites.	Heparin	35-42	fibroblast growth factor 2	Homo sapiens	114-118
8674845-10	1995	The presence of heparin (25 micrograms/ml) in the binding reaction eliminated the association of 125I-bFGF with the heparin-like sites but did not prevent binding to the high-affinity receptor.	Heparin	16-23	fibroblast growth factor 2	Homo sapiens	102-106
8674845-10	1995	The presence of heparin (25 micrograms/ml) in the binding reaction eliminated the association of 125I-bFGF with the heparin-like sites but did not prevent binding to the high-affinity receptor.	Heparin	116-123	fibroblast growth factor 2	Homo sapiens	102-106
7559509-8	1995	These studies indicated that PN-2/A beta PP in the assembled prothrombinase complex inhibited factor Xa comparable to antithrombin III in the presence of heparin.	Heparin	154-161	amyloid beta precursor protein	Homo sapiens	29-33
7670097-3	1995	We also found that IL-1 or TPA-stimulated IL-11 and GM-CSF expression in PU-34 cells can be abolished by heparin, a class of molecules related to extracellular matrix components, glycosaminoglycans.	Heparin	105-112	interleukin-11	Macaca fascicularis	42-47
7583544-6	1995	This increased mitogenic response to HB-EGF in STZ-SMCs was completely inhibited by treatment with heparitinase, chlorate, and a synthetic peptide corresponding to the heparin-binding domain of HB-EGF.	Heparin	168-175	heparin-binding EGF-like growth factor	Rattus norvegicus	37-43
7583544-6	1995	This increased mitogenic response to HB-EGF in STZ-SMCs was completely inhibited by treatment with heparitinase, chlorate, and a synthetic peptide corresponding to the heparin-binding domain of HB-EGF.	Heparin	168-175	heparin-binding EGF-like growth factor	Rattus norvegicus	194-200
7670097-4	1995	Because the growth inhibitory signals provided by extracellular factors were less understood, the mechanisms of heparin inhibition of IL-11 and GM-CSF gene expression were further investigated.	Heparin	112-119	interleukin-11	Macaca fascicularis	134-139
8562843-0	1995	Suppression of F1+2 (thrombin) generation in patients with DVT requires increased doses of heparin.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	21-29
7556445-8	1995	Whereas addition of suramin to COS cell cultures significantly increases the levels of all six Wnts in the medium, the addition of heparin only influences the levels of Wnt-1, Wnt-6, and Wnt-7b.	Heparin	131-138	wingless-type MMTV integration site family, member 7B	Mus musculus	187-193
8846683-0	1995	Effects of heparin-induced non-esterified free fatty acid on minimal model-derived insulin sensitivity in individuals with varying degrees of glucose intolerance.	Heparin	11-18	insulin	Homo sapiens	83-90
8846683-1	1995	The effects of heparin-induced non-esterified free fatty acid (NEFA) release on insulin sensitivity index were studied in individuals with varying degrees of glucose intolerance and beta cell dysfunction during the frequently sampled intravenous glucose tolerance test (IVGTT).	Heparin	15-22	insulin	Homo sapiens	80-87
8846683-8	1995	The higher plasma NEFA levels during heparin injections could worsen the model-derived, insulin sensitivity index and could impair the ability to achieve an acceptable modelling in Type 2 diabetic patients.	Heparin	37-44	insulin	Homo sapiens	88-95
8560429-0	1995	Effects of heparin and hirudin on thrombin generation and platelet aggregation after intrinsic activation of platelet rich plasma.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	34-42
7588746-9	1995	We have previously shown that heparin potentiates the catalytic activity of RMCP-1 and, in the present study, we show that the mechanism for chymase activation involves a sixfold reduction of the Km,app value of RMCP-1 for the chromogenic substrate S-2586.	Heparin	30-37	mast cell protease 1-like 1	Rattus norvegicus	76-82
7588746-9	1995	We have previously shown that heparin potentiates the catalytic activity of RMCP-1 and, in the present study, we show that the mechanism for chymase activation involves a sixfold reduction of the Km,app value of RMCP-1 for the chromogenic substrate S-2586.	Heparin	30-37	mast cell protease 1-like 1	Rattus norvegicus	212-218
8557728-5	1995	It is demonstrated that the rate of thrombin inactivation at the antithrombin-heparin surface equals the maximal rate of transport of thrombin toward the surface when the surface coverage of antithrombin exceeds 10 pmol/cm2.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	36-44
8557728-5	1995	It is demonstrated that the rate of thrombin inactivation at the antithrombin-heparin surface equals the maximal rate of transport of thrombin toward the surface when the surface coverage of antithrombin exceeds 10 pmol/cm2.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	69-77
8557728-10	1995	The rate of thrombin inactivation at surfaces with low heparin content (2 micrograms/cm2) fells below the transport limit of thrombin and became proportional with the heparin content of the surface.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	12-20
8557728-10	1995	The rate of thrombin inactivation at surfaces with low heparin content (2 micrograms/cm2) fells below the transport limit of thrombin and became proportional with the heparin content of the surface.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	12-20
8560405-5	1995	The only significant differences were seen for HDL cholesterol and the corresponding apolipoprotein apoA-I, which were significantly higher in the UFH group (HDL cholesterol: 0.97 +/- 0.35 mM/l vs. 0.87 +/- 0.37 mM/l, p &lt; 0.05; apoA-I 1.23 +/- 0.27 g/l vs. 1.15 +/- 0.27 g/l, p &lt; 0.05).	Heparin	147-150	apolipoprotein A1	Homo sapiens	100-106
8560405-5	1995	The only significant differences were seen for HDL cholesterol and the corresponding apolipoprotein apoA-I, which were significantly higher in the UFH group (HDL cholesterol: 0.97 +/- 0.35 mM/l vs. 0.87 +/- 0.37 mM/l, p &lt; 0.05; apoA-I 1.23 +/- 0.27 g/l vs. 1.15 +/- 0.27 g/l, p &lt; 0.05).	Heparin	147-150	apolipoprotein A1	Homo sapiens	231-237
7545872-8	1995	Our data indicate that mast cells, a primary source of heparin, also serve as a significant source of a heparin-binding growth factor, bFGF, in these disease processes.	Heparin	55-62	fibroblast growth factor 2	Homo sapiens	135-139
7548155-1	1995	This study was undertaken to characterize the potential heparin affinity of an amino-acid sequence within the 70 kDa heat-shock family of proteins (HSPs) that shares homology with a heparin-binding sequence present in the carboxy-terminus of fibronectin (FN), defined by the synthetic peptide, FN-C/H-II (KNNQKSEPLIGRKKT).	Heparin	56-63	fibronectin 1	Homo sapiens	242-253
7548155-1	1995	This study was undertaken to characterize the potential heparin affinity of an amino-acid sequence within the 70 kDa heat-shock family of proteins (HSPs) that shares homology with a heparin-binding sequence present in the carboxy-terminus of fibronectin (FN), defined by the synthetic peptide, FN-C/H-II (KNNQKSEPLIGRKKT).	Heparin	56-63	fibronectin 1	Homo sapiens	255-257
7548155-1	1995	This study was undertaken to characterize the potential heparin affinity of an amino-acid sequence within the 70 kDa heat-shock family of proteins (HSPs) that shares homology with a heparin-binding sequence present in the carboxy-terminus of fibronectin (FN), defined by the synthetic peptide, FN-C/H-II (KNNQKSEPLIGRKKT).	Heparin	182-189	fibronectin 1	Homo sapiens	242-253
7548155-1	1995	This study was undertaken to characterize the potential heparin affinity of an amino-acid sequence within the 70 kDa heat-shock family of proteins (HSPs) that shares homology with a heparin-binding sequence present in the carboxy-terminus of fibronectin (FN), defined by the synthetic peptide, FN-C/H-II (KNNQKSEPLIGRKKT).	Heparin	182-189	fibronectin 1	Homo sapiens	255-257
7548155-3	1995	Only the sequence LIGRKKT bound [3H] heparin, and the LIGRKKT peptide blocked heparin binding to intact fibronectin by 47% (+/- 0.4, p &lt; 0.001).	Heparin	78-85	fibronectin 1	Homo sapiens	104-115
7548155-9	1995	These data demonstrate that LIGRK or LIGRR represent a a common heparin binding motif in fibronectin, HSP70, and HSC70, and are consistent with a proposed role for heparin or similar polyanionic structures in the function of the 70 kDa heat-shock proteins.	Heparin	64-71	fibronectin 1	Homo sapiens	89-100
7547966-6	1995	Heparin increased markedly the kon values for antithrombin III and protease nexin-1 with all thrombin variants tested, but a more dramatic effect was observed with a thrombin mutant (des-ETW) lacking residues Glu146, Thr147, and Trp148 (on the opposite side of the catalytic site relative to the 60-loop insertion).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	50-58
7547966-6	1995	Heparin increased markedly the kon values for antithrombin III and protease nexin-1 with all thrombin variants tested, but a more dramatic effect was observed with a thrombin mutant (des-ETW) lacking residues Glu146, Thr147, and Trp148 (on the opposite side of the catalytic site relative to the 60-loop insertion).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	93-101
7547966-7	1995	At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	82-90
7547966-7	1995	At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin.	Heparin	193-200	coagulation factor II, thrombin	Homo sapiens	82-90
8549645-3	1995	Time-course studies showed that endothelin 1 (10(-7) M) progressively decreased both lipoprotein lipase fractions (heparin-releasable, extractable), until nadir at 24 h. Endothelin-1 reduced both lipoprotein lipase activities (heparin-releasable, extractable) in a concentration-dependent manner, whereas endothelin-3 did not produce any significant changes in either of them.	Heparin	115-122	endothelin 1	Homo sapiens	32-44
8549645-3	1995	Time-course studies showed that endothelin 1 (10(-7) M) progressively decreased both lipoprotein lipase fractions (heparin-releasable, extractable), until nadir at 24 h. Endothelin-1 reduced both lipoprotein lipase activities (heparin-releasable, extractable) in a concentration-dependent manner, whereas endothelin-3 did not produce any significant changes in either of them.	Heparin	115-122	endothelin 1	Homo sapiens	170-182
7677475-3	1995	METHODS: This initial study evaluated the impact of heparin-bonded CPB circuits on production of the cytokines interleukin-1 (IL-1), tumor necrosis factor-alpha (TNF-a), IL-6, and IL-8 in adults undergoing complex cardiac operations with prolonged CPB.	Heparin	52-59	tumor necrosis factor	Homo sapiens	133-160
7670961-1	1995	The amino acid sequence of interferon gamma (IFN-gamma) has basic amino acid clusters similar to the heparin-binding consensus sequences found in other proteins that bind to proteoglycans (PGs).	Heparin	101-108	interferon gamma	Homo sapiens	27-54
7677475-3	1995	METHODS: This initial study evaluated the impact of heparin-bonded CPB circuits on production of the cytokines interleukin-1 (IL-1), tumor necrosis factor-alpha (TNF-a), IL-6, and IL-8 in adults undergoing complex cardiac operations with prolonged CPB.	Heparin	52-59	interleukin 6	Homo sapiens	170-174
7677475-3	1995	METHODS: This initial study evaluated the impact of heparin-bonded CPB circuits on production of the cytokines interleukin-1 (IL-1), tumor necrosis factor-alpha (TNF-a), IL-6, and IL-8 in adults undergoing complex cardiac operations with prolonged CPB.	Heparin	52-59	C-X-C motif chemokine ligand 8	Homo sapiens	180-184
7677475-6	1995	RESULTS: The levels of IL-6 and IL-8 increased in a time-dependent fashion in both groups, but the response was significantly less over time in the heparin-bonded group (p &lt; 0.05) for both IL-6 and IL-8.	Heparin	148-155	interleukin 6	Homo sapiens	23-27
7677475-6	1995	RESULTS: The levels of IL-6 and IL-8 increased in a time-dependent fashion in both groups, but the response was significantly less over time in the heparin-bonded group (p &lt; 0.05) for both IL-6 and IL-8.	Heparin	148-155	interleukin 6	Homo sapiens	192-196
7677475-6	1995	RESULTS: The levels of IL-6 and IL-8 increased in a time-dependent fashion in both groups, but the response was significantly less over time in the heparin-bonded group (p &lt; 0.05) for both IL-6 and IL-8.	Heparin	148-155	C-X-C motif chemokine ligand 8	Homo sapiens	201-205
7673405-7	1995	FGF-2 was extracted from serum and amniotic fluid by heparin-Sepharose affinity chromatography and subjected to Western blot analysis or quantified by specific RIA.	Heparin	53-60	fibroblast growth factor 2	Homo sapiens	0-5
7578898-0	1995	Inhibition of extrinsic and intrinsic thrombin generation by a novel synthetic thrombin inhibitor (Ro 46-6240), recombinant hirudin and heparin in human plasma.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	38-46
7578898-5	1995	Heparin was the most potent inhibitor of extrinsic and intrinsic thrombin generation with IC50 values of 20 and 27 nM, respectively.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	65-73
7672514-5	1995	The biological effect of bFGF is conveyed through its binding to the high-affinity receptor sites and the binding is dependent on the presence of cell surface heparin-like molecules, as treatment of cells with heparitinase or sodium chlorate abolishes high-affinity binding and growth inhibition.	Heparin	159-166	fibroblast growth factor 2	Homo sapiens	25-29
7554444-4	1995	These MRL/lpr/lpr sera induced complement-dependent cleavage and release of 35SO4-labeled material containing primarily cell surface heparan sulfate proteoglycans from these cells, and react with heparin (a glycosaminoglycan related to heparan sulfate) by ELISA and liquid-phase competitive inhibition ELISA.	Heparin	196-203	Fas (TNF receptor superfamily member 6)	Mus musculus	10-13
7554444-4	1995	These MRL/lpr/lpr sera induced complement-dependent cleavage and release of 35SO4-labeled material containing primarily cell surface heparan sulfate proteoglycans from these cells, and react with heparin (a glycosaminoglycan related to heparan sulfate) by ELISA and liquid-phase competitive inhibition ELISA.	Heparin	196-203	Fas (TNF receptor superfamily member 6)	Mus musculus	14-17
7657800-4	1995	Fat/heparin infusion did not affect basal glucose uptake, but inhibited total stimulated (insulin stimulated plus basal) glucose uptake by 40-50% in isoglycemic and in euglycemic patients at plasma FFA concentration of approximately 950 and approximately 550 microM, respectively.	Heparin	4-11	insulin	Homo sapiens	90-97
8537449-0	1995	Distinct heparin-binding and neurite-promoting properties of laminin isoforms isolated from chick heart.	Heparin	9-16	laminin, beta 2 (laminin S)	Gallus gallus	61-68
7646463-4	1995	Second-order rate constants for thrombin and factor Xa inhibition determined in the absence and presence of heparin are in good agreement with values established for plasma antithrombin and these enzymes.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	32-40
7641350-2	1995	BACKGROUND: Direct thrombin inhibitors are a new class of drugs that may offer a more effective and potentially simpler alternative to heparin.	Heparin	135-142	coagulation factor II, thrombin	Homo sapiens	19-27
8568854-8	1995	No current activation by ATP was observed when cells were dialyzed with the IP3 receptor blocker, heparin (10 ng/ml).	Heparin	98-105	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	76-88
7615068-3	1995	This laminin binding is calcium-dependent and can be competed by heparin.	Heparin	65-72	laminin, beta 2 (laminin S)	Gallus gallus	5-12
7635945-9	1995	The affinity of apoE-1 (Lys146--&gt;Glu) to heparin was also markedly reduced compared with both apoE-2 (Arg158--&gt;Cys) and apoE-3.	Heparin	44-51	apolipoprotein E	Homo sapiens	16-20
8535285-0	1995	Isolation of ERp72 from guinea pig term placentae using heparin Sepharose affinity chromatography.	Heparin	56-63	protein disulfide isomerase family A member 4	Homo sapiens	13-18
17607884-3	1995	The interaction of heparin with antithrombin is, however, a kinetic one, with binding being followed by formation of a complex with thrombin and then release from the heparin.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	36-44
17607884-3	1995	The interaction of heparin with antithrombin is, however, a kinetic one, with binding being followed by formation of a complex with thrombin and then release from the heparin.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	36-44
8585000-4	1995	In the rTAP treatment group, 4/6 preparations developed occlusive thrombi, but with times to thrombosis delayed significantly compared to both the saline control as well as to the heparin treatment group (202.7 +/- 28.9 min; p &lt; 0.01 to both saline and heparin groups).	Heparin	256-263	nuclear RNA export factor 1	Rattus norvegicus	7-11
7628627-3	1995	TSP-4 was further enriched by heparin affinity chromatography.	Heparin	30-37	thrombospondin 4	Bos taurus	0-5
7631805-5	1995	BALF PLA2 activity in patients with ARDS was resolved into heparin binding and nonbinding activities.	Heparin	59-66	phospholipase A2 group IB	Homo sapiens	5-9
7631805-7	1995	The PLA2 activity that bound to heparin was identified as a group II PLA2 by its chromatographic characteristics, its inhibition by dithiothreitol, its substrate specificity, and its approximate molecular mass of 14 kDa.	Heparin	32-39	phospholipase A2 group IB	Homo sapiens	4-8
7631805-7	1995	The PLA2 activity that bound to heparin was identified as a group II PLA2 by its chromatographic characteristics, its inhibition by dithiothreitol, its substrate specificity, and its approximate molecular mass of 14 kDa.	Heparin	32-39	phospholipase A2 group IB	Homo sapiens	69-73
7614042-2	1995	AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	147-155
7582515-12	1995	Full-length SLPI showed high affinity for heparin while the binding capacities of both half-length SLPIs were lower.	Heparin	42-49	secretory leukocyte peptidase inhibitor	Homo sapiens	12-16
7654030-1	1995	We investigated the in vitro effects of heparin on the growth and interaction of SW480 colon adenocarcinoma cells with the extracellular matrix proteins laminin, fibronectin and collagen IV.	Heparin	40-47	fibronectin 1	Homo sapiens	162-173
7654030-4	1995	SW480 cell adhesion to the matrix proteins and migration to laminin/fibronectin precoated filters were inhibited by heparin in a dose- dependent manner, whereas cell growth and invasion through collagen IV gel were not affected.	Heparin	116-123	fibronectin 1	Homo sapiens	68-79
7614042-2	1995	AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	147-155
7614042-2	1995	AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	147-155
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	116-124
7588083-5	1995	The role of heparin as adjunctive therapy to thrombolysis remains to be fully defined but heparin administration appears to be more important in conjunction with alteplase than with streptokinase.	Heparin	90-97	plasminogen activator, tissue type	Homo sapiens	162-171
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	148-156
7601314-3	1995	This molecule was identified as bFGF on the basis of its molecular weight, its affinity for heparin, and its capacity to induce plasminogen activator production in cultured endothelial GM 7373 cells.	Heparin	92-99	fibroblast growth factor 2	Bos taurus	32-36
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	116-124
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	148-156
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	116-124
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	coagulation factor II, thrombin	Homo sapiens	148-156
7630130-7	1995	The ability of the splenocytes to release IL-2 and IL-3 in response to mitogen was markedly improved in hemorrhaged animals which were treated with GM1892 or conventional heparin compared to saline-treated mice.	Heparin	171-178	interleukin 3	Mus musculus	51-55
7615164-9	1995	Chondroitin sulfate binds to a basic surface on thrombin that is also involved in heparin interaction.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	48-56
8537332-1	1995	Midkine (MK) is a heparin-binding growth factor and forms a novel protein family together with another member, pleiotrophin (PTN)/heparin-binding growth-associated molecule (HB-GAM).	Heparin	18-25	midkine S homeolog	Xenopus laevis	0-7
8537332-1	1995	Midkine (MK) is a heparin-binding growth factor and forms a novel protein family together with another member, pleiotrophin (PTN)/heparin-binding growth-associated molecule (HB-GAM).	Heparin	18-25	midkine S homeolog	Xenopus laevis	9-11
8590594-1	1995	High-affinity binding of basic fibroblast growth factor (bFGF) to the tyrosine kinase receptor requires cell-surface heparan sulfate proteoglycan or exogenous addition of heparin.	Heparin	171-178	fibroblast growth factor 2	Homo sapiens	25-55
7790396-10	1995	In this highly responsive cell system, heparin could potentiate the mitogenic activity of HARP at very low doses (0.1-1 microgram/ml) and inhibit this activity at concentrations of 10 micrograms/ml.	Heparin	39-46	pleiotrophin	Homo sapiens	90-94
8588942-0	1995	Characterization of the high affinity heparin binding site of the Alzheimer"s disease beta A4 amyloid precursor protein (APP) and its enhancement by zinc(II).	Heparin	38-45	amyloid beta precursor protein	Homo sapiens	94-119
8590594-1	1995	High-affinity binding of basic fibroblast growth factor (bFGF) to the tyrosine kinase receptor requires cell-surface heparan sulfate proteoglycan or exogenous addition of heparin.	Heparin	171-178	fibroblast growth factor 2	Homo sapiens	57-61
7630130-8	1995	Furthermore, the capacity of splenic and peritoneal macrophages to release IL-6 was restored in the hemorrhaged animals that received GM1892 or conventional heparin.	Heparin	157-164	interleukin 6	Mus musculus	75-79
8590594-2	1995	The crystal structure of bFGF shows Arg40 and 45 on the surface opposite to the heparin-binding region, suggesting that these charged residues may be involved in the receptor binding.	Heparin	80-87	fibroblast growth factor 2	Homo sapiens	25-29
7569739-8	1995	Plasma kallikrein (KK) values increased significantly with subsequent decreased levels of prekallikrein (PKK) and kallikrein inhibitor (KKI) after heparin injection.	Heparin	147-154	serine peptidase inhibitor Kazal type 6	Homo sapiens	114-134
7612663-0	1995	Regulation of the activity of human chymase during storage and release from mast cells: the contributions of inorganic cations, pH, heparin and histamine.	Heparin	132-139	chymase 1	Homo sapiens	36-43
7612663-3	1995	Chymase was purified from human skin by high salt extraction, cetylpyridinium chloride precipitation, heparin agarose affinity chromatography and gel filtration.	Heparin	102-109	chymase 1	Homo sapiens	0-7
7793988-6	1995	Binding of 125I-labeled perlecan to A beta (1-28) was strongly inhibited by isolated perlecan and to a lesser extent by heparin, but not by chondroitin-6-sulfate or unsulfated dextran sulfate.	Heparin	120-127	amyloid beta precursor protein	Homo sapiens	36-42
7793988-9	1995	A significant decrease in binding of EC-derived perlecan to A beta (1-28) was observed when a sequence within the putative heparin-binding motif of A beta (His13His14Gln15Lys16) was replaced by the uncharged peptide sequence, Gly13Gly14Gln15Gly16, indicating a perlecan binding site on A beta near the postulated alpha-secretase site (at Lys-16).	Heparin	123-130	amyloid beta precursor protein	Homo sapiens	60-66
7612663-7	1995	Heparin, which is stored with chymase in the mast cell granule, accentuated this difference by enhancing activity at pH 7.5 by 33% and depressing it a pH 5.5 by 40%.	Heparin	0-7	chymase 1	Homo sapiens	30-37
7793988-9	1995	A significant decrease in binding of EC-derived perlecan to A beta (1-28) was observed when a sequence within the putative heparin-binding motif of A beta (His13His14Gln15Lys16) was replaced by the uncharged peptide sequence, Gly13Gly14Gln15Gly16, indicating a perlecan binding site on A beta near the postulated alpha-secretase site (at Lys-16).	Heparin	123-130	amyloid beta precursor protein	Homo sapiens	148-154
7793988-9	1995	A significant decrease in binding of EC-derived perlecan to A beta (1-28) was observed when a sequence within the putative heparin-binding motif of A beta (His13His14Gln15Lys16) was replaced by the uncharged peptide sequence, Gly13Gly14Gln15Gly16, indicating a perlecan binding site on A beta near the postulated alpha-secretase site (at Lys-16).	Heparin	123-130	amyloid beta precursor protein	Homo sapiens	148-154
7612663-9	1995	It is concluded that pH and the interaction with heparin are central to the regulation of chymase activity within the granule and following release.	Heparin	49-56	chymase 1	Homo sapiens	90-97
7778166-10	1995	In the syngeneic grafts treated with both heparin derivatives, a significant reduction in the antigen expression of alpha-actin-containing smooth muscle cells in the intima, transforming growth factor-beta 1 both in the media and adventitia, and platelet-derived growth factor-beta receptors in the adventitia was observed immunohistochemically.	Heparin	42-49	transforming growth factor, beta 1	Rattus norvegicus	174-207
7797488-2	1995	VEGF165 possesses a heparin binding ability and in the absence of heparin-like molecules does not bind efficiently to the VEGF receptors of vascular endothelial cells.	Heparin	20-27	vascular endothelial growth factor A	Homo sapiens	0-4
7563224-3	1995	The myelin-associated glycoprotein (MAG), an adhesion molecule of the immunoglobulin (Ig) superfamily with five Ig-like domains, was investigated with regard to its binding site(s) for the neuronal cell surface, collagen I, and heparin, using a panel of new monoclonal antibodies and cyanogen bromide cleavage fragments of MAG.	Heparin	228-235	LOC103161439	Cricetulus griseus	4-34
7563224-3	1995	The myelin-associated glycoprotein (MAG), an adhesion molecule of the immunoglobulin (Ig) superfamily with five Ig-like domains, was investigated with regard to its binding site(s) for the neuronal cell surface, collagen I, and heparin, using a panel of new monoclonal antibodies and cyanogen bromide cleavage fragments of MAG.	Heparin	228-235	LOC103161439	Cricetulus griseus	36-39
7554525-5	1995	After switching from Sandoparin to unfractionated heparin we observed significant decreases in total cholesterol (from 168.6 +/- 42.2 to 154.4 +/- 41.9 mg/dl, p &lt; 0.02), LDL cholesterol (from 106.4 +/- 35.2 to 89.9 +/- 32.3 mg/dl, p &lt; 0.005), triglycerides (from 148.7 +/- 85.0 to 121.4 +/- 88.8 mg/dl, p &lt; 0.05) and apolipoprotein B (from 100.0 +/- 35.3 to 89.9 +/- 30.4 mg/dl, p &lt; 0.05) and a significant increase in HDL cholesterol (from 32.8 +/- 12.5 to 37.7 +/- 17.5 mg/dl, p &lt; 0.02).	Heparin	50-57	apolipoprotein B	Homo sapiens	326-342
7768918-0	1995	Influence of low molecular mass heparin on the kinetics of neutrophil elastase inhibition by mucus proteinase inhibitor.	Heparin	32-39	secretory leukocyte peptidase inhibitor	Homo sapiens	93-119
7768918-1	1995	Commercial low molecular mass heparin accelerates the inhibition of neutrophil elastase by mucus proteinase inhibitor, the predominant antielastase of lung secretions (Faller, B., Mely, Y., Gerard, D., and Bieth, J.G.	Heparin	30-37	secretory leukocyte peptidase inhibitor	Homo sapiens	91-117
7574361-4	1995	Thrombogenic substances are mostly composed of activated factor X or thrombin, which raises the problem of purity of the substances and determination of the antithrombotic activities of the substance tested, especially heparin and hirudin and their derivatives, and consequently their efficacy.	Heparin	219-226	coagulation factor II, thrombin	Homo sapiens	69-77
7627507-6	1995	There was evidence of postoperative heparin excess with an activated partial thromboplastin time ratio of 1.3 (range 0.9-3.0) versus 1.0 (range 1.0-1.2) in controls and an activated clotting time of 206 (range 143-280) versus 137 (range 107-142) s. This was confirmed by raised plasma heparin levels and a prolonged thrombin time normalized by protamine.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	316-324
7662997-4	1995	By molecular analysis of the EC-SOD coding region from the group II individuals in Sweden, a single nucleotide substitution of G to C generating an amino acid change of arginine to glycine has been identified in the region associated with the heparin affinity of the enzyme.	Heparin	243-250	superoxide dismutase 3	Homo sapiens	29-35
7796887-5	1995	The binding can also be almost completely inhibited by preincubation of the 125I-labeled RIHB with heparin or with a monoclonal antibody which recognizes the heparin binding site of both RIHB and HBNF.	Heparin	99-106	midkine (neurite growth-promoting factor 2)	Gallus gallus	89-93
7796887-5	1995	The binding can also be almost completely inhibited by preincubation of the 125I-labeled RIHB with heparin or with a monoclonal antibody which recognizes the heparin binding site of both RIHB and HBNF.	Heparin	158-165	midkine (neurite growth-promoting factor 2)	Gallus gallus	89-93
7796887-5	1995	The binding can also be almost completely inhibited by preincubation of the 125I-labeled RIHB with heparin or with a monoclonal antibody which recognizes the heparin binding site of both RIHB and HBNF.	Heparin	158-165	midkine (neurite growth-promoting factor 2)	Gallus gallus	187-191
7539816-4	1995	FGF-2 was extracted from maternal serum (MS), cord serum (CS), and AF by heparin-Sepharose affinity chromatography and subjected to Western blot analysis or quantified by specific RIA.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	0-5
7769270-6	1995	Addition of heparin with KGF produced a further increase in MMP-9 activity, with heparin alone having no effect.	Heparin	12-19	fibroblast growth factor 7	Homo sapiens	25-28
7769270-7	1995	Precoating of polycarbonate membranes with matrix components showed that fibronectin and an engineered poly-RGD molecule substrate were required for KGF plus heparin to increase MMP-9 activity.	Heparin	158-165	fibronectin 1	Homo sapiens	73-84
7662997-6	1995	The amino acid substitution may result in the decrease of the heparin affinity which is favorable for the existence of EC-SOD in the serum.	Heparin	62-69	superoxide dismutase 3	Homo sapiens	119-125
7744762-2	1995	O-Sulfation at C-3 of N-sulfated GlcN units concludes polymer modification and the formation of antithrombin binding regions in the biosynthesis of heparin/heparan sulfate.	Heparin	148-155	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7744733-1	1995	The collagen-tailed form of acetylcholinesterase (AChE) binds to heparin and heparan sulfate proteoglycans.	Heparin	65-72	acetylcholinesterase (Cartwright blood group)	Homo sapiens	50-54
7744733-2	1995	We have employed synthetic peptides corresponding to the central collagenic region of the tail of AChE, to identify the heparin-binding domains of the tail of asymmetric AChE.	Heparin	120-127	acetylcholinesterase (Cartwright blood group)	Homo sapiens	98-102
7774576-7	1995	Heparin activation of FGFR-4 or of a chimeric receptor bearing FGFR-4 ectodomain and FGFR-1 cytodomain triggers downstream tyrosine phosphorylation of several signaling proteins, and induces proliferation of cells bearing the chimeric receptor.	Heparin	0-7	fibroblast growth factor receptor 1	Homo sapiens	85-91
7774576-8	1995	Consistent with these findings, a soluble FGFR-4 ectodomain has strong FGF-independent affinity for immobilized heparin resin, while soluble FGFR-1 requires FGF for stable heparin interaction.	Heparin	172-179	fibroblast growth factor receptor 1	Homo sapiens	141-147
7744769-0	1995	VEGF121, a vascular endothelial growth factor (VEGF) isoform lacking heparin binding ability, requires cell-surface heparan sulfates for efficient binding to the VEGF receptors of human melanoma cells.	Heparin	69-76	vascular endothelial growth factor A	Homo sapiens	0-4
7744733-2	1995	We have employed synthetic peptides corresponding to the central collagenic region of the tail of AChE, to identify the heparin-binding domains of the tail of asymmetric AChE.	Heparin	120-127	acetylcholinesterase (Cartwright blood group)	Homo sapiens	170-174
7744733-4	1995	Peptides containing such sequences (P-(145-159) and P-(249-262)) were able to release asymmetric AChE bound to heparin-agarose.	Heparin	111-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	97-101
7744769-5	1995	Unexpectedly, heparin inhibited the binding of VEGF121 as well as the binding of VEGF165 to the VEGF receptors of the melanoma cells.	Heparin	14-21	vascular endothelial growth factor A	Homo sapiens	47-51
7744762-3	1995	The resulting GlcNSO3(3-OSO3) units are largely restricted to heparin chains with high affinity for antithrombin (HA heparin).	Heparin	62-69	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	100-112
7744769-10	1995	They also indicate that heparin is not able to fully substitute for cell surface-associated heparan sulfates since VEGF121 binding to the VEGF receptors of heparinase-treated cells is not restored by heparin.	Heparin	156-163	vascular endothelial growth factor A	Homo sapiens	115-119
7540413-1	1995	Monoclonal antibody (MoAb) B724 to von Willebrand factor (vWF) completely inhibits its interaction with heparin, sulphatides and botrocetin and consequently botrocetin-induced binding of vWF to platelets.	Heparin	104-111	von Willebrand factor	Homo sapiens	35-56
7762612-5	1995	Concomitant hirudin or antithrombin III plus heparin inhibited chemotaxis by thrombin when added up to 2 h after addition of thrombin.	Heparin	45-52	coagulation factor II, thrombin	Homo sapiens	77-85
7654938-2	1995	The purpose of the present study was to assess the influence of liposomes on these response to heparin of four coagulation tests: the kaolin-induced coagulation time, the tissue factor-induced coagulation time, the factor Xa-induced coagulation time, and the thrombin-induced coagulation time.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	259-267
7540413-1	1995	Monoclonal antibody (MoAb) B724 to von Willebrand factor (vWF) completely inhibits its interaction with heparin, sulphatides and botrocetin and consequently botrocetin-induced binding of vWF to platelets.	Heparin	104-111	von Willebrand factor	Homo sapiens	58-61
7706382-1	1995	Previous studies have indicated that heparin differentially regulates heparin-binding EGF-like growth factor (HB-EGF) and amphiregulin (AR) mitogenic activity.	Heparin	37-44	amphiregulin	Mus musculus	122-134
7537691-3	1995	Cross-linking experiments reveal that binding of FGF-1 to the hepatocyte cell surface receptors can be accomplished in the absence of exogenous heparin, in contrast to human endothelial cells for which it remains as a limiting factor.	Heparin	144-151	fibroblast growth factor 1	Homo sapiens	49-54
7657726-4	1995	Human bone cells attached to fragments from each of the cell- and heparin-binding regions of fibronectin, but failed to attach to a fragment from the gelatin-binding region.	Heparin	66-73	fibronectin 1	Homo sapiens	93-104
7657726-7	1995	Monoclonal antibody, MAb 32, which binds to the heparin-binding region of fibronectin, failed to inhibit attachment of the human bone cells to fibronectin but reduced the attachment of these cells to the heparin-binding region fragment.	Heparin	48-55	fibronectin 1	Homo sapiens	74-85
7657726-7	1995	Monoclonal antibody, MAb 32, which binds to the heparin-binding region of fibronectin, failed to inhibit attachment of the human bone cells to fibronectin but reduced the attachment of these cells to the heparin-binding region fragment.	Heparin	204-211	fibronectin 1	Homo sapiens	74-85
7657726-8	1995	Heparin and chondroitin sulphate were able to inhibit human bone cell attachment to the heparin-binding fragment of fibronectin but had no effect on their attachment to intact fibronectin or the cell-binding region of fibronectin.	Heparin	0-7	fibronectin 1	Homo sapiens	116-127
7657726-8	1995	Heparin and chondroitin sulphate were able to inhibit human bone cell attachment to the heparin-binding fragment of fibronectin but had no effect on their attachment to intact fibronectin or the cell-binding region of fibronectin.	Heparin	88-95	fibronectin 1	Homo sapiens	116-127
8589262-2	1995	IL-7 binds to heparin and heparan sulfate, to a lesser extent to dermatan sulfate and does not bind to chondroitin sulfate.	Heparin	14-21	interleukin 7	Mus musculus	0-4
8589262-4	1995	We also measured the affinity of IL-7 for heparin using an affinity co-electrophoresis method and found an affinity of 25 nM.	Heparin	42-49	interleukin 7	Mus musculus	33-37
8589262-6	1995	However, addition of heparin to cultures of an IL-7-dependent pre-B cell line (2E8) inhibited IL-7-stimulated proliferation and IL-7 complexed with heparin was more resistant than free IL-7 to protease treatment.	Heparin	21-28	interleukin 7	Mus musculus	47-51
8589262-6	1995	However, addition of heparin to cultures of an IL-7-dependent pre-B cell line (2E8) inhibited IL-7-stimulated proliferation and IL-7 complexed with heparin was more resistant than free IL-7 to protease treatment.	Heparin	21-28	interleukin 7	Mus musculus	94-98
8589262-6	1995	However, addition of heparin to cultures of an IL-7-dependent pre-B cell line (2E8) inhibited IL-7-stimulated proliferation and IL-7 complexed with heparin was more resistant than free IL-7 to protease treatment.	Heparin	21-28	interleukin 7	Mus musculus	94-98
8589262-6	1995	However, addition of heparin to cultures of an IL-7-dependent pre-B cell line (2E8) inhibited IL-7-stimulated proliferation and IL-7 complexed with heparin was more resistant than free IL-7 to protease treatment.	Heparin	21-28	interleukin 7	Mus musculus	94-98
8589262-6	1995	However, addition of heparin to cultures of an IL-7-dependent pre-B cell line (2E8) inhibited IL-7-stimulated proliferation and IL-7 complexed with heparin was more resistant than free IL-7 to protease treatment.	Heparin	148-155	interleukin 7	Mus musculus	47-51
8589262-7	1995	Taken together, these results suggest that heparin may act as a carrier for IL-7, blocking its interaction with target cells and protecting it from degradation during transit.	Heparin	43-50	interleukin 7	Mus musculus	76-80
7607582-2	1995	We compared the value of heparin-induced extracorporeal LDL precipitation (HELP) which is a method that safely and effectively reduces plasma fibrinogen and lipoproteins and so improves the hemorheologic pattern and blood flow properties.	Heparin	25-32	fibrinogen beta chain	Homo sapiens	142-152
7730030-7	1995	Both the 70-to 85-kDa and the 55-kDa proteins were precipitated by FGF-2 heparin-Sepharose but not by heparin-Sepharose alone, suggesting that the interaction was dependent on the presence of FGF-2.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	67-72
7730030-7	1995	Both the 70-to 85-kDa and the 55-kDa proteins were precipitated by FGF-2 heparin-Sepharose but not by heparin-Sepharose alone, suggesting that the interaction was dependent on the presence of FGF-2.	Heparin	73-80	fibroblast growth factor 2	Homo sapiens	192-197
7706383-2	1995	Both AR and HB-EGF share with EGF the ability to interact with the type-1 EGF receptor; however, AR and HB-EGF differ from EGF in that both of these mitogens bind to heparin while EGF does not.	Heparin	166-173	amphiregulin	Mus musculus	5-7
7706383-2	1995	Both AR and HB-EGF share with EGF the ability to interact with the type-1 EGF receptor; however, AR and HB-EGF differ from EGF in that both of these mitogens bind to heparin while EGF does not.	Heparin	166-173	amphiregulin	Mus musculus	97-99
7706382-1	1995	Previous studies have indicated that heparin differentially regulates heparin-binding EGF-like growth factor (HB-EGF) and amphiregulin (AR) mitogenic activity.	Heparin	37-44	amphiregulin	Mus musculus	136-138
7706382-3	1995	The results of our present investigation demonstrated that AR-mediated mitogenic activity in the murine AKR-2B fibroblast-like cell line was inhibited by heparin, while HB-EGF activity was enhanced.	Heparin	154-161	amphiregulin	Mus musculus	59-61
7748810-2	1995	In hormone-dependent MCF-7 breast cancer cells, Decapeptyl can inhibit sulfatase activity, and this effect is significantly augmented in the presence of heparin.	Heparin	153-160	arylsulfatase family member H	Homo sapiens	71-80
7731256-2	1995	Heparin has an important adjunctive role in enhancing early vessel patency in patients who receive tissue-type plasminogen activator and in decreasing the frequency of reocclusion of an infarct-related artery during any thrombolytic therapy.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	99-132
8587067-4	1995	Similar matrix depletion could be induced by collagen VI, cell binding (120 k) and heparin binding (60 k) fragments of Fn, but not by gelatin binding fragment (45 k).	Heparin	83-90	fibronectin 1	Homo sapiens	119-121
7748810-3	1995	In the other hormone-dependent T-47D breast cancer cell line, the decrease of sulfatase activity was only significant when Decapeptyl was associated with heparin.	Heparin	154-161	arylsulfatase family member H	Homo sapiens	78-87
7748810-5	1995	TGF-alpha stimulates sulfatase activity in the MDA-MB-231 cells but has no effect in the MCF-7 cells; in contrast, TGF-alpha combined with heparin provokes a decrease of the sulfatase activity in both cell lines.	Heparin	139-146	arylsulfatase family member H	Homo sapiens	21-30
7748810-5	1995	TGF-alpha stimulates sulfatase activity in the MDA-MB-231 cells but has no effect in the MCF-7 cells; in contrast, TGF-alpha combined with heparin provokes a decrease of the sulfatase activity in both cell lines.	Heparin	139-146	arylsulfatase family member H	Homo sapiens	174-183
7748810-6	1995	It is concluded that the sulfatase activity in some types of breast cancer cell can be inhibited by heparin combined with the polypeptides Decapeptyl or TGF-alpha.	Heparin	100-107	arylsulfatase family member H	Homo sapiens	25-34
7717977-0	1995	Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low-density-lipoprotein-receptor-related protein by heparin fragments.	Heparin	13-20	LDL receptor related protein 1	Homo sapiens	121-151
7721852-6	1995	Its binding to LRP is inhibited by the 39-kDa receptor-associated protein (RAP), a known LRP antagonist, and by heparin.	Heparin	112-119	LDL receptor related protein 1	Homo sapiens	15-18
7703488-3	1995	Plasma, anticoagulated with low-molecular-weight heparin allowing tissue factor-dependent prothrombin activation, was perfused at a wall shear rate of 100 s-1 over tissue factor containing matrices of stimulated endothelial cells placed in a perfusion chamber.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	90-101
7717977-0	1995	Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low-density-lipoprotein-receptor-related protein by heparin fragments.	Heparin	204-211	LDL receptor related protein 1	Homo sapiens	121-151
7717977-8	1995	Heparin inhibits binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein.	Heparin	0-7	LDL receptor related protein 1	Homo sapiens	50-80
7717977-11	1995	This indicates that the inhibition of the binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein by heparin is exclusively mediated by binding of heparin to lipoprotein lipase.	Heparin	158-165	LDL receptor related protein 1	Homo sapiens	75-105
7717977-11	1995	This indicates that the inhibition of the binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein by heparin is exclusively mediated by binding of heparin to lipoprotein lipase.	Heparin	204-211	LDL receptor related protein 1	Homo sapiens	75-105
7538066-4	1995	Heparin caused extra epithelial growth in cooperation with aFGF, but its use resulted in luminal expansion instead of enhanced branching.	Heparin	0-7	fibroblast growth factor 1	Mus musculus	59-63
7895349-0	1995	Rebound increase in thrombin generation and activity after cessation of intravenous heparin in patients with acute coronary syndromes.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	20-28
7895349-3	1995	This study was designed to determine whether there is a true rebound, as defined by an increase followed by a subsequent decrease, in thrombin activity after discontinuation of intravenous heparin therapy.	Heparin	189-196	coagulation factor II, thrombin	Homo sapiens	134-142
7599930-0	1995	Heparin-insensitive calcium release from intracellular stores triggered by the recombinant human parathyroid hormone receptor.	Heparin	0-7	parathyroid hormone	Homo sapiens	97-116
7698249-0	1995	Binding site in human plasma fibronectin to HL-60 cells localizes in the C-terminal heparin-binding region independently of RGD and CS1.	Heparin	84-91	fibronectin 1	Homo sapiens	29-40
7698249-1	1995	A 29-kDa monomeric dispase-digestive fragment of human plasma fibronectin has been purified by heparin affinity chromatography.	Heparin	95-102	fibronectin 1	Homo sapiens	62-73
7698249-12	1995	These results indicate that the C-terminal cell- and heparin-binding domain of fibronectin mediates HL-60 cell binding by direct interaction independently of RGD, CS1, and melanoma cell adhesion domains in this fragment.	Heparin	53-60	fibronectin 1	Homo sapiens	79-90
7598914-1	1995	The effect of heparin-induced capacitation on the intracellular pH (pHi) of individual bovine sperm was determined with image analysis.	Heparin	14-21	glucose-6-phosphate isomerase	Bos taurus	68-71
7714817-3	1995	We undertook the present study to examine in an in vitro system the mechanism by which heparin might modulate the effects of ANG II and ET-1 on MC proliferation and MC uptake of immunoglobulin G (IgG) complexes.	Heparin	87-94	angiotensinogen	Homo sapiens	125-131
7714817-3	1995	We undertook the present study to examine in an in vitro system the mechanism by which heparin might modulate the effects of ANG II and ET-1 on MC proliferation and MC uptake of immunoglobulin G (IgG) complexes.	Heparin	87-94	endothelin 1	Homo sapiens	136-140
7714817-6	1995	ET-1 also was found to significantly increase MC uptake of IgG complexes (P &lt; .02), and this increase also was significantly antagonized by coincubation with heparin (P &lt; .02).	Heparin	161-168	endothelin 1	Homo sapiens	0-4
7714817-8	1995	MC [3H]thymidine incorporation was significantly enhanced by both ANG II (P &lt; .01) and ET-1 (P &lt; .001) and these mitogenic effects were significantly attenuated by coincubation of cells with heparin (P &lt; .01 and P &lt; .001, respectively).	Heparin	197-204	angiotensinogen	Homo sapiens	66-72
7714817-8	1995	MC [3H]thymidine incorporation was significantly enhanced by both ANG II (P &lt; .01) and ET-1 (P &lt; .001) and these mitogenic effects were significantly attenuated by coincubation of cells with heparin (P &lt; .01 and P &lt; .001, respectively).	Heparin	197-204	endothelin 1	Homo sapiens	90-94
9049329-8	1995	Phosphorylation of this Nef-associated protein was inhibited by heparin and is thus likely to be mediated by casein kinase II.	Heparin	64-71	S100 calcium binding protein B	Homo sapiens	24-27
7598914-9	1995	Following an NH4Cl-induced alkaline load, the pHi of both control- and heparin-treated sperm recovered toward the resting pHi with a half-time of recovery of 1.5-1.7 min.	Heparin	71-78	glucose-6-phosphate isomerase	Bos taurus	46-49
7598914-9	1995	Following an NH4Cl-induced alkaline load, the pHi of both control- and heparin-treated sperm recovered toward the resting pHi with a half-time of recovery of 1.5-1.7 min.	Heparin	71-78	glucose-6-phosphate isomerase	Bos taurus	122-125
7598914-5	1995	An increase in sperm head pHi was seen in heparin-treated sperm at 3, 4, and 5 h of incubation relative to sperm incubated without heparin (control, P &lt; 0.05).	Heparin	42-49	glucose-6-phosphate isomerase	Bos taurus	26-29
7598914-12	1995	Capacitation by heparin was associated with an 81% decrease in v(i) at a pHi of 7.00, but there was no effect of capacitation on the proton buffering power of the sperm, which was 87 +/- 8 mM/pH unit.	Heparin	16-23	glucose-6-phosphate isomerase	Bos taurus	73-76
7598914-6	1995	At 5 h of incubation, the pHi in heparin-treated sperm was 6.92 +/- 0.07, while control-treated sperm pHi was 6.70 +/- 0.03.	Heparin	33-40	glucose-6-phosphate isomerase	Bos taurus	26-29
7598914-13	1995	Results demonstrate that both the regulation of pHi and resting pHi were altered during capacitation of bovine sperm by heparin.	Heparin	120-127	glucose-6-phosphate isomerase	Bos taurus	48-51
7598914-13	1995	Results demonstrate that both the regulation of pHi and resting pHi were altered during capacitation of bovine sperm by heparin.	Heparin	120-127	glucose-6-phosphate isomerase	Bos taurus	64-67
7598914-7	1995	Initially a normal frequency distribution was seen for sperm pHi in both heparin- and control-treated sperm.	Heparin	73-80	glucose-6-phosphate isomerase	Bos taurus	61-64
7495073-9	1995	The heparin-independent inhibition of prothrombinase by antithrombin (4 microM) in the presence of prothrombin (0.2 microM) was virtually negligible.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	38-49
7705397-0	1995	Heparin inhibits the antiparasitic and immune modulatory effects of human recombinant interferon-gamma.	Heparin	0-7	interferon gamma	Homo sapiens	86-102
7495084-7	1995	Addition of heparin or ECGS (endothelial cell growth supplement) decreased the von Willebrand factor content in the matrix.	Heparin	12-19	von Willebrand factor	Homo sapiens	79-100
7648516-2	1995	The administration of fructose (10% solution in the drinking water for 4 days) to rats produced hypertriglyceridemia, but heparin-releasable LPL activity from perfused hearts and total and heparin-releasable LPL activities in isolated cardiomyocytes were not reduced.	Heparin	122-129	lipoprotein lipase	Rattus norvegicus	141-144
7648516-2	1995	The administration of fructose (10% solution in the drinking water for 4 days) to rats produced hypertriglyceridemia, but heparin-releasable LPL activity from perfused hearts and total and heparin-releasable LPL activities in isolated cardiomyocytes were not reduced.	Heparin	189-196	lipoprotein lipase	Rattus norvegicus	208-211
7648516-6	1995	Thus, the selective reduction in heparin-releasable LPL activity in perfused diabetic hearts is probably not the consequence of displacement by LPC, a lipolytic product of the LPL-catalyzed degradation of triacylglycerol-rich lipoproteins.	Heparin	33-40	lipoprotein lipase	Rattus norvegicus	52-55
7648516-7	1995	Circulating LPL activity in the plasma of diabetic rats was not decreased relative to control plasma enzyme activity; therefore, the reduction in heparin-releasable LPL activity is not because circulating LPL was less available for uptake by the endothelium in diabetic hearts.	Heparin	146-153	lipoprotein lipase	Rattus norvegicus	165-168
7648516-7	1995	Circulating LPL activity in the plasma of diabetic rats was not decreased relative to control plasma enzyme activity; therefore, the reduction in heparin-releasable LPL activity is not because circulating LPL was less available for uptake by the endothelium in diabetic hearts.	Heparin	146-153	lipoprotein lipase	Rattus norvegicus	165-168
7778065-7	1995	Heparin and Zn2+ were found to further augment each other"s ability to stimulate the inhibition of FXIa by PN-2/A beta PP.	Heparin	0-7	amyloid beta precursor protein	Homo sapiens	107-111
7535010-7	1995	Dialysis of cells with heparin (5 mg/ml) completely blocked SP-induced inward current but not BHQ-induced current.	Heparin	23-30	tachykinin precursor 1	Homo sapiens	60-62
7887980-7	1995	Our results demonstrate that low M(r) heparin fragments can modulate the steady-state levels of type III collagen and fibronectin mRNAs.	Heparin	38-45	fibronectin 1	Homo sapiens	118-129
7532589-1	1995	Recently we reported that carboxyl-reduced heparin (CR-heparin), despite binding acidic fibroblast growth factor (aFGF) as effectively as native heparin, was much less potent at augmenting aFGF-induced mitogenesis.	Heparin	43-50	fibroblast growth factor 1	Mus musculus	81-112
7532589-1	1995	Recently we reported that carboxyl-reduced heparin (CR-heparin), despite binding acidic fibroblast growth factor (aFGF) as effectively as native heparin, was much less potent at augmenting aFGF-induced mitogenesis.	Heparin	43-50	fibroblast growth factor 1	Mus musculus	114-118
7532589-1	1995	Recently we reported that carboxyl-reduced heparin (CR-heparin), despite binding acidic fibroblast growth factor (aFGF) as effectively as native heparin, was much less potent at augmenting aFGF-induced mitogenesis.	Heparin	43-50	fibroblast growth factor 1	Mus musculus	189-193
7532589-2	1995	This paper describes experiments which examined this phenomenon in more detail in the hope that it would shed light on the mechanism by which heparin potentiates aFGF activity.	Heparin	142-149	fibroblast growth factor 1	Mus musculus	162-166
7532589-3	1995	Initial studies confirmed that heparin, with 60% of its carboxyl groups reduced, although binding aFGF with the same affinity as native heparin (Kd 35 +/- 5 nM), was a poor potentiator of aFGF-induced mitogenic activity.	Heparin	31-38	fibroblast growth factor 1	Mus musculus	188-192
7532589-4	1995	Proteolysis protection experiments also revealed that CR-heparin was as effective as native heparin at protecting aFGF from proteolytic degradation.	Heparin	57-64	fibroblast growth factor 1	Mus musculus	114-118
7796831-9	1995	Finally (and obviously), intravenous fibrinolytic agents or heparin-induced extracorporeal low-density lipoprotein precipitation will lower fibrinogen dramatically; yet these procedures are rarely indicated for this purpose alone.	Heparin	60-67	fibrinogen beta chain	Homo sapiens	140-150
7705397-3	1995	Furthermore, it has been shown that IFN-gamma binds with a great affinity to the heparin-like structure of heparan sulfate, which is localized in basement membranes and on cell surfaces.	Heparin	81-88	interferon gamma	Homo sapiens	36-45
7532589-5	1995	In contrast, CR-heparin was considerably less effective than native heparin at enhancing the binding of aFGF to the fibroblast growth factor receptor (FGFR) on 3T3 cells.	Heparin	16-23	fibroblast growth factor 1	Mus musculus	104-108
7532589-7	1995	Based on these data, it is proposed that CR-heparin is less efficient than heparin at facilitating the formation of a quaternary complex among aFGF, the FGFR, and cell surface heparin receptors.	Heparin	44-51	fibroblast growth factor 1	Mus musculus	143-147
7705397-4	1995	In this study, we analyze the effect of heparin and heparan sulfate on three different IFN-gamma-mediated activities inducible in human glioblastoma cells (87HG31 and 86HG39).	Heparin	40-47	interferon gamma	Homo sapiens	87-96
7705397-5	1995	We find firstly that heparin is able to inhibit IFN-gamma-mediated induction of major histocompatibility complex (MHC) class II antigen expression on 87HG31 cells, an effect which can be abrogated by protamine.	Heparin	21-28	interferon gamma	Homo sapiens	48-57
7705397-6	1995	Secondly, we show that heparin inhibits the IFN-gamma-induced toxoplasmostasis within 86HG39 cells in a dose-dependent fashion, and thirdly that heparin inhibits the IFN-gamma-mediated induction of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase.	Heparin	23-30	interferon gamma	Homo sapiens	44-53
7705397-6	1995	Secondly, we show that heparin inhibits the IFN-gamma-induced toxoplasmostasis within 86HG39 cells in a dose-dependent fashion, and thirdly that heparin inhibits the IFN-gamma-mediated induction of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase.	Heparin	23-30	interferon gamma	Homo sapiens	166-175
7705397-6	1995	Secondly, we show that heparin inhibits the IFN-gamma-induced toxoplasmostasis within 86HG39 cells in a dose-dependent fashion, and thirdly that heparin inhibits the IFN-gamma-mediated induction of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase.	Heparin	145-152	interferon gamma	Homo sapiens	44-53
7705397-6	1995	Secondly, we show that heparin inhibits the IFN-gamma-induced toxoplasmostasis within 86HG39 cells in a dose-dependent fashion, and thirdly that heparin inhibits the IFN-gamma-mediated induction of the tryptophan-degrading enzyme indoleamine 2,3-dioxygenase.	Heparin	145-152	interferon gamma	Homo sapiens	166-175
7705397-8	1995	The possible mechanism of heparin-induced inhibition of IFN-gamma is discussed.	Heparin	26-33	interferon gamma	Homo sapiens	56-65
7867715-5	1995	The preincubation of the cells with heparitinase I resulted in significant inhibition of chemotactic migration to FN and its fragments containing the III13 and/or III14 modules of the heparin-binding domain.	Heparin	184-191	fibronectin 1	Homo sapiens	114-116
7867715-7	1995	Thus, the spread and migration responses of HT1080 cells onto FN fusion peptides require the adjacent coexistence of cell- and heparin-binding domains and are mediated by the interactions between cell surface heparan sulfate and the heparin-binding domain, in concert with the interaction between cell surface integrin and the cell-binding domain.	Heparin	127-134	fibronectin 1	Homo sapiens	62-64
7867715-7	1995	Thus, the spread and migration responses of HT1080 cells onto FN fusion peptides require the adjacent coexistence of cell- and heparin-binding domains and are mediated by the interactions between cell surface heparan sulfate and the heparin-binding domain, in concert with the interaction between cell surface integrin and the cell-binding domain.	Heparin	233-240	fibronectin 1	Homo sapiens	62-64
7538367-3	1995	Of the 6 IGFBPs, IGFBP-3 and IGFBP-5 had the greatest heparin affinity.	Heparin	54-61	insulin like growth factor binding protein 5	Homo sapiens	29-36
7860647-9	1995	M1Q-bFGF also induced an increase in cell-associated uPA activity only when added to the cell cultures in the presence of soluble heparin.	Heparin	130-137	fibroblast growth factor 2	Bos taurus	4-8
7745195-4	1995	The purpose of this study was to determine if the application of ice to subcutaneous heparin injection sites decreases the incidence and size of haematoma formation and/or minimizes patient discomfort.	Heparin	85-92	carboxylesterase 2	Homo sapiens	65-68
7860920-3	1995	In this study, adequate anticoagulation was defined as the amount of heparin needed to prevent a significant increase in serum fibrinopeptide A, a sensitive marker for thrombin activity.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	168-176
7860920-12	1995	CONCLUSIONS: Administration of a heparin bolus to maintain an activated clotting time &gt; 200 s prevented a significant increase in thrombin activity.	Heparin	33-40	coagulation factor II, thrombin	Homo sapiens	133-141
7775863-0	1995	Apolipoprotein E isoforms and rare mutations: parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia.	Heparin	92-99	apolipoprotein E	Homo sapiens	0-16
7883954-0	1995	Heparin-enhanced plasma phospholipase A2 activity and prostacyclin synthesis in patients undergoing cardiac surgery.	Heparin	0-7	phospholipase A2 group IB	Homo sapiens	24-40
7883954-6	1995	Protamine, administered to neutralize the heparin, caused an acute reduction of both plasma PLA2 activity and plasma 6-keto-PGF1 alpha, but no change in plasma TXB2 concentrations.	Heparin	42-49	phospholipase A2 group IB	Homo sapiens	92-96
7883954-8	1995	Enhanced plasma PLA2 activity was also measured in patients with lower doses of heparin used clinically for nonsurgical applications.	Heparin	80-87	phospholipase A2 group IB	Homo sapiens	16-20
7883954-9	1995	Human plasma PLA2 was identified as group II PLA2 by its sensitivity to deoxycholate and dithiothreitol, its substrate specificity, and its elution characteristics on heparin affinity chromatography.	Heparin	167-174	phospholipase A2 group IB	Homo sapiens	13-17
7883954-9	1995	Human plasma PLA2 was identified as group II PLA2 by its sensitivity to deoxycholate and dithiothreitol, its substrate specificity, and its elution characteristics on heparin affinity chromatography.	Heparin	167-174	phospholipase A2 group IB	Homo sapiens	45-49
7883954-10	1995	Heparin addition to PMNs in vitro resulted in dose-dependent increases in cellular PLA2 activity and release of PLA2.	Heparin	0-7	phospholipase A2 group IB	Homo sapiens	83-87
7883954-10	1995	Heparin addition to PMNs in vitro resulted in dose-dependent increases in cellular PLA2 activity and release of PLA2.	Heparin	0-7	phospholipase A2 group IB	Homo sapiens	112-116
7775863-5	1995	Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%).	Heparin	0-7	apolipoprotein E	Homo sapiens	100-106
7775863-5	1995	Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%).	Heparin	0-7	apolipoprotein E	Homo sapiens	122-128
7775863-5	1995	Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%).	Heparin	0-7	apolipoprotein E	Homo sapiens	100-104
7775863-5	1995	Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%).	Heparin	0-7	apolipoprotein E	Homo sapiens	122-126
7775863-7	1995	The functionally dominant mutation apoE-1(146) was most defective in heparin binding studies in vitro.	Heparin	69-76	apolipoprotein E	Homo sapiens	35-39
7545318-2	1995	Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical uses of heparin.	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	4-12
7545318-2	1995	Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical uses of heparin.	Heparin	142-149	coagulation factor II, thrombin	Homo sapiens	4-12
7763192-3	1995	The effects on bradykinin generation were compared between heparin and NM.	Heparin	59-66	kininogen 1	Homo sapiens	15-25
7863966-2	1995	Heparin is a potent inhibitor of thrombin and thrombin generation, but its ability to accelerate thrombolysis, prevent acute reocclusion after vascular injury in angioplasty, and prevent myocardial infarction in unstable angina is relatively limited, possibly because clot-bound thrombin plays an important role in these clinical situations.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	33-41
7863966-2	1995	Heparin is a potent inhibitor of thrombin and thrombin generation, but its ability to accelerate thrombolysis, prevent acute reocclusion after vascular injury in angioplasty, and prevent myocardial infarction in unstable angina is relatively limited, possibly because clot-bound thrombin plays an important role in these clinical situations.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	46-54
7863966-2	1995	Heparin is a potent inhibitor of thrombin and thrombin generation, but its ability to accelerate thrombolysis, prevent acute reocclusion after vascular injury in angioplasty, and prevent myocardial infarction in unstable angina is relatively limited, possibly because clot-bound thrombin plays an important role in these clinical situations.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	46-54
7863966-3	1995	Thus, when thrombin binds to fibrin, it remains enzymatically active and relatively impervious to inactivation by heparin or other fluid-phase inhibitors.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	11-19
7864806-1	1995	Phospholipase A2 (PLA2) activity was purified 12,544-fold with a 13% yield from the plasma of patients diagnosed of septic shock by the sequential use of heparin-agarose affinity chromatography, gel filtration, and reverse-phase f.p.l.c.	Heparin	154-161	phospholipase A2 group IB	Homo sapiens	0-16
7864806-1	1995	Phospholipase A2 (PLA2) activity was purified 12,544-fold with a 13% yield from the plasma of patients diagnosed of septic shock by the sequential use of heparin-agarose affinity chromatography, gel filtration, and reverse-phase f.p.l.c.	Heparin	154-161	phospholipase A2 group IB	Homo sapiens	18-22
7873546-0	1995	Mapping the heparin-binding site of mucus proteinase inhibitor.	Heparin	12-19	secretory leukocyte peptidase inhibitor	Homo sapiens	36-62
7873546-1	1995	Heparin accelerates the inhibition of neutrophil elastase by mucus proteinase inhibitor (MPI), the physiological antielastase of airways as a result of its binding with the inhibitor [Faller, B., Mely, Y., Gerard, D., &amp; Bieth, J. G. (1992) Biochemistry 31, 8285-8290].	Heparin	0-7	secretory leukocyte peptidase inhibitor	Homo sapiens	61-87
7873546-1	1995	Heparin accelerates the inhibition of neutrophil elastase by mucus proteinase inhibitor (MPI), the physiological antielastase of airways as a result of its binding with the inhibitor [Faller, B., Mely, Y., Gerard, D., &amp; Bieth, J. G. (1992) Biochemistry 31, 8285-8290].	Heparin	0-7	secretory leukocyte peptidase inhibitor	Homo sapiens	89-92
7873546-2	1995	To explore the heparin-binding site of the inhibitor, we have modified the lysine and arginine residues of MPI and its isolated C-terminal domain by using 4-N,N-(dimethylamino)azobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC) [Chang, J. Y.	Heparin	15-22	secretory leukocyte peptidase inhibitor	Homo sapiens	107-110
7873546-10	1995	Modification of a limited number of lysine and arginine residues in full-length MPI led to a 6-fold decrease in affinity for heparin.	Heparin	125-132	secretory leukocyte peptidase inhibitor	Homo sapiens	80-83
7873546-12	1995	Amino acid sequencing unambiguously identified the heparin-protected lysines as Lys 13 and Lys 87, located on the N-terminal and C-terminal domains of MPI, respectively.	Heparin	51-58	secretory leukocyte peptidase inhibitor	Homo sapiens	151-154
7843907-8	1995	The anti-beta 1 antibody inhibited cell adhesion to heparin-binding peptides of type IV collagen, type IV collagen, fibronectin, and GRGDSP: Antibodies to the alpha 2 integrin subunit inhibited cell adhesion to the heparin-binding peptides of type IV collagen and slightly inhibited cell adhesion to intact type IV.	Heparin	52-59	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	9-15
7532176-4	1995	b-FGF and HB-EGF binding to HS-modified CD44 was eliminated by pretreating the protein with heparitinase or by blocking with free heparin.	Heparin	130-137	fibroblast growth factor 2	Homo sapiens	0-5
7744578-12	1995	The antimetastatic and anticoagulant activities of heparin were unrelated, as indicated by using heparin fractions with high and low affinity for antithrombin III.	Heparin	97-104	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	146-162
7531794-4	1995	bFGF is known to be capable of binding to heparin, and our data demonstrate bFGF in mast cells (MCs) that also produce many other mediators (including heparin) important for wound healing and angiogenesis.	Heparin	42-49	fibroblast growth factor 2	Homo sapiens	0-4
7608124-4	1995	Short-pulse and pulse-chase experiments revealed that heparin inhibited the secretion of type I procollagen and stimulated the accumulation of type I collagen in the extracellular space.	Heparin	54-61	collagen type I alpha 2 chain	Homo sapiens	89-107
7844473-8	1995	Inhibition of ellagic acid-induced activation of Hageman factor by both forms of amyloid precursor protein was enhanced by heparin.	Heparin	123-130	amyloid beta precursor protein	Homo sapiens	81-106
7860635-11	1995	Furthermore, our results show that a fragment comprising site B8 and the most COOH-terminal G-like domain is sufficient for this activity, and that agrin domains required for binding to heparin and those for AChR aggregation are distinct from each other.	Heparin	186-193	agrin	Gallus gallus	148-153
7861244-2	1995	Lipoprotein lipase was extracted into the incubation medium by heparin release of lipoprotein lipase and measured by fatty acid release from a glyceroltriolein emulsion.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	0-18
7861244-2	1995	Lipoprotein lipase was extracted into the incubation medium by heparin release of lipoprotein lipase and measured by fatty acid release from a glyceroltriolein emulsion.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	82-100
7531794-4	1995	bFGF is known to be capable of binding to heparin, and our data demonstrate bFGF in mast cells (MCs) that also produce many other mediators (including heparin) important for wound healing and angiogenesis.	Heparin	151-158	fibroblast growth factor 2	Homo sapiens	76-80
7531794-8	1995	bFGF protein was also detected in MCs, but the intensity of labeling was dependent on prior treatment of the tissues with heparinase, suggesting that epitopes recognized by the bFGF-specific antiserum were masked by endogenous heparin.	Heparin	122-129	fibroblast growth factor 2	Homo sapiens	0-4
7531794-8	1995	bFGF protein was also detected in MCs, but the intensity of labeling was dependent on prior treatment of the tissues with heparinase, suggesting that epitopes recognized by the bFGF-specific antiserum were masked by endogenous heparin.	Heparin	122-129	fibroblast growth factor 2	Homo sapiens	177-181
7531794-9	1995	CONCLUSIONS: The results further elucidate the mechanism of involvement of MCs in tissue repair and angiogenesis and suggest that bFGF produced by MCs is bound to intracellular heparin.	Heparin	177-184	fibroblast growth factor 2	Homo sapiens	130-134
7531794-10	1995	Thus, it seems possible that release of heparin by degranulation from MCs also may result in the release of biologically active bFGF in vivo.	Heparin	40-47	fibroblast growth factor 2	Homo sapiens	128-132
7811995-3	1995	In this report, we provide evidence that lactoferrin has a potent heparin-neutralizing activity during thrombin inhibition by the serine proteinase inhibitors (serpins) antithrombin and heparin co-factor II.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	103-111
7811995-6	1995	Treatment of whole blood with specific inflammatory mediators, fMLP, lipopolysaccharide (LPS), and tumor necrosis factor-alpha (TNF-alpha) increased the concentration of both plasma lactoferrin and platelet factor 4 while inhibiting the blood anticoagulant activity of heparin as measured by the aPTT.	Heparin	269-276	formyl peptide receptor 1	Homo sapiens	63-67
7811995-6	1995	Treatment of whole blood with specific inflammatory mediators, fMLP, lipopolysaccharide (LPS), and tumor necrosis factor-alpha (TNF-alpha) increased the concentration of both plasma lactoferrin and platelet factor 4 while inhibiting the blood anticoagulant activity of heparin as measured by the aPTT.	Heparin	269-276	tumor necrosis factor	Homo sapiens	99-126
7811995-6	1995	Treatment of whole blood with specific inflammatory mediators, fMLP, lipopolysaccharide (LPS), and tumor necrosis factor-alpha (TNF-alpha) increased the concentration of both plasma lactoferrin and platelet factor 4 while inhibiting the blood anticoagulant activity of heparin as measured by the aPTT.	Heparin	269-276	tumor necrosis factor	Homo sapiens	128-137
7661690-8	1995	Human cytomegalovirus infection in differentiated THP-1 cells and in human fibroblasts was inhibited by incubation of the virus with 20 micrograms/ml of heparin before and during the adsorption period.	Heparin	153-160	GLI family zinc finger 2	Homo sapiens	50-55
7529229-1	1995	Fibroblast growth factor (FGF)-1 is released from NIH 3T3 cells in response to heat shock as a biologically inactive protein that is unable to bind heparin and requires activation by (NH4)2SO4 to generate a biologically active extracellular heparin-binding growth factor (Jackson, A., Friedman, S., Zhan, X., Engleka, K. A., Forough, R., and Maciag, T. (1992) Proc.	Heparin	148-155	fibroblast growth factor 1	Mus musculus	0-32
7999789-2	1995	Expression of both bFGF genes in Spodoptera frugiperda (SF-21) suspension cell culture using a recombinant baculovirus yielded approximately 2.5 mg of mitogenically fully active protein per 10(9) cells following heparin-affinity chromatography.	Heparin	212-219	fibroblast growth factor 2	Homo sapiens	19-23
7647107-4	1995	We have therefore devised a means of production of active recombinant FGF2 devoid of heparin traces.	Heparin	85-92	fibroblast growth factor 2	Bos taurus	70-74
7851376-8	1995	Heparin was shown to markedly enhance the rate of thrombin degradation by RMCP-1.	Heparin	0-7	coagulation factor II	Rattus norvegicus	50-58
7851376-8	1995	Heparin was shown to markedly enhance the rate of thrombin degradation by RMCP-1.	Heparin	0-7	mast cell protease 1-like 1	Rattus norvegicus	74-80
8744652-4	1995	Recent data indicate that heparin can bind cytokines with potent immune modulatory action (e.g. TNF-alpha, interferon gamma etc.).	Heparin	26-33	tumor necrosis factor	Homo sapiens	96-105
8744652-4	1995	Recent data indicate that heparin can bind cytokines with potent immune modulatory action (e.g. TNF-alpha, interferon gamma etc.).	Heparin	26-33	interferon gamma	Homo sapiens	107-123
7779581-9	1995	Although native SOD has no affinity for heparin, the modified enzyme bound to a heparin-agarose column.	Heparin	80-87	superoxide dismutase 1	Homo sapiens	16-19
7833248-6	1995	Cell adhesion studies to dishes coated with the fibronectin 40 kD fragment, containing the heparin-binding domain, demonstrated that adhesiveness of IL-3-treated cells was higher than that of untreated cells.	Heparin	91-98	interleukin 3	Mus musculus	149-153
8834771-2	1995	Heparin induces osteoporosis during long-term administration and has been shown in vitro to enhance the effects of other bone resorbing factors, including parathyroid hormone.	Heparin	0-7	parathyroid hormone	Rattus norvegicus	155-174
8834771-3	1995	In this study, we examined the effects of heparin on the bone-resorbing activity of the inflammatory cytokine IL-1 beta.	Heparin	42-49	interleukin 1 beta	Rattus norvegicus	110-119
7888254-3	1995	RESULTS: Heparin, at concentrations of 0.5-500 U/ml, caused a gradual inhibition of superoxide production stimulated by PMA, opsonised zymosan, or FMLP.	Heparin	9-16	formyl peptide receptor 1	Homo sapiens	147-151
7888254-4	1995	Tissue plasminogen activator was more potent than heparin in inhibiting superoxide production induced by opsonised zymosan or FMLP, but it did not affect the activity stimulated by PMA.	Heparin	50-57	formyl peptide receptor 1	Homo sapiens	126-130
7833248-7	1995	These results suggest that in multipotent haemopoietic cells IL-3 regulates the amount of membrane-associated proteoglycans, which in turn modify the adhesive interactions of cells with the heparin-binding domain of fibronectin.	Heparin	190-197	interleukin 3	Mus musculus	61-65
7805029-11	1995	Inhibition was also observed with heparin (10 micrograms/ml), suggesting the participation of TSP heparin-binding domain(s) and heparin-like molecules.	Heparin	34-41	thrombospondin 1	Homo sapiens	94-97
7805029-11	1995	Inhibition was also observed with heparin (10 micrograms/ml), suggesting the participation of TSP heparin-binding domain(s) and heparin-like molecules.	Heparin	98-105	thrombospondin 1	Homo sapiens	94-97
7805029-11	1995	Inhibition was also observed with heparin (10 micrograms/ml), suggesting the participation of TSP heparin-binding domain(s) and heparin-like molecules.	Heparin	98-105	thrombospondin 1	Homo sapiens	94-97
7750519-3	1995	bFGF-HRP association to adult bovine aortic endothelial (ABAE) cells or baby hamster kidney (BHK) cells was inhibited by a high molar excess of native bFGF, a 2 M NaCl wash at neutral pH, heparin and heparan sulfate, but not by chondroitin 4-sulfate or chondroitin 6-sulfate.	Heparin	188-195	fibroblast growth factor 2	Bos taurus	0-4
7813328-11	1995	Heparin presents an aspecific "nonfunctional" binding to plasma proteins such as fibrinogen, factor VIII, vitronectin, and fibronectin.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	81-91
7813328-11	1995	Heparin presents an aspecific "nonfunctional" binding to plasma proteins such as fibrinogen, factor VIII, vitronectin, and fibronectin.	Heparin	0-7	fibronectin 1	Homo sapiens	123-134
7588997-1	1995	[125I]-Labeled thrombin was incubated with human plasma and its interactions with the two plasma protease inhibitors antithrombin III (AT-III) or heparin cofactor II (HC-II) were investigated in the presence of oat spelts xylan sulfate (OSXS), sodium pentosan polysulfate (SP-54), and the results were compared with heparin and dermatan sulfate.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	15-23
7588997-4	1995	However after a 2 min interaction, heparin showed an increase in the HC-II-thrombin interaction at higher concentrations.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	75-83
7588997-6	1995	The Western blotting method of detecting thrombin showed that during the 10 s interaction, heparin enhanced the thrombin-AT-III complex formation while OSXS enhanced the thrombin-HC-II complex formation.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	41-49
7588997-6	1995	The Western blotting method of detecting thrombin showed that during the 10 s interaction, heparin enhanced the thrombin-AT-III complex formation while OSXS enhanced the thrombin-HC-II complex formation.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	112-120
7588997-6	1995	The Western blotting method of detecting thrombin showed that during the 10 s interaction, heparin enhanced the thrombin-AT-III complex formation while OSXS enhanced the thrombin-HC-II complex formation.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	112-120
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	50-57	vascular endothelial growth factor A	Homo sapiens	174-178
8619928-1	1995	Fibroblast growth factors (FGF) are multifunctional, heparin binding polypeptides that share structural similarity, but differ in their target cell specificity and expression pattern.	Heparin	53-60	fibroblast growth factor 9	Mus musculus	27-30
8619928-6	1995	Moreover, receptor binding of FGF9 requires heparin in a manner specific to the receptor type.	Heparin	44-51	fibroblast growth factor 9	Mus musculus	30-34
8619928-7	1995	In conclusion FGF9 presents a unique case of ligand-receptor specificity and fulfills the criteria as a high affinity, heparin-dependent ligand for FGFR3.	Heparin	119-126	fibroblast growth factor 9	Mus musculus	14-18
7706948-7	1995	The mutant apoE also displayed a reduced affinity for heparin compared to apoE3.	Heparin	54-61	apolipoprotein E	Homo sapiens	11-15
8679245-2	1995	Reports of the relative potency of these growth factors and the ability of heparin to potentiate the activity of bFGF are conflicting.	Heparin	75-82	fibroblast growth factor 2	Homo sapiens	113-117
8679245-6	1995	Heparin potentiated the mitogenic and metabolic effects of both bFGF and aFGF.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	64-68
8679245-6	1995	Heparin potentiated the mitogenic and metabolic effects of both bFGF and aFGF.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	73-77
7798503-0	1995	Thrombin generation and activity during thrombolysis and concomitant heparin therapy in patients with acute myocardial infarction.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	0-8
7798503-3	1995	Increased thrombin activity is suppressed by concomitant intravenous heparin, but it is unknown whether thrombin generation is also affected.	Heparin	69-76	coagulation factor II, thrombin	Homo sapiens	10-18
7536241-4	1995	Native, non-deamidated aFGF (complexed with heparin) has a half-life of 16 weeks at pH 7, 30 degrees C, and 4 weeks at pH 8, 40 degrees C. The mitogenic activity and biophysical properties of deamidated aFGF were compared to the non-deamidated protein.	Heparin	44-51	fibroblast growth factor 1	Homo sapiens	23-27
8714367-1	1995	Heparin affin regulatory peptide (HARP), also called Pleiotrophin (PTN), is a polypeptide that displays a high affinity for heparin and that shares approximately 50% sequence homology with Midkine (MK).	Heparin	124-131	pleiotrophin	Homo sapiens	0-32
7854159-9	1995	Similarly, lipid-heparin infusion nearly abolished the GH response to GHRH (peak, 4.9 +/- 1.0 micrograms/L, P &lt; .01) while only blunting the somatotrope response to hexarelin (peak, 34.2 +/- 4.5 micrograms/L, P &lt; .05).	Heparin	17-24	growth hormone 1	Homo sapiens	55-57
7854159-9	1995	Similarly, lipid-heparin infusion nearly abolished the GH response to GHRH (peak, 4.9 +/- 1.0 micrograms/L, P &lt; .01) while only blunting the somatotrope response to hexarelin (peak, 34.2 +/- 4.5 micrograms/L, P &lt; .05).	Heparin	17-24	growth hormone releasing hormone	Homo sapiens	70-74
21043709-0	1995	Inhibition of Binding of von Willebrand Factor to the Platelet Glycoprotein Ib-IX Complex, Heparin and Sulfatides by Polyanionic Compounds.	Heparin	91-98	von Willebrand factor	Homo sapiens	25-46
21043709-4	1995	Binding of vWF to the GP Ib-IX complex involves the vWF A1 internal repeat domain, which also contains distinct binding sites for sulfatides, heparin, and the non-physiological modulators of the vWF-GP Ib-IX interaction, ristocetin and botrocetin.	Heparin	142-149	von Willebrand factor	Homo sapiens	11-14
21043709-4	1995	Binding of vWF to the GP Ib-IX complex involves the vWF A1 internal repeat domain, which also contains distinct binding sites for sulfatides, heparin, and the non-physiological modulators of the vWF-GP Ib-IX interaction, ristocetin and botrocetin.	Heparin	142-149	von Willebrand factor	Homo sapiens	52-55
21043709-4	1995	Binding of vWF to the GP Ib-IX complex involves the vWF A1 internal repeat domain, which also contains distinct binding sites for sulfatides, heparin, and the non-physiological modulators of the vWF-GP Ib-IX interaction, ristocetin and botrocetin.	Heparin	142-149	von Willebrand factor	Homo sapiens	52-55
21043709-6	1995	Firstly, it was confirmed using a solid-phase binding assay that, like sulfatides, heparin specifically bound to a purified 39/WkiloDalton fragment of vWF (Leu-480 to Gly-718) that encompasses the A1 domain.	Heparin	83-90	von Willebrand factor	Homo sapiens	151-154
21043709-7	1995	Secondly, the ability of a number of polyanionic compounds to inhibit binding of vWF to heparin, but not to immobilized sulfatides, supported previous data suggesting that heparin and sulfatides bind to distinct sites on vWF.	Heparin	88-95	von Willebrand factor	Homo sapiens	81-84
21043709-7	1995	Secondly, the ability of a number of polyanionic compounds to inhibit binding of vWF to heparin, but not to immobilized sulfatides, supported previous data suggesting that heparin and sulfatides bind to distinct sites on vWF.	Heparin	172-179	von Willebrand factor	Homo sapiens	81-84
21043709-7	1995	Secondly, the ability of a number of polyanionic compounds to inhibit binding of vWF to heparin, but not to immobilized sulfatides, supported previous data suggesting that heparin and sulfatides bind to distinct sites on vWF.	Heparin	172-179	von Willebrand factor	Homo sapiens	221-224
8815283-1	1995	As shown by 125I-fibrinogen, in the course of 10-year investigation on low-dose heparin given in low doses (15000 U/day) to prevent postoperative thrombosis in the deep veins of the lower limbs, the investigators succeeded in the reduction of the thrombosis occurrence from 32 to 8%.	Heparin	80-87	fibrinogen beta chain	Homo sapiens	17-27
7845032-7	1995	We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin.	Heparin	174-181	fibroblast growth factor 2	Homo sapiens	48-52
7845032-7	1995	We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin.	Heparin	174-181	fibroblast growth factor 1	Homo sapiens	398-402
7845032-7	1995	We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin.	Heparin	423-430	fibroblast growth factor 2	Homo sapiens	48-52
7845032-7	1995	We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin.	Heparin	423-430	fibroblast growth factor 2	Homo sapiens	165-169
7845032-7	1995	We found that two cell lines were responsive to bFGF in different biological assays: (i) in K562 myeloid cells induced to differentiate by hemin, preincubation with bFGF and heparin increased cell viability and decreased hemin-induced DNA fragmentation, without affecting erythroid differentiation; and (ii) in U937 monocytic cells, the production of plasminogen activator was increased by bFGF or aFGF in combination with heparin.	Heparin	423-430	fibroblast growth factor 2	Homo sapiens	165-169
7845032-8	1995	Binding experiments with 125I-bFGF (up to 200 pM) in the presence of heparin revealed high affinity receptors on the K562 and U937 cell lines (1177 +/- 440 and 392 +/- 184 sites/cell, Kd = 61.7 +/- 8.6 and 43.1 +/- 13.5 pM, respectively).	Heparin	69-76	fibroblast growth factor 2	Homo sapiens	30-34
21043709-8	1995	In addition, aurintricarboxylic acid, Evans blue and fucoidan all inhibited binding of vWF to both heparin and sulfatides with similar ICso values.	Heparin	99-106	von Willebrand factor	Homo sapiens	87-90
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Heparin	71-78	von Willebrand factor	Homo sapiens	64-67
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Heparin	71-78	von Willebrand factor	Homo sapiens	159-162
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Heparin	71-78	von Willebrand factor	Homo sapiens	159-162
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Heparin	293-300	von Willebrand factor	Homo sapiens	64-67
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Heparin	293-300	von Willebrand factor	Homo sapiens	159-162
21043709-9	1995	Thirdly, many of the compounds tested that inhibited binding of vWF to heparin also effectively inhibited both ristocetin- and botrocetin-dependent binding of vWF to the GP Ib-IX complex on platelets, whereas none of the compounds tested blocked vWF binding to sulfatides and GP Ib-IX but not heparin.	Heparin	293-300	von Willebrand factor	Homo sapiens	159-162
21043709-11	1995	These combined experiments provide evidence for an electrostatic model of vWF modulation, and suggest that the heparin-binding domain of vWF may be an important regulatory site involved in the adhesion of vWF to the platelet GP Ib-IX complex.	Heparin	111-118	von Willebrand factor	Homo sapiens	74-77
21043709-11	1995	These combined experiments provide evidence for an electrostatic model of vWF modulation, and suggest that the heparin-binding domain of vWF may be an important regulatory site involved in the adhesion of vWF to the platelet GP Ib-IX complex.	Heparin	111-118	von Willebrand factor	Homo sapiens	137-140
21043709-11	1995	These combined experiments provide evidence for an electrostatic model of vWF modulation, and suggest that the heparin-binding domain of vWF may be an important regulatory site involved in the adhesion of vWF to the platelet GP Ib-IX complex.	Heparin	111-118	von Willebrand factor	Homo sapiens	137-140
8714367-1	1995	Heparin affin regulatory peptide (HARP), also called Pleiotrophin (PTN), is a polypeptide that displays a high affinity for heparin and that shares approximately 50% sequence homology with Midkine (MK).	Heparin	124-131	pleiotrophin	Homo sapiens	34-38
8552861-6	1995	FN was extracted with urea and heparin.	Heparin	31-38	fibronectin 1	Homo sapiens	0-2
8714367-1	1995	Heparin affin regulatory peptide (HARP), also called Pleiotrophin (PTN), is a polypeptide that displays a high affinity for heparin and that shares approximately 50% sequence homology with Midkine (MK).	Heparin	124-131	pleiotrophin	Homo sapiens	53-65
8714367-1	1995	Heparin affin regulatory peptide (HARP), also called Pleiotrophin (PTN), is a polypeptide that displays a high affinity for heparin and that shares approximately 50% sequence homology with Midkine (MK).	Heparin	124-131	pleiotrophin	Homo sapiens	67-70
8789468-1	1995	For quantitative comparison of thrombin generation during cardiopulmonary bypass (CPB) with heparin-coated vs conventional CPB circuits, thrombin-antithrombin III complex (TAT) and prothrombin fragment 1 + 2 (F1 + 2) were analyzed in 20 patients undergoing combined heart valve surgery and coronary artery bypass grafting (CABG), in ten cases with heparin-coated circuits (COMB-HC) and in ten with standard circuits (COMB-C).	Heparin	92-99	coagulation factor II, thrombin	Homo sapiens	31-39
7481155-9	1995	However, in spite of improved therapeutical protocols, a normal flow, which is the major criteria for a reduced mortality, is only obtained at the 90th minute in 54% of the patients who were administered the up-to-date treatment ie aspirin-accelerated t-PA-heparin in combination.	Heparin	257-264	plasminogen activator, tissue type	Homo sapiens	252-256
7652460-2	1995	Bovine beta 2-glycoprotein I (beta 2-GPI) was purified by heparin affinity and DEAE ion-exchange chromatography, and identified on immunoblots using a monoclonal antibody against human beta 2-GPI and by amino acid sequence analysis.	Heparin	58-65	apolipoprotein H	Bos taurus	7-28
7652460-2	1995	Bovine beta 2-glycoprotein I (beta 2-GPI) was purified by heparin affinity and DEAE ion-exchange chromatography, and identified on immunoblots using a monoclonal antibody against human beta 2-GPI and by amino acid sequence analysis.	Heparin	58-65	apolipoprotein H	Bos taurus	30-40
7798222-5	1994	Rather, adhesion of HT-29 cells was decreased by treatment of TSPs with EDTA, abolished by reduction of the TSPs, and, in the case of rTSP2, blocked by heparin.	Heparin	152-159	thrombospondin 2	Rattus norvegicus	134-139
7809939-1	1994	Heparin antagonizes the induction of class II MHC molecules by interferon-gamma.	Heparin	0-7	interferon gamma	Homo sapiens	63-79
7806495-8	1994	Specific mutations in exosite II (R89E, R245E, K248E, and K252E) disrupted thrombin binding to both dermatan sulfate and heparin, indicating that both glycosaminoglycans bind to a common site in exosite II.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	75-83
7806495-12	1994	Antithrombin employs a template mechanism that requires heparin to interact with thrombin exosite II, whereas HCII employs an allosteric mechanism that requires thrombin exosite I but is largely independent of exosite II.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	4-12
7806495-12	1994	Antithrombin employs a template mechanism that requires heparin to interact with thrombin exosite II, whereas HCII employs an allosteric mechanism that requires thrombin exosite I but is largely independent of exosite II.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	81-89
7989348-8	1994	Binding of the fragment to purified LRP was blocked by heparin.	Heparin	55-62	LDL receptor related protein 1	Homo sapiens	36-39
7528103-3	1994	Heparin exerts its effect by binding to many molecules of aFGF.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	58-62
7528103-4	1994	The resulting aFGF-heparin complex can bind to several receptor molecules, leading to FGFR dimerization.	Heparin	19-26	fibroblast growth factor 1	Homo sapiens	14-18
7528103-6	1994	Moreover, a synthetic heparin analog that binds monovalently to aFGF blocks FGFR dimerization, activation, and signaling via FGFR.	Heparin	22-29	fibroblast growth factor 1	Homo sapiens	64-68
7528103-7	1994	We propose that heparin causes oligomerization of aFGF such that its binding to FGFR results in dimerization and activation.	Heparin	16-23	fibroblast growth factor 1	Homo sapiens	50-54
7991602-0	1994	Heparin-dependent binding and autophosphorylation of epidermal growth factor (EGF) receptor by heparin-binding EGF-like growth factor but not by EGF.	Heparin	0-7	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	78-81
7818503-5	1994	This was not due to inactivation of lipoprotein lipase, since injection of an excess of heparin 10 min after injection of protamine released as much lipoprotein lipase activity to plasma as in controls.	Heparin	88-95	lipoprotein lipase	Rattus norvegicus	149-167
7818503-7	1994	Protamine was able to almost quantitatively release both lipoprotein lipase and hepatic lipase from columns of heparin-agarose.	Heparin	111-118	lipoprotein lipase	Rattus norvegicus	57-75
7818503-7	1994	Protamine was able to almost quantitatively release both lipoprotein lipase and hepatic lipase from columns of heparin-agarose.	Heparin	111-118	lipase C, hepatic type	Rattus norvegicus	80-94
7991602-7	1994	These results directly demonstrate that HB-EGF but not EGF requires heparin or cell surface HSPG for binding and activation of the EGF receptor and that HB-EGF receptor interactions can be tightly regulated by the available local concentration of heparin-like molecules.	Heparin	247-254	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	43-46
7991602-5	1994	Moreover, binding of radiolabeled EGF to HSPG-deficient EGF receptor-expressing cells is efficiently displaced by nonlabeled HB-EGF only in the presence of heparin.	Heparin	156-163	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	34-37
7982975-2	1994	Fc gamma 2a receptor-mediated activation of NF-kappa B was blocked by the presence of pyrrolidinedithiocarbamate, neutralizing anti-tumor necrosis factor (TNF)-alpha antibodies, various protein kinase inhibitors (H-89, genistein, or heparin) or intracellular calcium chelator (1,2-bis(O-aminophenoxy)-ethane-N,N,N",N"-tetraacetic acid tetra-(acetoxymethyl)-ester, BAPTA/AM) during stimulation.	Heparin	233-240	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	44-54
7991602-5	1994	Moreover, binding of radiolabeled EGF to HSPG-deficient EGF receptor-expressing cells is efficiently displaced by nonlabeled HB-EGF only in the presence of heparin.	Heparin	156-163	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	56-59
7991602-6	1994	Signal transduction by the EGF receptor tyrosine kinase as evidenced by receptor autophosphorylation is induced by HB-EGF only in the presence of heparin, in contrast to EGF-induced receptor autophosphorylation, which is independent of heparin.	Heparin	146-153	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	27-30
7991602-6	1994	Signal transduction by the EGF receptor tyrosine kinase as evidenced by receptor autophosphorylation is induced by HB-EGF only in the presence of heparin, in contrast to EGF-induced receptor autophosphorylation, which is independent of heparin.	Heparin	236-243	LOW QUALITY PROTEIN: pro-epidermal growth factor	Cricetulus griseus	27-30
7765681-6	1994	While Heparin-Membrane Adsorber were found to isolate and concentrate the Antithrombin III efficiently, the removal of the major bovine serum proteins (albumin, transferrin, immunoglobulins) required a multistage process.	Heparin	6-13	serpin family C member 1	Bos taurus	74-90
7998663-7	1994	In patients with systemic sclerosis with a shorter disease duration, greater spontaneous as well as collagen- and heparin-stimulated IL-6 production was observed, whereas decreased IL-6 levels were noted with longer disease duration (&gt; 21 years).	Heparin	114-121	interleukin 6	Homo sapiens	133-137
7765681-7	1994	By using a sequence of ultrafiltration, diafiltration, Cibacron Blue, anion exchanger, and Heparin-Membrane Adsorber, an electrophoretically pure Antithrombin III could be obtained.	Heparin	91-98	serpin family C member 1	Bos taurus	146-162
7634317-4	1994	Heparin is the principal antithrombin drug currently used in acute syndromes; it acts mainly by binding to antithrombin III and increasing its inhibitory effect on thrombin and other coagulation factors.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	29-37
7534486-5	1994	In the case of PMN-elastase, heparin (300 nM) further increases enzyme protection against alpha 1-protease inhibitor; the rate constant decreases from 41 x 10(3) M-1 s-1 to 23 x 10(3) M-1 s-1.	Heparin	29-36	serpin family A member 1	Homo sapiens	90-116
7949128-0	1994	Platelet adhesion to fibronectin in flow: dependence on surface concentration and shear rate, role of platelet membrane glycoproteins GP IIb/IIIa and VLA-5, and inhibition by heparin.	Heparin	175-182	fibronectin 1	Homo sapiens	21-32
7949128-8	1994	Preincubation of the immobilized fibronectin with UFH resulted in a maximal inhibition of 90%, whereas preincubation with LMWH had no effect.	Heparin	50-53	fibronectin 1	Homo sapiens	33-44
7634317-5	1994	The heparin-antithrombin III complex, however, does not inhibit thrombus-bound thrombin; moreover, iv heparin requires frequent laboratory monitoring and dose adjustments.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	16-24
7634317-7	1994	heparin has been found to be effective in unstable angina and in myocardial infarction, especially when treated with accelerated rt-PA. New antithrombin drugs that selectively and directly inhibit thrombin are hirudin, its synthetic derivate hirulog, and argatroban.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	144-152
7949128-10	1994	These results indicate that platelet adhesion to fibronectin in flow involves several receptors, is highly RGD-mediated, does not require physiologic levels of divalent cations, and can be inhibited by direct binding of heparin to the fibronectin surface.	Heparin	220-227	fibronectin 1	Homo sapiens	49-60
7949128-10	1994	These results indicate that platelet adhesion to fibronectin in flow involves several receptors, is highly RGD-mediated, does not require physiologic levels of divalent cations, and can be inhibited by direct binding of heparin to the fibronectin surface.	Heparin	220-227	fibronectin 1	Homo sapiens	235-246
7634317-8	1994	These drugs have several theoretical advantages over heparin: greater stability of the aPTT--with the need for less laboratory monitoring--and greater efficacy--associated mainly with its capacity to inhibit clot-bound thrombin.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	219-227
7530156-9	1994	Moreover, heparin inhibited thrombin-stimulated platelet/neutrophils rosetting (36% of inhibition, P &lt; 0.01).	Heparin	10-17	coagulation factor II	Rattus norvegicus	28-36
7537556-0	1994	Structural requirements in heparin for binding and activation of FGF-1 and FGF-4 are different from that for FGF-2.	Heparin	27-34	fibroblast growth factor 1	Homo sapiens	65-70
7527332-4	1994	The addition of heparin, heparan sulfate, and dermatan sulfate (100 micrograms/ml) to the medium of fibroblast monolayer cultures inhibited IGFBP-5 degradation, as determined by the conversion of intact IGFBP-5 to a 23-kilodalton fragment.	Heparin	16-23	insulin like growth factor binding protein 5	Homo sapiens	140-147
7527332-4	1994	The addition of heparin, heparan sulfate, and dermatan sulfate (100 micrograms/ml) to the medium of fibroblast monolayer cultures inhibited IGFBP-5 degradation, as determined by the conversion of intact IGFBP-5 to a 23-kilodalton fragment.	Heparin	16-23	insulin like growth factor binding protein 5	Homo sapiens	203-210
7527332-6	1994	Heparin and heparan sulfate inhibited IGFBP-5 degradation at concentrations of 1 or 2.5 micrograms/ml, but 100 micrograms/ml dermatan sulfate were required.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	38-45
7537556-0	1994	Structural requirements in heparin for binding and activation of FGF-1 and FGF-4 are different from that for FGF-2.	Heparin	27-34	fibroblast growth factor 4	Homo sapiens	75-80
7897316-8	1994	HDL density profiles of the study groups prior to the administration of heparin demonstrated two distinct peaks at density 1.09 g/ml (HDL2) and 1.13 g/ml (HDL3).	Heparin	72-79	HDL3	Homo sapiens	155-159
7706214-8	1994	In contrast, type V collagen or alpha1 (V) chain binds to heparin under the same conditions and therefore the conformational change of type V collagen in urea solution would not be discernible in terms of heparin affinity, even if the type V collagen molecules have altered conformation in urea, as is suggested for type I collagen.	Heparin	58-65	collagen type V alpha 1 chain	Homo sapiens	32-42
7740443-1	1994	Dermatan sulphate catalyses thrombin inhibition by heparin cofactor II; it has a lower haemorrhagic to antithrombotic ratio than that of heparin in animal models.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	28-36
7807964-0	1994	Heparin selectively inhibits synthesis of tissue type plasminogen activator and matrix deposition of plasminogen activator inhibitor 1 by human mesangial cells.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	42-75
7807964-10	1994	Heparin selectively and partially inhibited FCS-stimulated t-PA, but not PAI-1 synthesis.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	59-63
7807964-16	1994	CONCLUSIONS: In human mesangial cells, anticoagulant and nonanticoagulant heparin exert an antiproliferative effect and may prevent mesangial matrix changes by decreasing FCS-stimulated t-PA synthesis and PAI-1 deposition in the matrix.	Heparin	74-81	plasminogen activator, tissue type	Homo sapiens	186-190
7740451-0	1994	Thrombin regulation in children differs from adults in the absence and presence of heparin.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	0-8
7740451-7	1994	At low heparin concentrations (0.1 and 0.2 U/ml), thrombin generation was decreased by 30% in children compared to adults (p &lt; 0.001).	Heparin	7-14	coagulation factor II, thrombin	Homo sapiens	50-58
7947827-10	1994	The K290M,K294M,K297M variant had properties very similar to those of wild-type recombinant antithrombin in affinity for heparin, and in rates of inhibition of thrombin and factor Xa.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	96-104
7930274-0	1994	Failure of fixed dose intravenous heparin to suppress increases in thrombin activity after coronary thrombolysis with streptokinase.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	67-75
7526860-6	1994	Conversely, multifold growth stimulation by acidic FGF required heparin.	Heparin	64-71	fibroblast growth factor 1	Mus musculus	51-54
7961933-9	1994	The second-order inhibition rate constants k2/Ki* were 4300, 700, and 52 M-1 S-1 for alpha 1-antichymotrypsin, alpha 1-antitrypsin, and eglin c, respectively, indicating that, if heparin is present in vivo, the two former physiological inhibitors will be unable to prevent cathepsin G-mediated proteolysis.	Heparin	179-186	serpin family A member 1	Homo sapiens	111-130
7930274-1	1994	OBJECTIVES: This study was designed to define the extent of inhibition of thrombin activity achieved with conjunctive fixed dose intravenous sodium heparin compared with fixed dose subcutaneous calcium heparin in patients receiving intravenous streptokinase for acute myocardial infarction.	Heparin	141-155	coagulation factor II, thrombin	Homo sapiens	74-82
7947605-5	1994	The 29- and 38-kd heparin-binding thermolysin fragments of fibronectin, previously identified as the lipoprotein(a) binding domains, were digested with trypsin, and a peptide that retained the ability to bind r-apo(a) was isolated; the sequence of the peptide (AVTTIPAPTDLK) corresponds to the amino terminus of the 29- and 38-kd domains.	Heparin	18-25	fibronectin 1	Homo sapiens	59-70
7871494-4	1994	Both APC (300-3000 U/kg) and heparin (100-300 IU/kg) inhibited the decreases in platelet count and fibrinogen level equally.	Heparin	29-36	fibrinogen beta chain	Homo sapiens	99-109
7947604-2	1994	We have recently shown that a monoclonal antibody (mAb) to the NH2-terminal heparin-binding domain of TSP, MAII, inhibits platelet aggregation induced by thrombin in a dose-dependent manner.	Heparin	76-83	thrombospondin 1	Homo sapiens	102-105
7947604-2	1994	We have recently shown that a monoclonal antibody (mAb) to the NH2-terminal heparin-binding domain of TSP, MAII, inhibits platelet aggregation induced by thrombin in a dose-dependent manner.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	154-162
7947604-4	1994	After purification, both proteins reacted equally well with mAb MAII, whereas the reactivity of TSP18 for heparin was lower than that of TSP28 or native TSP.	Heparin	106-113	thrombospondin 1	Homo sapiens	96-99
7979371-2	1994	Heparin suppresses thrombin-stimulated endothelin-1 production in endothelial cells; this is consistent with its reported effect of lowering blood pressure.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	19-27
7979371-2	1994	Heparin suppresses thrombin-stimulated endothelin-1 production in endothelial cells; this is consistent with its reported effect of lowering blood pressure.	Heparin	0-7	endothelin 1	Homo sapiens	39-51
7979371-3	1994	Since heparin is a heterogeneous mixture of glycosaminoglycans, we examined the effects of different fractions of heparin in suppressing endothelin-1 production in cultured endothelial cells.	Heparin	114-121	endothelin 1	Homo sapiens	137-149
7979371-9	1994	Hirudin, like heparin, binds to the anion-binding exosite of thrombin.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	61-69
7979371-11	1994	These experiments demonstrate that the suppressive effect of heparin is the result of its binding to the traces of thrombin in the culture medium, preventing stimulation of endothelin-1 production.	Heparin	61-68	coagulation factor II, thrombin	Homo sapiens	115-123
7979371-11	1994	These experiments demonstrate that the suppressive effect of heparin is the result of its binding to the traces of thrombin in the culture medium, preventing stimulation of endothelin-1 production.	Heparin	61-68	endothelin 1	Homo sapiens	173-185
7947604-9	1994	The results suggest that interaction between the heparin-binding domain of TSP and membrane-bound fibrinogen may be critical in the platelet aggregation/secretion process.	Heparin	49-56	thrombospondin 1	Homo sapiens	75-78
7819071-7	1994	Platelet and plasma vWf bound to collagen with similar affinities; however, platelet vWf bound to thrombin-stimulated platelets and to heparin with a higher affinity than plasma vWf.	Heparin	135-142	von Willebrand factor	Homo sapiens	85-88
7819071-7	1994	Platelet and plasma vWf bound to collagen with similar affinities; however, platelet vWf bound to thrombin-stimulated platelets and to heparin with a higher affinity than plasma vWf.	Heparin	135-142	von Willebrand factor	Homo sapiens	85-88
7767864-1	1994	Administration of streptozotocin (100 mg/kg) to adult Sprague-Dawley rats reduced both functional (heparin releasable) lipoprotein lipase activity in perfused hearts and total and heparin-releasable lipoprotein lipase activity in isolated cardiomyocytes, and produced a hypothyroid state (decreased plasma levels of triiodothyronine and thyroxine).	Heparin	99-106	lipoprotein lipase	Rattus norvegicus	119-137
7959685-3	1994	The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin.	Heparin	159-166	coagulation factor II, thrombin	Homo sapiens	238-246
7955182-2	1994	BACKGROUND: Heparin needs the plasma protein antithrombin III to function as an inhibitor of thrombin, and local antithrombin III deficiency might therefore limit the antithrombotic effectiveness of heparin during percutaneous transluminal coronary angioplasty.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	49-57
7955182-2	1994	BACKGROUND: Heparin needs the plasma protein antithrombin III to function as an inhibitor of thrombin, and local antithrombin III deficiency might therefore limit the antithrombotic effectiveness of heparin during percutaneous transluminal coronary angioplasty.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	49-57
7900078-0	1994	The effect of subcutaneous injection of unfractionated and low molecular weight heparin on thrombin generation in platelet rich plasma--a study in human volunteers.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	91-99
7863825-5	1994	Partial purification of cartilage-derived bFGF was performed on crude extracts of cartilage using heparin-Sepharose affinity chromatography.	Heparin	98-105	fibroblast growth factor 2	Homo sapiens	42-46
7863825-6	1994	The presence of bFGF in the heparin-Sepharose column fractions was confirmed by immunoblotting and radioimmunoassay.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	16-20
7930624-7	1994	Consistent with the mAb data, the COOH-terminal 140-kDa proteolytic fragment of TSP was chemotactic for monocytes, whereas the NH2-terminal heparin-binding domain was inactive.	Heparin	140-147	thrombospondin 1	Homo sapiens	80-83
7863481-3	1994	In both cases, the expression of the mutation is pleiotropic, i.e. results in a reduction in the circulating concentration of antithrombin and impairs both its anti-thrombin activity and its ability to bind heparin.	Heparin	207-214	coagulation factor II, thrombin	Homo sapiens	130-138
7900078-4	1994	UFH administration caused only a 5-8% inhibition of the thrombin potential (i.e. the area under the thrombin generation curve).	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	56-64
7900078-4	1994	UFH administration caused only a 5-8% inhibition of the thrombin potential (i.e. the area under the thrombin generation curve).	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	100-108
7929392-2	1994	The Alzheimer beta-amyloid precursor protein (APP) contains an ectodomain zinc binding site that has been reported to modulate the heparin affinity and protease-inhibitory properties of the molecule.	Heparin	131-138	amyloid beta precursor protein	Homo sapiens	14-44
7900078-7	1994	UFH injection caused a prolongation of the lag-time before the thrombin burst.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	63-71
7929416-9	1994	We propose that part of the antithrombotic action of heparin and low molecular weight heparin is due to anti-thrombin-independent inhibition of intrinsic fXase and that heparin with low affinity for antithrombin may be useful as an antithrombotic agent.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	109-117
7929416-9	1994	We propose that part of the antithrombotic action of heparin and low molecular weight heparin is due to anti-thrombin-independent inhibition of intrinsic fXase and that heparin with low affinity for antithrombin may be useful as an antithrombotic agent.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	109-117
7900084-0	1994	Heparin enhances endothelial cell von Willebrand factor content by growth factor dependent mechanisms.	Heparin	0-7	von Willebrand factor	Homo sapiens	34-55
7929416-9	1994	We propose that part of the antithrombotic action of heparin and low molecular weight heparin is due to anti-thrombin-independent inhibition of intrinsic fXase and that heparin with low affinity for antithrombin may be useful as an antithrombotic agent.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	109-117
7900084-3	1994	We studied the effect of pharmacologic doses of heparin on the vWf content of endothelial cells.	Heparin	48-55	von Willebrand factor	Homo sapiens	63-66
7900084-4	1994	After a lag of 8 h and in the presence of crude or purified growth factor, heparin at doses between 0.25 and 2 U (1.4-11 micrograms)/ml, increased the content of high molecular weight vWf.	Heparin	75-82	von Willebrand factor	Homo sapiens	184-187
7900084-6	1994	Lower molecular weight highly sulfated heparin or heparin-like compounds were most active in growth factor dependent endothelial cell vWf expression.	Heparin	39-46	von Willebrand factor	Homo sapiens	134-137
7900084-6	1994	Lower molecular weight highly sulfated heparin or heparin-like compounds were most active in growth factor dependent endothelial cell vWf expression.	Heparin	50-57	von Willebrand factor	Homo sapiens	134-137
7980421-0	1994	Different effects of mucosal, bovine lung and chemically modified heparin on selected biological properties of basic fibroblast growth factor.	Heparin	66-73	fibroblast growth factor 2	Bos taurus	111-141
7980421-4	1994	In contrast, selective 2-O-desulphation, but not 6-O-desulphation, drastically reduced the capacity of heparin to protect bFGF from proteolytic cleavage, to affect its interaction with low- and high-affinity sites, and to inhibit its mitogenic activity.	Heparin	103-110	fibroblast growth factor 2	Bos taurus	122-126
7980421-5	1994	Two preparations of bovine lung heparin, differing in molecular mass, were as effective as mucosal heparin in the bFGF-tryptic-digestion assay and the endothelial-cell proteoglycan-binding assay, but they were highly inefficient at inhibiting the capacity of bFGF to interact with its tyrosine kinase receptors.	Heparin	32-39	fibroblast growth factor 2	Bos taurus	114-118
7980421-5	1994	Two preparations of bovine lung heparin, differing in molecular mass, were as effective as mucosal heparin in the bFGF-tryptic-digestion assay and the endothelial-cell proteoglycan-binding assay, but they were highly inefficient at inhibiting the capacity of bFGF to interact with its tyrosine kinase receptors.	Heparin	32-39	fibroblast growth factor 2	Bos taurus	259-263
7980421-6	1994	Bovine lung heparins were also less effective than mucosal heparin as bFGF antagonists in GM 7373-cell-proliferation assays.	Heparin	12-20	fibroblast growth factor 2	Bos taurus	70-74
7980421-6	1994	Bovine lung heparins were also less effective than mucosal heparin as bFGF antagonists in GM 7373-cell-proliferation assays.	Heparin	12-19	fibroblast growth factor 2	Bos taurus	70-74
7980421-7	1994	N-Desulphated/N-acetylated bovine lung heparin retained only a significant capacity to protect bFGF from tryptic cleavage.	Heparin	39-46	fibroblast growth factor 2	Bos taurus	95-99
7980421-8	1994	The results demonstrate that different chemical features of the heparin molecule, including decrease in molecular mass, selective desulphation, disaccharide composition and clustering, affect differently the capacity of the glycosaminoglycan to interact with bFGF and to influence its biological behaviour in different assays in vitro and in endothelial cell cultures.	Heparin	64-71	fibroblast growth factor 2	Bos taurus	259-263
7925646-7	1994	In SMC cultured from intimal thickening, heparin induced a reduction of cell proliferation without modifying their characteristic epithelioid shape; TGF-beta 1 increased the proliferative activity and induced an elongated cell shape as well as a "hills and valleys" growth pattern similar to that observed in control medial SMC; both heparin and TGF-beta 1 induced an increase of alpha-SM actin expression.	Heparin	41-48	transforming growth factor, beta 1	Rattus norvegicus	346-356
7943290-5	1994	Treatment of proliferating endothelial cells with heparin (0-900 micrograms/ml) induced a dose-dependent decrease in endothelial HSPG content, whereas the fibronectin content was unaltered.	Heparin	50-57	fibronectin 1	Homo sapiens	155-166
7944402-1	1994	A synthetic 22 residue peptide, N22W, with sequence NVSPPRRARVTDATETTITISW, derived from the amino terminus of type III module 13 in the carboxy-terminal hep-2 domain of fibronectin, was found to exhibit unusual heparin binding properties.	Heparin	212-219	fibronectin 1	Homo sapiens	170-181
7532447-7	1994	Vitronectin also decreased the inhibition rate of PCI-thrombin and PCI-APC in the presence of low concentrations of heparin.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	54-62
7925646-7	1994	In SMC cultured from intimal thickening, heparin induced a reduction of cell proliferation without modifying their characteristic epithelioid shape; TGF-beta 1 increased the proliferative activity and induced an elongated cell shape as well as a "hills and valleys" growth pattern similar to that observed in control medial SMC; both heparin and TGF-beta 1 induced an increase of alpha-SM actin expression.	Heparin	334-341	transforming growth factor, beta 1	Rattus norvegicus	149-159
7925647-1	1994	The adhesion of the myelogenous leukemia cell line, HL60, to fibronectin and its fragments, heparin binding fragment (40 kDa) and cell attachment fragment (120 kDa), was enhanced by culturing with benzyl-alpha-GalNAc (BZ alpha GalNAc).	Heparin	92-99	fibronectin 1	Homo sapiens	61-72
7660851-4	1994	In line with our previous findings it appears that blood, in the presence of heparin and 5mM Ca,2+ allows a consistent production of tumor necrosis factor a (TNF alpha) and the release of low and non-hazardous levels of free hemoglobin.	Heparin	77-84	tumor necrosis factor	Homo sapiens	158-167
7851943-6	1994	Interaction of DSF with heparin, insulin and Con A revealed that heparin can completely block DSF-mediated lysosomal release.	Heparin	65-72	insulin	Homo sapiens	33-40
7883629-4	1994	Treatment with .1 to 1.0 ng/mL of bFGF for 1 d, supplied with human serum albumin as a carrier protein, inhibited (P &lt; .05) FSH-induced estradiol production by bovine granulosa cells, with the greatest inhibition detected at 1.0 ng/mL; coculture with 10 micrograms/mL of heparin did not influence these effects.	Heparin	274-281	fibroblast growth factor 2	Bos taurus	34-38
7883629-6	1994	The presence of heparin (10 micrograms/mL) had variable effects on granulosa cell estradiol and progesterone production inhibited by carrier-free bFGF.	Heparin	16-23	fibroblast growth factor 2	Bos taurus	146-150
7523424-5	1994	Both the bFGF/uPA-inducing activity and the angiogenic activity of SK-Hep1 cell-conditioned medium copurify with a relatively acid-resistant peptide that has moderate affinity for heparin and M(r) &lt; 18 kDa &gt; 3.5 kDa.	Heparin	180-187	fibroblast growth factor 2	Homo sapiens	9-13
7929600-5	1994	When the same 24-kD bFGF cDNA was expressed in E. coli, the recombinant protein was purified to homogeneity by heparin-Sepharose and ion-exchange chromatography.	Heparin	111-118	fibroblast growth factor 2	Homo sapiens	20-24
8072119-9	1994	We conclude that, by binding near the carboxyl terminal region and adjacent to the heparin-binding domain of the fibronectin molecule, BCG may protect this region of the molecule from tumor proteases, and may thus allow the antitumor activity of the host immune cells to take place.	Heparin	83-90	fibronectin 1	Homo sapiens	113-124
8093049-5	1994	When mesangial cells were stimulated by IL-1 beta in the presence of heparin, transin expression was markedly suppressed in a dose-dependent manner.	Heparin	69-76	interleukin 1 beta	Homo sapiens	40-49
7522446-1	1994	The binding of the 165 amino-acid form of vascular endothelial growth factor (VEGF165) to the VEGF receptors of vascular endothelial cells was potentiated by heparin and heparan-sulfate, but not by other glycosaminoglycans.	Heparin	158-165	vascular endothelial growth factor A	Homo sapiens	42-76
7522446-1	1994	The binding of the 165 amino-acid form of vascular endothelial growth factor (VEGF165) to the VEGF receptors of vascular endothelial cells was potentiated by heparin and heparan-sulfate, but not by other glycosaminoglycans.	Heparin	158-165	vascular endothelial growth factor A	Homo sapiens	78-82
7522446-7	1994	These results suggest that the mechanism by which heparin modulates the binding of VEGF165 to the VEGF receptors may require an interaction with cell surface heparin binding molecules.	Heparin	50-57	vascular endothelial growth factor A	Homo sapiens	83-87
7522446-7	1994	These results suggest that the mechanism by which heparin modulates the binding of VEGF165 to the VEGF receptors may require an interaction with cell surface heparin binding molecules.	Heparin	158-165	vascular endothelial growth factor A	Homo sapiens	83-87
8093031-0	1994	Localization of heparin-binding, neurite outgrowth and antigenic regions in midkine molecule.	Heparin	16-23	midkine	Homo sapiens	76-83
8093031-1	1994	Midkine is a 13kDa heparin-binding polypeptide rich in basic amino acids and cysteine and has neurite outgrowth, neuronal cell survival and other activities.	Heparin	19-26	midkine	Homo sapiens	0-7
7923685-1	1994	BACKGROUND: Although the indirect thrombin inhibitor heparin and the more potent direct inhibitor hirudin are useful in preventing thrombosis, a substantial opportunity remains for improving the thrombus selectivity of thrombin inhibitors.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	34-42
7945195-6	1994	This lipoprotein lipase activity could be recovered into the perfusion medium completely by heparin perfusion of the liver.	Heparin	92-99	lipoprotein lipase	Rattus norvegicus	5-23
7945195-8	1994	However, heparin treatment of the liver decreases the ability of the liver to re-bind hepatic lipase by 80%.	Heparin	9-16	lipase C, hepatic type	Rattus norvegicus	86-100
7945195-12	1994	In these rats also, hepatic lipase bound only to livers which had been pre-perfused with heparin or 0.3 M NaCl.	Heparin	89-96	lipase C, hepatic type	Rattus norvegicus	20-34
7945195-13	1994	After heparin pre-perfusion, 88 +/- 12 m-units of hepatic lipase could be bound per g of liver, similar to that with livers of control rats not treated with ACTH.	Heparin	6-13	lipase C, hepatic type	Rattus norvegicus	50-64
7945195-16	1994	These results indicate that in rat liver the binding of hepatic lipase is heterogeneous in character and consists of heparin-resistant and heparin-sensitive components.	Heparin	117-124	lipase C, hepatic type	Rattus norvegicus	56-70
7945195-16	1994	These results indicate that in rat liver the binding of hepatic lipase is heterogeneous in character and consists of heparin-resistant and heparin-sensitive components.	Heparin	139-146	lipase C, hepatic type	Rattus norvegicus	56-70
7522051-5	1994	The mutant K128Q-K138Q required a 10-fold higher concentration of heparin to promote binding to heparan sulfate proteoglycan (HSPG)-deficient CHO cells transfected with fibroblast growth factor receptor-1 (FGFR1) or to induce DNA synthesis in HSPG-deficient myeloid cells transfected with FGFR1.	Heparin	66-73	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	96-124
7522051-5	1994	The mutant K128Q-K138Q required a 10-fold higher concentration of heparin to promote binding to heparan sulfate proteoglycan (HSPG)-deficient CHO cells transfected with fibroblast growth factor receptor-1 (FGFR1) or to induce DNA synthesis in HSPG-deficient myeloid cells transfected with FGFR1.	Heparin	66-73	LOW QUALITY PROTEIN: basement membrane-specific heparan sulfate proteoglycan core protein	Cricetulus griseus	126-130
7946786-2	1994	Additionally, if too much heparin is present it interferes with the INR, and the half life of prothrombin suggests that the patient should be anticoagulated with heparin for up to 96 hours after starting warfarin.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	94-105
7840725-4	1994	However, incubation of the vessels with heparin or a calcium channel blocker did prevented the vasoconstrictor effect of thrombin in human umbilical veins.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	121-129
8077206-5	1994	Both dexamethasone and heparin reduced ET-1-activated PGHS-2 mRNA expression and protein formation.	Heparin	23-30	endothelin 1	Rattus norvegicus	39-43
8092297-6	1994	The results of this study 1) imply that postischemic leukocyte/endothelium interaction can be attenuated by a low and clinically more relevant dose of SOD, and 2) caveat the administration of heparin in laboratory animals (i.e., to keep catheters patent) in studies of experimental ischemia/reperfusion injury or other oxygen radical-dependent pathomechanisms.	Heparin	192-199	superoxide dismutase 1	Homo sapiens	151-154
7988042-8	1994	Serum EC-SOD in Group I healthy persons is known to be heterogeneous with regard to heparin affinity and can be separated into three fractions: A without affinity, B with weak affinity and C with relatively strong heparin affinity, whereas the EC-SOD in Group II is mainly one fraction of C-type.	Heparin	84-91	superoxide dismutase 3	Homo sapiens	6-12
7988042-10	1994	EC-SOD in Group II showed two different profiles on heparin-Sepharose column chromatographies: one consisted mainly of EC-SOD C and the other consisted of EC-SOD A and C. It is probable that the high serum EC-SOD level in hemodialysis patients was due to two possible factors: the genetic transmitted factor and unknown pathophysiological factor(s).	Heparin	52-59	superoxide dismutase 3	Homo sapiens	0-6
7806968-4	1994	LPL activity was similar in the heparin-releasable (HR) fractions of heart and soleus (predominantly type I fibers), while in the EXT fraction LPL activity in soleus was 418 +/- 48 nEq/min per g, and in heart was 272 +/- 30 nEq/min per g (P &lt; 0.05).	Heparin	32-39	lipoprotein lipase	Rattus norvegicus	0-3
8087958-1	1994	Currently used antithrombotics such as heparin have a number of potential limitations that may be overcome by the new class of agents that directly inhibit thrombin.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	156-164
7520751-4	1994	The conditional reactions of bFGF and FGFR1 in the presence of heparin were then examined under conditions that saturate only the bFGF heparin site (1.5 equiv of HS/bFGF) or saturate the HS binding sites of both bFGF and FGFR1 (1.0 mM HS).	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	29-33
7992258-0	1994	Plasma TFPI activity after intravenous injection of pentasaccharide (PS) and unfractionated heparin in rabbits.	Heparin	92-99	tissue factor pathway inhibitor	Oryctolagus cuniculus	7-11
7992258-1	1994	Tissue Factor Pathway Inhibitor (TFPI), is known, to be released in plasma after injection of intravenous or subcutaneous injection of heparin or low molecular weight heparin (1,2).	Heparin	135-142	tissue factor pathway inhibitor	Oryctolagus cuniculus	0-31
7992258-1	1994	Tissue Factor Pathway Inhibitor (TFPI), is known, to be released in plasma after injection of intravenous or subcutaneous injection of heparin or low molecular weight heparin (1,2).	Heparin	135-142	tissue factor pathway inhibitor	Oryctolagus cuniculus	33-37
7992258-1	1994	Tissue Factor Pathway Inhibitor (TFPI), is known, to be released in plasma after injection of intravenous or subcutaneous injection of heparin or low molecular weight heparin (1,2).	Heparin	167-174	tissue factor pathway inhibitor	Oryctolagus cuniculus	0-31
7992258-1	1994	Tissue Factor Pathway Inhibitor (TFPI), is known, to be released in plasma after injection of intravenous or subcutaneous injection of heparin or low molecular weight heparin (1,2).	Heparin	167-174	tissue factor pathway inhibitor	Oryctolagus cuniculus	33-37
7520751-5	1994	Both 3-and 5-kDa low MW heparins increased the affinity for FGFR1 binding to bFGF by approximately 10-fold (Kd = 4.9 +/- 2.0 nM), relative to the reaction with no HS.	Heparin	24-32	fibroblast growth factor receptor 1	Homo sapiens	60-65
7520751-5	1994	Both 3-and 5-kDa low MW heparins increased the affinity for FGFR1 binding to bFGF by approximately 10-fold (Kd = 4.9 +/- 2.0 nM), relative to the reaction with no HS.	Heparin	24-32	fibroblast growth factor 2	Homo sapiens	77-81
7520755-7	1994	Binding of truncated (minimal) high-affinity ligands to VEGF is competitive with that of other truncated ligands and heparin.	Heparin	117-124	vascular endothelial growth factor A	Homo sapiens	56-60
8049432-5	1994	In contrast, when low-affinity heparin was added at the beginning of the reaction, there was an initial increase in PAI-1-thrombin complex formation, but this was rapidly followed by substantial proteolytic cleavage of unreacted PAI-1 and of the thrombin-PAI-1 complex.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	246-254
8049432-7	1994	Quantitative zymographic analysis of tissue plasminogen activator and PAI-1 activities and chromogenic substrate assay of thrombin activity showed that low-affinity heparin stimulated the inactivation of PAI-1 by an equimolar amount of thrombin, but caused only a minimal stimulation of thrombin inhibition.	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	122-130
8049432-0	1994	Low-affinity heparin stimulates the inactivation of plasminogen activator inhibitor-1 by thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	89-97
8049432-1	1994	The influence of heparin on the reaction between thrombin and plasminogen activator inhibitor-1 (PAI-1) has been examined.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	49-57
8049432-7	1994	Quantitative zymographic analysis of tissue plasminogen activator and PAI-1 activities and chromogenic substrate assay of thrombin activity showed that low-affinity heparin stimulated the inactivation of PAI-1 by an equimolar amount of thrombin, but caused only a minimal stimulation of thrombin inhibition.	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	236-244
8049432-2	1994	With a 50-fold excess of PAI-1, the rate constant for the inhibition of thrombin was 458 mol/L-1s-1, which increased to 5,000 mol/L-1s-1 in the presence of 25 micrograms/mL unfractionated heparin or heparin with low affinity for antithrombin.	Heparin	188-195	coagulation factor II, thrombin	Homo sapiens	72-80
8049432-7	1994	Quantitative zymographic analysis of tissue plasminogen activator and PAI-1 activities and chromogenic substrate assay of thrombin activity showed that low-affinity heparin stimulated the inactivation of PAI-1 by an equimolar amount of thrombin, but caused only a minimal stimulation of thrombin inhibition.	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	236-244
8049432-2	1994	With a 50-fold excess of PAI-1, the rate constant for the inhibition of thrombin was 458 mol/L-1s-1, which increased to 5,000 mol/L-1s-1 in the presence of 25 micrograms/mL unfractionated heparin or heparin with low affinity for antithrombin.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	72-80
8049432-4	1994	Thrombin and PAI-1 formed a stable stoichiometric complex in the absence of heparin, which did not dissociate after the addition of 25 micrograms/mL low-affinity heparin.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	0-8
8049432-8	1994	It is concluded that low-affinity heparin stimulates thrombin inhibition when PAI-1 is in excess, but, unexpectedly, that low-affinity heparin enhances PAI-1 inactivation when thrombin is equimolar to PAI-1.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	53-61
8049432-5	1994	In contrast, when low-affinity heparin was added at the beginning of the reaction, there was an initial increase in PAI-1-thrombin complex formation, but this was rapidly followed by substantial proteolytic cleavage of unreacted PAI-1 and of the thrombin-PAI-1 complex.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	122-130
8049432-8	1994	It is concluded that low-affinity heparin stimulates thrombin inhibition when PAI-1 is in excess, but, unexpectedly, that low-affinity heparin enhances PAI-1 inactivation when thrombin is equimolar to PAI-1.	Heparin	135-142	coagulation factor II, thrombin	Homo sapiens	176-184
7519608-0	1994	Heparin, heparan sulfate, and dermatan sulfate regulate formation of the insulin-like growth factor-I and insulin-like growth factor-binding protein complexes.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	73-101
7519608-5	1994	Heparin exposure was associated with a 17-fold decrease in the affinity of IGFBP-5 for IGF-I.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	75-82
7519608-3	1994	Heparin inhibited formation of the IGF-I.IGFBP-5 complex and also separated preformed IGF-I.IGFBP-5 complexes.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	35-40
7519608-5	1994	Heparin exposure was associated with a 17-fold decrease in the affinity of IGFBP-5 for IGF-I.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	87-92
7519608-3	1994	Heparin inhibited formation of the IGF-I.IGFBP-5 complex and also separated preformed IGF-I.IGFBP-5 complexes.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	41-48
7519608-6	1994	A synthetic peptide that contains residues from Arg221 to Arg238 of IGFBP-5, and a heparin binding domain prevented the inhibitory effects of heparin on formation of the IGF-I.IGFBP-5 complex.	Heparin	83-90	insulin like growth factor 1	Homo sapiens	170-175
7519608-6	1994	A synthetic peptide that contains residues from Arg221 to Arg238 of IGFBP-5, and a heparin binding domain prevented the inhibitory effects of heparin on formation of the IGF-I.IGFBP-5 complex.	Heparin	83-90	insulin like growth factor binding protein 5	Homo sapiens	176-183
7519608-3	1994	Heparin inhibited formation of the IGF-I.IGFBP-5 complex and also separated preformed IGF-I.IGFBP-5 complexes.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	86-91
7519608-6	1994	A synthetic peptide that contains residues from Arg221 to Arg238 of IGFBP-5, and a heparin binding domain prevented the inhibitory effects of heparin on formation of the IGF-I.IGFBP-5 complex.	Heparin	142-149	insulin like growth factor binding protein 5	Homo sapiens	68-75
7519608-6	1994	A synthetic peptide that contains residues from Arg221 to Arg238 of IGFBP-5, and a heparin binding domain prevented the inhibitory effects of heparin on formation of the IGF-I.IGFBP-5 complex.	Heparin	142-149	insulin like growth factor 1	Homo sapiens	170-175
7519608-6	1994	A synthetic peptide that contains residues from Arg221 to Arg238 of IGFBP-5, and a heparin binding domain prevented the inhibitory effects of heparin on formation of the IGF-I.IGFBP-5 complex.	Heparin	142-149	insulin like growth factor binding protein 5	Homo sapiens	176-183
7519608-3	1994	Heparin inhibited formation of the IGF-I.IGFBP-5 complex and also separated preformed IGF-I.IGFBP-5 complexes.	Heparin	0-7	insulin like growth factor binding protein 5	Homo sapiens	92-99
7519608-4	1994	Heparin also inhibited formation of the IGF-I.IGFBP-3 complex; however, it did not inhibit formation of complexes between IGF-I and IGFBP-1, -2, or -4.	Heparin	0-7	insulin like growth factor 1	Homo sapiens	40-45
8067851-5	1994	The maximum myeloperoxidase levels were significantly lower in the heparin-coated group than those in the uncoated group (p = 0.03).	Heparin	67-74	myeloperoxidase	Homo sapiens	12-27
8043862-10	1994	Removal of heparin-binding molecules from A4 cell lysates diminished binding to the 3T3 cells and digestion of the 3T3 cell surface with heparinase abolished the binding of CD45 and Mac-1.	Heparin	11-18	integrin alpha M	Mus musculus	182-187
7822240-5	1994	Apolipoprotein (apo) E-free HDL2 from the patients, separated by heparin-Sepharose column chromatography, was rich in CE, poor in triglycerides (TG), and enlarged in size on 4-30% nondenaturing polyacrylamide gradient gel electrophoresis.	Heparin	65-72	apolipoprotein E	Homo sapiens	0-22
7827407-0	1994	Structural features in heparin which modulate specific biological activities mediated by basic fibroblast growth factor.	Heparin	23-30	fibroblast growth factor 2	Homo sapiens	89-119
7827407-1	1994	The biological activity of basic fibroblast growth factor (bFGF) is influenced greatly by direct binding to heparin and heparan sulphate (HS).	Heparin	108-115	fibroblast growth factor 2	Homo sapiens	27-57
7827407-1	1994	The biological activity of basic fibroblast growth factor (bFGF) is influenced greatly by direct binding to heparin and heparan sulphate (HS).	Heparin	108-115	fibroblast growth factor 2	Homo sapiens	59-63
7827407-8	1994	The results of these studies indicate that both 2-O-sulphate and the negative charge of the carboxy group [L-iduronic acid (IdoA) residues] are required for specific interactions of heparin-derived oligosaccharides with bFGF and for modulation of bFGF mitogenic activity.	Heparin	182-189	fibroblast growth factor 2	Homo sapiens	220-224
7827407-8	1994	The results of these studies indicate that both 2-O-sulphate and the negative charge of the carboxy group [L-iduronic acid (IdoA) residues] are required for specific interactions of heparin-derived oligosaccharides with bFGF and for modulation of bFGF mitogenic activity.	Heparin	182-189	fibroblast growth factor 2	Homo sapiens	247-251
7992240-6	1994	In contrast, in the presence of heparin, the reaction rates of the G392P and wild-type AT forms with thrombin, differed by less than 25%.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	101-109
7806638-3	1994	Phosphorylation of caldesmon and casein by smooth muscle casein kinase II was optimal at approximately 0.1 M NaCl, did not require second messengers, and was inhibited by heparin.	Heparin	171-178	caldesmon 1	Homo sapiens	19-28
7990668-2	1994	Precipitation of apolipoprotein B containing lipoproteins takes place in wells of microtiter plates after 100 microL of serum are mixed with 20 microL of a heparin/MnCl2 solution.	Heparin	156-163	apolipoprotein B	Homo sapiens	17-33
8027055-7	1994	The mutant and wild type thrombin are inhibited at comparable rates by antithrombin +/- the pentasaccharide capable of inducing the "active" antithrombin conformation, but heparin acceleration of antithrombin inhibition of the mutant is reduced by more than 95%.	Heparin	172-179	coagulation factor II, thrombin	Homo sapiens	25-33
7518917-7	1994	Competition with heparin suggests that these RNAs bind the electropositive heparin-binding site of thrombin.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	99-107
7518917-7	1994	Competition with heparin suggests that these RNAs bind the electropositive heparin-binding site of thrombin.	Heparin	75-82	coagulation factor II, thrombin	Homo sapiens	99-107
7932105-2	1994	We described an amidolytic method for determining the anticoagulant activity of commercially available low molecular-weight heparin (LMWH) with the use of factor Xa (FXa) and thrombin (FIIa), and a chromogenic peptidyl substrate, S-2222 or S-2238.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	175-183
8034674-4	1994	The EC-SOD in the plasma of these individuals, collected both before and after intravenous injection of heparin, displayed a reduced heparin affinity when compared with samples from normal individuals.	Heparin	104-111	superoxide dismutase 3	Homo sapiens	4-10
8034674-4	1994	The EC-SOD in the plasma of these individuals, collected both before and after intravenous injection of heparin, displayed a reduced heparin affinity when compared with samples from normal individuals.	Heparin	133-140	superoxide dismutase 3	Homo sapiens	4-10
8034674-9	1994	Recombinant EC-SOD containing this mutation had a reduced heparin affinity similar to that of EC-SOD C from variant persons.	Heparin	58-65	superoxide dismutase 3	Homo sapiens	12-18
8025278-1	1994	The ability of heparin to dramatically enhance the inactivation of thrombin (IIa) by antithrombin III (ATIII) in buffer is negated through formation of a IIa-fibrin-heparin ternary complex (Hogg and Jackson, Proc Natl Acad Sci USA 86:3619, 1989; Hogg and Jackson, J Biol Chem 265:241, 1990).	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	67-75
8025278-4	1994	We found that soluble fibrin ablated the heparin-mediated prolongation of the thrombin time with half-maximal effect at 60 nmol/L fibrin.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	78-86
8027075-5	1994	Heparin was found to increase markedly the rate at which chymase activates procollagenase both by accelerating the cleavage of procollagenase and also by preventing its further degradation.	Heparin	0-7	chymase 1	Homo sapiens	57-64
8026029-10	1994	Time from recanalization to reocclusion (minutes, mean +/- SEM) was prolonged in the APC group (103.2 +/- 14.2) as compared with the control (10.2 +/- 2.3, P &lt; .001) and heparin (30.3 +/- 11.8, P &lt; .002) groups.	Heparin	173-180	APC regulator of WNT signaling pathway	Canis lupus familiaris	85-88
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	60-67	plasminogen activator, tissue type	Homo sapiens	282-315
8013074-0	1994	Heparin decreases activator protein-1 binding to DNA in part by posttranslational modification of Jun B.	Heparin	0-7	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	98-103
8013074-5	1994	The major effect of heparin is at the level of posttranslational modification of Jun B.	Heparin	20-27	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	81-86
8013074-7	1994	Evidence is presented suggesting that the heparin-inhibited event is phosphorylation of Jun B.	Heparin	42-49	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	88-93
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	60-67	plasminogen activator, tissue type	Homo sapiens	317-321
8040253-3	1994	In vitro nonezymatic glycosylation of basic fibroblast growth factor (bFGF) by fructose, glucose-6-phosphate (G6P), or glyceraldehyde-3-phosphate (G3P) reduced high affinity heparin-binding activity of recombinant bFGF by 73, 77, and 89%, respectively.	Heparin	174-181	fibroblast growth factor 2	Bos taurus	38-68
8040253-3	1994	In vitro nonezymatic glycosylation of basic fibroblast growth factor (bFGF) by fructose, glucose-6-phosphate (G6P), or glyceraldehyde-3-phosphate (G3P) reduced high affinity heparin-binding activity of recombinant bFGF by 73, 77, and 89%, respectively.	Heparin	174-181	fibroblast growth factor 2	Bos taurus	70-74
8040268-4	1994	The supernatant of thrombin-stimulated platelets contained an inhibitor of bFGF-induced mitogenesis; this activity coeluted with PF 4 upon gel filtration, heparin-agarose, and ion-exchange chromatography.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	19-27
8040268-4	1994	The supernatant of thrombin-stimulated platelets contained an inhibitor of bFGF-induced mitogenesis; this activity coeluted with PF 4 upon gel filtration, heparin-agarose, and ion-exchange chromatography.	Heparin	155-162	fibroblast growth factor 2	Homo sapiens	75-79
8040253-3	1994	In vitro nonezymatic glycosylation of basic fibroblast growth factor (bFGF) by fructose, glucose-6-phosphate (G6P), or glyceraldehyde-3-phosphate (G3P) reduced high affinity heparin-binding activity of recombinant bFGF by 73, 77, and 89%, respectively.	Heparin	174-181	fibroblast growth factor 2	Bos taurus	214-218
8040268-9	1994	Inhibition of bFGF activity by PF 4 could be overcome by exogenous heparin or chondroitin-4-sulfate, suggesting that inhibition of mitogenesis is caused by binding of PF 4 to cell-surface glycosaminoglycans.	Heparin	67-74	fibroblast growth factor 2	Homo sapiens	14-18
7965660-12	1994	Two lipophilic chains, lauryl (C12) and stearyl (C18), were then coupled to a single heparin chain, resulting in a heparin derivative having enhanced hydrophobicity.	Heparin	85-92	Bardet-Biedl syndrome 9	Homo sapiens	49-52
7965660-9	1994	Caprylic (C8), capric (C10), lauric (C12), and stearic (C18) hydrazide derivatives of heparin were prepared using this approach.	Heparin	86-93	Bardet-Biedl syndrome 9	Homo sapiens	56-59
7965660-12	1994	Two lipophilic chains, lauryl (C12) and stearyl (C18), were then coupled to a single heparin chain, resulting in a heparin derivative having enhanced hydrophobicity.	Heparin	115-122	Bardet-Biedl syndrome 9	Homo sapiens	49-52
7974380-4	1994	Heparin is shown to prolong the lag-time of thrombin generation more in native blood than in recalcified citrated blood.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	44-52
8011637-10	1994	Heparin was also found to potentiate the ability of wild-type glia-derived nexin to inhibit the thrombin-induced retraction of neurites from neuroblastoma NB2a cells.	Heparin	0-7	coagulation factor II	Mus musculus	96-104
7516895-5	1994	Pre-incubation of VN with purified heparin partially blocked the RMCP-1 inhibiting activity of VN.	Heparin	35-42	mast cell protease 1-like 1	Rattus norvegicus	65-71
8010949-6	1994	The antibody-binding protein (ABP) solubilized from platelets, cerebellum, and smooth muscle chromatographed identically on gel filtration, anion-exchange and heparin-TSK h.p.l.c.	Heparin	159-166	sex hormone binding globulin	Homo sapiens	30-33
7516895-5	1994	Pre-incubation of VN with purified heparin partially blocked the RMCP-1 inhibiting activity of VN.	Heparin	35-42	vitronectin	Rattus norvegicus	95-97
7516895-3	1994	In the present investigation it was shown that RMCP-1 is inhibited by vitronectin (VN), an RGD-containing adhesive glycoprotein with heparin-binding properties.	Heparin	133-140	mast cell protease 1-like 1	Rattus norvegicus	47-53
7516895-3	1994	In the present investigation it was shown that RMCP-1 is inhibited by vitronectin (VN), an RGD-containing adhesive glycoprotein with heparin-binding properties.	Heparin	133-140	vitronectin	Rattus norvegicus	70-81
7516895-7	1994	However, heat treatment of plasma VN, which is known to expose the heparin-binding domain, induced RMCP-1-inhibiting activity.	Heparin	67-74	vitronectin	Rattus norvegicus	34-36
7516895-3	1994	In the present investigation it was shown that RMCP-1 is inhibited by vitronectin (VN), an RGD-containing adhesive glycoprotein with heparin-binding properties.	Heparin	133-140	vitronectin	Rattus norvegicus	83-85
7516895-5	1994	Pre-incubation of VN with purified heparin partially blocked the RMCP-1 inhibiting activity of VN.	Heparin	35-42	vitronectin	Rattus norvegicus	18-20
7516895-7	1994	However, heat treatment of plasma VN, which is known to expose the heparin-binding domain, induced RMCP-1-inhibiting activity.	Heparin	67-74	mast cell protease 1-like 1	Rattus norvegicus	99-105
7516895-9	1994	The binding of RMCP-1 to VN was not heparin-dependent since free RMCP-1 bound with equal affinity to the immobilized VN as RMCP-1 present in complex with heparin.	Heparin	154-161	mast cell protease 1-like 1	Rattus norvegicus	15-21
8086338-5	1994	Western blot analysis of growth factors revealed the presence of the M(r) 18,000, 22,000 and 24,000 forms of basic fibroblast growth factor (bFGF or FGF2) both in HBL100 cell extracts partially purified on heparin-Sepharose beads and in concentrated conditioned medium.	Heparin	206-213	fibroblast growth factor 2	Homo sapiens	141-145
8013625-0	1994	Characterization of a novel monoclonal antibody (V58A4) raised against a recombinant NH2-terminal heparin-binding fragment of human endothelial cell thrombospondin.	Heparin	98-105	thrombospondin 1	Homo sapiens	149-163
8013625-1	1994	We report herein the characterization of a mouse monoclonal antibody (Mab) raised against the recombinant NH2-terminal heparin-binding domain (rHBD) of human endothelial cell thrombospondin (TSP).	Heparin	119-126	thrombospondin 1	Homo sapiens	175-189
8013625-1	1994	We report herein the characterization of a mouse monoclonal antibody (Mab) raised against the recombinant NH2-terminal heparin-binding domain (rHBD) of human endothelial cell thrombospondin (TSP).	Heparin	119-126	thrombospondin 1	Homo sapiens	191-194
8202520-0	1994	Molecular mapping of the heparin-binding exosite of thrombin.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	52-60
8202520-4	1994	To define the functional heparin-binding site on thrombin, purified recombinant alpha-thrombins were prepared with glutamic acid substitution for selected basic amino acid residues in exosite II or exosite I.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	49-57
8203472-5	1994	By in situ hybridization, the transcripts for elastin nd biglycan were primarily localized to smooth muscle cells in the intima and were diminished by heparin in proportion to the decrease in intimal mass.	Heparin	151-158	biglycan	Rattus norvegicus	57-65
7514646-9	1994	aFGF (20 ng/ml) plus heparin (17 micrograms/ml) induced a maximal 30-kDa increase at 8 h, which stayed stable for up to 24 h. The effect of aFGF was concentration dependent.	Heparin	21-28	fibroblast growth factor 1	Homo sapiens	140-144
7974349-4	1994	The epitope of MAb 710, which inhibits the binding of vWF to glycoprotein Ib (GPIb), was identified between Ser 593 and Ser 678 on the tryptic 52/48 kDa fragment (aa 449-728) which contains binding domains for GPIb, collagen, heparin, sulfatides and subendothelium extracellular matrices.	Heparin	226-233	von Willebrand factor	Homo sapiens	54-57
8189220-5	1994	More specifically, three distinct protein peaks eluted from the heparin-Sepharose column, two of which bound 125I-AngII with high affinity and saturability.	Heparin	64-71	angiotensinogen (serpin peptidase inhibitor, clade A, member 8)	Mus musculus	114-119
8086743-2	1994	Heparin-induced extracorporeal LDL precipitation (HELP) eliminates selectively fibrinogen, LDL cholesterol, cholesterol, triglycerides and LP(a) from the blood plasma using extracorporeal circulation.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	79-89
8182050-10	1994	The minimal heparin sequence required for binding to RMCP-1 was found in a 14-saccharide fraction.	Heparin	12-19	mast cell protease 1-like 1	Rattus norvegicus	53-59
8200348-5	1994	The activation of phospholipase C by vasopressin produced an influx of Mn2+ independent of the depletion of intracellular calcium stores if this depletion was delayed by the Ins(1,4,5)P3 receptor antagonist heparin or by the use of a low agonist concentration.	Heparin	207-214	arginine vasopressin	Rattus norvegicus	37-48
8182050-3	1994	The heparin.RMCP-1 complexes are stored in the secretory granules of the cells and are released following mast cell activation.	Heparin	4-11	mast cell protease 1-like 1	Rattus norvegicus	12-18
8182050-4	1994	We showed previously that dissociation of RMCP-1 from heparin resulted in loss of protease activity, as measured by its ability to inactivate thrombin.	Heparin	54-61	mast cell protease 1-like 1	Rattus norvegicus	42-48
8182050-4	1994	We showed previously that dissociation of RMCP-1 from heparin resulted in loss of protease activity, as measured by its ability to inactivate thrombin.	Heparin	54-61	coagulation factor II	Rattus norvegicus	142-150
8182050-5	1994	In the present report the binding of heparin to RMCP-1 was characterized.	Heparin	37-44	mast cell protease 1-like 1	Rattus norvegicus	48-54
8182050-6	1994	Affinity chromatography on heparin-Sepharose showed that RMCP-1 displayed high affinity for heparin, with approximately 1.2 M NaCl being required for elution of RMCP-1 from the affinity matrix.	Heparin	27-34	mast cell protease 1-like 1	Rattus norvegicus	57-63
8182050-6	1994	Affinity chromatography on heparin-Sepharose showed that RMCP-1 displayed high affinity for heparin, with approximately 1.2 M NaCl being required for elution of RMCP-1 from the affinity matrix.	Heparin	92-99	mast cell protease 1-like 1	Rattus norvegicus	57-63
8182050-7	1994	The structural requirements for the binding of heparin to RMCP-1 were investigated.	Heparin	47-54	mast cell protease 1-like 1	Rattus norvegicus	58-64
8182050-8	1994	Heparan sulfate, chondroitin sulfate, and dermatan sulfate, three glycosaminoglycans structurally related to heparin, were &gt; or = 80-fold less effective in binding to RMCP-1 than heparin.	Heparin	109-116	mast cell protease 1-like 1	Rattus norvegicus	170-176
8192672-0	1994	Interaction of transferrin and its iron-binding fragments with heparin.	Heparin	63-70	serotransferrin	Bos taurus	15-26
7910033-7	1994	Similar differential effects of heparin have been observed on the reactions of alpha-chymotrypsin with the two recombinant forms of SLPI.2=	Heparin	32-39	secretory leukocyte peptidase inhibitor	Homo sapiens	132-136
8074477-4	1994	Rather, both the basal and PMA-induced fibronectin adhesion of MDS cells could be inhibited by heparin and much less efficiently by chondroitin sulphate, suggesting that glycosaminoglycans of proteoglycans may be responsible for the change in adhesive phenotype.	Heparin	95-102	fibronectin 1	Homo sapiens	39-50
8192672-1	1994	The interaction of heparin with transferrin (Tf; bovine and rat) and the isolated iron-binding lobes of bovine Tf were investigated.	Heparin	19-26	serotransferrin	Bos taurus	32-43
8192672-1	1994	The interaction of heparin with transferrin (Tf; bovine and rat) and the isolated iron-binding lobes of bovine Tf were investigated.	Heparin	19-26	serotransferrin	Bos taurus	45-47
8192672-5	1994	In the presence of heparin, iron release from the N-terminal lobe of native bovine Tf was accelerated and from the C-terminal lobe it was slightly reduced.	Heparin	19-26	serotransferrin	Bos taurus	83-85
8043689-7	1994	Three hormone-binding sites in apoB-100 are located in different regions of the polypeptide chain which are distant from each other and lie outside the sites of heparin and cellular LDL receptor binding.	Heparin	161-168	apolipoprotein B	Homo sapiens	31-39
8192672-7	1994	The affinity of native bovine Tf for heparin was very close to that of its isolated N-terminal lobe, thus suggesting that it is this portion of the molecule that binds to the glycosaminoglycan.	Heparin	37-44	serotransferrin	Bos taurus	30-32
8192672-8	1994	It is concluded that the consequences for iron-binding strength of the two transferrin lobes are diagonally opposite when Tf is bound to heparin as opposed to its natural cell-surface receptor.	Heparin	137-144	serotransferrin	Bos taurus	75-86
8192672-8	1994	It is concluded that the consequences for iron-binding strength of the two transferrin lobes are diagonally opposite when Tf is bound to heparin as opposed to its natural cell-surface receptor.	Heparin	137-144	serotransferrin	Bos taurus	122-124
7921367-3	1994	The risk of coronary reocclusion after t-PA administration can be reduced with concomitant use of intravenous heparin given in therapeutic doses.	Heparin	110-117	plasminogen activator, tissue type	Homo sapiens	39-43
8167338-0	1994	Autoantibodies to heparin from patients with antiphospholipid antibody syndrome inhibit formation of antithrombin III-thrombin complexes.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	105-113
8167338-7	1994	Furthermore, APS IgG antiheparin antibodies inhibited heparin-accelerated formation of antithrombin III-thrombin complexes.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	91-99
8080937-2	1994	Fibrous, orientated mats, formed from solution under directional shear, could be made to incorporate heparin (typically 3.2 mu mg/mg fibronectin).	Heparin	101-108	fibronectin 1	Homo sapiens	133-144
7922353-5	1994	RESULTS: Using affinity co-electrophoresis we found that interleukin-8 preferentially bound a subfraction of heparin that also showed increased affinity for melanoma growth stimulating activity (also known as MGSA, GRO or GRO alpha).	Heparin	109-116	C-X-C motif chemokine ligand 8	Homo sapiens	57-70
8175651-4	1994	In contrast, similar concentrations of heparin potentiated the binding of 125I-VEGF165 to the endogenous VEGF receptors of the transfected cells, indicating that to some extent, the effect of heparin on 125I-VEGF165 binding is receptor type-dependent.	Heparin	39-46	vascular endothelial growth factor A	Homo sapiens	79-83
8056006-0	1994	Influence of heparin on fibrinogen and D-dimer plasma levels in acute myocardial infarction treated with streptokinase.	Heparin	13-20	fibrinogen beta chain	Homo sapiens	24-34
8056006-1	1994	The purpose of this study was to investigate whether, to what extent, and through which mechanisms intravenous heparin, administered before and after streptokinase, affects the plasma levels of D-dimer and fibrinogen in myocardial infarction.	Heparin	111-118	fibrinogen beta chain	Homo sapiens	206-216
7921790-8	1994	Further fractionation of the HDL2-HDL3 bound activity on heparin-agarose established that 70% of the recovered activity was bound to the apo-E containing HDL.	Heparin	57-64	apolipoprotein E	Mus musculus	137-142
8182139-3	1994	The procoagulant activity of TNF-alpha-stimulated endothelial cell monolayers was studied in a human ex vivo native (nonanticoagulated) blood flow system using the three thrombin inhibitors recombinant hirudin, Ro 46-6240, and heparin.	Heparin	227-234	tumor necrosis factor	Homo sapiens	29-38
8091386-9	1994	In the 5 hyperfibrinogenemic subjects, heparin administration significantly reduced fibrinogen (625.4 +/- 211.1 vs 455.2 +/- 112.3 mg/dl, p &lt; 0.03), prothrombin fragment (0.97 +/- 0.1 vs 0.63 +/- 0.2 nM, p &lt; 0.002) and D-dimer (336 +/- 101.8 vs 275.2 +/- 78.5 ng/ml, p &lt; 0.03).	Heparin	39-46	fibrinogen beta chain	Homo sapiens	14-24
8091386-9	1994	In the 5 hyperfibrinogenemic subjects, heparin administration significantly reduced fibrinogen (625.4 +/- 211.1 vs 455.2 +/- 112.3 mg/dl, p &lt; 0.03), prothrombin fragment (0.97 +/- 0.1 vs 0.63 +/- 0.2 nM, p &lt; 0.002) and D-dimer (336 +/- 101.8 vs 275.2 +/- 78.5 ng/ml, p &lt; 0.03).	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	152-163
8202668-9	1994	In contrast, the thrombin time shows--independently of OAC--a good correlation to heparin concentrations.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	17-25
8202668-10	1994	Therefore the thrombin time is more appropriate to monitor heparin therapy in the phase when oral anticoagulation is started.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	14-22
8175651-4	1994	In contrast, similar concentrations of heparin potentiated the binding of 125I-VEGF165 to the endogenous VEGF receptors of the transfected cells, indicating that to some extent, the effect of heparin on 125I-VEGF165 binding is receptor type-dependent.	Heparin	192-199	vascular endothelial growth factor A	Homo sapiens	79-83
8175651-9	1994	Both bFGF and aFGF inhibited the binding when low concentrations of heparin were added to the binding reaction.	Heparin	68-75	fibroblast growth factor 2	Homo sapiens	5-9
8175651-9	1994	Both bFGF and aFGF inhibited the binding when low concentrations of heparin were added to the binding reaction.	Heparin	68-75	fibroblast growth factor 1	Homo sapiens	14-18
8054461-6	1994	It was concluded that at least twice the dose of Fragmin (anti-FXa), compared with heparin, was required, suggesting that thrombin inhibition is crucial for the antithrombotic efficacy of heparin in CPB circuits.	Heparin	188-195	coagulation factor II, thrombin	Homo sapiens	122-130
8172600-7	1994	Heparin or ATP[S] inhibited, or delayed the onset of, both vasopressin-induced release of Ca2+ from intracellular stores and vasopressin-stimulated Ca2+ inflow.	Heparin	0-7	arginine vasopressin	Rattus norvegicus	59-70
8172600-7	1994	Heparin or ATP[S] inhibited, or delayed the onset of, both vasopressin-induced release of Ca2+ from intracellular stores and vasopressin-stimulated Ca2+ inflow.	Heparin	0-7	arginine vasopressin	Rattus norvegicus	125-136
8172600-8	1994	Vasopressin-induced oscillations in intracellular [Ca2+] were observed in some heparin-treated cells.	Heparin	79-86	arginine vasopressin	Rattus norvegicus	0-11
8172602-5	1994	A synthetic peptide with a sequence corresponding to the heparin-binding site of LPL (Ser-Arg-Thr-Asn-Thr-Lys-Val-Ser-Arg-Ile-Thr-Gly-Leu) was produced and used as an immunogen.	Heparin	57-64	lipoprotein lipase	Rattus norvegicus	81-84
8172612-7	1994	When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties.	Heparin	58-65	mast cell protease 1-like 1	Rattus norvegicus	5-11
8172612-8	1994	Affinity chromatography of endogenous [35S]heparin on matrix-linked RMCP-1 demonstrated that all of the heparin molecules contained high-affinity binding sites for the mast-cell protease.	Heparin	43-50	mast cell protease 1-like 1	Rattus norvegicus	68-74
8087553-1	1994	BACKGROUND: Antithrombin, a member of the serpin family of inhibitors, controls coagulation in human plasma by forming complexes with thrombin and other coagulation proteases in a process greatly accelerated by heparin.	Heparin	211-218	coagulation factor II, thrombin	Homo sapiens	16-24
8142385-2	1994	Previous reports have implicated the binding of heparin, or heparan sulfate, to FGF as essential for FGF-mediated signal transduction and mitogenicity.	Heparin	48-55	fibroblast growth factor 2	Homo sapiens	80-83
8142385-2	1994	Previous reports have implicated the binding of heparin, or heparan sulfate, to FGF as essential for FGF-mediated signal transduction and mitogenicity.	Heparin	48-55	fibroblast growth factor 2	Homo sapiens	101-104
8142385-4	1994	Amino acid residues on the surface of basic FGF (bFGF) were targeted as potential heparin contacts on the basis of the position of sulfate anions in the X-ray crystal structure of bFGF and of a modeled pentasaccharide heparin-bFGF complex.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	38-47
8142385-4	1994	Amino acid residues on the surface of basic FGF (bFGF) were targeted as potential heparin contacts on the basis of the position of sulfate anions in the X-ray crystal structure of bFGF and of a modeled pentasaccharide heparin-bFGF complex.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	49-53
8142385-4	1994	Amino acid residues on the surface of basic FGF (bFGF) were targeted as potential heparin contacts on the basis of the position of sulfate anions in the X-ray crystal structure of bFGF and of a modeled pentasaccharide heparin-bFGF complex.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	180-184
8142385-4	1994	Amino acid residues on the surface of basic FGF (bFGF) were targeted as potential heparin contacts on the basis of the position of sulfate anions in the X-ray crystal structure of bFGF and of a modeled pentasaccharide heparin-bFGF complex.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	180-184
8142385-6	1994	The combination of site-directed mutagenesis and titrating calorimetry permitted an analysis of the energetic contributions of individual bFGF residues in the binding of heparin to bFGF.	Heparin	170-177	fibroblast growth factor 2	Homo sapiens	138-142
8142385-6	1994	The combination of site-directed mutagenesis and titrating calorimetry permitted an analysis of the energetic contributions of individual bFGF residues in the binding of heparin to bFGF.	Heparin	170-177	fibroblast growth factor 2	Homo sapiens	181-185
8142385-7	1994	The key amino acids which comprise the heparin binding domain on bFGF constitute a discontinuous binding epitope and include K26, N27, R81, K119, R120, T121, Q123, K125, K129, Q134, and K135.	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	65-69
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	140-148
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	187-195
8159751-6	1994	TFPI-2 was expressed in baby hamster kidney cells and purified from the serum-free conditioned medium by a combination of heparin-agarose chromatography, Mono Q FPLC, Mono S FPLC, and Superose 12 FPLC.	Heparin	122-129	tissue factor pathway inhibitor 2	Homo sapiens	0-6
8159751-11	1994	In addition, the inhibition of factor VIIa-tissue factor amidolytic activity by recombinant TFPI-2 was markedly enhanced in the presence of heparin.	Heparin	140-147	tissue factor pathway inhibitor 2	Homo sapiens	92-98
8144627-0	1994	cDNA cloning and sequencing of mouse mastocytoma glucosaminyl N-deacetylase/N-sulfotransferase, an enzyme involved in the biosynthesis of heparin.	Heparin	138-145	sulfotransferase family 1D, member 1	Mus musculus	76-94
8144627-1	1994	A 110-kDa protein involved in heparin biosynthesis in mouse mastocytoma cells was previously shown to express both glucosaminyl N-deacetylase and N-sulfotransferase activity.	Heparin	30-37	sulfotransferase family 1D, member 1	Mus musculus	146-164
8154636-7	1994	Increased IL-4 ELISA levels in cultured supernatants were noted with heparin (P &lt; .25) and collagen (P &lt; .05).	Heparin	69-76	interleukin 4	Homo sapiens	10-14
8005535-1	1994	The high heparin-affinity subtype C of the secretory enzyme extracellular-superoxide dismutase (EC-SOD) mainly exists on the outside of endothelial cell surface in the vasculature.	Heparin	9-16	superoxide dismutase 3	Bos taurus	60-94
8005535-1	1994	The high heparin-affinity subtype C of the secretory enzyme extracellular-superoxide dismutase (EC-SOD) mainly exists on the outside of endothelial cell surface in the vasculature.	Heparin	9-16	superoxide dismutase 3	Bos taurus	96-102
7512972-6	1994	TN-X in conditioned medium, as well as the purified protein bind to heparin, but no binding to tenascin-C (TN-C), fibronectin, laminin or collagens could be detected.	Heparin	68-75	tenascin XB	Mus musculus	0-4
7812655-4	1994	With this in vitro system, Congo red and several sulfated polysaccharides, including heparin and pentosan polysulfate, were found to inhibit accumulation of protease-resistant PrP.	Heparin	85-92	prion protein	Homo sapiens	176-179
7812655-5	1994	These results and additional data confirming PrP binding to heparin suggested a possible role for sulfated glycosaminoglycans in the generation of protease-resistant PrP during scrapie infection.	Heparin	60-67	prion protein	Homo sapiens	45-48
7812655-5	1994	These results and additional data confirming PrP binding to heparin suggested a possible role for sulfated glycosaminoglycans in the generation of protease-resistant PrP during scrapie infection.	Heparin	60-67	prion protein	Homo sapiens	166-169
7511146-3	1994	Our previous work indicated that 1) TGF-beta 1 has strong heparin-binding properties that were not previously recognized because of neutralization by iodination, and 2) heparin, and certain other polyanions, could block the binding of TGF-beta 1 to alpha 2-macroglobulin (alpha 2-M).	Heparin	58-65	transforming growth factor beta 1	Homo sapiens	36-46
7511146-3	1994	Our previous work indicated that 1) TGF-beta 1 has strong heparin-binding properties that were not previously recognized because of neutralization by iodination, and 2) heparin, and certain other polyanions, could block the binding of TGF-beta 1 to alpha 2-macroglobulin (alpha 2-M).	Heparin	58-65	transforming growth factor beta 1	Homo sapiens	235-245
7511146-3	1994	Our previous work indicated that 1) TGF-beta 1 has strong heparin-binding properties that were not previously recognized because of neutralization by iodination, and 2) heparin, and certain other polyanions, could block the binding of TGF-beta 1 to alpha 2-macroglobulin (alpha 2-M).	Heparin	169-176	transforming growth factor beta 1	Homo sapiens	36-46
7511146-3	1994	Our previous work indicated that 1) TGF-beta 1 has strong heparin-binding properties that were not previously recognized because of neutralization by iodination, and 2) heparin, and certain other polyanions, could block the binding of TGF-beta 1 to alpha 2-macroglobulin (alpha 2-M).	Heparin	169-176	transforming growth factor beta 1	Homo sapiens	235-245
7511146-4	1994	The present studies investigated the influence of heparin-like molecules on the stability of the TGF-beta 1 signal in the pericellular environment.	Heparin	50-57	transforming growth factor beta 1	Homo sapiens	97-107
7511146-5	1994	The results indicate that heparin and fucoidan, a naturally occurring sulfated L-fucose polymer, suppress the formation of an initial non-covalent interaction between 125I-TGF-beta 1 and activated alpha 2-M.	Heparin	26-33	transforming growth factor beta 1	Homo sapiens	172-182
8006526-2	1994	Hepatic lipase activity was either reduced by preperfusion of livers with heparin or inhibited with specific rat hepatic lipase antibodies.	Heparin	74-81	lipase C, hepatic type	Rattus norvegicus	0-14
7511146-9	1994	Consistent with this protective effect, heparin- and fucoidan-treated SMC demonstrated elevated levels of active, but not latent, TGF-beta activity.	Heparin	40-47	transforming growth factor beta 1	Homo sapiens	130-138
8163669-8	1994	However, HuCIITg VLDL showed markedly decreased binding to heparin-Sepharose, suggesting that apoCII-rich, apoE-poor lipoprotein may be less accessible to cell surface lipases or receptors within their glycosaminoglycan matrices.	Heparin	59-66	apolipoprotein C2	Mus musculus	94-100
8163669-8	1994	However, HuCIITg VLDL showed markedly decreased binding to heparin-Sepharose, suggesting that apoCII-rich, apoE-poor lipoprotein may be less accessible to cell surface lipases or receptors within their glycosaminoglycan matrices.	Heparin	59-66	apolipoprotein E	Mus musculus	107-111
8028039-2	1994	One possible site of HSPG attachment is a heparin binding domain of fibronectin, which is present in the synthetic peptide FN-C/H II.	Heparin	42-49	syndecan 2	Rattus norvegicus	21-25
8117201-8	1994	Intramuscular implantation of bFGF in heparin-sepharose pellets at the time of arterial ligation markedly enhanced the blood flow for 3 weeks compared with untreated ischaemic limbs.	Heparin	38-45	fibroblast growth factor 2	Homo sapiens	30-34
8145071-2	1994	Heparin-releasable LPL activities, mass and mRNA were measured in heart, diaphragm and soleus muscle and epididymal fat after food deprivation and 1, 2, 4 and 8 h postprandially.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	19-22
8145071-4	1994	However, in cardiac and diaphragm muscle, heparin-releasable LPL activity was suppressed by HC but stimulated by HF meal-feeding at 4 h. Moreover, in adipose tissue, the HC meal increased LPL activity at 1, 2 and 4 h relative to the basal period.	Heparin	42-49	lipoprotein lipase	Rattus norvegicus	61-64
8145071-4	1994	However, in cardiac and diaphragm muscle, heparin-releasable LPL activity was suppressed by HC but stimulated by HF meal-feeding at 4 h. Moreover, in adipose tissue, the HC meal increased LPL activity at 1, 2 and 4 h relative to the basal period.	Heparin	42-49	lipoprotein lipase	Rattus norvegicus	188-191
8199741-12	1994	The thrombin time showed the same variation, which was also mirrored in the plasma heparin levels, although the circadian effect was not as marked.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	4-12
8135741-7	1994	Removal of EC-SOD from cell surfaces by heparin also did not influence SOD expression.	Heparin	40-47	superoxide dismutase 3	Homo sapiens	11-17
8135741-7	1994	Removal of EC-SOD from cell surfaces by heparin also did not influence SOD expression.	Heparin	40-47	superoxide dismutase 1	Homo sapiens	14-17
8135747-4	1994	The cytoplasmic domain of HPTP beta was strongly inhibited by vanadate, molybdate, heparin, poly(Glu, Tyr) (4:1) and zinc ions.	Heparin	83-90	protein tyrosine phosphatase receptor type B	Homo sapiens	26-35
8119547-6	1994	RESULTS: The inositol-1,4,5-trisphosphate (IP3) antagonist heparin blocked the contractions induced by CCK.	Heparin	59-66	cholecystokinin	Homo sapiens	103-106
7959358-3	1994	Thus, the mode of action of heparins on thrombin generation in plasma after addition of increasing amounts of unfractionated heparin (UH) or LMWH has been investigated in several studies, but a distinction has to be made between the effects on the intrinsic and the extrinsic system.	Heparin	28-36	coagulation factor II, thrombin	Homo sapiens	40-48
7959358-3	1994	Thus, the mode of action of heparins on thrombin generation in plasma after addition of increasing amounts of unfractionated heparin (UH) or LMWH has been investigated in several studies, but a distinction has to be made between the effects on the intrinsic and the extrinsic system.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	40-48
8056752-8	1994	The multimeric fibronectin retained heparin-binding and cell attachment activities, but had lost gelatin-binding activity.	Heparin	36-43	fibronectin 1	Homo sapiens	15-26
7959358-14	1994	Although thrombin inhibition seems essential for the antithrombotic activity of both heparins, reduction of thrombosis is a global effect to which "both anti-IIa and anti-Xa activity contribute but to a different exent" (C. Hemker et al.).	Heparin	85-93	coagulation factor II, thrombin	Homo sapiens	9-17
8011978-0	1994	Heparin suppresses endothelin-1 peptide and mRNA expression in cultured endothelial cells of spontaneously hypertensive rats.	Heparin	0-7	endothelin 1	Rattus norvegicus	19-31
8011978-2	1994	This study was designed to examine heparin"s effect on vasoconstrictor endothelin-1 production in cultured aortic endothelial cells (EC).	Heparin	35-42	endothelin 1	Rattus norvegicus	71-83
8011978-4	1994	Heparin suppressed endothelin-1 release and endothelin-1 mRNA expression in a dose- and a time-dependent fashion in both WKY and SHR.	Heparin	0-7	endothelin 1	Rattus norvegicus	19-31
8011978-4	1994	Heparin suppressed endothelin-1 release and endothelin-1 mRNA expression in a dose- and a time-dependent fashion in both WKY and SHR.	Heparin	0-7	endothelin 1	Rattus norvegicus	44-56
8011978-7	1994	These results suggest that heparin regulates endogenous endothelin-1 production by cultured EC, probably at the transcriptional level, and that this effect is more marked in SHR than in WKY.	Heparin	27-34	endothelin 1	Rattus norvegicus	56-68
8119932-1	1994	Lipoprotein lipase (LPL) was obtained from rat postheparin plasma by chromatographies on heparin-Sepharose and hydroxyapatite.	Heparin	51-58	lipoprotein lipase	Rattus norvegicus	0-18
8014574-10	1994	3) H-TGL-depleted rat livers were obtained by a 12-min preperfusion in the presence of heparin, displacing 90% of the enzymatic activity.	Heparin	87-94	lipase C, hepatic type	Rattus norvegicus	3-8
8133054-11	1994	Heparin, which is known to inhibit the interaction between SAP and C4BP, was also found to counteract the inhibitory effect of SAP on C4BP binding to C4(H2O).	Heparin	0-7	complement component 4 binding protein alpha	Homo sapiens	67-71
8133054-11	1994	Heparin, which is known to inhibit the interaction between SAP and C4BP, was also found to counteract the inhibitory effect of SAP on C4BP binding to C4(H2O).	Heparin	0-7	complement component 4 binding protein alpha	Homo sapiens	134-138
8133054-12	1994	However, the effect of heparin was biphasic because high concentrations of heparin directly inhibited binding of C4(H2O) to C4BP.	Heparin	23-30	complement component 4 binding protein alpha	Homo sapiens	124-128
8133054-12	1994	However, the effect of heparin was biphasic because high concentrations of heparin directly inhibited binding of C4(H2O) to C4BP.	Heparin	75-82	complement component 4 binding protein alpha	Homo sapiens	124-128
8139483-6	1994	PB treatment increased the heparin-releasable lipoprotein lipase (LPL) activity of epididymal fat in both control and low-dose diabetic groups; this was not assessed in the high-dose diabetic group.	Heparin	27-34	lipoprotein lipase	Rattus norvegicus	66-69
8016815-7	1994	The enhancement of the activation of plasminogen by t-PA or u-PA was more significant in the presence of HHS-5 than in the presence of chondroitin sulfate C, dextran sulfate or heparin.	Heparin	177-184	plasminogen activator, tissue type	Homo sapiens	52-56
8016815-7	1994	The enhancement of the activation of plasminogen by t-PA or u-PA was more significant in the presence of HHS-5 than in the presence of chondroitin sulfate C, dextran sulfate or heparin.	Heparin	177-184	plasminogen activator, urokinase	Homo sapiens	60-64
8029789-0	1994	Thrombin-based antithrombin assays show overestimation of antithrombin III activity in patients on heparin therapy due to heparin cofactor II influence.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	0-8
8029794-1	1994	We determined, in volunteers, the plasma levels of heparin above and below the critical chainlength necessary for thrombin inhibition (ACLM and BCLM), from 1 to 24 h after subcutaneous injection of 5000 IU unfractionated heparin (UFH), 40 mg enoxaparin and 1 mg/kg body weight of enoxaparin (LMWH) (n = 12 for each dose).	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	114-122
8119932-1	1994	Lipoprotein lipase (LPL) was obtained from rat postheparin plasma by chromatographies on heparin-Sepharose and hydroxyapatite.	Heparin	51-58	lipoprotein lipase	Rattus norvegicus	20-23
8180343-6	1994	Heparin species with longer polysaccharide chains appear to be required in order to enhance the inhibition of thrombin by antithrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	110-118
8043225-0	1994	Heparin specifically inhibits binding of V3 loop antibodies to HIV-1 gp120, an effect potentiated by CD4 binding.	Heparin	0-7	CD4 molecule	Homo sapiens	101-104
8043225-1	1994	OBJECTIVE: To investigate the binding of the sulphated polysaccharides, dextran sulphate and heparin, to CD4 and gp120 in order to examine the anti-HIV mechanisms of these compounds.	Heparin	93-100	CD4 molecule	Homo sapiens	105-108
8307950-8	1994	These results, in combination with the ability of heparin and chondroitin sulfate to compete for binding to DNs, demonstrate that these two glycosaminoglycans interact with similar or overlapping sites in FN.	Heparin	50-57	fibronectin 1	Homo sapiens	205-207
8307950-9	1994	One important difference between FN interactions with heparin and chondroitin sulfate is that, while FN and DNs bound equally to heparin, FN bound less efficiently than DNs to chondroitin sulfate.	Heparin	54-61	fibronectin 1	Homo sapiens	33-35
8307950-9	1994	One important difference between FN interactions with heparin and chondroitin sulfate is that, while FN and DNs bound equally to heparin, FN bound less efficiently than DNs to chondroitin sulfate.	Heparin	129-136	fibronectin 1	Homo sapiens	101-103
8307950-9	1994	One important difference between FN interactions with heparin and chondroitin sulfate is that, while FN and DNs bound equally to heparin, FN bound less efficiently than DNs to chondroitin sulfate.	Heparin	129-136	fibronectin 1	Homo sapiens	101-103
8305417-6	1994	The inhibitory activity of antithrombin III was enhanced in the presence of heparin, which on its own had no inhibitory effect on thrombin-induced DNA synthesis.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	31-39
8305417-7	1994	In contrast, the mitogenic activity of alpha-thrombin could be inhibited by heparin in the presence of low concentrations of serum.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	45-53
8305417-9	1994	Analysis of the enzymatic activity of thrombin showed that the influence on catalytic activity of thrombin corresponded to the mitogenic activity of thrombin in the presence of heparin, antithrombin III, and serum.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	38-46
8305417-9	1994	Analysis of the enzymatic activity of thrombin showed that the influence on catalytic activity of thrombin corresponded to the mitogenic activity of thrombin in the presence of heparin, antithrombin III, and serum.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	98-106
8305417-9	1994	Analysis of the enzymatic activity of thrombin showed that the influence on catalytic activity of thrombin corresponded to the mitogenic activity of thrombin in the presence of heparin, antithrombin III, and serum.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	98-106
8180343-7	1994	This may be because the enhancement of this reaction requires that heparin interacts simultaneously with both the antithrombin and the thrombin molecules.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	118-126
8180343-9	1994	The role of the heparin-induced conformational change in enhancing serine protease inhibition by antithrombin is also explored.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	67-82
8143454-1	1994	Fibronectin from human early pregnancy (5-8 weeks) placenta (epFN) has been isolated by 2M urea-PBS extraction and purified by heparin-Sepharose 4B affinity chromatography followed by Sepharose CL-6B gel filtration, and compared with that of term placenta (tpFN).	Heparin	127-134	fibronectin 1	Homo sapiens	0-11
8180139-6	1994	Small differences in the circular dichroism spectrum of gelatin affinity-purified fibronectin were observed before and after removal of aggregates by gel permeation FPLC, and similar changes were seen when heparin was added to FLPC-purified fibronectin, without subsequent removal of aggregates.	Heparin	206-213	fibronectin 1	Homo sapiens	241-252
7507851-7	1994	Although basic FGF showed little activity on rat hepatocytes, acidic FGF stimulated DNA synthesis by approximately twofold and was substantially enhanced by heparin.	Heparin	157-164	fibroblast growth factor 1	Homo sapiens	69-72
8076974-8	1994	Addition of glycosaminoglycans such as hyaluronic acid, chondroitin sulphate, and heparin into the medium cause significant increase in the synthesis and secretion of [3H]apoB into the medium indicating a possible secretory control of apoB by local reuptake.	Heparin	82-89	apolipoprotein B	Rattus norvegicus	171-175
8076974-8	1994	Addition of glycosaminoglycans such as hyaluronic acid, chondroitin sulphate, and heparin into the medium cause significant increase in the synthesis and secretion of [3H]apoB into the medium indicating a possible secretory control of apoB by local reuptake.	Heparin	82-89	apolipoprotein B	Rattus norvegicus	235-239
8180139-0	1994	Heparin binding to monodisperse plasma fibronectin induces aggregation without large-scale changes in conformation in solution.	Heparin	0-7	fibronectin 1	Homo sapiens	39-50
8180139-8	1994	We conclude that heparin binding to monomeric fibronectin occurs without large-scale changes in the conformation of the fibronectin molecule, although the possibility of more extended conformations in aggregated forms of fibronectin cannot be excluded.	Heparin	17-24	fibronectin 1	Homo sapiens	46-57
8180139-3	1994	Addition of heparin to FPLC-purified fibronectin, at physiological pH, ionic strength and temperature, induced fibronectin aggregation, as shown by an increase of up to 60% in the static light-scattering intensity.	Heparin	12-19	fibronectin 1	Homo sapiens	37-48
8180139-3	1994	Addition of heparin to FPLC-purified fibronectin, at physiological pH, ionic strength and temperature, induced fibronectin aggregation, as shown by an increase of up to 60% in the static light-scattering intensity.	Heparin	12-19	fibronectin 1	Homo sapiens	111-122
8292610-9	1994	It is concluded that the murine myocardial microvasculature harbors at least two pools of antithrombin, the minor of which is in an activated configuration characteristic of association with heparin.	Heparin	191-198	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	90-102
8114675-4	1994	The Kd1 for high affinity 125I-LDL binding in quiescent VSMC was comparable to the value for heparin-sensitive binding of 125I-LDL to apolipoprotein B/E receptors in fibroblasts (Kd approximately 1 microgram/ml).	Heparin	93-100	apolipoprotein B	Homo sapiens	134-150
8114675-10	1994	Further investigation is required to unequivocally demonstrate that the heparin-insensitive HDL3 and low affinity LDL binding sites in VSMC are those through which LDL and HDL3 stimulate transmembrane signaling.	Heparin	72-79	HDL3	Homo sapiens	172-176
8121293-11	1994	Hence, fatty acids cause a dose-, acyl chain-, and carboxyl group-dependent specific decrease of heparin-releasable and intracellular LPL activities in cultured rat adipocyte precursors; this effect is associated with and is likely caused at least in part by a decrease in LPL mRNA levels.	Heparin	97-104	lipoprotein lipase	Rattus norvegicus	273-276
8121306-4	1994	GHRH-induced GH secretion was potentiated by ARG (2,009.9 +/- 463.2 v 922.0 +/- 244.4 micrograms/L/h, P &lt; .05) and suppressed by lipid-heparin infusion (106.2 +/- 28.3 v 922.0 +/- 244.4 micrograms/L/h, P &lt; .01).	Heparin	138-145	growth hormone releasing hormone	Homo sapiens	0-4
8121306-4	1994	GHRH-induced GH secretion was potentiated by ARG (2,009.9 +/- 463.2 v 922.0 +/- 244.4 micrograms/L/h, P &lt; .05) and suppressed by lipid-heparin infusion (106.2 +/- 28.3 v 922.0 +/- 244.4 micrograms/L/h, P &lt; .01).	Heparin	138-145	growth hormone 1	Homo sapiens	0-2
8121306-5	1994	Moreover, the lipid-heparin infusion inhibited the potentiating effect of ARG on the GHRH-induced GH increase (527.9 +/- 113.6 v 2,009.9 +/- 463.2 micrograms/L/h, P &lt; .01).	Heparin	20-27	growth hormone releasing hormone	Homo sapiens	85-89
8121306-5	1994	Moreover, the lipid-heparin infusion inhibited the potentiating effect of ARG on the GHRH-induced GH increase (527.9 +/- 113.6 v 2,009.9 +/- 463.2 micrograms/L/h, P &lt; .01).	Heparin	20-27	growth hormone 1	Homo sapiens	85-87
8292610-4	1994	Addition of heparin educes antithrombin activity continuously into the perfusate during 6 min of recirculation.	Heparin	12-19	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
8292610-8	1994	The amount of antithrombin reacting rapidly with factor Xa is too low to detect as a burst of antithrombin activity eluted into the perfusate when the hearts are perfused with heparin.	Heparin	176-183	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	14-26
8292610-8	1994	The amount of antithrombin reacting rapidly with factor Xa is too low to detect as a burst of antithrombin activity eluted into the perfusate when the hearts are perfused with heparin.	Heparin	176-183	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	94-106
8171416-1	1994	Bleeding induced by unfractionated heparin (UFH) can be antagonized by protamine as shown by normalization of thrombin time and aPTT.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	110-118
7506739-4	1994	Undifferentiated HL-60 cells expressed a single class of heparin-inhibitable TSP receptors.	Heparin	57-64	thrombospondin 1	Homo sapiens	77-80
8300609-9	1994	We established that the apoE3-enriched beta-VLDL were bound to cell surface heparan sulfate proteoglycans, as was the newly synthesized and secreted apoE3 (approximately 12% of the total secreted apoE3 was released by heparinase and suramin; 4% by heparin).	Heparin	218-225	apolipoprotein E	Homo sapiens	24-29
8294453-6	1994	It was found that degradation of the heparin proteoglycan-bound apoB-100, even without accompanying particle fusion, increased the strength of LDL binding to the granule remnants, suggesting exposure of buried heparin binding regions of apoB-100.	Heparin	37-44	apolipoprotein B	Homo sapiens	64-72
8294453-6	1994	It was found that degradation of the heparin proteoglycan-bound apoB-100, even without accompanying particle fusion, increased the strength of LDL binding to the granule remnants, suggesting exposure of buried heparin binding regions of apoB-100.	Heparin	37-44	apolipoprotein B	Homo sapiens	237-245
8171416-1	1994	Bleeding induced by unfractionated heparin (UFH) can be antagonized by protamine as shown by normalization of thrombin time and aPTT.	Heparin	44-47	coagulation factor II, thrombin	Homo sapiens	110-118
8171416-3	1994	Whereas the prolongation of aPTT and thrombin time induced by both heparins was reversed, inhibition of anti F Xa activity was not.	Heparin	67-75	coagulation factor II, thrombin	Homo sapiens	37-45
8276857-0	1994	Inhibition by heparin of thrombin-catalyzed activation of the factor VIII-von Willebrand factor complex.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	25-33
8288646-4	1994	This paper describes further work on the binding properties of HS saccharides and their capacity to mediate bFGF activity in a mitogenesis assay in which responsiveness is dependent on the addition of HS or heparin.	Heparin	207-214	fibroblast growth factor 2	Homo sapiens	108-112
8276857-5	1994	We propose that, in addition to catalyzing the inhibition of thrombin and other intrinsic pathway coagulation proteases by antithrombin, heparin functions as an anticoagulant by direct inhibition of the activation of the fVIII-vWf complex by thrombin.	Heparin	137-144	von Willebrand factor	Homo sapiens	227-230
8288594-0	1994	Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	47-55
8288594-1	1994	The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	78-86
8288594-1	1994	The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	94-102
8288594-1	1994	The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	94-102
8288594-2	1994	Point mutations at Arg-180, Arg-245, Lys-248, and Lys-252 in thrombin markedly reduced the efficiency of heparin catalysis by decreasing the stability of the ternary intermediate, whereas the inactivation of thrombin by antithrombin alone was not affected by these mutations.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	61-69
8288594-2	1994	Point mutations at Arg-180, Arg-245, Lys-248, and Lys-252 in thrombin markedly reduced the efficiency of heparin catalysis by decreasing the stability of the ternary intermediate, whereas the inactivation of thrombin by antithrombin alone was not affected by these mutations.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	208-216
8288594-3	1994	These results together with an analysis of the x-ray crystal structure of thrombin yielded a model for the thrombin-heparin interaction, wherein heparin forms salt linkages along a groove in thrombin defined by Lys-252, Lys-248, Arg-245, Arg-89, Arg-98, and Arg-180.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	74-82
8288594-3	1994	These results together with an analysis of the x-ray crystal structure of thrombin yielded a model for the thrombin-heparin interaction, wherein heparin forms salt linkages along a groove in thrombin defined by Lys-252, Lys-248, Arg-245, Arg-89, Arg-98, and Arg-180.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	107-115
8288594-3	1994	These results together with an analysis of the x-ray crystal structure of thrombin yielded a model for the thrombin-heparin interaction, wherein heparin forms salt linkages along a groove in thrombin defined by Lys-252, Lys-248, Arg-245, Arg-89, Arg-98, and Arg-180.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	107-115
8288594-3	1994	These results together with an analysis of the x-ray crystal structure of thrombin yielded a model for the thrombin-heparin interaction, wherein heparin forms salt linkages along a groove in thrombin defined by Lys-252, Lys-248, Arg-245, Arg-89, Arg-98, and Arg-180.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	74-82
8288594-3	1994	These results together with an analysis of the x-ray crystal structure of thrombin yielded a model for the thrombin-heparin interaction, wherein heparin forms salt linkages along a groove in thrombin defined by Lys-252, Lys-248, Arg-245, Arg-89, Arg-98, and Arg-180.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	107-115
8288594-3	1994	These results together with an analysis of the x-ray crystal structure of thrombin yielded a model for the thrombin-heparin interaction, wherein heparin forms salt linkages along a groove in thrombin defined by Lys-252, Lys-248, Arg-245, Arg-89, Arg-98, and Arg-180.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	107-115
8280781-3	1994	The biochemical characterization of the variants and the kinetic study of thrombin and activated factor X (F Xa) inhibition in the presence of heparin and heparin derivatives suggest that Arg-129 plays a specific role in AT conformation and F Xa inhibition enhancement.	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	74-82
8280781-3	1994	The biochemical characterization of the variants and the kinetic study of thrombin and activated factor X (F Xa) inhibition in the presence of heparin and heparin derivatives suggest that Arg-129 plays a specific role in AT conformation and F Xa inhibition enhancement.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	74-82
8280781-9	1994	Moreover, the mutant AT was partially reactivated by heparin for thrombin inhibition, but did not respond to the specific pentasaccharide domain of heparin for F Xa inhibition.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	65-73
8276857-0	1994	Inhibition by heparin of thrombin-catalyzed activation of the factor VIII-von Willebrand factor complex.	Heparin	14-21	von Willebrand factor	Homo sapiens	74-95
8276782-0	1994	Differential structural requirements of heparin and heparan sulfate proteoglycans that promote binding of basic fibroblast growth factor to its receptor.	Heparin	40-47	fibroblast growth factor 2	Bos taurus	106-136
8276857-2	1994	In a defined, plasma-free assay of fVIII activation and at physiological ionic strength and pH, heparin inhibited the rate of activation of either human or porcine fVIII by thrombin in either the presence or absence of von Willebrand factor (vWf).	Heparin	96-103	coagulation factor II, thrombin	Homo sapiens	173-181
8276782-2	1994	The capacity of various species of heparin and heparan sulfate (HS) to promote bFGF receptor binding was investigated using both Chinese hamster ovary mutant cells deficient in cell surface HSPG and a soluble bFGF receptor-alkaline phosphatase fusion protein.	Heparin	35-42	fibroblast growth factor 2	Bos taurus	79-83
8276782-4	1994	O-Sulfation in heparin was found to be critical for its capacity to promote binding of bFGF to its receptors.	Heparin	15-22	fibroblast growth factor 2	Bos taurus	87-91
8276857-2	1994	In a defined, plasma-free assay of fVIII activation and at physiological ionic strength and pH, heparin inhibited the rate of activation of either human or porcine fVIII by thrombin in either the presence or absence of von Willebrand factor (vWf).	Heparin	96-103	von Willebrand factor	Homo sapiens	242-245
8276782-5	1994	The highest level of bFGF-receptor binding was achieved in the presence of over-sulfated heparin fragments (% sulfur &gt; 14) regardless of whether the N-position was sulfated or acetylated.	Heparin	89-96	fibroblast growth factor 2	Bos taurus	21-25
8276857-3	1994	The inhibitory effect of heparin was associated with inhibition of all three thrombin-catalyzed bond cleavages.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	77-85
8276782-6	1994	Unlike receptor binding of bFGF which requires oligosaccharides containing at least 8-10 sugar units, displacement of heparin- or HS-bound bFGF was obtained by oligosaccharides containing as little as four sugar units and by an N-sulfated, O-desulfated heparin fragment (% sulfur = 5.3).	Heparin	118-125	fibroblast growth factor 2	Bos taurus	139-143
8276857-4	1994	At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml).	Heparin	165-172	von Willebrand factor	Homo sapiens	59-62
8276782-6	1994	Unlike receptor binding of bFGF which requires oligosaccharides containing at least 8-10 sugar units, displacement of heparin- or HS-bound bFGF was obtained by oligosaccharides containing as little as four sugar units and by an N-sulfated, O-desulfated heparin fragment (% sulfur = 5.3).	Heparin	253-260	fibroblast growth factor 2	Bos taurus	139-143
8276782-10	1994	Moreover, most of these species of HS inhibited in a dose-dependent manner the restoration of bFGF-receptor binding induced by heparin or by total HSPG.	Heparin	127-134	fibroblast growth factor 2	Bos taurus	94-98
8276782-11	1994	These results suggest the involvement of defined heparin-like oligosaccharide sequences and unique species of cell surface and extracellular matrix HS in the regulation of bFGF receptor binding and biological activity.	Heparin	49-56	fibroblast growth factor 2	Bos taurus	172-176
8276857-4	1994	At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml).	Heparin	209-216	von Willebrand factor	Homo sapiens	59-62
8276857-5	1994	We propose that, in addition to catalyzing the inhibition of thrombin and other intrinsic pathway coagulation proteases by antithrombin, heparin functions as an anticoagulant by direct inhibition of the activation of the fVIII-vWf complex by thrombin.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	61-69
8185261-0	1994	Use of low molecular weight heparin in the treatment of venous thrombosis in a patient with anti-thrombin III deficiency: a case report.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	97-105
8185261-1	1994	This paper describes the use of a low molecular weight heparin (LMWH) in the treatment of a thrombotic episode in a patient with anti-thrombin III deficiency.	Heparin	55-62	coagulation factor II, thrombin	Homo sapiens	134-142
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	24-32
8311463-0	1994	Stoichiometry of heparin binding to basic fibroblast growth factor.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	36-66
8311463-2	1994	We have investigated the interactions of basic fibroblast growth factor (bFGF) with low- and high-molecular-weight heparin using size exclusion chromatography with on-line light scattering, absorbance, and refractive index detection.	Heparin	115-122	fibroblast growth factor 2	Homo sapiens	41-71
8311463-2	1994	We have investigated the interactions of basic fibroblast growth factor (bFGF) with low- and high-molecular-weight heparin using size exclusion chromatography with on-line light scattering, absorbance, and refractive index detection.	Heparin	115-122	fibroblast growth factor 2	Homo sapiens	73-77
8311463-3	1994	When heparin-bFGF mixtures with excess heparin are chromatographed using eluant that does not contain heparin, essentially all the protein is seen to elute as a complex with the heparin, indicating strong binding such that the complex does not dissociate significantly during chromatography (approximately 20 min).	Heparin	5-12	fibroblast growth factor 2	Homo sapiens	13-17
8311463-3	1994	When heparin-bFGF mixtures with excess heparin are chromatographed using eluant that does not contain heparin, essentially all the protein is seen to elute as a complex with the heparin, indicating strong binding such that the complex does not dissociate significantly during chromatography (approximately 20 min).	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	13-17
8311463-3	1994	When heparin-bFGF mixtures with excess heparin are chromatographed using eluant that does not contain heparin, essentially all the protein is seen to elute as a complex with the heparin, indicating strong binding such that the complex does not dissociate significantly during chromatography (approximately 20 min).	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	13-17
8311463-3	1994	When heparin-bFGF mixtures with excess heparin are chromatographed using eluant that does not contain heparin, essentially all the protein is seen to elute as a complex with the heparin, indicating strong binding such that the complex does not dissociate significantly during chromatography (approximately 20 min).	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	13-17
8311463-6	1994	At bFGF: heparin ratios above 1.5, a mix of complexes containing 3, 2, and 1 bFGF molecules is observed, with an average of 2.2 bFGF molecules per complex.	Heparin	9-16	fibroblast growth factor 2	Homo sapiens	77-81
8311463-6	1994	At bFGF: heparin ratios above 1.5, a mix of complexes containing 3, 2, and 1 bFGF molecules is observed, with an average of 2.2 bFGF molecules per complex.	Heparin	9-16	fibroblast growth factor 2	Homo sapiens	77-81
8311463-9	1994	When a high-molecular-weight heparin (HMWH, M(r) = 15,000) is used, complexes averaging 6.3 bFGF molecules per HMWH molecule are seen, while the overall amount of bFGF appearing in complexes implies six to seven sites per HMWH.	Heparin	29-36	fibroblast growth factor 2	Homo sapiens	92-96
8311463-9	1994	When a high-molecular-weight heparin (HMWH, M(r) = 15,000) is used, complexes averaging 6.3 bFGF molecules per HMWH molecule are seen, while the overall amount of bFGF appearing in complexes implies six to seven sites per HMWH.	Heparin	29-36	fibroblast growth factor 2	Homo sapiens	163-167
8311463-11	1994	Both types of heparin give a heparin mass of 2300 Da per bFGF binding site, which corresponds approximately to an octasaccharide.	Heparin	14-21	fibroblast growth factor 2	Homo sapiens	57-61
8311463-11	1994	Both types of heparin give a heparin mass of 2300 Da per bFGF binding site, which corresponds approximately to an octasaccharide.	Heparin	29-36	fibroblast growth factor 2	Homo sapiens	57-61
8198374-4	1994	Direct thrombin inhibitors have several potential advantages over heparin: They can inhibit thrombin bound to clots or extracellular matrices, which are relatively resistant to heparin; they do not require antithrombin III as a cofactor, which may lead to a more predictable dose response; and they are not inhibited by activated platelets, which release platelet factor 4 and other molecules that neutralize heparin.	Heparin	66-73	coagulation factor II, thrombin	Homo sapiens	92-100
8198374-4	1994	Direct thrombin inhibitors have several potential advantages over heparin: They can inhibit thrombin bound to clots or extracellular matrices, which are relatively resistant to heparin; they do not require antithrombin III as a cofactor, which may lead to a more predictable dose response; and they are not inhibited by activated platelets, which release platelet factor 4 and other molecules that neutralize heparin.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	7-15
8198374-4	1994	Direct thrombin inhibitors have several potential advantages over heparin: They can inhibit thrombin bound to clots or extracellular matrices, which are relatively resistant to heparin; they do not require antithrombin III as a cofactor, which may lead to a more predictable dose response; and they are not inhibited by activated platelets, which release platelet factor 4 and other molecules that neutralize heparin.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	7-15
8280115-3	1994	The destabilization of cytochrome c when mixed with heparin was not observed at high ionic strength, under which conditions complex was not formed.	Heparin	52-59	cytochrome c, somatic	Homo sapiens	23-35
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	24-32
8186357-2	1994	In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	28-36
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	71-79
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	71-79
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	71-79
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	24-32
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	110-117	coagulation factor II, thrombin	Homo sapiens	24-32
7734144-6	1994	The concentration of heparin required for half maximal stimulation of VEGF binding to KDR-expressing cells (500 ng/ml) was 25 times greater than that required for half maximal inhibition of binding to FLT1-expressing cells (20 ng/ml).	Heparin	21-28	vascular endothelial growth factor A	Homo sapiens	70-74
8011429-9	1994	Chromatography of human platelet extract on heparin-Sepharose resolved two peaks of MLC phosphatase activity: PP2A in 0.1 M NaCl eluate and PP1 in 0.5 NaCl eluate.	Heparin	44-51	modulator of VRAC current 1	Homo sapiens	84-87
8187245-2	1994	The kringles interact with thrombin at a site that has previously been proposed to be the heparin binding region.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	27-35
8187229-1	1994	Heparin-induced extracorporeal low-density lipoprotein precipitation (HELP) is based on the precipitation of apolipoprotein B (apo B) containing lipoproteins with heparin at low pH (4.85).	Heparin	0-7	apolipoprotein B	Homo sapiens	109-125
8187229-1	1994	Heparin-induced extracorporeal low-density lipoprotein precipitation (HELP) is based on the precipitation of apolipoprotein B (apo B) containing lipoproteins with heparin at low pH (4.85).	Heparin	0-7	apolipoprotein B	Homo sapiens	127-132
8187229-1	1994	Heparin-induced extracorporeal low-density lipoprotein precipitation (HELP) is based on the precipitation of apolipoprotein B (apo B) containing lipoproteins with heparin at low pH (4.85).	Heparin	163-170	apolipoprotein B	Homo sapiens	109-125
8187229-1	1994	Heparin-induced extracorporeal low-density lipoprotein precipitation (HELP) is based on the precipitation of apolipoprotein B (apo B) containing lipoproteins with heparin at low pH (4.85).	Heparin	163-170	apolipoprotein B	Homo sapiens	127-132
8187236-6	1994	u-PA-mediated activation of plasminogen is blocked on surfaces including heparin and chondroitin sulfate.	Heparin	73-80	plasminogen activator, urokinase	Homo sapiens	0-4
7530465-1	1994	The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate.	Heparin	182-189	fibroblast growth factor 1	Homo sapiens	73-78
7530465-1	1994	The fluorescence emission of a single tryptophan residue present in both FGF-1 and FGF-2 was used as a structural probe to directly assess the interaction of the growth factors with heparin or beta-cyclodextran tetradecasulfate.	Heparin	182-189	fibroblast growth factor 2	Homo sapiens	83-88
7530465-4	1994	The equilibrium dissociation constants, determined by this method, for heparin or beta-cyclodextrin tetradecasulfate binding to FGF-1 are about 1 nM, whereas the values for FGF-2 are 1 and 23 nM, respectively.	Heparin	71-78	fibroblast growth factor 1	Homo sapiens	128-133
7734144-5	1994	Heparin augmented VEGF binding to KDR-expressing cells (ABAE and WM35), but inhibited VEGF binding to FLT1-expressing cells (SK-MEL-37 and WM9).	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	18-22
7734144-7	1994	In WM9 cells, the effect of heparin was bimodal; low concentration inhibited, while higher concentrations stimulated binding of 125I-VEGF.	Heparin	28-35	vascular endothelial growth factor A	Homo sapiens	133-137
7734144-5	1994	Heparin augmented VEGF binding to KDR-expressing cells (ABAE and WM35), but inhibited VEGF binding to FLT1-expressing cells (SK-MEL-37 and WM9).	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	86-90
7734144-5	1994	Heparin augmented VEGF binding to KDR-expressing cells (ABAE and WM35), but inhibited VEGF binding to FLT1-expressing cells (SK-MEL-37 and WM9).	Heparin	0-7	fms related receptor tyrosine kinase 1	Homo sapiens	102-106
7734144-11	1994	The data indicate differential regulation of the two VEGF receptors by heparin and extended specificity of FLT1 receptor, but not KDR, for binding PIGF-1 growth factor.	Heparin	71-78	vascular endothelial growth factor A	Homo sapiens	53-57
7657521-7	1994	Both heparanase and lung colonization by A9 CTC 220 cells were inhibited to a large extent by heparin, suggesting the involvement of heparanase in the extravasation of these highly metastatic cells.	Heparin	94-101	heparanase	Mus musculus	5-15
7657521-7	1994	Both heparanase and lung colonization by A9 CTC 220 cells were inhibited to a large extent by heparin, suggesting the involvement of heparanase in the extravasation of these highly metastatic cells.	Heparin	94-101	heparanase	Mus musculus	133-143
7984618-1	1994	The plasma levels of immunoreactive fibronectin (IRF) and its functionally full-value fraction (FVF) were estimated from the capacity to bind to heparin to form a cold precipitate in 86 patients with various types of active pulmonary tuberculosis on admission, 1, 2-3, and 4-6 months after multimodality treatment.	Heparin	145-152	fibronectin 1	Homo sapiens	36-47
8127002-0	1994	Heparin inhibits endothelin-1 production in cultured rat mesangial cells.	Heparin	0-7	endothelin 1	Rattus norvegicus	17-29
8127002-1	1994	The present study was designed to examine whether heparin inhibits basal or stimulated endothelin-1 production by arginine vasopressin (AVP) and platelet-derived growth factor (PDGF) in cultured rat mesangial cells.	Heparin	50-57	endothelin 1	Rattus norvegicus	87-99
8127002-2	1994	In addition, the reversibility of the heparin effect on mesangial cell endothelin-1 production was examined.	Heparin	38-45	endothelin 1	Rattus norvegicus	71-83
8127002-4	1994	Heparin (10 to 100 U/ml) exhibited concentration-related inhibition of AVP- and PDGF-stimulated endothelin-1 secretion.	Heparin	0-7	endothelin 1	Rattus norvegicus	96-108
8127002-5	1994	Heparin also had weak but significant inhibitory effects on basal endothelin-1 secretion in these cells.	Heparin	0-7	endothelin 1	Rattus norvegicus	66-78
8127002-6	1994	The protein kinase (PKC)-activating phorbor ester, phorbor myristate acetate (PMA), stimulated endothelin-1 secretion and heparin inhibited PMA-stimulated endothelin-1 secretion.	Heparin	122-129	endothelin 1	Rattus norvegicus	155-167
8127002-8	1994	Mesangial cells which were exposed to a high concentration (100 U/ml) of heparin for 24 hours were capable of producing endothelin-1 after a short lag period of removal of heparin from the culture medium.	Heparin	73-80	endothelin 1	Rattus norvegicus	120-132
8127002-8	1994	Mesangial cells which were exposed to a high concentration (100 U/ml) of heparin for 24 hours were capable of producing endothelin-1 after a short lag period of removal of heparin from the culture medium.	Heparin	172-179	endothelin 1	Rattus norvegicus	120-132
8127002-10	1994	These results indicate that heparin potently inhibits mesangial cell endothelin-1 production, especially when stimulated by AVP or PDGF.	Heparin	28-35	endothelin 1	Rattus norvegicus	69-81
7734016-5	1994	Measurements of thrombin time in the post bypass period closely follow plasma heparin levels.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	16-24
7947469-0	1994	Heparin surface immobilization through hydrophilic spacers: thrombin and antithrombin III binding kinetics.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	60-68
7947469-2	1994	In this study, the effect of hydrophilic spacers (PEO) on the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin was investigated.	Heparin	94-101	coagulation factor II, thrombin	Homo sapiens	111-119
7947469-9	1994	Soluble heparin bound both thrombin and ATIII, while heparin immobilized directly onto the surface bound only thrombin.	Heparin	8-15	coagulation factor II, thrombin	Homo sapiens	27-35
7947469-9	1994	Soluble heparin bound both thrombin and ATIII, while heparin immobilized directly onto the surface bound only thrombin.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	110-118
7947469-10	1994	Spacer-immobilized heparin bound both ATIII and thrombin, although to a lesser extent than soluble heparin.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	48-56
10603512-0	1994	Heparin Binding Sites Are Located in a 40-kD gamma-Chain and a 36-kD beta-Chain Fragment Isolated from Human Fibrinogen.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	109-119
10603512-1	1994	Objective: We have previously shown that (125)I-fibrinogen binds to heparin sepharose CL-6B.	Heparin	68-75	fibrinogen beta chain	Homo sapiens	48-58
10603512-2	1994	To identify the localization of the heparin binding domain in human fibrinogen, reduced and alkylated fibrinogen was digested by limited-Staphylococcus aureus V8 protease.	Heparin	36-43	fibrinogen beta chain	Homo sapiens	68-78
10603512-2	1994	To identify the localization of the heparin binding domain in human fibrinogen, reduced and alkylated fibrinogen was digested by limited-Staphylococcus aureus V8 protease.	Heparin	36-43	fibrinogen beta chain	Homo sapiens	102-112
10603512-6	1994	Binding of (125)I-fibrinogen to heparin-sepharose CL-6B was completely inhibited by a mixture of these fragments, with an IC(50) of 3.2 microM.	Heparin	32-39	fibrinogen beta chain	Homo sapiens	18-28
10603512-9	1994	Conclusions: These data indicate that the domains for heparin binding may be present on both the gamma chain and the beta chain of fibrinogen, and that the domain on the gamma chain may be close to the binding domain on the carboxy terminus of the fibrinogen gamma chain to glycoprotein IIb-IIIa.	Heparin	54-61	fibrinogen beta chain	Homo sapiens	131-141
10603512-9	1994	Conclusions: These data indicate that the domains for heparin binding may be present on both the gamma chain and the beta chain of fibrinogen, and that the domain on the gamma chain may be close to the binding domain on the carboxy terminus of the fibrinogen gamma chain to glycoprotein IIb-IIIa.	Heparin	54-61	fibrinogen beta chain	Homo sapiens	248-258
10603518-1	1994	Background: Current strategies in the treatment of patients with acute coronary syndromes include antiplatelet agents and thrombin antagonists, most commonly aspirin and heparin, respectively.	Heparin	170-177	coagulation factor II, thrombin	Homo sapiens	122-130
7511240-6	1994	A formulation containing heparin (necessary for full biological and conformational stability of aFGF) at a mass ratio of 3:1 to aFGF was more efficacious than formulations with lower heparin: aFGF ratios.	Heparin	25-32	fibroblast growth factor 1	Mus musculus	96-100
7511240-6	1994	A formulation containing heparin (necessary for full biological and conformational stability of aFGF) at a mass ratio of 3:1 to aFGF was more efficacious than formulations with lower heparin: aFGF ratios.	Heparin	25-32	fibroblast growth factor 1	Mus musculus	128-132
7511240-6	1994	A formulation containing heparin (necessary for full biological and conformational stability of aFGF) at a mass ratio of 3:1 to aFGF was more efficacious than formulations with lower heparin: aFGF ratios.	Heparin	25-32	fibroblast growth factor 1	Mus musculus	128-132
7515293-8	1994	VEGF165 is a heparin binding growth factor, and its interaction with VEGF receptors on the cell surface of vascular endothelial cells depends on the presence of heparin-like molecules.	Heparin	13-20	vascular endothelial growth factor A	Homo sapiens	0-4
8165633-5	1994	Using heparin-derived oligosaccharides, we also demonstrated that a minimal chain length of 18 monosaccharides was required for heparin binding to vWF.	Heparin	6-13	von Willebrand factor	Homo sapiens	147-150
7824959-1	1994	The effect of heparin and partially desulfated heparin derivatives on thrombin and PAF-induced adhesion of PMNs to the endothelium was studied either by a fluorescence image analysis or by 111In-labeled PMNs.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	70-78
8165633-1	1994	To investigate the influence of the structure of heparin on its binding to vWF, we compared heparin fractions of different molecular weight (MW) or affinity for antithrombin III (ATIII).	Heparin	49-56	von Willebrand factor	Homo sapiens	75-78
8165633-6	1994	In addition, different fractions with low affinity for ATIII were compared as competitors of 125I-vWF binding to heparin-agarose.	Heparin	113-120	von Willebrand factor	Homo sapiens	98-101
8165633-8	1994	Thus, heparin interaction with vWF is independent of the presence of the ATIII binding site and is mostly dependent on the length of the heparin chain.	Heparin	6-13	von Willebrand factor	Homo sapiens	31-34
8165633-8	1994	Thus, heparin interaction with vWF is independent of the presence of the ATIII binding site and is mostly dependent on the length of the heparin chain.	Heparin	137-144	von Willebrand factor	Homo sapiens	31-34
8165633-9	1994	These data suggest that unfractionated heparin is a more potent inhibitor of vWF-dependent functions than low MW heparin fractions.	Heparin	39-46	von Willebrand factor	Homo sapiens	77-80
8165646-10	1994	The addition of heparin virtually suppressed thrombin formation since the F1 + 2 concentration remained low.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	45-53
8165646-11	1994	Moreover, the small amounts of thrombin formed were neutralized by antithrombin III to a greater extent than in the absence of heparin.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	31-39
7863705-8	1994	An anticoagulation with heparin seems to improve the efficacy of the more fibrin-specific thrombolytics t-PA, r-PA, and pro-urokinase.	Heparin	24-31	plasminogen activator, tissue type	Homo sapiens	104-108
7863705-9	1994	In dose-finding studies the specific thrombin inhibitor hirudin has been shown to significantly reduce reocclusions and reinfarctions compared to heparin.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	37-45
8263926-8	1993	The active material from the monoclinic crystals had an association rate constant with thrombin in the presence of heparin (kass) of 7.5 x 10(7) M-1 s-1 (kass for native antithrombin = 8.2 (+/- 1.0) x 10(7) M-1 s-1) indicating it still had effective heparin cofactor activity.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	87-95
8165623-6	1993	In vitro studies in blood and seminal plasma showed that heparin stimulated complexation of uPA and tPA with PCI, suggesting that negatively charged glycosaminoglycans in blood vessels and in the reproductive system may regulate PCI reactions with uPA and tPA.	Heparin	57-64	plasminogen activator, urokinase	Homo sapiens	92-95
8165623-6	1993	In vitro studies in blood and seminal plasma showed that heparin stimulated complexation of uPA and tPA with PCI, suggesting that negatively charged glycosaminoglycans in blood vessels and in the reproductive system may regulate PCI reactions with uPA and tPA.	Heparin	57-64	plasminogen activator, urokinase	Homo sapiens	248-251
8262929-10	1993	The enhancing effect of heparin on the inhibitory process is concentration dependent and exhibits an optimum, reminiscent of the "template" model for heparin"s acceleration of thrombin and factor IXa inhibition by antithrombin III.	Heparin	24-31	coagulation factor II, thrombin	Homo sapiens	176-184
8280070-7	1993	CKS2 was inhibited by heparin, but CKA was unaffected and CKS1 was stimulated.	Heparin	22-29	CDC28 protein kinase regulatory subunit 2	Homo sapiens	0-4
8313434-10	1993	These effects of heparin were completely reversed by the presence of a neutralising antiserum to transforming growth factor beta (TGF beta) and heparin attached to agarose beads was as effective as free heparin as a growth inhibitor of VSMCs.	Heparin	17-24	transforming growth factor, beta 1	Rattus norvegicus	130-138
8241100-6	1993	Additional studies show that levels of midkine and pleiotrophin peak at 10 to 30 minutes after injection of heparin.	Heparin	108-115	midkine	Homo sapiens	39-46
8241100-6	1993	Additional studies show that levels of midkine and pleiotrophin peak at 10 to 30 minutes after injection of heparin.	Heparin	108-115	pleiotrophin	Homo sapiens	51-63
8241100-7	1993	Heparin-releasable midkine and pleiotrophin do not originate from blood cells or the kidney.	Heparin	0-7	midkine	Homo sapiens	19-26
8241100-8	1993	Heparin-releasable midkine may originate from endothelial cells.	Heparin	0-7	midkine	Homo sapiens	19-26
8241100-9	1993	Soft agar culture of an adenocarcinoma cell line (SW-13) demonstrates growth-stimulating activity similar to that described for pleiotrophin in the heparin-agarose eluate of postheparin plasma but not in the heparin-agarose eluate of preheparin plasma.	Heparin	148-155	pleiotrophin	Homo sapiens	128-140
8241100-10	1993	It is concluded there are more heparin-releasable proteins than previously identified, including midkine and pleiotrophin, and that heparin-affinity chromatography of postheparin plasma is a useful technique for identifying novel heparin-releasable proteins.	Heparin	31-38	midkine	Homo sapiens	97-104
8241100-10	1993	It is concluded there are more heparin-releasable proteins than previously identified, including midkine and pleiotrophin, and that heparin-affinity chromatography of postheparin plasma is a useful technique for identifying novel heparin-releasable proteins.	Heparin	31-38	pleiotrophin	Homo sapiens	109-121
8281931-8	1993	Exposure of BRL-3A cells to thrombin also induced the apparent secretion of type-II PLA2, and thrombin-stimulated PGE2 generation was suppressed by heparin effectively.	Heparin	148-155	coagulation factor II	Rattus norvegicus	28-36
8281931-8	1993	Exposure of BRL-3A cells to thrombin also induced the apparent secretion of type-II PLA2, and thrombin-stimulated PGE2 generation was suppressed by heparin effectively.	Heparin	148-155	coagulation factor II	Rattus norvegicus	94-102
8279543-1	1993	Lipoprotein lipase (LPL) is synthesized by adipocytes, associated with the cell surface, and released from the cells when they are treated with heparin.	Heparin	144-151	lipoprotein lipase	Rattus norvegicus	0-18
8279543-1	1993	Lipoprotein lipase (LPL) is synthesized by adipocytes, associated with the cell surface, and released from the cells when they are treated with heparin.	Heparin	144-151	lipoprotein lipase	Rattus norvegicus	20-23
8279543-7	1993	When BFC-1 beta were treated with heparin to eliminate heparin-sensitive cell surface binding sites, LPL binding to the cells decreased and release of newly synthesized LPL activity increased.	Heparin	34-41	lipoprotein lipase	Rattus norvegicus	101-104
8279543-7	1993	When BFC-1 beta were treated with heparin to eliminate heparin-sensitive cell surface binding sites, LPL binding to the cells decreased and release of newly synthesized LPL activity increased.	Heparin	34-41	lipoprotein lipase	Rattus norvegicus	169-172
8279543-7	1993	When BFC-1 beta were treated with heparin to eliminate heparin-sensitive cell surface binding sites, LPL binding to the cells decreased and release of newly synthesized LPL activity increased.	Heparin	55-62	lipoprotein lipase	Rattus norvegicus	101-104
8279543-7	1993	When BFC-1 beta were treated with heparin to eliminate heparin-sensitive cell surface binding sites, LPL binding to the cells decreased and release of newly synthesized LPL activity increased.	Heparin	55-62	lipoprotein lipase	Rattus norvegicus	169-172
8279543-9	1993	The residual LPL binding to heparin-treated cells was, however, not decreased by the addition of unlabeled LPL.	Heparin	28-35	lipoprotein lipase	Rattus norvegicus	13-16
8279543-10	1993	These data imply that specific adipocyte surface LPL binding involves heparin-sensitive sites.	Heparin	70-77	lipoprotein lipase	Rattus norvegicus	49-52
8279543-11	1993	We hypothesize that the heparin-releasable, 116-kDa LPL-binding protein mediates specific LPL binding to adipocytes and that LPL activity within adipose tissue is regulated, in part, by the interaction of LPL with this binding protein.	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	52-55
8279543-11	1993	We hypothesize that the heparin-releasable, 116-kDa LPL-binding protein mediates specific LPL binding to adipocytes and that LPL activity within adipose tissue is regulated, in part, by the interaction of LPL with this binding protein.	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	90-93
8279543-11	1993	We hypothesize that the heparin-releasable, 116-kDa LPL-binding protein mediates specific LPL binding to adipocytes and that LPL activity within adipose tissue is regulated, in part, by the interaction of LPL with this binding protein.	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	90-93
8279543-11	1993	We hypothesize that the heparin-releasable, 116-kDa LPL-binding protein mediates specific LPL binding to adipocytes and that LPL activity within adipose tissue is regulated, in part, by the interaction of LPL with this binding protein.	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	90-93
8222077-6	1993	Heparinase or heparitinase treatment of conditioned media removed the bFGF-inhibitory effects, presumably by degrading heparin-like compounds.	Heparin	119-126	fibroblast growth factor 2	Homo sapiens	70-74
8222077-7	1993	Indeed, heparin itself mimicked the inhibitory effects of conditioned media on bFGF-mediated proliferation and binding to heparin sulfate proteoglycans.	Heparin	8-15	fibroblast growth factor 2	Homo sapiens	79-83
8137606-4	1993	LMW heparins are stronger inhibitors of factor Xa than unfractionated heparin, but their mechanisms of action, like that of unfractionated heparin, is predominantly the inhibition of thrombin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	183-191
8243298-5	1993	Serum PTH levels were significantly elevated from 1 week onward after starting heparin treatment, whereas no significant changes were seen in serum total calcium or ionized calcium levels.	Heparin	79-86	parathyroid hormone	Rattus norvegicus	6-9
8243298-8	1993	These results suggest that the enhanced bone resorption by high PTH blood levels and the reduction of 1 alpha, 25-dihydroxyvitamin D are involved in the pathogenesis of heparin-induced osteopenia.	Heparin	169-176	parathyroid hormone	Rattus norvegicus	64-67
8313434-13	1993	Heparin (&lt; 100 micrograms.ml-1) acted extracellularly to release TGF beta from serum, which accounted for the effects of heparin on proliferation and differentiation.	Heparin	0-7	transforming growth factor, beta 1	Rattus norvegicus	68-76
8313434-13	1993	Heparin (&lt; 100 micrograms.ml-1) acted extracellularly to release TGF beta from serum, which accounted for the effects of heparin on proliferation and differentiation.	Heparin	124-131	transforming growth factor, beta 1	Rattus norvegicus	68-76
8245966-4	1993	A beta(1-28) associates with heparin, heparan sulfate, dermatan sulfate, and chondroitin sulfate.	Heparin	29-36	amyloid beta precursor protein	Homo sapiens	0-6
8262149-6	1993	Furthermore, excess heparin added during the binding of 125I-HGF to hepatocytes, significantly diminished HGF bound to c-Met protein.	Heparin	20-27	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	119-124
8245966-7	1993	The pH profile of heparin-induced aggregation of A beta(1-28) has a midpoint pH of approximately 6.5, suggesting that one or more histidine residues must be protonated for binding to occur.	Heparin	18-25	amyloid beta precursor protein	Homo sapiens	49-55
8245966-8	1993	Analysis of the A beta sequence reveals a consensus heparin-binding domain at residues 12-17, and this motif contains histidines at positions 13 and 14 that may be involved in the interaction with glycosaminoglycans.	Heparin	52-59	amyloid beta precursor protein	Homo sapiens	16-22
8111962-2	1993	A subfraction of HDL enriched in apolipoprotein E (apo E), separated by heparin-Sepharose affinity chromatography, was present in lower concentrations (P &lt; 0.001) in the plasma of the coronary patients than in the control subjects.	Heparin	72-79	apolipoprotein E	Homo sapiens	33-49
8136018-5	1993	Heparin, a widely used anticoagulant drug, accelerates the rate of thrombin inhibition by AT, PCI, and HC.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	67-75
8136018-9	1993	gamma T-Thrombin and thrombin Quick I (Arg 67--&gt;Cys) are both altered in anion-binding exosite-I, yet bind to heparin-Sepharose and can be inhibited by AT, HC, and PCI in an essentially normal manner in the absence of heparin.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	8-16
8136018-9	1993	gamma T-Thrombin and thrombin Quick I (Arg 67--&gt;Cys) are both altered in anion-binding exosite-I, yet bind to heparin-Sepharose and can be inhibited by AT, HC, and PCI in an essentially normal manner in the absence of heparin.	Heparin	113-120	coagulation factor II, thrombin	Homo sapiens	21-29
8136018-9	1993	gamma T-Thrombin and thrombin Quick I (Arg 67--&gt;Cys) are both altered in anion-binding exosite-I, yet bind to heparin-Sepharose and can be inhibited by AT, HC, and PCI in an essentially normal manner in the absence of heparin.	Heparin	221-228	coagulation factor II, thrombin	Homo sapiens	8-16
8136018-9	1993	gamma T-Thrombin and thrombin Quick I (Arg 67--&gt;Cys) are both altered in anion-binding exosite-I, yet bind to heparin-Sepharose and can be inhibited by AT, HC, and PCI in an essentially normal manner in the absence of heparin.	Heparin	221-228	coagulation factor II, thrombin	Homo sapiens	21-29
8136018-12	1993	Thrombin lysine-modified in the presence of heparin has protected residues in anion-binding exosite-II and the loss of heparin-accelerated inhibition by HC is greater than that by AT.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	0-8
8136018-12	1993	Thrombin lysine-modified in the presence of heparin has protected residues in anion-binding exosite-II and the loss of heparin-accelerated inhibition by HC is greater than that by AT.	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	0-8
8241146-1	1993	The major sites of heparin binding by fibronectin are located in fragments of 30 or 40 kDa that contain type III modules 12 through 14 or 15.	Heparin	19-26	fibronectin 1	Homo sapiens	38-49
8308393-0	1993	[Midkine (MK): a retinoic acid-responsive, heparin-binding growth factor in relationship with differentiation, development, cancer and neural function].	Heparin	43-50	midkine	Homo sapiens	1-8
7508153-0	1993	Heparin stimulates the proliferation of bovine aortic endothelial cells probably through activation of endogenous basic fibroblast growth factor.	Heparin	0-7	fibroblast growth factor 2	Bos taurus	114-144
7508153-5	1993	By the addition of a neutralizing antibody to basic fibroblast growth factor (bFGF), the stimulating effect of heparin decreased, whereas an antibody to acidic fibroblast growth factor (aFGF) had no effect.	Heparin	111-118	fibroblast growth factor 2	Bos taurus	46-76
7508153-5	1993	By the addition of a neutralizing antibody to basic fibroblast growth factor (bFGF), the stimulating effect of heparin decreased, whereas an antibody to acidic fibroblast growth factor (aFGF) had no effect.	Heparin	111-118	fibroblast growth factor 2	Bos taurus	78-82
7508153-6	1993	The culture medium conditioned by heparin-treated BAE cells stimulated DNA synthesis in Balb/3T3 fibroblasts that proliferate in response to bFGF.	Heparin	34-41	fibroblast growth factor 2	Bos taurus	141-145
7508153-9	1993	These results suggest that heparin stimulates the proliferation of BAE cells by the activation of endogenous bFGF, but not by the induction of its synthesis.	Heparin	27-34	fibroblast growth factor 2	Bos taurus	109-113
8226930-1	1993	Experiments based on interaction in free solution between basic fibroblast growth factor (FGF-2) and saccharides related to heparin/heparan sulfate showed that the growth factor binds to heparin and to selectively glucosaminyl 6-O-desulfated heparin but poorly to iduronosyl 2-O-desulfated heparin.	Heparin	124-131	fibroblast growth factor 2	Homo sapiens	90-95
8226930-1	1993	Experiments based on interaction in free solution between basic fibroblast growth factor (FGF-2) and saccharides related to heparin/heparan sulfate showed that the growth factor binds to heparin and to selectively glucosaminyl 6-O-desulfated heparin but poorly to iduronosyl 2-O-desulfated heparin.	Heparin	187-194	fibroblast growth factor 2	Homo sapiens	90-95
8226930-1	1993	Experiments based on interaction in free solution between basic fibroblast growth factor (FGF-2) and saccharides related to heparin/heparan sulfate showed that the growth factor binds to heparin and to selectively glucosaminyl 6-O-desulfated heparin but poorly to iduronosyl 2-O-desulfated heparin.	Heparin	187-194	fibroblast growth factor 2	Homo sapiens	90-95
8111962-2	1993	A subfraction of HDL enriched in apolipoprotein E (apo E), separated by heparin-Sepharose affinity chromatography, was present in lower concentrations (P &lt; 0.001) in the plasma of the coronary patients than in the control subjects.	Heparin	72-79	apolipoprotein E	Homo sapiens	51-56
8226930-1	1993	Experiments based on interaction in free solution between basic fibroblast growth factor (FGF-2) and saccharides related to heparin/heparan sulfate showed that the growth factor binds to heparin and to selectively glucosaminyl 6-O-desulfated heparin but poorly to iduronosyl 2-O-desulfated heparin.	Heparin	187-194	fibroblast growth factor 2	Homo sapiens	90-95
8128448-2	1993	As reported in recent literature, heparin stimulated the activation of Lys-plasminogen by high molecular weight (HMW) and low molecular weight (LMW) two-chain urokinase-type plasminogen activator (u-PA) and two-chain tissue-type plasminogen activator (t-PA) 10- to 17-fold.	Heparin	34-41	plasminogen activator, urokinase	Homo sapiens	159-195
7504274-1	1993	Basic fibroblast growth factor (bFGF) is known to bind to its cell-surface receptors with high affinity and in a heparin-dependent manner.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	0-30
7504274-1	1993	Basic fibroblast growth factor (bFGF) is known to bind to its cell-surface receptors with high affinity and in a heparin-dependent manner.	Heparin	113-120	fibroblast growth factor 2	Homo sapiens	32-36
8128448-2	1993	As reported in recent literature, heparin stimulated the activation of Lys-plasminogen by high molecular weight (HMW) and low molecular weight (LMW) two-chain urokinase-type plasminogen activator (u-PA) and two-chain tissue-type plasminogen activator (t-PA) 10- to 17-fold.	Heparin	34-41	plasminogen activator, urokinase	Homo sapiens	197-201
8128448-2	1993	As reported in recent literature, heparin stimulated the activation of Lys-plasminogen by high molecular weight (HMW) and low molecular weight (LMW) two-chain urokinase-type plasminogen activator (u-PA) and two-chain tissue-type plasminogen activator (t-PA) 10- to 17-fold.	Heparin	34-41	plasminogen activator, tissue type	Homo sapiens	217-250
8128448-2	1993	As reported in recent literature, heparin stimulated the activation of Lys-plasminogen by high molecular weight (HMW) and low molecular weight (LMW) two-chain urokinase-type plasminogen activator (u-PA) and two-chain tissue-type plasminogen activator (t-PA) 10- to 17-fold.	Heparin	34-41	plasminogen activator, tissue type	Homo sapiens	252-256
8128448-6	1993	The binding of u-PA and t-PA to heparin-agarose was less salt sensitive.	Heparin	32-39	plasminogen activator, urokinase	Homo sapiens	15-19
7692970-6	1993	Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry.	Heparin	71-78	fibroblast growth factor 1	Homo sapiens	63-67
8128448-6	1993	The binding of u-PA and t-PA to heparin-agarose was less salt sensitive.	Heparin	32-39	plasminogen activator, tissue type	Homo sapiens	24-28
8128448-7	1993	Results were consistent with heparin binding sites on both LMW u-PA and the amino-terminal part of HMW u-PA.	Heparin	29-36	plasminogen activator, urokinase	Homo sapiens	63-67
7692970-8	1993	SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays.	Heparin	18-25	fibroblast growth factor 1	Homo sapiens	46-50
8128448-7	1993	Results were consistent with heparin binding sites on both LMW u-PA and the amino-terminal part of HMW u-PA.	Heparin	29-36	plasminogen activator, urokinase	Homo sapiens	103-107
8226804-4	1993	Since both PDGF A-chain and HB-EGF have affinity for heparin, we also examined the effect of thrombin and DEX on the release of heparin binding mitogenic activity from SMCs.	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	93-101
8167903-4	1993	Heparin (50 micrograms/ml) attenuated the induction by serum of bFGF mRNA, tPA mRNA, and tPA secretion.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	64-68
8167903-5	1993	Nonanticoagulant heparin also attenuated serum induction of bFGF and tPA mRNA levels.	Heparin	17-24	fibroblast growth factor 2	Homo sapiens	60-64
21573455-1	1993	Quantification of the amount of heparin-binding growth factor activity present in homogenates of normal and malignant human colon mucosa in terms of basic fibroblast growth factor (bFGF) indicates that 6-29 ng/g tissue of bFGF-like activity was present in five samples of normal human colon and in five corresponding samples of malignant colon mucosa.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	149-179
21573455-1	1993	Quantification of the amount of heparin-binding growth factor activity present in homogenates of normal and malignant human colon mucosa in terms of basic fibroblast growth factor (bFGF) indicates that 6-29 ng/g tissue of bFGF-like activity was present in five samples of normal human colon and in five corresponding samples of malignant colon mucosa.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	181-185
21573455-1	1993	Quantification of the amount of heparin-binding growth factor activity present in homogenates of normal and malignant human colon mucosa in terms of basic fibroblast growth factor (bFGF) indicates that 6-29 ng/g tissue of bFGF-like activity was present in five samples of normal human colon and in five corresponding samples of malignant colon mucosa.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	222-226
8227367-6	1993	PN-2/A beta PP inhibited Factor IXa with a Ki of 7.9 to 3.9 x 10(-11) M in the absence and presence of heparin, respectively.	Heparin	103-110	amyloid beta precursor protein	Homo sapiens	0-4
7511160-0	1993	Influence of heparin on the chemotactic activity of human thrombin.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	58-66
7511160-3	1993	Addition of heparins to thrombin led to an increase in the chemoattractant activity of this enzyme for at least one of the doses studied.	Heparin	12-20	coagulation factor II, thrombin	Homo sapiens	24-32
7511160-4	1993	Augmentation of the chemoattractant activity of thrombin by heparins was shown at concentrations equivalent to those found in-vivo after administration of therapeutic doses of heparin.	Heparin	60-68	coagulation factor II, thrombin	Homo sapiens	48-56
7511160-4	1993	Augmentation of the chemoattractant activity of thrombin by heparins was shown at concentrations equivalent to those found in-vivo after administration of therapeutic doses of heparin.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	48-56
7509511-7	1993	The inhibition of the thrombin peak by heparin, relative to an uninhibited control, remains unaltered by the presence of the substrate.	Heparin	39-46	coagulation factor II, thrombin	Homo sapiens	22-30
8215459-0	1993	Heparin-von Willebrand factor binding as assessed by isothermal titration calorimetry and by affinity fractionation of heparins using synthetic peptides.	Heparin	119-127	von Willebrand factor	Homo sapiens	8-29
8215459-2	1993	Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B.	Heparin	34-41	von Willebrand factor	Homo sapiens	112-133
8215459-2	1993	Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B.	Heparin	34-41	von Willebrand factor	Homo sapiens	135-138
8215459-2	1993	Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B.	Heparin	178-185	von Willebrand factor	Homo sapiens	112-133
8215459-2	1993	Based on the motif of a consensus heparin-binding synthetic peptide, a 23-residue sequence (Y565-A587) of human von Willebrand factor (vWF) was previously identified which binds heparin with affinity comparable to that of the native protein (Sobel, M., Soler, D. F., Kermode, J. C., and Harris, R. B.	Heparin	178-185	von Willebrand factor	Homo sapiens	135-138
8215459-11	1993	They bind a species of heparin which possesses significantly enhanced affinity for native vWF.	Heparin	23-30	von Willebrand factor	Homo sapiens	90-93
8215459-13	1993	Thus, the vWF peptides are a useful model for studying the physiological role of heparin binding to the native protein.	Heparin	81-88	von Willebrand factor	Homo sapiens	10-13
8222188-12	1993	After protamine is cleared, the protein-bound heparin dissociates slowly and binds to anti-thrombin III to produce an anticoagulant effect.	Heparin	46-53	coagulation factor II, thrombin	Homo sapiens	91-99
8034236-6	1993	After 15-day heparin treatment a decrease in euglobulin lysis time (p &lt; 0.05) and an increase in t-PA activity (act) (p &lt; 0.05) and in t-PA ag (p &lt; 0.01) in comparison with placebo were observed before VO.	Heparin	13-20	plasminogen activator, tissue type	Homo sapiens	100-104
8034236-6	1993	After 15-day heparin treatment a decrease in euglobulin lysis time (p &lt; 0.05) and an increase in t-PA activity (act) (p &lt; 0.05) and in t-PA ag (p &lt; 0.01) in comparison with placebo were observed before VO.	Heparin	13-20	plasminogen activator, tissue type	Homo sapiens	141-145
8034236-9	1993	These results indicate that medium-term low-dose heparin treatment increases t-PA ag formation and/or release with consequent t-PA act increase.	Heparin	49-56	plasminogen activator, tissue type	Homo sapiens	77-81
8034236-9	1993	These results indicate that medium-term low-dose heparin treatment increases t-PA ag formation and/or release with consequent t-PA act increase.	Heparin	49-56	plasminogen activator, tissue type	Homo sapiens	126-130
8211041-1	1993	Previous studies have demonstrated that heparin-induced extracorporeal LDL precipitation is able to reduce total cholesterol, LDL, triglycerides and plasma fibrinogen at the same time and thus improve the hemorheologic pattern.	Heparin	40-47	fibrinogen beta chain	Homo sapiens	156-166
8407970-2	1993	Chromatography of a retinal homogenate on a heparin column partially resolved six peaks of PLC activity, which differed in their relative selectivities for the substrates phosphatidyl 4,5-bisphosphate (PIP2) and phosphatidylinositol (PI).	Heparin	44-51	no receptor potential A	Drosophila melanogaster	91-94
7513265-6	1993	bFGF detected on the cell surface and within the cells could be partially removed by treatment with heparin or heparinase and with heparin or DNase, respectively.	Heparin	100-107	fibroblast growth factor 2	Homo sapiens	0-4
8291446-4	1993	This bioactive molecule was determined as bFGF by using the heparin-Sepharose affinity chromatography and western blot analysis.	Heparin	60-67	fibroblast growth factor 2	Homo sapiens	42-46
8399074-0	1993	Depletion of lipoprotein lipase after heparin administration.	Heparin	38-45	lipoprotein lipase	Rattus norvegicus	13-31
8399074-2	1993	Heparin greatly enhances this dissociation and delays but does not abolish uptake in the liver, raising the possibility that heparin could lead to accelerated catabolism of functional LPL.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	184-187
8399074-2	1993	Heparin greatly enhances this dissociation and delays but does not abolish uptake in the liver, raising the possibility that heparin could lead to accelerated catabolism of functional LPL.	Heparin	125-132	lipoprotein lipase	Rattus norvegicus	184-187
8399074-4	1993	The high dose (250 U/kg) of both heparins resulted in similar initial levels of LPL activity in plasma, but at 30 minutes the activity with LMWH had declined by more than 80%, whereas with UFH it remained essentially unchanged during this time.	Heparin	33-41	lipoprotein lipase	Rattus norvegicus	80-83
8399074-7	1993	These results agree with previous studies that indicate that LMWH has a similar ability as UFH to release LPL, but a lesser ability to delay its removal by the liver.	Heparin	91-94	lipoprotein lipase	Rattus norvegicus	106-109
8292720-8	1993	Since heparin shows strong binding to the C-terminus of TFPI, we also tested its effect on the binding of full length TFPI to VLDL.	Heparin	6-13	tissue factor pathway inhibitor	Oryctolagus cuniculus	56-60
8292720-8	1993	Since heparin shows strong binding to the C-terminus of TFPI, we also tested its effect on the binding of full length TFPI to VLDL.	Heparin	6-13	tissue factor pathway inhibitor	Oryctolagus cuniculus	118-122
8292720-9	1993	We found that co-incubation of TFPI with heparin inhibited this binding in a dose-dependent manner.	Heparin	41-48	tissue factor pathway inhibitor	Oryctolagus cuniculus	31-35
8292720-10	1993	Heparin was also capable of releasing TFPI from a preformed TFPI:VLDL complex, although this reaction required unphysiological amounts of heparin.	Heparin	0-7	tissue factor pathway inhibitor	Oryctolagus cuniculus	38-42
8292720-10	1993	Heparin was also capable of releasing TFPI from a preformed TFPI:VLDL complex, although this reaction required unphysiological amounts of heparin.	Heparin	0-7	tissue factor pathway inhibitor	Oryctolagus cuniculus	60-64
8292720-13	1993	Previous experiments indicated that heparin has a protective effect on exogenously added FL-TFPI, increasing its recovery by ten-fold.	Heparin	36-43	tissue factor pathway inhibitor	Oryctolagus cuniculus	92-96
8292721-0	1993	Effects of low molecular weight heparins on fibrin polymerization and clot sensitivity to t-PA-induced lysis.	Heparin	32-40	plasminogen activator, tissue type	Homo sapiens	90-94
8292721-1	1993	We have previously demonstrated that therapeutic concentrations of unfractionated heparin (UFH) impair fibrin polymerization leading to the formation of clots which are more sensitive to lysis induced by tissue plasminogen activator (t-PA).	Heparin	82-89	plasminogen activator, tissue type	Homo sapiens	204-238
8292721-1	1993	We have previously demonstrated that therapeutic concentrations of unfractionated heparin (UFH) impair fibrin polymerization leading to the formation of clots which are more sensitive to lysis induced by tissue plasminogen activator (t-PA).	Heparin	91-94	plasminogen activator, tissue type	Homo sapiens	204-238
8292721-2	1993	The aim of this study was to compare the effect of UFH with that of three different low molecular weight heparins (LMWHs) on clot sensitivity to t-PA-induced lysis.	Heparin	105-113	plasminogen activator, tissue type	Homo sapiens	145-149
8408476-9	1993	In contrast, the mitogenic activity of WRO cells bound to heparin with high affinity and was blocked by a basic fibroblast growth factor (bFGF) antibody.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	138-142
7691835-8	1993	The differential effects of these PA in potentiating the biological activities of aFGF are discussed in relation to their ability to compete for the heparin-binding site of aFGF.	Heparin	149-156	fibroblast growth factor 1	Mus musculus	82-86
7691835-8	1993	The differential effects of these PA in potentiating the biological activities of aFGF are discussed in relation to their ability to compete for the heparin-binding site of aFGF.	Heparin	149-156	fibroblast growth factor 1	Mus musculus	173-177
7691835-1	1993	The ability of several animal, plant, and bacterial derived polyanions (PAs) as well as synthetic PAs to compete with heparin for the binding of acidic fibroblast growth factor (aFGF) was correlated with their ability to potentiate the mitogenic and neurotrophic actions of this factor.	Heparin	118-125	fibroblast growth factor 1	Mus musculus	145-176
7691835-1	1993	The ability of several animal, plant, and bacterial derived polyanions (PAs) as well as synthetic PAs to compete with heparin for the binding of acidic fibroblast growth factor (aFGF) was correlated with their ability to potentiate the mitogenic and neurotrophic actions of this factor.	Heparin	118-125	fibroblast growth factor 1	Mus musculus	178-182
7691835-2	1993	Dextran sulphate, kappa-carrageenan, pentosan sulphate, polyanethole sulfonate, heparin, and fucoidin competed for the heparin binding site on aFGF at relatively low concentrations (&lt; 50 micrograms/ml).	Heparin	80-87	fibroblast growth factor 1	Mus musculus	143-147
7691835-2	1993	Dextran sulphate, kappa-carrageenan, pentosan sulphate, polyanethole sulfonate, heparin, and fucoidin competed for the heparin binding site on aFGF at relatively low concentrations (&lt; 50 micrograms/ml).	Heparin	119-126	fibroblast growth factor 1	Mus musculus	143-147
8408661-2	1993	The present study examined the effect of heparin on vasoconstrictor endothelin-1 (ET-1) production in cultured human umbilical vein endothelial cells (ECs) to elucidate the mechanism of antihypertensive effect of heparin.	Heparin	41-48	endothelin 1	Homo sapiens	68-80
8408661-2	1993	The present study examined the effect of heparin on vasoconstrictor endothelin-1 (ET-1) production in cultured human umbilical vein endothelial cells (ECs) to elucidate the mechanism of antihypertensive effect of heparin.	Heparin	41-48	endothelin 1	Homo sapiens	82-86
8408661-3	1993	Heparin suppressed both basal and thrombin-stimulated ET-1 mRNA expression paralleled with a decrease in ET-1 peptide release in a dose-dependent manner.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	34-42
8408661-3	1993	Heparin suppressed both basal and thrombin-stimulated ET-1 mRNA expression paralleled with a decrease in ET-1 peptide release in a dose-dependent manner.	Heparin	0-7	endothelin 1	Homo sapiens	54-58
8408661-3	1993	Heparin suppressed both basal and thrombin-stimulated ET-1 mRNA expression paralleled with a decrease in ET-1 peptide release in a dose-dependent manner.	Heparin	0-7	endothelin 1	Homo sapiens	105-109
8408661-4	1993	Heparin concomitantly enhanced nitric oxide (NO) formation measured by NO2/NO3 levels and cGMP production in ECs.	Heparin	0-7	NBL1, DAN family BMP antagonist	Homo sapiens	75-78
8408661-7	1993	Therefore, these results suggest that suppression of ET-1 production by heparin is EDNO mediated.	Heparin	72-79	endothelin 1	Homo sapiens	53-57
8232678-3	1993	Heparin-induced extracorporeal LDL precipitation (HELP) is a method that effectively reduces fibrinogen and lipoproteins at the same time, thus improving the hemorheologic pattern.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	93-103
7692141-3	1993	We determined that a heparin dose of 1 U/ml prevented clot formation in this model, but resulted in elevated plasma levels of fibrinopeptide A, the first cleavage product of fibrinogen.	Heparin	21-28	fibrinogen beta chain	Homo sapiens	174-184
8378944-2	1993	Heparin-induced extracorporeal low density lipoprotein precipitation (HELP) is a new method that safely and effectively reduces fibrinogen and plasma lipoproteins and improves blood flow properties.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	128-138
7505345-9	1993	3) Inflammatory reactants such as fibrinogen, alpha 2-PI,alpha 2-macroglobulin and alpha 1-antitrypsin decreased more significantly during this heparin-urokinase-pulse combined therapy than during our previous combined therapy consisting of only heparin and urokinase.	Heparin	144-151	serpin family A member 1	Homo sapiens	83-102
8360182-0	1993	Modulation of tissue plasminogen activator-catalyzed plasminogen activation by synthetic peptides derived from the amino-terminal heparin binding domain of fibronectin.	Heparin	130-137	fibronectin 1	Homo sapiens	156-167
8379940-0	1993	Heparin-affinity patterns and composition of extracellular superoxide dismutase in human plasma and tissues.	Heparin	0-7	superoxide dismutase 3	Homo sapiens	45-79
8379940-1	1993	The tetrameric extracellular superoxide dismutase (EC-SOD) in human tissues and plasma has previously been found to be heterogenous with regard to heparin affinity and could be divided into at least three classes: A, lacking heparin affinity; B, with weak affinity; and C, with strong affinity.	Heparin	147-154	superoxide dismutase 3	Homo sapiens	15-49
8379940-1	1993	The tetrameric extracellular superoxide dismutase (EC-SOD) in human tissues and plasma has previously been found to be heterogenous with regard to heparin affinity and could be divided into at least three classes: A, lacking heparin affinity; B, with weak affinity; and C, with strong affinity.	Heparin	147-154	superoxide dismutase 3	Homo sapiens	51-57
8379940-1	1993	The tetrameric extracellular superoxide dismutase (EC-SOD) in human tissues and plasma has previously been found to be heterogenous with regard to heparin affinity and could be divided into at least three classes: A, lacking heparin affinity; B, with weak affinity; and C, with strong affinity.	Heparin	225-232	superoxide dismutase 3	Homo sapiens	15-49
8379940-1	1993	The tetrameric extracellular superoxide dismutase (EC-SOD) in human tissues and plasma has previously been found to be heterogenous with regard to heparin affinity and could be divided into at least three classes: A, lacking heparin affinity; B, with weak affinity; and C, with strong affinity.	Heparin	225-232	superoxide dismutase 3	Homo sapiens	51-57
8379940-3	1993	Plasma EC-SOD on the other hand is shown to be mainly composed of a complex mixture of heterotetramers with modifications probably residing in the C-terminal heparin-binding domain.	Heparin	158-165	superoxide dismutase 3	Homo sapiens	7-13
8216346-12	1993	However, while the heparin-releasable fraction of capillary-bound LPL was inhibited in the plasma, LPL activity significantly increased in cardiac and skeletal muscle in poloxamer-injected animals compared with sham-injected controls.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	66-69
8216346-14	1993	Our studies would suggest that the predominant mechanism by which P-407 induced an increase in circulating TG was by a reduction in the rate at which TG was hydrolyzed due to inhibition of heparin-releasable LPL by the surfactant.	Heparin	189-196	lipoprotein lipase	Rattus norvegicus	208-211
8225173-11	1993	Platelet aggregation induced by KDH-8 tumor cells was inhibited by ADP inhibitor (apyrase, CP/CPK) and thrombin inhibitor (heparin, MD-805); KDH-8 tumor cells induced platelet aggregation by two different mechanisms: ADP-mediated aggregation and thrombin-mediated aggregation.	Heparin	123-130	coagulation factor II	Rattus norvegicus	103-111
8281615-2	1993	As secreted by tumor cells, VPF/VEGF is a 34-42 kDa heparin-binding, dimeric, disulfide-bonded glycoprotein that acts directly on endothelial cells (EC) by way of specific receptors to activate phospholipase C and induce [Ca2+]i transients.	Heparin	52-59	vascular endothelial growth factor A	Homo sapiens	28-31
8281615-2	1993	As secreted by tumor cells, VPF/VEGF is a 34-42 kDa heparin-binding, dimeric, disulfide-bonded glycoprotein that acts directly on endothelial cells (EC) by way of specific receptors to activate phospholipase C and induce [Ca2+]i transients.	Heparin	52-59	vascular endothelial growth factor A	Homo sapiens	32-36
8406134-4	1993	Heparin administration preceding renal artery clamping resulted in a twofold significant increase of baseline plasma myeloperoxidase (MPO) level (523 +/- 214 ng/ml).	Heparin	0-7	myeloperoxidase	Homo sapiens	117-132
8406134-4	1993	Heparin administration preceding renal artery clamping resulted in a twofold significant increase of baseline plasma myeloperoxidase (MPO) level (523 +/- 214 ng/ml).	Heparin	0-7	myeloperoxidase	Homo sapiens	134-137
8227183-5	1993	The antiproliferative activities of the peptides correlate with their ability to bind to heparin and to inhibit bFGF binding to heparin.	Heparin	128-135	fibroblast growth factor 2	Homo sapiens	112-116
8259546-0	1993	The additive effect of low molecular weight heparins on thrombin inhibition by dermatan sulfate.	Heparin	44-52	coagulation factor II, thrombin	Homo sapiens	56-64
8246925-2	1993	These proteins, corresponding to human Oct-1 and Oct-2A nuclear factors, were purified by ion exchange and heparin-agarose chromatography.	Heparin	107-114	POU domain, class 2, transcription factor 2	Mus musculus	49-55
8259548-7	1993	When heparin was administered 2 h following TFPI the recovery of FL-TFPI was similar to that found in the group receiving the two compounds simultaneously, suggesting that the releasable pool of FL-TFPI is removed very slowly in the absence of circulating heparin.	Heparin	5-12	tissue factor pathway inhibitor	Oryctolagus cuniculus	68-72
8259548-7	1993	When heparin was administered 2 h following TFPI the recovery of FL-TFPI was similar to that found in the group receiving the two compounds simultaneously, suggesting that the releasable pool of FL-TFPI is removed very slowly in the absence of circulating heparin.	Heparin	5-12	tissue factor pathway inhibitor	Oryctolagus cuniculus	68-72
8259548-3	1993	Full length (FL) TFPI, but not recombinant two-domain (2D) TFPI, has a poly cationic C-terminus showing very strong heparin binding.	Heparin	116-123	tissue factor pathway inhibitor	Oryctolagus cuniculus	17-21
8259548-4	1993	Therefore, we have investigated if heparin affects the pharmacokinetics of TFPI with and without this C-terminus.	Heparin	35-42	tissue factor pathway inhibitor	Oryctolagus cuniculus	75-79
8259548-6	1993	Heparin decreased the volume of distribution and the clearance of FL-TFPI by a factor 10-15, whereas the pharmacokinetics of 2D-TFPI were unaffected by heparin.	Heparin	0-7	tissue factor pathway inhibitor	Oryctolagus cuniculus	69-73
8259548-7	1993	When heparin was administered 2 h following TFPI the recovery of FL-TFPI was similar to that found in the group receiving the two compounds simultaneously, suggesting that the releasable pool of FL-TFPI is removed very slowly in the absence of circulating heparin.	Heparin	5-12	tissue factor pathway inhibitor	Oryctolagus cuniculus	44-48
8394353-14	1993	In rat liver cells, the increases in [Ca2+]i induced by TBHP and thimerosal were prevented by microinjection of the cells with the (1,4,5)IP3 receptor antagonist heparin.	Heparin	162-169	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	138-150
8342955-4	1993	Kinetic analysis demonstrates that YCK2 is similar to casein kinase-1 isolated from other organisms in its inability to use GTP as nucleotide substrate, in its sensitivity to heparin and ribofuranosyl-benzimidazole inhibitors, and in its peptide substrate selectivity.	Heparin	175-182	serine/threonine protein kinase YCK2	Saccharomyces cerevisiae S288C	35-39
8340381-10	1993	These results suggest that a type V collagen-binding site is present in the 80-residue portion of bovine TSP (Val333-Lys412) and is likely to be identical or lie very close to a heparin-binding site, which exists in the type I repeat structure.	Heparin	178-185	thrombospondin 1	Homo sapiens	105-108
8236137-2	1993	The present report describes the antithrombin mediated inhibition of thrombin and factor Xa by surfaces modified with end point immobilized heparin.	Heparin	140-147	coagulation factor II, thrombin	Homo sapiens	37-45
8236137-5	1993	The thrombin inhibitory capacity was enhanced when both high and low affinity heparin were preadsorbed with inhibitor.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	4-12
8236137-6	1993	The main part of the thrombin-antithrombin complex formed remained bound to the surface, however, without functionally blocking the activity of the high affinity sequence of the immobilized heparin.	Heparin	190-197	coagulation factor II, thrombin	Homo sapiens	21-29
8218851-3	1993	It is known that heparin impairs the binding of TH to isolated liver cells through the inhibition of high affinity receptors.	Heparin	17-24	coagulation factor II	Rattus norvegicus	48-50
7688769-12	1993	We conclude that adult human lung fibroblasts produce at least two soluble heparin-binding growth factors, KGF and HGF/SF, which promote DNA synthesis and proliferation of rat alveolar type II cells in primary culture.	Heparin	75-82	fibroblast growth factor 7	Homo sapiens	107-110
8394644-3	1993	Thrombin inhibition is also negligible when heparin is added to platelet-rich plasma.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	0-8
8236160-7	1993	Significant changes in APTT (1.9 +/- 0.3 fold over baseline) were only evident at the highest dose of rTAP while heparin caused a significant dose-dependent increase from 1.3 +/- 0.2 to greater than 4.2 +/- 0.6 fold over baseline.	Heparin	113-120	nuclear RNA export factor 1	Rattus norvegicus	102-106
8236161-1	1993	Thrombomodulin (TM) is an endothelial cell membrane glycoprotein which neutralizes thrombin procoagulant activity and accelerates the thrombin-catalyzed activation of protein C. We expressed recombinant human soluble TM (rhs-TM) in Chinese hamster ovary cells and compared the effects of rhs-TM and heparin on endotoxin-induced experimental disseminated intravascular coagulation (DIC) in rats.	Heparin	299-306	thrombomodulin	Rattus norvegicus	0-14
8236131-1	1993	Blood samples were collected from 43 patients undergoing elective cardiac surgery to determine the extent of thrombin generation and inhibition in patients when receiving heparin while undergoing cardiopulmonary bypass (CPB).	Heparin	171-178	coagulation factor II, thrombin	Homo sapiens	109-117
8236131-5	1993	Furthermore, thrombin generation increased following the neutralization of the heparin with protamine sulphate, and continued to be elevated significantly 24 h post surgery.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	13-21
8218851-4	1993	Using an isolated, exsanguinated and perfused rat liver preparation we confirmed that the TH hepatic clearance is calcium-independent and affected by heparin; PK clearance rates both in the presence (t1/2 10 +/- 2 min) or the absence (t1/2 10 +/- 1 min) of heparin were similar; the presence of beta-galactosides does not impair the TH clearance but adversely affects the PK clearance and a large excess of TH does not impair the PK clearance rate (t1/2 6 +/- 1 min).	Heparin	150-157	coagulation factor II	Rattus norvegicus	90-92
8218851-4	1993	Using an isolated, exsanguinated and perfused rat liver preparation we confirmed that the TH hepatic clearance is calcium-independent and affected by heparin; PK clearance rates both in the presence (t1/2 10 +/- 2 min) or the absence (t1/2 10 +/- 1 min) of heparin were similar; the presence of beta-galactosides does not impair the TH clearance but adversely affects the PK clearance and a large excess of TH does not impair the PK clearance rate (t1/2 6 +/- 1 min).	Heparin	257-264	coagulation factor II	Rattus norvegicus	90-92
8346230-0	1993	Binding to heparan sulfate or heparin enhances neutrophil responses to interleukin 8.	Heparin	30-37	C-X-C motif chemokine ligand 8	Homo sapiens	71-84
8346230-1	1993	The interaction of interleukin 8 (IL-8) with heparin was studied by using synthetic IL-8 analogs with C- and N-terminal truncations.	Heparin	45-52	C-X-C motif chemokine ligand 8	Homo sapiens	19-32
8346230-1	1993	The interaction of interleukin 8 (IL-8) with heparin was studied by using synthetic IL-8 analogs with C- and N-terminal truncations.	Heparin	45-52	C-X-C motif chemokine ligand 8	Homo sapiens	34-38
7694075-0	1993	Mitogenic activity of acidic fibroblast growth factor is enhanced by highly sulfated oligosaccharides derived from heparin and heparan sulfate.	Heparin	115-122	fibroblast growth factor 1	Homo sapiens	22-53
7694075-1	1993	The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains.	Heparin	195-202	fibroblast growth factor 1	Homo sapiens	26-57
8322775-8	1993	The heparin-releasable LPL pool is that pool bound to the vascular endothelium and represents the biologically active fraction.	Heparin	4-11	lipoprotein lipase	Rattus norvegicus	23-26
7694075-1	1993	The mitogenic activity of acidic fibroblast growth factor (aFGF) is potentiated by the highly sulfated hexasaccharide [IdoUA,2S-GlcNS,6S]2-[GlcUA-GlcNS,6S] the structural repetitive unit of lung heparin chains.	Heparin	195-202	fibroblast growth factor 1	Homo sapiens	59-63
8314753-9	1993	Binding of low molecular weight heparin to the uPA/K in 2H2O affects mainly the His37, His40, His48a, and Tyr50 resonances, in a concerted and saturable fashion (association constant approximately 58 mM-1).	Heparin	32-39	plasminogen activator, urokinase	Homo sapiens	47-50
8331659-6	1993	The most significant difference between ATIII and alpha 1-antitrypsin lies in the 45 residue N-terminal extension in ATIII which contribute to the definition of the heparin binding site.	Heparin	165-172	serpin family A member 1	Homo sapiens	50-69
8253022-0	1993	The effect of a heparin analogue, ITF-5005, on diabetes incidence and insulitis in the non-obese diabetic mouse.	Heparin	16-23	trefoil factor 3, intestinal	Mus musculus	34-37
7686785-15	1993	The near universal use of heparin during CPB is likely to contribute substantially to this defect via its inhibition of thrombin, the preeminent platelet activator.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	120-128
8268545-3	1993	When using heparin as the anticoagulant, large increases in bradykinin levels in plasma were observed after its passage through the column during the procedure.	Heparin	11-18	kininogen 1	Homo sapiens	60-70
8253022-2	1993	We have investigated whether a heparin analogue (ITF-5005) can alter lymphocytic infiltration of the endocrine pancreas (insulitis) and/or diabetes incidence in the non-obese diabetic (NOD) mouse.	Heparin	31-38	trefoil factor 3, intestinal	Mus musculus	49-52
8253024-0	1993	Relationship between urinary excretion of fibronectin degradation products and proteinuria in diabetic patients, and their suppression after continuous subcutaneous heparin infusion.	Heparin	165-172	fibronectin 1	Homo sapiens	42-53
7686045-3	1993	The presence of equimolar or greater amounts of heparin stabilizes aFGF from unfolding by more than 2.5 kcal mol-1 and slows the rate of unfolding by greater than 2000-fold.	Heparin	48-55	fibroblast growth factor 1	Homo sapiens	67-71
8243716-6	1993	Propranolol in the same dose also blocked the stimulatory action of i. v. injected alpha-thrombin (50 NIH/kg) on heparin secretion from mast cells of subcutaneous connective tissue.	Heparin	113-120	coagulation factor II	Rattus norvegicus	89-97
8243716-7	1993	The obtained results show that catecholamines participate in activation of heparin release from mast cells induced both by the stress and by thrombin injection.	Heparin	75-82	coagulation factor II	Rattus norvegicus	141-149
7686045-4	1993	The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	36-40
7686045-4	1993	The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	107-111
7686045-4	1993	The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide.	Heparin	135-142	fibroblast growth factor 1	Homo sapiens	36-40
7686045-4	1993	The ability of heparin to stabilize aFGF is critically dependent upon many factors including the number of aFGF molecules bound to the heparin chain, ionic strength, temperature, and the extent of sulfation of the polysaccharide.	Heparin	135-142	fibroblast growth factor 1	Homo sapiens	107-111
7686045-6	1993	Additional experiments demonstrate that increasing charge density enhances the ability of polyanions such as sulfated beta-cyclodextrins, phosphorylated inositols, and modified heparins to protect aFGF from urea-induced unfolding.	Heparin	177-185	fibroblast growth factor 1	Homo sapiens	197-201
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	129-137
8320843-4	1993	Each vWf subunit has binding sites for collagen, heparin, GP Ib, GPIIb/IIIa and factor VIII.	Heparin	49-56	von Willebrand factor	Homo sapiens	5-8
8100744-4	1993	The baseline expression of CD11b and CD18 on unstimulated neutrophils was similar in heparin and EDTA anti-coagulated blood but the response to activation with fMLP was significantly less for the EDTA anti-coagulated samples (p &lt; 0.01 in paired t-test).	Heparin	85-92	integrin subunit beta 2	Homo sapiens	37-41
8374170-4	1993	The COOH-terminal heparin-binding domain of fibronectin contains five separate heparin-binding amino acid sequences.	Heparin	18-25	fibronectin 1	Homo sapiens	44-55
8505310-9	1993	The thrombin-inactivating activity was markedly enhanced by optimal concentrations of heparin.	Heparin	86-93	coagulation factor II	Mus musculus	4-12
8508806-9	1993	Moreover, tryptic digestion studies performed with various heparin molecules and dextran sulfates of different size, ranging from 2.0 kDa to 500 kDa, indicate that the number of bFGF molecules which interact with a single molecule of polysaccharide is related to the molecular mass of the GAG and that six hexose residues are sufficient to protect 1-2 molecules bFGF.	Heparin	59-66	fibroblast growth factor 2	Homo sapiens	178-182
8340464-1	1993	A high-performance immunoaffinity chromatographic (HPIAC) method for fibrinogen was developed which had several advantages over existing methodologies including increased linear range and no interference from heparin.	Heparin	209-216	fibrinogen beta chain	Homo sapiens	69-79
8508806-4	1993	Heparin protects bFGF from trypsin digestion in a dose-dependent fashion.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	17-21
8508806-6	1993	In contrast, heparin protection is abolished when the full region bFGF(27-32) is deleted.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	66-70
8389078-10	1993	The presence of both gIII and the essential glycoprotein gp50 (gD) was shown to be critical for heparin-resistant binding.	Heparin	96-103	tumor associated calcium signal transducer 2	Homo sapiens	57-61
7684608-0	1993	Nature of the interaction of heparin with acidic fibroblast growth factor.	Heparin	29-36	fibroblast growth factor 1	Homo sapiens	42-73
7684608-2	1993	Static and dynamic light scattering as well as analytical ultracentrifugation analyses indicates that 14-15 molecules of a FGF can bind to a 16-kDa heparin chain, with approximately 10 of these bound relatively uniformly to high-affinity sites.	Heparin	148-155	fibroblast growth factor 1	Homo sapiens	123-126
7684608-3	1993	The dissociation constants of these latter sites are estimated to be approximately 50-140 nM on the basis of surface plasmon resonance experiments in which the association and dissociation rates of aFGF interaction with immobilized heparin were measured.	Heparin	232-239	fibroblast growth factor 1	Homo sapiens	198-202
7684608-4	1993	The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides.	Heparin	41-48	fibroblast growth factor 1	Homo sapiens	34-37
7684608-4	1993	The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides.	Heparin	41-48	fibroblast growth factor 1	Homo sapiens	101-104
7684608-4	1993	The size of the binding site of a FGF on heparin was also determined by heparin lyase digestion of a FGF/heparin complexes followed by isolation and characterization of protected oligosaccharides.	Heparin	72-79	fibroblast growth factor 1	Homo sapiens	34-37
7684608-6	1993	Thus, aFGF appears to bind at high density (one molecule every 4-5 polysaccharide units) and with high affinity to heparin.	Heparin	115-122	fibroblast growth factor 1	Homo sapiens	6-10
8387813-2	1993	The kringles interact with thrombin at a site that has previously been proposed to be the heparin binding region.	Heparin	90-97	coagulation factor II, thrombin	Homo sapiens	27-35
8490019-10	1993	The results indicate that fibronectin, type I collagen, and laminin--but not thrombospondin--each fractionate heparin into subpopulations that differ substantially in binding affinity.	Heparin	110-117	fibronectin 1	Homo sapiens	26-37
8508806-7	1993	The capacity of different GAGs to protect bFGF from proteolytic cleavage decreases in the following order: heparin &gt; heparan sulfate &gt; dermatan sulfate = chondroitin sulfates A and C &gt; hyaluronic acid = K5 polysaccharide, indicating that both the degree of sulfation and the backbone structure of GAG modulate its interaction with bFGF.	Heparin	107-114	fibroblast growth factor 2	Homo sapiens	42-46
8322266-1	1993	We developed a simple and fast method for studying the heparin binding of von Willebrand factor (vWF) in the plasma milieu.	Heparin	55-62	von Willebrand factor	Homo sapiens	74-95
8322266-1	1993	We developed a simple and fast method for studying the heparin binding of von Willebrand factor (vWF) in the plasma milieu.	Heparin	55-62	von Willebrand factor	Homo sapiens	97-100
8322266-3	1993	Further experiments performed with purified vWF of various multimeric composition, obtained either by gradual reduction or gel filtration, confirmed that heparin binding is dependent on the multimerization of vWF and that high molecular weight (HMW) multimers of vWF are required for normal heparin binding.	Heparin	154-161	von Willebrand factor	Homo sapiens	44-47
8322266-3	1993	Further experiments performed with purified vWF of various multimeric composition, obtained either by gradual reduction or gel filtration, confirmed that heparin binding is dependent on the multimerization of vWF and that high molecular weight (HMW) multimers of vWF are required for normal heparin binding.	Heparin	154-161	von Willebrand factor	Homo sapiens	209-212
8322266-3	1993	Further experiments performed with purified vWF of various multimeric composition, obtained either by gradual reduction or gel filtration, confirmed that heparin binding is dependent on the multimerization of vWF and that high molecular weight (HMW) multimers of vWF are required for normal heparin binding.	Heparin	154-161	von Willebrand factor	Homo sapiens	209-212
8322266-4	1993	After reduction of plasma vWF by 1.5 mM DTT, the vWF monomer still binds to heparin but to a lower extent.	Heparin	76-83	von Willebrand factor	Homo sapiens	49-52
8322266-5	1993	Under these conditions, no significant differences were obtained between control and patients showing that the heparin binding domain located on the vWF subunit is not altered in the subtypes IIA, IIB and IIC studied.	Heparin	111-118	von Willebrand factor	Homo sapiens	149-152
8509711-2	1993	Both apolipoprotein (apo) E-poor and apoE-rich Type IV VLDL subfractions, isolated by heparin-Sepharose chromatography, were capable of enhancing cellular cholesterol and triglyceride content.	Heparin	86-93	apolipoprotein E	Mus musculus	37-41
8387532-4	1993	These two proteins also showed higher heparin binding affinity than that of wt K-FGF.	Heparin	38-45	fibroblast growth factor 4	Homo sapiens	79-84
8387532-9	1993	Thus removal of the NH2-terminal 36 amino acids from the mature K-FGF produces growth factor molecules with an altered conformation, resulting in higher heparin affinity, and more efficient binding to FGF receptors.	Heparin	153-160	fibroblast growth factor 4	Homo sapiens	64-69
8320164-0	1993	Carboxyl-terminal heparin-binding fragments of platelet factor 4 retain the blocking effect on the receptor binding of basic fibroblast growth factor.	Heparin	18-25	fibroblast growth factor 2	Bos taurus	119-149
8483941-4	1993	Heparin, which blocks the binding of ligands to the LDL receptor, completely inhibited the effects of LDL on signal transduction and PtdCho secretion but did not inhibit the effects of HDL.	Heparin	0-7	low density lipoprotein receptor	Rattus norvegicus	52-64
8518334-0	1993	Heparin increased cell membrane-associated heparan sulfate proteoglycan in balloon-injured rat carotid artery.	Heparin	0-7	syndecan 2	Rattus norvegicus	43-71
8518334-1	1993	The effect of heparin on the amount of membrane-associated heparan sulfate proteoglycan (HSPG) was examined biochemically in balloon-injured rat carotid arteries.	Heparin	14-21	syndecan 2	Rattus norvegicus	59-87
8518334-1	1993	The effect of heparin on the amount of membrane-associated heparan sulfate proteoglycan (HSPG) was examined biochemically in balloon-injured rat carotid arteries.	Heparin	14-21	syndecan 2	Rattus norvegicus	89-93
8518334-7	1993	Heparin treatment significantly increased membrane-associated HSPG by 64% in the arteries incubated for 24 h, while heparin hardly increased the HSPG in 6 h incubated arteries.	Heparin	0-7	syndecan 2	Rattus norvegicus	62-66
8518334-7	1993	Heparin treatment significantly increased membrane-associated HSPG by 64% in the arteries incubated for 24 h, while heparin hardly increased the HSPG in 6 h incubated arteries.	Heparin	116-123	syndecan 2	Rattus norvegicus	145-149
8518334-8	1993	Since the 24-hour data seem to reflect a combination of biosynthesis and degradation of proteoglycans while the 6-hour data primarily reflect biosynthesis, these results suggest that inhibition of degradation of membrane-associated HSPG is involved in the mechanism of heparin action.	Heparin	269-276	syndecan 2	Rattus norvegicus	232-236
7686672-3	1993	It was found that in addition to the well-known protection of aFGF by heparin, a surprisingly wide variety of polyanions (including small sulfated and phosphorylated compounds) also stabilizes aFGF.	Heparin	70-77	fibroblast growth factor 1	Mus musculus	62-66
8497482-0	1993	Crystallization and preliminary X-ray diffraction data of two heparin-binding fragments of human fibronectin.	Heparin	62-69	fibronectin 1	Homo sapiens	97-108
8508903-7	1993	Moreover, lipoprotein lipase activity in heparin-injected plasma was increased in rats given EPA-E without there being an effect on hepatic triglyceride lipase activity.	Heparin	41-48	lipoprotein lipase	Rattus norvegicus	10-28
7681826-0	1993	Vascular endothelial growth factor is inactivated by binding to alpha 2-macroglobulin and the binding is inhibited by heparin.	Heparin	118-125	vascular endothelial growth factor A	Homo sapiens	0-34
7681826-12	1993	Heparin and heparan sulfate, but not other glycosaminoglycans such as chondroitin sulfate, efficiently inhibited the binding of 125I-VEGF to alpha 2M.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	133-137
8385492-5	1993	The specificity of the RBL cell IP3 receptor towards phosphoinositides, ATP and heparin parallels those previously described with excitable and nonexcitable tissues.	Heparin	80-87	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	32-44
8470887-6	1993	The presence of either hirudin or heparin blocked the binding of thrombin to p-CBA-agarose but dansyl-arginine-N-(3-ethyl-1,5-pentanediyl)amide had no effect.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	65-73
8463256-2	1993	The kinetics of formation and dissociation of heparin-resistant transcription initiation complexes between Escherichia coli RNA polymerase and the rrnB P1 and P2 promoters from Bacillus subtilis were investigated using a gel retardation assay.	Heparin	46-53	replication initiation protein	Escherichia coli	152-161
8456753-1	1993	Selective thrombin inhibitors are a new class of antithrombotic drugs that, unlike heparin, can effectively inhibit clot-bound thrombin and escape neutralization by activated platelets.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	10-18
8470887-4	1993	Modification of thrombin with pyridoxal 5"-phosphate is thought to occur at the fibrinogen-binding site and the heparin-binding site.	Heparin	112-119	coagulation factor II, thrombin	Homo sapiens	16-24
8458437-0	1993	Assignment of the ligand binding site of the porcine estradiol receptor to the N-terminal 17 kDa part of domain E. Ligand-filled porcine estradiol receptor was adsorbed to heparin-Sepharose, from which a 26 kDa fragment was released by papain.	Heparin	172-179	estrogen receptor 1	Homo sapiens	53-71
8458437-0	1993	Assignment of the ligand binding site of the porcine estradiol receptor to the N-terminal 17 kDa part of domain E. Ligand-filled porcine estradiol receptor was adsorbed to heparin-Sepharose, from which a 26 kDa fragment was released by papain.	Heparin	172-179	estrogen receptor 1	Homo sapiens	137-155
7682054-7	1993	Aprotinin blocks contact activation of the kallikrein system during cardiopulmonary bypass and in synergy with heparin prevents thrombin formation through inhibition of the intrinsic clotting cascade.	Heparin	111-118	coagulation factor II, thrombin	Homo sapiens	128-136
8484904-3	1993	bFGF purification comprises three steps: extraction and chromatographies on S-Sepharose and heparin-Sepharose.	Heparin	92-99	fibroblast growth factor 2	Homo sapiens	0-4
8461335-7	1993	We conclude: (1) any VLDL particle can interact with heparin, which is consistent with the presence of apo E in all the subfractions, and (2) triacylglycerols in apo E-rich VLDL are less efficiently hydrolyzed by LPL than those in apo E-poor particles.	Heparin	53-60	apolipoprotein E	Homo sapiens	103-108
8314680-2	1993	Heparin-induced Extracorporeal LDL &lt; total cholesterol, triglycerides, fibrinogen &gt; Precipitation (H.E.L.P.)	Heparin	0-7	fibrinogen beta chain	Homo sapiens	74-84
7685753-6	1993	Both aerosol and intravenous heparin attenuated the antigen effects on sRL in a time-dependent fashion.	Heparin	29-36	sarcalumenin	Ovis aries	71-74
7685753-7	1993	Prolonging the lag time between pretreatment and antigen challenge decreased the inhibitory effect of aerosol heparin; delta sRL was 31 +/- 29, 99 +/- 38, 142 +/- 40, and 306 +/- 60% for &lt; or = 20-min, 6-h, 12-h, and 24-h pretreatment protocols, respectively.	Heparin	110-117	sarcalumenin	Ovis aries	125-128
7685753-8	1993	In contrast, prolonging the lag time increased the inhibitory effect of intravenous heparin: delta sRL was 246 +/- 64, 66 +/- 26, and 76 +/- 32% for &lt; or = 20 min, 1 h, and 6 h, respectively.	Heparin	84-91	sarcalumenin	Ovis aries	99-102
8469911-2	1993	Glycation of LDL at a molar ratio of 4 mol glucose mol-1 apoB, decreases affinity for heparin, as shown by heparin-agarose affinity chromatography since salt molarity needed for elution decreases from 550 mmol l-1 for control LDL (c-LDL) to 350 mmol l-1 for glycated LDL (glc-LDL).	Heparin	86-93	apolipoprotein B	Homo sapiens	57-61
8469911-2	1993	Glycation of LDL at a molar ratio of 4 mol glucose mol-1 apoB, decreases affinity for heparin, as shown by heparin-agarose affinity chromatography since salt molarity needed for elution decreases from 550 mmol l-1 for control LDL (c-LDL) to 350 mmol l-1 for glycated LDL (glc-LDL).	Heparin	107-114	apolipoprotein B	Homo sapiens	57-61
8508143-2	1993	When heparin was injected 5 min before an emulsion, the clearance of the emulsion in CCA-fed rats was significantly improved, and lipoproteins in the remnant and HDL fractions of plasma became enriched in apolipoprotein E.	Heparin	5-12	apolipoprotein E	Rattus norvegicus	205-221
8455594-8	1993	The Env/K-FGF fusion protein expressed by the MFS virus has retained all of the biological properties of native K-FGF, including secretion, mitogenic activity, heparin binding, and neutralization by anti-K-FGF antibodies.	Heparin	160-167	fibroblast growth factor 4	Homo sapiens	8-13
8394172-10	1993	Heparin was found to be the most potent inhibitor for both kinases with IC50s of 1.4 and 1.1 microM for beta ARK1 and beta ARK2, respectively.	Heparin	0-7	G protein-coupled receptor kinase 2	Bos taurus	104-113
8454611-15	1993	Heparin inhibited recombinant casein kinase I delta when phosvitin was the substrate, with half-maximal inhibition at 11.5 micrograms/ml.	Heparin	0-7	casein kinase 2 beta	Rattus norvegicus	57-66
8389063-5	1993	Myeloperoxidase (MPO) released by PMNL was found to be significantly HMW- and LMW-heparins dose-dependent.	Heparin	82-90	myeloperoxidase	Homo sapiens	0-15
8383007-0	1993	A new family of heparin-binding growth/differentiation factors: increased midkine expression in Wilms" tumor and other human carcinomas.	Heparin	16-23	midkine	Homo sapiens	74-81
8383007-1	1993	Midkine (MK) and heparin-binding growth-associated molecule/pleiotrophin form a new family of heparin-binding growth/differentiation factors.	Heparin	17-24	pleiotrophin	Homo sapiens	60-72
8389063-5	1993	Myeloperoxidase (MPO) released by PMNL was found to be significantly HMW- and LMW-heparins dose-dependent.	Heparin	82-90	myeloperoxidase	Homo sapiens	17-20
8444842-11	1993	Collectively, these data indicate that a hexasaccharide can be as effective as heparin as an antagonist of bFGF-mediated cell mitogenesis.	Heparin	79-86	fibroblast growth factor 2	Homo sapiens	107-111
8444841-8	1993	The data derived from the five assay systems demonstrated that heparin-derived hexa- and octasaccharides inhibited the interaction between cell surface heparan sulfate proteoglycan and bFGF (assays 1 and 2) and bFGF-induced proliferation of ACE cells (assay 3) but were unable to enhance the binding of bFGF to its high affinity receptor in vitro (assay 5) or to support bFGF-induced mitogenesis in ACE cells (assay 4).	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	185-189
8452552-3	1993	Heparin and dextran sulphate 5000 inhibited the proteolysis, suggesting that EC-SOD C sequestered by heparan sulphate proteoglycan in vivo is partially protected against proteolysis.	Heparin	0-7	superoxide dismutase 3	Homo sapiens	77-83
8444841-8	1993	The data derived from the five assay systems demonstrated that heparin-derived hexa- and octasaccharides inhibited the interaction between cell surface heparan sulfate proteoglycan and bFGF (assays 1 and 2) and bFGF-induced proliferation of ACE cells (assay 3) but were unable to enhance the binding of bFGF to its high affinity receptor in vitro (assay 5) or to support bFGF-induced mitogenesis in ACE cells (assay 4).	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	211-215
8444841-8	1993	The data derived from the five assay systems demonstrated that heparin-derived hexa- and octasaccharides inhibited the interaction between cell surface heparan sulfate proteoglycan and bFGF (assays 1 and 2) and bFGF-induced proliferation of ACE cells (assay 3) but were unable to enhance the binding of bFGF to its high affinity receptor in vitro (assay 5) or to support bFGF-induced mitogenesis in ACE cells (assay 4).	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	211-215
8444841-8	1993	The data derived from the five assay systems demonstrated that heparin-derived hexa- and octasaccharides inhibited the interaction between cell surface heparan sulfate proteoglycan and bFGF (assays 1 and 2) and bFGF-induced proliferation of ACE cells (assay 3) but were unable to enhance the binding of bFGF to its high affinity receptor in vitro (assay 5) or to support bFGF-induced mitogenesis in ACE cells (assay 4).	Heparin	63-70	fibroblast growth factor 2	Homo sapiens	211-215
8444842-1	1993	We demonstrated previously that heparin-derived hexasaccharides are the smallest fragments of the polysaccharide with comparable basic fibroblast growth factor (bFGF)-modulating activity in vitro (Ishihara, M., Tyrrell, D.J., Stauber, G.B., Brown, S., Cousens, L., and Stack, R.J. (1993) J. Biol.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	129-159
8444842-1	1993	We demonstrated previously that heparin-derived hexasaccharides are the smallest fragments of the polysaccharide with comparable basic fibroblast growth factor (bFGF)-modulating activity in vitro (Ishihara, M., Tyrrell, D.J., Stauber, G.B., Brown, S., Cousens, L., and Stack, R.J. (1993) J. Biol.	Heparin	32-39	fibroblast growth factor 2	Homo sapiens	161-165
8443388-8	1993	Unfractionated heparin, but not low molecular weight heparin, apparently binds to rvWF445-733 and counteracts the inhibitory effects of the vWF fragment in vitro on shear-aggregation and platelet-collagen adhesion.	Heparin	15-22	von Willebrand factor	Homo sapiens	83-86
8443144-10	1993	Heparin is known to be a vWF ligand, but did not appear as a competitor of vWF binding to the ECM, nor did heparan sulfate.	Heparin	0-7	von Willebrand factor	Homo sapiens	25-28
8452552-1	1993	The heparin-binding affinity of the tetrameric extracellular superoxide dismutase (EC-SOD) is a result of the cooperative effect of the heparin-binding domains of the subunits, located in the hydrophilic, strongly positively charged C-terminal ends.	Heparin	4-11	superoxide dismutase 3	Homo sapiens	83-89
8452552-1	1993	The heparin-binding affinity of the tetrameric extracellular superoxide dismutase (EC-SOD) is a result of the cooperative effect of the heparin-binding domains of the subunits, located in the hydrophilic, strongly positively charged C-terminal ends.	Heparin	136-143	superoxide dismutase 3	Homo sapiens	83-89
8452552-2	1993	EC-SOD C, the high-heparin-affinity type, exposed to immobilized trypsin and plasmin was found to rapidly lose its affinity for heparin, without any loss of enzymic activity or major change in molecular mass as judged by size-exclusion chromatography.	Heparin	19-26	superoxide dismutase 3	Homo sapiens	0-6
8452552-2	1993	EC-SOD C, the high-heparin-affinity type, exposed to immobilized trypsin and plasmin was found to rapidly lose its affinity for heparin, without any loss of enzymic activity or major change in molecular mass as judged by size-exclusion chromatography.	Heparin	128-135	superoxide dismutase 3	Homo sapiens	0-6
8452552-4	1993	The loss of heparin-affinity occurred with the stepwise formation of intermediates, and the pattern upon chromatography on heparin-Sepharose and subsequent immunoblotting was compatible with the notion that the changes are due to sequential truncations of heparin-binding domains from subunits composing the EC-SOD tetramers.	Heparin	12-19	superoxide dismutase 3	Homo sapiens	308-314
8452552-6	1993	The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.	Heparin	48-55	superoxide dismutase 3	Homo sapiens	74-80
8452552-6	1993	The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.	Heparin	48-55	superoxide dismutase 3	Homo sapiens	264-270
8452552-6	1993	The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.	Heparin	113-120	superoxide dismutase 3	Homo sapiens	74-80
8452552-6	1993	The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.	Heparin	113-120	superoxide dismutase 3	Homo sapiens	264-270
8452552-6	1993	The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.	Heparin	113-120	superoxide dismutase 3	Homo sapiens	74-80
8452552-6	1993	The findings show that the unique design of the heparin-binding domain of EC-SOD allows easy modification of the heparin-affinity by means of limited proteolysis, and suggest that such proteolysis is a major contributor to the heterogeneity in heparin-affinity of EC-SOD in mammalian plasma.	Heparin	113-120	superoxide dismutase 3	Homo sapiens	264-270
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	77-85
8388350-4	1993	Earlier studies had shown that low molecular weight (LMW) heparin preparations result in lower LPL activities in blood than do corresponding amounts of conventional heparin.	Heparin	58-65	lipoprotein lipase	Rattus norvegicus	95-98
8388350-5	1993	Studies with organ perfusion in rats show that the two types of heparin have similar ability to release the lipases from their binding sites in extrahepatic tissues, but that LMW heparin is less effective than conventional heparin in preventing rapid uptake and degradation of LPL by the liver.	Heparin	64-71	lipoprotein lipase	Rattus norvegicus	277-280
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	145-152	coagulation factor II, thrombin	Homo sapiens	104-112
8388350-6	1993	After injection of heparin the metabolism of triglyceride-rich lipoproteins is initially accelerated, presumably as a result of the high levels of circulating LPL.	Heparin	19-26	lipoprotein lipase	Rattus norvegicus	159-162
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	161-168	coagulation factor II, thrombin	Homo sapiens	77-85
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	161-168	coagulation factor II, thrombin	Homo sapiens	104-112
8388358-1	1993	Antithrombotic activities of low molecular weight heparins (LMWHs) in a venous stasis thrombosis model, when compared to unfractionated heparin (UFH), correlated better with anti-IIa activities and inhibition of thrombin generation than with anti-Xa activities.	Heparin	50-58	coagulation factor II, thrombin	Homo sapiens	212-220
8462732-8	1993	These observations suggest that the phospholipase activities are attributable to the action of HTGL, which, in the mouse appears to be a freely circulating enzyme, whereas for other species this enzyme only appears in the blood following administration of heparin.	Heparin	256-263	lipase C, hepatic type	Rattus norvegicus	95-99
8388358-1	1993	Antithrombotic activities of low molecular weight heparins (LMWHs) in a venous stasis thrombosis model, when compared to unfractionated heparin (UFH), correlated better with anti-IIa activities and inhibition of thrombin generation than with anti-Xa activities.	Heparin	50-57	coagulation factor II, thrombin	Homo sapiens	212-220
8388358-3	1993	Comparing activities in intrinsic and extrinsic systems, higher concentrations of heparins were required in vitro to inhibit intrinsic thrombin generation than extrinsic thrombin production; however, higher doses were required to prevent in vivo thrombotic events initiated via the extrinsic pathway.	Heparin	82-90	coagulation factor II, thrombin	Homo sapiens	135-143
8382699-5	1993	We report here the purification of CISP to apparent homogeneity with an overall yield of 43% using a combination of heparin-agarose and Mono-Q chromatographies.	Heparin	116-123	thrombospondin 2	Bos taurus	35-39
8472862-4	1993	The inclusion of 10 micrograms/ml heparin (a concentration that is reported to block bFGF binding to heparan sulfate proteoglycans) with increasing bFGF concentrations had no effect on the inhibition of 125I-hCG binding by low bFGF concentrations, but completely blocked the secondary increase in binding by higher bFGF concentrations.	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	85-89
8472862-4	1993	The inclusion of 10 micrograms/ml heparin (a concentration that is reported to block bFGF binding to heparan sulfate proteoglycans) with increasing bFGF concentrations had no effect on the inhibition of 125I-hCG binding by low bFGF concentrations, but completely blocked the secondary increase in binding by higher bFGF concentrations.	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	148-152
8472862-4	1993	The inclusion of 10 micrograms/ml heparin (a concentration that is reported to block bFGF binding to heparan sulfate proteoglycans) with increasing bFGF concentrations had no effect on the inhibition of 125I-hCG binding by low bFGF concentrations, but completely blocked the secondary increase in binding by higher bFGF concentrations.	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	148-152
8472862-4	1993	The inclusion of 10 micrograms/ml heparin (a concentration that is reported to block bFGF binding to heparan sulfate proteoglycans) with increasing bFGF concentrations had no effect on the inhibition of 125I-hCG binding by low bFGF concentrations, but completely blocked the secondary increase in binding by higher bFGF concentrations.	Heparin	34-41	fibroblast growth factor 2	Homo sapiens	148-152
8472862-6	1993	These studies suggest that receptor-mediated actions of bFGF (inhibition of hCG binding by low bFGF concentrations) on cultured immature Leydig cells are unaffected by heparin; however, the secondary increase in 125I-hCG binding observed with higher bFGF concentrations (mediated by bFGF binding to heparan sulfate proteoglycans) is blocked by heparin.	Heparin	344-351	fibroblast growth factor 2	Homo sapiens	56-60
8429040-6	1993	The second order rate constant (k2) for inhibition by antithrombin III without heparin was 3.7 x 10(5) M-1 min-1 for wild-type thrombin; rates for the mutant thrombins varied less than 2-fold.	Heparin	79-86	coagulation factor II, thrombin	Homo sapiens	58-66
8429040-7	1993	For inhibition by antithrombin III with heparin, the rate constant was 4.5 x 10(8) M-1 min-1 for wild-type thrombin with no significant differences between any of the recombinant thrombins.	Heparin	40-47	CD59 molecule (CD59 blood group)	Homo sapiens	87-92
8429040-7	1993	For inhibition by antithrombin III with heparin, the rate constant was 4.5 x 10(8) M-1 min-1 for wild-type thrombin with no significant differences between any of the recombinant thrombins.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	22-30
8429040-8	1993	In contrast, the rate constant for inhibition by heparin cofactor II without glycosaminoglycan was 4.3 x 10(4) M-1 min-1 for wild-type thrombin; rates were 10-fold slower for thrombin K52E and 2- to 3-fold slower for thrombins R68E and R70E.	Heparin	49-56	CD59 molecule (CD59 blood group)	Homo sapiens	115-120
8429040-8	1993	In contrast, the rate constant for inhibition by heparin cofactor II without glycosaminoglycan was 4.3 x 10(4) M-1 min-1 for wild-type thrombin; rates were 10-fold slower for thrombin K52E and 2- to 3-fold slower for thrombins R68E and R70E.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	135-143
8429040-8	1993	In contrast, the rate constant for inhibition by heparin cofactor II without glycosaminoglycan was 4.3 x 10(4) M-1 min-1 for wild-type thrombin; rates were 10-fold slower for thrombin K52E and 2- to 3-fold slower for thrombins R68E and R70E.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	175-183
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Heparin	83-90	coagulation factor II, thrombin	Homo sapiens	47-55
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Heparin	83-90	CD59 molecule (CD59 blood group)	Homo sapiens	132-137
8429040-12	1993	These results suggest that heparin cofactor II interacts with residue Lys-52 in the proposed S1" subsite and with residues Arg-68 and Arg-70 in the anion-binding exosite of thrombin, and that these interactions contribute to the molecular basis of heparin cofactor II specificity for thrombin.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	173-181
8429040-12	1993	These results suggest that heparin cofactor II interacts with residue Lys-52 in the proposed S1" subsite and with residues Arg-68 and Arg-70 in the anion-binding exosite of thrombin, and that these interactions contribute to the molecular basis of heparin cofactor II specificity for thrombin.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	284-292
8470059-6	1993	The short-lived quenching of thrombin generation after AT-III concentrate could be partially explained by the infusion of heparin, rather than by supranormal AT-III levels.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	29-37
7679097-3	1993	Heparin binding activity was mapped to two different tenascin segments: one comprising the fourth and fifth fibronectin type III domains, and to TNfbg, the fibrinogen-like terminal knob.	Heparin	0-7	fibronectin 1	Homo sapiens	108-119
8434804-6	1993	Urokinase began to enhance the effect of heparin on PTT values as a result of reducing fibrinogen levels.	Heparin	41-48	fibrinogen beta chain	Homo sapiens	87-97
8427958-7	1993	bFGF could be released from these sites by soluble heparin or phosphatidylinositol-specific phospholipase C. This study supports the role of bFGF as a stromal cell mitogen and stimulator of myelopoiesis.	Heparin	51-58	fibroblast growth factor 2	Homo sapiens	0-4
8427958-7	1993	bFGF could be released from these sites by soluble heparin or phosphatidylinositol-specific phospholipase C. This study supports the role of bFGF as a stromal cell mitogen and stimulator of myelopoiesis.	Heparin	51-58	fibroblast growth factor 2	Homo sapiens	141-145
8381106-1	1993	Extracellular-superoxide dismutase C (EC-SOD C) is a secretory tetrameric Cu- and Zn-containing glycoprotein which has high affinity for heparin and heparan sulfate.	Heparin	137-144	superoxide dismutase 3	Homo sapiens	38-44
8381106-3	1993	Recombinant EC-SOD truncation variants with reduced, T216, and without, T213, heparin affinity were found to be sequestered to a reduced extent and not at all, respectively, establishing the importance of the heparin affinity for this behaviour.	Heparin	78-85	superoxide dismutase 3	Homo sapiens	12-18
8381106-3	1993	Recombinant EC-SOD truncation variants with reduced, T216, and without, T213, heparin affinity were found to be sequestered to a reduced extent and not at all, respectively, establishing the importance of the heparin affinity for this behaviour.	Heparin	209-216	superoxide dismutase 3	Homo sapiens	12-18
8487654-0	1993	Effect of heparin on insulin-glucose interactions measured by the minimal model technique: implications for reproducibility using this method.	Heparin	10-17	insulin	Homo sapiens	21-28
8470044-4	1993	We find that in the rabbit the heparin-releasable pool of TFPI activity, as measured in a capacity assay, may be smaller relative to the plasma pool than in humans; that the platelet pool of TFPI activity is comparable to that of humans; and that rabbit TFPI, unlike human TFPI, has the same apparent molecular mass in all vascular pools.	Heparin	31-38	tissue factor pathway inhibitor	Oryctolagus cuniculus	58-62
8440695-6	1993	The PLTP used was purified to homogeneity from human plasma using ultracentrifugation and a combination of hydrophobic, cation-exchange, heparin-Sepharose-, anion-exchange, and gel filtration chromatographies.	Heparin	137-144	phospholipid transfer protein	Homo sapiens	4-8
8429005-0	1993	Site-directed mutagenesis of a putative heparin binding domain of avian lipoprotein lipase.	Heparin	40-47	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	72-90
8429005-1	1993	Lipoprotein lipase (LPL) binds to heparin and heparan sulfate proteoglycans.	Heparin	34-41	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	0-18
8429005-1	1993	Lipoprotein lipase (LPL) binds to heparin and heparan sulfate proteoglycans.	Heparin	34-41	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	20-23
8429005-2	1993	We have employed site-directed mutagenesis to dissect one of the proposed heparin binding domains of avian LPL, which contains the sequence Arg-Lys-Asn-Arg (amino acids 281-284).	Heparin	74-81	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	107-110
8429005-5	1993	In general, the LPL mutants with a decrease in regional positive charge showed a decrease in affinity for heparin and heparan sulfate proteoglycans.	Heparin	106-113	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	16-19
8429005-7	1993	On a heparin-Sepharose column, LPL 5G eluted at 0.96 M NaCl compared with 1.35 M for wild-type LPL.	Heparin	5-12	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	31-34
8429005-11	1993	In conclusion, the region of avian LPL between Arg281 and Arg284 does appear to be involved in heparin-binding; however, additional regions must be involved since binding was not completely abolished.	Heparin	95-102	LOW QUALITY PROTEIN: lipoprotein lipase	Cricetulus griseus	35-38
8429008-3	1993	Quick I, Quick II, and alpha-thrombin were eluted at the same salt concentration from heparin-Sepharose suggesting that the putative heparin-binding site (also termed anion binding exosite-II) is functional.	Heparin	86-93	coagulation factor II, thrombin	Homo sapiens	29-37
8429008-3	1993	Quick I, Quick II, and alpha-thrombin were eluted at the same salt concentration from heparin-Sepharose suggesting that the putative heparin-binding site (also termed anion binding exosite-II) is functional.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	29-37
8431448-6	1993	Heparin, at concentrations between 0.1 and 1 microgram/mL, significantly promoted thrombin inhibition by PAI-1 as well as SDS-stable complex formation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	82-90
8428972-8	1993	Heparin binding properties were preserved with deletion of up to 28 amino-terminal residues of the mature KGF but lost by the deletion of an additional 10 residues.	Heparin	0-7	fibroblast growth factor 7	Homo sapiens	106-109
16695966-1	1993	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	49-56	tumor necrosis factor	Homo sapiens	18-39
16695966-1	1993	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	49-56	tumor necrosis factor	Homo sapiens	41-44
16695966-1	1993	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	113-120	tumor necrosis factor	Homo sapiens	18-39
16695966-1	1993	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	113-120	tumor necrosis factor	Homo sapiens	88-91
7679138-12	1993	Therefore, beta-VLDL were enriched with isolated LPL or heparin was injected simultaneously with beta-VLDL to increase the concentration of endogenous LPL bound to beta-VLDL.	Heparin	56-63	lipoprotein lipase	Rattus norvegicus	151-154
8381453-0	1993	Heparin releases newly synthesized cell surface-associated apolipoprotein E from HepG2 cells.	Heparin	0-7	apolipoprotein E	Homo sapiens	59-75
8381453-1	1993	Heparin significantly increased the amount of newly synthesized apolipoprotein E (apoE) released by HepG2 cells.	Heparin	0-7	apolipoprotein E	Homo sapiens	64-80
8459200-2	1993	Immunoreactive-bFGF (ir-bFGF) bound to heparin-Sepharose affinity columns eluted with 1.8-2.0 mol NaCl/l and had a molecular weight of approximately 17,000.	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	15-19
8381453-1	1993	Heparin significantly increased the amount of newly synthesized apolipoprotein E (apoE) released by HepG2 cells.	Heparin	0-7	apolipoprotein E	Homo sapiens	82-86
8429258-2	1993	We have used measurements of heparin-releasable LPL activity, immunohistochemistry, in situ hybridization, and Northern analysis to more fully characterize the location of LPL within the entire central nervous system (CNS) of the rat.	Heparin	29-36	lipoprotein lipase	Rattus norvegicus	48-51
8381453-2	1993	Culturing cells in the presence of 10 micrograms/ml of heparin for 2-6 days caused a 1.3-fold (day 2) to 3-fold (day 6) increase of extracellular apoE without affecting the total amount of apoE synthesized by the cells.	Heparin	55-62	apolipoprotein E	Homo sapiens	146-150
8381453-2	1993	Culturing cells in the presence of 10 micrograms/ml of heparin for 2-6 days caused a 1.3-fold (day 2) to 3-fold (day 6) increase of extracellular apoE without affecting the total amount of apoE synthesized by the cells.	Heparin	55-62	apolipoprotein E	Homo sapiens	189-193
8381453-4	1993	Surprisingly, short-term treatment with heparin (15-30 min) also increased extracellular apoE by 2- to 3-fold.	Heparin	40-47	apolipoprotein E	Homo sapiens	89-93
8381453-5	1993	In this situation, heparin exerted its effect on apoE post-translationally.	Heparin	19-26	apolipoprotein E	Homo sapiens	49-53
8381453-8	1993	Removal of cell surface-associated GAGs by culturing cells in 4-methylumbelliferyl-beta-D-xyloside ablated the effect of heparin on apoE.	Heparin	121-128	apolipoprotein E	Homo sapiens	132-136
8381453-10	1993	The results provide evidence that a heparin-releasable pool of newly synthesized apoE is associated with cell surface GAGs that resemble heparin and/or heparan sulfate.	Heparin	36-43	apolipoprotein E	Homo sapiens	81-85
8381453-10	1993	The results provide evidence that a heparin-releasable pool of newly synthesized apoE is associated with cell surface GAGs that resemble heparin and/or heparan sulfate.	Heparin	137-144	apolipoprotein E	Homo sapiens	81-85
8381846-2	1993	Superoxide anion generation in fMLP-stimulated PMN was dose-dependently reduced by heparin and oligo-heparin, while DS and oligo-DS lacked inhibitory activity.	Heparin	83-90	formyl peptide receptor 1	Homo sapiens	31-35
8381846-3	1993	FMLP-stimulated PMN adhesion to endothelial cells was reduced to a similar extent by both heparin and oligo-heparin, but not by DS and oligo-DS.	Heparin	90-97	formyl peptide receptor 1	Homo sapiens	0-4
8381846-5	1993	Heparin and oligo-heparin also inhibited the homotypic aggregation of fMLP-stimulated PMN.	Heparin	0-7	formyl peptide receptor 1	Homo sapiens	70-74
8459200-2	1993	Immunoreactive-bFGF (ir-bFGF) bound to heparin-Sepharose affinity columns eluted with 1.8-2.0 mol NaCl/l and had a molecular weight of approximately 17,000.	Heparin	39-46	fibroblast growth factor 2	Homo sapiens	24-28
8384381-0	1993	Comparative inhibition of extrinsic and intrinsic thrombin generation by standard heparin, a low molecular weight heparin and the synthetic ATIII-binding pentasaccharide.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	50-58
8441232-7	1993	Furthermore, heparin treatment markedly inhibited the mesangial matrix expansion for a variety of ECM proteins, including laminin, type I and IV collagen, fibronectin and entactin.	Heparin	13-20	nidogen 1	Rattus norvegicus	171-179
7678885-7	1993	These results support the promising angiogenic effect of ECGF-heparin in previously irradiated surgical wounds.	Heparin	62-69	fibroblast growth factor 1	Homo sapiens	57-61
7682732-2	1993	Unlike the intravenous injection of heparin which induces fast short-time inactivation of all clotting factors, single intratracheal injection of heparin inactivated the intrinsic pathway of thrombin generation.	Heparin	146-153	coagulation factor II	Rattus norvegicus	191-199
8384381-1	1993	The inhibiting effect of standard heparin, CY216 and the ATIII-binding synthetic pentasaccharide on extrinsic and intrinsic thrombin generation were quantified by evaluating the decrease of the total amount of active thrombin appearing in plasma after triggering coagulation.	Heparin	34-41	coagulation factor II, thrombin	Homo sapiens	124-132
8446937-0	1993	Effect of heparin on thrombin inhibition in the microcirculation.	Heparin	10-17	coagulation factor II	Rattus norvegicus	21-29
8422249-1	1993	In order to improve the therapeutic effectiveness of human Cu,Zn superoxide dismutase (HSOD) by targeting it to cell surfaces and increasing its circulatory half-life, we have designed and expressed a heparin-binding derivative of HSOD.	Heparin	201-208	superoxide dismutase 1	Homo sapiens	59-85
8419361-8	1993	Addition of heparin together with TNF resulted in release of type II PLA2 in the medium.	Heparin	12-19	phospholipase A2 group IB	Homo sapiens	69-73
8419361-11	1993	This binding was blocked by either heparin or a monoclonal antibody recognizing the heparin-binding domain of type II PLA2.	Heparin	35-42	phospholipase A2 group IB	Homo sapiens	118-122
8419361-11	1993	This binding was blocked by either heparin or a monoclonal antibody recognizing the heparin-binding domain of type II PLA2.	Heparin	84-91	phospholipase A2 group IB	Homo sapiens	118-122
8431762-11	1993	Human neuroblastoma proteoglycans may bind to the-Alzheimer amyloid A4 peptide in a region with a heparin binding consensus sequence [VHHQKL] which also contains the cleavage site of the beta-amyloid precursor protein.	Heparin	98-105	amyloid beta precursor protein	Homo sapiens	187-217
7678446-7	1993	MIP-1 beta was immobilized by binding to proteoglycan: a conjugate of heparin with bovine serum albumin and cellular proteoglycan CD44 were both effective.	Heparin	70-77	albumin	Homo sapiens	90-103
8380057-3	1993	This molecule was identified as bFGF on the basis of its molecular weight, its affinity for heparin, and its capacity to induce plasminogen activator production in cultured endothelial GM 7373 cells.	Heparin	92-99	fibroblast growth factor 2	Bos taurus	32-36
8446937-6	1993	At a subsequent recirculation with a heparin/thrombin mixture the loss of thrombin was decreased to the control level, as seen when recirculation with thrombin alone was performed.	Heparin	37-44	coagulation factor II	Rattus norvegicus	74-82
8446937-6	1993	At a subsequent recirculation with a heparin/thrombin mixture the loss of thrombin was decreased to the control level, as seen when recirculation with thrombin alone was performed.	Heparin	37-44	coagulation factor II	Rattus norvegicus	74-82
8446937-7	1993	It is concluded that disappearance of thrombin enzymatic activity from a solution when recirculated through the microcirculation can be considerably increased if recirculated together with heparin, which probably reacts with endogenous antithrombin III on the vessel wall.	Heparin	189-196	coagulation factor II	Rattus norvegicus	38-46
8439679-9	1993	Antithrombin III levels changed from 102 +/- 26% to 91 +/- 7% for heparin, compared with 123 +/- 12% to 118 +/- 12% for phospholipid.	Heparin	66-73	serpin family C member 1	Bos taurus	0-16
7514054-5	1993	Transforming growth factor beta 1 inhibited DNA synthesis (ID50 = 3.6 x 10(-10) mol/l) and so did heparin (1.4 x 10(-6) mol/l) and low molecular weight heparin (2.9 x 10(-6) mol/l).	Heparin	98-105	transforming growth factor beta 1	Homo sapiens	0-33
7514054-5	1993	Transforming growth factor beta 1 inhibited DNA synthesis (ID50 = 3.6 x 10(-10) mol/l) and so did heparin (1.4 x 10(-6) mol/l) and low molecular weight heparin (2.9 x 10(-6) mol/l).	Heparin	152-159	transforming growth factor beta 1	Homo sapiens	0-33
8154338-6	1993	Impairment by fibrin of thrombin inhibition by antithrombin III may account in part for the inability of unfractionated heparin to prevent post-operative deep vein thrombosis in up to 20% of patients who undergo major elective orthopaedic surgery, and may also explain the need for oral anticoagulants after unfractionated and low molecular weight heparins are used to initiate the treatment of established deep vein thrombi.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	24-32
8154338-6	1993	Impairment by fibrin of thrombin inhibition by antithrombin III may account in part for the inability of unfractionated heparin to prevent post-operative deep vein thrombosis in up to 20% of patients who undergo major elective orthopaedic surgery, and may also explain the need for oral anticoagulants after unfractionated and low molecular weight heparins are used to initiate the treatment of established deep vein thrombi.	Heparin	348-356	coagulation factor II, thrombin	Homo sapiens	24-32
7678726-1	1993	Acidic fibroblast growth factor (aFGF) is markedly stabilized by heparin.	Heparin	65-72	fibroblast growth factor 1	Homo sapiens	0-31
7678726-1	1993	Acidic fibroblast growth factor (aFGF) is markedly stabilized by heparin.	Heparin	65-72	fibroblast growth factor 1	Homo sapiens	33-37
7678726-8	1993	A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation.	Heparin	30-37	fibroblast growth factor 1	Homo sapiens	93-97
7678726-8	1993	A tetrasaccharide fragment of heparin is the smallest unit of heparin capable of stabilizing aFGF against thermal denaturation.	Heparin	62-69	fibroblast growth factor 1	Homo sapiens	93-97
7678726-10	1993	These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF.	Heparin	165-172	fibroblast growth factor 1	Homo sapiens	63-67
7678726-10	1993	These results are discussed in the context of a model of human aFGF based on the X-ray crystal structure of the bovine protein and previous studies by others of the heparin binding site of both acidic and basic FGF.	Heparin	165-172	fibroblast growth factor 1	Homo sapiens	64-67
7509996-0	1993	Effect of heparin on endothelin-1 production by cultured human endothelial cells.	Heparin	10-17	endothelin 1	Homo sapiens	21-33
7688519-5	1993	However, if heparin was present during the chase, readily detectable amounts (about 10-20% of total) of aFGF were found in the medium during the 15 hr chase.	Heparin	12-19	fibroblast growth factor 1	Homo sapiens	104-108
7688519-8	1993	Further analyses indicated that heparin both stabilized the protein from degradation and prevented the binding of released aFGF to extracellular heparan-sulfate proteoglycans.	Heparin	32-39	fibroblast growth factor 1	Homo sapiens	123-127
7688519-9	1993	Thus, both factors contributed to the increased recovery of aFGF in the presence of heparin.	Heparin	84-91	fibroblast growth factor 1	Homo sapiens	60-64
8148155-6	1993	Infection of Sf158 insect cells with recombinant baculoviruses specific for the two forms showed, that both, PlGF-1 and PlGF-2 are secreted efficiently into the supernatant and PlGF-2 can bind with high affinity to heparin.	Heparin	215-222	placental growth factor	Homo sapiens	109-113
8148155-6	1993	Infection of Sf158 insect cells with recombinant baculoviruses specific for the two forms showed, that both, PlGF-1 and PlGF-2 are secreted efficiently into the supernatant and PlGF-2 can bind with high affinity to heparin.	Heparin	215-222	placental growth factor	Homo sapiens	120-126
8148155-6	1993	Infection of Sf158 insect cells with recombinant baculoviruses specific for the two forms showed, that both, PlGF-1 and PlGF-2 are secreted efficiently into the supernatant and PlGF-2 can bind with high affinity to heparin.	Heparin	215-222	placental growth factor	Homo sapiens	177-183
8148156-7	1993	The uPA-inducing activity of M1Q-bFGF was fully restored by the presence of soluble heparin in the culture medium.	Heparin	84-91	plasminogen activator, urokinase	Homo sapiens	4-7
8148156-7	1993	The uPA-inducing activity of M1Q-bFGF was fully restored by the presence of soluble heparin in the culture medium.	Heparin	84-91	fibroblast growth factor 2	Homo sapiens	33-37
8419401-9	1993	This was the case also when 125I-bFGF was internalized in the presence of soluble heparin, suggesting that the complexes bFGF-cell surface glycosaminoglycan and bFGF-soluble heparin are maintained during the internalization of the growth factor.	Heparin	174-181	fibroblast growth factor 2	Bos taurus	33-37
8419401-10	1993	Moreover, the capacity of soluble heparin to inhibit the mitogenic activity of bFGF also when added to cell cultures several hours after the growth factor indicates that the requirement for a prolonged interaction of bFGF with GM 7373 cells in order to induce cell proliferation might be related to the late internalization of the growth factor via low affinity sites.	Heparin	34-41	fibroblast growth factor 2	Bos taurus	79-83
8419401-10	1993	Moreover, the capacity of soluble heparin to inhibit the mitogenic activity of bFGF also when added to cell cultures several hours after the growth factor indicates that the requirement for a prolonged interaction of bFGF with GM 7373 cells in order to induce cell proliferation might be related to the late internalization of the growth factor via low affinity sites.	Heparin	34-41	fibroblast growth factor 2	Bos taurus	217-221
8261475-2	1993	Conjunctive pharmacological agents such as heparin appear to play an important role in maintaining vessel patency, particularly following tissue plasminogen activator (t-PA) administration.	Heparin	43-50	plasminogen activator, tissue type	Homo sapiens	138-172
8200184-4	1993	When the latter phenomenon was corrected through the simultaneous administration of exogenous triglycerides and heparin, a reascension in C-peptide plasma concentration was observed despite persistent hyperinsulinemia.	Heparin	112-119	insulin	Homo sapiens	138-147
8261088-7	1993	To investigate whether the L2/HNK-1 carbohydrate and heparin use the same or different binding sites on laminin, adhesion of cells to laminin was determined in the presence of heparin and Fab fragments of a monoclonal L2 antibody, which gave an additive value of inhibition as compared to the inhibition caused by the single compounds.	Heparin	53-60	laminin, beta 2 (laminin S)	Gallus gallus	104-111
8261088-8	1993	This result, as well as studies of the binding of the L2/HNK-1 glycolipids to laminin in the presence of heparin, indicates that the L2/HNK-1 carbohydrate and heparin are implicated in different aspects of neural cell adhesion to laminin.	Heparin	105-112	laminin, beta 2 (laminin S)	Gallus gallus	78-85
8261088-8	1993	This result, as well as studies of the binding of the L2/HNK-1 glycolipids to laminin in the presence of heparin, indicates that the L2/HNK-1 carbohydrate and heparin are implicated in different aspects of neural cell adhesion to laminin.	Heparin	159-166	laminin, beta 2 (laminin S)	Gallus gallus	78-85
8261088-8	1993	This result, as well as studies of the binding of the L2/HNK-1 glycolipids to laminin in the presence of heparin, indicates that the L2/HNK-1 carbohydrate and heparin are implicated in different aspects of neural cell adhesion to laminin.	Heparin	159-166	laminin, beta 2 (laminin S)	Gallus gallus	230-237
8419396-5	1993	Heparin also inhibited the binding of bFGF to low affinity binding sites to the same degree as DS-4152, but had little effect on the binding of bFGF to high affinity sites and no effects on bFGF-induced endothelial cell growth.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	38-42
8419401-7	1993	This hypothesis was supported by the following experimental evidence: 1) soluble heparin inhibited the prolonged internalization of 125I-bFGF and its binding to low affinity sites with the same potency; 2) treatment of GM 7373 cells with heparinase, which removes most of the low affinity sites, also inhibited the prolonged internalization of 125I-bFGF.	Heparin	81-88	fibroblast growth factor 2	Bos taurus	137-141
8419401-7	1993	This hypothesis was supported by the following experimental evidence: 1) soluble heparin inhibited the prolonged internalization of 125I-bFGF and its binding to low affinity sites with the same potency; 2) treatment of GM 7373 cells with heparinase, which removes most of the low affinity sites, also inhibited the prolonged internalization of 125I-bFGF.	Heparin	81-88	fibroblast growth factor 2	Bos taurus	349-353
8419401-9	1993	This was the case also when 125I-bFGF was internalized in the presence of soluble heparin, suggesting that the complexes bFGF-cell surface glycosaminoglycan and bFGF-soluble heparin are maintained during the internalization of the growth factor.	Heparin	82-89	fibroblast growth factor 2	Bos taurus	121-125
8419401-9	1993	This was the case also when 125I-bFGF was internalized in the presence of soluble heparin, suggesting that the complexes bFGF-cell surface glycosaminoglycan and bFGF-soluble heparin are maintained during the internalization of the growth factor.	Heparin	82-89	fibroblast growth factor 2	Bos taurus	121-125
7509996-2	1993	This study was designed to examine the effect of heparin on vasoconstrictor endothelin-1 (ET-1) production by cultured human umbilical vein endothelial cells (HUVECs).	Heparin	49-56	endothelin 1	Homo sapiens	76-88
7509996-2	1993	This study was designed to examine the effect of heparin on vasoconstrictor endothelin-1 (ET-1) production by cultured human umbilical vein endothelial cells (HUVECs).	Heparin	49-56	endothelin 1	Homo sapiens	90-94
7509996-6	1993	Heparin suppressed both basal and thrombin-stimulated ET-1 secretion and its mRNA expression in a dose-dependent manner.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	34-42
7509996-6	1993	Heparin suppressed both basal and thrombin-stimulated ET-1 secretion and its mRNA expression in a dose-dependent manner.	Heparin	0-7	endothelin 1	Homo sapiens	54-58
7509996-9	1993	The production of cGMP stimulated by thrombin was significantly enhanced by heparin, but not in the presence of L-NMMA (10(-5) M).	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	37-45
7509996-10	1993	Heparin may suppress vasoconstrictor ET-1 production mediated by the enhancement of endothelium-derived nitric oxide in HUVECs.	Heparin	0-7	endothelin 1	Homo sapiens	37-41
8383273-0	1993	Release of lipoprotein lipase from cardiac myocytes by low-molecular weight heparin.	Heparin	76-83	lipoprotein lipase	Rattus norvegicus	11-29
8418384-11	1993	These studies indicated that ALL cells adhere to soluble fibronectin predominantly through the VLA-5 molecule (blockable with the PHM-2 antibody and a peptide containing the RGD sequence) although binding mediated by VLA-4 was also apparent in some experiments (blockable by a 40 kDa fragment containing the heparin-binding domain of FN and inhibitory antibodies).	Heparin	308-315	fibronectin 1	Homo sapiens	57-68
8121125-5	1993	Fibrinogen level increased from 3.34 +/- 0.15 to 3.95 +/- 0.18 g/l, p &lt; 0.001, and from 3.36 +/- 0.17 to 3.94 +/- 0.17 g/l p = 0.003 in aspirin and heparin groups, respectively.	Heparin	151-158	fibrinogen beta chain	Homo sapiens	0-10
8416465-0	1993	The effect of prophylactic heparin treatment on enhanced thrombin generation in pregnancy.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	57-65
8395725-0	1993	Effects of unfractionated and low molecular weight heparin on platelet-induced thrombin formation time and platelet adhesion.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	79-87
8362268-3	1993	In the plasma-based assays, heparin exhibited strong inhibition in both thrombin and Factor Xa-based assays, whereas pentasaccharide was only active in Factor Xa-based assays and lactobionic acid was only active in thrombin-based assays.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	72-80
8443592-2	1993	Baculoviral-insect cell-derived recombinant FGF-R1 was phosphorylated and fragmented with trypsin while immobilized on heparin-agarose beads.	Heparin	119-126	fibroblast growth factor receptor 1	Homo sapiens	44-50
8362268-4	1993	In the AT III supplemented systems, heparin was able to inhibit strongly both Factor Xa and thrombin, while pentasaccharide could only inhibit Factor Xa.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	92-100
1482688-2	1992	This cDNA encodes a peptide of 93 amino acids and contains a heparin binding domain similar to histone 2-B.	Heparin	61-68	histone cluster 1, H2bg	Rattus norvegicus	95-106
8465268-17	1993	Kringle F2 binds to thrombin at the heparin binding site through charge complementarity; a conformational change appears to occur on binding.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	20-28
8333205-3	1993	By applying heparin-induced extracorporeal LDL &lt; cholesterol, triglycerides, fibrinogen &gt; precipitation (H.E.L.P.	Heparin	12-19	fibrinogen beta chain	Homo sapiens	80-90
8367976-2	1993	To evaluate the association between fibrinogen and blood sedimentation rate (BSR) 40 patients suffering from cerebral multi-infarct disease underwent a single heparin-induced extracorporeal LDL &lt; fibrinogen &gt; precipitation (HELP).	Heparin	159-166	fibrinogen beta chain	Homo sapiens	199-209
1464614-8	1992	Heparin, heparan sulfate, and heparinase all induced the release of VEGF165 and VEGF189, suggesting heparin-containing proteoglycans as candidate VEGF-binding sites.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	68-72
1366018-6	1992	Full activation requires longer heparin chains in order to stabilize the ternary complex between antithrombin and thrombin.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	101-109
1335242-3	1992	Carboxymethylated HBNF and MK, which retain affinity for heparin-Sepharose, do not exhibit anti-viral activities.	Heparin	57-64	pleiotrophin	Homo sapiens	18-22
1447186-1	1992	Heparin, in Langmuirian fashion, binds stoichiometrically with high affinity, Kd approximately 100 nM, to both fibrinogen and fibrin adsorbed as monomolecular films to lecithin-coated, microscopic, polystyrene-divinylbenzene beads.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	111-121
1287886-6	1992	125I-vWF binding to ristocetin- and botrocetin-treated platelets, to heparin and to sulfatides as well as 125I-botrocetin binding to vWF was competitively inhibited by ATA.	Heparin	69-76	von Willebrand factor	Homo sapiens	5-8
1280262-10	1992	Heparin or HS glycosaminoglycans are a prerequisite for the FGF receptor encoded by flg gene to bind basic FGF (Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell 64, 841-848).	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	60-63
1457401-1	1992	Pleiotrophin (PTN), midkine (MK), and retinoic acid-induced heparin-binding (RI-HB) protein are members of a recently discovered family of developmentally regulated cytokines.	Heparin	60-67	pleiotrophin	Homo sapiens	0-12
1457401-1	1992	Pleiotrophin (PTN), midkine (MK), and retinoic acid-induced heparin-binding (RI-HB) protein are members of a recently discovered family of developmentally regulated cytokines.	Heparin	60-67	pleiotrophin	Homo sapiens	14-17
1309058-3	1992	Although heparin and aspirin may attenuate ongoing thrombin and thromboxane generation, respectively, a relatively high percentage (10-20%) of patients treated with heparin and aspirin still have complications associated with thrombolysis.	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	51-59
1477980-9	1992	The serum EC-SOD in Group I is heterogeneous with regard to affinity for heparin-Sepharose and could be separated into three approximately equal fractions, whereas the EC-SOD in Group II is mainly one fraction with a high affinity for the column.	Heparin	73-80	superoxide dismutase 3	Homo sapiens	10-16
1282813-0	1992	Effect of cytochrome C oxidase and polyanions on the alkaline transition of ferricytochrome C. Application of heparin, polyadenylate, polyglutamate and polygalacturonate resulted in changes in the electron absorption spectrum of cytochrome c that resembled those after cytochrome c oxidase application at neutral pH.	Heparin	110-117	cytochrome c, somatic	Homo sapiens	10-22
1282813-0	1992	Effect of cytochrome C oxidase and polyanions on the alkaline transition of ferricytochrome C. Application of heparin, polyadenylate, polyglutamate and polygalacturonate resulted in changes in the electron absorption spectrum of cytochrome c that resembled those after cytochrome c oxidase application at neutral pH.	Heparin	110-117	cytochrome c, somatic	Homo sapiens	229-241
1282813-0	1992	Effect of cytochrome C oxidase and polyanions on the alkaline transition of ferricytochrome C. Application of heparin, polyadenylate, polyglutamate and polygalacturonate resulted in changes in the electron absorption spectrum of cytochrome c that resembled those after cytochrome c oxidase application at neutral pH.	Heparin	110-117	cytochrome c, somatic	Homo sapiens	269-281
1478067-0	1992	Heparin-binding properties of lactoferrin and lysozyme.	Heparin	0-7	lysozyme	Homo sapiens	46-54
1478067-5	1992	The metal ions Cu2+, Zn2+, Fe2+ and Fe3+ inhibited heparin binding, with half-maximal inhibition of binding to lactoferrin occurring between 600 microM and 1 mM and for lysozyme between 500 and 800 microM.	Heparin	51-58	lysozyme	Homo sapiens	169-177
1469294-5	1992	Fetal and neonatal melanocytes showed a concentration-dependent attachment to two proteolytically derived fragments of the FN molecule: a 75-kD fragment, which contains the central cell-binding domain, and 33/66-kD fragments of the FN molecule, which encompass the heparin-binding domains V and VI.	Heparin	265-272	fibronectin 1	Homo sapiens	123-125
1479287-4	1992	LPL catalytic activity from the heparin-releasable fraction of adipocytes was inhibited by more than 70%, with similar decreases in LPL mass, when cells were cultured for 24 h in the presence of either tunicamycin or castanospermine.	Heparin	32-39	lipoprotein lipase	Rattus norvegicus	0-3
1479287-4	1992	LPL catalytic activity from the heparin-releasable fraction of adipocytes was inhibited by more than 70%, with similar decreases in LPL mass, when cells were cultured for 24 h in the presence of either tunicamycin or castanospermine.	Heparin	32-39	lipoprotein lipase	Rattus norvegicus	132-135
1460862-10	1992	In vivo, the local application of tumor necrosis factor-alpha resulted in formation of a typical granulation tissue: immunofluorescence showed that accumulated fibroblastic cells express alpha-smooth muscle actin only in the presence of heparin derivatives.	Heparin	237-244	tumor necrosis factor	Homo sapiens	34-61
1477980-11	1992	The high EC-SOD level in sera from some individuals may reflect the excessive stimulation of EC-SOD synthesis in vivo or the growth of selected cells in vivo, because EC-SOD is known to be expressed by a few cell types in vivo as a high-heparin-affinity subtype.	Heparin	237-244	superoxide dismutase 3	Homo sapiens	9-15
1279186-3	1992	We have shown that the heparinoid pentosan polysulfate (PPS) can block growth of subcutaneous human tumor xenografts in nude mice and angiogenesis induced by the heparin-binding, Kaposi"s sarcoma-derived fibroblast growth factor (K-FGF).	Heparin	23-30	fibroblast growth factor 4	Mus musculus	179-228
1444441-16	1992	By heparin affinity chromatography, it was shown that thrombin-nexin complexes dissociably associate with thrombospondin prior to formation of disulfide-linked complexes.	Heparin	3-10	coagulation factor II, thrombin	Homo sapiens	54-62
1279186-3	1992	We have shown that the heparinoid pentosan polysulfate (PPS) can block growth of subcutaneous human tumor xenografts in nude mice and angiogenesis induced by the heparin-binding, Kaposi"s sarcoma-derived fibroblast growth factor (K-FGF).	Heparin	23-30	fibroblast growth factor 4	Mus musculus	230-235
1429568-2	1992	Internalization of bFGF was completely blocked by the addition of 10 micrograms/ml heparin in the parental CHO cells but only partially inhibited in cells expressing transfected FGF receptors.	Heparin	83-90	fibroblast growth factor 2	Bos taurus	19-23
1279690-6	1992	The form of FGF-1 exposed by ammonium sulfate fractionation is similar in size to cytosolic FGF-1 and can bind and be eluted from immobilized heparin similarly to the recombinant human FGF-1 polypeptide.	Heparin	142-149	fibroblast growth factor 1	Homo sapiens	12-17
1280862-8	1992	Unexpectedly, after heparin the AUC of t-PA activity was 49% larger (range +19 to +245%) than after Org 10172 (p &lt; 0.05).	Heparin	20-27	plasminogen activator, tissue type	Homo sapiens	39-43
1429568-3	1992	Bovine aortic endothelial cells also exhibit heparin-sensitive and heparin-resistant internalization of bFGF.	Heparin	45-52	fibroblast growth factor 2	Bos taurus	104-108
1429568-3	1992	Bovine aortic endothelial cells also exhibit heparin-sensitive and heparin-resistant internalization of bFGF.	Heparin	67-74	fibroblast growth factor 2	Bos taurus	104-108
1429568-4	1992	The internalization of bFGF through the heparin-resistant pathway in CHO cells was efficiently competed by addition of unlabeled bFGF, was proportional to the number of receptors expressed, and approached saturation, suggesting that the heparin-resistant internalization was due to high affinity receptors.	Heparin	40-47	fibroblast growth factor 2	Bos taurus	23-27
1429568-4	1992	The internalization of bFGF through the heparin-resistant pathway in CHO cells was efficiently competed by addition of unlabeled bFGF, was proportional to the number of receptors expressed, and approached saturation, suggesting that the heparin-resistant internalization was due to high affinity receptors.	Heparin	40-47	fibroblast growth factor 2	Bos taurus	129-133
1429568-4	1992	The internalization of bFGF through the heparin-resistant pathway in CHO cells was efficiently competed by addition of unlabeled bFGF, was proportional to the number of receptors expressed, and approached saturation, suggesting that the heparin-resistant internalization was due to high affinity receptors.	Heparin	237-244	fibroblast growth factor 2	Bos taurus	23-27
1429568-4	1992	The internalization of bFGF through the heparin-resistant pathway in CHO cells was efficiently competed by addition of unlabeled bFGF, was proportional to the number of receptors expressed, and approached saturation, suggesting that the heparin-resistant internalization was due to high affinity receptors.	Heparin	237-244	fibroblast growth factor 2	Bos taurus	129-133
1429568-5	1992	Internalization of bFGF through the heparin-sensitive pathway was not efficiently competed by unlabeled bFGF and did not approach saturation at concentrations of bFGF up to 50 ng/ml, properties similar to the interaction of bFGF with low affinity heparan sulfate binding sites on the cell surface.	Heparin	36-43	fibroblast growth factor 2	Bos taurus	19-23
1429568-6	1992	Internalization of bFGF in CHO cells not expressing FGF receptors was inhibited by heparin, heparan sulfate, and dermatan sulfate, the same glycosaminoglycans that block binding to cell-surface heparin sulfates.	Heparin	83-90	fibroblast growth factor 2	Bos taurus	19-23
1429568-6	1992	Internalization of bFGF in CHO cells not expressing FGF receptors was inhibited by heparin, heparan sulfate, and dermatan sulfate, the same glycosaminoglycans that block binding to cell-surface heparin sulfates.	Heparin	83-90	fibroblast growth factor 2	Bos taurus	20-23
1429568-7	1992	Internalization of bFGF in the parental CHO cells was inhibited at the same concentrations of heparin that block binding to cell-surface heparan sulfates.	Heparin	94-101	fibroblast growth factor 2	Bos taurus	19-23
1486048-0	1992	Treatment of heparin-induced thrombocytopenia by use of argatroban, a synthetic thrombin inhibitor.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	80-88
1443220-0	1992	Heparin suppresses endothelin-1 action and production in spontaneously hypertensive rats.	Heparin	0-7	endothelin 1	Rattus norvegicus	19-31
1443220-3	1992	This study was designed to examine whether heparin affects endothelin-1 action and production, to further elucidate the mechanism of the antihypertensive effect of heparin.	Heparin	43-50	endothelin 1	Rattus norvegicus	59-71
1443220-4	1992	Four-week treatment with heparin (300 U/day sc) significantly decreased blood pressure in spontaneously hypertensive rats (SHR; 199 +/- 8 vs. 164 +/- 9 mmHg; P &lt; 0.001) and completely blunted pressor response to endothelin-1 in SHR.	Heparin	25-32	endothelin 1	Rattus norvegicus	215-227
1443220-6	1992	Heparin significantly suppressed endothelin-1-induced increase in intracellular calcium concentration and inositol 1,4,5-trisphosphate level in cultured vascular smooth muscle cells in a dose-dependent manner and endothelin-1 release from cultured endothelial cells.	Heparin	0-7	endothelin 1	Rattus norvegicus	33-45
1443220-6	1992	Heparin significantly suppressed endothelin-1-induced increase in intracellular calcium concentration and inositol 1,4,5-trisphosphate level in cultured vascular smooth muscle cells in a dose-dependent manner and endothelin-1 release from cultured endothelial cells.	Heparin	0-7	endothelin 1	Rattus norvegicus	213-225
1443220-8	1992	In conclusion, our findings indicate that the antihypertensive effect of heparin is mediated, at least in part, by the inhibition of endothelin-1 action on vascular smooth muscle cells and endothelin-1 production from endothelial cells.	Heparin	73-80	endothelin 1	Rattus norvegicus	133-145
1443220-8	1992	In conclusion, our findings indicate that the antihypertensive effect of heparin is mediated, at least in part, by the inhibition of endothelin-1 action on vascular smooth muscle cells and endothelin-1 production from endothelial cells.	Heparin	73-80	endothelin 1	Rattus norvegicus	189-201
1478276-1	1992	A biologically active fluorescent derivative of recombinant human basic fibroblast growth factor (bFGF) was prepared by immobilization on heparin-Sepharose 4B (HS) and derivatization with the fluorophore, Texas Red (TR).	Heparin	138-145	fibroblast growth factor 2	Homo sapiens	66-96
1423816-12	1992	Since chronic coumadin anticoagulation of cancer patients, and single pulse dose heparin prior to intravenous chemotherapy, both prevent thrombin generation, these agents may be of use in reducing the risk of chemotherapy-associated thrombosis.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	137-145
1426886-2	1992	The heparin-sensitive binding of 125I-low-density lipoprotein (LDL) to liver homogenates (reflecting the expression of the LDL receptor) was determined, together with the activities of the rate-limiting enzymes in cholesterol synthesis [3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase], bile acid production (cholesterol 7 alpha-hydroxylase), and cholesterol esterification (acyl CoA:cholesterol acyl transferase).	Heparin	4-11	cytochrome P450 family 7 subfamily A member 1	Homo sapiens	319-350
1478276-1	1992	A biologically active fluorescent derivative of recombinant human basic fibroblast growth factor (bFGF) was prepared by immobilization on heparin-Sepharose 4B (HS) and derivatization with the fluorophore, Texas Red (TR).	Heparin	138-145	fibroblast growth factor 2	Homo sapiens	98-102
1464752-7	1992	Preperfusion of the liver with heparin to deplete the liver of hepatic lipase resulted in about a 70% reduction in rHDL triolein hydrolysis and about a 75% reduction in rHDL cholesteryl oleate uptake.	Heparin	31-38	lipase C, hepatic type	Rattus norvegicus	63-77
1434535-5	1992	In order to identify TSP active domains, heparin, known to bind to the amino-terminal region of TSP, four monoclonal antibodies directed against specific domains of the molecule, and TSP fragments obtained by enzymatic digestion were used.	Heparin	41-48	thrombospondin 1	Homo sapiens	96-99
1434535-5	1992	In order to identify TSP active domains, heparin, known to bind to the amino-terminal region of TSP, four monoclonal antibodies directed against specific domains of the molecule, and TSP fragments obtained by enzymatic digestion were used.	Heparin	41-48	thrombospondin 1	Homo sapiens	96-99
1400429-4	1992	In type IIB vWD, plasma vWF exhibits increased affinity for platelet GPIb, but decreased binding to collagen and heparin.	Heparin	113-120	von Willebrand factor	Homo sapiens	24-27
1333636-1	1992	In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate.	Heparin	170-177	von Willebrand factor	Homo sapiens	66-87
1333636-1	1992	In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate.	Heparin	170-177	von Willebrand factor	Homo sapiens	89-92
1333636-1	1992	In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate.	Heparin	170-177	fibrinogen beta chain	Homo sapiens	95-105
1333636-1	1992	In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate.	Heparin	170-177	fibronectin 1	Homo sapiens	116-127
1333636-4	1992	The largest degree of coupling was found in heat-treated lyophilized heparin plasma, where C[fg/vWf] and C[fn/vWf] were 12.9 +/- 1.4 (mol/mol)% and 2.4 +/- 0.1 (mol/mol)% (mean +/- SD).	Heparin	69-76	von Willebrand factor	Homo sapiens	96-99
1333636-4	1992	The largest degree of coupling was found in heat-treated lyophilized heparin plasma, where C[fg/vWf] and C[fn/vWf] were 12.9 +/- 1.4 (mol/mol)% and 2.4 +/- 0.1 (mol/mol)% (mean +/- SD).	Heparin	69-76	von Willebrand factor	Homo sapiens	110-113
1384715-0	1992	Regulation of lipoprotein lipase by dibutyryl cAMP, cholera toxin, Hepes and heparin in F1 heart-cell cultures.	Heparin	77-84	lipoprotein lipase	Rattus norvegicus	14-32
1400429-13	1992	In type IIB vWD, the defective binding of plasma vWF to collagen and heparin may be secondary to post-synthetic modifications that occur in vivo, such as the loss of high molecular weight vWF multimers.	Heparin	69-76	von Willebrand factor	Homo sapiens	49-52
1329921-4	1992	These observations support the hypothesis that anti-IIa activity is important for inhibition of thrombin generation by LMW heparins in vitro.	Heparin	123-131	coagulation factor II, thrombin	Homo sapiens	96-104
1400330-0	1992	Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin.	Heparin	53-60	fibronectin 1	Homo sapiens	79-90
1329921-0	1992	Inhibition of thrombin generation by heparin and low molecular weight (LMW) heparins in the absence and presence of platelet factor 4 (PF4).	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	14-22
1329921-0	1992	Inhibition of thrombin generation by heparin and low molecular weight (LMW) heparins in the absence and presence of platelet factor 4 (PF4).	Heparin	76-84	coagulation factor II, thrombin	Homo sapiens	14-22
1383494-2	1992	In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9.	Heparin	29-36	fibroblast growth factor 1	Homo sapiens	52-56
1329921-1	1992	The ability of several low molecular weight (LMW) heparins and unfractionated heparin (UFH) to inhibit thrombin generation, and their anti-Xa and anti-IIa activities, were measured in the absence and presence of platelet factor 4 (PF4).	Heparin	87-90	coagulation factor II, thrombin	Homo sapiens	103-111
1329921-2	1992	The LMW heparins studied were 2-5 times less potent, on a weight basis, than UFH as inhibitors of thrombin generation in platelet-poor plasma; the inhibition of thrombin generation by LMW heparins correlated better with their anti-IIa activity (r = 0.98) than with their anti-Xa activity (r = 0.69).	Heparin	77-80	coagulation factor II, thrombin	Homo sapiens	98-106
1428206-2	1992	Heparin-assisted dialysis resulted in a significant rise of VIII:C and AT III; with defibrotide, instead, there was evidence of thrombin activation (increased FPA and TAT).	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	128-136
1383494-8	1992	Pretreatment of NFlg26 cell membranes with pertussis toxin resulted in a heparin-dependent decrease in the binding affinity (Kd values of 0.57-1.15 nM) of [125I]aFGF.	Heparin	73-80	fibroblast growth factor 1	Homo sapiens	161-165
1383494-10	1992	Guanine nucleotides were also found to significantly reduce 0.1 nM [125I]aFGF binding in a heparin-dependent fashion.	Heparin	91-98	fibroblast growth factor 1	Homo sapiens	73-77
1383494-11	1992	The present data demonstrate that, in the presence of heparin, [125I]aFGF binds with high affinity to the cloned FGF-flg receptor on NFlg26 cell membranes.	Heparin	54-61	fibroblast growth factor 1	Homo sapiens	69-73
1383494-12	1992	However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans.	Heparin	18-25	fibroblast growth factor 1	Homo sapiens	58-62
1383494-2	1992	In the presence of 5 U/ml of heparin to block [125I]aFGF binding to membrane bound heparan sulfate proteoglycans, specific [125I]aFGF binding was optimal in the presence of 0.2 M NaCl and in a pH range of 7 to 9.	Heparin	29-36	fibroblast growth factor 1	Homo sapiens	129-133
1383494-12	1992	However, at a low heparin concentration (0.1 U/ml), [125I]aFGF binds to the FGF-flg receptor with higher affinity than was observed in the presence of 5 U/ml of heparin, and also binds a class of lower affinity recognition sites which are consistent with the labeling of cell surface heparan sulfate proteoglycans.	Heparin	161-168	fibroblast growth factor 1	Homo sapiens	58-62
1383494-7	1992	Additional saturation studies, conducted in the presence of a lower (0.1 U/ml) heparin concentration, indicated that [125I] aFGF labeled both the high affinity (Kd = 0.02 nM) FGF-flg receptor and a separate class of lower affinity (Kd = 2 nM) recognition sites.	Heparin	79-86	fibroblast growth factor 1	Homo sapiens	124-128
1388162-6	1992	Heparin with high affinity for AT accelerated the substrate reaction with thrombin to an extent consistent with the reduced heparin affinity of the AT-peptide complex.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	74-82
1411301-5	1992	When two of the hormones known to be under dopamine control, i.e. prolactin (PRL) and thyrotropin (TSH), were tested, they were able to prevent dopamine-induced cell death if combined with heparin.	Heparin	189-196	prolactin	Homo sapiens	66-75
1390688-9	1992	In the case of aFGF, suramin interacts at or near its heparin binding site.	Heparin	54-61	fibroblast growth factor 1	Homo sapiens	15-19
1388162-6	1992	Heparin with high affinity for AT accelerated the substrate reaction with thrombin to an extent consistent with the reduced heparin affinity of the AT-peptide complex.	Heparin	124-131	coagulation factor II, thrombin	Homo sapiens	74-82
1388162-7	1992	These data show that blocking by the peptide of the putative intramolecular association of the P1 to P14 region of the AT reactive-bond loop with the A beta-sheet leads to AT functioning as a substrate of its target enzymes with an efficiency that equals or exceeds the action of uncomplexed AT as an inhibitor and with the expected heparin activation.	Heparin	333-340	amyloid beta precursor protein	Homo sapiens	150-156
1387642-0	1992	Interactions of a laminin-binding peptide from a 33-kDa protein related to the 67-kDa laminin receptor with laminin and melanoma cells are heparin-dependent.	Heparin	139-146	ribosomal protein SA	Homo sapiens	79-102
1520875-0	1992	Heparin enhances active site-dependent binding of tissue-type plasminogen activator to endothelial cells.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	50-83
1525174-4	1992	Furthermore, using heparan sulfate and heparin treated with heparinases I and III, we have shown that the interferon-gamma binding sites are localized on the N-sulfated glucosamine rich domains of the molecule.	Heparin	39-46	interferon gamma	Homo sapiens	106-122
1387642-1	1992	A laminin-binding peptide (peptide G), predicted from the cDNA sequence for a 33-kDa protein related to the 67-kDa laminin receptor, specifically inhibits binding of laminin to heparin and sulfatide.	Heparin	177-184	ribosomal protein SA	Homo sapiens	108-131
1332992-0	1992	[Low-molecular heparin complex formation with the blood coagulation proteins--thrombin and fibrinogen].	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	78-86
1497347-9	1992	The heparin effect was less pronounced with the non-heparin binding carboxy-terminal domain of fibronectin.	Heparin	4-11	fibronectin 1	Homo sapiens	95-106
1497347-9	1992	The heparin effect was less pronounced with the non-heparin binding carboxy-terminal domain of fibronectin.	Heparin	52-59	fibronectin 1	Homo sapiens	95-106
1493594-2	1992	Administration of 4-aminopyrazolopyrimidine (50 mg/kg) to control rats for 24 h reduced plasma triacylglycerol levels and increased the heparin-induced release of lipoprotein lipase into the incubation medium of cardiac myocytes.	Heparin	136-143	lipoprotein lipase	Rattus norvegicus	163-181
1493594-5	1992	Administration of Triton WR-1339 also resulted in hypertriglyceridemia, but the heparin-induced release of lipoprotein lipase from control cardiac myocytes was not reduced in the absence of lipolysis of triacylglycerol-rich lipoproteins.	Heparin	80-87	lipoprotein lipase	Rattus norvegicus	107-125
1493594-6	1992	Treatment with Triton WR-1339 did, however, increase the heparin-induced release of lipoprotein lipase from diabetic cardiac myocytes.	Heparin	57-64	lipoprotein lipase	Rattus norvegicus	84-102
1505778-1	1992	The secretory enzyme extracellular-superoxide dismutase (EC-SOD) has affinity for heparin and some other sulfated glycosaminoglycans and is in vivo bound to heparan sulfate proteoglycan.	Heparin	82-89	superoxide dismutase 3	Homo sapiens	21-55
1505778-1	1992	The secretory enzyme extracellular-superoxide dismutase (EC-SOD) has affinity for heparin and some other sulfated glycosaminoglycans and is in vivo bound to heparan sulfate proteoglycan.	Heparin	82-89	superoxide dismutase 3	Homo sapiens	57-63
1505778-2	1992	Nonenzymic glycation of EC-SOD, both in vivo and in vitro, is associated with a reduction in heparin affinity, whereas the enzymic activity is not affected.	Heparin	93-100	superoxide dismutase 3	Homo sapiens	24-30
1505778-8	1992	The primary glycation sites in EC-SOD are thus lysine-211 and lysine-212 in the putative heparin-binding domain in the carboxyterminal end.	Heparin	89-96	superoxide dismutase 3	Homo sapiens	31-37
1332992-0	1992	[Low-molecular heparin complex formation with the blood coagulation proteins--thrombin and fibrinogen].	Heparin	15-22	fibrinogen beta chain	Homo sapiens	91-101
1332992-1	1992	It has been found that low molecular heparin (LMH) forms complexes with fibrinogen and thrombin.	Heparin	37-44	fibrinogen beta chain	Homo sapiens	72-82
1332992-1	1992	It has been found that low molecular heparin (LMH) forms complexes with fibrinogen and thrombin.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	87-95
1412157-1	1992	The decay rate of thrombin in plasma is shown to be linearly proportional to the concentration of antithrombin III (AT III), not only in the absence but also in the presence of heparin.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	18-26
1323648-6	1992	Graded concentrations of heparin or NaCl competed with [125I]-labeled bFGF in a dose-dependent fashion, reducing [125I]-labeled bFGF binding by 75 and 97%, respectively.	Heparin	25-32	fibroblast growth factor 2	Bos taurus	128-132
1323648-11	1992	Binding of [125I]-labeled bFGF to these sites was also influenced by heparin, consistent with coregulation of binding to the two classes of binding sites.	Heparin	69-76	fibroblast growth factor 2	Bos taurus	26-30
1637178-0	1992	The heparin binding site of human extracellular-superoxide dismutase.	Heparin	4-11	superoxide dismutase 3	Homo sapiens	34-68
1637178-4	1992	EC-SOD in plasma is heterogeneous with regard to heparin affinity and can be divided into three fractions: A, without affinity; B, with intermediate affinity; and C, with high affinity.	Heparin	49-56	superoxide dismutase 3	Homo sapiens	0-6
1637178-9	1992	These results suggest that the heparin-binding site may occur on a "cluster" of basic amino acids at the C-terminal end of EC-SOD C. EC-SOD is speculated to be primarily synthesized as type C, and types A and B are probably the result of secondary modifications.	Heparin	31-38	superoxide dismutase 3	Homo sapiens	123-129
1637178-9	1992	These results suggest that the heparin-binding site may occur on a "cluster" of basic amino acids at the C-terminal end of EC-SOD C. EC-SOD is speculated to be primarily synthesized as type C, and types A and B are probably the result of secondary modifications.	Heparin	31-38	superoxide dismutase 3	Homo sapiens	133-139
1412223-4	1992	The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III.	Heparin	62-69	coagulation factor II, thrombin	Homo sapiens	17-25
1512327-9	1992	Heparin administration was associated with a smaller reduction in fibrinogen and a smaller increase in D-dimer level during and after alteplase administration.	Heparin	0-7	fibrinogen beta chain	Homo sapiens	66-76
1323648-6	1992	Graded concentrations of heparin or NaCl competed with [125I]-labeled bFGF in a dose-dependent fashion, reducing [125I]-labeled bFGF binding by 75 and 97%, respectively.	Heparin	25-32	fibroblast growth factor 2	Bos taurus	70-74
1498336-4	1992	Heparin is highly effective in inhibiting fluid phase thrombin, but is a relatively ineffective inhibitor of thrombus-bound thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	54-62
1412223-4	1992	The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	17-25
1322029-0	1992	Adjunctive therapy with low molecular weight heparin with recombinant tissue-type plasminogen activator causes sustained reflow in canine coronary thrombosis.	Heparin	45-52	tissue-type plasminogen activator	Canis lupus familiaris	70-103
1638523-4	1992	Both human and murine IL-6 reduced heparin-releasable LPL activity in 3T3-L1 adipocytes in a dose-dependent manner; half-maximal inhibition of LPL activity was achieved with 5000 hybridoma growth factor units/ml.	Heparin	35-42	interleukin 6	Mus musculus	22-26
1510155-3	1992	Vasopressin evoked a [Ca2+]i transient even in the absence of extracellular Ca2+, and intracellular perfusion with heparin completely blocked the response to vasopressin stimulation.	Heparin	115-122	arginine vasopressin	Homo sapiens	158-169
1497611-0	1992	Interaction of size-fractionated heparins with lipoprotein lipase and hepatic lipase in the rat.	Heparin	33-41	lipoprotein lipase	Rattus norvegicus	47-65
1497611-0	1992	Interaction of size-fractionated heparins with lipoprotein lipase and hepatic lipase in the rat.	Heparin	33-41	lipase C, hepatic type	Rattus norvegicus	70-84
1497611-4	1992	To evoke the same plasma activity of LPL and HL required about 10 times more by weight, or about 40 times more molecules, of this heparin than of hep 5 (mean M(r) 12,000, similar to conventional heparin).	Heparin	130-137	lipoprotein lipase	Rattus norvegicus	37-40
1497611-4	1992	To evoke the same plasma activity of LPL and HL required about 10 times more by weight, or about 40 times more molecules, of this heparin than of hep 5 (mean M(r) 12,000, similar to conventional heparin).	Heparin	130-137	lipase C, hepatic type	Rattus norvegicus	45-47
1497615-5	1992	In contrast, heparin-releasable lipoprotein lipase was not increased in perfused hearts of meal-fed rats on refeeding.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	32-50
1520027-0	1992	Varying heparin requirements in hemodialysis patients receiving erythropoietin.	Heparin	8-15	erythropoietin	Homo sapiens	64-78
1520027-1	1992	A two-phase study was undertaken to investigate the incidence, extent, and management of increased heparin needs occurring during erythropoietin (EPO) therapy in the hemodialysis patient.	Heparin	99-106	erythropoietin	Homo sapiens	130-144
1520027-1	1992	A two-phase study was undertaken to investigate the incidence, extent, and management of increased heparin needs occurring during erythropoietin (EPO) therapy in the hemodialysis patient.	Heparin	99-106	erythropoietin	Homo sapiens	146-149
1520027-3	1992	It appears that increased heparin requirements are frequently associated with EPO therapy, and awareness of this finding, coupled with close ACT monitoring, may possibly prevent complications associated with undetected increases in heparin requirement.	Heparin	26-33	erythropoietin	Homo sapiens	78-81
1392061-4	1992	The addition of 250 ng/mL of heparin to the culture medium resulted in about a tenfold increase in the proliferation-stimulating activity of bFGF and allowed the detection of as low as 10 pg/mL of bFGF.	Heparin	29-36	fibroblast growth factor 2	Bos taurus	141-145
1499567-2	1992	Recently we have shown that heparin and related sulfated polyanions are low-affinity ligands of the kringle domain in the amino-terminal region (ATF) of human urokinase (u-PA), and proposed that this may facilitate loading of u-PA onto its receptor at the focal contacts between adherent cells and their matrix.	Heparin	28-35	glial cell derived neurotrophic factor	Homo sapiens	145-148
1499567-2	1992	Recently we have shown that heparin and related sulfated polyanions are low-affinity ligands of the kringle domain in the amino-terminal region (ATF) of human urokinase (u-PA), and proposed that this may facilitate loading of u-PA onto its receptor at the focal contacts between adherent cells and their matrix.	Heparin	28-35	plasminogen activator, urokinase	Homo sapiens	170-174
1499567-2	1992	Recently we have shown that heparin and related sulfated polyanions are low-affinity ligands of the kringle domain in the amino-terminal region (ATF) of human urokinase (u-PA), and proposed that this may facilitate loading of u-PA onto its receptor at the focal contacts between adherent cells and their matrix.	Heparin	28-35	plasminogen activator, urokinase	Homo sapiens	226-230
1499567-5	1992	The long-arm terminal domain of laminin (fragment E3), which contains a heparin-binding site, competed for binding of u-PA to immobilised heparin.	Heparin	72-79	plasminogen activator, urokinase	Homo sapiens	118-122
1499567-5	1992	The long-arm terminal domain of laminin (fragment E3), which contains a heparin-binding site, competed for binding of u-PA to immobilised heparin.	Heparin	138-145	plasminogen activator, urokinase	Homo sapiens	118-122
1499567-6	1992	However nidogen, which does not bind to heparin, also inhibited binding of u-PA to heparin, and this effect was also observed with recombinant nidogen and with a fragment of nidogen lacking the carboxy-terminal domain.	Heparin	83-90	plasminogen activator, urokinase	Homo sapiens	75-79
1522018-4	1992	Uptake of DPPG was compared in normal, diabetic, tumor-bearing and heparin pretreated rats, revealing differences in uptake and clearance of radioactivity, correlating with hepatic lipase activity of these groups.	Heparin	67-74	lipase C, hepatic type	Rattus norvegicus	173-187
1639873-0	1992	Transforming growth factor-beta 1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-beta 1.	Heparin	39-46	transforming growth factor beta 1	Homo sapiens	0-33
1639873-0	1992	Transforming growth factor-beta 1 is a heparin-binding protein: identification of putative heparin-binding regions and isolation of heparins with varying affinity for TGF-beta 1.	Heparin	39-46	transforming growth factor beta 1	Homo sapiens	167-177
1639873-1	1992	Previous studies indicated that a major factor in heparin"s ability to suppress the proliferation of vascular smooth muscle cells is an interaction with transforming growth factor-beta 1 (TGF-beta 1).	Heparin	50-57	transforming growth factor beta 1	Homo sapiens	153-186
1639873-1	1992	Previous studies indicated that a major factor in heparin"s ability to suppress the proliferation of vascular smooth muscle cells is an interaction with transforming growth factor-beta 1 (TGF-beta 1).	Heparin	50-57	transforming growth factor beta 1	Homo sapiens	188-198
1639873-2	1992	Heparin appeared to bind directly to TGF-beta 1 and to prevent the association of TGF-beta 1 with alpha 2-macroglobulin (alpha 2-M).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	37-47
1639873-2	1992	Heparin appeared to bind directly to TGF-beta 1 and to prevent the association of TGF-beta 1 with alpha 2-macroglobulin (alpha 2-M).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	82-92
1639873-3	1992	The present studies indicate that 20-70% of iodinated TGF-beta 1 binds to heparin-Sepharose and the retained fraction is eluted with approximately 0.37 M NaCl.	Heparin	74-81	transforming growth factor beta 1	Homo sapiens	54-64
1639873-4	1992	Native, unlabelled platelet TGF-beta 1, however, is completely retained by heparin-Sepharose and eluted with 0.9-1.2 M NaCl.	Heparin	75-82	transforming growth factor beta 1	Homo sapiens	28-38
1639873-5	1992	Using synthetic peptides, the regions of TGF-beta 1 that might be involved in the binding of heparin and other polyanions were examined.	Heparin	93-100	transforming growth factor beta 1	Homo sapiens	41-51
1639873-9	1992	Synthetic peptides homologous to these three regions, but not to other regions of TGF-beta 1, were found to bind to heparin-Sepharose and were eluted with 0.15 M-0.30 M NaCl.	Heparin	116-123	transforming growth factor beta 1	Homo sapiens	82-92
1385458-0	1992	Anti-fibronectin antibodies that modify heparin binding and cell adhesion: evidence for a new cell binding site in the heparin binding region.	Heparin	40-47	fibronectin 1	Homo sapiens	5-16
1639873-10	1992	Only two of these regions were capable of blocking the binding of heparin to 125I-TGF-beta.	Heparin	66-73	transforming growth factor beta 1	Homo sapiens	82-90
1639873-11	1992	Immobilization of these peptides, followed by affinity purification of heparin, indicated that one peptide was capable of isolating subspecies of heparin with high and low affinity for authentic TGF-beta 1.	Heparin	146-153	transforming growth factor beta 1	Homo sapiens	195-205
1639873-12	1992	The ability of TGF-beta 1 to bind to heparin or related proteoglycans under physiological conditions may be useful in understanding the biology of this pluripotent growth and metabolic signal.	Heparin	37-44	transforming growth factor beta 1	Homo sapiens	15-25
1639873-13	1992	Conversely, a subspecies of heparin molecules with high affinity for TGF-beta 1 may be a factor in some of the diverse biological actions of heparin.	Heparin	28-35	transforming growth factor beta 1	Homo sapiens	69-79
1639873-13	1992	Conversely, a subspecies of heparin molecules with high affinity for TGF-beta 1 may be a factor in some of the diverse biological actions of heparin.	Heparin	141-148	transforming growth factor beta 1	Homo sapiens	69-79
1392061-4	1992	The addition of 250 ng/mL of heparin to the culture medium resulted in about a tenfold increase in the proliferation-stimulating activity of bFGF and allowed the detection of as low as 10 pg/mL of bFGF.	Heparin	29-36	fibroblast growth factor 2	Bos taurus	197-201
1378755-0	1992	Ability of different chemically modified heparins to potentiate the biological activity of heparin-binding growth factor 1: lack of correlation with growth factor binding.	Heparin	41-49	fibroblast growth factor 1	Mus musculus	91-122
1378755-8	1992	In contrast, the neurotrophic activity of HBGF-1 was potentiated by modified heparin species which failed to bind HBGF-1 and were without activity in the mitogenic assays.	Heparin	77-84	fibroblast growth factor 1	Mus musculus	42-48
1378755-1	1992	A range of chemically modified heparins was examined for their ability to bind heparin-binding growth factor 1 (HBGF-1; acidic fibroblast growth factor) and potentiate the in vitro mitogenic and neurotrophic activity of HBGF-1.	Heparin	31-39	fibroblast growth factor 1	Mus musculus	79-110
1378755-1	1992	A range of chemically modified heparins was examined for their ability to bind heparin-binding growth factor 1 (HBGF-1; acidic fibroblast growth factor) and potentiate the in vitro mitogenic and neurotrophic activity of HBGF-1.	Heparin	31-39	fibroblast growth factor 1	Mus musculus	112-118
1378755-1	1992	A range of chemically modified heparins was examined for their ability to bind heparin-binding growth factor 1 (HBGF-1; acidic fibroblast growth factor) and potentiate the in vitro mitogenic and neurotrophic activity of HBGF-1.	Heparin	31-39	fibroblast growth factor 1	Mus musculus	120-151
1378755-1	1992	A range of chemically modified heparins was examined for their ability to bind heparin-binding growth factor 1 (HBGF-1; acidic fibroblast growth factor) and potentiate the in vitro mitogenic and neurotrophic activity of HBGF-1.	Heparin	31-39	fibroblast growth factor 1	Mus musculus	220-226
1378755-2	1992	It was found that carboxyl-reduced heparin bound HBGF-1 as effectively as the native heparin molecule.	Heparin	35-42	fibroblast growth factor 1	Mus musculus	49-55
1378755-5	1992	In contrast, the ability of the modified heparins to potentiate the mitogenic activity of HBGF-1 correlated only to a limited extent with their affinity for HBGF-1.	Heparin	41-49	fibroblast growth factor 1	Mus musculus	90-96
1378755-5	1992	In contrast, the ability of the modified heparins to potentiate the mitogenic activity of HBGF-1 correlated only to a limited extent with their affinity for HBGF-1.	Heparin	41-49	fibroblast growth factor 1	Mus musculus	157-163
1387724-11	1992	As sustained higher FDP.D dimer means the existence of fibrin clots, heparin treatment should be continued for prevention of clot formation as long as FDP.D dimer shows higher value.	Heparin	69-76	otoraplin	Homo sapiens	20-23
1642146-6	1992	With chick osteoclasts, which could be maintained in serum-free conditions, a stimulatory effect of heparin was found both in the presence of 5% fetal calf serum and in serum-free media containing insulin, transferrin, and selenium.	Heparin	100-107	insulin	Gallus gallus	197-204
1377216-3	1992	SAP neutralized the catalytic effect of heparin on the thrombin-antithrombin III reaction more effectively than vitronectin, histidine-rich glycoprotein, fibronectin, and high-molecular-weight kininogen and almost as effectively as platelet factor 4.	Heparin	40-47	coagulation factor II, thrombin	Homo sapiens	55-63
1457941-0	1992	Binding kinetics of thrombin and antithrombin III with immobilized heparin using a spacer.	Heparin	67-74	coagulation factor II, thrombin	Homo sapiens	20-28
1457941-2	1992	In this study, the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin were investigated.	Heparin	51-58	coagulation factor II, thrombin	Homo sapiens	68-76
1457941-8	1992	The immobilized heparin bound with both ATIII and thrombin, and the binding mechanism was similar to that of free heparin.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	50-58
1607375-3	1992	More radiolabeled thrombin was adsorbed to heparin-polyvinyl alcohol (PVA) than to PVA, consistent with a specific interaction with the immobilized heparin.	Heparin	43-50	coagulation factor II, thrombin	Homo sapiens	18-26
1377216-4	1992	SAP also blocked the effects of heparin and dermatan sulfate on the inhibition of thrombin by heparin cofactor II.	Heparin	32-39	coagulation factor II, thrombin	Homo sapiens	82-90
1377216-5	1992	We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP.	Heparin	162-169	coagulation factor II, thrombin	Homo sapiens	129-137
1387724-11	1992	As sustained higher FDP.D dimer means the existence of fibrin clots, heparin treatment should be continued for prevention of clot formation as long as FDP.D dimer shows higher value.	Heparin	69-76	otoraplin	Homo sapiens	151-154
1618347-1	1992	Fibronectin type III-like sequences are present in many proteins from higher eukaryotes and are involved in protein-protein interactions, heparin binding and cell adhesion.	Heparin	138-145	fibronectin 1	Homo sapiens	0-11
1378264-1	1992	Basic residues Arg-118, Lys-119, Lys-128, and Arg-129 within a putative heparin-binding and receptor-binding region of the 155-amino acid form of basic fibroblast growth factor (bFGF) have been changed to neutral glutamine residues by site-directed mutagenesis of the human bFGF cDNA.	Heparin	72-79	fibroblast growth factor 2	Homo sapiens	146-176
1378264-1	1992	Basic residues Arg-118, Lys-119, Lys-128, and Arg-129 within a putative heparin-binding and receptor-binding region of the 155-amino acid form of basic fibroblast growth factor (bFGF) have been changed to neutral glutamine residues by site-directed mutagenesis of the human bFGF cDNA.	Heparin	72-79	fibroblast growth factor 2	Homo sapiens	178-182
1378264-3	1992	When compared to wild type bFGF, M6B-bFGF showed in cultured endothelial cells a similar receptor-binding capacity and mitogenic activity, but a reduced affinity for heparin-like low affinity binding sites, a reduced chemotactic activity, and a reduced capacity to induce the production of urokinase-type plasminogen activator.	Heparin	166-173	fibroblast growth factor 2	Homo sapiens	37-41
1618758-2	1992	The synthetic antithrombin-binding heparin pentasaccharide and a full-length heparin of approximately 26 saccharides containing this specific sequence have been compared with respect to their interactions with antithrombin and their ability to promote inhibition and substrate reactions of antithrombin with thrombin and factor Xa.	Heparin	35-42	coagulation factor II, thrombin	Homo sapiens	18-26
1618758-7	1992	In contrast, the full-length heparin produced large ionic strength-dependent enhancements in second order rate constants for both antithrombin reactions of 4,300-fold for thrombin and 580-fold for factor Xa at I 0.15.	Heparin	29-36	coagulation factor II, thrombin	Homo sapiens	134-142
1375939-7	1992	Further, in contrast to FGF-1 monomers, which dissociate from immobilized heparin in 1.0 M NaCl, preformed FGF-1 homodimers had reduced apparent affinity for immobilized heparin and eluted at 0.4 M NaCl.	Heparin	170-177	fibroblast growth factor 1	Homo sapiens	107-112
1376338-5	1992	It was shown that 125I-labeled Thy-1 directly bound to immobilized heparin.	Heparin	67-74	thymus cell antigen 1, theta	Mus musculus	31-36
1376338-6	1992	Sulfated glycans such as pentosan sulfate, dextran sulfate, and fucoidan were found to strongly inhibit the binding of Thy-1 to heparin.	Heparin	128-135	thymus cell antigen 1, theta	Mus musculus	119-124
1375937-4	1992	Caerulein-stimulated release of Ca2+ was completely blocked by either neomycin, an inhibitor of phospholipase C, or by heparin, an IP3 receptor antagonist.	Heparin	119-126	carbonic anhydrase 2	Rattus norvegicus	32-35
1375937-4	1992	Caerulein-stimulated release of Ca2+ was completely blocked by either neomycin, an inhibitor of phospholipase C, or by heparin, an IP3 receptor antagonist.	Heparin	119-126	inositol 1,4,5-trisphosphate receptor, type 3	Rattus norvegicus	131-143
1375939-8	1992	In contrast, the apparent affinity of human FGF-2 for immobilized heparin was unaffected after exposure to copper ions.	Heparin	66-73	fibroblast growth factor 2	Homo sapiens	44-49
1375939-9	1992	Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	96-101
1375939-9	1992	Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	164-169
1375939-9	1992	Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes.	Heparin	140-147	fibroblast growth factor 1	Homo sapiens	96-101
1375939-9	1992	Heparin appeared to modulate the formation of copper-induced intermolecular disulfide bonds for FGF-1 but not FGF-2, since co-incubation of heparin and copper with FGF-1 monomers resulted in dimers and other oligomeric complexes.	Heparin	140-147	fibroblast growth factor 1	Homo sapiens	164-169
1423034-0	1992	Exercise training has a heparin-like effect on lipoprotein lipase activity in muscle.	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	47-65
1322691-1	1992	Anti-factor Xa and anti-thrombin activities of unfractionated (UF) and low molecular weight (LMW) heparins have been measured in human plasma and with purified human antithrombin III (ATIII) in the absence and presence of 1.5 mM calcium.	Heparin	98-106	coagulation factor II, thrombin	Homo sapiens	24-32
1322691-2	1992	The anti-factor Xa and anti-thrombin activities were measured directly, by assessing the heparin-dependent pseudo-first order rate constants of inactivation of human factor Xa or thrombin.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	28-36
1322691-2	1992	The anti-factor Xa and anti-thrombin activities were measured directly, by assessing the heparin-dependent pseudo-first order rate constants of inactivation of human factor Xa or thrombin.	Heparin	89-96	coagulation factor II, thrombin	Homo sapiens	179-187
1322691-8	1992	Calcium reduced the anti-thrombin activities of all the heparin preparations studied about 1.5 times when purified ATIII was used, although in plasma this effect was less clear.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	25-33
1322691-9	1992	Consequently, in the presence of 1.5 mM calcium the ratio of the anti-factor Xa to the anti-thrombin activities of UF standard heparin approximated those of the LMW heparins.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	92-100
1643205-0	1992	Fibrin clots obtained from plasma containing heparin show a higher sensitivity to t-PA-induced lysis.	Heparin	45-52	plasminogen activator, tissue type	Homo sapiens	82-86
1643205-2	1992	We have evaluated the sensitivity to t-PA-induced lysis of clots prepared from plasma preincubated in vitro with therapeutic concentrations of heparin.	Heparin	143-150	plasminogen activator, tissue type	Homo sapiens	37-41
1643205-3	1992	The extent of t-PA-induced lysis was significantly increased by preincubation of plasma with 0.5 and 1.0 U/ml heparin.	Heparin	110-117	plasminogen activator, tissue type	Homo sapiens	14-18
1643205-4	1992	The concentration of t-PA required to give similar lysis rates were reduced by up to five times after adding 1.0 U/ml heparin to plasma prior to clot formation.	Heparin	118-125	plasminogen activator, tissue type	Homo sapiens	21-25
10078261-0	1992	C3a and C5a anaphylatoxins bind to heparin-based sorbent in low density lipoprotein apheresis: in vitro and in vivo investigations.	Heparin	35-42	complement C5a receptor 1	Homo sapiens	8-11
10078261-10	1992	The removal of C3a and C5a anaphylatoxins by heparin-based sorbent should be regarded as an advantage of this type of plasmasorbent.	Heparin	45-52	complement C5a receptor 1	Homo sapiens	23-26
1423034-5	1992	The total amount of LPL (i.e., pre-heparin perfusate plus post-heparin perfusate) was twofold greater in the hindlimb of the trained animals versus the controls.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	20-23
1423034-3	1992	At the same time, post-heparin perfusate LPL activity decreased from 63 +/- 2 to 13 +/- 1 U/hindlimb (p less than 0.001).	Heparin	23-30	lipoprotein lipase	Rattus norvegicus	41-44
1423034-4	1992	These results provide evidence that exercise-training has a heparin-like effect on capillary-bound LPL.	Heparin	60-67	lipoprotein lipase	Rattus norvegicus	99-102
1423034-5	1992	The total amount of LPL (i.e., pre-heparin perfusate plus post-heparin perfusate) was twofold greater in the hindlimb of the trained animals versus the controls.	Heparin	35-42	lipoprotein lipase	Rattus norvegicus	20-23
1378829-1	1992	The distributions of acidic fibroblast growth factor (aFGF) and basic FGF (bFGF) in extracts of various cultured mammalian cells were determined from their elution profiles on heparin-affinity chromatography, and assay of activity as ability to stimulate DNA synthesis in BALB/c3T3 cells.	Heparin	176-183	fibroblast growth factor 2	Homo sapiens	75-79
1613389-4	1992	Heparanase activity was found mainly in fractions containing the specific granules; this activity was inhibited by heparin.	Heparin	115-122	heparanase	Homo sapiens	0-10
1612188-6	1992	The purified PLA2 from human seminal plasma showed high affinity to heparin, sensitivity toward p-bromophenacyl bromide, Pb2+, dithioerythritol and EDTA and it was activated by Ca2+ and Mn2+.	Heparin	68-75	phospholipase A2 group IB	Homo sapiens	13-17
1332180-6	1992	These concentrations reflected a need for more heparin if, for example, inflammation, indicated by increasing C-reactive protein levels (CRP), occurred.	Heparin	47-54	C-reactive protein	Homo sapiens	110-128
1607927-2	1992	The 33 kDa C-terminal cell and heparin-binding fragment of FN, in particular, is a strong promoter of CNS neurite outgrowth.	Heparin	31-38	fibronectin 1	Homo sapiens	59-61
1375966-9	1992	Heparin suppressed alpha granule release induced by thrombin both in whole blood and in washed platelets.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	52-60
1509415-5	1992	It has been postulated that heparin acts by potentiating the effect of ECGF, but heparin inhibited thrombospondin release and enhanced that of von Willebrand factor in the absence of ECGS, while ECGS alone inhibited release of plasminogen activator inhibitor.	Heparin	28-35	fibroblast growth factor 1	Homo sapiens	71-75
1315738-1	1992	Protein C inhibitor is a plasma protein whose ability to inhibit activated protein C, thrombin, and other enzymes is stimulated by heparin.	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	86-94
1599459-1	1992	OSF-1 (also known as pleiotrophin, HB-GAM, HBGF-8 or HBNF) is a heparin-binding, neurotrophic protein.	Heparin	64-71	pleiotrophin	Homo sapiens	0-5
1599459-1	1992	OSF-1 (also known as pleiotrophin, HB-GAM, HBGF-8 or HBNF) is a heparin-binding, neurotrophic protein.	Heparin	64-71	pleiotrophin	Homo sapiens	21-33
1599459-1	1992	OSF-1 (also known as pleiotrophin, HB-GAM, HBGF-8 or HBNF) is a heparin-binding, neurotrophic protein.	Heparin	64-71	pleiotrophin	Homo sapiens	35-41
1599459-1	1992	OSF-1 (also known as pleiotrophin, HB-GAM, HBGF-8 or HBNF) is a heparin-binding, neurotrophic protein.	Heparin	64-71	pleiotrophin	Homo sapiens	43-49
1599459-1	1992	OSF-1 (also known as pleiotrophin, HB-GAM, HBGF-8 or HBNF) is a heparin-binding, neurotrophic protein.	Heparin	64-71	pleiotrophin	Homo sapiens	53-57
1319206-0	1992	Spectrophotometric detection of the interaction between cytochrome c and heparin.	Heparin	73-80	cytochrome c, somatic	Homo sapiens	56-68
1319206-1	1992	Heparin inhibits transport of electrons from reduced cytochrome c to cytochrome c oxidase.	Heparin	0-7	cytochrome c, somatic	Homo sapiens	53-65
1319206-1	1992	Heparin inhibits transport of electrons from reduced cytochrome c to cytochrome c oxidase.	Heparin	0-7	cytochrome c, somatic	Homo sapiens	69-81
1319206-2	1992	The effect is due to the interaction of heparin with cytochrome c.	Heparin	40-47	cytochrome c, somatic	Homo sapiens	53-65
1319206-3	1992	It has been observed that binding of heparin to the reduced or oxidized cytochrome c changes the spectrum of cytochrome c at the Soret region.	Heparin	37-44	cytochrome c, somatic	Homo sapiens	72-84
1319206-3	1992	It has been observed that binding of heparin to the reduced or oxidized cytochrome c changes the spectrum of cytochrome c at the Soret region.	Heparin	37-44	cytochrome c, somatic	Homo sapiens	109-121
1319206-4	1992	Affinity chromatography of heparin in cytochrome c immobilized to thiol-Sepharose shows that commercial heparin is eluted in the low-affinity and high-affinity fractions.	Heparin	27-34	cytochrome c, somatic	Homo sapiens	38-50
1319206-4	1992	Affinity chromatography of heparin in cytochrome c immobilized to thiol-Sepharose shows that commercial heparin is eluted in the low-affinity and high-affinity fractions.	Heparin	104-111	cytochrome c, somatic	Homo sapiens	38-50
1319206-6	1992	Polylysine induces decay of the cytochrome c-heparin complex.	Heparin	45-52	cytochrome c, somatic	Homo sapiens	32-44
1315738-7	1992	Heparin accelerated inhibition of alpha-thrombin, gamma T-thrombin, activated protein C, factor Xa, urokinase, and chymotrypsin, but not plasma kallikrein.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	40-48
1577724-1	1992	Human von Willebrand factor, a plasma glycoprotein which plays a critical role in regulating hemostasis, binds heparin, but the physiological importance and mode of this interaction is poorly understood.	Heparin	111-118	von Willebrand factor	Homo sapiens	6-27
1315738-7	1992	Heparin accelerated inhibition of alpha-thrombin, gamma T-thrombin, activated protein C, factor Xa, urokinase, and chymotrypsin, but not plasma kallikrein.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	58-66
1577724-2	1992	Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide.	Heparin	57-64	von Willebrand factor	Homo sapiens	139-160
1315739-4	1992	All three inhibitors obeyed a ternary complex mechanism for heparin-enhanced thrombin inhibition, and the optimum heparin concentration was related to the apparent heparin affinity of the inhibitor.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	77-85
1577724-2	1992	Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide.	Heparin	57-64	von Willebrand factor	Homo sapiens	264-285
1577724-2	1992	Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide.	Heparin	219-226	von Willebrand factor	Homo sapiens	139-160
1577724-2	1992	Using the motif of an amino acid sequence of a consensus heparin binding synthetic peptide, a 23-residue sequence (Tyr565-Ala587) of human von Willebrand factor was identified that retains the consensus motif and binds heparin with affinity comparable with native von Willebrand factor and the consensus peptide.	Heparin	219-226	von Willebrand factor	Homo sapiens	264-285
1315739-4	1992	All three inhibitors obeyed a ternary complex mechanism for heparin-enhanced thrombin inhibition, and the optimum heparin concentration was related to the apparent heparin affinity of the inhibitor.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	77-85
1577724-3	1992	In a fluid phase binding assay, the Tyr565-Ala587 peptide competed effectively with von Willebrand factor for binding heparin.	Heparin	118-125	von Willebrand factor	Homo sapiens	84-105
1315739-4	1992	All three inhibitors obeyed a ternary complex mechanism for heparin-enhanced thrombin inhibition, and the optimum heparin concentration was related to the apparent heparin affinity of the inhibitor.	Heparin	114-121	coagulation factor II, thrombin	Homo sapiens	77-85
1576116-5	1992	Continuous intravenous heparin infusion at a dose of 20,000 units/day, administered for 1 week to patients who had either received (n = 21) or not received (n = 17) streptokinase, led to a significant depression (p less than 0.05) of thrombin markers over the first 48 hours, an effect that did not persist over the subsequent days of treatment.	Heparin	23-30	coagulation factor II, thrombin	Homo sapiens	234-242
1590379-5	1992	Dexamethasone added in the presence of insulin increased heparin-releasable and total LPL activity approximately 8-fold but did not alter rates of LPL synthesis compared with insulin alone.	Heparin	57-64	insulin	Homo sapiens	39-46
1590376-2	1992	This effect of diabetes was rapidly reversed by in vivo treatment with insulin (5 U iv for 1 h); administration of insulin in vivo to control rats also increased heparin-releasable LPL activity.	Heparin	162-169	lipoprotein lipase	Rattus norvegicus	181-184
1590376-6	1992	Heparin- and decavanadate-induced release of LPL was not additive, and heparin pretreatment reduced the subsequent release of LPL by decavanadate.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	45-48
1590376-6	1992	Heparin- and decavanadate-induced release of LPL was not additive, and heparin pretreatment reduced the subsequent release of LPL by decavanadate.	Heparin	71-78	lipoprotein lipase	Rattus norvegicus	126-129
1590376-7	1992	Decavanadate displaced LPL bound to heparin-Sepharose and increased LPL release into the perfusate of hearts.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	23-26
1590376-8	1992	Therefore, decavanadate can mimic heparin in its effect on LPL.	Heparin	34-41	lipoprotein lipase	Rattus norvegicus	59-62
1590379-4	1992	At a maximal dose, insulin increased heparin-releasable and total LPL activity (approximately 7-fold) by specifically increasing the rate of LPL synthesis (approximately 5-fold) determined by pulse labeling with [35S]methionine and [35S]cysteine and immunoprecipitation.	Heparin	37-44	insulin	Homo sapiens	19-26
1569403-11	1992	DNA and heparin inhibited binding of CRP trimers to intact C1q, as well as to each peptide 14-26 and 76-92, suggesting involvement of these regions in C1q-CLR binding reactions generally.	Heparin	8-15	C-reactive protein	Homo sapiens	37-40
1505142-5	1992	Heparin produces its antithrombotic effect by binding to antithrombin III and this complex then binds to thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	61-69
1375562-9	1992	Prothrombin times (PT) were 21.9 +/- 3.0 s for control, 29.4 +/- 6.2 s for aprotinin, 40.7 +/- 2.5 s for heparin and 39.9 +/- 14.5 s for heparin + aprotinin (p less than 0.05 vs. control for all values).	Heparin	105-112	coagulation factor II	Rattus norvegicus	0-11
1375562-9	1992	Prothrombin times (PT) were 21.9 +/- 3.0 s for control, 29.4 +/- 6.2 s for aprotinin, 40.7 +/- 2.5 s for heparin and 39.9 +/- 14.5 s for heparin + aprotinin (p less than 0.05 vs. control for all values).	Heparin	137-144	coagulation factor II	Rattus norvegicus	0-11
1329253-7	1992	In dogs treated with t-PA associated to either heparin or enoxaparin, the thrombus weight was smaller (decreases of 34% and 44% respectively) than in animals given t-PA alone.	Heparin	47-54	tissue-type plasminogen activator	Canis lupus familiaris	21-25
1329253-10	1992	Plasma coagulation time was not modified by t-PA, but was slightly prolonged (2-fold) by enoxaparin and markedly (7-fold) by heparin on initiation of t-PA infusion.	Heparin	125-132	tissue-type plasminogen activator	Canis lupus familiaris	150-154
1329253-13	1992	In conclusion, these results indicate that enoxaparin, like heparin, enhances the thrombolytic effects of t-PA.	Heparin	60-67	tissue-type plasminogen activator	Canis lupus familiaris	106-110
1329253-8	1992	The plasma amidolytic activity, expressed as t-PA activity, was greater 15 min after the beginning of t-PA infusion, in dogs pretreated with either heparin or enoxaparin than in animals given t-PA alone.	Heparin	148-155	tissue-type plasminogen activator	Canis lupus familiaris	45-49
1329253-15	1992	Its mechanism may be the significant elevation of plasma t-PA activity produced by both heparin and enoxaparin during t-PA infusion.	Heparin	88-95	tissue-type plasminogen activator	Canis lupus familiaris	57-61
1329253-8	1992	The plasma amidolytic activity, expressed as t-PA activity, was greater 15 min after the beginning of t-PA infusion, in dogs pretreated with either heparin or enoxaparin than in animals given t-PA alone.	Heparin	148-155	tissue-type plasminogen activator	Canis lupus familiaris	102-106
1329253-15	1992	Its mechanism may be the significant elevation of plasma t-PA activity produced by both heparin and enoxaparin during t-PA infusion.	Heparin	88-95	tissue-type plasminogen activator	Canis lupus familiaris	118-122
1329253-8	1992	The plasma amidolytic activity, expressed as t-PA activity, was greater 15 min after the beginning of t-PA infusion, in dogs pretreated with either heparin or enoxaparin than in animals given t-PA alone.	Heparin	148-155	tissue-type plasminogen activator	Canis lupus familiaris	102-106
1315533-1	1992	We previously reported that heparin inhibits the proliferation of fibroblasts and vascular smooth muscle cells (SMC), in part, by binding to and increasing the antiproliferative activity of transforming growth factor-beta 1 (TGF-beta 1).	Heparin	28-35	transforming growth factor, beta 1	Rattus norvegicus	190-223
1412188-5	1992	Elevated thrombin-antithrombin III-complexes (TAT) despite adequate prolongation of aPTT under high dose heparin in 38.2% of patients indicate that therapeutic concentrations of heparin in these cases are insufficient for depressing this parameter completely.	Heparin	178-185	coagulation factor II, thrombin	Homo sapiens	9-17
1315533-1	1992	We previously reported that heparin inhibits the proliferation of fibroblasts and vascular smooth muscle cells (SMC), in part, by binding to and increasing the antiproliferative activity of transforming growth factor-beta 1 (TGF-beta 1).	Heparin	28-35	transforming growth factor, beta 1	Rattus norvegicus	225-235
1554734-2	1992	Heparin was fractionated according to its affinity for immobilized GDN, and the ability of various fractions to accelerate the inhibition rate of thrombin by either GDN or ATIII was examined.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	146-154
1315533-2	1992	We now report that certain other polyanions which are structurally distinct from heparin, such as fucoidan and polyinosinic acid, are more avid ligands for TGF-beta 1 and more potent antiproliferative agents than heparin.	Heparin	81-88	transforming growth factor, beta 1	Rattus norvegicus	156-166
1562725-7	1992	These results indicate that the interaction of TSP with the surface of activated platelets can be modulated at the level of a specific epitope located within the amino terminal heparin-binding domain of the molecule.	Heparin	177-184	thrombospondin 1	Homo sapiens	47-50
1562726-3	1992	Wild-type recombinant TFPI (rTFPI), expressed in mouse C127 cells, separates into two forms on heparin-agarose chromatography that elute at 0.3 mol/L and 0.6 mol/L NaCl.	Heparin	95-102	tissue factor pathway inhibitor	Mus musculus	22-26
1554734-4	1992	Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	84-92
1554734-4	1992	Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII.	Heparin	196-203	coagulation factor II, thrombin	Homo sapiens	84-92
1567914-11	1992	The effects of emulsion were quite different from those of heparin, which caused an immediate release of the lipase to plasma, decreased uptake of LPL in most extrahepatic tissues by 60-95%, and increased the fraction taken up in the liver.	Heparin	59-66	lipoprotein lipase	Rattus norvegicus	147-150
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	118-126
1313007-1	1992	The effective resolution of human platelet cytosolic phosphoinositide-phospholipase C (PLC) revealed five distinct activity peaks by Q-Sepharose and heparin-Sepharose column chromatographies when assayed using phosphatidylinositol (PI) and phosphatidylinositol 4,5-bisphosphate (PIP2).	Heparin	149-156	phospholipase C gamma 1	Homo sapiens	53-85
1313007-1	1992	The effective resolution of human platelet cytosolic phosphoinositide-phospholipase C (PLC) revealed five distinct activity peaks by Q-Sepharose and heparin-Sepharose column chromatographies when assayed using phosphatidylinositol (PI) and phosphatidylinositol 4,5-bisphosphate (PIP2).	Heparin	149-156	phospholipase C gamma 1	Homo sapiens	87-90
1551875-4	1992	The binding could be blocked by unlabeled heparin, dextran sulfate, and by a highly anionic benzylated synthetic peptide derived from human CD4 (amino acids 81-92).	Heparin	42-49	CD4 molecule	Homo sapiens	140-143
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	190-197	coagulation factor II, thrombin	Homo sapiens	118-126
1554734-7	1992	Fragment 63-144 was less effective in decreasing the heparin-accelerated rate of inhibition of thrombin by ATIII.	Heparin	53-60	coagulation factor II, thrombin	Homo sapiens	95-103
1554734-8	1992	The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	122-130
1638565-6	1992	To demonstrate the binding of EC-SOD C to the endothelium, heparin, which releases EC-SOD C from the endothelial surfaces, was added to the perfusate 30 min after initiation of reperfusion.	Heparin	59-66	superoxide dismutase 3	Homo sapiens	30-36
1555478-4	1992	Heparin administered intravenously appears to markedly attenuate the thrombin activity associated with thrombolysis and, in patients treated with tissue plasminogen activator (t-PA), prevents early recurrent coronary thrombosis.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	69-77
1638565-6	1992	To demonstrate the binding of EC-SOD C to the endothelium, heparin, which releases EC-SOD C from the endothelial surfaces, was added to the perfusate 30 min after initiation of reperfusion.	Heparin	59-66	superoxide dismutase 3	Homo sapiens	83-89
1552097-5	1992	After a 5,000-U intravenous dose of heparin given at the end of the infusion of rt-PA, concentrations of prothrombin fragment 1.2 decreased from 1.8 +/- 1.5 to 1.1 +/- 0.9 nM (n = 20, p less than 0.05), although values were still increased compared with concentrations before rt-PA.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	105-116
1547742-3	1992	Compared to sham-injected controls, heparin-releasable LPL activity and LPL mass in the dexamethasone-treated rats were 44% and 62% of those in control rats, respectively.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	55-58
1547742-8	1992	Dexamethasone decreased heparin-releasable LPL activity in cultured adipocytes to 40 +/- 6% of the control value (P less than 0.01).	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	43-46
1569928-15	1992	Direct interaction of polyanions with AT1 was suggested by the capacity of solubilized photoaffinity-labeled 125I-AT1 to adsorb to heparin-agarose gels.	Heparin	131-138	angiotensin II receptor type 1	Bos taurus	38-41
1569928-15	1992	Direct interaction of polyanions with AT1 was suggested by the capacity of solubilized photoaffinity-labeled 125I-AT1 to adsorb to heparin-agarose gels.	Heparin	131-138	angiotensin II receptor type 1	Bos taurus	114-117
1569928-16	1992	The adsorption of 125I-AT1 to heparin-agarose was inhibited by prior incubation of solubilized receptor with heparin or PVS.	Heparin	30-37	angiotensin II receptor type 1	Bos taurus	23-26
1569928-16	1992	The adsorption of 125I-AT1 to heparin-agarose was inhibited by prior incubation of solubilized receptor with heparin or PVS.	Heparin	109-116	angiotensin II receptor type 1	Bos taurus	23-26
1574077-1	1992	Basic fibroblast growth factor (bFGF) is a multifunctional, heparin-binding, mitogenic polypeptide found in all tissues or cells of multicellular organisms so far examined.	Heparin	60-67	fibroblast growth factor 2	Bos taurus	32-36
1378313-0	1992	Mediators of angiogenesis: the biological significance of basic fibroblast growth factor (bFGF)-heparin and heparan sulfate interactions.	Heparin	96-103	fibroblast growth factor 2	Homo sapiens	58-88
1614818-7	1992	These results provide direct evidence that single Ca-dependent K channel activity is regulated by the transmitters ACh and SP, as well as a second messenger, IP3, via the release of intracellular Ca from intracellular sites which are blocked by heparin.	Heparin	245-252	tachykinin precursor 1	Homo sapiens	123-125
1378313-0	1992	Mediators of angiogenesis: the biological significance of basic fibroblast growth factor (bFGF)-heparin and heparan sulfate interactions.	Heparin	96-103	fibroblast growth factor 2	Homo sapiens	90-94
1378313-2	1992	Heparin and heparan sulfate protect bFGF from inactivation by heat, extreme pH and protease degradation.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	36-40
1546950-0	1992	The N-terminal domain of antithrombin-III is essential for heparin binding and complex-formation with, but not cleavage by, alpha-thrombin.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	29-37
1556117-1	1992	Vascular endothelial growth factor (VEGF) induces the proliferation of endothelial cells and is a potent angiogenic factor that binds to heparin.	Heparin	137-144	vascular endothelial growth factor A	Homo sapiens	0-34
1556117-1	1992	Vascular endothelial growth factor (VEGF) induces the proliferation of endothelial cells and is a potent angiogenic factor that binds to heparin.	Heparin	137-144	vascular endothelial growth factor A	Homo sapiens	36-40
1556117-2	1992	We have therefore studied the effect of heparin upon the interaction of VEGF with its receptors.	Heparin	40-47	vascular endothelial growth factor A	Homo sapiens	72-76
1556117-3	1992	Heparin, at concentrations ranging from 0.1 to 10 micrograms/ml, strongly potentiated the binding of 125I-VEGF to its receptors on endothelial cells.	Heparin	0-7	vascular endothelial growth factor A	Homo sapiens	106-110
1556117-4	1992	Scatchard analysis of 125I-VEGF binding indicates that 1 microgram/ml heparin induces an 8-fold increase in the apparent density of high affinity binding sites for VEGF, but does not significantly affect the dissociation constant of VEGF.	Heparin	70-77	vascular endothelial growth factor A	Homo sapiens	27-31
1556117-4	1992	Scatchard analysis of 125I-VEGF binding indicates that 1 microgram/ml heparin induces an 8-fold increase in the apparent density of high affinity binding sites for VEGF, but does not significantly affect the dissociation constant of VEGF.	Heparin	70-77	vascular endothelial growth factor A	Homo sapiens	164-168
1556117-4	1992	Scatchard analysis of 125I-VEGF binding indicates that 1 microgram/ml heparin induces an 8-fold increase in the apparent density of high affinity binding sites for VEGF, but does not significantly affect the dissociation constant of VEGF.	Heparin	70-77	vascular endothelial growth factor A	Homo sapiens	164-168
1556117-5	1992	Cross-linking experiments showed that heparin strongly potentiates the formation of the 170-, 195- and 225-kDa 125I-VEGF-receptor complexes on endothelial cells.	Heparin	38-45	vascular endothelial growth factor A	Homo sapiens	116-120
1556117-6	1992	At high 125I-VEGF concentrations (4 ng/ml), heparin preferentially enhanced the formation of the 170- and 195-kDa complexes.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	13-17
1556117-7	1992	Preincubation of the cells with heparin, followed by extensive washes, produced a similar enhancement of subsequent 125I-VEGF binding.	Heparin	32-39	vascular endothelial growth factor A	Homo sapiens	121-125
1556117-8	1992	The binding of 125I-VEGF was completely inhibited following digestion of endothelial cells with heparinase and could be restored by the addition of exogenous heparin to the digested cells.	Heparin	96-103	vascular endothelial growth factor A	Homo sapiens	20-24
1556117-9	1992	The enhancing effect of heparin facilitated the detection of VEGF receptors on cell types that were not known previously to express such receptors.	Heparin	24-31	vascular endothelial growth factor A	Homo sapiens	61-65
1536567-0	1992	Binding of heparin to basic fibroblast growth factor induces a conformational change.	Heparin	11-18	fibroblast growth factor 2	Homo sapiens	22-52
1536567-1	1992	The binding of heparin to basic fibroblast growth factor (bFGF) induces a small but highly reproducible conformational change observable in the amide I region of the protein"s infrared spectrum.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	26-56
1536567-1	1992	The binding of heparin to basic fibroblast growth factor (bFGF) induces a small but highly reproducible conformational change observable in the amide I region of the protein"s infrared spectrum.	Heparin	15-22	fibroblast growth factor 2	Homo sapiens	58-62
1536567-5	1992	This spectroscopically observable change has allowed us to probe the functional determinants necessary for heparin to bind the bFGF and to induce the observed conformational change.	Heparin	107-114	fibroblast growth factor 2	Homo sapiens	127-131
1536567-8	1992	Further, heparin was observed to greatly increase the thermal stability of bFGF, raising the Tm by 25 degrees C. Sucrose octasulfate was also able to enhance the thermal stability of bFGF, but not to the same extent as heparin.	Heparin	9-16	fibroblast growth factor 2	Homo sapiens	75-79
1536567-8	1992	Further, heparin was observed to greatly increase the thermal stability of bFGF, raising the Tm by 25 degrees C. Sucrose octasulfate was also able to enhance the thermal stability of bFGF, but not to the same extent as heparin.	Heparin	9-16	fibroblast growth factor 2	Homo sapiens	183-187
1547341-11	1992	The minimal thrombin-complexing ability of the mutant AT-III protein that was observed was accelerated by heparin, but to subnormal levels.	Heparin	106-113	coagulation factor II, thrombin	Homo sapiens	12-20
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	136-144
1321995-4	1992	On the other hand, UF-heparin bound to F.Xa, thrombin and AT III with the strongest affinity to AT III followed by thrombin and F.Xa.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	45-53
1321995-4	1992	On the other hand, UF-heparin bound to F.Xa, thrombin and AT III with the strongest affinity to AT III followed by thrombin and F.Xa.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	115-123
1582991-7	1992	The mitogenic activity of the unretained serum fraction was restored by the addition of PDGF AA, AB, or BB dimers or of a fraction (RF I) that dissociated from Heparin-Sepharose at 0.2 to 0.6 M NaCl.	Heparin	160-167	ring finger protein 34	Homo sapiens	132-136
1597230-2	1992	A clinically relevant attenuation of the anticoagulant effect of a heparin bolus (40 U.kg-1) by a concomitant infusion of nitroglycerin (100 micrograms.min-1) was absent.	Heparin	67-74	CD59 molecule (CD59 blood group)	Homo sapiens	152-157
1582991-11	1992	Addition of heparin abolished DNA-synthesis when the PDGF dimers or RF I were combined with the unretained fraction.	Heparin	12-19	ring finger protein 34	Homo sapiens	68-72
1346414-2	1992	While heparin functions as an anticoagulant primarily by its ability to accelerate the action of the plasma protein inhibitor antithrombin III, dermatan sulphate acts selectively through a structurally related inhibitor, heparin co-factor II, to inhibit thrombin.	Heparin	6-13	coagulation factor II, thrombin	Homo sapiens	130-138
1540178-2	1992	VEGF was partially purified from the conditioned medium of transfected cells using heparin-sepharose affinity chromatography.	Heparin	83-90	vascular endothelial growth factor A	Homo sapiens	0-4
1540635-0	1992	Reversible unfolding of an isolated heparin and DNA binding fragment, the first type III module from fibronectin.	Heparin	36-43	fibronectin 1	Homo sapiens	101-112
1740413-2	1992	All of the thrombin derivatives were inhibited in a similar manner by AT, either in the absence or presence of heparin, which confirmed the integrity of both heparin binding abilities and serpin reactivities of epsilon- and gamma T-thrombin compared to alpha-thrombin.	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	11-19
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	203-211
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	255-263
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Heparin	102-109	CD59 molecule (CD59 blood group)	Homo sapiens	305-310
1740413-4	1992	Interestingly, in the presence of glycosaminoglycans the maximal inhibition rate constants by HC with heparin and dermatan sulfate, respectively, were as follows: 30.0 x 10(7) and 60.5 x 10(7) for alpha-thrombin, 14.6 x 10(7) and 24.3 x 10(7) for epsilon-thrombin, and 0.017 x 10(7) and 0.034 x 10(7) M-1 min-1 for gamma T-thrombin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	255-263
1740413-5	1992	A hirudin carboxyl-terminal peptide, which binds to anion-binding exosite-I of alpha-thrombin, dramatically reduced alpha-thrombin inhibition by HC in the presence of heparin but not in its absence.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	85-93
1740413-5	1992	A hirudin carboxyl-terminal peptide, which binds to anion-binding exosite-I of alpha-thrombin, dramatically reduced alpha-thrombin inhibition by HC in the presence of heparin but not in its absence.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	122-130
1536861-7	1992	Total binding of HDL3 was independent of divalent cations and was only slightly inhibited by heparin, but when the trypanosomes were preincubated with trypsin or pronase the binding was markedly reduced.	Heparin	93-100	HDL3	Homo sapiens	17-21
1586971-4	1992	The growth factor in the cells was purified and identified as a basic fibroblast growth factor (bFGF)--like factor on the basis of its elution profile on heparin-affinity chromatography and the result of immunoblotting.	Heparin	154-161	fibroblast growth factor 2	Homo sapiens	96-100
1733928-9	1992	83, 2797-2801) and were inhibited by low concentrations of heparin, an inhibitor of beta-adrenergic receptor kinase, (IC50 = 15 nM), suggesting that both mAChR and rhodopsin are phosphorylated by the same or very similar kinase(s) belonging to the beta-adrenergic receptor kinase family.	Heparin	59-66	rhodopsin	Homo sapiens	164-173
1539695-12	1992	Thus heparin enhances t-PA-induced thrombolysis and delays reocclusion.	Heparin	5-12	tissue-type plasminogen activator	Canis lupus familiaris	22-26
1367986-5	1992	bFGF was purified close to homogeneity using a Heparin-Sepharose column and Mono S cation exchange chromatography.	Heparin	47-54	fibroblast growth factor 2	Homo sapiens	0-4
1730778-0	1992	Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin.	Heparin	40-47	fibronectin 1	Homo sapiens	66-77
1730778-15	1992	Moreover, inhibition studies showed that binding of a lymphoblastoid cell line, KCA, to heparin binding peptides from COOH-terminal heparin binding fragment of fibronectin was mediated via CD44.	Heparin	88-95	fibronectin 1	Homo sapiens	160-171
1569376-3	1992	When compared to control rats, LPL activity, mass, and synthetic rate in hypothyroid rats were increased; heparin-releasable LPL activity and mass were increased to 448% and 300% of control, respectively, and [35S]methionine incorporation into LPL was increased to 250% of control.	Heparin	106-113	lipoprotein lipase	Rattus norvegicus	125-128
1569376-3	1992	When compared to control rats, LPL activity, mass, and synthetic rate in hypothyroid rats were increased; heparin-releasable LPL activity and mass were increased to 448% and 300% of control, respectively, and [35S]methionine incorporation into LPL was increased to 250% of control.	Heparin	106-113	lipoprotein lipase	Rattus norvegicus	125-128
1730728-6	1992	These two apoE variants were purified from cell lysates of the transfected Escherichia coli by ultracentrifugal flotation in the presence of phospholipid, by gel filtration chromatography, and by heparin-Sepharose chromatography.	Heparin	196-203	apolipoprotein E	Homo sapiens	10-14
1730728-10	1992	The mutation at residue 142 decreased the binding activity of apoE to both heparin and the monoclonal antibody 1D7 (this antibody inhibits receptor binding of apoE), whereas apoE2(Arg158----Cys), which is associated with recessive expression of type III hyperlipoproteinemia, binds normally to both.	Heparin	75-82	apolipoprotein E	Homo sapiens	62-66
1730729-0	1992	Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor.	Heparin	85-92	coagulation factor II, thrombin	Homo sapiens	18-26
1315989-2	1992	Since unfractionated heparin was reported to enhance fibrinogen binding to platelets responsible for the hyperaggregating effect of this drug, the purpose of this work was to determine whether or not heparin could also modulate platelet interaction to whole blood clot.	Heparin	21-28	fibrinogen beta chain	Homo sapiens	53-63
1579892-1	1992	Using biochemically defined conditions on a fast kinetic centrifugal analyzer the effect of recombinant hirudin (rH) and unfractionated heparin (UH) on thrombin and factor Xa generation was investigated.	Heparin	136-143	coagulation factor II, thrombin	Homo sapiens	152-160
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	32-40
1319617-2	1992	Both HRG and PF4 effectively neutralized the ability of heparin to accelerate the activated protein C (APC) and the thrombin inhibitions by protein C inhibitor (PCI).	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	116-124
1739751-6	1992	Whole liver perfusion experiments showed that the heparin-releasable HL activity in fenofibrate-treated livers dropped to 10% the activity in control livers.	Heparin	50-57	lipase C, hepatic type	Rattus norvegicus	69-71
1730217-2	1992	Heparin and dermatan sulfate prolong the lag phases associated with the activation of the three proteins by catalyzing the inhibition of endogenously generated thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	160-168
1730217-4	1992	The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III.	Heparin	25-32	coagulation factor II, thrombin	Homo sapiens	50-58
1279952-3	1992	(2) Heparin and its related polysaccharides stabilize bFGF and other growth factors.	Heparin	4-11	fibroblast growth factor 2	Homo sapiens	54-58
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	HDL3	Homo sapiens	141-145
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	HDL3	Homo sapiens	317-321
1729878-8	1992	Thrombin antagonism and platelet inhibition, primarily with heparin and aspirin, respectively, form the mainstay of conjunctive therapy.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	0-8
1279952-4	1992	(3) FGFs and thrombospondin are stored in the extracellular matrix bound to heparan sulfate; fragments of heparin or heparan sulfate may act as natural chaperones to shuttle bFGF or other growth factors to different cellular compartments.	Heparin	106-113	fibroblast growth factor 2	Homo sapiens	174-178
1466276-1	1992	High molecular weight kininogen (HK) or its procoagulant light-chain but not the heavy chain potentiated the heparin enhancement of antithrombin III inactivation of plasma kallikrein and factor XIa from 10-50-fold to approximately 1000-fold at I 0.15, pH 7.4, 25 degrees C. This potentiation resulted in antithrombin becoming a predominant inhibitor of kallikrein and factor XIa in heparinized normal but not HK-deficient plasmas.	Heparin	109-116	kininogen 1	Homo sapiens	0-36
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	140-148
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	187-195
1466276-1	1992	High molecular weight kininogen (HK) or its procoagulant light-chain but not the heavy chain potentiated the heparin enhancement of antithrombin III inactivation of plasma kallikrein and factor XIa from 10-50-fold to approximately 1000-fold at I 0.15, pH 7.4, 25 degrees C. This potentiation resulted in antithrombin becoming a predominant inhibitor of kallikrein and factor XIa in heparinized normal but not HK-deficient plasmas.	Heparin	109-116	kininogen 1	Homo sapiens	33-35
1466276-2	1992	The heparin chain-length and salt dependence of this potentiation suggested an anticoagulant action of HK analogous to its procoagulant action.	Heparin	4-11	kininogen 1	Homo sapiens	103-105
1592056-3	1992	The production of TNF in freshly drawn LPS stimulated blood in heparin, drawn from top athletes at rest was significantly lower than in the other subjects.	Heparin	63-70	tumor necrosis factor	Homo sapiens	18-21
1290382-3	1992	Drugs like heparin and vitamin K antagonists act because they inhibit thrombin formation.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	70-78
1290382-8	1992	It is shown that, contrary to current belief, low molecular weight heparins inhibit primarily via their action on thrombin and that the inhibition of factor Xa is of less importance.	Heparin	67-75	coagulation factor II, thrombin	Homo sapiens	114-122
1382772-6	1992	aFGF alone accelerated lesion coverage and this effect was enhanced by 40% over control values when heparin was added with aFGF.	Heparin	100-107	fibroblast growth factor 1	Homo sapiens	0-4
1306684-0	1992	Interaction of heparin-binding EGF-like growth factor (HB-EGF) with the epidermal growth factor receptor: modulation by heparin, heparinase, or synthetic heparin-binding HB-EGF fragments.	Heparin	15-22	epidermal growth factor receptor	Homo sapiens	72-104
1306684-4	1992	To map potential regions in the HB-EGF molecule that mediate its heparin-dependent interaction with the EGF receptor, HB-EGF peptides were synthesized that were non-homologous to EGF.	Heparin	65-72	epidermal growth factor receptor	Homo sapiens	104-116
1738372-3	1992	Epinephrine yielded a dose-dependent decrease in LPL activity; heparin-releasable LPL activity was reduced to 66% of control values after exposure to 10(-5) M epinephrine for 2 h. However, there was no effect of epinephrine on LPL immunoreactive mass, as measured by enzyme-linked immunosorbent assay.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	49-52
1728444-16	1992	Paradoxically, there appears to be an increase in ST shift and worsening of myocardial perfusion with t-PA compared with therapy with heparin alone.	Heparin	134-141	plasminogen activator, tissue type	Homo sapiens	102-106
1282947-2	1992	DNA synthesis was increased by fetal calf serum (10%) in SD cells more than in TGR VSMCs, and was decreased by heparin (400 micrograms/ml) and by phorbol-12,13-dibutyrate (10(-7) M) in TGR VSMCs to a higher degree than in SD cells.	Heparin	111-118	thioredoxin reductase 3	Mus musculus	185-188
1608022-4	1992	The arterial samples showed a significantly elevated APTT and thrombin time compared with venous samples, especially when the heparin level in the sample was higher than 0.1 IU/ml.	Heparin	126-133	coagulation factor II, thrombin	Homo sapiens	62-70
1379965-7	1992	Compared to heparin, which is a strong inhibitor of thrombin generation, Orgaran has only moderate inhibitory effects on thrombin generation.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	52-60
1552484-0	1992	Decrease in calmodulin concentrations during heparin-induced capacitation in bovine spermatozoa.	Heparin	45-52	calmodulin	Bos taurus	12-22
1552484-2	1992	Heparin reduced sperm CaM concentrations in a dose-dependent manner corresponding with an increase in in-vitro fertilization rates.	Heparin	0-7	calmodulin	Bos taurus	22-25
1738372-3	1992	Epinephrine yielded a dose-dependent decrease in LPL activity; heparin-releasable LPL activity was reduced to 66% of control values after exposure to 10(-5) M epinephrine for 2 h. However, there was no effect of epinephrine on LPL immunoreactive mass, as measured by enzyme-linked immunosorbent assay.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	82-85
1738372-3	1992	Epinephrine yielded a dose-dependent decrease in LPL activity; heparin-releasable LPL activity was reduced to 66% of control values after exposure to 10(-5) M epinephrine for 2 h. However, there was no effect of epinephrine on LPL immunoreactive mass, as measured by enzyme-linked immunosorbent assay.	Heparin	63-70	lipoprotein lipase	Rattus norvegicus	82-85
1529628-3	1992	Despite the administration of high doses of heparin during the fibrinolysis thrombin is formed, measured as thrombin-antithrombin III complex (TAT).	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	76-84
1553257-1	1992	While making use of the inside-out membrane patch, we examined the effects of caffeine and heparin on unitary currents of the large conductance Ca(2+)-dependent K+ (maxi-K+) channel in the rabbit portal vein.	Heparin	91-98	calcium-activated potassium channel subunit alpha-1	Oryctolagus cuniculus	165-181
1529628-3	1992	Despite the administration of high doses of heparin during the fibrinolysis thrombin is formed, measured as thrombin-antithrombin III complex (TAT).	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	108-116
1441296-4	1992	After administration of thrombin 3 NIH in content of protein C was decreased to 91.3% whereas heparin was released only after injection of 6 NIH.	Heparin	94-101	coagulation factor II	Rattus norvegicus	24-32
1534954-2	1992	Some papers report that the effect of heparin-mediated extracorporeal LDL less than cholesterol, LP(a), triglycerides, fibrinogen greater than precipitation (H.E.L.P.)	Heparin	38-45	fibrinogen beta chain	Homo sapiens	119-129
1764042-2	1991	Activated thrombin was separated from other components in a single step by taking advantage of its highly specific affinity to heparin immobilized on a matrix support of Sepharose CL-6B.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	10-18
1552484-3	1992	Such reductions were observed after heparin treatment for 4-6 h, which is in agreement with the length of the capacitation period in bulls and was concomitant with an increase in CaM concentration in the incubation medium, suggesting translocation of CaM from the spermatozoa to the surrounding milieu.	Heparin	36-43	calmodulin	Bos taurus	179-182
1552484-3	1992	Such reductions were observed after heparin treatment for 4-6 h, which is in agreement with the length of the capacitation period in bulls and was concomitant with an increase in CaM concentration in the incubation medium, suggesting translocation of CaM from the spermatozoa to the surrounding milieu.	Heparin	36-43	calmodulin	Bos taurus	251-254
1752960-0	1991	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	49-56	tumor necrosis factor	Homo sapiens	18-39
1721064-3	1991	In contrast, the endothelial cell mitogen, heparin-binding (acidic fibroblast) growth factor-1 (HBGF-1) inhibits the synthesis of prostacyclin in HUVEC.	Heparin	43-50	fibroblast growth factor 1	Homo sapiens	96-102
1721064-7	1991	Further, HBGF-1, in the presence of heparin, down-regulates the levels of the Cox transcript in a dose- and time-dependent manner.	Heparin	36-43	fibroblast growth factor 1	Homo sapiens	9-15
1721051-4	1991	When heparin, inositol hexasulfate, or sulfate ion are present, aFGF refolds below 30 degrees C with a slightly reduced activation energy (10-11 kcal/mol).	Heparin	5-12	fibroblast growth factor 1	Homo sapiens	64-68
1962651-1	1991	The present studies were undertaken to determine whether treatment with recombinant human erythropoietin (epoetin beta [Marogen Sterile Powder, Chugai-Upjohn, Rosemont, IL] ) necessitates an alteration in dialysis prescription or in heparin requirements.	Heparin	233-240	erythropoietin	Homo sapiens	90-104
1752960-0	1991	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	49-56	tumor necrosis factor	Homo sapiens	41-44
1752960-0	1991	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	113-120	tumor necrosis factor	Homo sapiens	18-39
1752960-0	1991	On the binding of tumor necrosis factor (TNF) to heparin and the release in vivo of the TNF-binding protein I by heparin.	Heparin	113-120	tumor necrosis factor	Homo sapiens	88-91
1752960-6	1991	The finding of a repeated release of TNF-BP-I into the circulation with intermittent injections of heparin indicates that TNF-BP-I is present both in a storage pool and in a circulating pool.	Heparin	99-106	tumor necrosis factor	Homo sapiens	37-40
1752960-6	1991	The finding of a repeated release of TNF-BP-I into the circulation with intermittent injections of heparin indicates that TNF-BP-I is present both in a storage pool and in a circulating pool.	Heparin	99-106	tumor necrosis factor	Homo sapiens	122-125
1752960-7	1991	The mechanism for the heparin-mediated release of TNF-BP-I was not explained; TNF-BP did not show affinity for heparin.	Heparin	22-29	tumor necrosis factor	Homo sapiens	50-53
1752960-8	1991	On the other hand, TNF was found to have affinity for heparin and it could also be dissociated from heparin by TNF-BP-I.	Heparin	54-61	tumor necrosis factor	Homo sapiens	19-22
1752960-8	1991	On the other hand, TNF was found to have affinity for heparin and it could also be dissociated from heparin by TNF-BP-I.	Heparin	100-107	tumor necrosis factor	Homo sapiens	19-22
1752960-8	1991	On the other hand, TNF was found to have affinity for heparin and it could also be dissociated from heparin by TNF-BP-I.	Heparin	100-107	tumor necrosis factor	Homo sapiens	111-114
1752960-9	1991	It is suggested that heparin-like molecules of the extracellular matrix can retain TNF in physical proximity with target cells and restrict the actions of TNF and protect against systemic harmful manifestations.	Heparin	21-28	tumor necrosis factor	Homo sapiens	83-86
1752960-9	1991	It is suggested that heparin-like molecules of the extracellular matrix can retain TNF in physical proximity with target cells and restrict the actions of TNF and protect against systemic harmful manifestations.	Heparin	21-28	tumor necrosis factor	Homo sapiens	155-158
1774011-8	1991	These findings suggest that the increase in thrombin activity affects unfavorably the patency of IRAs in the evolving of myocardial infarction, and that the responsiveness of endothelial cells to acute phase stimuli such as thrombin and heparin affects favorably the patency of IRAs in the chronic phase; Elevated plasma levels of D-dimer do not necessarily indicate coronary thrombolysis.	Heparin	237-244	coagulation factor II, thrombin	Homo sapiens	44-52
1819694-2	1991	Lipoprotein lipase (LPL) activity was enhanced by intravenous injection of PAF before intravenous injection of heparin when the PAF dose was low (0.2 micrograms/kg).	Heparin	111-118	lipoprotein lipase	Rattus norvegicus	0-18
1819694-2	1991	Lipoprotein lipase (LPL) activity was enhanced by intravenous injection of PAF before intravenous injection of heparin when the PAF dose was low (0.2 micrograms/kg).	Heparin	111-118	lipoprotein lipase	Rattus norvegicus	20-23
1763597-1	1991	Heparin has been suggested as an activator of the plasma kallikrein-kinin system, with possible formation of bradykinin, a potent vasodilator.	Heparin	0-7	kininogen 1	Homo sapiens	109-119
1718494-10	1991	On the addition of heparin (0.4 U/mL) to plasma, all four types of plasma inhibited thrombin to the same extent.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	84-92
1834252-10	1991	Further mapping of this new functional domain of vWF, based on experiments of competitive inhibition of binding by either heparin or monoclonal antibodies directed toward vWF, showed that the site interacting with sulfatides is distinct from those involved in binding to platelet glycoprotein Ib, collagen, or heparin.	Heparin	122-129	von Willebrand factor	Homo sapiens	49-52
1834252-10	1991	Further mapping of this new functional domain of vWF, based on experiments of competitive inhibition of binding by either heparin or monoclonal antibodies directed toward vWF, showed that the site interacting with sulfatides is distinct from those involved in binding to platelet glycoprotein Ib, collagen, or heparin.	Heparin	310-317	von Willebrand factor	Homo sapiens	49-52
1662323-6	1991	Apolipoprotein B decreased during the 6 months LMWH-period continuously, while Apolipoprotein A1 rapidly decreased during the first two months and then stabilized at a lower level.	Heparin	47-51	apolipoprotein B	Homo sapiens	0-16
1939083-3	1991	Dermatan sulfate and heparin increase the rate of inhibition of thrombin, but not of chymotrypsin, greater than 1000-fold.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	64-72
1939083-9	1991	However, deletion of residues 1-67 (first acidic repeat) or 1-74 (first and second acidic repeats) greatly decreased the rate of inhibition of alpha-thrombin in the presence of heparin, dermatan sulfate, or a dermatan sulfate hexasaccharide that comprises the minimum high-affinity binding site for HCII.	Heparin	177-184	coagulation factor II, thrombin	Homo sapiens	149-157
1918053-1	1991	A heparin binding, cell adhesion promoting domain, termed peptide F-9, from the B1 chain of human laminin, residues 641 to 660, i.e. RYVVLPRPVCFEKGMNYTVR, has been investigated by 1H NMR (500 MHz) spectroscopy and CD spectropolarimetry.	Heparin	2-9	coagulation factor IX	Homo sapiens	66-69
1918053-7	1991	These midchain reversals include the lysine and asparagine residues proposed to be involved in heparin binding and N-glycosylation, respectively, to laminin peptide F-9.	Heparin	95-102	coagulation factor IX	Homo sapiens	165-168
1918055-5	1991	A competition study of the binding using heparin derivatives demonstrated that follistatin seemed to recognize O-sulfate groups in the heparin molecule.	Heparin	41-48	follistatin	Rattus norvegicus	79-90
1918055-5	1991	A competition study of the binding using heparin derivatives demonstrated that follistatin seemed to recognize O-sulfate groups in the heparin molecule.	Heparin	135-142	follistatin	Rattus norvegicus	79-90
1811347-0	1991	Interference of heparin and analogues with hirudin in the chromogenic thrombin substrate assay.	Heparin	16-23	coagulation factor II, thrombin	Homo sapiens	70-78
1928066-7	1991	IgA-fibronectin aggregates also were detected in serum using an antifibronectin antibody capture assay; and could be depleted from serum by heparin-agarose affinity chromatography.	Heparin	140-147	fibronectin 1	Homo sapiens	4-15
1930145-1	1991	The secretory enzyme extracellular superoxide dismutase (EC-SOD) is in plasma heterogenous with regard to heparin-affinity and can be divided into three fractions, A that lacks affinity, B with intermediate affinity and C with high affinity.	Heparin	106-113	superoxide dismutase 3	Homo sapiens	21-55
1928350-1	1991	Fasted 1-day-old rat liver has high heparin-releasable (endothelial) lipoprotein lipase (LPL) activity, and its hepatocytes synthesize LPL protein.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	69-87
1928350-1	1991	Fasted 1-day-old rat liver has high heparin-releasable (endothelial) lipoprotein lipase (LPL) activity, and its hepatocytes synthesize LPL protein.	Heparin	36-43	lipoprotein lipase	Rattus norvegicus	89-92
1930145-1	1991	The secretory enzyme extracellular superoxide dismutase (EC-SOD) is in plasma heterogenous with regard to heparin-affinity and can be divided into three fractions, A that lacks affinity, B with intermediate affinity and C with high affinity.	Heparin	106-113	superoxide dismutase 3	Homo sapiens	57-63
1930145-10	1991	The findings suggest that glycation is one of the factors that contribute to the heterogeneity in heparin-affinity of plasma EC-SOD.	Heparin	98-105	superoxide dismutase 3	Homo sapiens	125-131
1918380-5	1991	The reduction was apparent during co-incubations as short as 2 h and as long as 24 h. Heparin, which blocks receptor-mediated binding of lipoproteins, abolished the effect of LpL on apo B output, without causing enzyme inhibition.	Heparin	86-93	apolipoprotein B	Homo sapiens	182-187
1658403-8	1991	We conclude that recombinant thrombomodulin inhibits venous thrombosis in a rat model with less prolongation of activated partial thromboplastin time and bleeding time than heparin or hirudin.	Heparin	173-180	thrombomodulin	Rattus norvegicus	29-43
1833087-11	1991	However, inhibition of thrombin with heparin, hirudin, or D-Phe-D-Pro-L-Arg-chloromethylketone was more effective in inhibiting the acceleration of platelet activation induced by plasminogen activation, despite the elaboration of plasmin activity.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	23-31
1666391-2	1991	The anti-thrombin activity of LHG measured by the prolongation of activated partial thromboplastin time and thrombin time and measured by the suppressive effect on thrombin-induced mortality was approximately 4 times weaker than those of Heparin on a weight basis, while the anti-Xa activity of LHG measured by the chromogenic method was approximately half of that of Heparin.	Heparin	238-245	coagulation factor II	Rattus norvegicus	9-17
1955380-6	1991	The tumor cell interaction with CH-271-substrate was inhibited by heparin, and monoclonal antibodies (IST-1 or IST-2) against the heparin-binding domain of fibronectin.	Heparin	130-137	fibronectin 1	Homo sapiens	156-167
1666391-2	1991	The anti-thrombin activity of LHG measured by the prolongation of activated partial thromboplastin time and thrombin time and measured by the suppressive effect on thrombin-induced mortality was approximately 4 times weaker than those of Heparin on a weight basis, while the anti-Xa activity of LHG measured by the chromogenic method was approximately half of that of Heparin.	Heparin	368-375	coagulation factor II	Rattus norvegicus	9-17
1663665-2	1991	With the help of a combined assay method heparin characterization is made possible using the TAT/XAT quotient under consideration of the simultaneous inhibition of the two serine proteases thrombin and factor Xa by antithrombin III.	Heparin	41-48	coagulation factor II, thrombin	Homo sapiens	189-197
1666460-3	1991	Since 1978, there have been several reports about reversible elevation in serum values of AST and ALT in patients and healthy volunteers given heparin in small and high doses.	Heparin	143-150	solute carrier family 17 member 5	Homo sapiens	90-93
1665594-0	1991	Low molecular weight heparin-catalyzed inactivation of factor Xa and thrombin by antithrombin III--effect of platelet factor 4.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	69-77
1759273-8	1991	The aPTT and thrombin time are, as in human beings, suited for the control of a heparin therapy.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	13-21
1716458-8	1991	Binding of both intact [125I]EC-TSP and of the 125I-labeled 70-kDa fragment was inhibited by unlabeled TSP, heparin, fibronectin (FN), monoclonal anti-TSP antibody directed against the 70-kDa fragment (B7-3), and by full serum, but not by heparin-absorbed serum or the cell-adhesion peptide GRGDS.	Heparin	108-115	thrombospondin 1	Homo sapiens	32-35
1665594-3	1991	Pseudo-first order rate constants of inactivation of factor Xa and thrombin by antithrombin III were determined as function of heparin concentration, in the presence of 4.0 mM CaCl2.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	67-75
1665594-6	1991	Analysis of CY216 subfractions, obtained by gel filtration, showed that the heparin molecules of the upper region of the molecular weight distribution are responsible for the anti-thrombin, but also to a large extent for the anti-factor Xa activities.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	180-188
1665594-8	1991	PF4-dependent neutralization of anti-factor Xa and anti-thrombin activities of fixed concentrations of the LMW heparins was studied by measuring rate constants as function of PF4 concentration.	Heparin	111-119	coagulation factor II, thrombin	Homo sapiens	56-64
1716989-0	1991	Potentiation of the activity of mouse liver-derived HBGF-1-like growth factor by heparin and dithiothreitol: evidence for the involvement of a plasma factor.	Heparin	81-88	fibroblast growth factor 1	Mus musculus	52-58
1716989-1	1991	The potentiation of mouse liver derived heparin binding growth factors 1 and 2 (HBGF-1, HBGF-2) activity has been investigated.	Heparin	40-47	fibroblast growth factor 1	Mus musculus	80-86
1716989-2	1991	It was found that both heparin and various sulfhydryl reagents (such as dithiothreitol, DTT) markedly potentiated HBGF-1 activity, but not HBGF-2 activity.	Heparin	23-30	fibroblast growth factor 1	Mus musculus	114-120
1716989-5	1991	When assayed in the absence of plasma, both heparin and DTT were required to reactivate plasma inactivated HBGF-1-ML.	Heparin	44-51	fibroblast growth factor 1	Mus musculus	107-113
1746001-6	1991	An extra inhibitory effect of heparin over the mixture is observed in situations where free factor IXa, not bound to factor VIIIa and phospholipid, limits the rate of thrombin formation, notably in contact activated plasma.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	167-175
1892820-0	1991	Heparin prevents the binding of phospholipase A2 to phospholipid micelles: importance of the amino-terminus.	Heparin	0-7	phospholipase A2, major isoenzyme	Sus scrofa	32-48
1892820-1	1991	The activity of the major isoform of porcine pancreatic phospholipase A2 (PLA2), designated B-PLA2, against micellar substrates is inhibited by heparin.	Heparin	144-151	phospholipase A2, major isoenzyme	Sus scrofa	56-72
1892820-1	1991	The activity of the major isoform of porcine pancreatic phospholipase A2 (PLA2), designated B-PLA2, against micellar substrates is inhibited by heparin.	Heparin	144-151	phospholipase A2, major isoenzyme	Sus scrofa	74-78
1892820-1	1991	The activity of the major isoform of porcine pancreatic phospholipase A2 (PLA2), designated B-PLA2, against micellar substrates is inhibited by heparin.	Heparin	144-151	phospholipase A2, major isoenzyme	Sus scrofa	94-98
1892820-2	1991	Inhibition is a consequence of binding of the enzyme to heparin, documented by a heparin-induced alteration in the intrinsic fluorescence of B-PLA2 and in the 8-anilino-1-naphthalene sulfonate fluorescence and by the enhanced rate of chemical modification of the active site residue His-48.	Heparin	56-63	phospholipase A2, major isoenzyme	Sus scrofa	143-147
1892820-2	1991	Inhibition is a consequence of binding of the enzyme to heparin, documented by a heparin-induced alteration in the intrinsic fluorescence of B-PLA2 and in the 8-anilino-1-naphthalene sulfonate fluorescence and by the enhanced rate of chemical modification of the active site residue His-48.	Heparin	81-88	phospholipase A2, major isoenzyme	Sus scrofa	143-147
1892820-3	1991	As a consequence of heparin binding, the conformation of B-PLA2 at the active site and at the amino-terminus is altered, and the enzyme does not bind to phospholipid micelles.	Heparin	20-27	phospholipase A2, major isoenzyme	Sus scrofa	59-63
1892820-4	1991	In spite of the heparin-induced conformational changes, B-PLA2 retains its ability to catalyze the hydrolysis of monomeric phospholipid.	Heparin	16-23	phospholipase A2, major isoenzyme	Sus scrofa	58-62
1892820-7	1991	A peptide corresponding to the amino-terminal 26 residues of B-PLA2 can rescue PLA2 from heparin inhibition.	Heparin	89-96	phospholipase A2, major isoenzyme	Sus scrofa	63-67
1892820-7	1991	A peptide corresponding to the amino-terminal 26 residues of B-PLA2 can rescue PLA2 from heparin inhibition.	Heparin	89-96	phospholipase A2, major isoenzyme	Sus scrofa	79-83
1892820-9	1991	A model for the inhibition of B-PLA2 by heparin is proposed in which the catalytically significant effect of heparin is to interact directly with the amino-terminus of B-PLA2, the interfacial recognition site, to prevent the enzyme from binding to micellar substrates.	Heparin	40-47	phospholipase A2, major isoenzyme	Sus scrofa	32-36
1892820-9	1991	A model for the inhibition of B-PLA2 by heparin is proposed in which the catalytically significant effect of heparin is to interact directly with the amino-terminus of B-PLA2, the interfacial recognition site, to prevent the enzyme from binding to micellar substrates.	Heparin	40-47	phospholipase A2, major isoenzyme	Sus scrofa	170-174
1892820-9	1991	A model for the inhibition of B-PLA2 by heparin is proposed in which the catalytically significant effect of heparin is to interact directly with the amino-terminus of B-PLA2, the interfacial recognition site, to prevent the enzyme from binding to micellar substrates.	Heparin	109-116	phospholipase A2, major isoenzyme	Sus scrofa	32-36
1892820-9	1991	A model for the inhibition of B-PLA2 by heparin is proposed in which the catalytically significant effect of heparin is to interact directly with the amino-terminus of B-PLA2, the interfacial recognition site, to prevent the enzyme from binding to micellar substrates.	Heparin	109-116	phospholipase A2, major isoenzyme	Sus scrofa	170-174
1885605-2	1991	This protein, designated HBp17, was found to bind the heparin-binding peptide growth factors HBGF-1 and HBGF-2 in a noncovalent, reversible manner.	Heparin	54-61	fibroblast growth factor 1	Homo sapiens	93-99
1885605-2	1991	This protein, designated HBp17, was found to bind the heparin-binding peptide growth factors HBGF-1 and HBGF-2 in a noncovalent, reversible manner.	Heparin	54-61	fibroblast growth factor 2	Homo sapiens	104-110
1885605-4	1991	Both the binding and inactivation of HBGF-1 and HBGF-2 by HBp17 were abolished by heparin.	Heparin	82-89	fibroblast growth factor 1	Homo sapiens	37-43
1885605-4	1991	Both the binding and inactivation of HBGF-1 and HBGF-2 by HBp17 were abolished by heparin.	Heparin	82-89	fibroblast growth factor 2	Homo sapiens	48-54
1780805-2	1991	Heparin affects the binding of hirudin to alpha-thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	48-56
1780805-5	1991	Heparin and dextran sulfate substantially reduced hirudin binding to thrombin in human plasma.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	69-77
1780805-6	1991	Inhibition by heparin was restored by addition of increasing amounts of antithrombin (AT) to samples containing constant amounts of heparin, thrombin and 125I-r.hirudin and was not neutralized by protamine sulfate.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	76-84
1780805-6	1991	Inhibition by heparin was restored by addition of increasing amounts of antithrombin (AT) to samples containing constant amounts of heparin, thrombin and 125I-r.hirudin and was not neutralized by protamine sulfate.	Heparin	132-139	coagulation factor II, thrombin	Homo sapiens	76-84
1780806-3	1991	The results in specimens collected in an anticoagulant containing ACD, EDTA, adenosine, and 25 U/ml of heparin (a) were highly correlated with those collected in an anticoagulant containing a synthetic thrombin inhibitor, EDTA, and aprotinin (b).	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	202-210
1746001-1	1991	We investigated whether the inactivation of factor IXa contributes to the partial inhibition of thrombin formation that is observed at therapeutic concentrations of heparin.	Heparin	165-172	coagulation factor II, thrombin	Homo sapiens	96-104
1746001-2	1991	The action of standard unfractionated heparin (0.05 U/ml) on thrombin formation in the intrinsic system was compared to that of a mixture of dermatan sulfate (DS) and a synthetic pentasaccharide (PS).	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	61-69
1746001-7	1991	We conclude that the inactivation of free factor IXa by heparin contributes importantly to the inhibition of thrombin formation in the intrinsic system such as e.g. measured in the activated partial thromboplastin time.	Heparin	56-63	coagulation factor II, thrombin	Homo sapiens	109-117
1882186-3	1991	We then characterized the interacting fragments on both molecules and found that under physiological conditions of pH and ionic strength both heavy and light chain of all multiple myeloma and normal IgG showed affinity to FN; the active fragment on FN was found to be the aminoterminal heparin-binding domain.	Heparin	286-293	fibronectin 1	Homo sapiens	222-224
1756438-0	1991	Does heparin inhibit renin activity?	Heparin	5-12	renin	Homo sapiens	21-26
1756438-1	1991	Although heparin was reported in the 1960s to inhibit renin activity, this has not always been confirmed by other investigators.	Heparin	9-16	renin	Homo sapiens	54-59
1875056-0	1991	Human keratinocytes adhere to two distinct heparin-binding synthetic peptides derived from fibronectin.	Heparin	43-50	fibronectin 1	Homo sapiens	91-102
1875058-6	1991	Supernatants from melanocyte cultures stimulated with either IL-1 alpha or TNF alpha and separated on a heparin-Sepharose column became positive for neutrophil and monocyte chemotactic activity in a dose- and time-dependent fashion.	Heparin	104-111	tumor necrosis factor	Homo sapiens	75-84
1875168-4	1991	(b) Primitive LTBMC-IC and multi-lineage CFU-MIX progenitors adhere to the 33/66 kD COOH-terminal heparin-binding cell-adhesion promoting fragment of fibronectin, but adhere significantly less to its 75 kD RGDS-dependent cell-binding fragment.	Heparin	98-105	fibronectin 1	Homo sapiens	150-161
1665089-7	1991	The ESR results show that heparin or high salt induces an increase in the domainal flexibility in both SH1 and SH2 regions, perhaps through the disruption of domain-domain interactions in the fibronectin molecule, and that the former is more effective than the latter in producing such an effect.	Heparin	26-33	fibronectin 1	Homo sapiens	192-203
1715220-5	1991	Our results show that: (1) Heparin exclusively increases the rate of inhibition of thrombin by PAI-1, whereas in the presence of heparin the rate of inhibition of the other proteases is not altered; (2) Vitronectin is an obligatory cofactor for the inhibition of thrombin by PAI-1.	Heparin	27-34	coagulation factor II, thrombin	Homo sapiens	83-91
1715572-12	1991	The factor dependence of these cells could be switched from interleukin 3 to FGF in the presence of heparin.	Heparin	100-107	interleukin 3	Mus musculus	60-73
1661447-0	1991	Standard heparin but not LMW heparin induces a concomitant increase of t-PA and PAI-1 without modification of global fibrinolysis: study after 60 days treatment.	Heparin	9-16	plasminogen activator, tissue type	Homo sapiens	71-75
1882186-3	1991	We then characterized the interacting fragments on both molecules and found that under physiological conditions of pH and ionic strength both heavy and light chain of all multiple myeloma and normal IgG showed affinity to FN; the active fragment on FN was found to be the aminoterminal heparin-binding domain.	Heparin	286-293	fibronectin 1	Homo sapiens	249-251
1875911-8	1991	Furthermore, the Ca2+ signals elicited by both bradykinin and epidermal growth factor were blocked in cells microinjected with the inositol 1,4,5-trisphosphate receptor antagonist heparin, whereas the intracellular Ca(2+)-ATPase inhibitor thapsigargin still mobilized Ca2+.	Heparin	180-187	kininogen 1	Homo sapiens	47-57
1768765-5	1991	In contrast modified thrombin, heparin-protected modified thrombin retained the ability to bind to GPIb, indicating that the lysyl residue(s) protected by heparin from the modification are essential for GPIb binding.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	58-66
1768765-5	1991	In contrast modified thrombin, heparin-protected modified thrombin retained the ability to bind to GPIb, indicating that the lysyl residue(s) protected by heparin from the modification are essential for GPIb binding.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	58-66
1768765-6	1991	While unprotected modified thrombin failed to bind hirudin, heparin-protected modified thrombin retained its ability to bind the carboxy-terminal hirudin peptide H54-65.	Heparin	60-67	coagulation factor II, thrombin	Homo sapiens	87-95
1768765-7	1991	Tritium-labelling of the modified lysyl residues and degradation of modified thrombins by CNBr or trypsin confirmed that the lysyl residue(s) protected by heparin and essential for GPIb binding are located in the thrombin binding domain for the carboxyl-terminal tail of hirudin, within the sequence 18-73 of the thrombin B chain.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	77-85
1768765-7	1991	Tritium-labelling of the modified lysyl residues and degradation of modified thrombins by CNBr or trypsin confirmed that the lysyl residue(s) protected by heparin and essential for GPIb binding are located in the thrombin binding domain for the carboxyl-terminal tail of hirudin, within the sequence 18-73 of the thrombin B chain.	Heparin	155-162	coagulation factor II, thrombin	Homo sapiens	213-221
1716876-0	1991	The structure of human acidic fibroblast growth factor and its interaction with heparin.	Heparin	80-87	fibroblast growth factor 1	Homo sapiens	23-54
2071579-0	1991	Heparin influence on the complex of serum amyloid P component and complement C4b-binding protein.	Heparin	0-7	complement component 4 binding protein alpha	Homo sapiens	77-96
1907203-4	1991	Results from earlier studies suggest that surface located segments of apo B-100 are responsible for the interaction of LDL with heparin and chondroitin sulphate-rich arterial proteoglycans.	Heparin	128-135	apolipoprotein B	Homo sapiens	70-79
2070077-0	1991	Purification and properties of heparin-releasable lipoprotein-associated coagulation inhibitor.	Heparin	31-38	tissue factor pathway inhibitor	Oryctolagus cuniculus	50-94
1715234-3	1991	The angiogenic activity in the RMT-1 conditioned medium was separated into two fractions on a column of heparin-Sepharose; one was eluted with 0.1 M NaCl and the other with 0.5 M NaCl, which are referred to hereafter as rAF-1 and rAF-2, respectively.	Heparin	104-111	small integral membrane protein 38	Rattus norvegicus	31-36
1865126-9	1991	U-EPX was purified by a two step procedure involving affinity chromatography on heparin Sepharose and size exclusion chromatography on Sephadex G-50 superfine.	Heparin	80-87	eosinophil peroxidase	Homo sapiens	2-5
1712815-7	1991	There were 1.5 x 10(3) heparin-inhibitable binding sites/cell with an apparent Kd of 8 nM that represented approximately 60% of the TSP-specific sites.	Heparin	23-30	thrombospondin 1	Homo sapiens	132-135
1712815-8	1991	Therefore, two distinct TSP receptors appeared to exist on unactivated PMN; one interacting with the heparin-binding domain of TSP and one interacting with a different site.	Heparin	101-108	thrombospondin 1	Homo sapiens	24-27
1712815-8	1991	Therefore, two distinct TSP receptors appeared to exist on unactivated PMN; one interacting with the heparin-binding domain of TSP and one interacting with a different site.	Heparin	101-108	thrombospondin 1	Homo sapiens	127-130
1712815-15	1991	The existence of a subset of TSP receptors that were heparin-inhibitable on PMN suggests that binding of TSP may trigger functionally independent responses.	Heparin	53-60	thrombospondin 1	Homo sapiens	29-32
1712815-15	1991	The existence of a subset of TSP receptors that were heparin-inhibitable on PMN suggests that binding of TSP may trigger functionally independent responses.	Heparin	53-60	thrombospondin 1	Homo sapiens	105-108
2070077-1	1991	The lipoprotein-associated coagulation inhibitor (LACI) is present in vivo in at least three different pools: sequestered in platelets, associated with plasma lipoproteins, and released into plasma by intravenous heparin, possibly from vascular endothelium.	Heparin	213-220	tissue factor pathway inhibitor	Oryctolagus cuniculus	4-48
2070077-1	1991	The lipoprotein-associated coagulation inhibitor (LACI) is present in vivo in at least three different pools: sequestered in platelets, associated with plasma lipoproteins, and released into plasma by intravenous heparin, possibly from vascular endothelium.	Heparin	213-220	tissue factor pathway inhibitor	Oryctolagus cuniculus	50-54
2070077-2	1991	In this study we have purified the heparin-relesable form of LACI from post-heparin plasma and show that it is structurally different from lipoprotein LACI.	Heparin	35-42	tissue factor pathway inhibitor	Oryctolagus cuniculus	61-65
2070077-2	1991	In this study we have purified the heparin-relesable form of LACI from post-heparin plasma and show that it is structurally different from lipoprotein LACI.	Heparin	76-83	tissue factor pathway inhibitor	Oryctolagus cuniculus	61-65
2071579-2	1991	this study demonstrated that heparin interacted with SAP in a calcium-dependent manner and prevented formation of the SAP.C4BP complex.	Heparin	29-36	complement component 4 binding protein alpha	Homo sapiens	122-126
2070077-4	1991	Heparin-releasable LACI (HRL), as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, under reducing conditions, appears as a major band at 40 Kd and a minor band at 36 Kd.	Heparin	0-7	tissue factor pathway inhibitor	Oryctolagus cuniculus	19-23
2070078-0	1991	Thrombin regulation of platelet interaction with damaged vessel wall and isolated collagen type I at arterial flow conditions in a porcine model: effects of hirudins, heparin, and calcium chelation.	Heparin	167-174	coagulation factor II, thrombin	Homo sapiens	0-8
2071579-13	1991	Dissociation of the SAP.C4BP complex by sulfated polysaccharides such as heparin may be a physiological response that could be important during tissue damage or complement activation.	Heparin	73-80	complement component 4 binding protein alpha	Homo sapiens	24-28
2070078-11	1991	Our study indicates that local thrombin generation at the site of severe injury will induce platelet activation and deposition even in the presence of average therapeutic heparin levels that inhibit blood coagulation.	Heparin	171-178	coagulation factor II, thrombin	Homo sapiens	31-39
2054354-1	1991	Thrombospondin (TSP) is a 450-kDa glycoprotein that is comprised of three identical disulfide-bonded subunits (1152 amino acids) held together near the heparin-binding amino-terminal globular domains.	Heparin	152-159	thrombospondin 1	Homo sapiens	0-14
2054354-1	1991	Thrombospondin (TSP) is a 450-kDa glycoprotein that is comprised of three identical disulfide-bonded subunits (1152 amino acids) held together near the heparin-binding amino-terminal globular domains.	Heparin	152-159	thrombospondin 1	Homo sapiens	16-19
2059236-3	1991	Because the release of monocyte-derived neutrophil chemotactic activity was markedly diminished by pretreatment of the monocytes with cycloheximide, and was completely removed from conditioned media by adsorption to heparin-agarose, we addressed the possibility that monocyte-derived neutrophil chemotactic factor/interleukin-8 (IL-8), a heparin-binding neutrophil-activating polypeptide, might modulate these activities.	Heparin	216-223	C-X-C motif chemokine ligand 8	Homo sapiens	329-333
2069469-0	1991	Formation of C5a during cardiopulmonary bypass: inhibition by precoating with heparin.	Heparin	78-85	complement C5a receptor 1	Homo sapiens	13-16
2069469-3	1991	Coating of the extracorporeal circuit with end-point-attached heparin completely abolished C5a formation in vitro during circulation of blood through the circuit for 120 minutes.	Heparin	62-69	complement C5a receptor 1	Homo sapiens	91-94
2069469-8	1991	We conclude that heparin coating improves biocompatibility by completely abolishing C5a formation in vitro.	Heparin	17-24	complement C5a receptor 1	Homo sapiens	84-87
1865106-5	1991	Basic fibroblast growth factor (bFGF) is a heparin binding growth factor which is involved in angiogenesis and also has neurite promoting activity.	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	0-30
1787232-2	1991	Single or chronic (7-8 days) per os administration to white rats of 0.1% solution of the heparin/acetylsalicylate complex (0.3 ml/200 g body weight) enhanced anticoagulative properties of blood plasma, increased the fibrinolytic activity in respect of stabilized fibrin, and diminished the thrombin-induced platelet aggregation.	Heparin	89-96	coagulation factor II	Rattus norvegicus	290-298
1839080-4	1991	Heparin stabilized surface u-PA activity during plasminogen activation, and we propose that a heparin binding site exists in the kringle structure of u-PA.	Heparin	0-7	proline rich acidic protein 1	Homo sapiens	27-31
1865106-5	1991	Basic fibroblast growth factor (bFGF) is a heparin binding growth factor which is involved in angiogenesis and also has neurite promoting activity.	Heparin	43-50	fibroblast growth factor 2	Homo sapiens	32-36
1839080-4	1991	Heparin stabilized surface u-PA activity during plasminogen activation, and we propose that a heparin binding site exists in the kringle structure of u-PA.	Heparin	0-7	proline rich acidic protein 1	Homo sapiens	150-154
1926336-2	1991	Release of HS-bound bFGF by heparin-like molecules and HS-degrading enzymes (i.e., heparanase) provides a novel mechanism for regulation of the growth of capillary blood vessels in normal and pathological situations.	Heparin	28-35	fibroblast growth factor 2	Homo sapiens	20-24
1839080-4	1991	Heparin stabilized surface u-PA activity during plasminogen activation, and we propose that a heparin binding site exists in the kringle structure of u-PA.	Heparin	94-101	proline rich acidic protein 1	Homo sapiens	150-154
1839080-5	1991	Heparin at 40 micrograms/ml could reduce u-PA loss to only 20% compared with 60% on control cells activating plasminogen.	Heparin	0-7	proline rich acidic protein 1	Homo sapiens	41-45
2039549-7	1991	A distinct heparin-unreleasable MAGL appears to exist in heart, that could be ethanol-insensitive.	Heparin	11-18	monoglyceride lipase	Rattus norvegicus	32-36
2050700-5	1991	TNF-treated endothelial cell monolayers exposed to blood anticoagulated with low molecular weight heparin induced activation of coagulation.	Heparin	98-105	tumor necrosis factor	Homo sapiens	0-3
1926059-4	1991	Thrombin generation was significantly inhibited by DS and heparin as compared to placebo.	Heparin	58-65	coagulation factor II, thrombin	Homo sapiens	0-8
1902471-1	1991	Heparin cofactor II (HC) is a plasma serine proteinase inhibitor (serpin) that inhibits alpha-thrombin in a reaction that is dramatically enhanced by heparin and other glycosaminoglycans/polyanions.	Heparin	150-157	coagulation factor II, thrombin	Homo sapiens	94-102
2036431-4	1991	Substitution of aspartic acid-19 by arginine in the first heparin-binding domain yielded a molecule that stimulated a higher total mitogenic response in fibroblasts as compared to bFGF.	Heparin	58-65	fibroblast growth factor 2	Homo sapiens	180-184
2036431-11	1991	We conclude that changes in all three of the putative heparin-binding domains result in altered mitogenic activity and heparin interaction of basic fibroblast growth factor.	Heparin	54-61	fibroblast growth factor 2	Bos taurus	142-172
1864390-8	1991	These changes were more pronounced in the two emergency cases, except for the heparin induced changes in PTT and thrombin time.	Heparin	78-85	coagulation factor II, thrombin	Homo sapiens	113-121
1750669-2	1991	The biotinylated bFGF derivatives, bio-bFGF.20 and bio-bFGF.200, conserved the same affinity for heparin as native bFGF, in contrast to bio-FGF.2000 which lost this property.	Heparin	97-104	fibroblast growth factor 2	Bos taurus	17-21
2066361-4	1991	High amounts of bFGF and heparin increased the initial rate of diffusion by displacement of bFGF bound to matrigel.	Heparin	25-32	fibroblast growth factor 2	Homo sapiens	92-96
2066361-7	1991	These results indicate that modulation of bFGF distribution in a tissue by a basement membrane is dependent on bFGF concentration, basement membrane composition, permeability of associated cells, and local presence of heparin.	Heparin	218-225	fibroblast growth factor 2	Homo sapiens	42-46
1902404-2	1991	BACKGROUND: This study addressed the need for heparin administration to be continued for more than 24 hours after coronary thrombolysis with recombinant tissue-type plasminogen activator (rt-PA).	Heparin	46-53	plasminogen activator, tissue type	Homo sapiens	153-186
1864486-6	1991	Heparin injection appeared to activate lipoprotein lipase in the diabetic rats by showing a marked fall in serum triglyceride and total low density lipoprotein levels but not in pseudocholinesterase activity.	Heparin	0-7	lipoprotein lipase	Rattus norvegicus	39-57
2022745-1	1991	The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels.	Heparin	34-41	von Willebrand factor	Homo sapiens	175-196
1710230-6	1991	The mitogens extracted from cell lysates and from the ECM are closely related to aFGF or bFGF by the criteria that they bind to heparin-sepharose and elute at 1.1 M (aFGF) or 1.5 M (bFGF) NaCl, have molecular weights of about 18,000, and react with anti-aFGF (1.1 M), or anti-bFGF (1.5 M) antibodies when analyzed by Western blots and by radioimmunoassay specific for aFGF and bFGF.	Heparin	128-135	fibroblast growth factor 2	Bos taurus	89-93
2061622-7	1991	In adherent cell-depleted murine and human marrow cultures, the addition of B-FGF possessed synergistic activity in combination with the optimal concentration of GM-CSF for CFU-gm at a dose of 10 ng/ml which was inhibited in the presence of protamine sulfate (LD50 dose, 100 mu gm/ml), an inhibitor of B-FGF mitogenic activity, or in the presence of heparin (LD50 dose, 100 U/ml), an effective B-FGF binding agent.	Heparin	350-357	fibroblast growth factor 2	Homo sapiens	76-81
2022745-1	1991	The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels.	Heparin	34-41	von Willebrand factor	Homo sapiens	300-321
2022745-1	1991	The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels.	Heparin	34-41	von Willebrand factor	Homo sapiens	323-326
2022745-1	1991	The intravenous administration of heparin to patients before open heart surgery reduced ristocetin cofactor activity by 58% (P less than 0.01, t test), and this impairment of von Willebrand factor-dependent platelet function was closely related to plasma heparin levels (r2 = 0.9), but not to plasma von Willebrand factor (vWF) levels.	Heparin	255-262	von Willebrand factor	Homo sapiens	175-196
2022745-2	1991	We hypothesized that heparin may inhibit vWF-dependent platelet hemostatic functions by directly binding vWF in solution and interfering with vWF-GpIb binding.	Heparin	21-28	von Willebrand factor	Homo sapiens	41-44
2022745-2	1991	We hypothesized that heparin may inhibit vWF-dependent platelet hemostatic functions by directly binding vWF in solution and interfering with vWF-GpIb binding.	Heparin	21-28	von Willebrand factor	Homo sapiens	105-108
2022745-2	1991	We hypothesized that heparin may inhibit vWF-dependent platelet hemostatic functions by directly binding vWF in solution and interfering with vWF-GpIb binding.	Heparin	21-28	von Willebrand factor	Homo sapiens	105-108
2022745-3	1991	Using the in vitro techniques of ristocetin-induced platelet agglutination, fluorescent flow cytometric measurement of vWF-platelet binding, and conventional radioligand binding assays we observed that heparin inhibited both vWF-dependent platelet function and vWF-platelet binding in a parallel and dose-dependent manner.	Heparin	202-209	von Willebrand factor	Homo sapiens	119-122
2022745-3	1991	Using the in vitro techniques of ristocetin-induced platelet agglutination, fluorescent flow cytometric measurement of vWF-platelet binding, and conventional radioligand binding assays we observed that heparin inhibited both vWF-dependent platelet function and vWF-platelet binding in a parallel and dose-dependent manner.	Heparin	202-209	von Willebrand factor	Homo sapiens	225-228
2022745-3	1991	Using the in vitro techniques of ristocetin-induced platelet agglutination, fluorescent flow cytometric measurement of vWF-platelet binding, and conventional radioligand binding assays we observed that heparin inhibited both vWF-dependent platelet function and vWF-platelet binding in a parallel and dose-dependent manner.	Heparin	202-209	von Willebrand factor	Homo sapiens	225-228
2019790-1	1991	Three recent studies have reported that fibrin in solution significantly inhibits the ability of heparin to catalyze the inhibition of thrombin by antithrombin III.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	135-143
2019790-2	1991	In addition, heparin inhibits the release of fibrinopeptide A by clot-bound thrombin less effectively than it inhibits the release of fibrinopeptide A by thrombin in solution.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	76-84
2019790-2	1991	In addition, heparin inhibits the release of fibrinopeptide A by clot-bound thrombin less effectively than it inhibits the release of fibrinopeptide A by thrombin in solution.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	154-162
2019790-4	1991	Because the results of these studies suggest that fibrin inhibits the reactivity of thrombin with antithrombin III-heparin but not with heparin cofactor II-dermatan sulfate, we compared the relative catalytic effects of heparin and dermatan sulfate on thrombin inhibition in plasma, both in the presence and absence of fibrin.	Heparin	115-122	coagulation factor II, thrombin	Homo sapiens	84-92
2022745-4	1991	Heparin also inhibited platelet agglutination induced by bovine vWF and inhibited the binding of human asialo-vWF to platelets in ristocetin-free systems.	Heparin	0-7	von Willebrand factor	Bos taurus	64-67
2022745-4	1991	Heparin also inhibited platelet agglutination induced by bovine vWF and inhibited the binding of human asialo-vWF to platelets in ristocetin-free systems.	Heparin	0-7	von Willebrand factor	Homo sapiens	110-113
2022745-6	1991	Heparin impairment of vWF function may explain why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin.	Heparin	85-92	von Willebrand factor	Homo sapiens	22-25
2022745-6	1991	Heparin impairment of vWF function may explain why some hemorrhagic complications of heparin therapy are not predictable based on techniques for monitoring the conventional anticoagulant effects of heparin.	Heparin	198-205	von Willebrand factor	Homo sapiens	22-25
2052362-5	1991	Heparin efficiently inhibited the p53 associated protein kinase whereas the polyamine spermidine stimulated enzymatic activity.	Heparin	0-7	tumor protein p53	Homo sapiens	34-37
2019604-0	1991	Localization of the major heparin-binding site in fibronectin.	Heparin	26-33	fibronectin 1	Homo sapiens	50-61
2019604-1	1991	We have identified the major site required for the interaction of fibronectin (FN) with heparin.	Heparin	88-95	fibronectin 1	Homo sapiens	66-77
1717176-6	1991	From P30 to adulthood a constant value of 2.5 ng/mg was measured, aFGF content in the different brain extracts was further characterized by its affinity for heparin-Sepharose, its elution at 1 M NaCl from this column and its capacity to induce thymidine incorporation in quiescent fibroblasts.	Heparin	157-164	fibroblast growth factor 1	Mus musculus	66-70
1708387-10	1991	In addition, these experiments indicate that Lp(a) may regulate fibrinolysis by competing with PAI-1 and plasminogen for fibrinogen- and heparin-bound t-PA.	Heparin	137-144	plasminogen activator, tissue type	Homo sapiens	151-155
1708387-7	1991	Previous studies demonstrated that Lp(a) competes with plasminogen for the active site of fibrinogen- and heparin-bound t-PA.	Heparin	106-113	plasminogen activator, tissue type	Homo sapiens	120-124
1708387-9	1991	The data suggest that fibrinogen and heparin may enhance the rate of inhibition through an interaction with t-PA, and that vitronectin may enhance the inhibition through an interaction with PAI-1.	Heparin	37-44	plasminogen activator, tissue type	Homo sapiens	108-112
1707539-9	1991	bFGF is the more active of the two factors and shows marked long-term (20-hr) survival-promoting activity alone, whereas aFGF requires heparin for long-term activity.	Heparin	135-142	fibroblast growth factor 1	Mus musculus	121-125
2009092-7	1991	MK-733 significantly (P less than 0.05) increased LPL activity in the post-heparin plasma by 21.5%, although it did not affect hepatic triacylglycerol lipase (H-TGL) activity.	Heparin	75-82	lipoprotein lipase	Rattus norvegicus	50-53
2007587-2	1991	Equilibrium binding of human alpha-thrombin to heparin was investigated at pH 7.4 as a function of thrombin and heparin concentrations, NaCl concentration, temperature, and heparin chain length with the extrinsic fluorescence probe, p-aminobenzamidine, or by quantitative affinity chromatography, in order to distinguish between sequence-specific and nonspecific electrostatic modes of binding.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	35-43
1901881-1	1991	The present study investigates the regulatory effects of glycosaminoglycans such as heparin and heparan sulfate on T cell proliferation induced by thymic stromal cell monolayer or its derived T cell growth factor (TCGF).	Heparin	84-91	interleukin 2	Homo sapiens	192-212
1901881-1	1991	The present study investigates the regulatory effects of glycosaminoglycans such as heparin and heparan sulfate on T cell proliferation induced by thymic stromal cell monolayer or its derived T cell growth factor (TCGF).	Heparin	84-91	interleukin 2	Homo sapiens	214-218
1901881-5	1991	A similar growth-inhibiting effect of heparin was observed in IL-7-dependent proliferation of pre-B cell line or Th, but not in IL-2-dependent T cell proliferation or IL-3-dependent myeloid cell proliferation.	Heparin	38-45	interleukin 7	Homo sapiens	62-66
1901881-6	1991	A strong affinity of TSTGF and IL-7 for heparin was confirmed by the fact that both TSTGF and IL-7 adhered to columns of heparin-agarose and were eluted by salt.	Heparin	40-47	interleukin 7	Homo sapiens	31-35
1901881-6	1991	A strong affinity of TSTGF and IL-7 for heparin was confirmed by the fact that both TSTGF and IL-7 adhered to columns of heparin-agarose and were eluted by salt.	Heparin	40-47	interleukin 7	Homo sapiens	94-98
1901881-6	1991	A strong affinity of TSTGF and IL-7 for heparin was confirmed by the fact that both TSTGF and IL-7 adhered to columns of heparin-agarose and were eluted by salt.	Heparin	121-128	interleukin 7	Homo sapiens	31-35
1901881-6	1991	A strong affinity of TSTGF and IL-7 for heparin was confirmed by the fact that both TSTGF and IL-7 adhered to columns of heparin-agarose and were eluted by salt.	Heparin	121-128	interleukin 7	Homo sapiens	94-98
1901881-8	1991	These results indicate that the activity of thymic and/or bone marrow stroma-derived lymphocyte growth factor (TSTGF/IL-7) but not of Th-producing TCGF (IL-2) is negatively regulated by heparin or heparan sulfate, which would represent major glycosaminoglycans in the extra-cellular matrix of stromal cells.	Heparin	186-193	interleukin 7	Homo sapiens	117-121
1849658-4	1991	Analysis of the three-dimensional structure in light of functional studies of bFGF suggests that the receptor binding site and the positively charged heparin binding site correspond to adjacent but separate loci on the beta-barrel.	Heparin	150-157	fibroblast growth factor 2	Homo sapiens	78-82
2007588-5	1991	Equilibrium binding and kinetic studies of the binary complex interactions as a function of salt concentration indicated a similar large ionic component for thrombin-heparin and AT-heparin interactions, but a predominantly nonionic contribution to the thrombin-AT interaction.	Heparin	166-173	coagulation factor II, thrombin	Homo sapiens	157-165
2007588-6	1991	Stopped-flow kinetic studies of ternary complex formation under conditions where heparin was always saturated with AT demonstrated that the ternary complex was assembled primarily from free thrombin and AT-heparin binary complex at all salt concentrations.	Heparin	81-88	coagulation factor II, thrombin	Homo sapiens	190-198
2007588-7	1991	Moreover, the ternary complex interaction of thrombin with AT bound to heparin exhibited a substantial ionic component similar to that of the thrombin-heparin binary complex interaction.	Heparin	71-78	coagulation factor II, thrombin	Homo sapiens	45-53
2007588-7	1991	Moreover, the ternary complex interaction of thrombin with AT bound to heparin exhibited a substantial ionic component similar to that of the thrombin-heparin binary complex interaction.	Heparin	151-158	coagulation factor II, thrombin	Homo sapiens	142-150
2007588-8	1991	Comparison of the ionic and nonionic components of thrombin binary and ternary complex interactions indicated that: 1) additive contributions of ionic thrombin-heparin and nonionic thrombin-AT binary complex interactions completely accounted for the binding energy of the thrombin ternary complex interaction, and 2) the heparin-induced AT conformational change made a relatively insignificant contribution to this binding energy.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	151-159
2007588-8	1991	Comparison of the ionic and nonionic components of thrombin binary and ternary complex interactions indicated that: 1) additive contributions of ionic thrombin-heparin and nonionic thrombin-AT binary complex interactions completely accounted for the binding energy of the thrombin ternary complex interaction, and 2) the heparin-induced AT conformational change made a relatively insignificant contribution to this binding energy.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	151-159
2007588-8	1991	Comparison of the ionic and nonionic components of thrombin binary and ternary complex interactions indicated that: 1) additive contributions of ionic thrombin-heparin and nonionic thrombin-AT binary complex interactions completely accounted for the binding energy of the thrombin ternary complex interaction, and 2) the heparin-induced AT conformational change made a relatively insignificant contribution to this binding energy.	Heparin	160-167	coagulation factor II, thrombin	Homo sapiens	151-159
2007588-9	1991	The results thus suggest that heparin promotes the encounter of thrombin and AT primarily by approximating the proteinase and inhibitor on the polysaccharide surface.	Heparin	30-37	coagulation factor II, thrombin	Homo sapiens	64-72
2007588-10	1991	Evidence was further obtained for alternative modes of thrombin binding to the AT-heparin complex, either with or without the active site of the enzyme complexed with AT.	Heparin	82-89	coagulation factor II, thrombin	Homo sapiens	55-63
2007588-11	1991	This finding is consistent with the ternary complex encounter of thrombin and AT being mediated by thrombin binding to nonspecific heparin sites, followed by diffusion along the heparin surface to a unique site adjacent to the bound inhibitor.	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	65-73
2007588-11	1991	This finding is consistent with the ternary complex encounter of thrombin and AT being mediated by thrombin binding to nonspecific heparin sites, followed by diffusion along the heparin surface to a unique site adjacent to the bound inhibitor.	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	99-107
2007588-11	1991	This finding is consistent with the ternary complex encounter of thrombin and AT being mediated by thrombin binding to nonspecific heparin sites, followed by diffusion along the heparin surface to a unique site adjacent to the bound inhibitor.	Heparin	178-185	coagulation factor II, thrombin	Homo sapiens	65-73
2007587-3	1991	Analysis of binding data by a nonspecific binding model developed for protein-nucleic acid interactions, or by the discrete binding site model previously used to analyze the thrombin-heparin interaction, indicated that both models described the binding interaction equally well over the range of thrombin binding densities accessible to measurement.	Heparin	183-190	coagulation factor II, thrombin	Homo sapiens	174-182
2007587-4	1991	However, the strong dependence of the thrombin-heparin binding interaction on NaCl concentration, its minimal dependence on temperature, and the increase in apparent binding affinity with increasing heparin oligosaccharide chain length were best accounted for by a nonspecific electrostatic association of thrombin with 5 to 6 anionic residues contained in a 3-disaccharide binding site of heparin.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	38-46
2007587-4	1991	However, the strong dependence of the thrombin-heparin binding interaction on NaCl concentration, its minimal dependence on temperature, and the increase in apparent binding affinity with increasing heparin oligosaccharide chain length were best accounted for by a nonspecific electrostatic association of thrombin with 5 to 6 anionic residues contained in a 3-disaccharide binding site of heparin.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	306-314
2007587-4	1991	However, the strong dependence of the thrombin-heparin binding interaction on NaCl concentration, its minimal dependence on temperature, and the increase in apparent binding affinity with increasing heparin oligosaccharide chain length were best accounted for by a nonspecific electrostatic association of thrombin with 5 to 6 anionic residues contained in a 3-disaccharide binding site of heparin.	Heparin	199-206	coagulation factor II, thrombin	Homo sapiens	38-46
2007587-6	1991	Although the nonspecific binding model satisfactorily described the binding of thrombin to heparin chains ranging in size from 3 to approximately 13 disaccharides in terms of a single intrinsic KD,obs, deviations from this model were apparent with longer heparin chains (approximately 22 to approximately 35 disaccharides) from a progressive decrease in the intrinsic KD,obs of up to 4-fold.	Heparin	91-98	coagulation factor II, thrombin	Homo sapiens	79-87
2007587-6	1991	Although the nonspecific binding model satisfactorily described the binding of thrombin to heparin chains ranging in size from 3 to approximately 13 disaccharides in terms of a single intrinsic KD,obs, deviations from this model were apparent with longer heparin chains (approximately 22 to approximately 35 disaccharides) from a progressive decrease in the intrinsic KD,obs of up to 4-fold.	Heparin	255-262	coagulation factor II, thrombin	Homo sapiens	79-87
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	38-46
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	107-115
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	107-115
1905550-0	1991	Effects of monoclonal antibodies on tissue-type plasminogen activator (t-PA) binding to lysine, fibrin and heparin and on fibrin-mediated enhancement of one-chain t-PA amidolytic activity.	Heparin	107-114	plasminogen activator, tissue type	Homo sapiens	71-75
1883625-2	1991	Heparin added to whole blood at a concentration of 1 U/ml prevented thrombin-induced secretion of granule contents and irreversible aggregation of platelets.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	68-76
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	47-54	coagulation factor II, thrombin	Homo sapiens	107-115
1905550-1	1991	The effects of 4 monoclonal antibodies against human tissue-type plasminogen activator (t-PA) on binding of t-PA to lysine, fibrin, and heparin, and on fibrin-mediated activation of one-chain t-PA-amidolytic activity were investigated.	Heparin	136-143	plasminogen activator, tissue type	Homo sapiens	53-86
1905550-1	1991	The effects of 4 monoclonal antibodies against human tissue-type plasminogen activator (t-PA) on binding of t-PA to lysine, fibrin, and heparin, and on fibrin-mediated activation of one-chain t-PA-amidolytic activity were investigated.	Heparin	136-143	plasminogen activator, tissue type	Homo sapiens	88-92
1905550-1	1991	The effects of 4 monoclonal antibodies against human tissue-type plasminogen activator (t-PA) on binding of t-PA to lysine, fibrin, and heparin, and on fibrin-mediated activation of one-chain t-PA-amidolytic activity were investigated.	Heparin	136-143	plasminogen activator, tissue type	Homo sapiens	108-112
1905550-1	1991	The effects of 4 monoclonal antibodies against human tissue-type plasminogen activator (t-PA) on binding of t-PA to lysine, fibrin, and heparin, and on fibrin-mediated activation of one-chain t-PA-amidolytic activity were investigated.	Heparin	136-143	plasminogen activator, tissue type	Homo sapiens	108-112
1905550-6	1991	Binding of t-PA to heparin is only moderately affected by the 4 antibodies.	Heparin	19-26	plasminogen activator, tissue type	Homo sapiens	11-15
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	38-46
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	107-115
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	107-115
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	107-115
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	38-46
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	107-115
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	107-115
2007587-7	1991	Sedimentation equilibrium analyses of thrombin-heparin complexes suggested a second weaker binding site on thrombin for heparin, which accounted for these deviations as well as the observed insolubility of thrombin-heparin complexes at high thrombin binding densities.	Heparin	120-127	coagulation factor II, thrombin	Homo sapiens	107-115
2007588-0	1991	Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	102-110
2007588-2	1991	Heparin has been shown to accelerate the inactivation of alpha-thrombin by antithrombin III (AT) by promoting the initial encounter of proteinase and inhibitor in a ternary thrombin-AT-heparin complex.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	63-71
2007588-2	1991	Heparin has been shown to accelerate the inactivation of alpha-thrombin by antithrombin III (AT) by promoting the initial encounter of proteinase and inhibitor in a ternary thrombin-AT-heparin complex.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	79-87
2007588-3	1991	The aim of the present work was to evaluate the relative contributions of an AT conformational change induced by heparin and of a thrombin-heparin interaction to the promotion by heparin of the thrombin-AT interaction in this ternary complex.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	130-138
2015674-2	1991	The interference seems to be caused by fibrinogen, which, in the presence of heparin, produces an almost constant increase of the measuring signal over the whole range of suitable wavelengths (550 to 700 nm).	Heparin	77-84	fibrinogen beta chain	Homo sapiens	39-49
2007588-3	1991	The aim of the present work was to evaluate the relative contributions of an AT conformational change induced by heparin and of a thrombin-heparin interaction to the promotion by heparin of the thrombin-AT interaction in this ternary complex.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	194-202
2007588-3	1991	The aim of the present work was to evaluate the relative contributions of an AT conformational change induced by heparin and of a thrombin-heparin interaction to the promotion by heparin of the thrombin-AT interaction in this ternary complex.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	130-138
2007588-3	1991	The aim of the present work was to evaluate the relative contributions of an AT conformational change induced by heparin and of a thrombin-heparin interaction to the promotion by heparin of the thrombin-AT interaction in this ternary complex.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	194-202
1706340-1	1991	Acidic fibroblast growth factor (aFGF) is a broad spectrum mitogen that is stabilized by complexation with heparin and heparan proteoglycans.	Heparin	107-114	fibroblast growth factor 1	Homo sapiens	0-31
1849269-1	1991	A recombinant deletion mutant of the 155-amino acid form of human basic fibroblast growth factor (bFGF), lacking amino acid residues 27-32 (Lys-Asp-Pro-Lys-Arg-Leu), was expressed in Escherichia coli and purified to homogeneity by heparin-Sepharose affinity chromatography.	Heparin	231-238	fibroblast growth factor 2	Homo sapiens	66-96
1849269-2	1991	When maintained in the presence of an equimolar concentration of soluble heparin, the bFGF mutant (M1-bFGF) is as potent as bFGF in stimulating cell proliferation in normal and transformed fetal bovine aortic endothelial cells, in adult bovine aortic endothelial cells, and in NIH 3T3 fibroblasts.	Heparin	73-80	fibroblast growth factor 2	Bos taurus	86-90
1849269-2	1991	When maintained in the presence of an equimolar concentration of soluble heparin, the bFGF mutant (M1-bFGF) is as potent as bFGF in stimulating cell proliferation in normal and transformed fetal bovine aortic endothelial cells, in adult bovine aortic endothelial cells, and in NIH 3T3 fibroblasts.	Heparin	73-80	fibroblast growth factor 2	Bos taurus	102-106
1849269-2	1991	When maintained in the presence of an equimolar concentration of soluble heparin, the bFGF mutant (M1-bFGF) is as potent as bFGF in stimulating cell proliferation in normal and transformed fetal bovine aortic endothelial cells, in adult bovine aortic endothelial cells, and in NIH 3T3 fibroblasts.	Heparin	73-80	fibroblast growth factor 2	Bos taurus	102-106
1849269-4	1991	In the presence of heparin, M1-bFGF binds to bFGF plasma membrane receptors present on endothelial cells in a manner undistinguishable from bFGF.	Heparin	19-26	fibroblast growth factor 2	Bos taurus	31-35
2013315-5	1991	Binding of heparin induces a higher heparin affinity conformation in which the salt bridge is disrupted to reveal the reactive centre for inhibition of thrombin.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	152-160
2013315-5	1991	Binding of heparin induces a higher heparin affinity conformation in which the salt bridge is disrupted to reveal the reactive centre for inhibition of thrombin.	Heparin	36-43	coagulation factor II, thrombin	Homo sapiens	152-160
2005115-1	1991	Incubation of 16-kDa 125I-labeled heparin binding (acidic fibroblast) growth factor type one (HBGF-1) with human hepatoma cells and normal rat hepatocytes resulted in the appearance of a stable 125I-labeled complex with an apparent molecular mass of 40 kDa.	Heparin	34-41	fibroblast growth factor 1	Homo sapiens	94-100
1706340-1	1991	Acidic fibroblast growth factor (aFGF) is a broad spectrum mitogen that is stabilized by complexation with heparin and heparan proteoglycans.	Heparin	107-114	fibroblast growth factor 1	Homo sapiens	33-37
1706340-4	1991	Mutants of aFGF in which either any 2 or all 3 cysteine residues are substituted by serines are more active, have longer activity half-lives, and are less heparin dependent than wild-type aFGF.	Heparin	155-162	fibroblast growth factor 1	Homo sapiens	11-15
1706340-5	1991	In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin.	Heparin	129-136	fibroblast growth factor 1	Homo sapiens	23-27
1706340-5	1991	In contrast, wild-type aFGF and the three mutants that each retain 2 cysteine residues inactivate more rapidly in the absence of heparin by a nonproteolytic mechanism but are markedly stabilized by heparin.	Heparin	198-205	fibroblast growth factor 1	Homo sapiens	23-27
1705837-1	1991	We have extended our earlier observation that growing primary cultures of human umbilical vein endothelial cells (HUVEC) with heparin binding growth factor 1 (HBGF-1) 20 micrograms/mL and heparin 12 U/mL inhibits expression of tissue factor (TF) activity on HUVC monolayers perturbed with thrombin.	Heparin	126-133	fibroblast growth factor 1	Homo sapiens	159-165
1706340-6	1991	This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes.	Heparin	98-105	fibroblast growth factor 1	Homo sapiens	42-46
1705837-8	1991	These data establish that growing primary cultures of HUVEC with HBGF-1/heparin impairs their ability to synthesize TF apoprotein after perturbation.	Heparin	72-79	fibroblast growth factor 1	Homo sapiens	65-71
1706340-6	1991	This cysteine-mediated destabilization of aFGF not only diminishes its activity in the absence of heparin in tissue culture but also could functionally restrict its activity in vivo to the vicinity of mast cell-derived heparins and heparan proteoglycans associated with cell surfaces and basement membranes.	Heparin	219-227	fibroblast growth factor 1	Homo sapiens	42-46
1705837-9	1991	This may be part of a generalized response of endothelial cells to HBGF-1/heparin facilitating migration during angiogenesis.	Heparin	74-81	fibroblast growth factor 1	Homo sapiens	67-73
1899806-0	1991	Requirement of heparin for arterial and venous thrombolysis with recombinant tissue-type plasminogen activator.	Heparin	15-22	tissue-type plasminogen activator	Canis lupus familiaris	77-110
1849331-7	1991	These results suggest that heparin decreased plasma aldosterone owing to attenuation of the angiotensin II-induced aldosterone production.	Heparin	27-34	angiotensinogen	Homo sapiens	92-106
1848407-0	1991	Diabetes reduces heparin- and phospholipase C-releasable lipoprotein lipase from cardiomyocytes.	Heparin	17-24	lipoprotein lipase	Rattus norvegicus	57-75
1848407-2	1991	The release of LPL by the combination of heparin and PLC was not additive, and preincubation of cardiac myocytes with heparin eliminated the release of LPL in a subsequent incubation with PLC.	Heparin	41-48	lipoprotein lipase	Rattus norvegicus	15-18
1848407-2	1991	The release of LPL by the combination of heparin and PLC was not additive, and preincubation of cardiac myocytes with heparin eliminated the release of LPL in a subsequent incubation with PLC.	Heparin	118-125	lipoprotein lipase	Rattus norvegicus	152-155
1848407-4	1991	The induction of diabetes by the administration of streptozotocin (100 mg/kg for 3-4 days) to rats resulted in a decrease in the initial cellular activity of LPL and a marked reduction in the heparin-induced secretion of LPL into the medium of cardiac myocytes.	Heparin	192-199	lipoprotein lipase	Rattus norvegicus	221-224
1848407-5	1991	The intravenous administration of insulin (5 U for 1 h) in diabetic rats reversed the effects of diabetes on cellular and heparin-releasable LPL activities.	Heparin	122-129	lipoprotein lipase	Rattus norvegicus	141-144
1706595-1	1991	This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis.	Heparin	116-123	coagulation factor II, thrombin	Homo sapiens	177-185
1706595-1	1991	This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis.	Heparin	146-153	coagulation factor II, thrombin	Homo sapiens	177-185
2007182-11	1991	(4) A prior 10-12-min washout of the liver vascular bed with heparin removed over 80% of the hepatic lipase activity, as assessed by specific immunoinhibition.	Heparin	61-68	lipase C, hepatic type	Rattus norvegicus	93-107
2046484-11	1991	The results suggest that the decrease of LPL activity in the plasma of Mg-deficient rats may be due to a selective decrease in the heparin-releasable pool of enzyme.	Heparin	131-138	lipoprotein lipase	Rattus norvegicus	41-44
1900310-7	1991	Furthermore, the carboxy-terminal part of the interferon-gamma molecule contains an amino acid cluster, very closely related to a consensus sequence, present in more than 20 proteins known to bind sulfated glycosaminoglycans such as heparin.	Heparin	233-240	interferon gamma	Homo sapiens	46-62
2009304-7	1991	Heparin affinity chromatography therefore offers a convenient route to the isolation of structurally and functionally distinct classes of PLA2 enzymes.	Heparin	0-7	phospholipase A2, major isoenzyme	Sus scrofa	138-142
2009304-0	1991	Porcine pancreatic phospholipase A2 isoforms: differential regulation by heparin.	Heparin	73-80	phospholipase A2, major isoenzyme	Sus scrofa	19-35
2009304-8	1991	The existence of classes of PLA2 that can be differentially regulated by heparin may have important physiological consequences.	Heparin	73-80	phospholipase A2, major isoenzyme	Sus scrofa	28-32
2009304-1	1991	Isoforms of porcine pancreatic phospholipase A2 (PLA2) can be differentially regulated by heparin.	Heparin	90-97	phospholipase A2, major isoenzyme	Sus scrofa	31-47
2009304-1	1991	Isoforms of porcine pancreatic phospholipase A2 (PLA2) can be differentially regulated by heparin.	Heparin	90-97	phospholipase A2, major isoenzyme	Sus scrofa	49-53
2009304-2	1991	The major isoform of PLA2 can bind to heparin-Affigel and its catalytic activity can be inhibited by heparin.	Heparin	38-45	phospholipase A2, major isoenzyme	Sus scrofa	21-25
2009304-2	1991	The major isoform of PLA2 can bind to heparin-Affigel and its catalytic activity can be inhibited by heparin.	Heparin	101-108	phospholipase A2, major isoenzyme	Sus scrofa	21-25
2009304-3	1991	The interaction between this PLA2 isoform and heparin does not require calcium ion or a functional active site.	Heparin	46-53	phospholipase A2, major isoenzyme	Sus scrofa	29-33
2009304-5	1991	A minor isoform of porcine pancreatic PLA2 cannot bind to heparin and is resistant to heparin inhibition.	Heparin	58-65	phospholipase A2, major isoenzyme	Sus scrofa	38-42
2009304-5	1991	A minor isoform of porcine pancreatic PLA2 cannot bind to heparin and is resistant to heparin inhibition.	Heparin	86-93	phospholipase A2, major isoenzyme	Sus scrofa	38-42
1996970-0	1991	Low-Mr heparin is as potent as conventional heparin in releasing lipoprotein lipase, but is less effective in preventing hepatic clearance of the enzyme.	Heparin	7-14	lipoprotein lipase	Rattus norvegicus	65-83
1993172-0	1991	Interaction of fibronectin with heparin in model extracellular matrices: role of arginine residues and sulfate groups.	Heparin	32-39	fibronectin 1	Homo sapiens	15-26
1993172-1	1991	The interaction of heparin with the NH2-terminal domain of human plasma fibronectin was studied by using matrix-driven translocation, an assay for the adhesion of extracellular macromolecules with cell or particle surfaces within artificial collagen matrices.	Heparin	19-26	fibronectin 1	Homo sapiens	72-83
1993172-3	1991	Analysis of the fibronectin domain in terms of its primary structure, its proposed organization into "type I modules", and its hydrophilic and flexible segments led to the identification of several arginine-containing sites of potential interaction with the sulfate groups of heparin.	Heparin	276-283	fibronectin 1	Homo sapiens	16-27
1854945-2	1991	It was found that t1/2 of protein C was of 2.3 h. The intravenous administration of heparin resulted in the prolongation of t1/2 to 6.5 h, that could be explained by inhibition of thrombin generation.	Heparin	84-91	coagulation factor II	Rattus norvegicus	180-188
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	46-54
1901466-6	1991	The cautious use of t-PA with heparin in patients who are elderly or demented may be advisable.	Heparin	30-37	plasminogen activator, tissue type	Homo sapiens	20-24
1996970-1	1991	This study compares a low-Mr heparin preparation with conventional heparin with respect to its interaction with lipoprotein lipase (LPL) in vitro and its effects on the enzyme in vivo.	Heparin	29-36	lipoprotein lipase	Rattus norvegicus	112-130
1996970-1	1991	This study compares a low-Mr heparin preparation with conventional heparin with respect to its interaction with lipoprotein lipase (LPL) in vitro and its effects on the enzyme in vivo.	Heparin	29-36	lipoprotein lipase	Rattus norvegicus	132-135
1996970-1	1991	This study compares a low-Mr heparin preparation with conventional heparin with respect to its interaction with lipoprotein lipase (LPL) in vitro and its effects on the enzyme in vivo.	Heparin	67-74	lipoprotein lipase	Rattus norvegicus	112-130
1996970-1	1991	This study compares a low-Mr heparin preparation with conventional heparin with respect to its interaction with lipoprotein lipase (LPL) in vitro and its effects on the enzyme in vivo.	Heparin	67-74	lipoprotein lipase	Rattus norvegicus	132-135
1996970-2	1991	Both heparin preparations were polydisperse in binding to LPL, but on average the low-Mr preparation showed lower affinity.	Heparin	5-12	lipoprotein lipase	Rattus norvegicus	58-61
1996970-3	1991	Thus both conventional and low-Mr heparin bound quantitatively to immobilized LPL, and were eluted as broad peaks when a salt gradient was applied, but the peak for low-Mr heparin was shifted towards lower salt concentrations.	Heparin	34-41	lipoprotein lipase	Rattus norvegicus	78-81
1713785-1	1991	Basic fibroblast growth factor (bFGF) is a heparin-binding angiogenic polypeptide mitogen.	Heparin	43-50	fibroblast growth factor 2	Cavia porcellus	0-30
1996970-4	1991	To displace LPL from immobilized heparin a higher concentration of low-Mr than of conventional heparin was needed.	Heparin	95-102	lipoprotein lipase	Rattus norvegicus	12-15
1713785-1	1991	Basic fibroblast growth factor (bFGF) is a heparin-binding angiogenic polypeptide mitogen.	Heparin	43-50	fibroblast growth factor 2	Cavia porcellus	32-36
1996970-5	1991	Injection of the low-Mr heparin into intact rats resulted in lower plasma LPL activity than did injection of an equal mass of conventional heparin, but when the liver was excluded from the circulation both heparin preparations resulted in similar plasma LPL activities.	Heparin	24-31	lipoprotein lipase	Rattus norvegicus	74-77
1996970-7	1991	In perfused livers, on the other hand, low-Mr heparin was less effective than conventional heparin in preventing the rapid uptake of exogenous labelled LPL.	Heparin	46-53	lipoprotein lipase	Rattus norvegicus	152-155
1996970-7	1991	In perfused livers, on the other hand, low-Mr heparin was less effective than conventional heparin in preventing the rapid uptake of exogenous labelled LPL.	Heparin	91-98	lipoprotein lipase	Rattus norvegicus	152-155
1996970-8	1991	Hence the apparently lower average affinity of low-Mr heparin for LPL does not result in a demonstrably lower potency to release the enzyme from endothelial binding sites in peripheral tissues, but does result in a substantially decreased effect on the hepatic clearance of the enzyme.	Heparin	54-61	lipoprotein lipase	Rattus norvegicus	66-69
1988290-2	1991	Biologically active immunoreactive Mr 18,000 bFGF can be isolated by heparin-Sepharose affinity chromatography from the extract of GM 7372 cell nuclei.	Heparin	69-76	fibroblast growth factor 2	Bos taurus	45-49
2071190-1	1991	Fibronectin was extracted from 20 units of 3 days old plasma by the heparin cold precipitation technique using 15 or 30 units of sodium heparin per ml of plasma.	Heparin	68-75	fibronectin 1	Homo sapiens	0-11
2071190-1	1991	Fibronectin was extracted from 20 units of 3 days old plasma by the heparin cold precipitation technique using 15 or 30 units of sodium heparin per ml of plasma.	Heparin	129-143	fibronectin 1	Homo sapiens	0-11
1704799-4	1991	The alpha 2M-plasmin/TGF-beta complexes were minimally dissociated by heparin.	Heparin	70-77	transforming growth factor beta 1	Homo sapiens	21-29
1711526-4	1991	In this report, we summarize evidence that indicates that the heparin-binding and mitogenic activities of HBGF-1 can be dissociated from the receptor-binding activities of the growth factor by site-directed mutagenesis of a single lysine residue.	Heparin	62-69	fibroblast growth factor 1	Homo sapiens	106-112
1999476-3	1991	The addition of EGF, TGF alpha, or aFGF reversed heparin-induced growth inhibition, while bFGF partially negated this effect.	Heparin	49-56	fibroblast growth factor 1	Homo sapiens	35-39
1704799-5	1991	Reaction of alpha 2M with thrombin or trypsin reduced the binding of 125I-TGF-beta 1 and 125I-TGF-beta 2; the resulting complexes were readily dissociated by heparin.	Heparin	158-165	coagulation factor II, thrombin	Homo sapiens	26-34
1990781-6	1991	Thrombin inhibitors, including heparin and synthetic inhibitors, given with t-PA and aspirin, appear to shorten the time to thrombolysis and delay or prevent coronary artery reocclusion in experimental canine models.	Heparin	31-38	tissue-type plasminogen activator	Canis lupus familiaris	76-80
1990781-7	1991	Aspirin coupled with intravenous streptokinase reduces mortality in patients with presumed acute myocardial infarction, and a combination of heparin and t-PA results in infarct-artery patency more frequently than t-PA without heparin.	Heparin	226-233	plasminogen activator, tissue type	Homo sapiens	153-157
1703436-8	1991	In the presence of heparin, the protease specificity of PAI-1 toward thrombin is substantially increased.	Heparin	19-26	coagulation factor II, thrombin	Homo sapiens	69-77
1703436-9	1991	This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin.	Heparin	80-87	coagulation factor II, thrombin	Homo sapiens	34-42
1703436-9	1991	This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin.	Heparin	178-185	coagulation factor II, thrombin	Homo sapiens	156-164
1704799-5	1991	Reaction of alpha 2M with thrombin or trypsin reduced the binding of 125I-TGF-beta 1 and 125I-TGF-beta 2; the resulting complexes were readily dissociated by heparin.	Heparin	158-165	transforming growth factor beta 1	Homo sapiens	74-84
1704799-5	1991	Reaction of alpha 2M with thrombin or trypsin reduced the binding of 125I-TGF-beta 1 and 125I-TGF-beta 2; the resulting complexes were readily dissociated by heparin.	Heparin	158-165	transforming growth factor beta 1	Homo sapiens	74-82
1850874-0	1991	The initial release of t-PA induced by dDAVP is more important with low molecular weight heparin than with unfractionated heparin.	Heparin	89-96	plasminogen activator, tissue type	Homo sapiens	23-27
1703153-4	1991	HT1080 and C32 cell attachment to TSP was inhibited by the combination of heparin and a monoclonal (or polyclonal) antibody to GPIV but not by either alone.	Heparin	74-81	thrombospondin 1	Homo sapiens	34-37
1703153-9	1991	No attachment to the heparin-binding fragment was observed, but the addition of the heparin fragment to 140-kDa heparin-domainless TSP restored the heparin sensitivity of binding.	Heparin	84-91	thrombospondin 1	Homo sapiens	131-134
1703153-9	1991	No attachment to the heparin-binding fragment was observed, but the addition of the heparin fragment to 140-kDa heparin-domainless TSP restored the heparin sensitivity of binding.	Heparin	84-91	thrombospondin 1	Homo sapiens	131-134
1703153-9	1991	No attachment to the heparin-binding fragment was observed, but the addition of the heparin fragment to 140-kDa heparin-domainless TSP restored the heparin sensitivity of binding.	Heparin	84-91	thrombospondin 1	Homo sapiens	131-134
1703153-11	1991	The combination of heparin and Arg-Gly-Asp-Ser inhibited G361 attachment to TSP.	Heparin	19-26	thrombospondin 1	Homo sapiens	76-79
1850874-0	1991	The initial release of t-PA induced by dDAVP is more important with low molecular weight heparin than with unfractionated heparin.	Heparin	122-129	plasminogen activator, tissue type	Homo sapiens	23-27
1863264-0	1991	The salting-out behavior of human plasma fibronectin and its possible correlation with heparin-induced cryoprecipitation of the protein.	Heparin	87-94	fibronectin 1	Homo sapiens	41-52
1703153-13	1991	HT1080 fibrosarcoma and C32 melanoma cells utilize GPIV in concert with a heparin-modulated binding systems to attach and spread on TSP.	Heparin	74-81	thrombospondin 1	Homo sapiens	132-135
1664701-9	1991	Specifically, we conclude that (a) the cysteines in our bFGF mutant do not form a disulfide bond, (b) the high-affinity heparin binding of bFGF critically depends on an intact 3-dimensional structure of the growth factor rather than on specific heparin-binding sequence domains, and (c) the bFGF sequence between residues 70 and 122 is important for high biological activity.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	56-60
1664701-9	1991	Specifically, we conclude that (a) the cysteines in our bFGF mutant do not form a disulfide bond, (b) the high-affinity heparin binding of bFGF critically depends on an intact 3-dimensional structure of the growth factor rather than on specific heparin-binding sequence domains, and (c) the bFGF sequence between residues 70 and 122 is important for high biological activity.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	139-143
1664701-9	1991	Specifically, we conclude that (a) the cysteines in our bFGF mutant do not form a disulfide bond, (b) the high-affinity heparin binding of bFGF critically depends on an intact 3-dimensional structure of the growth factor rather than on specific heparin-binding sequence domains, and (c) the bFGF sequence between residues 70 and 122 is important for high biological activity.	Heparin	120-127	fibroblast growth factor 2	Homo sapiens	139-143
1664701-9	1991	Specifically, we conclude that (a) the cysteines in our bFGF mutant do not form a disulfide bond, (b) the high-affinity heparin binding of bFGF critically depends on an intact 3-dimensional structure of the growth factor rather than on specific heparin-binding sequence domains, and (c) the bFGF sequence between residues 70 and 122 is important for high biological activity.	Heparin	245-252	fibroblast growth factor 2	Homo sapiens	139-143
1664701-9	1991	Specifically, we conclude that (a) the cysteines in our bFGF mutant do not form a disulfide bond, (b) the high-affinity heparin binding of bFGF critically depends on an intact 3-dimensional structure of the growth factor rather than on specific heparin-binding sequence domains, and (c) the bFGF sequence between residues 70 and 122 is important for high biological activity.	Heparin	245-252	fibroblast growth factor 2	Homo sapiens	139-143
1995063-0	1991	Stimulation by NaCl, polylysine and heparin of two forms of spleen tyrosine protein kinase immunologically related with the protein expressed by lyn oncogene.	Heparin	36-43	LYN proto-oncogene, Src family tyrosine kinase	Homo sapiens	145-148
1877388-0	1991	The biological significance of lipoprotein lipase modulation by phenobarbital and heparin.	Heparin	82-89	lipoprotein lipase	Rattus norvegicus	31-49
1877388-6	1991	Rats infused with heparin by means of peritoneal implantation of osmotic minipumps demonstrated dose-dependent increases in circulating LPL, accompanied by reduction in heart muscle LPL but inconsistent changes in other tissues examined.	Heparin	18-25	lipoprotein lipase	Rattus norvegicus	136-139
1877388-6	1991	Rats infused with heparin by means of peritoneal implantation of osmotic minipumps demonstrated dose-dependent increases in circulating LPL, accompanied by reduction in heart muscle LPL but inconsistent changes in other tissues examined.	Heparin	18-25	lipoprotein lipase	Rattus norvegicus	182-185
1664701-7	1991	This fragment was generated by pronase treatment of heparin-bound recombinant Glu3,5Ser78,96-bFGF mutant and is active in vitro at an ED50 of about 100 ng/ml.	Heparin	52-59	fibroblast growth factor 2	Homo sapiens	93-97
1863264-4	1991	The possibility of a correlation between the heparin-induced cryoprecipitation of fibronectin and the dependence of its solubility parameters on pH and temperature is considered.	Heparin	45-52	fibronectin 1	Homo sapiens	82-93
1863264-5	1991	It is suggested that heparin-induced precipitation of human plasma fibronectin at low temperatures is caused by (i) a cold effect and (ii) conformational change in the protein due to heparin binding.	Heparin	21-28	fibronectin 1	Homo sapiens	67-78
1863264-5	1991	It is suggested that heparin-induced precipitation of human plasma fibronectin at low temperatures is caused by (i) a cold effect and (ii) conformational change in the protein due to heparin binding.	Heparin	183-190	fibronectin 1	Homo sapiens	67-78
1934005-1	1991	Heparan sulfate and heparin, new targets for IFN-gamma, protect, relax the cytokine and regulate its activity.	Heparin	20-27	interferon gamma	Homo sapiens	45-54
1665467-0	1991	Determination of the levels of unfractionated and low-molecular-weight heparins in plasma: their effect on thrombin-mediated feedback reactions in vivo.	Heparin	71-79	coagulation factor II, thrombin	Homo sapiens	107-115
1768437-3	1991	ASM cells release in the medium a VEGF-like endothelial cell mitogen which binds to heparin-sepharose and has an apparent molecular weight of 40-45 kDa as assessed by an HPLC gel filtration column.	Heparin	84-91	vascular endothelial growth factor A	Homo sapiens	34-38
1702705-11	1991	Heparin is known to interact with clusters of basic residues, and these residues are concentrated in the midregion of apoA-I.	Heparin	0-7	apolipoprotein A1	Homo sapiens	118-124
1665467-2	1991	We define a standard independent unit (SIU) of heparin as that amount that, in plasma containing 1 mumol of ATIII, raises the (pseudo-)first-order breakdown constant of factor Xa by 1 min-1.	Heparin	47-54	CD59 molecule (CD59 blood group)	Homo sapiens	184-189
1768439-4	1991	Complementary DNA constructs coding for the mature HBNF and MK proteins were expressed in bacteria and purified by heparin affinity chromatography.	Heparin	115-122	pleiotrophin	Homo sapiens	51-55
1665467-13	1991	The essential difference between UFH and LMWH appears in the feedback effect of thrombin in PRP, where thrombin generation is both inhibited and retarded by LMWH, while it is only retarded but hardly inhibited by UFH.	Heparin	33-36	coagulation factor II, thrombin	Homo sapiens	80-88
1794749-1	1991	The polyanions heparin and dermatan sulfate catalyze alpha-thrombin inhibition and can delay the onset of factor VIII and factor V necessary for intrinsic prothrombin activation to begin in plasma.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	59-67
1665467-13	1991	The essential difference between UFH and LMWH appears in the feedback effect of thrombin in PRP, where thrombin generation is both inhibited and retarded by LMWH, while it is only retarded but hardly inhibited by UFH.	Heparin	33-36	coagulation factor II, thrombin	Homo sapiens	103-111
1794749-5	1991	In contrast, heparin and a bis-lactobionic acid, both of which catalyzed alpha-thrombin inhibition, could effectively inhibit factor VIII and factor V activation.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	79-87
1665467-13	1991	The essential difference between UFH and LMWH appears in the feedback effect of thrombin in PRP, where thrombin generation is both inhibited and retarded by LMWH, while it is only retarded but hardly inhibited by UFH.	Heparin	213-216	coagulation factor II, thrombin	Homo sapiens	80-88
1938222-3	1991	Plasma fibrinogen level after haemodialysis was significantly lower after administration of heparin alone as compared with the group treated by prostacyclin-heparin infusion.	Heparin	92-99	fibrinogen beta chain	Homo sapiens	7-17
2050602-5	1991	In two patients, preoperative anticoagulation with either heparin or nafamostat mesilate was followed by an increase in plasma fibrinogen level from 0.7 to 5.6 g/L and a decrease in FDP from 64 to 8 micrograms/ml in one patient, and fibrinogen from 1.0 to 2.8 g/L and FDP from 40 to 5 micrograms/mL in another patient.	Heparin	58-65	fibrinogen beta chain	Homo sapiens	127-137
2050602-5	1991	In two patients, preoperative anticoagulation with either heparin or nafamostat mesilate was followed by an increase in plasma fibrinogen level from 0.7 to 5.6 g/L and a decrease in FDP from 64 to 8 micrograms/ml in one patient, and fibrinogen from 1.0 to 2.8 g/L and FDP from 40 to 5 micrograms/mL in another patient.	Heparin	58-65	fibrinogen beta chain	Homo sapiens	233-243
1856049-9	1991	Since interaction with heparin has been observed also for selenoprotein P isolated from rat plasma, the protein in the heparin-binding fraction, demonstrated in this paper, may be a human analogue to selenoprotein P.	Heparin	23-30	selenoprotein P	Homo sapiens	200-215
1856049-9	1991	Since interaction with heparin has been observed also for selenoprotein P isolated from rat plasma, the protein in the heparin-binding fraction, demonstrated in this paper, may be a human analogue to selenoprotein P.	Heparin	119-126	selenoprotein P	Homo sapiens	200-215
1724512-3	1991	Excessive heparin-dependent activity of monocytes in this case reflects the activity of the rheumatoid process, the NBT test with heparin being more sensitive in the diagnosis of disease activity than measurement of red cell sedimentation rate or of blood C-reactive protein, gamma- and alpha 2-globulin levels.	Heparin	10-17	C-reactive protein	Homo sapiens	256-274
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	48-55	apolipoprotein E	Homo sapiens	56-60
1895872-6	1991	This phospholipase A2 showed high affinity for heparin, and was recognized by a monoclonal antibody raised against phospholipase A2 from human synovial fluid.	Heparin	47-54	phospholipase A2 group IB	Homo sapiens	5-21
1895872-6	1991	This phospholipase A2 showed high affinity for heparin, and was recognized by a monoclonal antibody raised against phospholipase A2 from human synovial fluid.	Heparin	47-54	phospholipase A2 group IB	Homo sapiens	115-131
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	48-55	apolipoprotein E	Homo sapiens	178-182
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	48-55	apolipoprotein E	Homo sapiens	178-182
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	151-158	apolipoprotein E	Homo sapiens	178-182
1846019-5	1991	Heparin"s inhibition of growth of HepG2 cells correlated with changes in the mRNA synthesis and abundance of insulinlike growth factor II (IGF II) and transforming growth factor beta (TGF beta).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	151-182
1846019-5	1991	Heparin"s inhibition of growth of HepG2 cells correlated with changes in the mRNA synthesis and abundance of insulinlike growth factor II (IGF II) and transforming growth factor beta (TGF beta).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	184-192
1846019-8	1991	Transcriptionally, IGF II was regulated by the additive effects of insulin, glucagon, and growth hormone in combination with heparin; TGF beta was regulated primarily by the synergistic effects of insulin and growth hormone in combination with heparin.	Heparin	244-251	transforming growth factor beta 1	Homo sapiens	134-142
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	151-158	apolipoprotein E	Homo sapiens	178-182
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	151-158	apolipoprotein E	Homo sapiens	178-182
1762571-1	1991	The methods and approaches taken to investigate heparin-apoE peptide interactions have involved a series of steps, including (1) identification of the heparin-binding domains of apoE, (2) determination of the minimal amino acid sequence regions involved in heparin binding, heparin-induced conformational changes, and stability of apoE peptide structures in solution, (3) modeling of these peptide and oligosaccharide structures, and (4) examination of their behavior during molecular dynamics calculations to determine if the modeled complexes simulate the results of the solution study.	Heparin	151-158	apolipoprotein E	Homo sapiens	178-182
1762571-2	1991	The heparin-binding regions of apoE were determined by fragmentation of the protein and identification of the heparin-binding fragments by ligand-blotting procedures using 125I-labeled heparin.	Heparin	4-11	apolipoprotein E	Homo sapiens	31-35
1762571-2	1991	The heparin-binding regions of apoE were determined by fragmentation of the protein and identification of the heparin-binding fragments by ligand-blotting procedures using 125I-labeled heparin.	Heparin	110-117	apolipoprotein E	Homo sapiens	31-35
1762571-2	1991	The heparin-binding regions of apoE were determined by fragmentation of the protein and identification of the heparin-binding fragments by ligand-blotting procedures using 125I-labeled heparin.	Heparin	110-117	apolipoprotein E	Homo sapiens	31-35
1762571-4	1991	These studies also showed that heparin binds to the apoE(211-243) and apoE(129-169) regions to induce and stabilize beta-strand and alpha-helical peptide conformations.	Heparin	31-38	apolipoprotein E	Homo sapiens	52-56
1762571-4	1991	These studies also showed that heparin binds to the apoE(211-243) and apoE(129-169) regions to induce and stabilize beta-strand and alpha-helical peptide conformations.	Heparin	31-38	apolipoprotein E	Homo sapiens	70-74
1923913-0	1991	The influence of heparin on the prothrombin time.	Heparin	17-24	coagulation factor II, thrombin	Homo sapiens	32-43
1923913-1	1991	We studied the effect of known concentrations of heparin on the prothrombin time (PT) in patients receiving warfarin and in controls who were not anticoagulated.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	64-75
1658965-1	1991	In determining heparin one has the choice to test a specific activity, such as the decay constant of thrombin or factor Xa on a global test such as the aPTT.	Heparin	15-22	coagulation factor II, thrombin	Homo sapiens	101-109
1830993-3	1991	Extracorporeal heparin precipitation by using fibronectin is ascertained to be promising in removing plasma proteins in rheumatic immunocomplex diseases.	Heparin	15-22	fibronectin 1	Homo sapiens	46-57
1948093-0	1991	Low-dose intermittent heparin therapy decreases plasma fibrinogen levels.	Heparin	22-29	fibrinogen beta chain	Homo sapiens	55-65
2089037-10	1990	The biochemical features of the activity observed in the heparin-non-binding fraction generally resembled those of human platelet soluble phospholipase A2 [Kim, D.K., Kudo, I., &amp; Inoue, K. (1988) J. Biochem.	Heparin	57-64	phospholipase A2 group IB	Homo sapiens	138-154
2268289-1	1990	Fluorescence polarization, gel exclusion chromatography and affinity chromatography were used to characterize the interaction of heparins of different size with human plasma fibronectin (Fn) and several of its isolated domains.	Heparin	129-137	fibronectin 1	Homo sapiens	174-185
2268289-1	1990	Fluorescence polarization, gel exclusion chromatography and affinity chromatography were used to characterize the interaction of heparins of different size with human plasma fibronectin (Fn) and several of its isolated domains.	Heparin	129-137	fibronectin 1	Homo sapiens	187-189
2268289-2	1990	The fluid-phase interaction of Fn with heparin was dominated by the 30 kDa and 40 kDa Hep-2 domains located near the C-terminal ends of the A and B chains respectively.	Heparin	39-46	fibronectin 1	Homo sapiens	31-33
2268289-6	1990	Fn and Hep-2 fragments were rather undiscriminating in their reaction with fluoresceinamine-labelled heparins of different sizes.	Heparin	101-109	fibronectin 1	Homo sapiens	0-2
2268268-11	1990	Heparin prolonged by 15 s and 45 s the time required to demonstrate Factor V activation in CAP supplemented with Factor Xa and thrombin respectively.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	127-135
1703455-3	1990	Heparin is an effective anticoagulant, but it has poor bioavailability and effects on thrombin and platelets that predispose it to life-threatening complications such as hemorrhage and thrombocytopenia.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	86-94
1706698-2	1990	The stimulation of endothelial cell growth by HBGF type one (HBGF-1) in particular requires heparin or a similar glycosaminoglycan.	Heparin	92-99	fibroblast growth factor 1	Homo sapiens	61-67
2269666-3	1990	Thrombospondin (TSP), a 450-kD ECM protein whose major proteolytic fragments are a COOH-terminal 140-kD fragment and an NH2-terminal heparin-binding domain (HBD), is secreted by platelets, endothelial cells, and smooth muscle cells.	Heparin	133-140	thrombospondin 1	Homo sapiens	0-14
2269666-3	1990	Thrombospondin (TSP), a 450-kD ECM protein whose major proteolytic fragments are a COOH-terminal 140-kD fragment and an NH2-terminal heparin-binding domain (HBD), is secreted by platelets, endothelial cells, and smooth muscle cells.	Heparin	133-140	thrombospondin 1	Homo sapiens	16-19
2089037-6	1990	The activity detected in the heparin-binding fraction appeared to belong to the secretory 14-kDa phospholipase A2, because it bound to anti-human 14-kDa group II phospholipase A2 monoclonal antibody.	Heparin	29-36	phospholipase A2 group IB	Homo sapiens	97-113
2089037-6	1990	The activity detected in the heparin-binding fraction appeared to belong to the secretory 14-kDa phospholipase A2, because it bound to anti-human 14-kDa group II phospholipase A2 monoclonal antibody.	Heparin	29-36	phospholipase A2 group IB	Homo sapiens	162-178
2277084-0	1990	Recognition of the A chain carboxy-terminal heparin binding region of fibronectin involves multiple sites: two contiguous sequences act independently to promote neural cell adhesion.	Heparin	44-51	fibronectin 1	Homo sapiens	70-81
2277084-2	1990	A carboxy-terminal cell and heparin binding region of fibronectin (FN) is particularly interesting because it is a strong promoter of neurite outgrowth (Rogers, S.L., J.B. McCarthy, S.L.	Heparin	28-35	fibronectin 1	Homo sapiens	54-65
2277084-2	1990	A carboxy-terminal cell and heparin binding region of fibronectin (FN) is particularly interesting because it is a strong promoter of neurite outgrowth (Rogers, S.L., J.B. McCarthy, S.L.	Heparin	28-35	fibronectin 1	Homo sapiens	67-69
2277084-14	1990	To further understand the molecular mechanisms of neuronal interactions with this region of FN, we screened two peptides from the 33-kD heparin binding fragment of the FN A chain, FN-C/H II (KNNQKSEPLIGRKKT) and CS1 (Humphries, M.J., A. Komoriya, S.K.	Heparin	136-143	fibronectin 1	Homo sapiens	92-94
2277084-14	1990	To further understand the molecular mechanisms of neuronal interactions with this region of FN, we screened two peptides from the 33-kD heparin binding fragment of the FN A chain, FN-C/H II (KNNQKSEPLIGRKKT) and CS1 (Humphries, M.J., A. Komoriya, S.K.	Heparin	136-143	fibronectin 1	Homo sapiens	168-170
2277084-28	1990	These data further support the hypothesis that cell responses to FN are mediated by multiple sites involving both heparin-sensitive and -insensitive mechanisms.	Heparin	114-121	fibronectin 1	Homo sapiens	65-67
2096488-1	1990	Heparin cofactor II (HCII) is a thrombin inhibitor present in human plasma whose activity is enhanced by heparin.	Heparin	105-112	coagulation factor II, thrombin	Homo sapiens	32-40
2083485-6	1990	Adenosine-diphosphate (0.5-2 microM) or thrombin (0.1-0.4 NIH units ml-1) induced dose-dependent aggregation of platelets in citrate- or heparin-containing PRP; such aggregation was, however, not affected by ET-1 (1-100 microM) either.	Heparin	137-144	coagulation factor II, thrombin	Homo sapiens	40-48
2172248-1	1990	Three isozymes of diacylglycerol kinase (DGK), DGK-I, DGK-II, and DGK-III, were purified from the cytosol of human platelets by successive chromatography on DEAE-cellulose, Ultrogel AcA34, heparin-Sepharose, ATP-agarose, Mono Q, phenyl-Superose, HCA-hydroxyapatite, Wakopak G40, and TSK-3000SW columns.	Heparin	189-196	diacylglycerol kinase beta	Homo sapiens	18-39
2172248-1	1990	Three isozymes of diacylglycerol kinase (DGK), DGK-I, DGK-II, and DGK-III, were purified from the cytosol of human platelets by successive chromatography on DEAE-cellulose, Ultrogel AcA34, heparin-Sepharose, ATP-agarose, Mono Q, phenyl-Superose, HCA-hydroxyapatite, Wakopak G40, and TSK-3000SW columns.	Heparin	189-196	diacylglycerol kinase beta	Homo sapiens	41-44
2243108-9	1990	Inclusion of heparin, but not chondroitin sulfate, in the assay medium resulted in partial inhibition of process extension, but at concentrations of heparin which were higher than that needed to disrupt laminin-HSPG association in vitro.	Heparin	13-20	syndecan 2	Rattus norvegicus	211-215
2083485-6	1990	Adenosine-diphosphate (0.5-2 microM) or thrombin (0.1-0.4 NIH units ml-1) induced dose-dependent aggregation of platelets in citrate- or heparin-containing PRP; such aggregation was, however, not affected by ET-1 (1-100 microM) either.	Heparin	137-144	endothelin 1	Homo sapiens	208-212
1699952-9	1990	Mitogenic assays established two points: (a) human recombinant HBGF-1 is highly dependent on the presence of heparin for optimal mitogenic activity, and (b) the change of lysine 132 to glutamic acid drastically reduces the specific mitogenic activity of HBGF-1.	Heparin	109-116	fibroblast growth factor 1	Homo sapiens	63-69
2226312-3	1990	ApoB-100 contains 13 binding sites for heparin, a known inhibitor of T4 binding to the major T4 carrier plasma proteins; however, heparin failed to inhibit T4 binding to apoB-100 and fragments thereof.	Heparin	39-46	apolipoprotein B	Homo sapiens	0-8
2226312-6	1990	We conclude that the three T4-binding sites of apoB-100 are outside the LDL receptor binding domain, distant from the heparin binding sites and, assuming no allosteric effects, in the vicinity of residues 474-539 (T4 site of apoB-26), 1438-1481 (T4 site of apoB-44), and in the C terminal quarter of apoB-30.	Heparin	118-125	apolipoprotein B	Homo sapiens	47-55
2146276-12	1990	Scatter factor was purified to homogeneity from conditioned medium of human fibroblasts by heparin-Sepharose chromatography, followed by cation exchange chromatography, gel filtration, or preparative SDS gel electrophoresis.	Heparin	91-98	hepatocyte growth factor	Canis lupus familiaris	0-14
1699952-8	1990	Replacement of this lysine with glutamic acid reduces the apparent affinity of HBGF-1 for immobilized heparin (elutes at 0.45 M NaCl vs. 1.1 M NaCl for wild-type).	Heparin	102-109	fibroblast growth factor 1	Homo sapiens	79-85
2121016-0	1990	Recombinant tissue-type plasminogen activator followed by heparin compared with heparin alone for refractory unstable angina pectoris.	Heparin	58-65	plasminogen activator, tissue type	Homo sapiens	12-45
2246329-7	1990	Nuclear extracts prepared from transfected cells were found to contain bFGF as determined using heparin-sepharose affinity chromatography, followed by Western blot analysis of fractions, which stimulated the proliferation BHK-21 cells.	Heparin	96-103	fibroblast growth factor 2	Homo sapiens	71-75
2104522-8	1990	These results demonstrate a role for the local action of thrombin synthesized on the surfaces of thrombi even under conditions when the thrombin exerts no bulk effect, such as under heparin anticoagulation.	Heparin	182-189	coagulation factor II, thrombin	Homo sapiens	57-65
1700197-3	1990	A uniform concentration of 1 micrograms/ml of heparin was included in most experiments to exploit heparin"s potentiating effect on aFGF activity.	Heparin	98-105	fibroblast growth factor 1	Homo sapiens	131-135
2226463-7	1990	The similarity was higher than 60% on peptide mapping with trypsin digestion, the 105-kDa protein cross-reacted with anti-HSP90 antibody, both were bound similarly to heparin-Sepharose gel and both are located in the cytosol fraction.	Heparin	167-174	heat shock protein 90 alpha family class A member 1	Rattus norvegicus	122-127
2272956-9	1990	Thus the decline in fibronectin concentration with cardiopulmonary bypass may be due to dilution as well as opsonic consumption and possible complexing with heparin in the cold.	Heparin	157-164	fibronectin 1	Homo sapiens	20-31
1698787-12	1990	Ligand binding of rPAI-1 to nitrocellulose replicas from sodium dodecyl sulfate-polyacrylamide gels containing electrophoretically separated peptides from VN digests documented the association of PAI-1 with Mr = 10,000-20,000 fragments originating from the heparin-binding domain of VN.	Heparin	257-264	serpin family E member 1	Rattus norvegicus	18-24
1699533-1	1990	Heparin potentiates the mitogenic activity of acidic fibroblast growth factor (aFGF) by 20-100 fold but mechanisms detailing this potentiation have not yet been fully elucidated.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	46-77
1699533-1	1990	Heparin potentiates the mitogenic activity of acidic fibroblast growth factor (aFGF) by 20-100 fold but mechanisms detailing this potentiation have not yet been fully elucidated.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	79-83
1699533-2	1990	We report that heparin increases the binding affinity of aFGF for the two cloned and overexpressed human FGF receptors, flg and bek, by 2-3 fold.	Heparin	15-22	fibroblast growth factor 1	Homo sapiens	57-61
1699533-3	1990	This increase in binding affinity, together with previous data demonstrating a 3-5 fold increase in the stability of aFGF, are likely to account for a significant portion of heparin"s potentiation of aFGF activity observed in biological assay systems.	Heparin	174-181	fibroblast growth factor 1	Homo sapiens	117-121
1699533-3	1990	This increase in binding affinity, together with previous data demonstrating a 3-5 fold increase in the stability of aFGF, are likely to account for a significant portion of heparin"s potentiation of aFGF activity observed in biological assay systems.	Heparin	174-181	fibroblast growth factor 1	Homo sapiens	200-204
2170402-8	1990	The type I and type II (membrane-bound or cytosolic) PIP kinases are modulated differentially by spermine and heparin.	Heparin	110-117	prolactin induced protein	Homo sapiens	53-56
2170425-2	1990	Iodinated 125I-bFGF diffuses further in agarose, fibrin, and on a monolayer of bovine aortic endothelial (BAE) cells in the presence of heparin than in its absence.	Heparin	136-143	fibroblast growth factor 2	Bos taurus	15-19
2222535-0	1990	Binding of anti-DNA antibodies and inhibition of glomerulonephritis in MRL-lpr/lpr mice by heparin.	Heparin	91-98	Fas (TNF receptor superfamily member 6)	Mus musculus	75-78
2222535-0	1990	Binding of anti-DNA antibodies and inhibition of glomerulonephritis in MRL-lpr/lpr mice by heparin.	Heparin	91-98	Fas (TNF receptor superfamily member 6)	Mus musculus	79-82
2222535-1	1990	Heparin was found to inhibit the DNA binding of antibodies eluted from kidneys of both humans and MRL-lpr/lpr mice with systemic lupus erythematosus.	Heparin	0-7	Fas (TNF receptor superfamily member 6)	Mus musculus	102-105
2222535-1	1990	Heparin was found to inhibit the DNA binding of antibodies eluted from kidneys of both humans and MRL-lpr/lpr mice with systemic lupus erythematosus.	Heparin	0-7	Fas (TNF receptor superfamily member 6)	Mus musculus	106-109
2222535-2	1990	Treatment of MRL-lpr/lpr mice with low doses of heparin significantly inhibited renal damage.	Heparin	48-55	Fas (TNF receptor superfamily member 6)	Mus musculus	17-20
2222535-2	1990	Treatment of MRL-lpr/lpr mice with low doses of heparin significantly inhibited renal damage.	Heparin	48-55	Fas (TNF receptor superfamily member 6)	Mus musculus	21-24
2223864-0	1990	Inhibition of phospholipase A2 by heparin.	Heparin	34-41	phospholipase A2 group IB	Homo sapiens	14-30
2223864-2	1990	The hydrolysis of phosphatidylcholine in vitro catalyzed by porcine pancreatic PLA2 was inhibited by heparin.	Heparin	101-108	phospholipase A2 group IB	Homo sapiens	79-83
2223864-3	1990	Other glycosaminoglycans inhibited PLA2 activity to a significantly lesser extent, with a pattern of inhibition: heparin much greater than chondroitin sulfate (CS)-C greater than CS-A greater than CS-B greater than keratan sulfate.	Heparin	113-120	phospholipase A2 group IB	Homo sapiens	35-39
2223864-5	1990	Heparin"s ability to inhibit PLA2 activity did not depend on substrate concentration, but did depend on ionic strength, with inhibition decreasing with increasing ionic strength.	Heparin	0-7	phospholipase A2 group IB	Homo sapiens	29-33
2223864-7	1990	As a consequence, heparin induced a shift of the pH optimum of PLA2 from 7 to 8.	Heparin	18-25	phospholipase A2 group IB	Homo sapiens	63-67
2223864-8	1990	Histone IIA and protamine sulfate, heparin-binding proteins, reversed heparin-induced PLA2 inhibition.	Heparin	35-42	phospholipase A2 group IB	Homo sapiens	86-90
2223864-9	1990	The concentration of heparin which inhibited PLA2 activity by 50% increased with increasing enzyme concentration.	Heparin	21-28	phospholipase A2 group IB	Homo sapiens	45-49
2223864-10	1990	Furthermore, PLA2 bound to heparin-Affigel.	Heparin	27-34	phospholipase A2 group IB	Homo sapiens	13-17
2229822-2	1990	This enzyme can rapidly inactivate fibrinogen and, as a complex with heparin, may prevent coagulation that may otherwise occur when plasma enters tissues at sites of immediate reactions.	Heparin	69-76	fibrinogen beta chain	Homo sapiens	35-45
2170425-5	1990	These results suggest that bFGF-heparin and/or heparan sulfate complexes may be more effective than bFGF alone in stimulating cells located away from the bFGF source because the bFGF-glycosaminoglycan complex partitions into the soluble phase rather than binding to insoluble glycosaminoglycans in the extracellular matrix.	Heparin	32-39	fibroblast growth factor 2	Bos taurus	27-31
2271570-2	1990	The interaction between ATIII and thrombin is enhanced several thousandfold by the glycosaminoglycan, heparin.	Heparin	102-109	coagulation factor II, thrombin	Homo sapiens	34-42
2217203-1	1990	The major dithiothreitol-resistant phospholipase A2 activity present in the cytosol of U937 cells has been purified greater than 200,000-fold by sequential chromatography on phenyl-5PW, heparin-Sepharose CL-6B, high-performance hydroxylapatite, TSK-gel G3000-SW, and Mono Q columns.	Heparin	186-193	phospholipase A2 group IB	Homo sapiens	35-51
1962908-0	1990	Effect of low molecular weight heparin preparations on the inhibition of thrombin by heparin cofactor II.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	73-81
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	127-135
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	20-27	coagulation factor II, thrombin	Homo sapiens	222-230
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	127-135
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	103-110	coagulation factor II, thrombin	Homo sapiens	222-230
2271570-10	1990	Additionally, occupancy of the heparin binding site by these same monovalent and bivalent IgG"s at least partially substituted for heparin, accelerating linkage formation between ATIII and thrombin.	Heparin	31-38	coagulation factor II, thrombin	Homo sapiens	189-197
2271570-10	1990	Additionally, occupancy of the heparin binding site by these same monovalent and bivalent IgG"s at least partially substituted for heparin, accelerating linkage formation between ATIII and thrombin.	Heparin	131-138	coagulation factor II, thrombin	Homo sapiens	189-197
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	73-81
2168346-3	1990	Basic FGF (bFGF) was identified in SW-13 lysates by both its chromatographic behavior on heparin-Sepharose and its reactivity with an antibody specific for bFGF.	Heparin	89-96	fibroblast growth factor 2	Homo sapiens	0-9
2168346-3	1990	Basic FGF (bFGF) was identified in SW-13 lysates by both its chromatographic behavior on heparin-Sepharose and its reactivity with an antibody specific for bFGF.	Heparin	89-96	fibroblast growth factor 2	Homo sapiens	11-15
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	13-20	coagulation factor II, thrombin	Homo sapiens	103-111
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	73-81
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	148-155	coagulation factor II, thrombin	Homo sapiens	103-111
2169239-2	1990	When LPL activity in cardiac myocytes was depleted by treatment of rats with cycloheximide (2 mg/kg; 2.5 h) and inclusion of the protein-synthesis inhibitor in the isolation solutions, incubation with CPT-cAMP or forskolin did not influence the rate of repletion of LPL activity in cells or the recovery of heparin-releasable LPL activity.	Heparin	307-314	lipoprotein lipase	Rattus norvegicus	5-8
2169239-5	1990	Therefore interventions that stimulate adenylate cyclase activity (forskolin, cholera toxin) or incubation with CPT-cAMP do not increase cellular LPL activity or promote the translocation of LPL to a heparin-releasable fraction in cardiac myocytes.	Heparin	200-207	lipoprotein lipase	Rattus norvegicus	191-194
2254959-3	1990	The identity of the PA-stimulating activity of neuronal cell extract with bFGF was confirmed by its high affinity for heparin and by its cross-reactivity with polyclonal antibodies to human placental bFGF.	Heparin	118-125	fibroblast growth factor 2	Homo sapiens	74-78
2400395-7	1990	3H-labelled HDL2 and HDL3 subfractions behaved differently under the precipitant action of heparin-Mn2+; fraction C (the richest in apolipoprotein E) produced the largest amount of radioactive and chemical precipitate.	Heparin	91-98	HDL3	Homo sapiens	21-25
2202741-0	1990	Human recombinant interleukin-1 beta- and tumor necrosis factor alpha-mediated suppression of heparin-like compounds on cultured porcine aortic endothelial cells.	Heparin	94-101	interleukin 1 beta	Homo sapiens	18-69
1706636-1	1990	Acidic fibroblast growth factor (aFGF) is a heparin-binding polypeptide that acts as a neurotrophic factor for certain central and peripheral neurons.	Heparin	44-51	fibroblast growth factor 1	Mus musculus	0-31
1706636-1	1990	Acidic fibroblast growth factor (aFGF) is a heparin-binding polypeptide that acts as a neurotrophic factor for certain central and peripheral neurons.	Heparin	44-51	fibroblast growth factor 1	Mus musculus	33-37
2380171-10	1990	Thus, unlike active site-directed competitive inhibitors, hirugen should act in concert with AT and heparin to reduce the amount of fibrinogen that is processed during the lifetime of alpha-thrombin in plasma.	Heparin	100-107	fibrinogen beta chain	Homo sapiens	132-142
2203476-4	1990	The heparin binding site of type V collagen was located in a 30 kDa CNBr fragment of the alpha 1(V) chain, and the amino acid sequence of this fragment was determined.	Heparin	4-11	collagen type V alpha 1 chain	Homo sapiens	89-99
2387419-3	1990	The resulting enzyme (HB-SOD) bound to a heparin-Sepharose column and cultured endothelial cells; binding was inhibited either by high NaCl concentrations or heparin.	Heparin	41-48	superoxide dismutase 1	Homo sapiens	25-28
2387419-3	1990	The resulting enzyme (HB-SOD) bound to a heparin-Sepharose column and cultured endothelial cells; binding was inhibited either by high NaCl concentrations or heparin.	Heparin	158-165	superoxide dismutase 1	Homo sapiens	25-28
2203397-1	1990	Because paradoxical increase in thrombin activity was reported after the administration of streptokinase in patients with acute myocardial infarction the velocity of reperfusion and degree of myocardial damage were studied when heparin was infused during rather than after streptokinase infusion.	Heparin	228-235	coagulation factor II, thrombin	Homo sapiens	32-40
2396990-8	1990	Binding of heparin to intact fibronectin and to its N-terminal fragment stabilized the proteins against thermal unfolding.	Heparin	11-18	fibronectin 1	Homo sapiens	29-40
2380554-12	1990	However, with SP such as heparin, fucoidan, the carrageenans, and polyanethole sulfonate, although CD4 blocking may contribute to anti-HIV activity, some other anti-viral mechanism is also operating.	Heparin	25-32	CD4 molecule	Homo sapiens	99-102
2384594-6	1990	Heparin, hirudin, hirudin dodecapeptide (hirugen), and D-phenylalanyl-L-prolyl-L-arginyl chloromethyl ketone (PPACK) produce concentration-dependent inhibition of FPA release mediated by fluid-phase thrombin.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	199-207
2279298-0	1990	Regucalcin-induced Ca2+ release from rat liver microsomes: the effect is inhibited by heparin.	Heparin	86-93	regucalcin	Rattus norvegicus	0-10
2279298-1	1990	The effect of heparin on the calcium-binding protein regucalcin-stimulated Ca2+ release from rat liver microsomes was investigated.	Heparin	14-21	regucalcin	Rattus norvegicus	53-63
2165828-8	1990	While neutralization of in situ generated factor IXa in normal plasma was negligible, unfractionated heparin dramatically enhanced the rate of inactivation of factor IXa (apparent second order rate constant of inhibition of 5.2 min-1/per microgram heparin/mL).	Heparin	101-108	CD59 molecule (CD59 blood group)	Homo sapiens	228-233
2165828-9	1990	The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL).	Heparin	30-37	CD59 molecule (CD59 blood group)	Homo sapiens	219-224
2225476-4	1990	GHRH-induced GH secretion was significantly reduced following elevation of circulating FFA levels by lipid-heparin infusion and significantly potentiated by previous pyridostigmine treatment.	Heparin	107-114	growth hormone releasing hormone	Homo sapiens	0-4
2146125-3	1990	The apo(a) portion of Lp(a) binds to the carboxy-terminal heparin-binding domain of fibronectin.	Heparin	58-65	fibronectin 1	Homo sapiens	84-95
2384594-7	1990	However, heparin is much less effective at inhibiting thrombin bound to fibrin because a 20-fold higher concentration is necessary to block 70% of the activity of the clot-bound enzyme than is required for equivalent inhibition of fluid-phase thrombin (2.0 and 0.1 U/ml, respectively).	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	54-62
2384594-7	1990	However, heparin is much less effective at inhibiting thrombin bound to fibrin because a 20-fold higher concentration is necessary to block 70% of the activity of the clot-bound enzyme than is required for equivalent inhibition of fluid-phase thrombin (2.0 and 0.1 U/ml, respectively).	Heparin	9-16	coagulation factor II, thrombin	Homo sapiens	243-251
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	43-51
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	149-157
2196322-2	1990	A role for HCII as an inhibitor of thrombin in the presence of dermatan sulfate and heparin has been proposed.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	35-43
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	149-157
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	149-157
2120427-17	1990	The discharge of Ca stores by dialysis with 0.1 mM-GTP gamma S was prevented completely by heparin included in the pipette solution, suggesting that activation of a G-protein associated with phospholipase C (PLC) enzyme accelerates PLC activity.	Heparin	91-98	LOC100009319	Oryctolagus cuniculus	191-206
2120427-17	1990	The discharge of Ca stores by dialysis with 0.1 mM-GTP gamma S was prevented completely by heparin included in the pipette solution, suggesting that activation of a G-protein associated with phospholipase C (PLC) enzyme accelerates PLC activity.	Heparin	91-98	LOC100009319	Oryctolagus cuniculus	208-211
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	43-51
2120427-17	1990	The discharge of Ca stores by dialysis with 0.1 mM-GTP gamma S was prevented completely by heparin included in the pipette solution, suggesting that activation of a G-protein associated with phospholipase C (PLC) enzyme accelerates PLC activity.	Heparin	91-98	LOC100009319	Oryctolagus cuniculus	232-235
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	149-157
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	149-157
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	125-132	coagulation factor II, thrombin	Homo sapiens	149-157
2237824-4	1990	As affinity decreased, the ability of the heparin fractions to increase the rate of the ATIII-thrombin reactions decreased, and these fractions slightly more effectively increased the rate of thrombin inhibition by the higher-affinity ATIII isoform.	Heparin	42-49	coagulation factor II, thrombin	Homo sapiens	94-102
1699446-9	1990	In addition, we use the procedure to characterize the heparin-binding properties of heparin-binding growth factor 1 (acidic fibroblast growth factor) with synthetic peptide competitors and site-directed mutants of the growth factor.	Heparin	54-61	fibroblast growth factor 1	Homo sapiens	84-115
2122536-6	1990	Levels of thrombin-antithrombin complexes (TAT) were significantly increased in the heparin group 2 hours after embolization, indicating that thrombin activity had been formed.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	10-18
2122536-6	1990	Levels of thrombin-antithrombin complexes (TAT) were significantly increased in the heparin group 2 hours after embolization, indicating that thrombin activity had been formed.	Heparin	84-91	coagulation factor II, thrombin	Homo sapiens	23-31
2237824-1	1990	Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin.	Heparin	44-51	coagulation factor II, thrombin	Homo sapiens	78-86
2237824-1	1990	Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin.	Heparin	181-188	coagulation factor II, thrombin	Homo sapiens	78-86
2237824-2	1990	Heparin with low-affinity for ATIII increased the rate of thrombin inhibition by the higher affinity isoform about 10-fold more effectively than by the other isoform.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	58-66
2078567-0	1990	Structural requirements for neural cell adhesion molecule-heparin interaction.	Heparin	58-65	neural cell adhesion molecule 1	Mus musculus	28-57
2176902-4	1990	Heparin promotion of thrombin inactivation by heparin cofactor II may occur by a similar mechanism.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	21-29
2176902-6	1990	Binding of heparin to both thrombin and antithrombin III interferes with thrombin inactivation.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	27-35
2176902-6	1990	Binding of heparin to both thrombin and antithrombin III interferes with thrombin inactivation.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	44-52
2176902-8	1990	Low ionic strength in in vitro reactions also results in cleavage of antithrombin III by thrombin in the presence of heparin and effectively converts antithrombin III from an inhibitor to a substrate.	Heparin	117-124	coagulation factor II, thrombin	Homo sapiens	73-81
2078567-1	1990	Two biological domains have been identified in the amino terminal region of the neural cell adhesion molecule (NCAM): a homophilic-binding domain, responsible for NCAM-NCAM interactions, and a heparin-binding domain (HBD).	Heparin	193-200	neural cell adhesion molecule 1	Mus musculus	80-109
2078567-1	1990	Two biological domains have been identified in the amino terminal region of the neural cell adhesion molecule (NCAM): a homophilic-binding domain, responsible for NCAM-NCAM interactions, and a heparin-binding domain (HBD).	Heparin	193-200	neural cell adhesion molecule 1	Mus musculus	111-115
2078567-1	1990	Two biological domains have been identified in the amino terminal region of the neural cell adhesion molecule (NCAM): a homophilic-binding domain, responsible for NCAM-NCAM interactions, and a heparin-binding domain (HBD).	Heparin	193-200	exocyst complex component 6	Mus musculus	217-220
2078567-3	1990	To approach this question, we have further defined the relationship between NCAM-heparin binding and cell adhesion.	Heparin	81-88	neural cell adhesion molecule 1	Mus musculus	76-80
2078567-10	1990	These results confirm that this region of the NCAM polypeptide does indeed mediate not only the large majority of NCAM"s affinity for heparin but also a significant portion of the cell-adhesion-mediating capability of NCAM.	Heparin	134-141	neural cell adhesion molecule 1	Mus musculus	46-50
2078567-10	1990	These results confirm that this region of the NCAM polypeptide does indeed mediate not only the large majority of NCAM"s affinity for heparin but also a significant portion of the cell-adhesion-mediating capability of NCAM.	Heparin	134-141	neural cell adhesion molecule 1	Mus musculus	114-118
2078567-10	1990	These results confirm that this region of the NCAM polypeptide does indeed mediate not only the large majority of NCAM"s affinity for heparin but also a significant portion of the cell-adhesion-mediating capability of NCAM.	Heparin	134-141	neural cell adhesion molecule 1	Mus musculus	114-118
2143417-2	1990	Kinetic studies indicate that both heparin and heparan increase the kcat of t-PA-mediated Pg activation by 25- and 3.5-fold, respectively.	Heparin	35-42	plasminogen activator, tissue type	Homo sapiens	76-80
2119386-1	1990	Basic fibroblast growth factor (bFGF) is a heparin-binding growth factor, so it was usually purified by affinity chromatography on a heparin-grafted support.	Heparin	43-50	fibroblast growth factor 2	Bos taurus	0-30
2143417-4	1990	Both heparin and heparan stimulate the activity of t-PA by interacting with the finger domain of t-PA, with association constants of 1 microM and 200 nM, respectively.	Heparin	5-12	plasminogen activator, tissue type	Homo sapiens	51-55
2119386-1	1990	Basic fibroblast growth factor (bFGF) is a heparin-binding growth factor, so it was usually purified by affinity chromatography on a heparin-grafted support.	Heparin	43-50	fibroblast growth factor 2	Bos taurus	32-36
2143417-4	1990	Both heparin and heparan stimulate the activity of t-PA by interacting with the finger domain of t-PA, with association constants of 1 microM and 200 nM, respectively.	Heparin	5-12	plasminogen activator, tissue type	Homo sapiens	97-101
2350542-1	1990	A tetrasaccharide possessing a biosynthetically permissible structural variability in and adjacent to the antithrombin III (ATIII) binding site has been isolated from heparin lyase depolymerized bovine lung heparin by using strong anion-exchange high-pressure liquid chromatography (SAX-HPLC).	Heparin	167-174	serpin family C member 1	Bos taurus	106-122
2112543-7	1990	The inhibition of factor XIa by PN-2/APP was augmented by heparin and resulted in a Ki = 5.5 x 10(-11) M. Trypsin and chymotrypsin were also effectively inhibited with a Ki = 4.2 x 10(-10) and 1.6 x 10(-9), respectively.	Heparin	58-65	amyloid beta precursor protein	Homo sapiens	32-36
2214638-3	1990	Consequent to heparin treatment controlled by measurements of residual thrombin activity, the indices showed a trend towards normalization.	Heparin	14-21	coagulation factor II, thrombin	Homo sapiens	71-79
2372116-1	1990	125I-labeled heparin was used to detect basic fibroblast growth factor (bFGF) in crude tumor cell extracts after separation by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	40-70
2372116-1	1990	125I-labeled heparin was used to detect basic fibroblast growth factor (bFGF) in crude tumor cell extracts after separation by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	72-76
2372116-2	1990	125I-labeled heparin bound avidly to native recombinant bFGF immobilized on nitrocellulose and eluted with 1.5-2.0 M NaCl.	Heparin	13-20	fibroblast growth factor 2	Homo sapiens	56-60
2372116-3	1990	However, Western transfer of bFGF to nitrocellulose after SDS-polyacrylamide gel electrophoresis destroyed heparin-binding ability.	Heparin	107-114	fibroblast growth factor 2	Homo sapiens	29-33
2372116-4	1990	In contrast, bFGF was detected by incubation of the polyacrylamide gels directly with 125I-labeled heparin in a gel overly technique.	Heparin	99-106	fibroblast growth factor 2	Homo sapiens	13-17
2205950-4	1990	Protease I destroyed the heparin binding domain in human vWF.	Heparin	25-32	von Willebrand factor	Homo sapiens	57-60
2402743-4	1990	The minimum dose of heparin which protected mice from the lethal effect of thrombin or tissue factor was 6 units or approximately 3.3 nmoles.	Heparin	20-27	coagulation factor II	Mus musculus	75-83
2166971-4	1990	UFH to subcutaneous Fraxiparine induced a significant increase of the thrombin time and of the APTT, so explained by the activity of UFH.	Heparin	0-3	coagulation factor II, thrombin	Homo sapiens	70-78
2166971-4	1990	UFH to subcutaneous Fraxiparine induced a significant increase of the thrombin time and of the APTT, so explained by the activity of UFH.	Heparin	133-136	coagulation factor II, thrombin	Homo sapiens	70-78
2192729-4	1990	The appearance of DIC in shock and shock in DIC are potentially life-threatening conditions in the critically ill. Medical management can include anticoagulant therapy, such as heparin, and replacement of clotting factors and platelets.	Heparin	177-184	solute carrier family 25 member 10	Homo sapiens	18-21
2192729-4	1990	The appearance of DIC in shock and shock in DIC are potentially life-threatening conditions in the critically ill. Medical management can include anticoagulant therapy, such as heparin, and replacement of clotting factors and platelets.	Heparin	177-184	solute carrier family 25 member 10	Homo sapiens	44-47
1972179-3	1990	This TNF-dependent EO cytotoxicity is strongly inhibited by heparin and methyprednisolone but unaffected by the platelet-activating factor antagonist BN52012 or scavengers of superoxide anion and H2O2, superoxide dismutase and catalase.	Heparin	60-67	tumor necrosis factor	Homo sapiens	5-8
2116167-2	1990	Kinetic analyses showed a marked increase in the affinity of t-PA for Lys-plasminogen in the presence of heparin-inserted phosphatidylcholine (PC) liposomes.	Heparin	105-112	plasminogen activator, tissue type	Homo sapiens	61-65
2116167-3	1990	The catalytic efficiency (kcat/Km) of t-PA for the plasminogen activation on the surface of heparin-inserted PC liposomes was 5.4 times that on the surface of heparin-free PC liposomes.	Heparin	92-99	plasminogen activator, tissue type	Homo sapiens	38-42
2116167-3	1990	The catalytic efficiency (kcat/Km) of t-PA for the plasminogen activation on the surface of heparin-inserted PC liposomes was 5.4 times that on the surface of heparin-free PC liposomes.	Heparin	159-166	plasminogen activator, tissue type	Homo sapiens	38-42
2116167-7	1990	t-PA-induced clot lysis of euglobulin or whole plasma, which contained native (Glu-) plasminogen and the above inhibitors, was also accelerated by addition of heparin-inserted PC liposomes.	Heparin	159-166	plasminogen activator, tissue type	Homo sapiens	0-4
2350542-1	1990	A tetrasaccharide possessing a biosynthetically permissible structural variability in and adjacent to the antithrombin III (ATIII) binding site has been isolated from heparin lyase depolymerized bovine lung heparin by using strong anion-exchange high-pressure liquid chromatography (SAX-HPLC).	Heparin	167-174	serpin family C member 1	Bos taurus	124-129
2350542-6	1990	The predominant ATIII-binding site in porcine heparin contained an N-acetylated glucosamine residue.	Heparin	46-53	serpin family C member 1	Bos taurus	16-21
2350542-7	1990	We now report the structure of the predominant ATIII-binding site in bovine heparin as----4)-alpha-D-GlcNp2S6S(1----4)-beta-D-GlcAp(1----4)-alph a-D- GlcNp2S3S6S(1----4)-alpha-L-IdoAp2S(1----4)-alpha-D-GlcNp 2S6S(1----.	Heparin	76-83	serpin family C member 1	Bos taurus	47-52
2183588-10	1990	More heparin would have been used during the LSH period compared to the HSH period of physicians were to use the APTT ratio method for monitoring the therapy.	Heparin	5-12	helicase, lymphoid specific	Homo sapiens	45-48
2349545-1	1990	I: Impaired heparin binding caused by an Arg47 to his (CGT to CAT) substitution.	Heparin	12-19	catalase	Homo sapiens	62-65
2337981-0	1990	Effects of methylamine and heparin on a rapid chromogenic assay of C1-esterase inhibitor in plasma.	Heparin	27-34	complement C1s	Homo sapiens	67-78
2337121-1	1990	Treatment with neutral protamine Hagedorn (NPH) insulin predisposes individuals with diabetes to anaphylactoid reactions when given bolus protamine for heparin reversal during cardiovascular procedures.	Heparin	152-159	insulin	Homo sapiens	48-55
2337121-10	1990	Because of the frequency of protamine antibody production and the risk of anaphylaxis to bolus protamine administration in NPH treated diabetics, the authors suggest that NPH insulin-treated individuals should avoid heparin reversal by protamine.	Heparin	216-223	insulin	Homo sapiens	175-182
2341158-2	1990	Determination of THBS1 gene structure has revealed that the type I repeat modules are encoded by symmetrical exons and that the heparin-binding domain is encoded by a single exon.	Heparin	128-135	thrombospondin 1	Homo sapiens	17-22
2327990-4	1990	Complex-formation between kallikrein and the binding protein is inhibited by heparin, whereas that between kallikrein and alpha 1-antitrypsin is heparin-resistant.	Heparin	145-152	serpin family A member 1	Homo sapiens	122-141
2334697-7	1990	Heparin or high salt, which drastically affects the hydrodynamic properties of fibronectin, had virtually no effect on the distance between the SH1-SH1 or the SH1-SH2 pair.	Heparin	0-7	fibronectin 1	Homo sapiens	79-90
2340212-4	1990	Serial thrombin times and platelet aggregation improved during heparin-free hemodialysis.	Heparin	63-70	coagulation factor II, thrombin	Homo sapiens	7-15
2347433-3	1990	The heparin cofactor heparin and dermatan sulfate-dependent inhibition of thrombin was significantly reduced, showing a remarkable decrease of the maximum second order rate constant.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	74-82
2318909-3	1990	In the presence of heparin (90 micrograms/ml), this effect is reproduced upon treatment with acidic fibroblast growth factor (aFGF, 6 ng/ml) or endothelial cell growth supplement (ECGS, 100 micrograms/ml), in both human umbilical vein endothelial cells (HUVEC) and BAEC.	Heparin	19-26	fibroblast growth factor 1	Homo sapiens	93-124
2318909-3	1990	In the presence of heparin (90 micrograms/ml), this effect is reproduced upon treatment with acidic fibroblast growth factor (aFGF, 6 ng/ml) or endothelial cell growth supplement (ECGS, 100 micrograms/ml), in both human umbilical vein endothelial cells (HUVEC) and BAEC.	Heparin	19-26	fibroblast growth factor 1	Homo sapiens	126-130
2307707-0	1990	RGD-independent cell adhesion to the carboxy-terminal heparin-binding fragment of fibronectin involves heparin-dependent and -independent activities.	Heparin	54-61	fibronectin 1	Homo sapiens	82-93
2322465-7	1990	This range of specificities of biological action was also seen with both acidic and basic FGF in the presence of heparin.	Heparin	113-120	fibroblast growth factor 10	Gallus gallus	90-93
2275170-2	1990	The heparin test enables in heparin-treated patients to distinguish real afibrinogenemia from false when the blood plasma retains fibrinogen blocked and noncoagulable with thrombin.	Heparin	4-11	coagulation factor II, thrombin	Homo sapiens	172-180
2341544-1	1990	The heparin-binding growth factors aFGF and bFGF (acidic and basic fibroblast growth factor) from crude bovine brain extract were co-eluted with purified [125I]aFGF and/or [125I]bFGF as tracers from heparin-Sepharose and from several insoluble substituted polystyrenes used as stationary phases in low-pressure affinity chromatography.	Heparin	4-11	fibroblast growth factor 2	Bos taurus	44-48
2341544-1	1990	The heparin-binding growth factors aFGF and bFGF (acidic and basic fibroblast growth factor) from crude bovine brain extract were co-eluted with purified [125I]aFGF and/or [125I]bFGF as tracers from heparin-Sepharose and from several insoluble substituted polystyrenes used as stationary phases in low-pressure affinity chromatography.	Heparin	4-11	fibroblast growth factor 2	Bos taurus	61-91
2155580-3	1990	Incubation of cytosol with heparin resulted in a shift of the [3H]TCDD:AhR complex to a smaller sedimenting form in all species.	Heparin	27-34	aryl-hydrocarbon receptor	Mus musculus	71-74
2155580-4	1990	Mouse TCDD:AhR complex sedimented at 8-10 S when cytosol was simultaneously incubated with high salt and heparin, indicating that the interaction of heparin with the AhR was electrostatic in nature.	Heparin	105-112	aryl-hydrocarbon receptor	Mus musculus	11-14
2155580-4	1990	Mouse TCDD:AhR complex sedimented at 8-10 S when cytosol was simultaneously incubated with high salt and heparin, indicating that the interaction of heparin with the AhR was electrostatic in nature.	Heparin	105-112	aryl-hydrocarbon receptor	Mus musculus	166-169
2155580-4	1990	Mouse TCDD:AhR complex sedimented at 8-10 S when cytosol was simultaneously incubated with high salt and heparin, indicating that the interaction of heparin with the AhR was electrostatic in nature.	Heparin	149-156	aryl-hydrocarbon receptor	Mus musculus	11-14
2155580-4	1990	Mouse TCDD:AhR complex sedimented at 8-10 S when cytosol was simultaneously incubated with high salt and heparin, indicating that the interaction of heparin with the AhR was electrostatic in nature.	Heparin	149-156	aryl-hydrocarbon receptor	Mus musculus	166-169
2155580-5	1990	Incubation of heparin-dissociated mouse TCDD:AhR complex (5-6 S) with high salt resulted in reassociation of AhR to a form which sediments at 8-10 S. Our data suggests that the resistance of mouse AhR to salt-mediated dissociation may be due to a property of the receptor protein itself and also indicates that mouse hepatic cytosolic AhR is distinctly different from that present in all other species examined to date.	Heparin	14-21	aryl-hydrocarbon receptor	Mus musculus	45-48
2155580-5	1990	Incubation of heparin-dissociated mouse TCDD:AhR complex (5-6 S) with high salt resulted in reassociation of AhR to a form which sediments at 8-10 S. Our data suggests that the resistance of mouse AhR to salt-mediated dissociation may be due to a property of the receptor protein itself and also indicates that mouse hepatic cytosolic AhR is distinctly different from that present in all other species examined to date.	Heparin	14-21	aryl-hydrocarbon receptor	Mus musculus	109-112
2155580-5	1990	Incubation of heparin-dissociated mouse TCDD:AhR complex (5-6 S) with high salt resulted in reassociation of AhR to a form which sediments at 8-10 S. Our data suggests that the resistance of mouse AhR to salt-mediated dissociation may be due to a property of the receptor protein itself and also indicates that mouse hepatic cytosolic AhR is distinctly different from that present in all other species examined to date.	Heparin	14-21	aryl-hydrocarbon receptor	Mus musculus	109-112
2155580-5	1990	Incubation of heparin-dissociated mouse TCDD:AhR complex (5-6 S) with high salt resulted in reassociation of AhR to a form which sediments at 8-10 S. Our data suggests that the resistance of mouse AhR to salt-mediated dissociation may be due to a property of the receptor protein itself and also indicates that mouse hepatic cytosolic AhR is distinctly different from that present in all other species examined to date.	Heparin	14-21	aryl-hydrocarbon receptor	Mus musculus	109-112
2107185-2	1990	We observed a marked diminution in both spontaneous and inducible production of prostacyclin (PGI2) by human umbilical vein and saphenous vein endothelial cells when they were cultured in the presence of the heparin-binding growth factor, acidic fibroblast growth factor (aFGF) and heparin, compared with PGI2 production during culture in medium lacking these factors.	Heparin	208-215	fibroblast growth factor 1	Homo sapiens	239-270
2107185-2	1990	We observed a marked diminution in both spontaneous and inducible production of prostacyclin (PGI2) by human umbilical vein and saphenous vein endothelial cells when they were cultured in the presence of the heparin-binding growth factor, acidic fibroblast growth factor (aFGF) and heparin, compared with PGI2 production during culture in medium lacking these factors.	Heparin	208-215	fibroblast growth factor 1	Homo sapiens	272-276
2107185-4	1990	Heparin (1-100 micrograms/ml) strongly potentiated the effects of aFGF but had a limited and variable effect alone.	Heparin	0-7	fibroblast growth factor 1	Homo sapiens	66-70
2107185-8	1990	These studies indicate that heparin acts as a modulator of prostaglandin synthesis in endothelial cells through its interaction with aFGF, mediated by alterations in two key enzymes in the arachidonate metabolic pathway.	Heparin	28-35	fibroblast growth factor 1	Homo sapiens	133-137
2106684-1	1990	Heparin stimulates the activity of tissue plasminogen activator (t-PA) and binds to t-PA.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	35-69
2106684-6	1990	Both fractions of heparin effectively accelerate inactivation of thrombin by antithrombin III.	Heparin	18-25	coagulation factor II, thrombin	Homo sapiens	65-73
2339369-6	1990	Forty-eight hours after SK, a new fibrinogen hyperfunction, related to an increase in fibrinogen level and especially HMW synthesized fibrinogen (82 +/- 1 or 81 +/- 1%, 800,000 and 1.5 mill U SK, respectively) was observed, which was neutralized by heparin therapy (1,660 U/h with continuous infusion).	Heparin	249-256	fibrinogen beta chain	Homo sapiens	34-44
2388713-2	1990	Because of its mitogenic activity for vascular endothelial cells and its ability to strongly bind heparin it was termed heparin-binding brain mitogen (HBBM).	Heparin	98-105	pleiotrophin	Homo sapiens	120-149
2388713-2	1990	Because of its mitogenic activity for vascular endothelial cells and its ability to strongly bind heparin it was termed heparin-binding brain mitogen (HBBM).	Heparin	98-105	pleiotrophin	Homo sapiens	151-155
2310762-4	1990	When isolated livers from both 1- and 5-day-old pups were perfused with heparin, a sharp peak of lipoprotein lipase activity appeared in the perfusate.	Heparin	72-79	lipoprotein lipase	Rattus norvegicus	97-115
2180218-3	1990	Although all patients who receive heparin may have reduced aldosterone levels, most are able to compensate through increased renin production and therefore remain asymptomatic.	Heparin	34-41	renin	Homo sapiens	125-130
2160449-8	1990	The inhibitory rates for activated protein C and thrombin were accelerated significantly in the presence of heparin or negatively charged dextran sulfate.	Heparin	108-115	coagulation factor II, thrombin	Homo sapiens	49-57
2106874-10	1990	In the nine investigated cases, the secreted EC-SOD was of the high-heparin-affinity C type.	Heparin	68-75	superoxide dismutase 3	Homo sapiens	45-51
2307707-0	1990	RGD-independent cell adhesion to the carboxy-terminal heparin-binding fragment of fibronectin involves heparin-dependent and -independent activities.	Heparin	103-110	fibronectin 1	Homo sapiens	82-93
2307707-2	1990	Our previous results have demonstrated that normal and transformed cells adhere and spread on a 33-kD heparin binding fragment that originates from the carboxy-terminal end of particular isoforms (A-chains) of human fibronectin.	Heparin	102-109	fibronectin 1	Homo sapiens	216-227
2307707-4	1990	Two synthetic peptides from this region of fibronectin were recently identified that bound [3H]heparin in a solid-phase assay and promoted the adhesion and spreading of melanoma cells (McCarthy, J.	Heparin	95-102	fibronectin 1	Homo sapiens	43-54
2303431-5	1990	Sulfatide binding by both forms of properdin is inhibited by dextran sulfate (Mr = 500,000) or fucoidan, whereas only the activated form is inhibited by dextran sulfate (Mr = 5,000) or heparin.	Heparin	185-192	complement factor properdin	Homo sapiens	35-44
2083241-6	1990	Fibronectin could also dissociate LDL-heparin complexes formed on heparin-Sepharose affinity columns.	Heparin	38-45	fibronectin 1	Homo sapiens	0-11
2158150-0	1990	Heparin enhances thrombin-stimulated prostaglandin I2 production by cultured endothelial cells.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	17-25
2158150-3	1990	Pretreatment of cells with either UFH or LMWH also enhanced the thrombin stimulation.	Heparin	34-37	coagulation factor II, thrombin	Homo sapiens	64-72
2310377-7	1990	Immunoblotting of heparin-purified beta UDGF indicated that the beta UDGF doublet is immunologically related to the 146-amino-acid form of bovine basic fibroblast growth factor (bFGF), and that the 17.2 kDa component is an N-terminally truncated form of the 17.7 kDa component.	Heparin	18-25	fibroblast growth factor 2	Bos taurus	146-176
2153562-2	1990	The activity binds to heparin-Sepharose and it is quenched by polyclonal anti-human placental basic fibroblast growth factor (bFGF) antibodies.	Heparin	22-29	fibroblast growth factor 2	Bos taurus	94-124
2153562-2	1990	The activity binds to heparin-Sepharose and it is quenched by polyclonal anti-human placental basic fibroblast growth factor (bFGF) antibodies.	Heparin	22-29	fibroblast growth factor 2	Bos taurus	126-130
2153562-3	1990	In the serum-free conditioned medium of FBAE cells, the anti-bFGF antiserum recognizes an immunorective Mr 20,000 molecule which co-purifies with the mitogenic and PA-inducing activity on a heparin-Sepharose column.	Heparin	190-197	fibroblast growth factor 2	Bos taurus	61-65
1963017-6	1990	Therefore, unfractionated heparin in platelet rich plasma acts only on the lag phase of thrombin production and not on the amount of thrombin produced.	Heparin	26-33	coagulation factor II, thrombin	Homo sapiens	88-96
2298919-2	1990	In this report we describe the purification from several normal human hearts (including a very fresh, nonischemic sample) of heparin-binding, acid-, heat- and trypsin-sensitive 14-18-kD peptides that crossreact with antisera against aFGF and bFGF.	Heparin	125-132	fibroblast growth factor 1	Homo sapiens	233-237
2298919-2	1990	In this report we describe the purification from several normal human hearts (including a very fresh, nonischemic sample) of heparin-binding, acid-, heat- and trypsin-sensitive 14-18-kD peptides that crossreact with antisera against aFGF and bFGF.	Heparin	125-132	fibroblast growth factor 2	Homo sapiens	242-246
2303528-3	1990	In the presence of heparin, aFGF was as potent as EGF.	Heparin	19-26	fibroblast growth factor 1	Mus musculus	28-32
2315894-5	1990	The high affinity fractions of native heparin and the sulfated material were almost equally effective in enhancing the rate of thrombin neutralization by ATIII.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	127-135
2294104-0	1990	Heparin promotes the binding of thrombin to fibrin polymer.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	32-40
2294104-6	1990	These studies indicate that heparin enhances the binding of thrombin to fibrin polymer 6.4-fold with an overall dissociation constant for ternary complex formation of 705 nM2.	Heparin	28-35	coagulation factor II, thrombin	Homo sapiens	60-68
2294104-8	1990	Heparins of molecular weights 11,200-20,300 behave similarly with respect to their influence on ternary complex formation, whereas heparins of lower molecular weight are less effective in promoting thrombin binding to fibrin polymer.	Heparin	131-139	coagulation factor II, thrombin	Homo sapiens	198-206
2294105-2	1990	The effects of fibrin II monomer and heparin on chromogenic substrate hydrolysis can be described by a hyperbolic mixed inhibition model in which substrate can interact with four possible enzyme species (IIa, IIa.H, IIa.FnIIm, and IIa.FnIIm.H) that arise as a result of random formation of a ternary complex among thrombin, fibrin II monomer, and heparin (Hogg, P. J. and Jackson, C. M. (1990) J. Biol.	Heparin	37-44	coagulation factor II, thrombin	Homo sapiens	314-341
2294105-6	1990	Fibrin II monomer and heparin in combination also decrease the efficiency (kc/Km) with which thrombin cleaves prothrombin to produce Fragment 1 and Prethrombin 1 by 2.3-fold from 607 +/- 30 to 264 +/- 13 M-1 s-1.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	93-101
2294105-13	1990	These observations indicate that the substrate specificity of thrombin is altered when it is bound in a complex with fibrin II monomer and heparin and suggest that the catalytic efficiency of thrombin for its physiological substrates will be affected differentially by these interactions.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	62-70
2294105-13	1990	These observations indicate that the substrate specificity of thrombin is altered when it is bound in a complex with fibrin II monomer and heparin and suggest that the catalytic efficiency of thrombin for its physiological substrates will be affected differentially by these interactions.	Heparin	139-146	coagulation factor II, thrombin	Homo sapiens	192-200
2105372-0	1990	Heparin inhibits spontaneous thrombolysis and the thrombolytic effect of both streptokinase and tissue-type plasminogen activator.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	96-129
2105372-4	1990	Heparin (1 U/ml), when added with streptokinase (SK) or tissue-type plasminogen activator (rt-PA) prior to thrombus formation, considerably delayed thrombolysis.	Heparin	0-7	plasminogen activator, tissue type	Homo sapiens	56-89
1963017-7	1990	Low molecular weight heparins significantly prolong the lag time and inhibit the thrombin peak in platelet rich plasma.	Heparin	21-29	coagulation factor II, thrombin	Homo sapiens	81-89
2288180-6	1990	have described an increase in t-PA and u-PA binding to endothelium by pre-incubation of endothelial cells with unfractionated heparin.	Heparin	126-133	plasminogen activator, tissue type	Homo sapiens	30-34
2288180-6	1990	have described an increase in t-PA and u-PA binding to endothelium by pre-incubation of endothelial cells with unfractionated heparin.	Heparin	126-133	plasminogen activator, urokinase	Homo sapiens	39-43
1688695-8	1990	Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III.	Heparin	76-83	coagulation factor II, thrombin	Homo sapiens	60-68
1706557-5	1990	Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF).	Heparin	49-56	fibroblast growth factor 1	Homo sapiens	107-117
1706557-5	1990	Mitogenic activity in the 1.2 M NaCl fraction of Heparin-Sepharose chromatography suggests the presence of acidic FGF (aFGF).	Heparin	49-56	fibroblast growth factor 1	Homo sapiens	119-123
2138364-5	1990	These data in vitro confirm that thrombin inhibition induced by DS is accompanied by a far lesser aPTT prolongation compared to heparin, without any appreciable interference with platelet function.	Heparin	128-135	coagulation factor II, thrombin	Homo sapiens	33-41
1688695-8	1990	Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III.	Heparin	109-116	coagulation factor II, thrombin	Homo sapiens	60-68
2302436-4	1990	We demonstrate that this activity actually corresponds to LPL, since it is inhibited by either 1.5 M NaCl or 1.5 mg/ml protamine sulfate, is serum-dependent, and could be separated from hepatic lipase activity by using heparin-Sepharose affinity chromatography.	Heparin	219-226	lipoprotein lipase	Rattus norvegicus	58-61
2155017-6	1990	PTT and thrombin time were only marginally effected by LMW heparin, whereas they were markedly prolonged by SH heparin.	Heparin	59-66	coagulation factor II, thrombin	Homo sapiens	8-16
2099218-7	1990	Heparin-sorbent is the sorbent of limited selectivity, apo-B content in eluate is 40-60% of the total protein content, but it is important that it does not bind HDL.	Heparin	0-7	apolipoprotein B	Homo sapiens	55-60
2344455-1	1990	Using affinity chromatography on heparin-Sepharose 4B, triglyceride lipase was isolated from rabbit liver tissue and purified.	Heparin	33-40	pancreatic triacylglycerol lipase	Oryctolagus cuniculus	55-74
2083864-3	1990	Heparin subcutaneously (200 U/kg) injected for 2 weeks resulted in an enhanced inactivation of thrombin and factor Xa by the endothelium.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	95-103
2142645-2	1990	Sequence analysis predicted the hst-1 product to be a novel growth factor with 30-50% homology with six other heparin-binding growth factors: basic and acidic fibroblast growth factors (FGFs), the int-2 protein, FGF5, the hst-2/FGF6 protein and keratinocyte growth factor (KGF).	Heparin	110-117	fibroblast growth factor 4	Homo sapiens	32-37
2245044-6	1990	Heparin greatly potentiates the stimulatory effect of low concentrations of bFGF.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	76-80
2257150-3	1990	This molecule was identified as bFGF on the basis of its molecular weight, its affinity for heparin, its capacity to induce plasminogen activator production and cell proliferation in endothelial GM 7373 cells, and its cross-reactivity with various anti-bFGF antibodies.	Heparin	92-99	fibroblast growth factor 2	Bos taurus	32-36
2081384-1	1990	The thrombin clotting time (TCT) has been used at our institution, along with the activated partial thromboplastin time (aPTT), for monitoring heparin therapy.	Heparin	143-150	coagulation factor II, thrombin	Homo sapiens	4-12
2318134-2	1990	The above rTNF effect could be considerably inhibited by the single heparin injection.	Heparin	68-75	tumor necrosis factor	Rattus norvegicus	10-14
1688801-0	1990	The effect of heparin on fibronectin and thrombospondin synthesis and mRNA levels in cultured human endothelial cells.	Heparin	14-21	fibronectin 1	Homo sapiens	25-36
1688801-0	1990	The effect of heparin on fibronectin and thrombospondin synthesis and mRNA levels in cultured human endothelial cells.	Heparin	14-21	thrombospondin 1	Homo sapiens	41-55
1688801-2	1990	Using pulse-labeling and ELISA techniques, we found that EC grown in the presence of heparin (90 micrograms/ml) and endothelial cell growth factor (ECGF) synthesized 50% less fibronectin (FN) than did ECGF-treated control cultures.	Heparin	85-92	fibronectin 1	Homo sapiens	175-186
1688801-2	1990	Using pulse-labeling and ELISA techniques, we found that EC grown in the presence of heparin (90 micrograms/ml) and endothelial cell growth factor (ECGF) synthesized 50% less fibronectin (FN) than did ECGF-treated control cultures.	Heparin	85-92	fibronectin 1	Homo sapiens	188-190
1688801-2	1990	Using pulse-labeling and ELISA techniques, we found that EC grown in the presence of heparin (90 micrograms/ml) and endothelial cell growth factor (ECGF) synthesized 50% less fibronectin (FN) than did ECGF-treated control cultures.	Heparin	85-92	fibroblast growth factor 1	Homo sapiens	201-205
1688801-4	1990	The effect of heparin on EC FN synthesis was independent of whether the cells were cultivated on plastic or gelatin substrates.	Heparin	14-21	fibronectin 1	Homo sapiens	28-30
1688801-5	1990	However, ECGF modulates the effect of heparin on EC synthesis of FN.	Heparin	38-45	fibroblast growth factor 1	Homo sapiens	9-13
1688801-5	1990	However, ECGF modulates the effect of heparin on EC synthesis of FN.	Heparin	38-45	fibronectin 1	Homo sapiens	65-67
1688801-6	1990	RNA slot-blot analysis demonstrated that heparin treatment specifically decreased the steady-state mRNA levels for both FN and TSP in the cells.	Heparin	41-48	fibronectin 1	Homo sapiens	120-122
1688801-6	1990	RNA slot-blot analysis demonstrated that heparin treatment specifically decreased the steady-state mRNA levels for both FN and TSP in the cells.	Heparin	41-48	thrombospondin 1	Homo sapiens	127-130
1688801-8	1990	These data suggest that heparin decreases EC expression of FN at least in part by decreasing the amount of FN mRNA available for translation.	Heparin	24-31	fibronectin 1	Homo sapiens	59-61
1688801-8	1990	These data suggest that heparin decreases EC expression of FN at least in part by decreasing the amount of FN mRNA available for translation.	Heparin	24-31	fibronectin 1	Homo sapiens	107-109
1964661-1	1990	Low molecular weight (LMW) heparins achieve their anticoagulant effects by inhibiting prothrombin activation, catalyzing endogenous thrombin inhibition, and binding thrombin.	Heparin	27-35	coagulation factor II, thrombin	Homo sapiens	89-97
1964661-1	1990	Low molecular weight (LMW) heparins achieve their anticoagulant effects by inhibiting prothrombin activation, catalyzing endogenous thrombin inhibition, and binding thrombin.	Heparin	27-35	coagulation factor II, thrombin	Homo sapiens	132-140
1964667-0	1990	Mode of action of unfractionated and low molecular weight heparins on the generation of thrombin in plasma.	Heparin	58-66	coagulation factor II, thrombin	Homo sapiens	88-96
1964667-1	1990	Heparins, unfractionated and low molecular weight, act primarily by their scavenging of thrombin (S-type heparins).	Heparin	0-8	coagulation factor II, thrombin	Homo sapiens	88-96
1964667-1	1990	Heparins, unfractionated and low molecular weight, act primarily by their scavenging of thrombin (S-type heparins).	Heparin	105-113	coagulation factor II, thrombin	Homo sapiens	88-96
1964667-5	1990	In platelet-rich plasma heparins retard platelet activation by lowering thrombin levels.	Heparin	24-32	coagulation factor II, thrombin	Homo sapiens	72-80
1964669-3	1990	Heparin binding by monocytes is affected by cell stimulation with an increase of the availability of binding sites after challenge with calcium ionophore, lipopolysaccharide, and interleukin 2.	Heparin	0-7	interleukin 2	Homo sapiens	179-192
2083865-8	1990	The activities of thrombin and other serine proteases are modulated by the serine protease inhibitors (serpins), including antithrombin III and heparin cofactor II which are important in regulating the physiological anticoagulant action of glycosaminoglycans at the endothelium and the pharmacological action of heparin.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	18-26
2099323-1	1990	Defibrotide (DEF), an antithrombotic drug with no anticoagulant activity, given concomitantly with heparin potentiates its effects on thrombin time and lipase-releasing activity.	Heparin	99-106	coagulation factor II, thrombin	Homo sapiens	134-142
2295682-5	1990	N-CAM-coated beads did not aggregate, but did so after addition of heparin.	Heparin	67-74	neural cell adhesion molecule 1	Mus musculus	0-5
2084119-1	1990	Basic fibroblast growth factor (bFGF), a heparin-binding mitogen for mesoderm-derived cells, also acts as a mitogen, differentiation inducing and maintenance factor for many neuroectodermal cells including glial cells, neurons, paraneurons, and their tumor counterparts.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	0-30
2084119-1	1990	Basic fibroblast growth factor (bFGF), a heparin-binding mitogen for mesoderm-derived cells, also acts as a mitogen, differentiation inducing and maintenance factor for many neuroectodermal cells including glial cells, neurons, paraneurons, and their tumor counterparts.	Heparin	41-48	fibroblast growth factor 2	Homo sapiens	32-36
2298818-10	1990	The plasma thrombin inhibitor, antithrombin III, stimulated neurite outgrowth but only when its thrombin inhibitory activity was accelerated by heparin.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	11-19
2298818-10	1990	The plasma thrombin inhibitor, antithrombin III, stimulated neurite outgrowth but only when its thrombin inhibitory activity was accelerated by heparin.	Heparin	144-151	coagulation factor II, thrombin	Homo sapiens	35-43
2136880-0	1990	The localization of heparin-binding fragments on human C4b-binding protein.	Heparin	20-27	complement component 4 binding protein alpha	Homo sapiens	55-74
2345158-6	1990	Pretreatment of the column with heparin reduced the loss of fibrinogen to less than 10%.	Heparin	32-39	fibrinogen beta chain	Homo sapiens	60-70
2136880-3	1990	We now demonstrate that C4BP contains heparin-binding fragments, which are located within the C4b binding domain.	Heparin	38-45	complement component 4 binding protein alpha	Homo sapiens	24-28
2136880-4	1990	We have used an assay using heparin coupled to Sepharose CL-6B to show that 125I-C4BP binds to heparin in a time-dependent, saturable, and reversible manner.	Heparin	28-35	complement component 4 binding protein alpha	Homo sapiens	81-85
2136880-4	1990	We have used an assay using heparin coupled to Sepharose CL-6B to show that 125I-C4BP binds to heparin in a time-dependent, saturable, and reversible manner.	Heparin	95-102	complement component 4 binding protein alpha	Homo sapiens	81-85
2136880-6	1990	mAb against native C4BP and the isolated 160-kDa central core fragment were evaluated for their ability to block the binding of 125I-C4BP to heparin and C4b.	Heparin	141-148	complement component 4 binding protein alpha	Homo sapiens	133-137
2136880-7	1990	The relative efficacy of mAb against intact C4BP in blocking C4BP binding to heparin-Sepharose was similar to that for blocking 125I-C4BP binding to C4b.	Heparin	77-84	complement component 4 binding protein alpha	Homo sapiens	44-48
2136880-8	1990	In addition, heparin blocked the binding of 125I-C4BP to C4b and vice versa.	Heparin	13-20	complement component 4 binding protein alpha	Homo sapiens	49-53
2136880-9	1990	It is therefore likely that the heparin-binding fragments are localized on or close to the C4b-binding site of C4BP.	Heparin	32-39	complement component 4 binding protein alpha	Homo sapiens	111-115
1983502-2	1990	Low molecular weight heparin (LMWH), which is derived from unfractionated heparin (UFH), exhibits marked anti-Xa activity and minor thrombin inhibition.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	132-140
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	99-107
1983502-2	1990	Low molecular weight heparin (LMWH), which is derived from unfractionated heparin (UFH), exhibits marked anti-Xa activity and minor thrombin inhibition.	Heparin	83-86	coagulation factor II, thrombin	Homo sapiens	132-140
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	68-75	coagulation factor II, thrombin	Homo sapiens	99-107
33771558-0	2021	VEGF and VEGFR2 bind to similar pH-sensitive sites on fibronectin, exposed by heparin-mediated conformational changes.	Heparin	78-85	vascular endothelial growth factor A	Homo sapiens	0-4
21551582-4	1990	Heparin-affinity HPLC showed that this increase was due to a large increase in levels of basic FGF (bFGF), and a much smaller increase in levels of acidic FGF (aFGF) after injury.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	89-98
21551582-4	1990	Heparin-affinity HPLC showed that this increase was due to a large increase in levels of basic FGF (bFGF), and a much smaller increase in levels of acidic FGF (aFGF) after injury.	Heparin	0-7	fibroblast growth factor 2	Homo sapiens	100-104
2749591-5	1989	Heparin inhibits this effect and retards the explosive thrombin formation.	Heparin	0-7	coagulation factor II, thrombin	Homo sapiens	55-63
33771558-0	2021	VEGF and VEGFR2 bind to similar pH-sensitive sites on fibronectin, exposed by heparin-mediated conformational changes.	Heparin	78-85	fibronectin 1	Homo sapiens	54-65
33771558-3	2021	These interactions can be further fine-tuned through changes in the availability of the VEGF binding sites on fibronectin, regulated by conformational changes induced by heparin and heparan sulfate chains within the extracellular matrix.	Heparin	170-177	vascular endothelial growth factor A	Homo sapiens	88-92
33771558-3	2021	These interactions can be further fine-tuned through changes in the availability of the VEGF binding sites on fibronectin, regulated by conformational changes induced by heparin and heparan sulfate chains within the extracellular matrix.	Heparin	170-177	fibronectin 1	Homo sapiens	110-121
33771558-6	2021	The VEGFR2 binding sites on fibronectin show great similarity to the VEGF binding sites, as they were also exposed upon heparin-induced conformational changes in fibronectin, and the interaction was enhanced at acidic pH.	Heparin	120-127	fibronectin 1	Homo sapiens	28-39
33771558-6	2021	The VEGFR2 binding sites on fibronectin show great similarity to the VEGF binding sites, as they were also exposed upon heparin-induced conformational changes in fibronectin, and the interaction was enhanced at acidic pH.	Heparin	120-127	vascular endothelial growth factor A	Homo sapiens	4-8
33771558-6	2021	The VEGFR2 binding sites on fibronectin show great similarity to the VEGF binding sites, as they were also exposed upon heparin-induced conformational changes in fibronectin, and the interaction was enhanced at acidic pH.	Heparin	120-127	fibronectin 1	Homo sapiens	162-173
2403617-3	1990	Injection of heparin to stimulate the action of lipoprotein lipase increased the removal rates in both control and insulin-deficient rats, but control values were not restored by heparin given to insulin-deficient rats and compared with controls the difference due to insulin deficiency persisted.	Heparin	13-20	lipoprotein lipase	Rattus norvegicus	48-66
33822474-5	2021	Based on the anticoagulant, co-culture of human umbilical vein endothelial cells, and subcapsular transplantation of kidney experiments, HEP-VEGF-DKSs are shown to reduce platelet adhesion, which is crucial for subsequent vascularization and slow release of heparin and VEGF, suggesting its ability of improve neovascularization.	Heparin	258-265	vascular endothelial growth factor A	Homo sapiens	141-145
33805059-7	2021	Consequently, a simultaneous blockade of thrombin and P-selectin binding seems to be a powerful approach, as mediated by heparin to crucially reduce the hypercoagulable state of pancreatic cancer patients.	Heparin	121-128	coagulation factor II, thrombin	Homo sapiens	41-49
34933004-1	2022	Human fibroblast growth factor 1 (hFGF1) binding to its receptor and heparin play critical roles in cell proliferation, angiogenesis and wound healing but is also implicated in cancer.	Heparin	69-76	fibroblast growth factor 1	Homo sapiens	6-32
33801235-4	2021	We further elucidated the underlying molecular mechanism via transcriptome analyses, observing that the insulin/PI3K/mTOR and Wnt signaling pathways were significantly downregulated by heparin-mimicking moieties through the inhibition of FAK/Cav3.	Heparin	185-192	insulin	Homo sapiens	104-111
33801235-4	2021	We further elucidated the underlying molecular mechanism via transcriptome analyses, observing that the insulin/PI3K/mTOR and Wnt signaling pathways were significantly downregulated by heparin-mimicking moieties through the inhibition of FAK/Cav3.	Heparin	185-192	mechanistic target of rapamycin kinase	Homo sapiens	117-121
33801235-5	2021	Taken together, the easy-to-adapt heparin-mimicking polymer-based in vitro cell culture platform could be an attractive platform for potential applications in drug screening, providing clear readouts of changes in insulin/PI3K/mTOR and Wnt signaling pathways.	Heparin	34-41	insulin	Homo sapiens	214-221
33801235-5	2021	Taken together, the easy-to-adapt heparin-mimicking polymer-based in vitro cell culture platform could be an attractive platform for potential applications in drug screening, providing clear readouts of changes in insulin/PI3K/mTOR and Wnt signaling pathways.	Heparin	34-41	mechanistic target of rapamycin kinase	Homo sapiens	227-231
33820675-7	2021	Increased release of heparin-binding protein (HBP) and the expression of P2RX1 on the neutrophil surface are related to fluid leakage and decreased chemotaxis during burn shock stage, respectively.	Heparin	21-28	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	46-49
29409708-4	2018	Fluorescence polarization competition experiments revealed that the synthesized tetrasaccharide strongly interacts with two heparin-binding growth factors, midkine and FGF-2 (IC50 of 270 nM and 2.4 microM, respectively).	Heparin	124-131	midkine	Homo sapiens	156-163
29409708-4	2018	Fluorescence polarization competition experiments revealed that the synthesized tetrasaccharide strongly interacts with two heparin-binding growth factors, midkine and FGF-2 (IC50 of 270 nM and 2.4 microM, respectively).	Heparin	124-131	fibroblast growth factor 2	Homo sapiens	168-173
25363620-4	2015	In the present study, we immobilized heparin onto electrospun polycaprolactone scaffolds as a means of incorporating basic fibroblast growth factor (bFGF) onto the scaffold.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	117-147
25363620-4	2015	In the present study, we immobilized heparin onto electrospun polycaprolactone scaffolds as a means of incorporating basic fibroblast growth factor (bFGF) onto the scaffold.	Heparin	37-44	fibroblast growth factor 2	Homo sapiens	149-153
33232799-3	2021	The BMP2/4 subfamily has been deeply characterized to have a N-terminal heparin/HS binding domain (HBD), whose basic residues contact the sulfate groups on heparin and HS.	Heparin	72-79	bone morphogenetic protein 2	Cricetulus griseus	4-10
33232799-3	2021	The BMP2/4 subfamily has been deeply characterized to have a N-terminal heparin/HS binding domain (HBD), whose basic residues contact the sulfate groups on heparin and HS.	Heparin	156-163	bone morphogenetic protein 2	Cricetulus griseus	4-10
25351814-0	2015	Thrombin generation assay identifies individual variability in responses to low molecular weight heparin in pregnancy: implications for anticoagulant monitoring.	Heparin	97-104	coagulation factor II, thrombin	Homo sapiens	0-8
16404702-5	2005	The functionality of the heparinized collagen matrices was then enhanced by immobilization of VEGF via its heparin-binding domain.	Heparin	25-32	vascular endothelial growth factor A	Homo sapiens	94-98
34933004-1	2022	Human fibroblast growth factor 1 (hFGF1) binding to its receptor and heparin play critical roles in cell proliferation, angiogenesis and wound healing but is also implicated in cancer.	Heparin	69-76	fibroblast growth factor 1	Homo sapiens	34-39
34987706-10	2021	Heparin downregulated the expression of hepcidin and DMT1, increased FPN1, and exerted protective effects that were equivalent to those of ebselen on ferroptosis and EBI.	Heparin	0-7	hepcidin antimicrobial peptide	Rattus norvegicus	40-48
34871836-7	2022	Heparinase inhibits the anticoagulant ability of heparin by forming a heparin-antithrombin-thrombin complex during coagulation.	Heparin	49-56	coagulation factor II, thrombin	Homo sapiens	91-99
34871836-7	2022	Heparinase inhibits the anticoagulant ability of heparin by forming a heparin-antithrombin-thrombin complex during coagulation.	Heparin	70-77	coagulation factor II, thrombin	Homo sapiens	91-99
34657240-4	2022	And we found that when cells were treated with different vesicles uptake inhibitors (chlorpromazine, methyl-beta-cyclodextrin (MbetaCD), cytochalasin D, chloroquine and heparin) and heparinase (HSPE), only heparin and HSPE counteracted the uptake enhancement effect caused by DAL-1/4.1B.	Heparin	169-176	erythrocyte membrane protein band 4.1 like 3	Homo sapiens	282-286
34657240-4	2022	And we found that when cells were treated with different vesicles uptake inhibitors (chlorpromazine, methyl-beta-cyclodextrin (MbetaCD), cytochalasin D, chloroquine and heparin) and heparinase (HSPE), only heparin and HSPE counteracted the uptake enhancement effect caused by DAL-1/4.1B.	Heparin	206-213	erythrocyte membrane protein band 4.1 like 3	Homo sapiens	282-286
34815178-2	2022	Here, we showed that heparin interacts with the Mpro of SARS-CoV-2 and inhibits its activity.	Heparin	21-28	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	48-52
34815178-3	2022	Protein fluorescence quenching showed that heparin strongly binds to the Mpro protein with dissociation constants KD of 16.66 and 31.60 muM at 25 and 35  C, respectively.	Heparin	43-50	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	73-77
34815178-5	2022	Fluorescence resonance energy transfer (FRET) assay demonstrated that heparin inhibits the proteolytic activity of Mpro with an inhibition constant Ki of 6.9 nM and a half maximal inhibitory concentrations (IC50) of 7.8 +- 2.6 nM.	Heparin	70-77	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	115-119
34815178-6	2022	Furthermore, molecular docking analysis revealed that the recognition and binding groups of heparin within the active site of SARS-CoV-2 Mpro provide important new information for the characteristics of the interactions of heparin with the protease.	Heparin	92-99	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	137-141
34815178-6	2022	Furthermore, molecular docking analysis revealed that the recognition and binding groups of heparin within the active site of SARS-CoV-2 Mpro provide important new information for the characteristics of the interactions of heparin with the protease.	Heparin	223-230	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	137-141
34815178-7	2022	Our finding suggested that heparin might have a potential role in inhibiting SARS-CoV-2 infection through inhibiting Mpro activity of SARS-CoV-2.	Heparin	27-34	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	117-121
34868360-7	2022	Heparin binding epidermal growth factor (EGF)-like growth factor, transforming growth factor beta1 (TGFB1) and thyroid hormone receptor alpha (THRA) mRNA expression was higher in HER2-positive patients (P=0.026, P<0.001 and P<0.001).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	66-98
34868360-7	2022	Heparin binding epidermal growth factor (EGF)-like growth factor, transforming growth factor beta1 (TGFB1) and thyroid hormone receptor alpha (THRA) mRNA expression was higher in HER2-positive patients (P=0.026, P<0.001 and P<0.001).	Heparin	0-7	transforming growth factor beta 1	Homo sapiens	100-105
34868360-7	2022	Heparin binding epidermal growth factor (EGF)-like growth factor, transforming growth factor beta1 (TGFB1) and thyroid hormone receptor alpha (THRA) mRNA expression was higher in HER2-positive patients (P=0.026, P<0.001 and P<0.001).	Heparin	0-7	erb-b2 receptor tyrosine kinase 2	Homo sapiens	179-183
34987706-10	2021	Heparin downregulated the expression of hepcidin and DMT1, increased FPN1, and exerted protective effects that were equivalent to those of ebselen on ferroptosis and EBI.	Heparin	0-7	solute carrier family 40 member 1	Rattus norvegicus	69-73
34743814-4	2021	Herein, we found that the S protein can competitively inhibit the bindings of antithrombin and heparin cofactor II to heparin/HS, causing abnormal increase in thrombin activity.	Heparin	95-102	coagulation factor II, thrombin	Homo sapiens	159-167
34937023-0	2021	Crosslinked layered surfaces of heparin and poly(L-lysine) enhance mesenchymal stromal cells behavior in the presence of soluble interferon gamma.	Heparin	32-39	interferon gamma	Homo sapiens	129-145
34937023-3	2021	The aim of this study is to evaluate multilayers of heparin and poly(L-lysine) (HEP/PLL) as a bioactive surface for hMSCs stimulated with soluble interferon gamma (IFN-gamma).	Heparin	52-59	interferon gamma	Homo sapiens	146-173
34839601-13	2021	Urea nitrogen level, creatinine level, and CRP value of patients in citrate group were significantly lower than those in heparin group (P<0.05).	Heparin	121-128	C-reactive protein	Homo sapiens	43-46
34743814-4	2021	Herein, we found that the S protein can competitively inhibit the bindings of antithrombin and heparin cofactor II to heparin/HS, causing abnormal increase in thrombin activity.	Heparin	118-125	coagulation factor II, thrombin	Homo sapiens	159-167
34536674-3	2021	To enhance growth factor (GF) availability in DFUs, heparin (HN)-mimetic alginate sulfate/polycaprolactone (AlgSulf/PCL) double emulsion nanoparticles (NPs) with high affinity and sustained release of CTGF and IGF-I were synthesized.	Heparin	52-59	insulin like growth factor 1	Homo sapiens	210-215
33754901-3	2021	Here, heparin-coupled polyvinyl alcohol (PVA-H) microspheres have been developed as an adsorbent for selectively remove tumour-induced immunosuppressive cytokines, such as vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta), but not tumour necrosis factor-alpha (TNF-alpha) which has an immune-stimulating effect and can inhibit tumour growth.	Heparin	6-13	vascular endothelial growth factor A	Homo sapiens	172-206
33754901-3	2021	Here, heparin-coupled polyvinyl alcohol (PVA-H) microspheres have been developed as an adsorbent for selectively remove tumour-induced immunosuppressive cytokines, such as vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta), but not tumour necrosis factor-alpha (TNF-alpha) which has an immune-stimulating effect and can inhibit tumour growth.	Heparin	6-13	vascular endothelial growth factor A	Homo sapiens	208-212
33754901-3	2021	Here, heparin-coupled polyvinyl alcohol (PVA-H) microspheres have been developed as an adsorbent for selectively remove tumour-induced immunosuppressive cytokines, such as vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta), but not tumour necrosis factor-alpha (TNF-alpha) which has an immune-stimulating effect and can inhibit tumour growth.	Heparin	6-13	tumor necrosis factor	Homo sapiens	218-249
34895060-8	2021	High levels of HBP in the pancreas were detected at 48 h, and heparin inhibited HBP expression in AP pancreatic tissue.	Heparin	62-69	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	80-83
34895060-9	2021	Inhibiting HBP expression by injecting heparin before AP can alleviate pancreatic necrosis and inhibit F4/80 labeled M1 macrophage infiltration and IL-6, TNF-alpha, and iNOS mRNA expression.	Heparin	39-46	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	11-14
34895060-9	2021	Inhibiting HBP expression by injecting heparin before AP can alleviate pancreatic necrosis and inhibit F4/80 labeled M1 macrophage infiltration and IL-6, TNF-alpha, and iNOS mRNA expression.	Heparin	39-46	interleukin 6	Mus musculus	148-152
34895060-9	2021	Inhibiting HBP expression by injecting heparin before AP can alleviate pancreatic necrosis and inhibit F4/80 labeled M1 macrophage infiltration and IL-6, TNF-alpha, and iNOS mRNA expression.	Heparin	39-46	tumor necrosis factor	Mus musculus	154-163
34895060-9	2021	Inhibiting HBP expression by injecting heparin before AP can alleviate pancreatic necrosis and inhibit F4/80 labeled M1 macrophage infiltration and IL-6, TNF-alpha, and iNOS mRNA expression.	Heparin	39-46	nitric oxide synthase 2, inducible	Mus musculus	169-173
34895060-11	2021	HBP is critical for pancreatic necrosis response in acute pancreatitis by increasing the infiltration of M1 macrophages and promoting the secretion of inflammatory factors, such as TNF-alpha, IL-6, IL-1beta, which can be reduced by heparin.	Heparin	232-239	signal transducing adaptor molecule (SH3 domain and ITAM motif) 2	Mus musculus	0-3
34895060-11	2021	HBP is critical for pancreatic necrosis response in acute pancreatitis by increasing the infiltration of M1 macrophages and promoting the secretion of inflammatory factors, such as TNF-alpha, IL-6, IL-1beta, which can be reduced by heparin.	Heparin	232-239	tumor necrosis factor	Mus musculus	181-190
34895060-11	2021	HBP is critical for pancreatic necrosis response in acute pancreatitis by increasing the infiltration of M1 macrophages and promoting the secretion of inflammatory factors, such as TNF-alpha, IL-6, IL-1beta, which can be reduced by heparin.	Heparin	232-239	interleukin 6	Mus musculus	192-196
34536674-3	2021	To enhance growth factor (GF) availability in DFUs, heparin (HN)-mimetic alginate sulfate/polycaprolactone (AlgSulf/PCL) double emulsion nanoparticles (NPs) with high affinity and sustained release of CTGF and IGF-I were synthesized.	Heparin	61-63	insulin like growth factor 1	Homo sapiens	210-215
34370931-6	2021	Serum nucleosome levels, as well as the white blood cell counts, neutrophil counts, and high-sensitivity C-reactive protein levels, were significantly higher in anti-heparin/PF4 antibody-positive patients compared to the control.	Heparin	166-173	C-reactive protein	Homo sapiens	105-123
34762427-0	2021	Mechanistic Picture for Monomeric Human Fibroblast Growth Factor 1 Stabilization by Heparin Binding.	Heparin	84-91	fibroblast growth factor 1	Homo sapiens	40-66
34762427-2	2021	hFGF1, which is associated with low stability in vivo, is known to be stabilized by binding heparin sulfate, a glycosaminoglycan that aids the protein in the activation of its cell surface receptor.	Heparin	92-99	fibroblast growth factor 1	Homo sapiens	0-5
34762427-3	2021	The poor thermal and proteolytic stability of hFGF1 and the stabilizing role of heparin have long been observed experimentally; however, the mechanistic details of these phenomena are not well understood.	Heparin	80-87	fibroblast growth factor 1	Homo sapiens	46-51
34762427-5	2021	We have observed a conformational change in the heparin-binding pocket of hFGF1 that occurs only in the absence of heparin.	Heparin	48-55	fibroblast growth factor 1	Homo sapiens	74-79
34762427-5	2021	We have observed a conformational change in the heparin-binding pocket of hFGF1 that occurs only in the absence of heparin.	Heparin	115-122	fibroblast growth factor 1	Homo sapiens	74-79
34762427-6	2021	Several intramolecular interactions were also identified within the heparin-binding pocket that form only when hFGF1 interacts with heparin.	Heparin	68-75	fibroblast growth factor 1	Homo sapiens	111-116
34762427-6	2021	Several intramolecular interactions were also identified within the heparin-binding pocket that form only when hFGF1 interacts with heparin.	Heparin	132-139	fibroblast growth factor 1	Homo sapiens	111-116
34762427-8	2021	This conformational transition results in increased flexibility of the heparin-binding pocket and provides an explanation for the susceptibility of apo hFGF1 to proteolytic degradation and thermal instability.	Heparin	71-78	fibroblast growth factor 1	Homo sapiens	152-157
34762427-9	2021	This study provides a glimpse into mechanistic details of the heparin-mediated stabilization of hFGF1 and encourages the use of microsecond-level MD in studying the effect of binding on protein structure and dynamics.	Heparin	62-69	fibroblast growth factor 1	Homo sapiens	96-101
34762427-10	2021	In addition, the observed differential behavior of hFGF1 in the absence and presence of heparin provides an example, where microsecond-level all-atom MD simulations are necessary to see functionally relevant biomolecular phenomena that otherwise will not be observed on sub-microsecond time scales.	Heparin	88-95	fibroblast growth factor 1	Homo sapiens	51-56
34184187-13	2021	FFA abolish a decrease in circulating SFRP5 caused by insulin, but Intralipid/heparin infusion alone does not regulate SFRP5 concentration.	Heparin	78-85	secreted frizzled related protein 5	Homo sapiens	38-43
34884486-11	2021	Preincubation with heparin, autotaxin (ATX) inhibitor HA130 or lysophosphatidic acid (LPA) receptor antagonist Ki16425 reduced PLA1A-induced-secretion of IL-8.	Heparin	19-26	C-X-C motif chemokine ligand 8	Homo sapiens	154-158
34724185-5	2021	Here we describe improvements in the method by adding bFGF, TGFbeta inhibitor and heparin to the culture, which increases the yield of CD34+CD43+ HPCs 50-fold compared with the original protocol.	Heparin	82-89	CD34 molecule	Homo sapiens	135-139
34724185-5	2021	Here we describe improvements in the method by adding bFGF, TGFbeta inhibitor and heparin to the culture, which increases the yield of CD34+CD43+ HPCs 50-fold compared with the original protocol.	Heparin	82-89	sialophorin	Homo sapiens	140-144
34769095-3	2021	In order to regulate such interactions between proteins and the Alg matrix, we propose to complex proteins of interest in this study - CXCL12, FGF-2, VEGF - with polyanionic heparin prior to their encapsulation into Alg microbeads of high content of alpha-L-guluronic acid units (high-G).	Heparin	174-181	vascular endothelial growth factor A	Homo sapiens	150-154
34769095-3	2021	In order to regulate such interactions between proteins and the Alg matrix, we propose to complex proteins of interest in this study - CXCL12, FGF-2, VEGF - with polyanionic heparin prior to their encapsulation into Alg microbeads of high content of alpha-L-guluronic acid units (high-G).	Heparin	174-181	fibroblast growth factor 2	Homo sapiens	143-148
34643035-0	2022	The modification of the thrombin generation assay for the clinical assessment of hypercoagulability in patients receiving heparin therapy.	Heparin	122-129	coagulation factor II, thrombin	Homo sapiens	24-32
34769095-0	2021	Complexation of CXCL12, FGF-2 and VEGF with Heparin Modulates the Protein Release from Alginate Microbeads.	Heparin	44-51	fibroblast growth factor 2	Homo sapiens	24-29
34769095-0	2021	Complexation of CXCL12, FGF-2 and VEGF with Heparin Modulates the Protein Release from Alginate Microbeads.	Heparin	44-51	vascular endothelial growth factor A	Homo sapiens	34-38
34712574-7	2021	Whilst both control heparin, and MPS IIIA HS GAGs had a similar binding affinity for FGF2, only the latter inhibited FGF signalling, suggesting accumulated MPS IIIA HS GAGs disrupt the FGF2:FGF2 receptor:HS signalling complex.	Heparin	20-27	fibroblast growth factor 2	Homo sapiens	85-89
34663835-4	2021	To carry out this screening for sFLT1, we developed an easier and relatively low-cost sandwich-type ELISA method using a single mixture of human serum sample with an anti-FLT1 antibody and heparin-beads, namely heparin-beads-coupled ELISA (HB-ELISA).	Heparin	211-218	fms related receptor tyrosine kinase 1	Homo sapiens	171-175
34643035-1	2022	BACKGROUND: Heparin diminishes thrombin generation (TG) because it decreases the survival time of thrombin in plasma.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	31-39
34643035-1	2022	BACKGROUND: Heparin diminishes thrombin generation (TG) because it decreases the survival time of thrombin in plasma.	Heparin	12-19	coagulation factor II, thrombin	Homo sapiens	98-106
34347378-0	2021	Blockage of undesirable endocytosis of recombinant human growth/differentiation factor-5 in Chinese hamster ovary cell cultures requires heparin analogs with specific chain lengths.	Heparin	137-144	growth differentiation factor 5	Homo sapiens	57-88
34639073-1	2021	Our objective is to reveal the molecular mechanism of the anti-inflammatory action of low-molecular-weight heparin (LMWH) based on its influence on the activity of two key cytokines, IFNgamma and IL-6.	Heparin	107-114	interferon gamma	Homo sapiens	183-191
34639073-1	2021	Our objective is to reveal the molecular mechanism of the anti-inflammatory action of low-molecular-weight heparin (LMWH) based on its influence on the activity of two key cytokines, IFNgamma and IL-6.	Heparin	107-114	interleukin 6	Homo sapiens	196-200
34639073-2	2021	The mechanism of heparin binding to IFNgamma and IL-6 and the resulting inhibition of their activity were studied by means of extensive molecular-dynamics simulations.	Heparin	17-24	interferon gamma	Homo sapiens	36-44
34639073-2	2021	The mechanism of heparin binding to IFNgamma and IL-6 and the resulting inhibition of their activity were studied by means of extensive molecular-dynamics simulations.	Heparin	17-24	interleukin 6	Homo sapiens	49-53
34677445-1	2021	Sugar-based molecules such as heparins or natural heparan sulfate polysaccharides have been developed and widely studied for controlling heparanase (HPSE) enzymatic activity, a key player in extracellular matrix remodelling during cancer pathogenesis.	Heparin	30-38	heparanase	Homo sapiens	149-153
34596979-3	2021	In this study, we compared the binding of four inflammatory cytokines (CCL8, IL-1beta, IL-2 and IL-6) to immobilized heparin by an SPR analysis.	Heparin	117-124	interleukin 2	Homo sapiens	87-91
34596979-3	2021	In this study, we compared the binding of four inflammatory cytokines (CCL8, IL-1beta, IL-2 and IL-6) to immobilized heparin by an SPR analysis.	Heparin	117-124	interleukin 6	Homo sapiens	96-100
34677453-10	2021	Furthermore, the sulfated polysaccharide strongly stimulated the inhibition of thrombin by potentiating antithrombin-III (AT-III) or heparin cofactor-II, and it also largely promoted the inhibition of factor Xa mediated by AT-III.	Heparin	133-140	coagulation factor II, thrombin	Homo sapiens	79-87
34331952-2	2021	Midkine is a heparin-binding growth factor and forms a small protein family with pleiotrophin.	Heparin	13-20	midkine	Homo sapiens	0-7
34404617-10	2021	In multiple myeloma patients who received heparin, the mean collected CD34+ cell number was 8 x 106/kg, and the mean CD34+ cell number yield was 12,555/mul.	Heparin	42-49	CD34 molecule	Homo sapiens	70-74
34404617-12	2021	In lymphoma patients who received heparin, the mean collected CD34+ cell number was 6,8 x 106/kg, and the mean CD34+ cell number was 1421/mul.	Heparin	34-41	CD34 molecule	Homo sapiens	62-66
34298051-5	2021	The findings indicated the reduced tumor-derived exosome secretion and protein cargo as reflected by lower levels of CD63, TSG101, heparinase and IL-6 in exosomes derived from heparin-induced B16F10 cells as compared with 6-O-desulfated heparin-induced tumor cells.	Heparin	176-183	CD63 antigen	Mus musculus	117-121
34298051-5	2021	The findings indicated the reduced tumor-derived exosome secretion and protein cargo as reflected by lower levels of CD63, TSG101, heparinase and IL-6 in exosomes derived from heparin-induced B16F10 cells as compared with 6-O-desulfated heparin-induced tumor cells.	Heparin	176-183	tumor susceptibility gene 101	Mus musculus	123-129
34298051-5	2021	The findings indicated the reduced tumor-derived exosome secretion and protein cargo as reflected by lower levels of CD63, TSG101, heparinase and IL-6 in exosomes derived from heparin-induced B16F10 cells as compared with 6-O-desulfated heparin-induced tumor cells.	Heparin	176-183	interleukin 6	Mus musculus	146-150
34298051-5	2021	The findings indicated the reduced tumor-derived exosome secretion and protein cargo as reflected by lower levels of CD63, TSG101, heparinase and IL-6 in exosomes derived from heparin-induced B16F10 cells as compared with 6-O-desulfated heparin-induced tumor cells.	Heparin	237-244	CD63 antigen	Mus musculus	117-121
34298051-5	2021	The findings indicated the reduced tumor-derived exosome secretion and protein cargo as reflected by lower levels of CD63, TSG101, heparinase and IL-6 in exosomes derived from heparin-induced B16F10 cells as compared with 6-O-desulfated heparin-induced tumor cells.	Heparin	237-244	tumor susceptibility gene 101	Mus musculus	123-129
34298051-5	2021	The findings indicated the reduced tumor-derived exosome secretion and protein cargo as reflected by lower levels of CD63, TSG101, heparinase and IL-6 in exosomes derived from heparin-induced B16F10 cells as compared with 6-O-desulfated heparin-induced tumor cells.	Heparin	237-244	interleukin 6	Mus musculus	146-150
34660719-0	2021	Effects of Heparin and Bivalirudin on Thrombin-Induced Platelet Activation: Differential Modulation of PAR Signaling Drives Divergent Prothrombotic Responses.	Heparin	11-18	coagulation factor II, thrombin	Homo sapiens	38-46
34660719-4	2021	At physiological antithrombin levels, heparin treatment resulted in complete and sustained inhibition of thrombin-induced PAR4-mediated platelet activation, but transient PAR1 signaling was sufficient to elicit significant alpha-granule release and platelet aggregation.	Heparin	38-45	coagulation factor II, thrombin	Homo sapiens	105-113
34660719-7	2021	Our results show that heparin and bivalirudin have different and complementary inhibitory effects on the activation of PAR1 and PAR4 by thrombin.	Heparin	22-29	coagulation factor II thrombin receptor	Homo sapiens	119-123
34660719-7	2021	Our results show that heparin and bivalirudin have different and complementary inhibitory effects on the activation of PAR1 and PAR4 by thrombin.	Heparin	22-29	coagulation factor II, thrombin	Homo sapiens	136-144
34677445-4	2021	In this work, we assessed the effects of an original marine lambda-carrageenan derived oligosaccharide (lambda-CO) we previously described, along with those of its native counterpart and heparins, on cell viability, proliferation, migration, and invasion of MDA-MB-231 breast cancer cells but also of sh-MDA-MB-231 cells, in which the expression of HPSE was selectively downregulated.	Heparin	187-195	heparanase	Homo sapiens	349-353
34569328-0	2021	Low-Molecular-Weight Heparin Anti-Xa Guided Reversal of Apixaban With Prothrombin Complex Concentrate in a Patient on Hemodialysis.	Heparin	21-28	coagulation factor II, thrombin	Homo sapiens	70-81
34447676-8	2021	In the UFH group, ALT, AST, eGFR, and creatinine clearance were lower after CAG (p<=0.001, all).	Heparin	7-10	solute carrier family 17 member 5	Homo sapiens	23-26
34510782-2	2022	We herein present a case of a 40-year-old woman with type 2 diabetes mellitus who had been diagnosed with SIR syndrome since the age of 29 and had been persistently treated with continuous subcutaneous insulin infusion using a mixture of insulin lispro and heparin.	Heparin	257-264	insulin	Homo sapiens	202-209
34153666-0	2021	The ERK/CREB/PTN/syndecan-3 pathway involves in heparin-mediated neuro-protection and neuro-regeneration against cerebral ischemia-reperfusion injury following cardiac arrest.	Heparin	48-55	Eph receptor B1	Rattus norvegicus	4-7
34153666-5	2021	CREB antagonist (KG-501), ERK antagonist (PD98059) and si-PTN were used respectively to inhibit the expression of CREB, ERK and PTN in cells, so as to explore the role of heparin in regulating neuronal regeneration.	Heparin	171-178	Eph receptor B1	Rattus norvegicus	120-123
34153666-9	2021	In terms of the mechanism, heparin upregulated the expression of ERK, CREB, NF200, BDNF, NGF, PTN and syndecan-3 in the rat brains.	Heparin	27-34	Eph receptor B1	Rattus norvegicus	65-68
34166830-7	2021	UFH TID also showed a trend toward lower rates of DVT (beta = -0.0893, p=0.295; TID rate = 18.5%, BID rate = 21.2%) when compared to UFH BID.	Heparin	0-3	BH3 interacting domain death agonist	Homo sapiens	98-101
34459268-2	2022	OBJECTIVE: The purpose of this study was to compare the safety and effectiveness of thrice-daily (TID) versus twice-daily (BID) administration of UFH during a heparin shortage for VTEP.	Heparin	146-149	BH3 interacting domain death agonist	Homo sapiens	123-126
34459268-3	2022	METHODS: A single-center retrospective analysis was conducted in patients with orders for BID subcutaneous UFH during a heparin shortage from September 1, 2019, to February 4, 2020.	Heparin	107-110	BH3 interacting domain death agonist	Homo sapiens	90-93
34459268-3	2022	METHODS: A single-center retrospective analysis was conducted in patients with orders for BID subcutaneous UFH during a heparin shortage from September 1, 2019, to February 4, 2020.	Heparin	120-127	BH3 interacting domain death agonist	Homo sapiens	90-93
34459268-7	2022	RESULTS: A total of 277 patients with orders for BID UFH and meeting inclusion criteria were evaluated and matched to patients who received TID UFH.	Heparin	53-56	BH3 interacting domain death agonist	Homo sapiens	49-52
34529926-1	2021	Objective: Heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF), which binds to the EGF receptor, plays an important role in the occurrence and development of inflammation in various diseases.	Heparin	11-18	epidermal growth factor receptor	Homo sapiens	105-117
34529712-12	2021	An identical label on different constructs of IgG1 can cause different affinities for FcRn and heparin.	Heparin	95-102	Fc gamma receptor and transporter	Homo sapiens	86-90
34153666-10	2021	Inhibition of ERK, CREB and interference with PTN expression notably weakened the heparin-mediated neuroprotective effects and restrained the expression of ERK/CREB and PTN/syndecan-3 pathway.	Heparin	82-89	Eph receptor B1	Rattus norvegicus	14-17
34153666-11	2021	CONCLUSION: Heparin attenuates the secondary brain injury induced by CA-CPR through regulating the ERK/CREB-mediated PTN/syndecan-3 pathway.	Heparin	12-19	Eph receptor B1	Rattus norvegicus	99-102
34433435-2	2021	Fibroblast growth factor-2 (FGF-2), a leading member of the FGF family of heparin-binding growth factors, contributes to normal as well as pathological angiogenesis.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	0-26
34433435-2	2021	Fibroblast growth factor-2 (FGF-2), a leading member of the FGF family of heparin-binding growth factors, contributes to normal as well as pathological angiogenesis.	Heparin	74-81	fibroblast growth factor 2	Homo sapiens	28-33
34144107-0	2021	Dual mechanistic TRAIL nanocarrier based on PEGylated heparin taurocholate and protamine which exerts both pro-apoptotic and anti-angiogenic effects.	Heparin	54-61	TNF superfamily member 10	Homo sapiens	17-22
34144137-0	2021	Heparin-decorated nanostructured lipid carriers of artemether-protoporphyrin IX-transferrin combination for therapy of malaria.	Heparin	0-7	transferrin	Homo sapiens	80-91
34341408-4	2021	Systematic analyses of the thermal and chemical denaturation data on hFGF1 variants (Q54P, K126N, R136E, K126N/R136E, Q54P/K126N, Q54P/R136E, and Q54P/K126N/R136E) indicate that nullification of charges in the heparin-binding pocket can significantly increase the stability of wtFGF1.	Heparin	210-217	fibroblast growth factor 1	Homo sapiens	69-74
34413778-14	2021	Increased subcutaneous and organ tissue permeability after thrombin treatment was observed in thrombin + saline and thrombin + heparin groups while treatment of bivalirudin and JTE-013 absent this effect.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	59-67
34413778-14	2021	Increased subcutaneous and organ tissue permeability after thrombin treatment was observed in thrombin + saline and thrombin + heparin groups while treatment of bivalirudin and JTE-013 absent this effect.	Heparin	127-134	coagulation factor II, thrombin	Homo sapiens	116-124
34367668-3	2021	This patient was being treated with a subcutaneous administration of low-molecular-weight heparin (100UI/kg/BID).	Heparin	90-97	BH3 interacting domain death agonist	Homo sapiens	108-111
34358963-6	2021	Laboratory data showed gradual reduction in the WBC (7700 cells/mm3), as well as in the serum LDH (355 IU/L) and CRP (0.76 mg/dL) levels, 7 days after heparin initiation.	Heparin	151-158	C-reactive protein	Homo sapiens	113-116
34552285-1	2021	Midkine (MK), a heparin-binding growth factor, is associated with the poor prognosis of the pediatric tumor, neuroblastoma.	Heparin	16-23	midkine	Homo sapiens	0-7
34552285-1	2021	Midkine (MK), a heparin-binding growth factor, is associated with the poor prognosis of the pediatric tumor, neuroblastoma.	Heparin	16-23	midkine	Homo sapiens	9-11
34126147-7	2021	GDFXa-induced alpha2M neutralized dabigatran and heparins in plasma and whole blood.	Heparin	49-56	alpha-2-macroglobulin	Mus musculus	14-21
34132790-5	2021	Herein we discuss the molecular involvement of HSPGs and Heparanase in SARS-CoV-2 infection, namely cell entry and release, and the accompanied coagulopathy complications, which assumedly could be blocked by Heparanase inhibitors such as Heparin and Pixatimod.	Heparin	238-245	heparanase	Homo sapiens	57-67
34132790-5	2021	Herein we discuss the molecular involvement of HSPGs and Heparanase in SARS-CoV-2 infection, namely cell entry and release, and the accompanied coagulopathy complications, which assumedly could be blocked by Heparanase inhibitors such as Heparin and Pixatimod.	Heparin	238-245	heparanase	Homo sapiens	208-218
34087306-0	2021	Conformational changes of GDNF-derived peptide induced by heparin, heparan sulfate, and sulfated hyaluronic acid - Analysis by circular dichroism spectroscopy and molecular dynamics simulation.	Heparin	58-65	glial cell derived neurotrophic factor	Homo sapiens	26-30
34270559-0	2021	Mycobacterial heparin-binding hemagglutinin (HBHA)-induced interferon-gamma release assay (IGRA) for discrimination of latent and active tuberculosis: A systematic review and meta-analysis.	Heparin	14-21	interferon gamma	Homo sapiens	59-75
34358104-4	2021	Multivariate logistic regression showed that, among women, drug classes significantly associated with an increased risk of hospitalization were heparins (ROR 1.41, CI 1.13-176), antidepressants (ROR 1.12, CI 1.03-1.23) and antidiabetics (ROR 1.13, CI 1.02-1.24).	Heparin	144-152	receptor tyrosine kinase like orphan receptor 1	Homo sapiens	154-159
34293069-9	2021	A recombinant LDLR protein could block heparin-mediated apoE pulldown, suggesting that LDLR may act as an HBV cell attachment receptor via binding to the HBV-associated apoE.	Heparin	39-46	apolipoprotein E	Homo sapiens	56-60
34293069-9	2021	A recombinant LDLR protein could block heparin-mediated apoE pulldown, suggesting that LDLR may act as an HBV cell attachment receptor via binding to the HBV-associated apoE.	Heparin	39-46	apolipoprotein E	Homo sapiens	169-173
34288440-9	2021	For monitoring the heparin anticoagulant therapy, the anti-Xa assay is suggested, because the severe acute-phase reaction (high fibrinogen and high factor VIII) shortens the aPTT.	Heparin	19-26	fibrinogen beta chain	Homo sapiens	128-138
34202416-5	2021	In addition, a previous study has revealed that PTH is a heparin/polyanion binding protein because of the similarity of heparin to the cell surface proteoglycans.	Heparin	57-64	parathyroid hormone	Homo sapiens	48-51
34511835-0	2021	Early Suspicion of Heparin-Induced Thrombocytopenia for Successful Free Flap Salvage: Reports of Two Cases.	Heparin	19-26	arachidonate 5-lipoxygenase activating protein	Homo sapiens	72-76
34210960-6	2021	The binding of heparin as well as a second HGF to the 2:1 c-MET:HGF complex further stabilize this active conformation.	Heparin	15-22	MET proto-oncogene, receptor tyrosine kinase	Homo sapiens	58-63
34202416-5	2021	In addition, a previous study has revealed that PTH is a heparin/polyanion binding protein because of the similarity of heparin to the cell surface proteoglycans.	Heparin	120-127	parathyroid hormone	Homo sapiens	48-51
34061194-7	2021	CONCLUSIONS: Risk factors for heparin resistance include antithrombin deficiency, elevation of factor VIII or fibrinogen level, elevation in heparin-binding proteins, increased heparin clearance, sepsis, trauma, and burns.	Heparin	30-37	fibrinogen beta chain	Homo sapiens	110-120
34088930-0	2021	Investigation of the mechanisms of VEGF-mediated compensatory lung growth: the role of the VEGF heparin-binding domain.	Heparin	96-103	vascular endothelial growth factor A	Homo sapiens	91-95
34461133-8	2021	Interestingly, this inhibition was diminished when EL was bound to endothelial cells or in the presence of heparin.	Heparin	107-114	lipase G, endothelial type	Homo sapiens	51-53
34095245-2	2021	The heparin sulfate proteoglycan, syndecan-2/CD362, has been identified as a functional marker for MSC isolation, allowing one to obtain a homogeneous cell product that meets regulatory requirements for clinical use.	Heparin	4-11	syndecan 2	Mus musculus	34-44
34925716-1	2021	Introduction: Midkine (MK), a heparin-binding growth factor, is involved in neurological diseases by mediating the inflammatory responses through enhancing the leukocyte migration.	Heparin	30-37	midkine	Homo sapiens	14-21
34925716-1	2021	Introduction: Midkine (MK), a heparin-binding growth factor, is involved in neurological diseases by mediating the inflammatory responses through enhancing the leukocyte migration.	Heparin	30-37	midkine	Homo sapiens	23-25
34259146-5	2021	It has been proposed that NCAM polysialylation could be inhibited by two types of heparin inhibitors, low molecular heparin (LMWH) and heparin tetrasaccharide (DP4).	Heparin	82-89	neuronal cell adhesion molecule	Homo sapiens	26-30
34259146-5	2021	It has been proposed that NCAM polysialylation could be inhibited by two types of heparin inhibitors, low molecular heparin (LMWH) and heparin tetrasaccharide (DP4).	Heparin	116-123	neuronal cell adhesion molecule	Homo sapiens	26-30
34259146-5	2021	It has been proposed that NCAM polysialylation could be inhibited by two types of heparin inhibitors, low molecular heparin (LMWH) and heparin tetrasaccharide (DP4).	Heparin	135-142	neuronal cell adhesion molecule	Homo sapiens	26-30
34259146-5	2021	It has been proposed that NCAM polysialylation could be inhibited by two types of heparin inhibitors, low molecular heparin (LMWH) and heparin tetrasaccharide (DP4).	Heparin	135-142	transcription factor Dp family member 3	Homo sapiens	160-163
34780727-5	2021	For LPL purification, we used heparin-Sepharose affinity chromatography, which disrupted LPL-GPIHBP1 complexes causing GPIHBP1 to elute with the flow-through of the conditioned media.	Heparin	30-37	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	93-100
34780727-5	2021	For LPL purification, we used heparin-Sepharose affinity chromatography, which disrupted LPL-GPIHBP1 complexes causing GPIHBP1 to elute with the flow-through of the conditioned media.	Heparin	30-37	glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1	Homo sapiens	119-126
34277977-0	2021	Heparin impairs skeletal muscle glucose uptake by inhibiting insulin binding to insulin receptor.	Heparin	0-7	insulin	Homo sapiens	61-68
34277977-4	2021	OGTT, ITT, 2-NBDG uptake and muscle GLUT4 immunofluorescence were detected in chronic intraperitoneal injection of heparin or heparinase (16 days) and muscle-specific loss-of-function mice.	Heparin	115-122	solute carrier family 2 (facilitated glucose transporter), member 4	Mus musculus	36-41
34277977-8	2021	Consistently, a chronic intraperitoneal injection of heparin results in hyperglycaemia, glucose intolerance and insulin resistance.	Heparin	53-60	insulin	Homo sapiens	112-119
34277977-9	2021	These effects are independent of heparin"s anticoagulant function and associated with decreases in glucose uptake and translocation of glucose transporter type 4 (GLUT4) in skeletal muscle.	Heparin	33-40	solute carrier family 2 (facilitated glucose transporter), member 4	Mus musculus	135-161
34277977-9	2021	These effects are independent of heparin"s anticoagulant function and associated with decreases in glucose uptake and translocation of glucose transporter type 4 (GLUT4) in skeletal muscle.	Heparin	33-40	solute carrier family 2 (facilitated glucose transporter), member 4	Mus musculus	163-168
34277977-10	2021	By using a muscle-specific loss-of-function mouse model, we further demonstrated that muscle GLUT4 is required for the detrimental effects of heparin on glucose homeostasis.	Heparin	142-149	solute carrier family 2 (facilitated glucose transporter), member 4	Mus musculus	93-98
34277977-11	2021	Conclusions: Heparin reduced insulin binding to its receptor by interacting with insulin and inhibited insulin-mediated activation of the PI3K/Akt signalling pathway in skeletal muscle, which leads to impaired glucose uptake and hyperglycaemia.	Heparin	13-20	insulin	Homo sapiens	29-36
34277977-11	2021	Conclusions: Heparin reduced insulin binding to its receptor by interacting with insulin and inhibited insulin-mediated activation of the PI3K/Akt signalling pathway in skeletal muscle, which leads to impaired glucose uptake and hyperglycaemia.	Heparin	13-20	insulin	Homo sapiens	81-88
34277977-11	2021	Conclusions: Heparin reduced insulin binding to its receptor by interacting with insulin and inhibited insulin-mediated activation of the PI3K/Akt signalling pathway in skeletal muscle, which leads to impaired glucose uptake and hyperglycaemia.	Heparin	13-20	insulin	Homo sapiens	103-110
34277977-11	2021	Conclusions: Heparin reduced insulin binding to its receptor by interacting with insulin and inhibited insulin-mediated activation of the PI3K/Akt signalling pathway in skeletal muscle, which leads to impaired glucose uptake and hyperglycaemia.	Heparin	13-20	thymoma viral proto-oncogene 1	Mus musculus	143-146
35570377-8	2022	Moreover, selective heparin-scavenging behavior over serum albumin is realized through adjusting the localized scavenger or surrounding salt concentrations at application-relevant circumstances.	Heparin	20-27	albumin	Homo sapiens	53-66
35420777-6	2022	Furthermore, the anticoagulant activity of H/C 12-mer 5 is reversible by protamine, a U.S. Food and Drug Administration-approved polypeptide to neutralize anticoagulant drug heparin.	Heparin	174-181	antigen identified by monoclonal antibody 2D8	Homo sapiens	50-55
35578904-2	2022	Here, on the basis of the synthetic methods of zeolitic imidazolate framework-90 (ZIF-90), we prepared bimetal organic material (BMOM) microreactors that successfully encapsulated Pasteurella multocida heparosan synthase 2 (PmHS2), a critical glycosyltransferase in the enzymatic synthesis of heparin and heparan sulfate.	Heparin	293-300	glycosyltransferase family 9 protein	Pasteurella multocida	243-262
35212883-9	2022	Intralipid/heparin diminished insulin-induced increase in muscle FKBP5.	Heparin	11-18	insulin	Homo sapiens	30-37
35212883-9	2022	Intralipid/heparin diminished insulin-induced increase in muscle FKBP5.	Heparin	11-18	FKBP prolyl isomerase 5	Homo sapiens	65-70
35021888-0	2022	Combining Heparin and a FX/Xa Aptamer to Reduce Thrombin Generation in Cardiopulmonary Bypass and COVID-19.	Heparin	10-17	coagulation factor II, thrombin	Homo sapiens	48-56
35021888-5	2022	This aptamer-UFH combination (1) supports continuous circulation of human blood through an ex vivo membrane oxygenation circuit, as is required for patients undergoing CPB and COVID-19 patients requiring extracorporeal membrane oxygenation, (2) allows for a reduced level of UFH to be employed, (3) more effectively limits thrombin generation compared to UFH alone, and (4) is rapidly reversed by the administration of protamine sulfate, the standard treatment for reversing UFH clinically following CPB.	Heparin	13-16	coagulation factor II, thrombin	Homo sapiens	323-331
35485302-3	2022	The hE/N-cadherin-functionalized PLGA/chitosan-heparin-TGFbeta1 (Duo hE/N-cad@P/C-h-TGFbeta1) microparticles spatiotemporally upregulates the endogenous E/N-cadherin expression of hMSC aggregates which further amplifies the chondrogenic differentiation and modulate paracrine and anti-inflammatory functions of hMSCs toward constructing a favorable microenvironment for chondrogenesis.	Heparin	47-54	transforming growth factor beta 1	Homo sapiens	55-63
35513125-3	2022	A recent structural analysis revealed that the complex of FGF23 and FGFR1, the physiologic FGF23 receptor in the kidney, includes soluble alpha-klotho (klotho) and heparin, which both act as co-factors for FGF23/FGFR1 signaling.	Heparin	164-171	fibroblast growth factor receptor 1	Homo sapiens	68-73
35513125-3	2022	A recent structural analysis revealed that the complex of FGF23 and FGFR1, the physiologic FGF23 receptor in the kidney, includes soluble alpha-klotho (klotho) and heparin, which both act as co-factors for FGF23/FGFR1 signaling.	Heparin	164-171	fibroblast growth factor receptor 1	Homo sapiens	212-217
35563446-8	2022	Fragment molecular orbital calculation revealed a strong binding of sulfated hyaluronan tetrasaccharide to the heparanase molecule based on electrostatic interactions, particularly characterized by interactions of (-1)- and (-2)-positioned sulfated sugar residues with basic amino acid residues composing the heparin-binding domain-1 of heparanase.	Heparin	309-316	heparanase	Mus musculus	111-121
35485302-3	2022	The hE/N-cadherin-functionalized PLGA/chitosan-heparin-TGFbeta1 (Duo hE/N-cad@P/C-h-TGFbeta1) microparticles spatiotemporally upregulates the endogenous E/N-cadherin expression of hMSC aggregates which further amplifies the chondrogenic differentiation and modulate paracrine and anti-inflammatory functions of hMSCs toward constructing a favorable microenvironment for chondrogenesis.	Heparin	47-54	transforming growth factor beta 1	Homo sapiens	84-92
35038779-9	2022	Thrombin stimulation markedly increased the procoagulant platelet response with HIT+ plasma that was heparin-independent and only partially reversed by FcgammaRIIa blockade, possibly reflecting ongoing thrombotic risk after heparin cessation.	Heparin	101-108	coagulation factor II, thrombin	Homo sapiens	0-8
35563215-2	2022	Owing to the special pentasaccharide sequence, heparin specifically binds to antithrombin (AT) and increases the inhibitory activity of AT towards coagulation enzymes.	Heparin	47-54	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	77-89
35514744-0	2022	Building Block Analysis of ATIII Affinity Fractions of Heparins: Application to the ATIII Binding Capacity of Non-conventional 3-O-Sulfated Sequences.	Heparin	55-63	serpin family C member 1	Bos taurus	27-32
35514744-0	2022	Building Block Analysis of ATIII Affinity Fractions of Heparins: Application to the ATIII Binding Capacity of Non-conventional 3-O-Sulfated Sequences.	Heparin	55-63	serpin family C member 1	Bos taurus	84-89
35514744-3	2022	In a previous paper (Mourier P. Heparinase digestion of 3-O-sulfated sequences: selective heparinase II digestion for separation and identification of binding sequences present in ATIII affinity fractions of bovine intestine heparins), we demonstrated that unsaturated 3-O-sulfated disaccharides detected in exhaustive heparin digests were specifically cleaved by heparinase I. Consequently, building blocks analyses of heparins using heparinases I+II+III digestion could be compared with experiments where only heparinase II is used.	Heparin	319-326	serpin family C member 1	Bos taurus	180-185
35498738-2	2022	As a potential therapeutic agent in the treatment of sepsis, 2-O, 3-O desulfated heparin (ODSH) reduces histones and platelet factor 4 (PF4) in mouse sepsis models.	Heparin	81-88	platelet factor 4	Mus musculus	136-139
35248846-4	2022	Further, FN1 possesses multiple binding domains including collagen, integrin, and heparin that can interact with heparan sulfate proteoglycans at the surface of chondrocyte leading to promote cell signaling and differentiation.	Heparin	82-89	fibronectin 1	Homo sapiens	9-12
35338216-2	2022	We determined whether negatively-charged heparin enhanced TMPRSS2 inhibition by alpha-1-antitrypsin (AAT).	Heparin	41-48	transmembrane serine protease 2	Homo sapiens	58-65
35433769-1	2022	Binding to antithrombin-III (ATIII) determines the anticoagulant activity of heparin.	Heparin	77-84	serpin family C member 1	Bos taurus	11-27
35433769-1	2022	Binding to antithrombin-III (ATIII) determines the anticoagulant activity of heparin.	Heparin	77-84	serpin family C member 1	Bos taurus	29-34
35433769-2	2022	The complexes formed between heparin and ATIII result from a specific pentasaccharide sequence containing a 3-O-sulfated glucosamine in medium position.	Heparin	29-36	serpin family C member 1	Bos taurus	41-46
35433769-6	2022	This specificity was erroneously generalized to other heparinases when it was observed that in exhaustive digests of heparins with the heparinase mixture, resistant 3-O-sulfated tetrasaccharides were also obtained from the specific ATIII-binding pentasaccharides.	Heparin	117-125	serpin family C member 1	Bos taurus	232-237
35338216-2	2022	We determined whether negatively-charged heparin enhanced TMPRSS2 inhibition by alpha-1-antitrypsin (AAT).	Heparin	41-48	serpin family A member 1	Homo sapiens	80-99
35338216-2	2022	We determined whether negatively-charged heparin enhanced TMPRSS2 inhibition by alpha-1-antitrypsin (AAT).	Heparin	41-48	serpin family A member 1	Homo sapiens	101-104
35338216-5	2022	Detailed molecular modeling was undertaken with the heparin-TMPRSS2-AAT ternary complex.	Heparin	52-59	transmembrane serine protease 2	Homo sapiens	60-67
35338216-5	2022	Detailed molecular modeling was undertaken with the heparin-TMPRSS2-AAT ternary complex.	Heparin	52-59	serpin family A member 1	Homo sapiens	68-71
35338216-7	2022	Underlying these findings, detailed molecular modeling revealed that: (i) the reactive center loop of AAT adopts an inhibitory-competent conformation compared with the crystal structure of TMPRSS2 bound to an exogenous (nafamostat) or endogenous (HAI-2) TMPRSS2 inhibitor and (ii) negatively-charged heparin bridges adjacent electropositive patches at the TMPRSS2-AAT interface, neutralizing otherwise repulsive forces.	Heparin	300-307	serpin family A member 1	Homo sapiens	102-105
35338216-7	2022	Underlying these findings, detailed molecular modeling revealed that: (i) the reactive center loop of AAT adopts an inhibitory-competent conformation compared with the crystal structure of TMPRSS2 bound to an exogenous (nafamostat) or endogenous (HAI-2) TMPRSS2 inhibitor and (ii) negatively-charged heparin bridges adjacent electropositive patches at the TMPRSS2-AAT interface, neutralizing otherwise repulsive forces.	Heparin	300-307	transmembrane serine protease 2	Homo sapiens	189-196
35235323-4	2022	The recognition of heparin by the most amplified members of the dynamic library has been studied with different experimental (SPR, fluorescence, NMR) and theoretical approaches, rendering a detailed interaction model.	Heparin	19-26	sepiapterin reductase	Mus musculus	126-129
35074553-4	2022	IFNgamma-loaded heparin-coated beads were included in injectable in situ crosslinking alginate hydrogels, providing a 3D microenvironment that ensured continuous inflammatory licensing, cell persistence and implant retrievability.	Heparin	16-23	interferon gamma	Mus musculus	0-8
35582539-4	2022	A number of factors such as anti-thrombin deficiency or raised coagulation Factor VIII levels may confer resistance to heparin in these patients, however, the optimal method of clinically evaluating this is unclear at present, though some groups have attempted its characterisation with thrombin generation testing (TGT).	Heparin	119-126	coagulation factor II, thrombin	Homo sapiens	287-295
35386772-10	2022	When TG levels spiked again, the patient was put on an insulin infusion with heparin, glucose, and potassium to rapidly reduce TG level.	Heparin	77-84	insulin	Homo sapiens	55-62
35229724-7	2022	GPIHBP1 trafficking across ECs in the mutant mice was normalized by disrupting LPL-HSPG electrostatic interactions with either heparin or an AD peptide.	Heparin	127-134	syndecan 2	Mus musculus	83-87
35270411-5	2022	The efficacy of steroids was investigated in quantitative, oxygen, steroid plus erythropoietin (EPO), levodopa/carbidopa, memantine, and heparin-induced extracorporeal LDL/fibrinogen precipitation (HELP) therapies and other therapeutic modalities in qualitative synthesis.	Heparin	137-144	fibrinogen beta chain	Homo sapiens	172-182
34708678-0	2022	Efficient drug delivery by novel cell-penetrating peptide derived from Midkine, with two heparin binding sites braced by a length-specific helix.	Heparin	89-96	midkine	Homo sapiens	71-78
34708678-3	2022	In this study, a tumour-targeted CPP with high efficiency derived from heparin-binding domain (HBD) of Midkine (named HMD) was discovered.	Heparin	71-78	midkine	Homo sapiens	103-110
35281253-7	2022	Furthermore, an MTT assay was applied to evaluate the anti-Abeta fibril formation function of heparin tetrasaccharide, and indicated that the heparin tetrasaccharide with the defined sequence represents a promising inhibitor of Abeta aggregation.	Heparin	94-101	amyloid beta precursor protein	Homo sapiens	59-64
35281253-4	2022	Using 2D-NMR analysis and molecular modelling, the binding motif of heparin oligoaccharides to Abeta was determined to be HexA-GlcNS-IdoA2S-GlcNS6S.	Heparin	68-75	amyloid beta precursor protein	Homo sapiens	95-100
35281253-7	2022	Furthermore, an MTT assay was applied to evaluate the anti-Abeta fibril formation function of heparin tetrasaccharide, and indicated that the heparin tetrasaccharide with the defined sequence represents a promising inhibitor of Abeta aggregation.	Heparin	142-149	amyloid beta precursor protein	Homo sapiens	59-64
35173145-3	2022	Heparanase (HPSE) is the only known mammalian endoglycosidase capable of degrading heparin sulfates and has a prominent role in DN pathogenesis.	Heparin	83-90	heparanase	Homo sapiens	0-10
35242277-7	2022	Here, we used pharmacological inhibitors and transfection with siRNA to evaluate whether matrix metalloprotease (MMP)2/9, heparin-binding- (HB-) epidermal growth factor (EGF), EGF receptor (EGFR), PI3K/Akt, MAPKs, and transcription factor AP-1 participated in the S1P-induced COX-2/PGE2 system determined by Western blotting, real-time polymerase chain reaction (RT-PCR), chromatin immunoprecipitation (ChIP), and promoter-reporter assays in HCFs.	Heparin	122-129	epidermal growth factor receptor	Homo sapiens	190-194
35242277-7	2022	Here, we used pharmacological inhibitors and transfection with siRNA to evaluate whether matrix metalloprotease (MMP)2/9, heparin-binding- (HB-) epidermal growth factor (EGF), EGF receptor (EGFR), PI3K/Akt, MAPKs, and transcription factor AP-1 participated in the S1P-induced COX-2/PGE2 system determined by Western blotting, real-time polymerase chain reaction (RT-PCR), chromatin immunoprecipitation (ChIP), and promoter-reporter assays in HCFs.	Heparin	122-129	AKT serine/threonine kinase 1	Homo sapiens	202-205
35242277-7	2022	Here, we used pharmacological inhibitors and transfection with siRNA to evaluate whether matrix metalloprotease (MMP)2/9, heparin-binding- (HB-) epidermal growth factor (EGF), EGF receptor (EGFR), PI3K/Akt, MAPKs, and transcription factor AP-1 participated in the S1P-induced COX-2/PGE2 system determined by Western blotting, real-time polymerase chain reaction (RT-PCR), chromatin immunoprecipitation (ChIP), and promoter-reporter assays in HCFs.	Heparin	122-129	prostaglandin-endoperoxide synthase 2	Homo sapiens	276-281
35173145-3	2022	Heparanase (HPSE) is the only known mammalian endoglycosidase capable of degrading heparin sulfates and has a prominent role in DN pathogenesis.	Heparin	83-90	heparanase	Homo sapiens	12-16
35068341-0	2022	Specificity protein 1-induced serine peptidase inhibitor, Kunitz Type 1 antisense RNA1 regulates colorectal cancer cell proliferation, migration, invasion and apoptosis through targeting heparin binding growth factor via sponging microRNA-214.	Heparin	187-194	Sp1 transcription factor	Homo sapiens	0-21
35185059-0	2022	A Case of Atrial Fibrillation in a Patient with Heparin-induced Thrombocytopenia Successfully Treated by Radiofrequency Catheter Ablation Using a Direct Thrombin Inhibitor.	Heparin	48-55	coagulation factor II, thrombin	Homo sapiens	153-161
35178035-5	2021	We also show that YadA can target other glycan moieties as found in heparin, for example.	Heparin	68-75	Adhesin	Yersinia enterocolitica	18-22
34995358-7	2022	RESULTS: Low-molecular-weight heparin (LMWH, an indirect inhibitor of thrombin) restrained both papain- and fungus-induced type 2 immune responses in mice by inhibiting IL-33 cleavage.	Heparin	30-37	coagulation factor II	Mus musculus	70-78
35163075-1	2022	Gremlin-1 is a secreted cystine-knot protein that acts as an antagonist of bone morphogenetic proteins (BMPs), and as a ligand of heparin and the vascular endothelial growth factor receptor 2 (VEGFR2), thus regulating several physiological and pathological processes, including embryonic development, tissue fibrosis and cancer.	Heparin	130-137	gremlin 1, DAN family BMP antagonist	Homo sapiens	0-9
35163075-4	2022	Ion metal affinity chromatography (IMAC) of crude supernatant followed by heparin-affinity chromatography enables obtaining a highly pure recombinant dimeric gremlin-1 protein, exhibiting both BMP antagonist and potent VEGFR2 agonist activities.	Heparin	74-81	gremlin 1, DAN family BMP antagonist	Homo sapiens	158-167
2612912-6	1989	We suggest that free fatty acids (FFA) and heparin to some extent share the same site of interaction on the LPL molecule; and that a high local concentration of FFA can displace LPL from its site of action--the vascular endothelium--by competing for binding to heparan sulfate.	Heparin	43-50	lipoprotein lipase	Cavia porcellus	108-111
34626387-4	2022	Heparins with other sulfation patterns are able to bind to a variety of other proteins such as FGF, VEGF, and CXCL-3.	Heparin	0-8	vascular endothelial growth factor A	Homo sapiens	100-104
34626387-4	2022	Heparins with other sulfation patterns are able to bind to a variety of other proteins such as FGF, VEGF, and CXCL-3.	Heparin	0-8	C-X-C motif chemokine ligand 3	Homo sapiens	110-116
34991339-2	2022	Methods: The authors functionalized collagen nanofibers by conjugating heparin to the following growth factors for sustained release: PDGF-BB, TGF-beta1 and CTGF.	Heparin	71-78	transforming growth factor beta 1	Homo sapiens	143-152
2512987-3	1989	In this study we assayed in rats the DAO-releasing capability of heparan sulphate, dermatan sulphate, chondroitin sulphate A and hyaluronic acid, all heparin related compounds.	Heparin	150-157	amine oxidase, copper containing 1	Rattus norvegicus	37-40
2509262-6	1989	Heparin potentiated the inhibitory effect of RGDS peptides on intact fibronectin, but not on the 105-kDa fragment.	Heparin	0-7	ral guanine nucleotide dissociation stimulator	Homo sapiens	45-49
2612912-6	1989	We suggest that free fatty acids (FFA) and heparin to some extent share the same site of interaction on the LPL molecule; and that a high local concentration of FFA can displace LPL from its site of action--the vascular endothelium--by competing for binding to heparan sulfate.	Heparin	43-50	lipoprotein lipase	Cavia porcellus	178-181
2512987-1	1989	Plasma diamine oxidase (DAO) values are enhanced by intravenous injection of heparin which releases the enzyme, synthesized in small bowel enterocytes, from binding sites located on endothelial cells of the intestinal microvasculature.	Heparin	77-84	amine oxidase, copper containing 1	Rattus norvegicus	7-22
2511229-0	1989	Diamine oxidase plasma activities after treatment with heparin and jejunal morphometry in untreated coeliac disease.	Heparin	55-62	amine oxidase copper containing 1	Homo sapiens	0-15
2512987-1	1989	Plasma diamine oxidase (DAO) values are enhanced by intravenous injection of heparin which releases the enzyme, synthesized in small bowel enterocytes, from binding sites located on endothelial cells of the intestinal microvasculature.	Heparin	77-84	amine oxidase, copper containing 1	Rattus norvegicus	24-27
2684963-4	1989	Heparin affinity chromatography and Western blot analysis demonstrated that the cell-associated growth factor was basic fibroblast growth factor (bFGF).	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	114-144
2684963-4	1989	Heparin affinity chromatography and Western blot analysis demonstrated that the cell-associated growth factor was basic fibroblast growth factor (bFGF).	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	146-150
2556811-1	1989	Protein C inhibitor (PCI) was purified from human plasma using immunoaffinity chromatography and heparin Sepharose chromatography, a method that allowed the purification of active and inactive inhibitor.	Heparin	97-104	serpin family A member 5	Homo sapiens	0-25
2556120-4	1989	Mr 25,000 ir-bFGF from regenerating rat liver, partially purified by heparin-affinity chromatography, induces plasminogen activator activity and cell proliferation in transformed fetal bovine aortic endothelial GM 7373 cells and competes with Mr 18,000 [125I]bFGF for the binding to high affinity bFGF receptors.	Heparin	69-76	fibroblast growth factor 2	Rattus norvegicus	13-17
2511229-1	1989	Diamine oxidase plasma concentrations after treatment with heparin were measured and compared with the surface to volume ratio of jejunal biopsy samples assessed by a morphometric technique in patients with untreated and treated coeliac disease and in biopsied controls.	Heparin	59-66	amine oxidase copper containing 1	Homo sapiens	0-15
2677012-4	1989	The purified HDGF was identified to be acidic fibroblast growth factor based on the following properties: molecular weight of 18,000, isoelectric point of 5.2, amino acid composition and sequence, its dissociation from a heparin affinity column at 0.9 M NaCl, potentiation of activity in the presence of heparin, and antigenicity.	Heparin	221-228	fibroblast growth factor 1	Bos taurus	39-70
2677012-4	1989	The purified HDGF was identified to be acidic fibroblast growth factor based on the following properties: molecular weight of 18,000, isoelectric point of 5.2, amino acid composition and sequence, its dissociation from a heparin affinity column at 0.9 M NaCl, potentiation of activity in the presence of heparin, and antigenicity.	Heparin	304-311	fibroblast growth factor 1	Bos taurus	39-70
2575969-8	1989	These data suggest that an increase in plasma Tg concentration, induced by lipid-heparin infusion, inhibits GRF-mediated GH secretion, possibly through stimulation of SRIF secretion.	Heparin	81-88	growth hormone releasing hormone	Bos taurus	108-111
2529161-1	1989	Topically applied heparin and heparan sulfate disaccharides, with the basic structure delta-4,5 uronyl-(1----4)-glucosamine and bearing a sulfate at the C-6 position of the glucosamine residue, are antihemostatics as potent as heparin, producing uncontrollable hemorrhage from small blood vessels.	Heparin	18-25	complement C6	Homo sapiens	153-156
2553707-4	1989	Chromatography on DEAE-cellulose, S-Sepharose, heptyl-Sepharose, heparin-agarose, and Mono Q results in greater than 20,000-fold purification of the insulin-stimulated enzyme with a 12% recovery.	Heparin	65-72	insulin	Oryctolagus cuniculus	149-156
2479114-1	1989	Influence of heparin, chondroitin sulfate C and dextran sulfate (MW 3,500 and 7,000) on plasmin catalyzed conversion of single-chain (scu-PA) to two-chain (u-PA) urokinase-type plasminogen activator and generation of plasmin in mixtures of scu-PA and Glu-plasminogen (Glu-plg) was investigated.	Heparin	13-20	plasminogen	Homo sapiens	88-95
2479114-2	1989	Conversion of scu-PA to u-PA catalyzed by plasmin was enhanced by chondroitin sulfate C and heparin, maximally by 10-fold and 3-fold, respectively.	Heparin	92-99	plasminogen	Homo sapiens	42-49
2590190-4	1989	Several arguments suggested that the mitogenic factor was related to bFGF: a) its affinity for heparin; b) the loss of its mitogenic activity by heating at 65 degrees C, which was prevented in the presence of heparin; c) the abolition of its mitogenic activity in the presence of protamine sulfate; d) finally, its mitogenic effect was reduced in the presence of antibody to bFGF.	Heparin	95-102	fibroblast growth factor 2	Mus musculus	69-73
2590190-4	1989	Several arguments suggested that the mitogenic factor was related to bFGF: a) its affinity for heparin; b) the loss of its mitogenic activity by heating at 65 degrees C, which was prevented in the presence of heparin; c) the abolition of its mitogenic activity in the presence of protamine sulfate; d) finally, its mitogenic effect was reduced in the presence of antibody to bFGF.	Heparin	209-216	fibroblast growth factor 2	Mus musculus	69-73
2592631-8	1989	All treatments (except heparin addition) also promoted lipolysis/unit cream LPL.	Heparin	23-30	lipoprotein lipase	Bos taurus	76-79
2534055-0	1989	[The effect of heparin on the proteolytic and fibrinolytic activity on plasmin(ogen) and fibrin clot lysis].	Heparin	15-22	plasminogen	Homo sapiens	71-78
2534055-1	1989	The effect of heparin on the proteolytic and fibrinolytic activities of plasmin and plasminogen was studied.	Heparin	14-21	plasminogen	Homo sapiens	72-79
2534055-5	1989	It was supposed that heparin inhibits the fibrinolytic effect of plasmin by way of formation of complexes with plasmin and reduction of plasmin specificity to the solid phase substrate, i. e., polymeric fibrin.	Heparin	21-28	plasminogen	Homo sapiens	65-72
2534055-5	1989	It was supposed that heparin inhibits the fibrinolytic effect of plasmin by way of formation of complexes with plasmin and reduction of plasmin specificity to the solid phase substrate, i. e., polymeric fibrin.	Heparin	21-28	plasminogen	Homo sapiens	111-118
2534055-5	1989	It was supposed that heparin inhibits the fibrinolytic effect of plasmin by way of formation of complexes with plasmin and reduction of plasmin specificity to the solid phase substrate, i. e., polymeric fibrin.	Heparin	21-28	plasminogen	Homo sapiens	111-118
2760054-1	1989	Heparin cofactor II (HCII) is a highly specific serine proteinase inhibitor, which complexes covalently with thrombin in a reaction catalyzed by heparin and other polyanions.	Heparin	145-152	serpin family D member 1	Homo sapiens	0-19
2760054-1	1989	Heparin cofactor II (HCII) is a highly specific serine proteinase inhibitor, which complexes covalently with thrombin in a reaction catalyzed by heparin and other polyanions.	Heparin	145-152	serpin family D member 1	Homo sapiens	21-25
2601789-4	1989	The increased PF4 levels explained the initial heparin resistance observed during anticoagulant treatment in this patient.	Heparin	47-54	platelet factor 4	Homo sapiens	14-17
2542313-6	1989	At 5.4 micrograms/ml heparin, H-TGL levels, as determined by triacyglycerol hydrolase activity, increased 7-fold after a 44-h incubation.	Heparin	21-28	lipase C, hepatic type	Homo sapiens	30-35
2542313-7	1989	Heparin exposure decreased intracellular H-TGL activity from 21.3 to 4.8 nmol of oleic acids released/h/10(8) cells and increased enzyme activity in the medium from 16.2 to 165.3 nmol of oleic acids released/h/10(8) cells.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	41-46
2542313-9	1989	The addition of actinomycin D or cycloheximide reversed the heparin-induced increase in H-TGL activity and mRNA.	Heparin	60-67	lipase C, hepatic type	Homo sapiens	88-93
2542313-10	1989	Heparin treatment did not increase the level of actin mRNA suggesting that elevated H-TGL mRNA is due to enhanced tissue-specific expression of H-TGL.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	84-89
2542313-10	1989	Heparin treatment did not increase the level of actin mRNA suggesting that elevated H-TGL mRNA is due to enhanced tissue-specific expression of H-TGL.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	144-149
2542313-12	1989	We conclude that heparin stimulates the de novo synthesis of H-TGL in liver parenchymal cells in vivo by influencing both transcriptional and post-transcriptional events.	Heparin	17-24	lipase C, hepatic type	Homo sapiens	61-66
2591923-1	1989	Apo E was purified from the very low density lipoprotein (VLDL) of normal and hypertriglyceridemic subjects by Sephadex G-75, heparin-Sepharose 4B affinity chromatography, and preparative SDS polyacrylamide gel electrophoresis.	Heparin	126-133	apolipoprotein E	Capra hircus	0-5
2777898-12	1989	Heparin also inhibited [3H]thymidine incorporation in AKR-2B and partially inhibited AKR-2B cell stimulation by TGFe; however, it further potentiated the already potent stimulation by bFGF.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	184-188
2554521-3	1989	In the presence of heparin the neutralization of APC was found to be biphasic.	Heparin	19-26	APC regulator of WNT signaling pathway	Homo sapiens	49-52
2570779-7	1989	The kinase activity was found to co-purify with TH activity through ammonium sulfate precipitation and DEAE-cellulose chromatography and could be only partially resolved from TH by heparin-agarose affinity chromatography.	Heparin	181-188	tyrosine hydroxylase	Rattus norvegicus	48-50
2551066-13	1989	Incubation of 10 micrograms/ml APC with NHP in the presence of 10 U/ml heparin yielded 11 micrograms/ml complexes after 90 min, which represent more than 90% of the maximum possible value.	Heparin	71-78	APC regulator of WNT signaling pathway	Homo sapiens	31-34
2801725-0	1989	Antithrombin inactivation by neutrophil elastase requires heparin.	Heparin	58-65	elastase, neutrophil expressed	Homo sapiens	29-48
2801725-3	1989	Specifically, antithrombin was rendered nonfunctional as an inhibitor of clotting enzymes as a result of a limited, heparin-dependent cleavage by neutrophil elastase.	Heparin	116-123	elastase, neutrophil expressed	Homo sapiens	146-165
2566609-4	1989	TFIIF enters into the transcription cycle via a preinitiation complex, and it is required for the formation of a complex capable of initiating transcription in the presence of heparin concentrations that inhibit the action of a free factor.	Heparin	176-183	general transcription factor IIF subunit 2 pseudogene 1	Homo sapiens	0-5
2801725-5	1989	Interestingly, neutrophil elastase was found to bind tightly to heparin and heparin-like materials.	Heparin	64-71	elastase, neutrophil expressed	Homo sapiens	15-34
2601789-5	1989	Subsequent heparin loading tests revealed an abnormal reaction of the PF4 plasma levels, i.e. no increase of PF4.	Heparin	11-18	platelet factor 4	Homo sapiens	70-73
2801725-5	1989	Interestingly, neutrophil elastase was found to bind tightly to heparin and heparin-like materials.	Heparin	76-83	elastase, neutrophil expressed	Homo sapiens	15-34
2601789-6	1989	However, upon repeated heparin injections this PF4 response normalized, which may be due to depletion of the endothelial cell associated heparin mobilizable PF4 pool.	Heparin	23-30	platelet factor 4	Homo sapiens	47-50
2717945-2	1989	This antibody localized bFGF in the extracellular matrix of mouse skeletal muscle, primarily in the fiber endomysium, which includes the heparin-containing basal lamina.	Heparin	137-144	fibroblast growth factor 2	Mus musculus	24-28
2601789-6	1989	However, upon repeated heparin injections this PF4 response normalized, which may be due to depletion of the endothelial cell associated heparin mobilizable PF4 pool.	Heparin	23-30	platelet factor 4	Homo sapiens	157-160
2627890-2	1989	Fractionation of P19 medium conditioned in the presence of heparin reveals the existence of two biochemically distinct growth factor species both of which exhibit high affinity for immobilised heparin and significant activity as amphibian mesoderm-inducing agents.	Heparin	59-66	interleukin 23, alpha subunit p19	Mus musculus	17-20
2548005-4	1989	Because this activity was diminished by heparin, a known inhibitor of casein kinase II, isolated gpI was incubated with purified casein kinase II and shown to be phosphorylated in an in vitro assay containing [gamma-32P]ATP.	Heparin	40-47	glucose-6-phosphate isomerase	Homo sapiens	97-100
2551064-8	1989	The second order rate constants for inhibition of bovine APC and Gla-domainless bovine APC by human PCI were 0.61 x 10(4) and 0.26 x 10(4) M-1s-1 in the absence of heparin and 0.54 x 10(6) and 0.71 x 10(6) M-1s-1 in the presence of heparin, respectively.	Heparin	164-171	APC regulator of WNT signaling pathway	Homo sapiens	87-90
2551064-8	1989	The second order rate constants for inhibition of bovine APC and Gla-domainless bovine APC by human PCI were 0.61 x 10(4) and 0.26 x 10(4) M-1s-1 in the absence of heparin and 0.54 x 10(6) and 0.71 x 10(6) M-1s-1 in the presence of heparin, respectively.	Heparin	232-239	APC regulator of WNT signaling pathway	Homo sapiens	87-90
2627890-2	1989	Fractionation of P19 medium conditioned in the presence of heparin reveals the existence of two biochemically distinct growth factor species both of which exhibit high affinity for immobilised heparin and significant activity as amphibian mesoderm-inducing agents.	Heparin	193-200	interleukin 23, alpha subunit p19	Mus musculus	17-20
2763268-3	1989	In every instance, after elution from heparin affinity and cation exchange chromatography, SDS gel electrophoresis reveals a single band attributable to PF4.	Heparin	38-45	platelet factor 4	Homo sapiens	153-156
2777882-4	1989	In the presence of heparin, bovine aFGF at doses between 0.5 and 1.0 ng/ml (30-60 pM) elicited half the maximum AHEC growth over a 4-day period depending on the cell line tested; in the absence of heparin, significant growth was not observed at aFGF concentrations less than 10-20 ng/ml.	Heparin	19-26	fibroblast growth factor 1	Bos taurus	35-39
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Heparin	122-129	serpin family D member 1	Homo sapiens	49-53
2732232-4	1989	A potentially complex reaction mechanism is suggested by the binding of both neutrophil elastase and antithrombin to heparin.	Heparin	117-124	elastase, neutrophil expressed	Homo sapiens	77-96
2524251-15	1989	The stimulation of DNA synthesis induced by HPTA was totally abrogated by transforming growth factor-beta and markedly reduced in the presence of heparin.	Heparin	146-153	hepatocyte growth factor	Homo sapiens	44-48
2777882-4	1989	In the presence of heparin, bovine aFGF at doses between 0.5 and 1.0 ng/ml (30-60 pM) elicited half the maximum AHEC growth over a 4-day period depending on the cell line tested; in the absence of heparin, significant growth was not observed at aFGF concentrations less than 10-20 ng/ml.	Heparin	197-204	fibroblast growth factor 1	Bos taurus	35-39
2542313-0	1989	Heparin induces the expression of hepatic triglyceride lipase in a human hepatoma (HepG2) cell line.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	34-61
2777882-7	1989	In contrast, the mitogenic activity of bovine aFGF preincubated in the presence of heparin-containing culture medium without cells was dramatically stabilized (half-life 24-29 hours).	Heparin	83-90	fibroblast growth factor 1	Bos taurus	46-50
2542313-4	1989	In the present study, the effects of heparin exposure on the secretion of H-TGL were examined in a human parenchymal hepatoma (HepG2) cell line.	Heparin	37-44	lipase C, hepatic type	Homo sapiens	74-79
2542313-5	1989	The addition of heparin to serum-supplemented medium induced the secretion of H-TGL in a time- and concentration-dependent manner.	Heparin	16-23	lipase C, hepatic type	Homo sapiens	78-83
2708348-0	1989	Importance of size, sulfation, and anticoagulant activity in the potentiation of acidic fibroblast growth factor by heparin.	Heparin	116-123	fibroblast growth factor 1	Bos taurus	81-112
2708348-12	1989	The potentiation of aFGF by the high sulfate fraction correlated with the saccharide size: 12 or more monosaccharide units were necessary to achieve potentiation equivalent to whole heparin, octa- and decasaccharides were mildly stimulatory, and hexasaccharides were without effect.	Heparin	182-189	fibroblast growth factor 1	Bos taurus	20-24
2544038-7	1989	Plasma or pure protein C inhibitor (at the same concentration) showed the same effect of heparin on activated protein C inhibition, indicating that protein C inhibitor accounts for all the heparin-dependent inhibition of activated protein C in vivo.	Heparin	89-96	serpin family A member 5	Homo sapiens	15-34
2544038-7	1989	Plasma or pure protein C inhibitor (at the same concentration) showed the same effect of heparin on activated protein C inhibition, indicating that protein C inhibitor accounts for all the heparin-dependent inhibition of activated protein C in vivo.	Heparin	89-96	serpin family A member 5	Homo sapiens	148-167
2544038-7	1989	Plasma or pure protein C inhibitor (at the same concentration) showed the same effect of heparin on activated protein C inhibition, indicating that protein C inhibitor accounts for all the heparin-dependent inhibition of activated protein C in vivo.	Heparin	189-196	serpin family A member 5	Homo sapiens	148-167
2523801-3	1989	Although GCP/IL-8 and beta-thromboglobulin had a similar affinity for heparin, they could be separated on a cation-exchange column.	Heparin	70-77	pro-platelet basic protein	Homo sapiens	22-42
2739146-2	1989	The lipoprotein lipase (LpL) and hepatic triglyceride lipase (HTGL) activities of the post-heparin plasma were low, but detectable.	Heparin	91-98	lipase C, hepatic type	Homo sapiens	33-60
2739146-2	1989	The lipoprotein lipase (LpL) and hepatic triglyceride lipase (HTGL) activities of the post-heparin plasma were low, but detectable.	Heparin	91-98	lipase C, hepatic type	Homo sapiens	62-66
2543098-0	1989	Effect of rabbit thrombomodulin on thrombin inhibition by antithrombin in the presence of heparin.	Heparin	90-97	thrombomodulin	Oryctolagus cuniculus	17-31
2553304-2	1989	A human hepatoma-derived growth factor with potent growth-promoting activity, was partially purified from the conditioned medium of HuH-7 cells, using ion-exchange, heparin affinity chromatography and gel filtration.	Heparin	165-172	heparin binding growth factor	Homo sapiens	8-38
2543098-4	1989	The acidic form (retarded on ion-exchange chromatography) of thrombomodulin is now shown to prevent the rapid inactivation of thrombin by antithrombin in the presence of heparin, presumably by preventing the formation of the ternary thrombin-AT-heparin complex.	Heparin	170-177	thrombomodulin	Oryctolagus cuniculus	61-75
2543098-8	1989	It is concluded that the acidic domain of rabbit thrombomodulin, a chondroitin (dermatan) sulfate glycosaminoglycan, interacts with a site of the thrombin molecule that is not involved in the protein C activation cofactor function, but is essential to the cleavage of fibrinogen or binding of heparin.	Heparin	293-300	thrombomodulin	Oryctolagus cuniculus	49-63
2752479-6	1989	Inhibition of thrombin activity by the ATIII-APC-heparin mixture was weak as compared with that by the ATIII-heparin mixture after a 1-min incubation, but after a 2-min incubation the inhibitory activities were equal.	Heparin	49-56	APC regulator of WNT signaling pathway	Homo sapiens	45-48
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	APC regulator of WNT signaling pathway	Homo sapiens	46-49
2521859-7	1989	Both forms co-eluted with the sole lipoprotein lipase activity peak from heparin-Sepharose; this indicates that both were dimeric.	Heparin	73-80	lipoprotein lipase	Cavia porcellus	35-53
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	APC regulator of WNT signaling pathway	Homo sapiens	167-170
2509208-1	1989	In addition to LDL, Lp(a) can be quantitatively eliminated from plasma in an extracorporeal LDL-apheresis procedure based on precipitation with heparin at pH 5.12.	Heparin	144-151	lipoprotein(a)	Homo sapiens	20-25
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	APC regulator of WNT signaling pathway	Homo sapiens	167-170
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	144-151	APC regulator of WNT signaling pathway	Homo sapiens	46-49
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	144-151	APC regulator of WNT signaling pathway	Homo sapiens	167-170
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	144-151	APC regulator of WNT signaling pathway	Homo sapiens	167-170
2706002-5	1989	Heparin (10 units/ml) increased remnant uptake by 63% (P less than 0.01), [3H]cholesteryl ester accumulation in the cell pellet by 110% (P less than 0.025) and hepatic lipase activity secreted in the medium by 2.4-fold (P less than 0.01) and by 3.3-fold (P less than 0.01) at the end of the preincubation and incubation periods respectively.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	160-174
2706002-9	1989	Hepatic lipase, which seems to underly the stimulating effect of heparin, facilitates remnant uptake in vitro, and this could be mediated by at least one (or both) of its hydrolytic properties.	Heparin	65-72	lipase C, hepatic type	Homo sapiens	0-14
2752479-8	1989	When the inhibitory effect of APC alone or the APC-heparin mixture on the platelet prothrombin converting activity (PPCA) was examined, heparin accelerated the PPCA inhibition by APC.	Heparin	136-143	APC regulator of WNT signaling pathway	Homo sapiens	30-33
2752479-8	1989	When the inhibitory effect of APC alone or the APC-heparin mixture on the platelet prothrombin converting activity (PPCA) was examined, heparin accelerated the PPCA inhibition by APC.	Heparin	136-143	APC regulator of WNT signaling pathway	Homo sapiens	47-50
2763268-6	1989	PF4 affinity for GAGs is as follows: heparin greater than heparan sulphate much greater than dermatan sulphate.	Heparin	37-44	platelet factor 4	Homo sapiens	0-3
2752479-8	1989	When the inhibitory effect of APC alone or the APC-heparin mixture on the platelet prothrombin converting activity (PPCA) was examined, heparin accelerated the PPCA inhibition by APC.	Heparin	136-143	APC regulator of WNT signaling pathway	Homo sapiens	47-50
2713350-8	1989	In all tissues that we have examined, STOP activity elutes as a single peak from heparin affinity columns, and in common with brain STOP, all activity is Ca2+-calmodulin sensitive.	Heparin	81-88	microtubule-associated protein 6	Rattus norvegicus	38-42
2785868-2	1989	Among the factors examined, bovine brain acidic fibroblast growth factor (FGF) at 1 to 10 ng/ml significantly promoted DNA synthesis of the cells in the presence of 5 U/ml heparin, whereas type beta transforming growth factor inhibited it in a dose-dependent manner.	Heparin	172-179	fibroblast growth factor 1	Bos taurus	41-72
2465300-1	1989	The mechanism(s) by which heparin influences the biological activities of acidic and basic fibroblast growth factors (aFGF and bFGF) is not completely understood.	Heparin	26-33	fibroblast growth factor 2	Rattus norvegicus	127-131
2465300-2	1989	One mechanism by which heparin could alter the biological activities of aFGF and bFGF is by altering their biological half-lives.	Heparin	23-30	fibroblast growth factor 2	Rattus norvegicus	81-85
2543347-1	1989	The purpose of this study was to compare lipoprotein lipase (LPL) and hepatic lipase (HL) releasing activities of different low molecular weight heparins (LMWH) and of a standard heparin.	Heparin	145-152	lipase C, hepatic type	Homo sapiens	86-88
2692957-6	1989	Recent progress in the isolation of osteogenin, a specific bone differentiation factor, by heparin affinity chromatography permits the further investigation of the commitment and clonal expansion of the putative osteoprogenitor stem cells.	Heparin	91-98	bone morphogenetic protein 3	Homo sapiens	36-46
2735657-0	1989	Interaction of lipoprotein lipase with heparin.	Heparin	39-46	lipoprotein lipase	Bos taurus	15-33
2735657-2	1989	We previously reported that LPL binds to cultured endothelial cells with a Km of 2.7 x 10(-7) M and that this binding is inhibited by heparinase, heparin, or heparan sulfate.	Heparin	134-141	lipoprotein lipase	Bos taurus	28-31
2735657-6	1989	Amino acid residues 292 to 300 of bovine LPL are extremely similar to the reported heparin binding sites on apolipoproteins B-100 (amino acid residues 3359-3367) and E (amino acid residues 142-150).	Heparin	83-90	lipoprotein lipase	Bos taurus	41-44
2735664-1	1989	In vitro, PF4 is comparable to protamine sulfate in the neutralization of heparin, but the complexes formed with heparin are different.	Heparin	74-81	platelet factor 4	Homo sapiens	10-13
2735664-4	1989	When excess protamine is used to neutralize heparin in the presence of PF4, large heparin-protamine complexes are formed incorporating PF4.	Heparin	44-51	platelet factor 4	Homo sapiens	71-74
2735664-4	1989	When excess protamine is used to neutralize heparin in the presence of PF4, large heparin-protamine complexes are formed incorporating PF4.	Heparin	44-51	platelet factor 4	Homo sapiens	135-138
2735664-4	1989	When excess protamine is used to neutralize heparin in the presence of PF4, large heparin-protamine complexes are formed incorporating PF4.	Heparin	82-89	platelet factor 4	Homo sapiens	71-74
2475734-3	1989	Western-blotting of the fractions from the heparin-Sepharose column with a monoclonal antibody prepared against postheparin plasma H-TGL and which binds to an epitope in the carboxyl-terminus of H-TGL gave a single immunoreactive protein band of 65 kDa.	Heparin	43-50	lipase C, hepatic type	Homo sapiens	131-136
2735664-4	1989	When excess protamine is used to neutralize heparin in the presence of PF4, large heparin-protamine complexes are formed incorporating PF4.	Heparin	82-89	platelet factor 4	Homo sapiens	135-138
2735664-6	1989	Since PF4 is liberated during ECB procedures, its contribution to the stability of heparin-protamine complexes in vivo may influence the amount of protamine needed to neutralize heparin as well as affect the reactions which have been reported on injection of protamine after ECB.	Heparin	83-90	platelet factor 4	Homo sapiens	6-9
2735664-6	1989	Since PF4 is liberated during ECB procedures, its contribution to the stability of heparin-protamine complexes in vivo may influence the amount of protamine needed to neutralize heparin as well as affect the reactions which have been reported on injection of protamine after ECB.	Heparin	178-185	platelet factor 4	Homo sapiens	6-9
2543347-0	1989	In vivo and in vitro release of lipoprotein lipase and hepatic lipase by low molecular weight heparins.	Heparin	94-102	lipase C, hepatic type	Homo sapiens	55-69
2484952-1	1989	Heparin has been shown to interact with acidic fibroblast growth factor (aFGF) and to potentiate the biological activity of aFGF on fibroblastic cells.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	40-71
2484952-1	1989	Heparin has been shown to interact with acidic fibroblast growth factor (aFGF) and to potentiate the biological activity of aFGF on fibroblastic cells.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	73-77
2484952-1	1989	Heparin has been shown to interact with acidic fibroblast growth factor (aFGF) and to potentiate the biological activity of aFGF on fibroblastic cells.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	124-128
2484952-5	1989	We have shown that 20 micrograms of heparin or 400 micrograms of DDE added to 1 ml of culture medium has no effect on cell proliferation alone but potentiates the mitogenic activity of aFGF ten fold if aFGF is added at doses corresponding to half maximum stimulation (ED50).	Heparin	36-43	fibroblast growth factor 1	Bos taurus	185-189
2484952-5	1989	We have shown that 20 micrograms of heparin or 400 micrograms of DDE added to 1 ml of culture medium has no effect on cell proliferation alone but potentiates the mitogenic activity of aFGF ten fold if aFGF is added at doses corresponding to half maximum stimulation (ED50).	Heparin	36-43	fibroblast growth factor 1	Bos taurus	202-206
2484952-6	1989	We have also studied the effect of various concentrations of heparin and DDE on the binding of 125I-aFGF on bovine brain membranes.	Heparin	61-68	fibroblast growth factor 1	Bos taurus	100-104
2484952-7	1989	Interestingly, the binding of 125I-aFGF increased three-fold as the concentration of heparin was increased up to 0.2 microgram/ml.	Heparin	85-92	fibroblast growth factor 1	Bos taurus	35-39
2484952-8	1989	At 1 microgram/ml of heparin, the amount of bound 125I-aFGF is comparable to that obtained in the absence of heparin.	Heparin	21-28	fibroblast growth factor 1	Bos taurus	55-59
2484952-9	1989	At higher concentrations, heparin displaces bound 125I-aFGF, and a 50% displacement is seen with 20 micrograms/ml of heparin.	Heparin	26-33	fibroblast growth factor 1	Bos taurus	55-59
2730347-9	1989	(e) Commercial heparin releases enzymes from the endothelium, lipoprotein lipase and histaminase (D.A.O.).	Heparin	15-22	amine oxidase copper containing 1	Homo sapiens	85-96
2475734-3	1989	Western-blotting of the fractions from the heparin-Sepharose column with a monoclonal antibody prepared against postheparin plasma H-TGL and which binds to an epitope in the carboxyl-terminus of H-TGL gave a single immunoreactive protein band of 65 kDa.	Heparin	43-50	lipase C, hepatic type	Homo sapiens	195-200
3232122-2	1988	Possible mechanisms include altered heparin pharmacokinetics and/or a decreased expression of anticoagulant activity of heparin in new-born plasma because of low levels of antithrombin III (AT-III).	Heparin	120-127	serpin family C member 1	Sus scrofa	172-188
2491946-0	1989	Modifications in enterocyte diamine oxidase distribution induced by heparin in the rat.	Heparin	68-75	amine oxidase, copper containing 1	Rattus norvegicus	28-43
2491946-3	1989	In this study we assessed the changes in DAO distribution into the enterocytes induced by a high dose of intraperitoneal heparin (1000 IU) in the rat, by assaying DAO activity on subcellular fractions obtained from ileal mucosa homogenate.	Heparin	121-128	amine oxidase, copper containing 1	Rattus norvegicus	41-44
2491946-3	1989	In this study we assessed the changes in DAO distribution into the enterocytes induced by a high dose of intraperitoneal heparin (1000 IU) in the rat, by assaying DAO activity on subcellular fractions obtained from ileal mucosa homogenate.	Heparin	121-128	amine oxidase, copper containing 1	Rattus norvegicus	163-166
2491946-4	1989	Heparin injection induced a marked reduction of enzyme activity in the S2 fraction (cytosol): after 30 min less than 20% of DAO activity is still found and only 8% after 150 min.	Heparin	0-7	amine oxidase, copper containing 1	Rattus norvegicus	124-127
2491946-7	1989	These results indicate that enterocytic DAO is distributed in two different compartments: DAO located in the cytosol is quickly released by heparin, while the organelles-linked enzyme is more slowly released.	Heparin	140-147	amine oxidase, copper containing 1	Rattus norvegicus	40-43
2491946-7	1989	These results indicate that enterocytic DAO is distributed in two different compartments: DAO located in the cytosol is quickly released by heparin, while the organelles-linked enzyme is more slowly released.	Heparin	140-147	amine oxidase, copper containing 1	Rattus norvegicus	90-93
2624780-5	1989	Heparin consistently altered the pattern: slowing the rate of clearance (t1/2 = 4.5 min), increasing the plateau concentration in the blood during continuous infusion (32.5 +/- 14.3% of the amount infused), and allowing intact (as determined by gel analysis) bFGF to cross from the circulation into the urine.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	259-263
2922702-1	1989	Heparins from different species and tissues show similar levels of ATIII and HCII mediated anti-IIa activities.	Heparin	0-8	serpin family D member 1	Homo sapiens	77-81
2922702-3	1989	Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity.	Heparin	106-113	serpin family D member 1	Homo sapiens	246-250
3181626-5	1988	It is shown that the adhesion of ectodermal cells is modified by their interaction with a heparin-binding domain of the FN molecule.	Heparin	90-97	fibronectin 1 S homeolog	Xenopus laevis	120-122
3178799-4	1988	The molecule has been identified as a bFGF-like molecule on the basis of its biological activity, its affinity for heparin-Sepharose, and its cross-reactivity with anti-human bFGF antibodies.	Heparin	115-122	fibroblast growth factor 2	Rattus norvegicus	38-42
3178799-7	1988	On the basis of its affinity for heparin-Sepharose and its immunological characteristics, this protein appears to be an high molecular weight form of bFGF.	Heparin	33-40	fibroblast growth factor 2	Rattus norvegicus	150-154
2842338-8	1988	Although topoisomerase II was phosphorylated in homogenates under conditions that specifically stimulate protein kinase C, calcium/calmodulin-dependent protein kinase, or cAMP-dependent protein kinase, modification was always sensitive to anti-casein kinase II antiserum or heparin.	Heparin	274-281	Topoisomerase 2	Drosophila melanogaster	9-25
2458767-5	1988	The heparin structure conferring high-affinity binding to antithrombin III is thus not specifically involved in binding to EC-SOD C. The non-biosynthetic compound dextran sulfate 5000 was an order of magnitude more efficient than heparin.	Heparin	4-11	serpin family C member 1	Sus scrofa	58-74
3232122-2	1988	Possible mechanisms include altered heparin pharmacokinetics and/or a decreased expression of anticoagulant activity of heparin in new-born plasma because of low levels of antithrombin III (AT-III).	Heparin	120-127	serpin family C member 1	Sus scrofa	190-196
2458767-5	1988	The heparin structure conferring high-affinity binding to antithrombin III is thus not specifically involved in binding to EC-SOD C. The non-biosynthetic compound dextran sulfate 5000 was an order of magnitude more efficient than heparin.	Heparin	230-237	serpin family C member 1	Sus scrofa	58-74
2460147-0	1988	In vitro effects of pregnancy-associated plasma protein-A: artifacts due to heparin.	Heparin	76-83	pappalysin 1	Homo sapiens	20-57
2460147-4	1988	A PAPP-A-free washing of the heparin-Sepharose column used during the purification of PAPP-A showed inhibitory activities similar to those of purified PAPP-A.	Heparin	29-36	pappalysin 1	Homo sapiens	2-8
2460147-4	1988	A PAPP-A-free washing of the heparin-Sepharose column used during the purification of PAPP-A showed inhibitory activities similar to those of purified PAPP-A.	Heparin	29-36	pappalysin 1	Homo sapiens	86-92
2460147-8	1988	A protocol to eliminate free and PAPP-A-bound heparin is presented herein, and implications for other previously reported in vitro effects of PAPP-A are discussed.	Heparin	46-53	pappalysin 1	Homo sapiens	33-39
3232122-8	1988	Thus apparent heparin resistance of the newborn is due to both an increased volume of distribution and the low AT-III level which limits the measurement of the anticoagulant activity of heparin in conventional anti-factor Xa assays.	Heparin	14-21	serpin family C member 1	Sus scrofa	111-117
2460147-4	1988	A PAPP-A-free washing of the heparin-Sepharose column used during the purification of PAPP-A showed inhibitory activities similar to those of purified PAPP-A.	Heparin	29-36	pappalysin 1	Homo sapiens	86-92
3232122-8	1988	Thus apparent heparin resistance of the newborn is due to both an increased volume of distribution and the low AT-III level which limits the measurement of the anticoagulant activity of heparin in conventional anti-factor Xa assays.	Heparin	186-193	serpin family C member 1	Sus scrofa	111-117
3217919-11	1988	The assay is also sensitive to other HC II activators such as heparin and pentosan polysulfate.	Heparin	62-69	serpin family D member 1	Homo sapiens	37-42
3134178-1	1988	The highest diamine oxidase activity is contained in small-bowel mucosa and, after heparin administration, the enzyme is released by the intestine into the plasma.	Heparin	83-90	amine oxidase copper containing 1	Homo sapiens	12-27
2839510-1	1988	Hepatic triglyceride lipase (H-TGL) was isolated from human postheparin plasma by column chromatography on heparin-Sepharose and phenyl-Sepharose and immunoaffinity chromatography with monoclonal antibodies.	Heparin	64-71	lipase C, hepatic type	Homo sapiens	0-27
2839510-1	1988	Hepatic triglyceride lipase (H-TGL) was isolated from human postheparin plasma by column chromatography on heparin-Sepharose and phenyl-Sepharose and immunoaffinity chromatography with monoclonal antibodies.	Heparin	64-71	lipase C, hepatic type	Homo sapiens	29-34
3217922-0	1988	Antithrombotic properties of heparin in a neonatal piglet model of thrombin-induced thrombosis.	Heparin	29-36	coagulation factor II, thrombin	Sus scrofa	67-75
3217922-1	1988	The relative deficiency of antithrombin III (AT III) in neonatal plasma results in lower recovery of heparin in some assay systems.	Heparin	101-108	serpin family C member 1	Sus scrofa	27-43
3217922-1	1988	The relative deficiency of antithrombin III (AT III) in neonatal plasma results in lower recovery of heparin in some assay systems.	Heparin	101-108	serpin family C member 1	Sus scrofa	45-51
2843763-1	1988	The progesterone receptor (PR) was partially purified from T47D human breast cancer cells by sequential chromatography on phosphocellulose, heparin-Sepharose, and DNA-cellulose.	Heparin	140-147	progesterone receptor	Homo sapiens	4-25
3288621-4	1988	The recombinant PF4 (rPF4) was purified by heparin-agarose affinity chromatography and reverse-phase high performance liquid chromatography.	Heparin	43-50	platelet factor 4	Homo sapiens	16-19
3288621-4	1988	The recombinant PF4 (rPF4) was purified by heparin-agarose affinity chromatography and reverse-phase high performance liquid chromatography.	Heparin	43-50	platelet factor 4	Rattus norvegicus	21-25
3409080-6	1988	Lipoprotein lipase activity in post-heparin plasma showed no correlation with either abdominal fat or total body fat content.	Heparin	36-43	lipoprotein lipase	Gallus gallus	0-18
2843763-1	1988	The progesterone receptor (PR) was partially purified from T47D human breast cancer cells by sequential chromatography on phosphocellulose, heparin-Sepharose, and DNA-cellulose.	Heparin	140-147	progesterone receptor	Homo sapiens	27-29
3360217-8	1988	Overall, preheparin plasma HTGL and LPL activities may reflect ongoing lipoprotein lipolytic activity in tissue beds, and because these measurements do not require the administration of intravenous heparin, they should prove useful for additional studies of short-term regulation of the lipases.	Heparin	12-19	lipase C, hepatic type	Homo sapiens	27-31
3217922-8	1988	However, pretreatment with AT III concentrate significantly improved the antithrombotic properties of heparin in this age group (p less than 0.0001).	Heparin	102-109	serpin family C member 1	Sus scrofa	27-33
3217922-9	1988	We conclude that physiologically low AT III levels reduce the efficacy of heparin in neutralizing thrombin activity in newborn piglets.	Heparin	74-81	serpin family C member 1	Sus scrofa	37-43
2967302-17	1988	Heparan sulfate and chondroitin sulfate showed concentration-dependent potentiation of NGF; maximally active concentrations of heparan sulfate (100 micrograms/ml) and chondroitin sulfate (1 mg/ml) increased the potency of NGF 3-fold, whereas heparin, dermatan sulfate and hyaluronic acid had no effect.	Heparin	242-249	nerve growth factor	Rattus norvegicus	87-90
3217922-9	1988	We conclude that physiologically low AT III levels reduce the efficacy of heparin in neutralizing thrombin activity in newborn piglets.	Heparin	74-81	coagulation factor II, thrombin	Sus scrofa	98-106
2967302-11	1988	Heparin also altered the activity of bFGF; increasing concentrations of heparin (0.01-1 micrograms/ml) correlated with increased potentiation.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	37-41
2967302-11	1988	Heparin also altered the activity of bFGF; increasing concentrations of heparin (0.01-1 micrograms/ml) correlated with increased potentiation.	Heparin	72-79	fibroblast growth factor 2	Rattus norvegicus	37-41
3206560-3	1988	The specific activity of hepatic lipase purified from the ordinary heparin-containing homogenate by affinity chromatography on heparin-sepharose 4B was equal to 3800 microM of FFA/h per mg of protein.	Heparin	67-74	hepatic triacylglycerol lipase	Oryctolagus cuniculus	25-39
2967302-14	1988	Maximally active concentrations of heparin (1 microgram/ml) and chondroitin sulfate (1 mg/ml) increased the potency of bFGF 5-fold.	Heparin	35-42	fibroblast growth factor 2	Rattus norvegicus	119-123
3286063-5	1988	The assay cannot be carried out in heparin-anticoagulated plasma, because the free heparin competes with the immobilized heparin for the binding of transcobalamin II.	Heparin	83-90	transcobalamin 2	Homo sapiens	148-165
3286063-5	1988	The assay cannot be carried out in heparin-anticoagulated plasma, because the free heparin competes with the immobilized heparin for the binding of transcobalamin II.	Heparin	83-90	transcobalamin 2	Homo sapiens	148-165
3286063-0	1988	Application of heparin-conjugated Sepharose for the measurement of cobalamin-saturated and unsaturated transcobalamin II.	Heparin	15-22	transcobalamin 2	Homo sapiens	103-120
3286063-1	1988	The cobalamin-binding plasma protein transcobalamin II has a high affinity for the anticoagulant heparin.	Heparin	97-104	transcobalamin 2	Homo sapiens	37-54
3286063-3	1988	Transcobalamin II is adsorbed from human plasma to heparin-conjugated Sepharose under suitable conditions and either cobalamin from adsorbed holo-transcobalamin II is measured by a radioisotope dilution assay or apo-transcobalamin II is determined by measuring the adsorbed unsaturated cobalamin-binding capacity with radioactive cobalamin.	Heparin	51-58	transcobalamin 2	Homo sapiens	0-17
3286063-6	1988	The amount of heparin in plasma from patients being treated with subcutaneous or intravenous heparin is too low to interfere significantly with the measurement of transcobalamin II.	Heparin	14-21	transcobalamin 2	Homo sapiens	163-180
3206560-3	1988	The specific activity of hepatic lipase purified from the ordinary heparin-containing homogenate by affinity chromatography on heparin-sepharose 4B was equal to 3800 microM of FFA/h per mg of protein.	Heparin	127-134	hepatic triacylglycerol lipase	Oryctolagus cuniculus	25-39
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Heparin	106-113	serpin family D member 1	Homo sapiens	0-19
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Heparin	106-113	serpin family D member 1	Homo sapiens	21-25
3206560-4	1988	If the homogenate previously treated with liquid nitrogen was used as a source of enzyme, the specific activity of hepatic lipase was higher, namely, 13,000 and 19,000 microM of FFA/h per mg of protein in the presence or absence of heparin, respectively.	Heparin	232-239	hepatic triacylglycerol lipase	Oryctolagus cuniculus	115-129
2894851-11	1988	The recombinant HCII formed a complex with 125I-thrombin in a reaction that required the presence of heparin or dermatan sulfate.	Heparin	101-108	serpin family D member 1	Homo sapiens	16-20
3261294-3	1988	The second inhibitor was isolated based on its heparin-independent ability to inhibit and complex with APC.	Heparin	47-54	APC regulator of WNT signaling pathway	Homo sapiens	103-106
3501246-10	1987	The addition of 250 micrograms/ml heparin to the collagen suspension potentiated the response to PDGF and bFGF, but not to TGF beta or EGF.	Heparin	34-41	fibroblast growth factor 2	Rattus norvegicus	106-110
3401503-0	1988	Studies on the structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II.	Heparin	42-49	serpin family D member 1	Homo sapiens	94-113
3068010-5	1988	Studies with primary rat osteoblast-like cells exposed either to mixed BDGFs, pure TGF-beta, or heparin-purified PDGF, aFGF, or bFGF from bovine bone have shown a general dose-dependent mitogenic effect.	Heparin	96-103	fibroblast growth factor 2	Rattus norvegicus	128-132
3678131-8	1987	Recombinant aFGF (bovine sequence) also stimulated cell proliferation (1.5-fold), and its potency was augmented by heparin (50 micrograms/ml), about 2-fold.	Heparin	115-122	fibroblast growth factor 1	Bos taurus	12-16
3401503-1	1988	The structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II (HC II) were investigated.	Heparin	31-38	serpin family D member 1	Homo sapiens	83-102
3401503-1	1988	The structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II (HC II) were investigated.	Heparin	31-38	serpin family D member 1	Homo sapiens	104-109
3401503-2	1988	A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III).	Heparin	31-38	serpin family D member 1	Homo sapiens	168-173
2906331-9	1988	The mitogenic activities of aFGF and bFGF were potentiated similarly by heparan sulfate and by heparin, with a maximum stimulation of about 100% at 100 micrograms/ml heparin.	Heparin	95-102	fibroblast growth factor 2	Rattus norvegicus	37-41
2847353-1	1988	Heparin and a low molecular heparin fragment, injected intravenously in volunteers, increased the plasma concentrations of platelet factor 4, but did not induce platelet activation as judged from excretion of 2,3-dinor-TxB2 (a major thromboxane A2 metabolite) and beta-thromboglobulin (btg) in urine and from btg levels in plasma.	Heparin	0-7	pro-platelet basic protein	Homo sapiens	264-284
2906331-9	1988	The mitogenic activities of aFGF and bFGF were potentiated similarly by heparan sulfate and by heparin, with a maximum stimulation of about 100% at 100 micrograms/ml heparin.	Heparin	166-173	fibroblast growth factor 2	Rattus norvegicus	37-41
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Heparin	11-18	serpin family D member 1	Homo sapiens	134-153
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Heparin	171-178	serpin family D member 1	Homo sapiens	0-19
3691797-2	1987	The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate.	Heparin	84-91	serpin family D member 1	Homo sapiens	30-35
3691797-3	1987	However, this enhancement by heparin dwindled to 110- and 9.6-fold when the modified HC II and the modified thrombin, respectively, were substituted for native proteins.	Heparin	29-36	serpin family D member 1	Homo sapiens	85-90
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	serpin family D member 1	Homo sapiens	92-97
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	serpin family D member 1	Homo sapiens	195-200
2962279-5	1987	In two patients prophylaxis with s.c. heparin (2 X 7500 IU/d) was started at the time of the first increase of BTG (around 10th week of gestation), leading to normalization of BTG.	Heparin	38-45	pro-platelet basic protein	Homo sapiens	111-114
2962279-5	1987	In two patients prophylaxis with s.c. heparin (2 X 7500 IU/d) was started at the time of the first increase of BTG (around 10th week of gestation), leading to normalization of BTG.	Heparin	38-45	pro-platelet basic protein	Homo sapiens	176-179
2962279-6	1987	When BTG was again elevated, the dose of heparin was increased stepwise to 2 x 15,000 IU/d; in this way functional AT III levels remained in the range of 28-50%.	Heparin	41-48	pro-platelet basic protein	Homo sapiens	5-8
2824468-1	1987	Purified plasma and urinary protein C inhibitors (PCI) formed heparin-dependent complexes with activated protein C (APC) which were detected by immunoblotting after nondenaturing gel electrophoresis.	Heparin	62-69	serpin family A member 5	Homo sapiens	50-53
2824468-2	1987	Bands representing APC.PCI complexes were also seen on immunoblots after incubation of plasma with APC and heparin.	Heparin	107-114	serpin family A member 5	Homo sapiens	23-26
2824468-5	1987	Purified plasma PCI was fully reactive in an enzyme-linked immunoabsorbent assay for PAI-3, and plasma and urinary PCI inhibited urokinase activity in a heparin-dependent manner.	Heparin	153-160	serpin family A member 5	Homo sapiens	16-19
2824468-5	1987	Purified plasma PCI was fully reactive in an enzyme-linked immunoabsorbent assay for PAI-3, and plasma and urinary PCI inhibited urokinase activity in a heparin-dependent manner.	Heparin	153-160	serpin family A member 5	Homo sapiens	115-118
3663717-3	1987	The core histones H2A and H3 both incorporate 32P from [gamma-32P]ATP as well as from [gamma-32P]GTP but their phosphorylation is differentially affected by heparin.	Heparin	157-164	H2A clustered histone 18	Homo sapiens	18-28
3663717-6	1987	Of the non-histone protein kinase substrates, we could only detect two, the 44-kDa and 115-kDa proteins, which are heparin sensitive with either ATP or GTP and, thus, strictly meet the criteria for casein kinase type II-specific phosphorylation.	Heparin	115-122	PDLIM1 interacting kinase 1 like	Homo sapiens	198-211
2445254-3	1987	Heparin manganese isolates had the highest HDL cholesterol concentrations and the lowest HLD2:HDL3 cholesterol ratios, which differed further from the other isolates at higher HDL concentrations.	Heparin	0-7	gap junction protein gamma 2	Homo sapiens	89-93
2962279-11	1987	AT III in plasma 51-72%) in addition to heparin (2 x 12,500 IU/d), resulting in BTG levels of 33-51 ng/ml.	Heparin	40-47	pro-platelet basic protein	Homo sapiens	80-83
3134174-3	1988	The purpose of this study was to develop a simple heparin stimulation test for assessing postheparin plasma diamine oxidase activity in Crohn"s disease.	Heparin	50-57	amine oxidase copper containing 1	Homo sapiens	108-123
2446864-7	1987	Binding of MAG to collagen G is most effectively blocked by a high molecular weight dextran sulfate, heparan sulfate and heparin, with chondroitin sulfate and a low molecular weight dextran sulfate being less potent blockers.	Heparin	121-128	myelin-associated glycoprotein	Mus musculus	11-14
2956994-3	1987	Heparin was incorporated into the complex in a saturable manner, and was released in active anticoagulant form by plasmin but not by urokinase.	Heparin	0-7	plasminogen	Homo sapiens	114-121
3113515-4	1987	The PAI-1 could not be removed by incubating ECM in high salt (2 mol/L NaCl), sugars (1 mol/L galactose, 1 mol/L mannose), glycosaminoglycans (10 mmol/L heparin, 10 mmol/L dermatan sulfate), or epsilon-aminocaproic acid (0.1 mol/L).	Heparin	153-160	serpin family E member 1	Bos taurus	4-9
3134174-5	1988	Plasma DAO activity increased significantly, compared with basal values, 30 minutes after 3000 units of heparin in both volunteers (26.2 +/- 5.0 vs. 4.5 +/- 0.5 units/ml) and patients with Crohn"s disease (14.6 +/- 2.0 vs. 4.0 +/- 1.1 units/ml, P less than .05) and was significantly greater in the volunteers.	Heparin	104-111	amine oxidase copper containing 1	Homo sapiens	7-10
3611087-12	1987	Lipoprotein lipase released heparin, in contrast, was fully active and more stable.	Heparin	28-35	lipoprotein lipase	Bos taurus	0-18
3134174-7	1988	Plasma DAO activity increased significantly within 15 minutes after 3000 units of heparin and remained at this high level at 60 minutes.	Heparin	82-89	amine oxidase copper containing 1	Homo sapiens	7-10
3584394-2	1987	The activity of lipoprotein lipase (LPL), the enzyme responsible for HDL cholesterol production, and the activity of hepatic triglyceride lipase (HTGL), the enzyme that facilitates the catabolism of HDL, were measured in plasma obtained after iv injection of heparin.	Heparin	259-266	lipase C, hepatic type	Homo sapiens	146-150
3032574-5	1987	Exposure to PTH and, to a lesser extent, 1,25-dihydroxyvitamin D3, prostaglandin E2, retinoic acid, and epidermal growth factor stimulated the release of collagenase, an effect not seen with interleukin-1 or heparin.	Heparin	208-215	epidermal growth factor like 1	Rattus norvegicus	104-127
3032991-8	1987	Heparin blocked the binding of bFGF to the receptor but had only a small inhibitory effect on the binding of aFGF to the receptor.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	31-35
3032991-9	1987	Thus, it appears that heparin inhibition of the neurotropic effects of bFGF occurs, at least in part, by impairing the interaction of bFGF with the receptor, while having little effect on that of aFGF.	Heparin	22-29	fibroblast growth factor 2	Rattus norvegicus	71-75
3032991-9	1987	Thus, it appears that heparin inhibition of the neurotropic effects of bFGF occurs, at least in part, by impairing the interaction of bFGF with the receptor, while having little effect on that of aFGF.	Heparin	22-29	fibroblast growth factor 2	Rattus norvegicus	134-138
3032991-10	1987	The stimulatory effects of heparin on the neurotropic activity of aFGF, bFGF, and NGF may occur through a site not associated with the respective cellular receptor for the growth factors.	Heparin	27-34	fibroblast growth factor 2	Rattus norvegicus	72-76
3576117-0	1987	Plasma kinetics of lipoprotein lipase and hepatic lipase activities induced by heparin and a low molecular weight heparin fragment.	Heparin	79-86	lipase C, hepatic type	Homo sapiens	42-56
3576117-0	1987	Plasma kinetics of lipoprotein lipase and hepatic lipase activities induced by heparin and a low molecular weight heparin fragment.	Heparin	114-121	lipase C, hepatic type	Homo sapiens	42-56
3576117-5	1987	The peak values and the plasma half-life of HL activity were the same for heparin and LMWH in the clinically relevant doses (50 and 100 U (antiFXa)/kg).	Heparin	74-81	lipase C, hepatic type	Homo sapiens	44-46
3576117-5	1987	The peak values and the plasma half-life of HL activity were the same for heparin and LMWH in the clinically relevant doses (50 and 100 U (antiFXa)/kg).	Heparin	86-90	lipase C, hepatic type	Homo sapiens	44-46
3100530-2	1987	The LDL receptor kinase shared several properties with casein kinase II: use of either GTP or ATP; phosphorylation of a typical casein kinase II recognition sequence in the LDL receptor (a serine followed by a cluster of three negatively charged amino acids); and inhibition by heparin.	Heparin	278-285	low density lipoprotein receptor	Bos taurus	4-16
3814169-0	1987	The anticoagulant, hepatic lipase-releasing and lipoprotein lipase-releasing activities of several natural and chemically modified heparins differ.	Heparin	131-139	lipase C, hepatic type	Homo sapiens	19-33
3814169-1	1987	Several "natural" heparins have been found to have different potencies for releasing hepatic lipase and lipoprotein lipase.	Heparin	18-26	lipase C, hepatic type	Homo sapiens	85-99
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Heparin	26-33	serpin family D member 1	Homo sapiens	47-51
3028582-4	1987	The present study showed that thrombin bound to acidic thrombomodulin was inactivated at a lower rate by antithrombin in the presence of exogenous heparin than was free thrombin or thrombin bound to the non-acidic form of thrombomodulin.	Heparin	147-154	thrombomodulin	Oryctolagus cuniculus	55-69
3028582-5	1987	The data suggest that the acidic component of thrombomodulin is primarily responsible for the retardation of thrombin-antithrombin complex formation in the presence of exogenous heparin.	Heparin	178-185	thrombomodulin	Oryctolagus cuniculus	46-60
3028582-6	1987	It is proposed that the polyanionic component of thrombomodulin blocks a site on thrombin required for heparin binding, thus rendering the antithrombin-heparin complex ineffective.	Heparin	103-110	thrombomodulin	Oryctolagus cuniculus	49-63
2448211-3	1987	Intravenous heparin injection displaces PF 4 from vessels wall.	Heparin	12-19	platelet factor 4	Homo sapiens	40-44
2442111-4	1987	The inhibitory effect was dependent on the sulfate content of the reagents used but independent of their anticoagulant activity as heparin preparations with high and low affinity for antithrombin III inhibited IC binding to E-CR1 to approximately the same extent.	Heparin	131-138	complement C3b/C4b receptor 1 (Knops blood group)	Homo sapiens	226-229
2442111-10	1987	Heparin induced IC-release was rapid (40-45% after 3 min) and incubation beyond 30 min caused only an insignificant further release of IC from E-CR1.	Heparin	0-7	complement C3b/C4b receptor 1 (Knops blood group)	Homo sapiens	145-148
2837726-7	1987	In doses where the lipoprotein lipase activities released by the 2 heparins were similar, the hepatic lipase released with low molecular weight heparin was significantly higher than with standard heparin.	Heparin	144-151	lipase C, hepatic type	Homo sapiens	94-108
3559389-3	1986	LPL activation was achieved by the infusion of normal plasma containing apoC-II and HL was released by the injection of heparin.	Heparin	120-127	lipase C, hepatic type	Homo sapiens	84-86
3769936-1	1986	Two forms of acidic fibroblast growth factor were isolated from bovine brain by a combination of ammonium sulfate precipitation, cation-exchange chromatography, heparin-Sepharose affinity chromatography, and reverse-phase high-performance liquid chromatography.	Heparin	161-168	fibroblast growth factor 1	Bos taurus	13-44
3760032-9	1986	Rather, our data suggest that heparin is slowly internalized by SMC following binding to specific, non-PF4 dissociable sites.	Heparin	30-37	platelet factor 4	Homo sapiens	103-106
3016729-10	1986	We propose that these activities as well as the negative charge and the higher buoyant density of the acidic, Mr 68,000 form of thrombomodulin are due to a heparin-like polysaccharide and, further, that this component can be separated from the major portion of the molecule, which contains the protein C activation site, through the action of a proteinase.	Heparin	156-163	thrombomodulin	Oryctolagus cuniculus	128-142
2943315-1	1986	The amidolytic plasmin activity of a mixture of tissue plasminogen activator (tPA) and plasminogen is enhanced by heparin at therapeutic concentrations.	Heparin	114-121	plasminogen	Homo sapiens	15-22
2943315-2	1986	Heparin also increases the activity in mixtures of urokinase-type plasminogen activator (uPA) and plasminogen but has no effect on streptokinase or plasmin.	Heparin	0-7	plasminogen	Homo sapiens	66-73
2943315-6	1986	The ability of heparin to promote plasmin generation is destroyed by incubation of the heparin with heparinase, whereas incubation with chondroitinase ABC or AC has no effect.	Heparin	15-22	plasminogen	Homo sapiens	34-41
2943315-6	1986	The ability of heparin to promote plasmin generation is destroyed by incubation of the heparin with heparinase, whereas incubation with chondroitinase ABC or AC has no effect.	Heparin	87-94	plasminogen	Homo sapiens	34-41
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Heparin	88-95	serpin family D member 1	Homo sapiens	0-19
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Heparin	88-95	serpin family D member 1	Homo sapiens	21-25
2870916-3	1986	In contrast, GH response to 50 ng GHRF/100 g body weight in lipid heparin-treated rats, which showed high plasma FFA levels, was significantly suppressed compared with the control group (plasma peak GH: control, 1526 +/- 263 ng/ml; lipid-heparin group, 377 +/- 69 ng/ml P less than 0.05, mean +/- SEM).	Heparin	66-73	growth hormone releasing hormone	Rattus norvegicus	34-38
2870916-3	1986	In contrast, GH response to 50 ng GHRF/100 g body weight in lipid heparin-treated rats, which showed high plasma FFA levels, was significantly suppressed compared with the control group (plasma peak GH: control, 1526 +/- 263 ng/ml; lipid-heparin group, 377 +/- 69 ng/ml P less than 0.05, mean +/- SEM).	Heparin	238-245	growth hormone releasing hormone	Rattus norvegicus	34-38
3747493-7	1986	Twenty units of heparin given subcutaneously daily for 5 days improved the survival rate to 66.7% following CLPS (P less than 0.05).	Heparin	16-23	colipase	Rattus norvegicus	108-112
3747493-11	1986	In comparing FN levels, no significant differences were found between the groups except on the second day--the CLPS + heparin group had a significantly lower FN level on Day 2 than CLP +/- heparin.	Heparin	189-196	colipase	Rattus norvegicus	111-115
3707569-4	1986	Further purification of Cibacron blue purified EDGF with heparin sepharose chromatography yielded two active fractions after elution with a sodium chloride gradient.	Heparin	57-64	fibroblast growth factor 1	Bos taurus	47-51
3458207-2	1986	The hepatoma-derived growth factor (HDGF) has been purified to homogeneity by a combination of Bio-Rex 70, heparin-Sepharose, and reverse-phase chromatography; it is a cationic polypeptide with a molecular weight of about 18,500-19,000.	Heparin	107-114	heparin binding growth factor	Homo sapiens	4-34
3458207-2	1986	The hepatoma-derived growth factor (HDGF) has been purified to homogeneity by a combination of Bio-Rex 70, heparin-Sepharose, and reverse-phase chromatography; it is a cationic polypeptide with a molecular weight of about 18,500-19,000.	Heparin	107-114	heparin binding growth factor	Homo sapiens	36-40
3518132-3	1986	QAE-Sephadex A-50 chromatography provides a good separation of HCII from antithrombin III (AT) and most contaminants having a heparin affinity similar to that of HCII.	Heparin	126-133	serpin family D member 1	Homo sapiens	63-67
3518132-4	1986	HCII is eluted at 0.28 M NaCl from the heparin-Sepharose column.	Heparin	39-46	serpin family D member 1	Homo sapiens	0-4
3006413-2	1986	Heparin-treated rats had low plasma aldosterone levels, high plasma renin activity and plasma AII levels, and normal plasma corticosterone level 6 weeks after the treatment (1500 IU/kg, twice daily).	Heparin	0-7	renin	Rattus norvegicus	68-73
3779055-2	1986	The adsorption isotherms of heparin onto normal and neuraminidase-treated RBC surfaces were determined by radioactive heparin labeled with 125I-Bolton-Hunter Reagent.	Heparin	28-35	neuraminidase 1	Homo sapiens	52-65
3096631-3	1986	Heparin reduced or abolished the inhibition of lipoprotein lipase by plasma, serum and purified vitellogenin.	Heparin	0-7	lipoprotein lipase	Gallus gallus	47-65
3096631-4	1986	The results suggest that inhibition of lipoprotein lipase by vitellogenin requires the presence of charged phosphate groups on vitellogenin and an unoccupied heparin-binding site on the enzyme.	Heparin	158-165	lipoprotein lipase	Gallus gallus	39-57
3009990-11	1986	By application of the newly found property of the mineralcorticoid receptor, an overall 10-fold purified, CBG-free preparation of this receptor can be obtained from kidney cytosol with a single chromatography on Sepharose-heparin.	Heparin	222-229	serpin family A member 6	Rattus norvegicus	106-109
2939551-8	1986	Heparin also exerted a marked, dose-dependent inhibitory effect on the binding of presolubilized IC to RBC-CR1, whereas the binding was unaffected by the addition of monosaccharides or by the concentration of Ca2+ or Mg2+ ions.	Heparin	0-7	complement C3b/C4b receptor 1 (Knops blood group)	Homo sapiens	107-110
2416361-1	1985	The observation that pregnancy-associated plasma protein A (PAPP-A) concentrations are higher in plasma compared to serum obtained from the same patient, together with fact that PAPP-A binds to heparin, prompted us to study the interaction between PAPP-A and the clotting system.	Heparin	194-201	pappalysin 1	Homo sapiens	178-184
2416361-1	1985	The observation that pregnancy-associated plasma protein A (PAPP-A) concentrations are higher in plasma compared to serum obtained from the same patient, together with fact that PAPP-A binds to heparin, prompted us to study the interaction between PAPP-A and the clotting system.	Heparin	194-201	pappalysin 1	Homo sapiens	178-184
3866952-6	1985	Electrostatic repulsion of the negative heparin molecule through the increased negativity of the malignant cell is discussed as an explanation of this finding which can be corrected/inhibited by neuraminidase incubation.	Heparin	40-47	neuraminidase 1	Homo sapiens	195-208
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	115-122	serpin family D member 1	Homo sapiens	0-19
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	115-122	serpin family D member 1	Homo sapiens	21-25
4041618-4	1985	Addition of Polybrene to the assay permits determination of HCII activity in samples containing less than or equal to 12 U/mL of heparin.	Heparin	129-136	serpin family D member 1	Homo sapiens	60-64
3840916-2	1985	HC II was functionally determined by thrombin inhibition in the presence of heparin in AT III-free plasma prepared by immunoadsorption on anti-AT III-Sepharose 4B column.	Heparin	76-83	serpin family D member 1	Homo sapiens	0-5
4035366-6	1985	Finally, we have shown that heparin alone promotes thromboxane production and PF4 release in a whole blood system.	Heparin	28-35	platelet factor 4	Homo sapiens	78-81
3970943-6	1985	In these circumstances the lipoprotein lipase-apolipoprotein C-II interaction is much tighter (Kd = (7-10) X 10(-9) M) and is insensitive to salt and heparin.	Heparin	150-157	apolipoprotein C2	Homo sapiens	46-65
2410403-0	1985	Effects of heparin and polyamines on the phosphorylation of high mobility group proteins by cyclic nucleotide-independent phosvitin kinase from pig testis.	Heparin	11-18	casein kinase II subunit beta	Sus scrofa	122-131
2410403-2	1985	The enzyme was shown to be inhibited by heparin, nd the inhibition was removed by the addition of polyamines, when phosvitin (the best exogenous substrate for the enzyme) was used as substrate.	Heparin	40-47	casein kinase II subunit beta	Sus scrofa	115-124
4005311-7	1985	Cibacron Blue purified EDGF was also further fractionated by heparin sepharose.	Heparin	61-68	fibroblast growth factor 1	Bos taurus	23-27
3989070-9	1985	When heparin was added to milk the LPL activity associated with the fat increased substantially; again, this effect was greater in afternoon milk from late lactation than in morning milk from early lactation.	Heparin	5-12	lipoprotein lipase	Bos taurus	35-38
2581862-1	1985	When heparin is injected intravenously, it can induce an immediate release of platelet factor 4 PF4), probably from the non-platelet pool of endothelial cells.	Heparin	5-12	platelet factor 4	Homo sapiens	96-99
2581862-5	1985	Only three cardiovascular patients had an elevated level of PF4 released by heparin (HR-PF4) that could be the expression of an increased platelet turnover, whereas all the patients with thrombocytosis had an extremely elevated level of HR-PF4.	Heparin	76-83	platelet factor 4	Homo sapiens	60-63
2581862-5	1985	Only three cardiovascular patients had an elevated level of PF4 released by heparin (HR-PF4) that could be the expression of an increased platelet turnover, whereas all the patients with thrombocytosis had an extremely elevated level of HR-PF4.	Heparin	76-83	platelet factor 4	Homo sapiens	88-91
2961064-6	1987	However, PF4 was found to be an even more potent inhibitor, approximating unfractionated heparin in this respect.	Heparin	89-96	platelet factor 4	Homo sapiens	9-12
3585139-1	1987	Human hepatic triglyceride lipase (HTGL), purified from plasma obtained after heparin injection, markedly enhanced the anti-Xa clotting activity of normal plasma.	Heparin	78-85	lipase C, hepatic type	Homo sapiens	6-33
3585139-1	1987	Human hepatic triglyceride lipase (HTGL), purified from plasma obtained after heparin injection, markedly enhanced the anti-Xa clotting activity of normal plasma.	Heparin	78-85	lipase C, hepatic type	Homo sapiens	35-39
3585139-4	1987	Heparin, and low-affinity heparin, reduced the anti-Xa activity of HTGL, suggesting that heparin and factor Xa compete for the same binding sites on the lipase molecule.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	67-71
3585139-4	1987	Heparin, and low-affinity heparin, reduced the anti-Xa activity of HTGL, suggesting that heparin and factor Xa compete for the same binding sites on the lipase molecule.	Heparin	26-33	lipase C, hepatic type	Homo sapiens	67-71
3585139-5	1987	These results suggest that at least part of the enhanced anti-Xa clotting activity observed after injection of heparin and heparin analogues is caused by the release of HTGL.	Heparin	111-118	lipase C, hepatic type	Homo sapiens	169-173
3585139-5	1987	These results suggest that at least part of the enhanced anti-Xa clotting activity observed after injection of heparin and heparin analogues is caused by the release of HTGL.	Heparin	123-130	lipase C, hepatic type	Homo sapiens	169-173
3576117-6	1987	Compared with LMWH, the total release of HL was twice as large after the heparin injections, possibly due to mobilization of an additional enzyme pool by the conventional heparin.	Heparin	171-178	lipase C, hepatic type	Homo sapiens	41-43
3590116-1	1987	To determine the interaction of platelet factor 4 (PF4) and protamine sulfate in the neutralization of heparin in plasma in vitro studies were carried out using a tritium-labeled heparin and a PF4 tagged with 14C.	Heparin	103-110	platelet factor 4	Homo sapiens	51-54
3590116-3	1987	PF4 was comparable to protamine in its ability to neutralize heparin, but the complexes formed with heparin were different.	Heparin	61-68	platelet factor 4	Homo sapiens	0-3
3590116-3	1987	PF4 was comparable to protamine in its ability to neutralize heparin, but the complexes formed with heparin were different.	Heparin	100-107	platelet factor 4	Homo sapiens	0-3
3590116-4	1987	In contrast to protamine, when heparinized plasma was treated with an excess of PF4, no large PF4-heparin complexes were formed and none of the PF4-heparin complexes which did form were able to activate antithrombin III (ATIII).	Heparin	31-38	platelet factor 4	Homo sapiens	80-83
3566288-0	1987	The kinetics of heparin inhibition of the esterase and basal lipase activities of lipoprotein lipase.	Heparin	16-23	lipoprotein lipase	Bos taurus	82-100
3566288-5	1987	On the other hand, the basal lipase activity of LPL against emulsified trioleoylglycerol (TG) was very sensitive to inhibition by heparin: 1 microgram/ml inhibited about 80% of the reaction and 3 micrograms/ml drove the reaction to zero.	Heparin	130-137	lipoprotein lipase	Bos taurus	48-51
3566288-13	1987	It is concluded that TG and heparin as well as C-II and heparin are mutually exclusive and that lipoprotein lipase is a multisite enzyme, possibly a tetramer, with three high-affinity catalytic sites, and an equal number of sites for C-II and heparin per oligomer.	Heparin	28-35	lipoprotein lipase	Bos taurus	96-114
3102190-1	1987	Diamine oxidase (DAO) is an enzyme whose low plasma values are enhanced by an intravenous injection of heparin, which releases the enzyme from the enterocytes of the villous tips.	Heparin	103-110	amine oxidase copper containing 1	Homo sapiens	0-15
3102190-1	1987	Diamine oxidase (DAO) is an enzyme whose low plasma values are enhanced by an intravenous injection of heparin, which releases the enzyme from the enterocytes of the villous tips.	Heparin	103-110	amine oxidase copper containing 1	Homo sapiens	17-20
3028582-6	1987	It is proposed that the polyanionic component of thrombomodulin blocks a site on thrombin required for heparin binding, thus rendering the antithrombin-heparin complex ineffective.	Heparin	152-159	thrombomodulin	Oryctolagus cuniculus	49-63
2438194-8	1987	All PAPP-A species interacted reversibly with immobilised heparin and were determined by molecular sieve chromatography to have an apparent molecular weight of 820,000 daltons.	Heparin	58-65	pappalysin 1	Homo sapiens	4-10
2436331-2	1986	Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively.	Heparin	0-7	serpin family D member 1	Homo sapiens	114-119
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Heparin	32-39	serpin family D member 1	Homo sapiens	152-157
3766757-2	1986	Heparin resulted in a single-compartment disappearance of 125I-labeled PF4 (half-life = 25-40 min).	Heparin	0-7	platelet factor 4	Homo sapiens	71-74
3766757-9	1986	Simultaneous or subsequent injection of heparin did not affect the distribution of 131I-labeled beta-TG but caused partial loss of 131I-labeled PF4 radioactivity from the liver and accelerated its appearance in the urinary bladder.	Heparin	40-47	platelet factor 4	Homo sapiens	144-147
2431400-0	1986	The lung lysosomal hydrolases and phospholipase A in acute experimental pancreatitis with reference to heparin treatment.	Heparin	103-110	phospholipase A and acyltransferase 1	Rattus norvegicus	34-49
2431400-8	1986	Heparin prevented the increase of activity of B-glucuronidase, depressed the relative free activity of all investigated lysosomal hydrolases and inhibited the phospholipase A activity in the lung homogenate.	Heparin	0-7	phospholipase A and acyltransferase 1	Rattus norvegicus	159-174
2581862-5	1985	Only three cardiovascular patients had an elevated level of PF4 released by heparin (HR-PF4) that could be the expression of an increased platelet turnover, whereas all the patients with thrombocytosis had an extremely elevated level of HR-PF4.	Heparin	76-83	platelet factor 4	Homo sapiens	88-91
6084876-6	1984	Heparin, dextran sulfate and chondroitin polysulfates 1 and 5 activated both HC II and AT III, while dermatan sulfate activated only HC II.	Heparin	0-7	serpin family D member 1	Homo sapiens	77-82
6598053-4	1984	Hepatic lipase and lipoprotein lipase activities were measured selectively in post-heparin plasma from all 18 patients using a substrate-specific method.	Heparin	83-90	lipase C, hepatic type	Homo sapiens	0-14
3134174-10	1988	Plasma DAO activity, 30 minutes after the intravenous administration of 3000 units of heparin, should reflect intestinal involvement in Crohn"s disease.	Heparin	86-93	amine oxidase copper containing 1	Homo sapiens	7-10
6393024-4	1984	After the heparin bolus and during the exchange transfusion, lipoprotein and hepatic lipase activities in group 1 were higher than in term infants.	Heparin	10-17	lipase C, hepatic type	Homo sapiens	77-91
2945283-0	1986	Stimulation by heparin of the plasmin-mediated conversion of single-chain to two-chain urokinase-type plasminogen activator.	Heparin	15-22	plasminogen	Homo sapiens	30-37
2844223-9	1988	Addition of heparin potentiated the inhibition of APC [(1.2 +/- 0.2) X 10(4) M-1 s-1] and factor XIa [(9.1 +/- 0.7) X 10(4) M-1 s-1] by PCI, whereas the inhibition of kallikrein by PCI was unchanged [(10 +/- 1) X 10(4) M-1 s-1].	Heparin	12-19	APC regulator of WNT signaling pathway	Homo sapiens	50-53
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Heparin	115-122	serpin family D member 1	Homo sapiens	0-4
2844223-9	1988	Addition of heparin potentiated the inhibition of APC [(1.2 +/- 0.2) X 10(4) M-1 s-1] and factor XIa [(9.1 +/- 0.7) X 10(4) M-1 s-1] by PCI, whereas the inhibition of kallikrein by PCI was unchanged [(10 +/- 1) X 10(4) M-1 s-1].	Heparin	12-19	serpin family A member 5	Homo sapiens	136-139
2844223-9	1988	Addition of heparin potentiated the inhibition of APC [(1.2 +/- 0.2) X 10(4) M-1 s-1] and factor XIa [(9.1 +/- 0.7) X 10(4) M-1 s-1] by PCI, whereas the inhibition of kallikrein by PCI was unchanged [(10 +/- 1) X 10(4) M-1 s-1].	Heparin	12-19	serpin family A member 5	Homo sapiens	181-184
6382607-0	1984	Heparin binds endothelial cell growth factor, the principal endothelial cell mitogen in bovine brain.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	14-44
3458170-2	1986	Radioimmunoassay, using monoclonal antibodies, of fractions from the heparin-Sepharose chromatography showed one peak of EDN activity and two peaks of ECP activity (termed ECP-1 and ECP-2).	Heparin	69-76	ribonuclease A family member 2	Homo sapiens	121-124
3470171-4	1986	The phosphorylation of nuclear proteins and phosvitin is heparin-sensitive, indicating that they are phosphorylated by casein kinase NII.	Heparin	57-64	casein kinase 2 beta	Homo sapiens	44-53
6382607-1	1984	Endothelial cell growth factor (ECGF), an anionic polypeptide mitogen, binds to immobilized heparin.	Heparin	92-99	fibroblast growth factor 1	Bos taurus	0-30
6382607-1	1984	Endothelial cell growth factor (ECGF), an anionic polypeptide mitogen, binds to immobilized heparin.	Heparin	92-99	fibroblast growth factor 1	Bos taurus	32-36
6382607-4	1984	These data indicate that ECGF is the principal mitogen for endothelial cells from bovine brain, that heparin affinity chromatography may be used to purify and concentrate ECGF, and that the affinity of ECGF for heparin may have structural and perhaps biological significance.	Heparin	211-218	fibroblast growth factor 1	Bos taurus	25-29
6466700-0	1984	Post-heparin plasma hepatic triacylglycerol lipase-catalyzed tributyrin hydrolysis.	Heparin	5-12	lipase C, hepatic type	Homo sapiens	20-50
2836066-2	1988	The trans-acting factors were purified from mouse myeloma NS1 cells, and HIG1-inducing activity was found mainly in fractions of molecular weight 53-127 kd and in a fraction eluted from a heparin-Sepharose column with 0.5 M KCI.	Heparin	188-195	HIG1 domain family, member 1A	Mus musculus	73-77
6743573-3	1984	The results demonstrate that purified PF4 neutralizes heparin activity when added in increasing amounts to normal platelet-poor plasma containing a fixed concentration of commercial porcine gut mucosal heparin.	Heparin	54-61	platelet factor 4	Homo sapiens	38-41
6743573-3	1984	The results demonstrate that purified PF4 neutralizes heparin activity when added in increasing amounts to normal platelet-poor plasma containing a fixed concentration of commercial porcine gut mucosal heparin.	Heparin	202-209	platelet factor 4	Homo sapiens	38-41
6743573-7	1984	These data confirm that both purified and secreted PF4 have significant antiheparin activity when heparin is added in vitro to normal plasma.	Heparin	76-83	platelet factor 4	Homo sapiens	51-54
6743573-8	1984	Neutralization of circulating heparin by PF4 secreted during blood collection from anticoagulated patients could result in underestimation of the actual in vivo heparin concentration.	Heparin	30-37	platelet factor 4	Homo sapiens	41-44
6743573-8	1984	Neutralization of circulating heparin by PF4 secreted during blood collection from anticoagulated patients could result in underestimation of the actual in vivo heparin concentration.	Heparin	161-168	platelet factor 4	Homo sapiens	41-44
6743573-13	1984	There was a significant difference between heparin activities measured in the CIT+ (secreted PF4 58 ng/ml) and CIT60 (secreted PF4 1074 ng/ml) plasma samples by both thrombin time and Xa inactivation.	Heparin	43-50	platelet factor 4	Homo sapiens	93-96
3098500-5	1986	The development of new technologies to better recover FVIII allows reduction of the pool size: crush-thaw, controlled pore-glass chromatography, and heparin double-cold precipitation techniques.	Heparin	149-156	coagulation factor VIII	Homo sapiens	54-59
3009990-1	1986	Interaction with heparin and purification to a CBG-free stage.	Heparin	17-24	serpin family A member 6	Rattus norvegicus	47-50
3009990-7	1986	We show that when kidney cytosol is incubated with heparin covalently linked to Sepharose (Sepharose-heparin), after 30 min at 0 degrees C more than 80% of the mineralcorticoid-specific binding sites interact strongly with Sepharose-heparin while CBG is not bound at all.	Heparin	51-58	serpin family A member 6	Rattus norvegicus	247-250
3009990-7	1986	We show that when kidney cytosol is incubated with heparin covalently linked to Sepharose (Sepharose-heparin), after 30 min at 0 degrees C more than 80% of the mineralcorticoid-specific binding sites interact strongly with Sepharose-heparin while CBG is not bound at all.	Heparin	101-108	serpin family A member 6	Rattus norvegicus	247-250
3009990-7	1986	We show that when kidney cytosol is incubated with heparin covalently linked to Sepharose (Sepharose-heparin), after 30 min at 0 degrees C more than 80% of the mineralcorticoid-specific binding sites interact strongly with Sepharose-heparin while CBG is not bound at all.	Heparin	101-108	serpin family A member 6	Rattus norvegicus	247-250
2417623-11	1985	Cathepsin D digestion produced an 83K heparin-binding, monoclonal antibody reactive fragment that contains the interchain disulfide bond(s) linking the two fibronectin chains at their C-termini.	Heparin	38-45	cathepsin D	Homo sapiens	0-11
3172990-2	1988	This analog of the natural substrate, 1(3)pyrene decanoic-2,3 (1,2)-dioleoyl-sn-glycerol, has been tested as substrate for determining lipoprotein lipase and hepatic triacylglycerol lipase activities in post-heparin plasma.	Heparin	208-215	lipase C, hepatic type	Homo sapiens	158-188
3841420-4	1985	The biological activity of the HC II was unchanged after labelling as was its migratory pattern by crossed immunoelectrophoresis in the presence of heparin or dermatan sulfate.	Heparin	148-155	serpin family D member 1	Homo sapiens	31-36
6539779-6	1984	p75 kinase activity, as well as viral tyrosine protein kinase activity, is stimulated by heparin.	Heparin	89-96	nerve growth factor receptor	Rattus norvegicus	0-3
2451918-1	1988	Heparin inhibits proteolytic digestion of heparin-binding growth factor-I (HBGF-I) by trypsin, plasmin and other proteases.	Heparin	0-7	plasminogen	Homo sapiens	95-102
6713636-0	1984	Sensitive non-radioisotopic method for measuring lipoprotein lipase and hepatic triglyceride lipase in post-heparin plasma.	Heparin	108-115	lipase C, hepatic type	Homo sapiens	72-99
6713636-1	1984	In this method for measuring lipoprotein lipase (LPL) and hepatic triglyceride lipase (H-TGL) in post-heparin plasma, we determine the released free fatty acids enzymically.	Heparin	102-109	lipase C, hepatic type	Homo sapiens	58-85
6713636-1	1984	In this method for measuring lipoprotein lipase (LPL) and hepatic triglyceride lipase (H-TGL) in post-heparin plasma, we determine the released free fatty acids enzymically.	Heparin	102-109	lipase C, hepatic type	Homo sapiens	87-92
6713636-5	1984	A 5-microL sample of post-heparin plasma suffices to measure the activity of LPL and H-TGL; thus the method is as sensitive as the radioisotopic method.	Heparin	26-33	lipase C, hepatic type	Homo sapiens	85-90
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Heparin	13-20	serpin family D member 1	Homo sapiens	34-38
3900060-2	1985	Endothelial cell growth factor (ECGF) can be rapidly purified from bovine brain to high specific activity using heparin-Sepharose affinity chromatography.	Heparin	112-119	fibroblast growth factor 1	Bos taurus	0-30
3900060-2	1985	Endothelial cell growth factor (ECGF) can be rapidly purified from bovine brain to high specific activity using heparin-Sepharose affinity chromatography.	Heparin	112-119	fibroblast growth factor 1	Bos taurus	32-36
3900060-5	1985	The two forms of ECGF can be separated by either NaCl gradient elution from heparin-Sepharose or reversed-phase high pressure liquid chromatography.	Heparin	76-83	fibroblast growth factor 1	Bos taurus	17-21
3382640-1	1988	Incubation of bovine brain derived acidic fibroblast growth factor (aFGF) with bovine or human thrombin, 0.5 NIH unit/mL, for 24 h at 37 degrees C results in cleavage of the mitogen, generating a 14-kilodalton fragment which has significantly reduced affinity for immobilized heparin as compared to aFGF, and is at least 50-fold less potent at stimulating mitogenesis.	Heparin	276-283	fibroblast growth factor 1	Bos taurus	35-66
3898072-0	1985	Heparin-treated, v-myc-transformed chicken heart mesenchymal cells assume a normal morphology but are hypersensitive to epidermal growth factor (EGF) and brain fibroblast growth factor (bFGF); cells transformed by the v-Ha-ras oncogene are refractory to EGF and bFGF but are hypersensitive to insulin-like growth factors.	Heparin	0-7	fibroblast growth factor 2	Gallus gallus	186-190
3898072-0	1985	Heparin-treated, v-myc-transformed chicken heart mesenchymal cells assume a normal morphology but are hypersensitive to epidermal growth factor (EGF) and brain fibroblast growth factor (bFGF); cells transformed by the v-Ha-ras oncogene are refractory to EGF and bFGF but are hypersensitive to insulin-like growth factors.	Heparin	0-7	fibroblast growth factor 2	Gallus gallus	262-266
3898072-6	1985	We hypothesize, therefore, (i) that heparin prevents the generation by cells of a mitogen from plasma protein precursors in the culture medium; (ii) that the v-myc oncogene renders cells hypersensitive to EGF, bFGF, PDGF, and the putative plasma-protein-derived mitogen; and (iii) that MC29-infected cells must proliferate in order to manifest the transformed morphology.	Heparin	36-43	fibroblast growth factor 2	Gallus gallus	210-214
2992605-4	1985	Casein kinase I, accounting for the whole casein kinase S activity of cytosol, also contains a phosphorylatable 31-kDa protein (p31) which is a substrate of casein kinase S, since its phosphorylation is insensitive to heparin, the heat-stable inhibitor and trifluoperazine, but it is prevented by beryllium.	Heparin	218-225	casein kinase 1, epsilon	Rattus norvegicus	0-15
2992605-4	1985	Casein kinase I, accounting for the whole casein kinase S activity of cytosol, also contains a phosphorylatable 31-kDa protein (p31) which is a substrate of casein kinase S, since its phosphorylation is insensitive to heparin, the heat-stable inhibitor and trifluoperazine, but it is prevented by beryllium.	Heparin	218-225	ATPase H+ transporting V1 subunit E1	Rattus norvegicus	128-131
6471667-4	1984	Hepatic lipase and lipoprotein lipase activities were selectively measured in post-heparin plasma in 59 patients.	Heparin	83-90	lipase C, hepatic type	Homo sapiens	0-14
6198333-3	1984	Further characterization showed that ovarian follicular PAPP-A bound reversibly to heparin-Sepharose.	Heparin	83-90	pappalysin 1	Homo sapiens	56-62
6202020-0	1984	Selective PF4 release in vitro induced by heparin and related glycosaminoglycans (GAGs)--correlation with beta-TG release and platelet aggregation.	Heparin	42-49	platelet factor 4	Homo sapiens	10-13
6202020-0	1984	Selective PF4 release in vitro induced by heparin and related glycosaminoglycans (GAGs)--correlation with beta-TG release and platelet aggregation.	Heparin	42-49	pro-platelet basic protein	Homo sapiens	106-113
6202020-1	1984	We studied human platelet aggregation and beta-TG/PF4 release induced by heparin and related GAGs in vitro both in normal PRP and in PRP after aspirin.	Heparin	73-80	pro-platelet basic protein	Homo sapiens	42-49
6202020-1	1984	We studied human platelet aggregation and beta-TG/PF4 release induced by heparin and related GAGs in vitro both in normal PRP and in PRP after aspirin.	Heparin	73-80	platelet factor 4	Homo sapiens	50-53
6202020-2	1984	In our experimental conditions, heparin and related GAGs always caused PF4 release in vitro from normal platelets, whether or not there was measurable platelet aggregation in the aggregometer.	Heparin	32-39	platelet factor 4	Homo sapiens	71-74
6202020-3	1984	Significant beta-TG release was induced only by the mucosal heparin preparation (which also induced platelet aggregation in some citrated PRP).	Heparin	60-67	pro-platelet basic protein	Homo sapiens	12-19
6202020-4	1984	Therefore, while beta-TG release in vitro seems to correlate with platelet aggregating activity of heparin, the selective PF4 release, caused by heparin and related GAGs also in conditions in which neither platelet aggregation nor beta-TG are measurable, is probably associated with the high affinity of PF4 for heparin.	Heparin	99-106	pro-platelet basic protein	Homo sapiens	17-24
6202020-4	1984	Therefore, while beta-TG release in vitro seems to correlate with platelet aggregating activity of heparin, the selective PF4 release, caused by heparin and related GAGs also in conditions in which neither platelet aggregation nor beta-TG are measurable, is probably associated with the high affinity of PF4 for heparin.	Heparin	145-152	platelet factor 4	Homo sapiens	122-125
6202020-4	1984	Therefore, while beta-TG release in vitro seems to correlate with platelet aggregating activity of heparin, the selective PF4 release, caused by heparin and related GAGs also in conditions in which neither platelet aggregation nor beta-TG are measurable, is probably associated with the high affinity of PF4 for heparin.	Heparin	145-152	platelet factor 4	Homo sapiens	122-125
6202020-5	1984	The degree of affinity of GAGs for PF4 (heparin greater than DeS greater than HS) seems to correlate with PF4 release.	Heparin	40-47	platelet factor 4	Homo sapiens	35-38
3382640-1	1988	Incubation of bovine brain derived acidic fibroblast growth factor (aFGF) with bovine or human thrombin, 0.5 NIH unit/mL, for 24 h at 37 degrees C results in cleavage of the mitogen, generating a 14-kilodalton fragment which has significantly reduced affinity for immobilized heparin as compared to aFGF, and is at least 50-fold less potent at stimulating mitogenesis.	Heparin	276-283	fibroblast growth factor 1	Bos taurus	68-72
6202020-5	1984	The degree of affinity of GAGs for PF4 (heparin greater than DeS greater than HS) seems to correlate with PF4 release.	Heparin	40-47	platelet factor 4	Homo sapiens	106-109
2931280-9	1985	Nevertheless, the activation of the clotting system seems to be predominant, as supported by the improved effect of heparin on beta TG and FPA amounts.	Heparin	116-123	pro-platelet basic protein	Homo sapiens	127-134
3382640-4	1988	The cleavage of aFGF by thrombin is inhibited by heparin (50 micrograms/mL) and is completely blocked by the irreversible thrombin inhibitors D-Phe-Pro-Arg chloromethyl ketone and hirudin.	Heparin	49-56	fibroblast growth factor 1	Bos taurus	16-20
3382640-7	1988	The results show that the C-terminal region of aFGF is of functional importance in both mitogenesis and heparin binding.	Heparin	104-111	fibroblast growth factor 1	Bos taurus	47-51
3342932-1	1988	Heparin or heparan sulfate proteoglycan (HeSPG), but not chondroitin sulfate or hyaluronic acid, exerts a pronounced inhibitory effect on muscle growth in vitro, as determined by total protein, myosin accumulation or synthesis, and [3H]thymidine incorporation studies.	Heparin	0-7	myosin, heavy chain 15	Gallus gallus	194-200
4065099-1	1985	Acidic fibroblast growth factor (FGF) from bovine brain has been isolated by a combination of salt precipitation, ion-exchange chromatography, heparin-Sepharose affinity chromatography and reverse phase h.p.l.c.	Heparin	143-150	fibroblast growth factor 1	Bos taurus	0-31
6420398-7	1984	Similar studies with O-sulfated heparin intermediates showed that O-sulfate groups either at C-2 of the L-iduronosyl moieties or at C-6 of vicinal D-glucosaminyl moieties prevent 5-epimerization.	Heparin	32-39	complement component 6	Mus musculus	132-135
3346544-2	1988	Purified MBP was studied for capacity to regulate the generation of classical and alternative-amplification pathway C3 convertases because previous studies have shown that other polycations (protamine, poly-L-lysine) and polyanions (heparin) may play important roles in regulating C activation.	Heparin	233-240	myelin basic protein	Homo sapiens	9-12
6469101-4	1984	We tested the use of pyridoxal 5"-phosphate (PLP) to prevent heparin neutralization.	Heparin	61-68	pyridoxal phosphatase	Homo sapiens	45-48
6469101-5	1984	As the use of PLP in the citrate tube decreased the heparin neutralization to a negligible effect, PLP-citrate tubes are to be preferred for all plasma heparin determinations.	Heparin	52-59	pyridoxal phosphatase	Homo sapiens	14-17
6363061-1	1983	Heparin is shown to produce modulatory effects on the amidolytic activity of trypsin, thrombin and plasmin with various synthetic peptide substrates.	Heparin	0-7	plasminogen	Homo sapiens	99-106
2986975-11	1985	Heparin, a potent inhibitor of casein kinase II, inhibits p68 activity too, but ten-times higher concentrations were required for the same degree of inhibition.	Heparin	0-7	GATA zinc finger domain containing 2B	Homo sapiens	58-61
3988735-3	1985	Both apo-C-II and apo-E produced enhanced lipolysis in comparison to unsupplemented emulsions, at appropriate enzyme densities on the heparin-Sepharose.	Heparin	134-141	apolipoprotein C2	Homo sapiens	5-13
3838315-5	1985	The thrombin-HCII complex was undetectable when 5 units/ml of heparin was present or when prothrombin-deficient plasma was used.	Heparin	62-69	serpin family D member 1	Homo sapiens	13-17
2987072-0	1985	Hepatic triglyceride lipase and lipoprotein lipase activities in post-heparin plasma of patients with various cancers.	Heparin	70-77	lipase C, hepatic type	Homo sapiens	0-27
2843005-2	1988	Heparin activates lipoprotein lipase (LPL) and hepatic lipase (HL), enhances plasma lipolytic activity and elevates plasma levels of free fatty acids (FFA).	Heparin	0-7	lipase C, hepatic type	Homo sapiens	47-61
2944347-0	1985	Glucocorticoid receptor is activated by heparin and deactivated by plasmin.	Heparin	40-47	nuclear receptor subfamily 3 group C member 1	Gallus gallus	0-23
2944347-1	1985	Chick thymus glucocorticoid receptor activation was followed in the presence of heparin and/or plasmin.	Heparin	80-87	nuclear receptor subfamily 3 group C member 1	Gallus gallus	13-36
2944348-5	1985	However, at high concentration of heparin, plasmin inactivation by antithrombin III is accelerated even in the presence of fibrinogen or fibrin.	Heparin	34-41	plasminogen	Homo sapiens	43-50
6141763-2	1983	The first kinase, present in greatest activity in microsomal extracts, appears to be identical to casein kinase I by characteristic molecular size on gel filtration (Mr 40,000) and sodium dodecyl sulfate-gel electrophoresis (Mr 34,000), autophosphorylation of this single subunit, inability to efficiently utilize GTP, and resistance to inhibition by heparin and 2,3-diphosphoglycerate.	Heparin	351-358	casein kinase 1, epsilon	Rattus norvegicus	98-113
2843005-2	1988	Heparin activates lipoprotein lipase (LPL) and hepatic lipase (HL), enhances plasma lipolytic activity and elevates plasma levels of free fatty acids (FFA).	Heparin	0-7	lipase C, hepatic type	Homo sapiens	63-65
2843005-8	1988	The immediate release of HL activity was the same for both heparins, the release of LPL activity was dose-dependent and the elimination followed first-order kinetics.	Heparin	59-67	lipase C, hepatic type	Homo sapiens	25-27
2411256-1	1985	Brain fucosyltransferase reaction (GDP-fucose: glycoprotein fucosyltransferase, EC 2.4.1.68) was found to be inhibited by heparin.	Heparin	122-129	fucosyltransferase 8	Homo sapiens	35-78
2462440-6	1988	Heparin, in combination with 0.1 mu/ml IL1, stimulated significant calcium release compared to heparin but not to IL1 tested alone.	Heparin	95-102	interleukin 1 complex	Mus musculus	39-42
6661357-1	1983	A low molecular weight heparin (MW 4000-6000), PK 10169 (Pharmuka), with much reduced anticoagulant in vitro capacity, retains the properties of the standard heparin in releasing lipoprotein lipase and hepatic lipase activity after being injected intravenously.	Heparin	23-30	lipase C, hepatic type	Homo sapiens	202-216
6197764-1	1983	Concentrations of immunoreactive PAPP-A have been found significantly lower in the serum as compared to heparin or EDTA plasma from the same patients.	Heparin	104-111	pappalysin 1	Homo sapiens	33-39
2936542-5	1985	Graphic comparison of these proteins suggests that a point mutation at position 55 (human PF-4 numbering) could cause a significant difference among the folding properties of these 3 proteins and might be critical for their different heparin binding properties.	Heparin	234-241	platelet factor 4	Homo sapiens	90-94
6197764-6	1983	The fact that protamine sulphate is capable of neutralizing the inhibitory effects of PAPP-A made us postulate that PAPP-A, like heparin, possesses strongly acidic residues which bind to protamine.	Heparin	129-136	pappalysin 1	Homo sapiens	116-122
2462440-8	1988	Two of the heparin fragments combined with 0.1 U/ml IL1 significantly inhibited calcium release compared to IL1 alone.	Heparin	11-18	interleukin 1 complex	Mus musculus	108-111
2462440-9	1988	In combination with 1.0 U/ml of IL1, heparin and hyaluronic acid inhibited calcium release compared to IL1 alone but this inhibition was not significant.	Heparin	37-44	interleukin 1 complex	Mus musculus	103-106
3144470-8	1988	Plasma DAO values assayed 1 h (T60) after the injection of 15,000 IU of heparin proved to be the best discriminator curve point and the use of the T60 point alone may be usefully employed instead of the area under the 120-min curve.	Heparin	72-79	amine oxidase copper containing 1	Homo sapiens	7-10
6888269-0	1983	Lipoprotein lipase and hepatic lipase activity after heparin administration in abetalipoproteinemia and hypobetalipoproteinemia.	Heparin	53-60	lipase C, hepatic type	Homo sapiens	23-37
6888269-4	1983	Hepatic lipase activity in plasma samples from these three patients obtained 15 minutes after intravenous injection of heparin was 55%, 87%, and 46% of that of the controls, whereas corresponding values in plasma samples obtained 30 minutes after heparin were 47%, 70%, and 57%, respectively.	Heparin	119-126	lipase C, hepatic type	Homo sapiens	0-14
6888269-6	1983	We conclude that an inherent absence of triglyceride-rich lipoproteins, as occurs in abetalipoproteinemia, is associated with reduced enzyme activity of both hepatic lipase and lipoprotein lipase in plasma after heparin administration.	Heparin	212-219	lipase C, hepatic type	Homo sapiens	158-172
4059181-1	1985	Lipoprotein lipase was purified to homogeneity from bovine skim milk by a two-step procedure using chromatography on heparin-Sepharose.	Heparin	117-124	lipoprotein lipase	Bos taurus	0-18
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipase C, hepatic type	Homo sapiens	184-198
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipase C, hepatic type	Homo sapiens	184-198
3123254-2	1987	The animals pretreated with heparin showed high initial PF4 levels with a subsequent slow monoexponential clearance.	Heparin	28-35	platelet factor 4	Homo sapiens	56-59
6440307-3	1984	Platelet factor 4 (PF4), protamine, and Polybrene inhibit heparin activity by neutralizing heparin negative charges.	Heparin	58-65	platelet factor 4	Homo sapiens	0-17
6440307-3	1984	Platelet factor 4 (PF4), protamine, and Polybrene inhibit heparin activity by neutralizing heparin negative charges.	Heparin	58-65	platelet factor 4	Homo sapiens	19-22
6440307-3	1984	Platelet factor 4 (PF4), protamine, and Polybrene inhibit heparin activity by neutralizing heparin negative charges.	Heparin	91-98	platelet factor 4	Homo sapiens	0-17
6440307-3	1984	Platelet factor 4 (PF4), protamine, and Polybrene inhibit heparin activity by neutralizing heparin negative charges.	Heparin	91-98	platelet factor 4	Homo sapiens	19-22
6084323-5	1984	Under these circumstances plasma beta TG, but not PF4 or TSP, levels are elevated because of impaired renal catabolism, and the presence of a heparin-releasable reservoir of PF4 on the endothelium complicates the use of the PF4 assay.	Heparin	142-149	platelet factor 4	Homo sapiens	174-177
6084323-5	1984	Under these circumstances plasma beta TG, but not PF4 or TSP, levels are elevated because of impaired renal catabolism, and the presence of a heparin-releasable reservoir of PF4 on the endothelium complicates the use of the PF4 assay.	Heparin	142-149	platelet factor 4	Homo sapiens	174-177
6240116-7	1984	Administration of heparin results in a heparin-induced increase in plasma PF4 levels but not for BTG, and this PF4 increase can be as great as 20-fold.	Heparin	18-25	platelet factor 4	Homo sapiens	74-77
6240116-7	1984	Administration of heparin results in a heparin-induced increase in plasma PF4 levels but not for BTG, and this PF4 increase can be as great as 20-fold.	Heparin	18-25	platelet factor 4	Homo sapiens	111-114
6240116-7	1984	Administration of heparin results in a heparin-induced increase in plasma PF4 levels but not for BTG, and this PF4 increase can be as great as 20-fold.	Heparin	39-46	platelet factor 4	Homo sapiens	74-77
6240116-7	1984	Administration of heparin results in a heparin-induced increase in plasma PF4 levels but not for BTG, and this PF4 increase can be as great as 20-fold.	Heparin	39-46	platelet factor 4	Homo sapiens	111-114
6415848-5	1983	The VIII:CAg amount detected in the internal volume increased following the series heparin less than citrate less than EDTA.	Heparin	83-90	cytochrome c oxidase subunit 8A	Homo sapiens	4-8
6408108-6	1983	Measurement of lipoprotein lipase and hepatic lipase enzymic activity in post-heparin plasma revealed no major change in lipoprotein lipase activity, but showed a significant decrease (43.8%) in hepatic lipase activity during estrogen administration.	Heparin	78-85	lipase C, hepatic type	Homo sapiens	38-52
6408108-6	1983	Measurement of lipoprotein lipase and hepatic lipase enzymic activity in post-heparin plasma revealed no major change in lipoprotein lipase activity, but showed a significant decrease (43.8%) in hepatic lipase activity during estrogen administration.	Heparin	78-85	lipase C, hepatic type	Homo sapiens	195-209
6687888-2	1983	Heparin, dermatan sulfate, and heparan sulfate from bovine liver (in order of decreasing activity) activated HCII.	Heparin	0-7	serpin family D member 1	Homo sapiens	109-113
6495255-4	1984	Intravenous heparin liberates large amounts of PF4 from an unknown reservoir, perhaps the endothelium, into the plasma.	Heparin	12-19	platelet factor 4	Homo sapiens	47-50
3123254-4	1987	Protamine, at dosages that totally neutralized 1000 USP units of heparin pretreatment, caused an immediate disappearance in the circulating PF4.	Heparin	65-72	platelet factor 4	Homo sapiens	140-143
6495255-6	1984	If a second heparin injection is given 24 hr after the first, the resultant plasma PF4 level was on average half that achieved after the first injection and again the patients had higher levels than the controls.	Heparin	12-19	platelet factor 4	Homo sapiens	83-86
3123254-5	1987	However, a second heparin injection 10 min after protamine, induced a PF4 peak release.	Heparin	18-25	platelet factor 4	Homo sapiens	70-73
3123254-6	1987	It is possible that protamine displaced the PF4 from the binding sites of heparin, releasing it for storage in the body "pool", from where it can be harvested again.	Heparin	74-81	platelet factor 4	Homo sapiens	44-47
6495255-7	1984	Thus the reservoir originally "emptied" of PF4 by the heparin had been partially refilled in 24 hr and the reservoir in the atherosclerotic patients then contained more than the controls.	Heparin	54-61	platelet factor 4	Homo sapiens	43-46
6495255-8	1984	Patients with atherosclerosis and especially diabetics differ from controls in the PF4 content of their platelets and in their response to heparin and in the rate of refill of the "heparin-mobilisable pool of PF4".	Heparin	181-188	platelet factor 4	Homo sapiens	209-212
7159570-3	1982	The same protein and same active site are involved in hydrolysis of water-soluble p-nitrophenyl esters and emulsified trioleoylglycerol since (a) trioleoylglycerol hydrolysis and PNPB hydrolysis activities coelute from the heparin-Sepharose affinity column used to purify LpL and (b) LpL-catalyzed hydrolyses of trioleoylglycerol and PNPB are inhibited to equal extents by phenylmethanesulfonyl fluoride.	Heparin	223-230	lipoprotein lipase	Bos taurus	272-275
7159570-3	1982	The same protein and same active site are involved in hydrolysis of water-soluble p-nitrophenyl esters and emulsified trioleoylglycerol since (a) trioleoylglycerol hydrolysis and PNPB hydrolysis activities coelute from the heparin-Sepharose affinity column used to purify LpL and (b) LpL-catalyzed hydrolyses of trioleoylglycerol and PNPB are inhibited to equal extents by phenylmethanesulfonyl fluoride.	Heparin	223-230	lipoprotein lipase	Bos taurus	284-287
3448103-2	1987	Heparin can dissociate lipoprotein lipase from casein micelles, and addition of heparin enhances lipolysis in bovine but not in caprine milk.	Heparin	0-7	lipoprotein lipase	Bos taurus	23-41
6234027-1	1984	Phosphorylation of acidic substrates such as casein and phosvitin by nuclear protein kinase II is stimulated by polyamines and inhibited by heparin, which mimics an endogenous proteoglycan inhibitor.	Heparin	140-147	casein kinase 2 beta	Homo sapiens	56-65
6740570-6	1984	The bound heparin (HRH2) had a high affinity for AT-III and precipitated LDL in the presence of Ca2+.	Heparin	10-17	histamine receptor H2	Homo sapiens	19-23
3448103-3	1987	Heparin shortened the lag-time for binding of lipoprotein lipase to milk fat globules and for lipolysis.	Heparin	0-7	lipoprotein lipase	Bos taurus	46-64
7175378-5	1982	HDL2 cholesterol is calculated as the difference between total HDL cholesterol (heparin-Mn2+ supernatant) and HDL3 cholesterol (dextran sulfate supernatant).	Heparin	80-87	junctophilin 3	Homo sapiens	0-4
3448103-11	1987	Heparin had only small effects on the distribution of lipoprotein lipase in caprine milk, which explains why heparin has so little effect on lipolysis in caprine milk.	Heparin	0-7	lipoprotein lipase	Bos taurus	54-72
3423020-7	1987	Heparin inhibited binding and uptake of 125I-PF4 radioactivity by hepatocytes.	Heparin	0-7	platelet factor 4	Homo sapiens	45-48
6812640-1	1982	Whole-irradiated rabbit pre-heparin plasma had an important inhibitory effect on hepatic triacylglycerol lipase and lipoprotein lipase activities, whereas control rabbit pre-heparin plasma slightly inhibited hepatic triacylglycerol lipase activity at a high concentration and enhanced lipoprotein lipase activity.	Heparin	28-35	hepatic triacylglycerol lipase	Oryctolagus cuniculus	81-111
6429888-3	1984	In previous studies a diminished release of PF4 upon heparin stimuli was observed in plasma from patients with Behcet"s disease and interpreted as an additional indicator for endothelial cell dysfunction.	Heparin	53-60	platelet factor 4	Homo sapiens	44-47
6381855-5	1984	Isotopic studies showed dose-dependent saturable binding of PF 4 to GBM which was reversed by heparin.	Heparin	94-101	platelet factor 4	Rattus norvegicus	60-64
6381855-8	1984	An ionic interaction between PF 4 and GPA was indicated by elimination of staining by washing PF 4-treated sections with buffer containing 1.0 and 3.0 M NaCl or with heparin.	Heparin	166-173	platelet factor 4	Rattus norvegicus	29-33
6381855-10	1984	Heparin administration in vivo removed previously bound PF 4.	Heparin	0-7	platelet factor 4	Rattus norvegicus	56-60
3676295-4	1987	We now show that a major mitogenic fraction, isolated from heparin-Sepharose-purified material by Mono-S cation-exchange chromatography and reverse-phase high-performance liquid chromatography, is related to acidic fibroblast growth factor (aFGF).	Heparin	59-66	fibroblast growth factor 1	Bos taurus	208-239
6230409-1	1984	The abilities of four heparin regimens to inhibit activation of blood coagulation, fibrinolysis, and the platelet release reaction in humans during renal dialysis have been assessed by visible examination of the extracorporeal circulation and by use of radioimmunoassays to FPA, beta 15-42 antigen, beta gamma G, and PF4.	Heparin	22-29	platelet factor 4	Homo sapiens	317-320
6230409-3	1984	Injection of 10,000 IU heparin s.c. in five patients could sustain dialysis in only three patients for 5 hours, and allowed progressively increasing concentrations of FPA, beta gamma G, and PF4, as well as fibrin formation, in the extracorporeal circulation.	Heparin	23-30	platelet factor 4	Homo sapiens	172-193
6230409-6	1984	The concentration of the fibrinolytic system marker beta 15-42 antigen did not change significantly in any of the regimens, and the concentration of PF4 altered in response to infused heparin as well as to inadequate heparinization.	Heparin	184-191	platelet factor 4	Homo sapiens	149-152
6697533-1	1984	Gidez et al described a double precipitation method with polyanions to separate high density lipoprotein (HDL) subfractions, using sodium heparin to precipitate very low density lipoprotein (VLDL) and low density lipoprotein (LDL) first, and dextran sulphate 15000 to precipitate HDL2 from total HDL afterwards.	Heparin	131-145	junctophilin 3	Homo sapiens	280-284
7057400-0	1982	Pharmacological activities of heparins obtained from different tissues: enrichment of heparin fractions with high lipoprotein lipase, antihemolytic and anticoagulant activities by molecular sieving and antithrombin III affinity chromatography.	Heparin	30-38	lipoprotein lipase	Bos taurus	114-132
7057400-2	1982	Two groups of heparins can be distinguished regarding the lipoprotein lipase releasing activity (LPL) and the activated partial thromboplastin time (APTT).	Heparin	14-22	lipoprotein lipase	Bos taurus	58-76
7057400-2	1982	Two groups of heparins can be distinguished regarding the lipoprotein lipase releasing activity (LPL) and the activated partial thromboplastin time (APTT).	Heparin	14-22	lipoprotein lipase	Bos taurus	97-100
7057400-3	1982	Heparins prepared from liver, lung, pancreas and thymus have a ratio of LPL/APTT of 3.6, whereas heparins prepared from placenta and intestine show a ratio of only 2.1.	Heparin	0-8	lipoprotein lipase	Bos taurus	72-75
7053378-3	1982	The upper 10% of these two pools, either LMW or HMW highly active heparin, appears to be relatively homogeneous with respect to interactions with antithrombin and possessed anticoagulant potencies of 350 units/mg and 731 units/mg, respectively.	Heparin	66-73	cilia and flagella associated protein 97	Homo sapiens	48-51
7053378-4	1982	The HMW highly active heparin has been examined by analytic ultracentrifugation.	Heparin	22-29	cilia and flagella associated protein 97	Homo sapiens	4-7
7053378-6	1982	The stoichiometries of interaction of antithrombin and platelet factor 4 with HMW highly active heparin as determined by fluorescence spectroscopy indicated that 2 molecules of either protein are able to bind to 1 molecule of the mucopolysaccharide.	Heparin	96-103	cilia and flagella associated protein 97	Homo sapiens	78-81
7053378-7	1982	These studies also reveal that the binding of antithrombin to HMW highly active heparin is characterized by KDISSHAT = 5.0 X 10(-8) M and KDISSHAT2 = 1.0 x 10(-7) M, respectively.	Heparin	80-87	cilia and flagella associated protein 97	Homo sapiens	62-65
6426077-2	1984	Heparin has been shown to be of importance in increasing yields and stability of FVIII in the purification and concentration process.	Heparin	0-7	coagulation factor VIII	Homo sapiens	81-86
6426077-3	1984	Work has been done to develop on a routine scale the heparin double cold precipitation technique for the production of a freeze-dried high yield purified FVIII concentrate.	Heparin	53-60	coagulation factor VIII	Homo sapiens	154-159
6426077-7	1984	No side-effects justify further exploration of the potential of heparin for high yield purified FVIII production.	Heparin	64-71	coagulation factor VIII	Homo sapiens	96-101
3676295-4	1987	We now show that a major mitogenic fraction, isolated from heparin-Sepharose-purified material by Mono-S cation-exchange chromatography and reverse-phase high-performance liquid chromatography, is related to acidic fibroblast growth factor (aFGF).	Heparin	59-66	fibroblast growth factor 1	Bos taurus	241-245
3649921-0	1987	Heparin promotes the inactivation of antithrombin by neutrophil elastase.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	53-72
6203557-9	1984	One of the components from dissociated LDLe containing the immunodeterminant B-III, has been separated by chromatography on heparin-agarose.	Heparin	124-131	calcium voltage-gated channel subunit alpha1 B	Homo sapiens	77-82
6203109-1	1984	Pregnancy-associated plasma protein A (PAPP-A), a macromolecular glycoprotein associated with pregnancy, was shown to inhibit complement-induced haemolysis and to bind heparin reversibly.	Heparin	168-175	pappalysin 1	Homo sapiens	0-37
6203109-1	1984	Pregnancy-associated plasma protein A (PAPP-A), a macromolecular glycoprotein associated with pregnancy, was shown to inhibit complement-induced haemolysis and to bind heparin reversibly.	Heparin	168-175	pappalysin 1	Homo sapiens	39-45
6203109-3	1984	This work demonstrates that heparin exerts an inhibitory effect on complement activity but that heparin-free PAPP-A is also inhibitory.	Heparin	96-103	pappalysin 1	Homo sapiens	109-115
6457061-8	1981	Bound lipoprotein lipase could be detached from cultured cells by increasing concentrations of heparin, and at and above 0.6 microgram/ml of heparin, 90% of the cell-bound lipoprotein lipase activity was released.	Heparin	95-102	lipoprotein lipase	Bos taurus	6-24
6457061-8	1981	Bound lipoprotein lipase could be detached from cultured cells by increasing concentrations of heparin, and at and above 0.6 microgram/ml of heparin, 90% of the cell-bound lipoprotein lipase activity was released.	Heparin	141-148	lipoprotein lipase	Bos taurus	6-24
6457061-8	1981	Bound lipoprotein lipase could be detached from cultured cells by increasing concentrations of heparin, and at and above 0.6 microgram/ml of heparin, 90% of the cell-bound lipoprotein lipase activity was released.	Heparin	141-148	lipoprotein lipase	Bos taurus	172-190
6457061-10	1981	The release of lipoprotein lipase with heparin was not associated with a release of [3S]glycosaminoglycans from 35S-prelabeled cells.	Heparin	39-46	lipoprotein lipase	Bos taurus	15-33
6457061-13	1981	These results provide direct evidence for lipoprotein lipase attachment to endothelial cells through heparan sulfate on the cell surface, and provide evidence for the release of lipoprotein lipase by heparin through a detachment from this binding site.	Heparin	200-207	lipoprotein lipase	Bos taurus	178-196
3649921-3	1987	In apparent opposition to this function, heparin was found to greatly accelerate the in vitro inactivation of antithrombin by neutrophil elastase.	Heparin	41-48	elastase, neutrophil expressed	Homo sapiens	126-145
3474662-5	1987	Small effects seen with aFGF could be potentiated by adding heparin at 1 microgram/ml.	Heparin	60-67	fibroblast growth factor 1	Gallus gallus	24-28
7309711-1	1981	Cytochrome P-450 was solubilized from kidney cortex microsomes of rabbits treated with 3-methylcholanthrene and partially purified by chromatography on 6-amino-n-hexyl Sepharose 4B and heparin-Sepharose CL-6B columns.	Heparin	185-192	cytochrome P-450	Oryctolagus cuniculus	0-16
6171246-1	1981	A specific interaction between pregnancy associated plasma protein A- (PAPP A) and heparin has been demonstrated using heparin affinity crossed immunoelectrophoresis applied to late pregnancy serum.	Heparin	83-90	pappalysin 1	Homo sapiens	71-77
6171246-5	1981	The interaction of PAPP-A with heparin was therefore independent of molecular size, charge, and site of origin indicating a specific high affinity interaction between PAPP-A and heparin.	Heparin	31-38	pappalysin 1	Homo sapiens	19-25
6171246-5	1981	The interaction of PAPP-A with heparin was therefore independent of molecular size, charge, and site of origin indicating a specific high affinity interaction between PAPP-A and heparin.	Heparin	178-185	pappalysin 1	Homo sapiens	19-25
6788567-5	1980	The mean contribution of hepatic lipase to VLDL-TG hydrolysis by post-heparin plasma was 35% in normal controls, but the contribution to IDL-TG hydrolysis was significantly higher (mean - 58%).	Heparin	70-77	lipase C, hepatic type	Homo sapiens	25-39
6414552-7	1983	When heparin plasma and CPD plasma were chromatographed on Sepharose CL-6B at 37 degrees C, all the factor-VIII-related activities eluted together as large protein complexes.	Heparin	5-12	cytochrome c oxidase subunit 8A	Homo sapiens	107-111
6882775-0	1983	The effect of the chain length of heparin on its interaction with lipoprotein lipase.	Heparin	34-41	lipoprotein lipase	Bos taurus	66-84
6885787-17	1983	These include: 1) formation of sodium dodecyl sulfate-stable complexes with thrombin, urokinase, and plasmin; 2) inhibition of protease activity; 3) heparin-enhanced inhibition of thrombin; and 4) cellular binding of protease-PN complexes in a heparin-sensitive reaction.	Heparin	149-156	plasminogen	Homo sapiens	101-108
6688430-5	1983	In contrast, with HC II inhibitor, the activities of the heparins depended only upon their charge densities and were independent of AT affinity.	Heparin	57-65	serpin family D member 1	Homo sapiens	18-23
6688430-9	1983	The behavior of the AT-inactive heparins, being fully active with HC II, demonstrates the functional domain necessary for AT binding is not needed to produce HC II activity.	Heparin	32-40	serpin family D member 1	Homo sapiens	66-71
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Heparin	248-255	serpin family D member 1	Homo sapiens	48-52
7408210-1	1980	The methods proposed by Nilsson-Ehle and Ekman [8] for the specific estimation of lipoprotein lipase and hepatic lipase activities in post-heparin plasma were investigated.	Heparin	139-146	lipase C, hepatic type	Homo sapiens	105-119
6839017-9	1983	Competitive radioimmunoassay demonstrated a low but significant immunologic cross-reactivity between human and porcine platelet factor 4, and between porcine platelet basic protein and a group of human secreted platelet proteins that bind to heparin with low affinity (beta-thromboglobulin [beta TG] and low affinity platelet factor 4).	Heparin	242-249	pro-platelet basic protein	Homo sapiens	158-180
3311146-4	1987	CKI-1 and CKI-2 correspond to mammalian type I casein kinase, because they bind to CM-Sephadex, they are monomeric enzymes of molecular weights below 50,000, they accept ATP exclusively (CKI-1) or predominantly (CKI-2) as phosphate donor, and they are either completely or relatively heparin insensitive.	Heparin	284-291	bifunctional choline kinase/ethanolamine kinase CKI1	Saccharomyces cerevisiae S288C	0-5
6839021-1	1983	Intravenous injection of heparin (100 U/kg) into normal volunteers resulted in an increase of platelet factor 4 (PF4) level in platelet-poor plasma from a mean value of 18.1 +/- 6.6 ng/ml before the injection to 257.9 +/- 68.3 ng/ml at 5 min after injection.	Heparin	25-32	platelet factor 4	Homo sapiens	113-116
6839021-2	1983	PF4 antigen isolated from "postheparin plasma" by adsorption on heparin-agarose and elution with 2.0 M NaCl and "authentic PF4" isolated from human platelets showed identical patterns of migration as determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE).	Heparin	31-38	platelet factor 4	Homo sapiens	0-3
6839021-6	1983	Heparin significantly extended the half-life of human PF4 in rat circulation.	Heparin	0-7	platelet factor 4	Homo sapiens	54-57
6839021-8	1983	Administration of heparin to rats that had been previously injected with human platelet releasate resulted in a 30-fold increase of plasma PF4 level in their circulation.	Heparin	18-25	platelet factor 4	Homo sapiens	139-142
6839021-10	1983	We propose that PF4 is originally secreted by platelets into circulation and subsequently bound reversibly to vascular sites from which it can be released back into the circulation by heparin.	Heparin	184-191	platelet factor 4	Homo sapiens	16-19
6839021-11	1983	The fast component of PF4 clearance that is abolished by heparin may reflect binding of this protein to the endothelial cells.	Heparin	57-64	platelet factor 4	Homo sapiens	22-25
7426736-1	1980	It has been shown for the first time that heparin, one of the natural polyanions, is capable of dissociating the histones H1, H2A and H2B from chromatin in a medium of "physiological" ionic strength: 0.15 M NaCl + 0.7 mM Na-phosphate buffer, pH 7.0.	Heparin	42-49	H2A clustered histone 18	Homo sapiens	126-137
2442016-7	1987	In order to get a better understanding of the nature of this binding, we performed the incubation of the frozen sections with iodinated FGFs preincubated with various compounds: (i) heparin which is known to have a strong affinity for aFGF and bFGF partially decreases the labeling, and (ii) chondroitin sulfate B and dextran sulfate at high concentrations were also partially effective.	Heparin	182-189	fibroblast growth factor 2	Mus musculus	244-248
6771147-1	1980	Rats treated acutely with aminoguanidine, a potent inhibitor of diamine oxidase, or with heparin display reduced ability to metabolize 14C-putrescine to radioactive carbon dioxide.	Heparin	89-96	amine oxidase, copper containing 1	Rattus norvegicus	64-79
506755-3	1979	In the whole homogenate a rise in the total activity of beta-glucuronidase was observed, proportional to heparin dose while there was no effect of heparin on the latent activity of beta-glucuronidase and acid phosphatase.	Heparin	105-112	glucuronidase beta	Canis lupus familiaris	56-74
6192806-9	1983	Type-L HSL activity measured in acetone/diethyl ether powders of control and stimulated rat heart exhibited properties that include alkaline pH optimum, serum requirement, activation by heparin and inhibition by high salt and protamine sulphate.	Heparin	186-193	lipase E, hormone sensitive type	Rattus norvegicus	7-10
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	serpin family D member 1	Homo sapiens	87-106
6193728-0	1983	Interaction between heparin and human pregnancy-associated plasma protein A (PAPP-A): a simple purification procedure.	Heparin	20-27	pappalysin 1	Homo sapiens	38-75
6193728-0	1983	Interaction between heparin and human pregnancy-associated plasma protein A (PAPP-A): a simple purification procedure.	Heparin	20-27	pappalysin 1	Homo sapiens	77-83
6193728-1	1983	Human pregnancy-associated plasma protein A (PAPP-A) binds to heparin-Sepharose.	Heparin	62-69	pappalysin 1	Homo sapiens	6-43
522483-3	1979	One of these, called lectin-2, interacts with specific glycosaminoglycans, especially heparin and dermatan sulfate.	Heparin	86-93	galectin 3	Gallus gallus	21-27
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	serpin family D member 1	Homo sapiens	108-113
6193728-1	1983	Human pregnancy-associated plasma protein A (PAPP-A) binds to heparin-Sepharose.	Heparin	62-69	pappalysin 1	Homo sapiens	45-51
3660328-9	1987	A modification of the distribution of both HC II and heparin between the vascular wall and the circulating blood is evoked to explain the relative increase in HC II activity and the need for higher heparin dosage in patients with low HC II levels.	Heparin	53-60	serpin family D member 1	Homo sapiens	159-164
6223404-0	1983	Interaction of heparin with lipoproteins - role of the complex in the inactivation of thrombin and plasmin.	Heparin	15-22	plasminogen	Homo sapiens	99-106
6223404-4	1983	Heparin, complexed with LDL, retains its enhancing effect on the rate of thrombin and plasmin inactivation by antithrombin III.	Heparin	0-7	plasminogen	Homo sapiens	86-93
6221433-7	1983	The single patient who did have a decrease in platelet count and a severe rise in beta-thromboglobulin with heparin died intraoperatively of a massive myocardial infarction.	Heparin	108-115	pro-platelet basic protein	Homo sapiens	82-102
6847629-3	1983	That these fractions bound to immobilized PF4 was indicated by the complete binding under near physiological conditions of 3H-labelled unfractionated commercial heparin.	Heparin	161-168	platelet factor 4	Homo sapiens	42-45
701283-2	1978	Heparin triggered a prompt release of phospholipase A from perfused liver.	Heparin	0-7	phospholipase A and acyltransferase 1	Rattus norvegicus	38-53
701283-4	1978	Heparin (20 u/ml) doubled the release of phospholipase A and triglyceride lipase from hepatocytes.	Heparin	0-7	phospholipase A and acyltransferase 1	Rattus norvegicus	41-56
701283-5	1978	Colchicine (0.1 mM), but not puromycin (0.2 mM), inhibited basal and heparin-stimulated phospholipase A release by 40%.	Heparin	69-76	phospholipase A and acyltransferase 1	Rattus norvegicus	88-103
3660328-9	1987	A modification of the distribution of both HC II and heparin between the vascular wall and the circulating blood is evoked to explain the relative increase in HC II activity and the need for higher heparin dosage in patients with low HC II levels.	Heparin	198-205	serpin family D member 1	Homo sapiens	43-48
6222929-0	1983	The interaction of heparin with human plasmin.	Heparin	19-26	plasminogen	Homo sapiens	38-45
2437338-8	1987	After intraoperative administration of heparin, plasma levels of platelet factor 4 increased from 19 to 200 ng/ml, and beta-thromboglobulin levels increased from 56 to 76 ng/ml.	Heparin	39-46	pro-platelet basic protein	Homo sapiens	119-139
6222929-2	1983	The interaction of heparin with human plasmin was investigated measuring plasmin activity and enzyme inactivation in the presence of heparin.	Heparin	19-26	plasminogen	Homo sapiens	38-45
6222929-2	1983	The interaction of heparin with human plasmin was investigated measuring plasmin activity and enzyme inactivation in the presence of heparin.	Heparin	19-26	plasminogen	Homo sapiens	73-80
6222929-2	1983	The interaction of heparin with human plasmin was investigated measuring plasmin activity and enzyme inactivation in the presence of heparin.	Heparin	133-140	plasminogen	Homo sapiens	38-45
6222929-3	1983	Hydrolysis of synthetic substrates (H-D-Val-Leu-Lys-pNA, H-D-Val-Phe-Lys-pNA and H-D-Pro-Phe-Lys-pNA) by plasmin was enhanced by heparin through an increase in kcat values.	Heparin	129-136	plasminogen	Homo sapiens	105-112
6222929-8	1983	Furthermore, heparin increased the heat sensitivity of plasmin, when synthetic substrate H-D-Val-Leu-Lys-pNA was used but it did not affect enzyme activity towards N-benzoyl-L-arginine-ethylester substrate.	Heparin	13-20	plasminogen	Homo sapiens	55-62
6222929-10	1983	The data show that microenvironmental conformation around the active center of plasmin is influenced by heparin.	Heparin	104-111	plasminogen	Homo sapiens	79-86
7147210-2	1982	The assay is very sensitive and will measure heparin concentrations down to 10 ng ml-1.	Heparin	45-52	interleukin 17F	Homo sapiens	82-86
417236-0	1978	[Possible clinical importance of the activation of diamine oxidase (histaminase) in heparin treatment of renal diseases (author"s transl)].	Heparin	84-91	amine oxidase copper containing 1	Homo sapiens	51-66
417236-0	1978	[Possible clinical importance of the activation of diamine oxidase (histaminase) in heparin treatment of renal diseases (author"s transl)].	Heparin	84-91	amine oxidase copper containing 1	Homo sapiens	68-79
417236-2	1978	An additional property of heparin is the activation of the diamine oxidase (histaminase).	Heparin	26-33	amine oxidase copper containing 1	Homo sapiens	59-74
417236-2	1978	An additional property of heparin is the activation of the diamine oxidase (histaminase).	Heparin	26-33	amine oxidase copper containing 1	Homo sapiens	76-87
417236-3	1978	Whether a possible clinical importance of the diamine oxidase activation in heparin treatment of renal diseases exists or not remains unknown and is discussed.	Heparin	76-83	amine oxidase copper containing 1	Homo sapiens	46-61
3590116-8	1987	When a neutralizing dose of protamine was added to PF4-neutralized, heparinized plasma, the protamine displaced the PF4 from its complexes with heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	51-54
105491-0	1978	[Activation of diaminooxidase (histaminase) by heparin.	Heparin	47-54	amine oxidase copper containing 1	Homo sapiens	31-42
7123544-3	1982	The result, in conjunction with the HDL-cholesterol concentration simultaneously determined by the heparin-Ca2+ method, enabled us to calculate the HDL2- and HDL3-cholesterol concentrations.	Heparin	99-106	junctophilin 3	Homo sapiens	148-152
3590116-8	1987	When a neutralizing dose of protamine was added to PF4-neutralized, heparinized plasma, the protamine displaced the PF4 from its complexes with heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	116-119
6214868-0	1982	The in vivo release of human platelet factor 4 by heparin.	Heparin	50-57	platelet factor 4	Homo sapiens	29-46
6214868-1	1982	Intravenous and subcutaneous injection of heparin or the heparin analogue SSHA into normal volunteers induced release of platelet factor 4 (PF4) but not beta-thromboglobulin (beta-TG).	Heparin	42-49	platelet factor 4	Homo sapiens	121-138
3590116-9	1987	The large protamine-heparin complexes which formed also contained PF4 but could not activate fresh ATIII as has been demonstrated with protamine-heparin complexes without PF4.	Heparin	20-27	platelet factor 4	Homo sapiens	66-69
6214868-1	1982	Intravenous and subcutaneous injection of heparin or the heparin analogue SSHA into normal volunteers induced release of platelet factor 4 (PF4) but not beta-thromboglobulin (beta-TG).	Heparin	42-49	platelet factor 4	Homo sapiens	140-143
6214868-1	1982	Intravenous and subcutaneous injection of heparin or the heparin analogue SSHA into normal volunteers induced release of platelet factor 4 (PF4) but not beta-thromboglobulin (beta-TG).	Heparin	57-64	platelet factor 4	Homo sapiens	121-138
563231-0	1977	Interaction of lipoprotein lipase with heparin-Sepharose.	Heparin	39-46	lipoprotein lipase	Bos taurus	15-33
3590116-10	1987	On incubation of the protamine-PF4-neutralized, heparinized plasmas for 5 hours at 37 degrees C, the large complexes were broken down but no active heparin appeared.	Heparin	48-55	platelet factor 4	Homo sapiens	31-34
563231-29	1977	These and other results suggested that, whereas the enzyme preparation was rather homogeneous in its binding to heparin, the heparin preparation was polydisperse in binding of lipoprotein lipase.	Heparin	125-132	lipoprotein lipase	Bos taurus	176-194
6214868-1	1982	Intravenous and subcutaneous injection of heparin or the heparin analogue SSHA into normal volunteers induced release of platelet factor 4 (PF4) but not beta-thromboglobulin (beta-TG).	Heparin	57-64	platelet factor 4	Homo sapiens	140-143
6214868-2	1982	At low heparin doses the amount of PF4 released was related to the plasma heparin concentration achieved.	Heparin	7-14	platelet factor 4	Homo sapiens	35-38
6214868-2	1982	At low heparin doses the amount of PF4 released was related to the plasma heparin concentration achieved.	Heparin	74-81	platelet factor 4	Homo sapiens	35-38
6214868-3	1982	The rise in plasma PF4 was coincident with, and appeared to be a response to, the increase in plasma heparin concentration rather than to the absolute heparin level.	Heparin	101-108	platelet factor 4	Homo sapiens	19-22
6214868-3	1982	The rise in plasma PF4 was coincident with, and appeared to be a response to, the increase in plasma heparin concentration rather than to the absolute heparin level.	Heparin	151-158	platelet factor 4	Homo sapiens	19-22
6214868-7	1982	We have demonstrated the presence of PF4 on the vascular endothelium, and suggest that this is the immediate source of the PF4 released by heparin, though it is probably initially derived from platelets.	Heparin	139-146	platelet factor 4	Homo sapiens	37-40
7101237-1	1982	The role of heparin structure in neutralization by the neutralizing substances (NS) platelet factor 4 (PF4) and protamine sulfate (PS) was investigated using a thrombin clotting assay and a series of more homogeneous heparin fractions varying systematically in charge density (Z).	Heparin	12-19	platelet factor 4	Homo sapiens	103-106
7101237-2	1982	For a given heparin, plotting inverse clotting times measured without NS, and in the presence of PF4 or PS, vs heparin concentration yielded approximately parallel straight lines displaced horizontally according to the amount of NS.	Heparin	12-19	platelet factor 4	Homo sapiens	97-100
7101237-2	1982	For a given heparin, plotting inverse clotting times measured without NS, and in the presence of PF4 or PS, vs heparin concentration yielded approximately parallel straight lines displaced horizontally according to the amount of NS.	Heparin	111-118	platelet factor 4	Homo sapiens	97-100
7101237-4	1982	Small but significant quantitative differences in potency among equivalent fractions from different heparins showed both PF4 and PS had a slight preference for the least active subfraction of decolorized heparins, but for the most active subfraction of undecolorized heparins.	Heparin	100-108	platelet factor 4	Homo sapiens	121-124
603758-8	1977	Heparin and A73025 were neutralized to approximately the same degree by a crude PF4 preparation.	Heparin	0-7	platelet factor 4	Homo sapiens	80-83
894146-3	1977	Rechromatography of purified H-TGL on heparin-Sepharose resulted in recoveries of 74 and 97% of these enzyme activities, respectively.	Heparin	38-45	lipase C, hepatic type	Homo sapiens	29-34
402498-5	1977	The plasmatic level changes of DAO and LL after heparin application (200 U/kg b.wt., i.v.)	Heparin	48-55	amine oxidase copper containing 1	Homo sapiens	31-34
7101237-4	1982	Small but significant quantitative differences in potency among equivalent fractions from different heparins showed both PF4 and PS had a slight preference for the least active subfraction of decolorized heparins, but for the most active subfraction of undecolorized heparins.	Heparin	204-212	platelet factor 4	Homo sapiens	121-124
3590116-11	1987	The results of these experiments may have some bearing on the amount of protamine needed for the neutralization of heparin following extracorporeal bypass procedures, when large amounts of PF4 may have been released from activated or disrupted platelets.	Heparin	115-122	platelet factor 4	Homo sapiens	189-192
7101237-4	1982	Small but significant quantitative differences in potency among equivalent fractions from different heparins showed both PF4 and PS had a slight preference for the least active subfraction of decolorized heparins, but for the most active subfraction of undecolorized heparins.	Heparin	204-212	platelet factor 4	Homo sapiens	121-124
7101237-5	1982	Neutralization of heparin by PF4 and PS probably proceeds by similar mechanisms, but the details of structure outside the antithrombin III-binding oligosaccharide of heparin may enter in differently.	Heparin	18-25	platelet factor 4	Homo sapiens	29-32
200085-0	1977	Lipoprotein lipase and hepatic lipase activity in post-heparin plasma of patients with hypertriglyceridemia.	Heparin	55-62	lipase C, hepatic type	Homo sapiens	23-37
2952119-3	1987	It was partially purified by affinity chromatography heparin-agarose column and was shown to be a serine protease.	Heparin	53-60	kallikrein 1-related peptidase C8	Rattus norvegicus	98-113
826537-2	1976	Lipoprotein lipase of high purity has been isolated from bovine milk by affinity chromatography on heparin-Sepharose, adsorption to Cgamma-aluminum hydroxide gel, and intervent dilution chromatography on heparin-Sepharose.	Heparin	99-106	lipoprotein lipase	Bos taurus	0-18
6802184-1	1982	Lipoprotein lipase was purified from guinea pig milk by chromatography on heparin-Sepharose followed by chromatography on an immobilized preparation of heparin that had been N-desulphated and then acetylated.	Heparin	74-81	lipoprotein lipase	Cavia porcellus	0-18
6802184-1	1982	Lipoprotein lipase was purified from guinea pig milk by chromatography on heparin-Sepharose followed by chromatography on an immobilized preparation of heparin that had been N-desulphated and then acetylated.	Heparin	152-159	lipoprotein lipase	Cavia porcellus	0-18
6802184-5	1982	Antibodies raised against the guinea pig milk enzyme inhibited not only this enzyme but also  the lipoprotein lipase activity in post-heparin plasma and in homogenates from adipose tissue and heart.	Heparin	134-141	lipoprotein lipase	Cavia porcellus	98-116
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	Heparin	26-33	serpin family D member 1	Homo sapiens	47-51
3546304-3	1987	Rat platelet factor 4 was specifically isolated and characterized by its high affinity for heparin-Sepharose and its amino-terminal sequence homology to human and rabbit platelet factor 4.	Heparin	91-98	platelet factor 4	Rattus norvegicus	4-21
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	130-137	serpin family D member 1	Homo sapiens	70-74
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	174-181	serpin family D member 1	Homo sapiens	70-74
6800421-0	1982	Distribution of plasma fibronectin (cold-insoluble globulin) and components of the factor VIII complex after heparin-induced precipitation of plasma.	Heparin	109-116	cytochrome c oxidase subunit 8A	Homo sapiens	90-94
6800421-2	1982	Following heparin induced precipitation, most measurable VIII:C activity (77% +/- 24%) was recovered in the HS.	Heparin	10-17	cytochrome c oxidase subunit 8A	Homo sapiens	57-61
6800421-10	1982	The ability of heparin to induce precipitation of CIg while leaving most VIII:C activity in the supernatant plasma may be useful in the preparation of procoagulant-rich plasma subfractions, since VIII:C can subsequently be recovered in good yield by cryoprecipitation.	Heparin	15-22	cytochrome c oxidase subunit 8A	Homo sapiens	196-200
184362-6	1976	The final MnCl2 and heparin concentrations of 0.046 M and 184 USP units/ml, which are incorporated in widely used procedures, gave C-HDL values for the precipitation method which were in close agreement with the ultracentrifugal method.	Heparin	20-27	chromodomain helicase DNA binding protein 1 like	Homo sapiens	131-136
3818795-3	1987	When HBGF-2 is adsorbed to artificial extracellular matrices consisting of heparin or chondroitin sulfate, it causes the formation of cellular aggregates or circles of cells, respectively.	Heparin	75-82	fibroblast growth factor 2	Gallus gallus	5-11
7076945-1	1982	The influence of mastitis and early lactation, and the effect of treating milk with heparin, blood serum and trypsin, on the proportion of lipoprotein lipase (LPL) activity in mild serum was investigated.	Heparin	84-91	lipoprotein lipase	Bos taurus	139-157
7076945-1	1982	The influence of mastitis and early lactation, and the effect of treating milk with heparin, blood serum and trypsin, on the proportion of lipoprotein lipase (LPL) activity in mild serum was investigated.	Heparin	84-91	lipoprotein lipase	Bos taurus	159-162
7076945-5	1982	The addition of 5 microgram/ml heparin resulted in a consistent increase in serum LPL which varied between 14 and 50% of total milk LPL.	Heparin	31-38	lipoprotein lipase	Bos taurus	82-85
7076945-5	1982	The addition of 5 microgram/ml heparin resulted in a consistent increase in serum LPL which varied between 14 and 50% of total milk LPL.	Heparin	31-38	lipoprotein lipase	Bos taurus	132-135
7053378-8	1982	The avidity of platelet factor 4 for HMW highly active heparin could not be quantitated but appears to be at least 10 to 100 times greater than that of antithrombin for mucopolysaccharide.	Heparin	55-62	cilia and flagella associated protein 97	Homo sapiens	37-40
8061-7	1976	The activity of the purified enzyme (i) had a pH optimum between 7.8 and 8.0; (ii) required serum for full enzymatic activity; apoC-II could be substituted for serum; (iii) was inhibited by by apoC-I in the presence of activated substrate; (iv) was markedly inhibited by NaCl; and (v) was stimulated by heparin.	Heparin	303-310	apolipoprotein C2	Homo sapiens	127-134
8061-7	1976	The activity of the purified enzyme (i) had a pH optimum between 7.8 and 8.0; (ii) required serum for full enzymatic activity; apoC-II could be substituted for serum; (iii) was inhibited by by apoC-I in the presence of activated substrate; (iv) was markedly inhibited by NaCl; and (v) was stimulated by heparin.	Heparin	303-310	apolipoprotein C1	Homo sapiens	127-133
7579-5	1976	The enzyme is activated by apolipoprotein C-II (apolipoprotein-glutamic acid), serum, and by heparin to which it also binds.	Heparin	93-100	apolipoprotein C2	Bos taurus	27-46
2876053-4	1986	Furthermore, compared to TH extracted from control tissues, that from 7-OH-DPAT-exposed striatal slices was more sensitive to the stimulatory effects of exogenous heparin and cyclic AMP-dependent phosphorylation.	Heparin	163-170	tyrosine hydroxylase	Rattus norvegicus	25-27
818862-3	1976	Normally, the intravenous injection of heparin is promptly followed by a marked rise of plasma DAO.	Heparin	39-46	amine oxidase copper containing 1	Homo sapiens	95-98
818862-9	1976	), in contrary to human viral hepatitis plasma DAO increased about 5-fold after heparin application.	Heparin	80-87	amine oxidase copper containing 1	Homo sapiens	47-50
818862-13	1976	Increased basal DAO levels correspond to the enhanced release after heparin application, both possibly induced by less stable binding of the enzyme to the cells of the small intestine in inflammation.	Heparin	68-75	amine oxidase copper containing 1	Homo sapiens	16-19
6462134-4	1981	Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx.	Heparin	0-7	plasminogen	Homo sapiens	78-85
6462134-4	1981	Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx.	Heparin	0-7	plasminogen	Homo sapiens	146-153
6462134-4	1981	Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx.	Heparin	134-141	plasminogen	Homo sapiens	78-85
6462134-6	1981	Heparin at a molar concentration well below that of plasmin still accelerates the reaction: one molecule of the polysaccharide is able to facilitate the inactivation of about 100 molecules of plasmin.	Heparin	0-7	plasminogen	Homo sapiens	192-199
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	0-7	plasminogen	Homo sapiens	21-28
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	0-7	plasminogen	Homo sapiens	47-54
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	0-7	plasminogen	Homo sapiens	47-54
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	0-7	plasminogen	Homo sapiens	47-54
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	191-198	plasminogen	Homo sapiens	21-28
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	191-198	plasminogen	Homo sapiens	47-54
4122-2	1976	The activity of a partially purified preparation of tyrosine hydroxylase (EC 1.14.16.2) from the bovine caudate nucleus was increased by heparin, chondroitin sulfate, phosphatidylserine, polyacrylic acid, polyvinyl sulfuric acid and both poly-D-, and poly-L-glutamic acids, all polyanions.	Heparin	137-144	tyrosine hydroxylase	Bos taurus	52-72
3530335-3	1986	Lipoprotein lipase released by heparin from adipocytes and from perfused hearts had the same apparent size.	Heparin	31-38	lipoprotein lipase	Cavia porcellus	0-18
808238-3	1975	Contaminant proteins were removed by high concentrations of NaCl (up to 1.0M), and the histaminase was then eluted from the column with a buffer containing 300--400 units/ml of sodium heparin.	Heparin	177-191	amine oxidase copper containing 1	Homo sapiens	87-98
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	191-198	plasminogen	Homo sapiens	47-54
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	191-198	plasminogen	Homo sapiens	47-54
6462134-9	1981	By contrast, the effect of increasing the amount of plasmin in the presence of constant amount of heparin and antithrombin III is such that higher plasmin-to-heparin ratios are associated with lower rates of inactivation.	Heparin	98-105	plasminogen	Homo sapiens	52-59
6462134-9	1981	By contrast, the effect of increasing the amount of plasmin in the presence of constant amount of heparin and antithrombin III is such that higher plasmin-to-heparin ratios are associated with lower rates of inactivation.	Heparin	98-105	plasminogen	Homo sapiens	147-154
6462134-9	1981	By contrast, the effect of increasing the amount of plasmin in the presence of constant amount of heparin and antithrombin III is such that higher plasmin-to-heparin ratios are associated with lower rates of inactivation.	Heparin	158-165	plasminogen	Homo sapiens	52-59
6462134-9	1981	By contrast, the effect of increasing the amount of plasmin in the presence of constant amount of heparin and antithrombin III is such that higher plasmin-to-heparin ratios are associated with lower rates of inactivation.	Heparin	158-165	plasminogen	Homo sapiens	147-154
6462134-10	1981	It seems, therefore, that to obtain ;optimal" conditions for fast enzyme inactivation, the amount of heparin should be matched to plasmin rather than to antithrombin III.	Heparin	101-108	plasminogen	Homo sapiens	130-137
6462134-11	1981	Arrhenius plots of the plasmin-antithrombin III reaction are linear both in the absence and presence of heparin, at concentrations of 1 or 2mug/ml, over a range of 26K.	Heparin	104-111	plasminogen	Homo sapiens	23-30
6175048-8	1981	The increase in PF4 levels at 15 min (55.2 +/- 19.6 ng/ml, p less than 0.01) and 1 hr (23.7 +/- 8.4 ng/ml, p less than 0.01) of hemodialysis from the level before it (7.7 +/- 1.3 ng/ml) is thought to be caused the effect of heparin infusion.	Heparin	224-231	platelet factor 4	Homo sapiens	16-19
1141104-3	1975	Nhe electrode surface is maintained in a fixed position parallel to the flow of blood; blood velocity dependency is small owing to the high flow rate achieved (more than 40 cm/s); clotting is prevented by the material used and the continuous instillation of heparin through the arterial end of the shunt.	Heparin	258-265	solute carrier family 9 member C1	Homo sapiens	0-3
3766757-10	1986	Injection of heparin resulted in a 100-fold increase of excretion in the urine of 125I-labeled Pf4 precipitable by 10% trichloroacetic acid.	Heparin	13-20	platelet factor 4	Homo sapiens	95-98
3823117-3	1986	Thrombin is able to inhibit the increase of myosin content caused by heparin.	Heparin	69-76	coagulation factor II, thrombin	Sus scrofa	0-8
1112940-2	1975	Intravenous injection of heparin increases lipoprotein lipase activity of circulating serum presumably by removing the enzyme from its location on the capillary endothelium.	Heparin	25-32	lipoprotein lipase	Capra hircus	43-61
7285347-5	1981	The method provides an alternative to the recently described heparin/MnCl2/dextran sulphate double-precipitation procedure, with the advantage of permitting quantitative recovery of intact HDL2.	Heparin	61-68	junctophilin 3	Homo sapiens	189-193
3509863-3	1986	The most potent inhibitor of neutrophil elastase was alpha 1AT (Leu358), which also proved to be effective against cathepsin G. The alpha 1AT (Arg358) variant inactivated thrombin with kinetics similar to antithrombin III in the presence of heparin.	Heparin	241-248	elastase, neutrophil expressed	Homo sapiens	29-48
3768894-5	1986	The silkworm lectin had the highest affinity for dermatan sulfate and hyaluronic acid, followed by protuberic acid, heparin, and chondroitin sulfate A.	Heparin	116-123	hemocytin	Bombyx mori	13-19
7253846-1	1981	A study of the in vitro activity of lipoprotein lipase of guinea pigs has shown that (a) the lipolytic activity of activated post-heparin serum is depressed in hypercholesteremic guinea pigs compared to the serum of normocholesteremic guinea pigs; and (b) this depressed lipolytic activity in hypercholesteremic guinea pigs is not due to the presence of an inhibitor.	Heparin	130-137	lipoprotein lipase	Cavia porcellus	36-54
6164044-4	1981	Cardiac patients treated with heparin had higher beta TG levels than non heparin-treated patients, which raises queries about a possible influence of heparin on this particular blood protein.	Heparin	30-37	pro-platelet basic protein	Homo sapiens	49-56
33848529-3	2021	Here we demonstrated that AP2M1A was a heparin-binding protein abundantly stored in eggs and embryos of zebrafish, and its gene expression was markedly up-regulated by LPS and LTA treatment.	Heparin	39-46	adaptor related protein complex 2 subunit mu 1a	Danio rerio	26-32
3717950-1	1986	Solution characterization of heparin with high affinity (HA) and low affinity (LA) for antithrombin III was performed using the methods of small-angle x-ray scattering (SAXS), viscometry, and aqueous gel permeation chromatography (GPC).	Heparin	29-36	serpin family C member 1	Sus scrofa	87-103
32985077-3	2021	In this study bone morphogenetic protein2 (BMP-2) was delivered fromtitania nanotubes (Nt)modified with chitosan/heparin polyelectrolyte multilayers (PEMs).	Heparin	113-120	bone morphogenetic protein 2	Rattus norvegicus	14-41
32985077-3	2021	In this study bone morphogenetic protein2 (BMP-2) was delivered fromtitania nanotubes (Nt)modified with chitosan/heparin polyelectrolyte multilayers (PEMs).	Heparin	113-120	bone morphogenetic protein 2	Rattus norvegicus	43-48
32876926-9	2021	The score was designated as Probability of Secondary Structure Change (PSSC) and it significantly correlated with the BMax (R = 0.942, P < 0.001) and the Kds (R = - 0.744, P < 0.01) of heparin binding of hTgP and of the "mutant" peptides.	Heparin	185-192	transglutaminase 4	Homo sapiens	204-208
6787849-7	1981	Heparin (up to 15,000 U/kg), which releases DAO from the small (0.1 mg/kg), intestine, and aminoguanidine (0.1 mg/kg), which inhibits the enzyme powerfully, both cause decreased rates of catabolism of the diamine in rats.	Heparin	0-7	amine oxidase, copper containing 1	Rattus norvegicus	44-47
6787849-8	1981	The putrescine-catabolizing ability returns with a half-time of recovery of 15-18 h, corresponding to the estimates of SHAFF and BEAVEN [36] for recovery of intestinal DAO activity following administration of heparin or cycloheximide.	Heparin	209-216	amine oxidase, copper containing 1	Rattus norvegicus	168-171
6448845-4	1980	Subsequently, we demonstrated that labeled heparin could be utilized in conjunction with fluorescence polarization spectroscopy to monitor the binding of mucopolysaccharide to thrombin, factor IXa, factor Xa, and plasmin.	Heparin	43-50	plasminogen	Homo sapiens	213-220
6448845-6	1980	factor IXa complex is characterized by a stoichiometry of 1:1 with KHIXa DISS = 2.58 x 10(-7) M. The binding of heparin to factor Xa or plasmin occurred with low avidity.	Heparin	112-119	plasminogen	Homo sapiens	136-143
3755043-1	1986	Two molecular forms of prostatropin distributed among five chromatographic peaks have been isolated from bovine brain by heparin-Sepharose affinity and reverse phase high performance liquid chromatography.	Heparin	121-128	fibroblast growth factor 1	Bos taurus	23-35
6448846-17	1980	Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor.	Heparin	43-50	plasminogen	Homo sapiens	198-205
33789211-3	2021	SARS-CoV-2 Spike S1 protein receptor binding domain (SARS-CoV-2 S1 RBD) binds to heparin and heparin binding proteins.	Heparin	81-88	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	11-16
3964663-2	1986	Interfacial catalysis of hepatic triacylglycerol lipase (H-TGL) and lipoprotein lipase (LpL) isolated from human post-heparin plasma was investigated with mixed monolayers of trioleoylglycerol (TO) and egg phosphatidylcholine.	Heparin	118-125	lipase C, hepatic type	Homo sapiens	25-55
33789211-3	2021	SARS-CoV-2 Spike S1 protein receptor binding domain (SARS-CoV-2 S1 RBD) binds to heparin and heparin binding proteins.	Heparin	93-100	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	11-16
7004910-3	1980	When given in a dose inhibiting angiotensin II formation and renin-secreting effect of catecholamines, heparin also diminishes their activating effect on tubular sodium transport.	Heparin	103-110	renin	Rattus norvegicus	61-66
6109005-0	1980	Studies on a molecular basis for the heparin-induced regulation of enzymatic activity of mouse striatal tyrosine hydroxylase in vitro.	Heparin	37-44	tyrosine hydroxylase	Mus musculus	104-124
6109005-2	1980	Tyrosine hydroxylase was purified up to 10-fold from hypotonic extracts of mouse striatum by heparin affinity chromatography.	Heparin	93-100	tyrosine hydroxylase	Mus musculus	0-20
6109005-4	1980	The interaction of heparin with tyrosine hydroxylase was studied in ways relating to the known interaction with antithrombin.	Heparin	19-26	tyrosine hydroxylase	Mus musculus	32-52
6109005-5	1980	Heparin and keratan sulfates failed to activate tyrosine hydroxylase in place of heparin; several fractions of the bulk heparin (constituting 5 and 15%) had enriched tyrosine hydroxylase-activating potency; and two lysine copolypeptides ((polylysyltyrosine and polylysylphenylalanine) inhibited the activation of tyrosine hydroxylase by heparin.	Heparin	120-127	tyrosine hydroxylase	Mus musculus	166-186
6109005-5	1980	Heparin and keratan sulfates failed to activate tyrosine hydroxylase in place of heparin; several fractions of the bulk heparin (constituting 5 and 15%) had enriched tyrosine hydroxylase-activating potency; and two lysine copolypeptides ((polylysyltyrosine and polylysylphenylalanine) inhibited the activation of tyrosine hydroxylase by heparin.	Heparin	120-127	tyrosine hydroxylase	Mus musculus	166-186
33984481-0	2022	Pseudo heparin resistance after pulmonary endarterectomy: Role of thrombus production of Factor VIII.	Heparin	7-14	coagulation factor VIII	Homo sapiens	89-100
33984481-3	2022	In pseudo heparin resistance, APTT response to heparin is blunted due to elevated Factor VIII (FVIII) which can underestimate anticoagulation.	Heparin	10-17	coagulation factor VIII	Homo sapiens	82-93
33984481-3	2022	In pseudo heparin resistance, APTT response to heparin is blunted due to elevated Factor VIII (FVIII) which can underestimate anticoagulation.	Heparin	10-17	coagulation factor VIII	Homo sapiens	95-100
33984481-3	2022	In pseudo heparin resistance, APTT response to heparin is blunted due to elevated Factor VIII (FVIII) which can underestimate anticoagulation.	Heparin	47-54	coagulation factor VIII	Homo sapiens	82-93
33984481-3	2022	In pseudo heparin resistance, APTT response to heparin is blunted due to elevated Factor VIII (FVIII) which can underestimate anticoagulation.	Heparin	47-54	coagulation factor VIII	Homo sapiens	95-100
33984481-13	2022	Pseudo heparin resistance is common after PEA likely due to highly elevated postoperative FVIII levels indicating that anti-Xa reflects postoperative heparinization better than APTT in these patients.	Heparin	7-14	coagulation factor VIII	Homo sapiens	90-95
6109005-5	1980	Heparin and keratan sulfates failed to activate tyrosine hydroxylase in place of heparin; several fractions of the bulk heparin (constituting 5 and 15%) had enriched tyrosine hydroxylase-activating potency; and two lysine copolypeptides ((polylysyltyrosine and polylysylphenylalanine) inhibited the activation of tyrosine hydroxylase by heparin.	Heparin	120-127	tyrosine hydroxylase	Mus musculus	166-186
6109005-5	1980	Heparin and keratan sulfates failed to activate tyrosine hydroxylase in place of heparin; several fractions of the bulk heparin (constituting 5 and 15%) had enriched tyrosine hydroxylase-activating potency; and two lysine copolypeptides ((polylysyltyrosine and polylysylphenylalanine) inhibited the activation of tyrosine hydroxylase by heparin.	Heparin	120-127	tyrosine hydroxylase	Mus musculus	166-186
6109005-7	1980	Heparin (but not heparan and keratan sulfates) protected tyrosine hydroxylase from this inhibition.	Heparin	0-7	tyrosine hydroxylase	Mus musculus	57-77
3741180-4	1986	Time of exposure to heparin was 6.4 +/- 4 (m +/- sd) days.	Heparin	20-27	MSD	Homo sapiens	43-51
6109005-10	1980	This enzyme preparation exhibited an eightfold greater sensitivity to lysyltyrosylamide than tyrosine hydroxylase purified by heparin affinity.	Heparin	126-133	tyrosine hydroxylase	Mus musculus	93-113
6158345-1	1980	Low-affinity platelet factor 4 and beta-thromboglobulin are platelet-secreted proteins that bind with low affinity to heparin.	Heparin	118-125	pro-platelet basic protein	Homo sapiens	35-55
33692650-0	2021	Towards better understanding of the heparin role in NETosis: feasibility of using native mass spectrometry to monitor interactions of neutrophil elastase with heparin oligomers.	Heparin	159-166	elastase, neutrophil expressed	Homo sapiens	134-153
33692650-3	2021	Retention of neutrophil elastase within NETs is provided by ejected DNA chains, although this protein is also capable of interacting with a range of other endogenous polyanions, such as heparin and heparan sulfate.	Heparin	186-193	elastase, neutrophil expressed	Homo sapiens	13-32
33692650-4	2021	In this work, we evaluate the feasibility of using native mass spectrometry (MS) as a means of studying interactions of neutrophil elastase with heparin oligomers ranging from structurally homogeneous synthetic pentasaccharide fondaparinux to relatively long (up to twenty saccharide units) and structurally heterogeneous chains produced by partial depolymerization of heparin.	Heparin	145-152	elastase, neutrophil expressed	Homo sapiens	120-139
33692650-9	2021	Lastly, the use of MS allows the binding preferences of heparin oligomers to neutrophil elastase to be studied with respect to specific structural properties of heparin, such as the level of sulfation (i.e., charge density).	Heparin	56-63	elastase, neutrophil expressed	Homo sapiens	77-96
3085265-1	1986	Factor VIII coagulant activity (VIII:C) has been shown by several investigators to exhibit increased stability in vitro when physiological levels of plasma ionized calcium are maintained by anticoagulation with heparin rather than citrate.	Heparin	211-218	cytochrome c oxidase subunit 8A	Homo sapiens	7-11
33249594-9	2021	In addition, we found that monomeric Ng and its C-terminal fragments bind to heparin via a heparin-binding motif, which might be of relevance for their export mechanism from neurons.	Heparin	77-84	neurogranin	Homo sapiens	37-39
33249594-9	2021	In addition, we found that monomeric Ng and its C-terminal fragments bind to heparin via a heparin-binding motif, which might be of relevance for their export mechanism from neurons.	Heparin	91-98	neurogranin	Homo sapiens	37-39
7418200-5	1980	Heparin affinity chromatography of HDL2 in the presence of Ca2+ and Mn2+ showed an interaction of apolipoprotein E-containing HDL2 subfraction only in conditions involving Mn2+.	Heparin	0-7	junctophilin 3	Homo sapiens	35-39
7418200-5	1980	Heparin affinity chromatography of HDL2 in the presence of Ca2+ and Mn2+ showed an interaction of apolipoprotein E-containing HDL2 subfraction only in conditions involving Mn2+.	Heparin	0-7	junctophilin 3	Homo sapiens	126-130
7408210-0	1980	The validation and use of specific methods for the estimation of lipoprotein lipase and hepatic lipase activities in post-heparin plasma of children with hyperlipidaemia.	Heparin	122-129	lipase C, hepatic type	Homo sapiens	88-102
3085265-1	1986	Factor VIII coagulant activity (VIII:C) has been shown by several investigators to exhibit increased stability in vitro when physiological levels of plasma ionized calcium are maintained by anticoagulation with heparin rather than citrate.	Heparin	211-218	cytochrome c oxidase subunit 8A	Homo sapiens	32-36
7414568-0	1980	Inhibition of mitogenic activity of a platelet growth factor (platelet basic protein) in 3T3 cells by heparin.	Heparin	102-109	pro-platelet basic protein	Mus musculus	62-84
3085265-2	1986	An increase in initial activity of VIII:C in heparin over that of VIII:C in citrate has been reported but this has not been confirmed.	Heparin	45-52	cytochrome c oxidase subunit 8A	Homo sapiens	35-39
7436742-1	1980	Lipoprotein lipase of bovine aortic intima has been purified to homogeneity by affinity chromatography on heparin-Sepharose.	Heparin	106-113	lipoprotein lipase	Bos taurus	0-18
33871066-0	2021	Clinical application of heparin in the treatment of severe acute pancreatitis -- new discovery of the HMGB1 pathway.	Heparin	24-31	high mobility group box 1	Homo sapiens	102-107
33827271-7	2021	In this vein, a heparin-conjugated mechanically-robust collagen fabric was developed for sustained delivery of TGF-beta3.	Heparin	16-23	transforming growth factor beta 3	Homo sapiens	111-120
33827271-8	2021	The amount of conjugated heparin was varied to enhance the amount of TGF-beta3 uptake and release from the scaffold.	Heparin	25-32	transforming growth factor beta 3	Homo sapiens	69-78
6166520-15	1980	This allows PPK assays during extracorporeal circulation in the presence of circulating heparin.	Heparin	88-95	kallikrein B1	Homo sapiens	12-15
3085265-4	1986	A one-stage clotting assay for VIII:C has been developed where heparin is neutralized by Polybrene, a synthetic polymerized quaternary ammonium salt.	Heparin	63-70	cytochrome c oxidase subunit 8A	Homo sapiens	31-35
3739751-7	1986	Post-heparin plasma activity of hepatic lipase was virtually absent and that of lipoprotein lipase was reduced by 50%.	Heparin	5-12	lipase C, hepatic type	Homo sapiens	32-46
44065-3	1979	Plasmin also digests histones in complexes with heparin.	Heparin	48-55	plasminogen	Homo sapiens	0-7
33691128-3	2021	propose that heparin provides protection during gram-negative sepsis by dampening harmful CASP11-dependent signaling through inhibition of HMGB1- and heparanase-mediated cytosolic delivery of LPS.	Heparin	13-20	high mobility group box 1	Homo sapiens	139-144
2999440-1	1985	Human cytomegalovirus-induced DNA polymerase and cellular DNA polymerase alpha were purified by successive chromatography on DEAE-cellulose, phosphocellulose, heparin agarose, and single-stranded DNA agarose columns.	Heparin	159-166	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	58-78
33086397-0	2021	Characterization of New Monoclonal PF4-Specific Antibodies as Useful Tools for Studies on Typical and Autoimmune Heparin-Induced Thrombocytopenia.	Heparin	113-120	platelet factor 4	Homo sapiens	35-38
33086397-1	2021	BACKGROUND:  Heparin-induced thrombocytopenia (HIT) is typically caused by platelet-activating immunoglobulin G (IgG) antibodies (Abs) against platelet factor 4 (PF4) complexed with heparin (H).	Heparin	13-20	platelet factor 4	Homo sapiens	162-165
420853-4	1979	This enzyme has all the properties of the other mammalian DNA polymerases-alpha: sensitivity to sulfhydryl-blocking agents, to heparin, and to the level of salt in the assay, neutral pH optimum, use of ribonucleotide-initiated DNA templates, and inability to copy the ribostrand of hybrids.	Heparin	127-134	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	58-79
155386-2	1979	Free protamine is digested by plasmin giving products with a greatly decreased ability to form complexes with heparin and lower antiheparin action.	Heparin	110-117	plasminogen	Homo sapiens	30-37
33086397-1	2021	BACKGROUND:  Heparin-induced thrombocytopenia (HIT) is typically caused by platelet-activating immunoglobulin G (IgG) antibodies (Abs) against platelet factor 4 (PF4) complexed with heparin (H).	Heparin	182-189	platelet factor 4	Homo sapiens	162-165
2935971-1	1985	Plasmin and kallikrein but not thrombin cleave purified histidine-rich glycoprotein (HRG), and heparin binding inhibits the proteolysis of HRG.	Heparin	95-102	plasminogen	Homo sapiens	0-7
33086397-4	2021	OBJECTIVES:  To characterize 1E12, 1C12, and 2E1 in comparison to the heparin-dependent monoclonal anti-PF4/H Abs 5B9 and KKO, and polyclonal Abs from patients with typical HIT (group-2) and autoimmune HIT (group-3).	Heparin	70-77	platelet factor 4	Homo sapiens	104-117
155386-3	1979	Bound protamine, on the other hand, is resistant to the action of plasmin as a result of which the enzyme does not release heparin from the complexes.	Heparin	123-130	plasminogen	Homo sapiens	66-73
704362-2	1978	Only DNA polymerase-alpha was inhibited by polyanions, such as polyvinyl sufate, dextran sulfate, heparin, poly(G), poly(I), poly(U) and poly(ADP-Rib).	Heparin	98-105	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	5-25
4043407-1	1985	Heparin was fractionated on an affinity column of bovine milk lipoprotein lipase (LpL) immobilized to Affi-Gel-15.	Heparin	0-7	lipoprotein lipase	Bos taurus	82-85
206703-0	1978	Response of plasma histaminase activity to heparin in normal subjects and in patients with small cell carcinoma of the lung.	Heparin	43-50	amine oxidase copper containing 1	Homo sapiens	19-30
206703-2	1978	To determine whether heparin might release histaminase from tumor tissue into the circulation as it does from some normal tissues, we studied the response of PH activity to small doses of heparin in 41 patients with SCC and in 57 normal subjects.	Heparin	21-28	amine oxidase copper containing 1	Homo sapiens	43-54
33125711-7	2021	KEY RESULTS: All the UFH preparations had potent antiviral effects, with IC50 values ranging between 25-41 mug ml-1 whereas LMWHs were less inhibitory by ~150-fold (IC50 range 3.4 - 7.8 mg ml-1 ).	Heparin	21-24	interleukin 17F	Homo sapiens	111-115
33125711-7	2021	KEY RESULTS: All the UFH preparations had potent antiviral effects, with IC50 values ranging between 25-41 mug ml-1 whereas LMWHs were less inhibitory by ~150-fold (IC50 range 3.4 - 7.8 mg ml-1 ).	Heparin	21-24	interleukin 17F	Homo sapiens	189-193
33125711-8	2021	Mechanistically we observed that heparin binds and destabilizes the RBD protein, and furthermore we show heparin directly inhibits the binding of RBD to the human ACE2 protein receptor.	Heparin	33-40	angiotensin converting enzyme 2	Homo sapiens	163-167
33125711-8	2021	Mechanistically we observed that heparin binds and destabilizes the RBD protein, and furthermore we show heparin directly inhibits the binding of RBD to the human ACE2 protein receptor.	Heparin	105-112	angiotensin converting enzyme 2	Homo sapiens	163-167
33125711-10	2021	UFH acts to directly inhibit binding of spike protein to the human ACE2 protein receptor.	Heparin	0-3	angiotensin converting enzyme 2	Homo sapiens	67-71
33035717-2	2021	Herein, we proposed a kind of heparanase (HPSE)-driven sequential released nanoparticles, which modified with beta-cyclodextrin (beta-CD) grafted heparin (NLC/H(D + F + S) NPs) co-loading with doxorubicin (DOX), ferrocene (Fc), and TGF-beta receptor inhibitor (SB431542).	Heparin	146-153	transforming growth factor alpha	Homo sapiens	232-240
2995409-4	1985	Furthermore, the biological activity of ECGF, acidic FGF, and EDGF-II is potentiated by the glycosaminoglycan, heparin.	Heparin	111-118	fibroblast growth factor 1	Bos taurus	40-44
149555-6	1978	Thus only between 3 and 11% of the in vivo formed plasmin is neutralized by antithrombin-heparin complex.	Heparin	89-96	plasminogen	Homo sapiens	50-57
2995409-4	1985	Furthermore, the biological activity of ECGF, acidic FGF, and EDGF-II is potentiated by the glycosaminoglycan, heparin.	Heparin	111-118	fibroblast growth factor 1	Bos taurus	62-69
203038-1	1978	Human platelet factor 4 (PF4) is known to bind to heparin and inhibit its anticoagulant effect.	Heparin	50-57	platelet factor 4	Homo sapiens	25-28
33386560-0	2021	Clinical validation of immunoassay HemosIL  AcuStar HIT-IgG (PF4-H) in the diagnosis of Heparin-induced thrombocytopenia.	Heparin	88-95	platelet factor 4	Homo sapiens	61-64
4082106-8	1985	The effects on HTGL were three times larger compared to normal heparin.	Heparin	63-70	lipase C, hepatic type	Homo sapiens	15-19
33336117-10	2021	The downstream signaling of the FGF10 was also investigated, with the western blot results showing that FGF10 coacervate activated the p-FGFR, PI3K/Akt and ERK1/2 pathways to a more proper level than free FGF10 or heparin+FGF10.	Heparin	214-221	mitogen-activated protein kinase 3	Mus musculus	156-162
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	lipocalin 2	Mus musculus	71-113
203038-4	1978	Thus PF4 inhibits collagenase, in addition to neutralizing heparin.	Heparin	59-66	platelet factor 4	Homo sapiens	5-8
75564-6	1978	These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography.	Heparin	134-141	lipase C, hepatic type	Homo sapiens	104-109
75564-6	1978	These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography.	Heparin	152-159	lipase C, hepatic type	Homo sapiens	104-109
745631-1	1978	These experiments were performed to test if heparin inhibits the production of angiotensin I from rat renin substrate acted upon by either rat or hog renin.	Heparin	44-51	renin	Rattus norvegicus	102-107
745631-1	1978	These experiments were performed to test if heparin inhibits the production of angiotensin I from rat renin substrate acted upon by either rat or hog renin.	Heparin	44-51	renin	Rattus norvegicus	150-155
33368089-0	2020	Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin.	Heparin	0-7	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	98-103
745631-4	1978	Heparin (0 and 50 units/ml, final concentration) was added to rat plasma which contained renin and renin substrate.	Heparin	0-7	renin	Rattus norvegicus	89-94
4033424-1	1985	Two enzymes, lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL), are released into human plasma after intravenous injection of heparin.	Heparin	140-147	lipase C, hepatic type	Homo sapiens	42-69
745631-4	1978	Heparin (0 and 50 units/ml, final concentration) was added to rat plasma which contained renin and renin substrate.	Heparin	0-7	renin	Rattus norvegicus	99-104
146278-0	1977	Role of heparin in the inactivation of thrombin, factor Xa, and plasmin by antithrombin III.	Heparin	8-15	plasminogen	Homo sapiens	64-71
33368089-0	2020	Heparin Inhibits Cellular Invasion by SARS-CoV-2: Structural Dependence of the Interaction of the Spike S1 Receptor-Binding Domain with Heparin.	Heparin	136-143	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	98-103
33368089-5	2020	Surface plasmon resonance and circular dichroism spectroscopy demonstrate that heparin and enoxaparin, a low-molecular-weight heparin which is a clinical anticoagulant, bind and induce a conformational change in the spike (S1) protein receptor-binding domain (S1 RBD) of SARS-CoV-2.	Heparin	79-86	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	216-221
33368089-5	2020	Surface plasmon resonance and circular dichroism spectroscopy demonstrate that heparin and enoxaparin, a low-molecular-weight heparin which is a clinical anticoagulant, bind and induce a conformational change in the spike (S1) protein receptor-binding domain (S1 RBD) of SARS-CoV-2.	Heparin	126-133	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	216-221
33368089-8	2020	It is likely that inhibition of viral infection arises from an overlap between the binding sites of heparin/HS on S1 RBD and that of the angiotensin-converting enzyme 2.	Heparin	100-107	angiotensin converting enzyme 2	Homo sapiens	137-168
4033424-1	1985	Two enzymes, lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL), are released into human plasma after intravenous injection of heparin.	Heparin	140-147	lipase C, hepatic type	Homo sapiens	71-75
4082099-9	1985	After heparin the peak levels of PF4 were 139.9 ng/ml, 65.3 ng/ml and 52.7 ng/ml, respectively.	Heparin	6-13	platelet factor 4	Homo sapiens	33-36
3839761-0	1985	Histone H1 in nuclei of butyrate-treated murine lymphosarcoma cells has increased affinity for heparin.	Heparin	95-102	H1.0 linker histone	Mus musculus	0-10
33298900-3	2020	We show that heparin/HS binds to Spike directly, and facilitates the attachment of Spike-bearing viral particles to the cell surface to promote viral entry.	Heparin	13-20	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	33-38
33298900-3	2020	We show that heparin/HS binds to Spike directly, and facilitates the attachment of Spike-bearing viral particles to the cell surface to promote viral entry.	Heparin	13-20	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	83-88
270721-0	1977	Estradiol receptor of calf uterus: interactions with heparin-agarose and purification.	Heparin	53-60	estrogen receptor 1	Bos taurus	0-18
270721-1	1977	Heparin attached covalently to agarose beads binds the "native" form of the estradiol receptor with very high affinity.	Heparin	0-7	estrogen receptor 1	Bos taurus	76-94
3839761-2	1985	Unlike isolated histone H1, histone H1 in the nuclei of butyrate-treated cells was found to display an enhanced affinity for the binding to heparin as compared to histone H1 from control cells.	Heparin	140-147	H1.0 linker histone	Mus musculus	28-38
270721-4	1977	Only the "native" and not the "nuclear" or the "derived" (i.e., after activation by a calcium-dependent enzyme) forms of the estradiol receptor interact with heparin.	Heparin	158-165	estrogen receptor 1	Bos taurus	125-143
3839761-2	1985	Unlike isolated histone H1, histone H1 in the nuclei of butyrate-treated cells was found to display an enhanced affinity for the binding to heparin as compared to histone H1 from control cells.	Heparin	140-147	H1.0 linker histone	Mus musculus	28-38
3839761-3	1985	Dephosphorylation of histone H1 as a result of butyrate treatment of the cells is discussed as a possible factor involved in the observed higher affinity of the protein for heparin.	Heparin	173-180	H1.0 linker histone	Mus musculus	21-31
32417430-3	2020	HIT is an immune prothrombotic disorder caused by antibodies that recognize complexes between platelet factor 4 (PF4) and polyanions such as heparin (H).The pathogenicity of anti-PF4/H antibodies is likely due to the formation of immune complexes that initiate intense procoagulant responses by vascular and hematopoietic cells that lead to the generation of platelet microparticles, monocyte and endothelial cell procoagulant activity, and neutrophil extracellular traps, among other outcomes.	Heparin	141-148	platelet factor 4	Homo sapiens	113-116
32417430-3	2020	HIT is an immune prothrombotic disorder caused by antibodies that recognize complexes between platelet factor 4 (PF4) and polyanions such as heparin (H).The pathogenicity of anti-PF4/H antibodies is likely due to the formation of immune complexes that initiate intense procoagulant responses by vascular and hematopoietic cells that lead to the generation of platelet microparticles, monocyte and endothelial cell procoagulant activity, and neutrophil extracellular traps, among other outcomes.	Heparin	141-148	platelet factor 4	Homo sapiens	179-182
2860207-9	1985	Clear distinction between the two activating processes was further confirmed by the facts that heparin- and cyclic AMP-dependent phosphorylation stimulated TH activity from K+-exposed (and control) tissues but not that from striatal slices incubated with forskolin (or dibutyryl cyclic AMP).	Heparin	95-102	tyrosine hydroxylase	Rattus norvegicus	156-158
32417430-4	2020	The development of anti-PF4/H antibodies after exposure to UFH greatly exceeds the incidence of clinical disease, but the biochemical features that distinguish pathogenic from nonpathogenic antibodies have not been identified.	Heparin	59-62	platelet factor 4	Homo sapiens	24-27
32304324-9	2020	The addition of 2-O-sulfotransferase, the next enzyme involved in heparin synthesis, in the absence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS), also resulted in C5-epi exhibiting a more conventional Michaelis-Menten kinetic behavior in the forward reaction accompanied by a significant increase in apparent Vmax.	Heparin	66-73	heparan sulfate 2-O-sulfotransferase 1	Homo sapiens	16-36
33070765-2	2021	A critical factor impacting platelet factor-4 (PF4)-heparin antibody formation is plasma PF4 concentration.	Heparin	52-59	platelet factor 4	Homo sapiens	47-50
33070765-2	2021	A critical factor impacting platelet factor-4 (PF4)-heparin antibody formation is plasma PF4 concentration.	Heparin	52-59	platelet factor 4	Homo sapiens	89-92
33070765-5	2021	PF4-heparin ratios were estimated using an assumed heparin concentration of 0.4 IU/mL.	Heparin	4-11	platelet factor 4	Homo sapiens	0-3
195631-6	1977	Heparin is a potent inhibitor of phosvitin kinase but has no effect on histone kinase.	Heparin	0-7	casein kinase 2 beta	Homo sapiens	33-42
330064-4	1977	However, heparin, added together with thrombin, is capable of abolishing the MIF effect completely.	Heparin	9-16	macrophage migration inhibitory factor	Homo sapiens	77-80
924340-1	1977	The effect of calcium on the activation of lipoprotein lipase by heparin was studied using ammonia buffer extracts of acetone powder from guinea pig adipose tissue as the lipoprotein lipase source.	Heparin	65-72	lipoprotein lipase	Cavia porcellus	43-61
868792-2	1977	In the proposed procedure (I) a heparin thrombin time curve is constructed by adding gradually increasing amounts of heparin to a commercial plasma substrate and determining thrombin times, (2) a suitable concentration of heparin that gives highest reproducible thrombin time is selected and added to the substrate, (3) thrombin times are determined for the heparinized substrate before and after addition of a test material containing platelet factor 4.	Heparin	32-39	platelet factor 4	Homo sapiens	436-453
868792-4	1977	The difference in heparin concentrations represents platelet factor 4 activity.	Heparin	18-25	platelet factor 4	Homo sapiens	52-69
33070765-10	2021	Estimated median PF4-heparin ratios were 0.04, 0.03, and 0.02 respectively.	Heparin	21-28	platelet factor 4	Homo sapiens	17-20
33070765-13	2021	No patient had an estimated PF4-heparin ratio between 0.7 and 1.4, which is the reported optimal range for PF4-heparin antibody formation.	Heparin	111-118	platelet factor 4	Homo sapiens	107-110
4008652-8	1985	The TSP-HRGP-Plg complex bound a similar amount of heparin as the TSP-HRGP complex, demonstrating that the HRGP within the trimolecular complex maintained functional capability.	Heparin	51-58	plasminogen	Homo sapiens	13-16
32483835-5	2020	We find that soluble heparin and heparan sulfate efficiently inhibit human IL-27 activity as shown by decreased STAT signaling and downstream biological effects.	Heparin	21-28	interleukin 27	Homo sapiens	75-80
142314-0	1977	The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin.	Heparin	90-97	plasminogen	Homo sapiens	33-40
870397-2	1977	Platelets from a FXI-deficient patient treated in a similar fashion also released a coagulant activity which could be absorbed onto Sepharose-heparin and eluted similarly to plasma FXI.	Heparin	142-149	coagulation factor XI	Homo sapiens	17-20
870398-3	1977	Hirudin completely inhibited the release of both [3H]5HT and beta-glucuronidase whereas heparin completely inhibited release of beta-glucuronidase but only partly inhibited release of [3H] 5HT.	Heparin	88-95	glucuronidase beta	Homo sapiens	128-146
32483835-10	2020	Together, our data identify GAGs as new players in the regulation of human IL-27 activity that might act under physiological conditions and may also have a clinical impact in heparin-treated patients.	Heparin	175-182	interleukin 27	Homo sapiens	75-80
2581953-2	1985	Lipoprotein lipase was purified from bovine skim milk by chromatography on heparin-Sepharose.	Heparin	75-82	lipoprotein lipase	Bos taurus	0-18
32897051-4	2020	Here, we dissect the biophysical factors that facilitate the GMCSF-heparin interaction, previously shown to be pH-dependent, using NMR spectroscopy, SPR, and molecular dynamics simulations.	Heparin	67-74	sepiapterin reductase	Homo sapiens	149-152
826537-2	1976	Lipoprotein lipase of high purity has been isolated from bovine milk by affinity chromatography on heparin-Sepharose, adsorption to Cgamma-aluminum hydroxide gel, and intervent dilution chromatography on heparin-Sepharose.	Heparin	204-211	lipoprotein lipase	Bos taurus	0-18
1009091-1	1976	Lipoprotein lipase has been purified from bovine milk by affinity chromatography on Sepharose containing covalently linked heparin.	Heparin	123-130	lipoprotein lipase	Bos taurus	0-18
2581953-6	1985	Incubation of partially purified lipoprotein lipase for 24 h at 37 degrees C results in breakdown of the 55,000-dalton protein with concomitant enrichment in lower Mr components; the proteolytic activity is prevented by incubating the milk with phenylmethane, sulfonyl fluoride prior to chromatography on heparin-Sepharose.	Heparin	305-312	lipoprotein lipase	Bos taurus	33-51
33071957-10	2020	Unexpected hyperkalemia in CS patients under treatment with heparin might be the signal of aldosterone suppression.	Heparin	60-67	citrate synthase	Homo sapiens	27-29
3968434-5	1985	The pretreatment of Er with 5 micrograms and 40 micrograms of the disulfide-linked, cathepsin D derivatives isolated from high and low affinity heparin fractions, respectively, inhibited the proportion of ingesting monocytes by 60%, but these types of fragments had little effect when concurrently incubated with the opsonic fragment and Er.	Heparin	144-151	cathepsin D	Homo sapiens	84-95
137671-3	1976	The VIII-ratio returned to normal in each of 2 patients with DIC and 1 paitent with PE after treatment with heparin, heparin and alpha-amino-caproic acid, and heparin and coumadin respectively.	Heparin	108-115	cytochrome c oxidase subunit 8A	Homo sapiens	4-8
137671-3	1976	The VIII-ratio returned to normal in each of 2 patients with DIC and 1 paitent with PE after treatment with heparin, heparin and alpha-amino-caproic acid, and heparin and coumadin respectively.	Heparin	117-124	cytochrome c oxidase subunit 8A	Homo sapiens	4-8
137671-3	1976	The VIII-ratio returned to normal in each of 2 patients with DIC and 1 paitent with PE after treatment with heparin, heparin and alpha-amino-caproic acid, and heparin and coumadin respectively.	Heparin	117-124	cytochrome c oxidase subunit 8A	Homo sapiens	4-8
3968434-8	1985	At 42 micrograms, cathepsin D-derived, non-gelatin-binding, low affinity heparin fragments that contained both BD4 and CE9 determinants or only the BD4 determinant inhibited monocyte ingestion by 53 and 74%, respectively, when concurrently incubated with 180K-opFnf and target Er, but were without effect when used to pretreat Er before the addition of 180K-opFnf.	Heparin	73-80	cathepsin D	Homo sapiens	18-29
32335456-6	2020	We suppose that host cell proteases including furin (as expressed highly in lungs), factor Xa and cathepsin are possible targets to decrease viral burden, therefore unfractioned heparin and low molecular weight heparin-LMWH (specifically dalteparin and tinzaparin for their anti inflammatory action) can be potential inhibitors of multiple endoproteases involved in virus infectivity.	Heparin	178-185	furin, paired basic amino acid cleaving enzyme	Homo sapiens	46-51
32824699-3	2020	Previous reports have suggested that the glycosaminoglycan heparin is a ligand for the natural cytotoxicity receptors NKp30, NKp44 (human), and NKp46 (both human and mouse).	Heparin	59-66	natural cytotoxicity triggering receptor 1	Homo sapiens	144-149
32736596-14	2020	Bemcentinib could potentially reduce viral infection and blocks SARS-CoV-2 spike protein; MEDI3506 is a clinic-ready anti-IL-33 monoclonal antibody with the potential to treat respiratory failure caused by COVID; acalabrutinib is a BTK inhibitor which is anti-viral and anti-inflammatory; zilucoplan is a complement C5 inhibitor which may block the severe inflammatory response in COVID-19 and; nebulised heparin has been shown to bind with the spike protein.	Heparin	405-412	interleukin 33	Homo sapiens	122-127
951844-1	1976	These studies clearly indicate that heparin has 2 antagonistic effects in this platelet-foreign surface interaction; it acts directly on platelets to increase retention, while acting on the foreign surface to reduce platelet retention, perhaps by competing for cationic sites.	Heparin	36-43	hyaluronan synthase 2	Homo sapiens	44-49
1218970-3	1975	For plasma lipoproteinlipase, the enzyme is induced by injection of optimal doses of heparin associated with different quantities of gall-bladder extract and the activity is evaluated by measuring the clarifying power of the plasmas of the treated animals.	Heparin	85-92	lipoprotein lipase	Bos taurus	11-28
2983432-2	1985	Once bound to the endothelium, PF4 can be released by heparin in a time-dependent manner; recovery is greater the sooner heparin is administered following PF4 infusion.	Heparin	54-61	platelet factor 4	Homo sapiens	31-34
1173308-8	1975	The insulinotrophic effect of both peptides was verified by the fact that injection of lipid emulsion plus heparin led to a comparable increase in FFA and glucose, but to no change in insulin concentrations.	Heparin	107-114	insulin	Oryctolagus cuniculus	4-11
32748603-3	2020	In this study, the heparin C5 epimerase gene Glce from zebrafish was expressed and molecularly modified in Escherichia coli.	Heparin	19-26	glucuronic acid epimerase b	Danio rerio	45-49
2983432-2	1985	Once bound to the endothelium, PF4 can be released by heparin in a time-dependent manner; recovery is greater the sooner heparin is administered following PF4 infusion.	Heparin	121-128	platelet factor 4	Homo sapiens	31-34
806819-0	1975	Proceedings: Influence of heparin on diamine oxidase (histaminase) in acute and chronic inflammatory diseases.	Heparin	26-33	amine oxidase copper containing 1	Homo sapiens	54-65
2983432-2	1985	Once bound to the endothelium, PF4 can be released by heparin in a time-dependent manner; recovery is greater the sooner heparin is administered following PF4 infusion.	Heparin	121-128	platelet factor 4	Homo sapiens	155-158
2983432-3	1985	This heparin-induced release of PF4 can be abolished if the heparin is first complexed with hexadimethrine bromide.	Heparin	5-12	platelet factor 4	Homo sapiens	32-35
32699847-3	2020	Here we use murine leukemia viruses pseudotyped with Spike from SARS-CoV or SARS-CoV-2 to demonstrate that ACE2-mediated coronavirus entry can be mitigated by heparin, a heparan sulfate-related glycan, or by genetic ablation of biosynthetic enzymes for the cell surface heparan sulfate proteoglycans (HSPGs).	Heparin	159-166	angiotensin converting enzyme 2	Homo sapiens	107-111
2983432-3	1985	This heparin-induced release of PF4 can be abolished if the heparin is first complexed with hexadimethrine bromide.	Heparin	60-67	platelet factor 4	Homo sapiens	32-35
32699853-2	2020	Docking studies suggest a putative heparin/heparan sulfate-binding site adjacent to the domain that binds to ACE2.	Heparin	35-42	angiotensin converting enzyme 2	Homo sapiens	109-113
32699853-3	2020	In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template.	Heparin	30-37	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	41-46
2983432-4	1985	Likewise, this heparin-induced release of PF4 is dependent upon the type of heparin used; low molecular weight heparin fractions and fragments do not cause the PF4 rebound seen with intact heparin.	Heparin	15-22	platelet factor 4	Homo sapiens	42-45
32699853-3	2020	In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template.	Heparin	133-140	angiotensin converting enzyme 2	Homo sapiens	21-25
4121438-0	1973	Heparin-induced increase of diamine oxidase-histaminase(EC 1.4.3.6.)	Heparin	0-7	amine oxidase copper containing 1	Homo sapiens	28-43
4121438-0	1973	Heparin-induced increase of diamine oxidase-histaminase(EC 1.4.3.6.)	Heparin	0-7	amine oxidase copper containing 1	Homo sapiens	44-55
2983432-4	1985	Likewise, this heparin-induced release of PF4 is dependent upon the type of heparin used; low molecular weight heparin fractions and fragments do not cause the PF4 rebound seen with intact heparin.	Heparin	76-83	platelet factor 4	Homo sapiens	42-45
32699853-3	2020	In vitro, binding of ACE2 and heparin to spike protein ectodomains occurs independently and a ternary complex can be generated using heparin as a template.	Heparin	133-140	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	41-46
32699853-5	2020	Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus.	Heparin	15-22	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	131-136
3915615-2	1985	Besides ETO there must be other substances involved which are not extractable from the dialyzer (e.g. heparin).	Heparin	102-109	RUNX1 partner transcriptional co-repressor 1	Homo sapiens	8-11
32699853-5	2020	Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus.	Heparin	15-22	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	170-175
32699853-5	2020	Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	131-136
32699853-5	2020	Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	170-175
32699853-5	2020	Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	131-136
32699853-5	2020	Unfractionated heparin, non-anticoagulant heparin, treatment with heparin lyases, and purified lung heparan sulfate potently block spike protein binding and infection by spike protein-pseudotyped virus and SARS-CoV-2 virus.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	170-175
4282511-0	1972	[Complex compounds of plasminogen with heparin (PGH) and plasmin with heparin (PH) and their importance in regulating the liquid state of the blood].	Heparin	39-46	plasminogen	Homo sapiens	22-29
4282511-0	1972	[Complex compounds of plasminogen with heparin (PGH) and plasmin with heparin (PH) and their importance in regulating the liquid state of the blood].	Heparin	70-77	plasminogen	Homo sapiens	22-29
32697931-0	2020	Detection of anti-heparin-PF4 complex antibodies in COVID-19 patients on heparin therapy.	Heparin	18-25	platelet factor 4	Homo sapiens	26-29
32697931-0	2020	Detection of anti-heparin-PF4 complex antibodies in COVID-19 patients on heparin therapy.	Heparin	73-80	platelet factor 4	Homo sapiens	26-29
32187355-5	2020	Induction of FXa activity by ICs containing IgG antibodies to platelet factor 4 (PF4) involved in heparin-induced thrombocytopenia (HIT), beta-2-glycoprotein-1 implicated in antiphospholipid syndrome, or red blood cells coated with anti-(alpha)-Rh(D) antibodies that mediate hemolysis in vivo was inhibited by a humanized monoclonal antibody (mAb) that blocks IgG binding to human FcRn.	Heparin	98-105	platelet factor 4	Homo sapiens	81-84
5445687-2	1970	The isolation of human plasma prekallikrein was achieved by fractionating human plasma on diethylaminoethyl cellulose (DEAE) in the presence of heparin.2.	Heparin	144-151	kallikrein B1	Homo sapiens	23-43
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	40-47	serpin family D member 1	Homo sapiens	69-74
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	40-47	serpin family D member 1	Homo sapiens	139-144
4979841-0	1969	Release of diamine oxidase by heparin in the rat.	Heparin	30-37	amine oxidase, copper containing 1	Rattus norvegicus	11-26
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	69-74
33043139-2	2020	Fibroblast Growth Factor-2 (FGF-2) and Vascular Endothelial Growth Factor-A (VEGF-A) induce hemorrhage in murine models with heparin exposure.	Heparin	125-132	fibroblast growth factor 2	Mus musculus	0-26
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	139-144
33043139-2	2020	Fibroblast Growth Factor-2 (FGF-2) and Vascular Endothelial Growth Factor-A (VEGF-A) induce hemorrhage in murine models with heparin exposure.	Heparin	125-132	fibroblast growth factor 2	Mus musculus	28-33
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	69-74
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	139-144
6523432-0	1984	Clearance and in vivo release by heparin of human platelet factor 4 (PF4) in the rabbit.	Heparin	33-40	platelet factor 4	Homo sapiens	50-67
32302701-3	2020	In this study, we evaluated if heparin prevents early brain injury (EBI) after subarachnoid hemorrhage (SAH) by anti-apoptotic mechanisms including SphK1.	Heparin	31-38	sphingosine kinase 1	Mus musculus	148-153
32302701-7	2020	RESULTS: Low-dose heparin posttreatment improved neurobehavioral function, brain edema, blood-brain barrier disruption and death in the cortex, associated with an increase in SphK1 and phosphorylated Akt, and a decrease in cleaved caspase-3.	Heparin	18-25	sphingosine kinase 1	Mus musculus	175-180
14328967-0	1965	USE OF HEPARIN IN DISTINGUISHING PLASMA KALLIKREIN FROM PF/DIL.	Heparin	7-14	kallikrein B1	Homo sapiens	33-50
6523432-5	1984	of heparin 30 min after PF4 administration induced a partial release of the injected protein and its clearance from plasma was slow, with half-life of 23.3 +/- 5.9 min and 30.9 +/- 2.19 min respectively.	Heparin	3-10	platelet factor 4	Homo sapiens	24-27
13950275-0	1963	Protamine-heparin complex as a substrate for plasmin.	Heparin	10-17	plasminogen	Homo sapiens	45-52
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	21-28	bone morphogenetic protein 2	Homo sapiens	162-166
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	21-28	bone morphogenetic protein 2	Homo sapiens	317-322
6466689-0	1984	Post-heparin plasma hepatic triacylglycerol lipase-catalyzed hydrolysis of tributyrin.	Heparin	5-12	lipase C, hepatic type	Homo sapiens	20-50
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	102-109	matrix metallopeptidase 2	Homo sapiens	58-62
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	102-109	bone morphogenetic protein 2	Homo sapiens	162-166
33463282-7	2020	The LZ backbone with heparin-binding domain containing an MMP2 cleavage site facilitated tethering of heparin-binding growth factors, such as VEGF, TGF-beta1 and BMP2 and demonstrated controlled release of these active growth factor both in vitro and in vivo and demonstrated growth factor specific activity in vivo (BMP-2 and TGF-beta1).	Heparin	102-109	bone morphogenetic protein 2	Homo sapiens	317-322
6466689-2	1984	The mechanism of action of hepatic triacylglycerol lipase (EC 3.1.1.3) was examined by comparing the hydrolysis of a water-soluble substrate, tributyrin, with that of triolein by hepatic triacylglycerol lipase purified from human post-heparin plasma.	Heparin	235-242	lipase C, hepatic type	Homo sapiens	27-57
6330250-4	1984	N-Acetyl-beta-D-glucosaminidase was previously shown to be exquisitely sensitive to small amounts of heparin; paradoxically, larger amounts restore activity.	Heparin	101-108	O-GlcNAcase	Homo sapiens	0-31
31879779-0	2020	Heparin induces neutrophil elastase-dependent vital and lytic NET formation.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	16-35
34051613-3	2021	However, anti-SARS-CoV-2 adenoviral-vectored-DNA vaccines -initially shown for the ChAdOx1 vaccine-may rarely exhibit autoimmunity with autoantibodies to Platelet Factor-4 (PF4) that is termed Vaccine-Induced Thrombotic Thrombocytopenia (VITT), an entity pathophysiologically similar to Heparin-Induced Thrombocytopenia (HIT).	Heparin	287-294	platelet factor 4	Homo sapiens	173-176
34051613-4	2021	The PF4 autoantigen is a polyanion molecule capable of independent interactions with negatively charged bacterial cellular wall, heparin and DNA molecules, thus linking intravascular innate immunity to both bacterial cell walls and pathogen-derived DNA.	Heparin	129-136	platelet factor 4	Homo sapiens	4-7
34051613-10	2021	Hence, electrochemical DNA-PF4 interactions and PF4-heparin interactions, but at different locations, represent the common denominator in HIT and VITT related autoimmune-mediated thrombosis.	Heparin	52-59	platelet factor 4	Homo sapiens	48-51
34056422-0	2021	Sulfonated Nonsaccharide Heparin Mimetics Are Potent and Noncompetitive Inhibitors of Human Neutrophil Elastase.	Heparin	25-32	elastase, neutrophil expressed	Homo sapiens	92-111
32523960-1	2020	Background: Fibroblast growth factors (FGFs) are heparin-binding proteins involved in a variety of biological processes, and part of them may act through binding with cell membrane receptor FGFR2.	Heparin	49-56	fibroblast growth factor receptor 2	Mus musculus	190-195
6323392-4	1984	The inhibition of activated protein C by plasma protein C inhibitor was also accelerated by heparin.	Heparin	92-99	serpin family A member 5	Homo sapiens	48-67
32228920-6	2020	The interaction between SDF-1 and heparin could sustain SDF-1 release, which has been shown to enhance human umbilical vein endothelial cell (HUVEC) 2D/3D migration.	Heparin	34-41	C-X-C motif chemokine ligand 12	Homo sapiens	56-61
31998886-6	2020	Further, heparin and the heparin-binding angiogenic factors VEGF, FGF-2 and CXCL12 were immobilized onto the peptide in a modular assembly.	Heparin	25-32	C-X-C motif chemokine ligand 12	Homo sapiens	76-82
31998886-8	2020	In subsequent investigations, peptide-heparin-complexes loaded with CXCL12 or VEGF had an additional increasing effect on cell viability, differentiation and migration.	Heparin	38-45	C-X-C motif chemokine ligand 12	Homo sapiens	68-74
33550713-1	2021	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe adverse reaction to heparin caused by heparin-dependent, platelet activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	12-19	platelet factor 4	Homo sapiens	164-167
33550713-1	2021	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe adverse reaction to heparin caused by heparin-dependent, platelet activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	83-90	platelet factor 4	Homo sapiens	164-167
33550713-1	2021	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe adverse reaction to heparin caused by heparin-dependent, platelet activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	101-108	platelet factor 4	Homo sapiens	164-167
33550713-1	2021	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe adverse reaction to heparin caused by heparin-dependent, platelet activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	101-108	platelet factor 4	Homo sapiens	164-167
31891520-1	2020	Published studies indicate that TMEM184A is a heparin receptor that interacts with and transduces stimulation from heparin in vascular cells.	Heparin	46-53	transmembrane protein 184A	Rattus norvegicus	32-40
6198531-8	1984	The therapeutic effects of heparin were assessed by prolonged APTT (45-250 sec) and elevated Anti-FXa activity (0.2-1.2 u/ml of plasma heparin concentration) as an indicator for the evaluation of anticoagulation activity and by normalized FPA, Fbg, FDP, Plg and AT III as an indicator for evaluation of antithrombolic activity.	Heparin	27-34	plasminogen	Homo sapiens	254-257
31891520-1	2020	Published studies indicate that TMEM184A is a heparin receptor that interacts with and transduces stimulation from heparin in vascular cells.	Heparin	115-122	transmembrane protein 184A	Rattus norvegicus	32-40
31891520-7	2020	eNOS can be immunoprecipitated with TMEM184A and is internalized to the perinuclear region in a TMEM184A-dependent manner in response to heparin.	Heparin	137-144	transmembrane protein 184A	Rattus norvegicus	36-44
31891520-7	2020	eNOS can be immunoprecipitated with TMEM184A and is internalized to the perinuclear region in a TMEM184A-dependent manner in response to heparin.	Heparin	137-144	transmembrane protein 184A	Rattus norvegicus	96-104
31891520-8	2020	We also examined how heparin treatment leads to phosphorylation of eNOS and confirmed that TMEM184A and Ca2+ were required to mediate heparin-elicited eNOS phosphorylation.	Heparin	21-28	transmembrane protein 184A	Rattus norvegicus	91-99
31891520-8	2020	We also examined how heparin treatment leads to phosphorylation of eNOS and confirmed that TMEM184A and Ca2+ were required to mediate heparin-elicited eNOS phosphorylation.	Heparin	134-141	transmembrane protein 184A	Rattus norvegicus	91-99
33607500-0	2021	Binding of the human antioxidation protein alpha1-microglobulin (A1M) to heparin and heparan sulfate.	Heparin	73-80	alpha-1-microglobulin/bikunin precursor	Homo sapiens	65-68
33607500-5	2021	In this work, it was shown that A1M binds to heparin and HS and can be purified from human plasma by heparin affinity chromatography and size exclusion chromatography.	Heparin	45-52	alpha-1-microglobulin/bikunin precursor	Homo sapiens	32-35
33607500-5	2021	In this work, it was shown that A1M binds to heparin and HS and can be purified from human plasma by heparin affinity chromatography and size exclusion chromatography.	Heparin	101-108	alpha-1-microglobulin/bikunin precursor	Homo sapiens	32-35
33607500-7	2021	Potential heparin binding sites, located on the outside of the barrel-shaped A1M molecule, were determined using hydrogen deuterium exchange mass spectrometry (HDX-MS).	Heparin	10-17	alpha-1-microglobulin/bikunin precursor	Homo sapiens	77-80
33968948-8	2021	Moreover, heparin may present anti-SARS-CoV-2 potential once it can impact viral infectivity and alter SARS-CoV-2 Spike protein architecture.	Heparin	10-17	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	114-119
6639055-0	1983	The comparative kinetics of soluble and heparin-Sepharose-immobilized bovine lipoprotein lipase.	Heparin	40-47	lipoprotein lipase	Bos taurus	77-95
33857630-2	2021	An underlying immunological mechanism similar to that of spontaneous heparin-induced thrombocytopenia (HIT) is suspected, with the identification of antibodies to platelet factor-4 (PF4), but without previous heparin exposure.	Heparin	69-76	platelet factor 4	Homo sapiens	163-180
33857630-2	2021	An underlying immunological mechanism similar to that of spontaneous heparin-induced thrombocytopenia (HIT) is suspected, with the identification of antibodies to platelet factor-4 (PF4), but without previous heparin exposure.	Heparin	69-76	platelet factor 4	Homo sapiens	182-185
31944769-10	2020	Complexes formed between lyophilized PF4 and heparin were bigger and en-hanced binding of aPF4/H Abs in EIA compared to complexes between non-lyophilized PF4 and heparin, both in HBSS and PBS and may strongly influence in vitro test results.	Heparin	45-52	platelet factor 4	Homo sapiens	91-94
31944769-10	2020	Complexes formed between lyophilized PF4 and heparin were bigger and en-hanced binding of aPF4/H Abs in EIA compared to complexes between non-lyophilized PF4 and heparin, both in HBSS and PBS and may strongly influence in vitro test results.	Heparin	162-169	platelet factor 4	Homo sapiens	37-40
6639055-2	1983	Hence kinetic parameters of S-LPL and heparin-Sepharose-immobilized LPL (B-LPL) were compared.	Heparin	38-45	lipoprotein lipase	Bos taurus	68-71
6639055-6	1983	Dixon plots of experiments with S-LPL indicated that heparin is a competitive inhibitor against both C-II and TG, and that the binding of either C-II or heparin to the enzyme is a mutually exclusive event.	Heparin	53-60	lipoprotein lipase	Bos taurus	34-37
31573759-9	2020	Upon complexation with PF4, 6-mer and S12-mer heparins showed much lower enthalpy, induced less conformational changes in PF4, and interacted with weaker forces than 8-, 10-, and 12-mer heparins.	Heparin	46-54	platelet factor 4	Homo sapiens	23-26
6639055-8	1983	From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate.	Heparin	63-70	lipoprotein lipase	Bos taurus	59-62
31573759-9	2020	Upon complexation with PF4, 6-mer and S12-mer heparins showed much lower enthalpy, induced less conformational changes in PF4, and interacted with weaker forces than 8-, 10-, and 12-mer heparins.	Heparin	46-54	platelet factor 4	Homo sapiens	122-125
31573759-9	2020	Upon complexation with PF4, 6-mer and S12-mer heparins showed much lower enthalpy, induced less conformational changes in PF4, and interacted with weaker forces than 8-, 10-, and 12-mer heparins.	Heparin	186-194	platelet factor 4	Homo sapiens	23-26
31573759-10	2020	Anti-PF4/heparin antibodies bind more weakly to complexes formed between PF4 and heparins <= 8-mer than with complexes formed between PF4 and heparins >= 10-mer.	Heparin	81-89	platelet factor 4	Homo sapiens	5-8
31573759-10	2020	Anti-PF4/heparin antibodies bind more weakly to complexes formed between PF4 and heparins <= 8-mer than with complexes formed between PF4 and heparins >= 10-mer.	Heparin	81-89	platelet factor 4	Homo sapiens	73-76
31573759-10	2020	Anti-PF4/heparin antibodies bind more weakly to complexes formed between PF4 and heparins <= 8-mer than with complexes formed between PF4 and heparins >= 10-mer.	Heparin	81-89	platelet factor 4	Homo sapiens	73-76
31573759-10	2020	Anti-PF4/heparin antibodies bind more weakly to complexes formed between PF4 and heparins <= 8-mer than with complexes formed between PF4 and heparins >= 10-mer.	Heparin	142-150	platelet factor 4	Homo sapiens	5-8
33878212-0	2021	False-positive heparin-PF4 latex immunoturbidimetric assay due to lupus anti-coagulant interference: a case report.	Heparin	15-22	platelet factor 4	Homo sapiens	23-26
33877737-8	2021	Blood test revealed platelet factor 4 (PF-4) reactive antibodies, imitating what is seen in heparin-induced thrombocytopenia.	Heparin	92-99	platelet factor 4	Homo sapiens	39-43
6639055-8	1983	From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate.	Heparin	63-70	lipoprotein lipase	Bos taurus	171-174
32191827-4	2020	The purpose of this study was to report the frequency of VTE and ICH progression after initiation of PTP with a continuous infusion of unfractionated heparin in patients with moderate to severe TBI, and to identify risk factors associated with development of VTE.	Heparin	150-157	protein tyrosine phosphatase receptor type U	Homo sapiens	101-104
6639055-8	1983	From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate.	Heparin	63-70	lipoprotein lipase	Bos taurus	171-174
33515654-5	2021	While, the orexin-A-induced potentiation was blocked when Ca2+ was chelated by internal infusion of BAPTA, and the orexin-A effect was abolished by the IP3 receptor antagonists heparin and Xe-C.	Heparin	177-184	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	152-164
6639055-8	1983	From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate.	Heparin	142-149	lipoprotein lipase	Bos taurus	59-62
6639055-8	1983	From the Dixon plots, the dissociation constant Ki for the LPL:heparin binary complex was determined to be 5.0 X 10(-8) M. In contrast to the heparin inhibitory effect on LPL activity against triolein, heparin had no effect on the esterase activity of LPL against p-nitrophenylacetate or p-nitrophenylbutyrate.	Heparin	142-149	lipoprotein lipase	Bos taurus	59-62
6639055-10	1983	It is concluded that most of the LPL bound to heparin-Sepharose is probably inaccessible to substrate, hence a low Vmax.	Heparin	46-53	lipoprotein lipase	Bos taurus	33-36
6639055-11	1983	However, Km (C-II) and Km (TG) were higher for B-LPL due to the competitive inhibitory effect of heparin on LPL.	Heparin	97-104	lipoprotein lipase	Bos taurus	47-52
31809536-1	2019	Activation of the platelet Fc-receptor CD32a (FcgammaRIIA) is an early and crucial step in the pathogenesis of heparin-induced thrombocytopenia type II (HIT) that has not been therapeutically targeted.	Heparin	111-118	Fc gamma receptor IIa	Homo sapiens	39-44
6639055-11	1983	However, Km (C-II) and Km (TG) were higher for B-LPL due to the competitive inhibitory effect of heparin on LPL.	Heparin	97-104	lipoprotein lipase	Bos taurus	49-52
31809536-1	2019	Activation of the platelet Fc-receptor CD32a (FcgammaRIIA) is an early and crucial step in the pathogenesis of heparin-induced thrombocytopenia type II (HIT) that has not been therapeutically targeted.	Heparin	111-118	Fc gamma receptor IIa	Homo sapiens	46-57
33409509-4	2021	To address this challenge, biomaterials that strongly bind BMP-2, such as heparin methacrylamide microparticles (HMPs), may be used to limit exposure and spatially constrain proteins within the injury site.	Heparin	74-81	bone morphogenetic protein 2	Homo sapiens	59-64
6639055-12	1983	Consistent with these kinetic analyses and with the use of human very low density lipoproteins (VLDL) as substrate, S-LPL, even in the presence of heparin, was found to have an apparent rate of lipolysis of VLDL approximately ninefold greater than B-LPL.	Heparin	147-154	lipoprotein lipase	Bos taurus	118-121
6352571-2	1983	It was proposed that this could reflect binding of PF4 to heparin or heparan sulphate, known granule constituents.	Heparin	58-65	platelet factor 4	Homo sapiens	51-54
33326124-1	2021	IgG-specific and polyspecific PF4-dependent enzyme-immunoassays (EIAs) have exceptionally high sensitivity (>=99%) for diagnosis of heparin-induced thrombocytopenia (HIT), a drug reaction caused by platelet-activating antibodies detectable by serotonin-release assay (SRA).	Heparin	132-139	platelet factor 4	Homo sapiens	30-33
31420311-2	2019	In 2010, she developed thrombotic thrombocytopenic purpura (TTP) (ADAMTS-13 &lt;5%, inhibitor at 1.0 BU/mL), which was treated successfully with corticotherapy, plasmapheresis, and intravenous heparin.	Heparin	193-200	SH3 domain binding protein 4	Homo sapiens	23-64
31898566-0	2019	[Effect of heparin on histone-mediated the expression of von Willebrand factor and fibrinogen in lung tissue].	Heparin	11-18	fibrinogen alpha chain	Mus musculus	83-93
6137972-4	1983	Purification procedure for TH involved chromatographies with DEAE-Sephacel, Bio-Gel A-1.5 m, and heparin-Sepharose.	Heparin	97-104	tyrosine hydroxylase	Rattus norvegicus	27-29
31898566-16	2019	The FIB mRNA expression of lung tissue in the histone group was about 49.82 times of the control group (2-DeltaDeltaCT: 55.30+-18.84 vs. 1.11+-0.45, P &lt; 0.01), and the expression of FIB mRNA in the histone+heparin group was decreased, which was 23.87 times of the control group (2-DeltaDeltaCT: 26.50+-9.97 vs. 1.11+-0.45, P &lt; 0.01), but it was significantly lower than that in the histone group (2-DeltaDeltaCT: 26.50+-9.97 vs. 55.30+-18.84, P &lt; 0.01), indicating that heparin could inhibit histone-induced hypercoagulable environment in lung.	Heparin	209-216	fibrinogen alpha chain	Mus musculus	4-7
31898566-16	2019	The FIB mRNA expression of lung tissue in the histone group was about 49.82 times of the control group (2-DeltaDeltaCT: 55.30+-18.84 vs. 1.11+-0.45, P &lt; 0.01), and the expression of FIB mRNA in the histone+heparin group was decreased, which was 23.87 times of the control group (2-DeltaDeltaCT: 26.50+-9.97 vs. 1.11+-0.45, P &lt; 0.01), but it was significantly lower than that in the histone group (2-DeltaDeltaCT: 26.50+-9.97 vs. 55.30+-18.84, P &lt; 0.01), indicating that heparin could inhibit histone-induced hypercoagulable environment in lung.	Heparin	479-486	fibrinogen alpha chain	Mus musculus	4-7
31215255-1	2019	Objective: Heparanase (HPA) is an endo-beta-D-glucuronidase capable of degrading heparin sulphate (HS) and heparin side chains.	Heparin	81-88	glucuronidase beta	Homo sapiens	39-59
31210206-8	2019	Sample 25 mM_4-1Hep with the highest loading amount of heparin was selected as carrier for BMP-2 and BMP-2 loaded CaCO3 microspheres were further entrapped in fibrin-glue hydrogel (FC-B).	Heparin	55-62	bone morphogenetic protein 2	Homo sapiens	91-96
31210206-8	2019	Sample 25 mM_4-1Hep with the highest loading amount of heparin was selected as carrier for BMP-2 and BMP-2 loaded CaCO3 microspheres were further entrapped in fibrin-glue hydrogel (FC-B).	Heparin	55-62	bone morphogenetic protein 2	Homo sapiens	101-106
33508081-3	2021	Heparin and a glycol-split low molecular weight heparin (gsHep) with low anticoagulant potency has been shown to enhance myometrial contraction and interleukin (IL)-8 production by cervical fibroblasts.	Heparin	0-7	chemokine (C-X-C motif) ligand 15	Mus musculus	148-166
33357843-3	2021	Several biochemical studies show strong binding of heparin and heparin-like molecules to the Spike protein, which resulted in inhibition of viral infection to cells.	Heparin	51-58	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	93-98
33357843-3	2021	Several biochemical studies show strong binding of heparin and heparin-like molecules to the Spike protein, which resulted in inhibition of viral infection to cells.	Heparin	63-70	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	93-98
33869655-5	2021	We also fused the heparin-binding (HB) domain from HB epidermal growth factor-like growth factor (HB-EGF) to LAMA2(G1-5) to test whether this would increase muscle ECM expression.	Heparin	18-25	laminin, alpha 2	Mus musculus	109-114
6224310-0	1983	Kinetic study of the effect of heparin on the amidase activity of trypsin, plasmin and urokinase.	Heparin	31-38	plasminogen	Homo sapiens	75-82
31121497-3	2019	Previous studies indicate that the p40 subunit of human and murine IL-12 is responsible for the heparin-binding activity of this heterodimeric cytokine.	Heparin	96-103	interleukin 9	Homo sapiens	35-38
33544386-1	2021	Connective tissue growth factor (CTGF), a matricellular protein of the CCN family of extracellular matrix-associated heparin-binding proteins, is highly expressed in various organ fibrosis and several malignant tumors.	Heparin	117-124	cellular communication network factor 2	Homo sapiens	0-31
6406546-3	1983	This study was designed to determine whether a provocative test for increasing the level of plasma DAO activity by heparin administration could be used to monitor the extent and severity of acute, severe, small intestinal mucosal injury.	Heparin	115-122	amine oxidase, copper containing 1	Rattus norvegicus	99-102
33544386-1	2021	Connective tissue growth factor (CTGF), a matricellular protein of the CCN family of extracellular matrix-associated heparin-binding proteins, is highly expressed in various organ fibrosis and several malignant tumors.	Heparin	117-124	cellular communication network factor 2	Homo sapiens	33-37
32812381-11	2021	Discordant changes of CRP and FVIII in plasma could contribute to aPTT/anti-Xa discrepancies observed during heparin therapy in the pediatric population.	Heparin	109-116	coagulation factor VIII	Homo sapiens	30-35
32892505-12	2021	tPA, TFPI and VEGF were increased in critical patients, which are hypothesized to reflect endothelial dysfunction and/or contribution of heparin (which may cause endothelial TFPI/tPA release).	Heparin	137-144	tissue factor pathway inhibitor	Homo sapiens	174-178
31107976-6	2019	42.2% (27/64) anti-PF4-heparin-negative samples were negative for anti-platelet and anti-RBC antibodies.	Heparin	23-30	platelet factor 4	Homo sapiens	19-22
6406546-9	1983	Our previous data have suggested that DAO is unique among intestinal mucosal enzymes in that circulating levels can serve as a marker of mucosal injury; this study illustrates that the addition of a low-dose heparin administration enhances the use of DAO even further as a sensitive, quantitative, circulating marker for monitoring the extent of small intestinal mucosal injury in the rat.	Heparin	208-215	amine oxidase, copper containing 1	Rattus norvegicus	38-41
31274032-1	2019	Introduction: Heparin-induced thrombocytopenia (HIT) is known for its strong association with thrombosis and distinct pathogenesis involving anti-PF4/polyanion antibodies that activate platelets strongly through clustering of platelet FcgammaIIa receptors.	Heparin	14-21	platelet factor 4	Homo sapiens	146-149
6406546-9	1983	Our previous data have suggested that DAO is unique among intestinal mucosal enzymes in that circulating levels can serve as a marker of mucosal injury; this study illustrates that the addition of a low-dose heparin administration enhances the use of DAO even further as a sensitive, quantitative, circulating marker for monitoring the extent of small intestinal mucosal injury in the rat.	Heparin	208-215	amine oxidase, copper containing 1	Rattus norvegicus	251-254
6838494-0	1983	Human neutrophil N-acetyl-beta-D-glucosaminidase: heparin inhibition.	Heparin	50-57	O-GlcNAcase	Homo sapiens	17-48
31009154-1	2019	Essentials At low pH and low salt concentrations: Maximal conformational change of PF4 upon complexation with heparin occurs.	Heparin	110-117	platelet factor 4	Homo sapiens	83-86
33579485-6	2021	Heparin liposomes (HLp) were formulated by solvent evaporation and extrusion process and possessed hydrodynamic diameter of 242 +- 4.3 nm.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	19-22
33579485-7	2021	Size, shape and surface morphology was confirmed by TEM, SEM and AFM micrographs while encapsulation efficiency and loading of heparin in optimized HLp were 59.61% and 12.27%, respectively.	Heparin	127-134	lipase C, hepatic type	Homo sapiens	148-151
33968333-7	2021	Docking studies using GlycoTorch Vina and subsequent MD simulations of the spike trimer in the presence of dodecasaccharides of the GAGs heparin and heparan sulfate supported this possibility.	Heparin	137-144	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	75-80
31009154-8	2019	METHODS: We investigated first the conformational change of PF4 when binding to heparin under various pH and salt conditions using circular dichroism spectroscopy, and then the binding of aPF4/H Abs to PF4/H complexes by EIA.	Heparin	80-87	platelet factor 4	Homo sapiens	60-63
31009154-9	2019	RESULTS: Maximal conformational change of PF4 on complexation with heparin was identified at low pH and low salt concentrations.	Heparin	67-74	platelet factor 4	Homo sapiens	42-45
6838494-1	1983	To determine N-acetyl-beta-D-glucosaminidase (EC 3.2.1.30) in human neutrophil granules separated by a method requiring heparin, the inhibition of this enzyme by heparin was studied.	Heparin	162-169	O-GlcNAcase	Homo sapiens	13-44
6838494-6	1983	Heparin was shown to reduce neutrophil lysate N-acetyl-beta-D-glucosaminidase to a specific activity of 46% at a heparin concentration of 2 units per assay and to 43% (maximal inhibition) at 17 and 50 units of heparin per assay.	Heparin	0-7	O-GlcNAcase	Homo sapiens	46-77
6838494-6	1983	Heparin was shown to reduce neutrophil lysate N-acetyl-beta-D-glucosaminidase to a specific activity of 46% at a heparin concentration of 2 units per assay and to 43% (maximal inhibition) at 17 and 50 units of heparin per assay.	Heparin	113-120	O-GlcNAcase	Homo sapiens	46-77
6838494-6	1983	Heparin was shown to reduce neutrophil lysate N-acetyl-beta-D-glucosaminidase to a specific activity of 46% at a heparin concentration of 2 units per assay and to 43% (maximal inhibition) at 17 and 50 units of heparin per assay.	Heparin	210-217	O-GlcNAcase	Homo sapiens	46-77
30412462-0	2019	Free PAPP-A as a biomarker: heparin-induced release is not related to coronary atherosclerotic burden.	Heparin	28-35	pappalysin 1	Homo sapiens	5-11
30771687-10	2019	UFH also protected TJs against lipopolysaccharide-stimulated damage and functioned upstream by inhibiting the ERK1/2 MAPK pathway to attenuate endothelial hyperpermeability and downregulating the expression of TJ proteins such as claudin-5, occludin, and ZO-1.	Heparin	0-3	claudin 5	Homo sapiens	230-239
30771687-10	2019	UFH also protected TJs against lipopolysaccharide-stimulated damage and functioned upstream by inhibiting the ERK1/2 MAPK pathway to attenuate endothelial hyperpermeability and downregulating the expression of TJ proteins such as claudin-5, occludin, and ZO-1.	Heparin	0-3	occludin	Homo sapiens	241-249
33596779-4	2021	Follow-up investigations indicated polyspecificity of ABT-736, including unintended high-affinity binding to monkey and human plasma protein platelet factor 4 (PF-4), known to be involved in heparin-induced thrombocytopenia (HIT) in humans.	Heparin	191-198	platelet factor 4	Homo sapiens	160-164
33362545-5	2020	For example, single-nucleotide polymorphisms (SNPs) in FGG, FGA, and F5 mediate increases in D-dimer and SNPs in ABO, CBS, CPS1 and MTHFR mediate differences in homocysteine levels, and SNPs in TDAG8 associate with Heparin-induced Thrombocytopenia.	Heparin	215-222	carbamoyl-phosphate synthase 1	Homo sapiens	123-127
33306320-13	2020	CONCLUSION: Although the incidence of HIT was low in patients undergoing open heart surgery, an increased rate of early mortality was observed in patients with positive heparin/PF4 antibodies.	Heparin	169-176	platelet factor 4	Homo sapiens	177-180
6838494-8	1983	Protamine sulfate was assessed for its ability to restore N-acetyl-beta-D-glucosaminidase activity in the presence of heparin.	Heparin	118-125	O-GlcNAcase	Homo sapiens	58-89
6838494-10	1983	These studies of human neutrophil N-acetyl-beta-D-glucosaminidase demonstrate: (1) specific enzyme activity is 28.8 +/- 7.0 nmole p-nitrophenol released per minute per milligram of protein or 1.7 +/- 0.5 nmole p-nitrophenol released per minute per 10(6) neutrophils; (2) heparin rapidly but finitely inhibits enzyme activity at very low concentrations and paradoxically restores it toward normal at high concentrations; and (3) protamine sulfate restores enzyme activity inhibited by heparin.	Heparin	271-278	O-GlcNAcase	Homo sapiens	34-65
30917957-0	2019	Cleavage of anti-PF4/heparin IgG by a bacterial protease and potential benefit in heparin-induced thrombocytopenia.	Heparin	82-89	platelet factor 4	Homo sapiens	17-20
30917957-1	2019	Heparin-induced thrombocytopenia (HIT) is due to immunoglobulin G (IgG) antibodies, which bind platelet factor 4 (PF4) modified by polyanions, such as heparin (H).	Heparin	0-7	platelet factor 4	Homo sapiens	114-117
33111388-9	2020	RESULTS: Plasma lipase activities, as measured using the DGGR-based assay, increased significantly 10 minutes after heparin administration in both cats (P = .003) and dogs (P = .006) and returned to baseline by 120 minutes.	Heparin	116-123	pancreatic lipase related protein 1	Canis lupus familiaris	16-22
30917957-1	2019	Heparin-induced thrombocytopenia (HIT) is due to immunoglobulin G (IgG) antibodies, which bind platelet factor 4 (PF4) modified by polyanions, such as heparin (H).	Heparin	151-158	platelet factor 4	Homo sapiens	114-117
6838494-10	1983	These studies of human neutrophil N-acetyl-beta-D-glucosaminidase demonstrate: (1) specific enzyme activity is 28.8 +/- 7.0 nmole p-nitrophenol released per minute per milligram of protein or 1.7 +/- 0.5 nmole p-nitrophenol released per minute per 10(6) neutrophils; (2) heparin rapidly but finitely inhibits enzyme activity at very low concentrations and paradoxically restores it toward normal at high concentrations; and (3) protamine sulfate restores enzyme activity inhibited by heparin.	Heparin	484-491	O-GlcNAcase	Homo sapiens	34-65
30917957-7	2019	In addition, incubating IdeS in whole blood containing 5B9 or HIT plasma samples led to cleavage of anti-PF4/H antibodies, which fully abolished the ability to induce heparin-dependent platelet aggregation and tissue factor messenger RNA synthesis by monocytes.	Heparin	167-174	platelet factor 4	Homo sapiens	105-108
6185522-5	1983	Removing PAPP-A-like material from seminal plasma by adsorbtion to heparin-Sepharose reduced the inhibitory effect of seminal plasma on phytohemagglutinin-induced lymphocyte transformation.	Heparin	67-74	pappalysin 1	Homo sapiens	9-15
30917957-10	2019	In conclusion, cleavage of anti-PF4/H IgG by IdeS abolishes heparin-dependent cellular activation induced by HIT antibodies.	Heparin	60-67	platelet factor 4	Homo sapiens	32-35
31023176-6	2019	The [Ca2+]i in Jurkat T cells significantly decreased after treatment with heparin as an inhibitor of inositol trisphosphate receptors (IP3 R), or procaine as an inhibitor of ryanodine receptors (RyR).	Heparin	75-82	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	136-141
34035190-4	2020	Subsequently, bFGF is loaded by binding to heparin.	Heparin	43-50	fibroblast growth factor 2	Mus musculus	14-18
34035190-5	2020	The loading yield of bFGF on heparin-immobilized PDA-coated PCL membrane significantly increases to around 7 times as compared with that of pure PCL membrane.	Heparin	29-36	fibroblast growth factor 2	Mus musculus	21-25
6838953-6	1983	It was found that immobilized heparin forms complexes with fibrinogen, thrombin and plasmin that produce lytic action on unstabilized fibrin.	Heparin	30-37	plasminogen	Homo sapiens	84-91
6190160-1	1983	An interaction between heparin and circulating pregnancy-associated plasma protein A (PAPP-A) has been observed.	Heparin	23-30	pappalysin 1	Homo sapiens	47-84
32970989-2	2020	Docking studies suggest a heparin/heparan sulfate-binding site adjacent to the ACE2-binding site.	Heparin	26-33	angiotensin converting enzyme 2	Homo sapiens	79-83
32970989-3	2020	Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold.	Heparin	14-21	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	48-53
30894640-4	2019	Here, we investigated the molecular interplay of MMP2 with different GAG (chondroitin sulfate, hyaluronan (HA), sulfated hyaluronan (SH) and heparin (HE)) and the impact of GAG on MMP2/TIMP3 complex formation using in vitro-experiments with human bone marrow stromal cells, in silico docking and molecular dynamics simulations.	Heparin	141-148	matrix metallopeptidase 2	Homo sapiens	49-53
6190160-1	1983	An interaction between heparin and circulating pregnancy-associated plasma protein A (PAPP-A) has been observed.	Heparin	23-30	pappalysin 1	Homo sapiens	86-92
32970989-3	2020	Both ACE2 and heparin can bind independently to spike protein in vitro, and a ternary complex can be generated using heparin as a scaffold.	Heparin	117-124	angiotensin converting enzyme 2	Homo sapiens	5-9
32970989-4	2020	Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2.	Heparin	52-59	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	24-29
6190160-3	1983	In the presence of heparin, crossed immunoelectrophoretic analysis revealed an alteration in the electrophoretic mobility of PAPP-A, while a significant increase (22 to 64 per cent, P less than 0.02) in measured levels of PAPP-A was seen in electroimmunoassays.	Heparin	19-26	pappalysin 1	Homo sapiens	125-131
32970989-4	2020	Electron micrographs of spike protein suggests that heparin enhances the open conformation of the RBD that binds ACE2.	Heparin	52-59	angiotensin converting enzyme 2	Homo sapiens	113-117
32970989-6	2020	Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus.	Heparin	15-22	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	107-112
32970989-6	2020	Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	107-112
32970989-6	2020	Unfractionated heparin, non-anticoagulant heparin, heparin lyases, and lung heparan sulfate potently block spike protein binding and/or infection by pseudotyped virus and authentic SARS-CoV-2 virus.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	107-112
30862915-8	2019	The heparin chains allowed us to load the scaffolds with TGF-beta1, which induced cartilage-like matrix deposition both in vitro and in vivo in a subcutaneous mouse model.	Heparin	4-11	transforming growth factor, beta 1	Mus musculus	57-66
30850576-1	2019	BACKGROUND Autoimmune heparin-induced thrombocytopenia (aHIT) refers to a condition, in which antiplatelet factor-4 (PF4) antibodies activate platelets even in the absence of heparin (heparin independent platelet activation).	Heparin	22-29	platelet factor 4	Homo sapiens	117-120
6190160-3	1983	In the presence of heparin, crossed immunoelectrophoretic analysis revealed an alteration in the electrophoretic mobility of PAPP-A, while a significant increase (22 to 64 per cent, P less than 0.02) in measured levels of PAPP-A was seen in electroimmunoassays.	Heparin	19-26	pappalysin 1	Homo sapiens	222-228
32829146-6	2020	In these hydrogels, PEG provides the needed structural and mechanical properties, whereas heparin is used as an anchor for the cytokine CCL21, which is present in the lymph nodes, and can affect cell migration and proliferation.	Heparin	90-97	C-C motif chemokine ligand 21	Homo sapiens	136-141
6123557-7	1982	Heparin and NaCl activated native TH at pH 6.0, but not at pH 7.0.	Heparin	0-7	tyrosine hydroxylase	Bos taurus	34-36
30418682-2	2019	Heparin released during mast cell degranulation in the gastrointestinal tract might liberate DAO from heparin-sensitive storage sites.	Heparin	0-7	amine oxidase copper containing 1	Homo sapiens	93-96
30418682-2	2019	Heparin released during mast cell degranulation in the gastrointestinal tract might liberate DAO from heparin-sensitive storage sites.	Heparin	102-109	amine oxidase copper containing 1	Homo sapiens	93-96
30418682-9	2019	CONCLUSION: During severe anaphylaxis in mastocytosis patients, DAO is likely released from heparin-sensitive gastrointestinal storage sites.	Heparin	92-99	amine oxidase copper containing 1	Homo sapiens	64-67
32348723-1	2020	Association of platelet factor 4 (PF4) with heparin is a first step in formation of aggregates implicated in the development of heparin-induced thrombocytopenia (HIT), a potentially fatal immune disorder affecting 1-5% of patients receiving heparin.	Heparin	44-51	platelet factor 4	Homo sapiens	34-37
6123557-8	1982	Phosphorylated TH was unaffected by heparin or salt at pH 6.0, but was relatively inhibited at pH 7.0.	Heparin	36-43	tyrosine hydroxylase	Bos taurus	15-17
32348723-1	2020	Association of platelet factor 4 (PF4) with heparin is a first step in formation of aggregates implicated in the development of heparin-induced thrombocytopenia (HIT), a potentially fatal immune disorder affecting 1-5% of patients receiving heparin.	Heparin	128-135	platelet factor 4	Homo sapiens	34-37
32348723-1	2020	Association of platelet factor 4 (PF4) with heparin is a first step in formation of aggregates implicated in the development of heparin-induced thrombocytopenia (HIT), a potentially fatal immune disorder affecting 1-5% of patients receiving heparin.	Heparin	128-135	platelet factor 4	Homo sapiens	34-37
30017992-16	2019	This variant is expected to generate a truncated FGF14 protein lacking the heparin binding sites, those are likely to modify the activity of FGF14.	Heparin	75-82	fibroblast growth factor 14	Homo sapiens	49-54
6214868-7	1982	We have demonstrated the presence of PF4 on the vascular endothelium, and suggest that this is the immediate source of the PF4 released by heparin, though it is probably initially derived from platelets.	Heparin	139-146	platelet factor 4	Homo sapiens	123-126
30017992-16	2019	This variant is expected to generate a truncated FGF14 protein lacking the heparin binding sites, those are likely to modify the activity of FGF14.	Heparin	75-82	fibroblast growth factor 14	Homo sapiens	141-146
32348723-2	2020	Despite being a critically important element in HIT etiology, relatively little is known about the specific molecular mechanism of PF4-heparin interactions.	Heparin	135-142	platelet factor 4	Homo sapiens	131-134
32348723-3	2020	This work uses native mass spectrometry to investigate PF4 interactions with relatively short heparin chains (up to decasaccharides).	Heparin	94-101	platelet factor 4	Homo sapiens	55-58
32348723-8	2020	Similar results are obtained for PF4 association with longer and structurally heterogeneous heparin oligomers (decamers).	Heparin	92-99	platelet factor 4	Homo sapiens	33-36
32348723-9	2020	These longer polyanions can also induce PF4 dimer assembly when bound to the protein in relatively low numbers, lending support to a model of PF4/heparin interaction in which the latter wraps around the protein, making contacts with multiple subunits.	Heparin	146-153	platelet factor 4	Homo sapiens	40-43
7046999-1	1982	Recent evidence has suggested that the major physiological substrate of the heparin-releasable (postheparin plasma) hepatic lipase is HDL2-phospholipid.	Heparin	76-83	lipase C, hepatic type	Homo sapiens	116-130
32348723-9	2020	These longer polyanions can also induce PF4 dimer assembly when bound to the protein in relatively low numbers, lending support to a model of PF4/heparin interaction in which the latter wraps around the protein, making contacts with multiple subunits.	Heparin	146-153	platelet factor 4	Homo sapiens	142-145
33019549-7	2020	However, digitonin and heparin stimulated the conversion of PrP 91-104 into PrPSc 91-104 even after incubation with RML- and 22L-PrPSc-prions.	Heparin	23-30	prion protein	Mus musculus	76-81
33019549-7	2020	However, digitonin and heparin stimulated the conversion of PrP 91-104 into PrPSc 91-104 even after incubation with RML- and 22L-PrPSc-prions.	Heparin	23-30	prion protein	Mus musculus	129-134
33019549-8	2020	These results suggest that residues 91-106 or 91-104 of PrPC are crucially involved in prion pathogenesis in a strain-dependent manner and may play a similar role to digitonin and heparin in the conversion of PrPC into PrPSc.	Heparin	180-187	prion protein	Mus musculus	56-60
30582672-0	2019	Characterization of platelet factor 4 amino acids that bind pathogenic antibodies in heparin-induced thrombocytopenia.	Heparin	85-92	platelet factor 4	Homo sapiens	20-37
30582672-10	2019	Each PF4 mutant was used in an enzyme immunoassay (EIA) to test their capacity to bind a platelet-activating murine monoclonal anti-PF4/heparin antibody (KKO) and HIT patient sera (n = 9).	Heparin	136-143	platelet factor 4	Homo sapiens	5-8
30612329-1	2019	A high frequency of PF4-ELISA testing in patients suspected to have heparin-induced thrombocytopenia (HIT) despite low 4T scores has been observed in multiple medical centers.	Heparin	68-75	platelet factor 4	Homo sapiens	20-23
33019549-8	2020	These results suggest that residues 91-106 or 91-104 of PrPC are crucially involved in prion pathogenesis in a strain-dependent manner and may play a similar role to digitonin and heparin in the conversion of PrPC into PrPSc.	Heparin	180-187	prion protein	Mus musculus	209-213
7046999-1	1982	Recent evidence has suggested that the major physiological substrate of the heparin-releasable (postheparin plasma) hepatic lipase is HDL2-phospholipid.	Heparin	76-83	junctophilin 3	Homo sapiens	134-138
33019549-8	2020	These results suggest that residues 91-106 or 91-104 of PrPC are crucially involved in prion pathogenesis in a strain-dependent manner and may play a similar role to digitonin and heparin in the conversion of PrPC into PrPSc.	Heparin	180-187	prion protein	Mus musculus	219-224
32688092-3	2020	The loading efficiency of growth factors into these biomaterials was found to be >90%, revealing a strong affinity of VEGF and BMP-2 to heparin and alginate.	Heparin	136-143	bone morphogenetic protein 2	Homo sapiens	127-132
30085261-1	2019	Background: The PIFA PLUSS PF4 Rapid Assay (PIFA) is a rapid screening test used for the diagnosis of heparin-induced thrombocytopenia (HIT).	Heparin	102-109	platelet factor 4	Homo sapiens	27-30
30569872-0	2019	The Inhibition of Polysialyltranseferase ST8SiaIV Through Heparin Binding to Polysialyltransferase Domain (PSTD).	Heparin	58-65	ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4	Homo sapiens	41-49
30569872-4	2019	Heparin has been found to be effective in inhibiting the ST8Sia IV activity, but no clear molecular rationale.	Heparin	0-7	ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4	Homo sapiens	57-66
7076131-6	1982	The same fragment also formed during prolonged digestion of a previously described cathepsin D-derived heparin-binding piece of Mr 140000 which consisted of disulfide-linked chains of Mr 65000 and Mr 75000.	Heparin	103-110	cathepsin D	Homo sapiens	83-94
30309891-11	2018	These studies demonstrate that variability in plasma IgM levels correlates with functional complement responses to PF4/heparin.	Heparin	119-126	platelet factor 4	Homo sapiens	115-118
29956017-9	2018	These results demonstrated that heparin impairs CLG by reducing VEGFR2 activation.	Heparin	32-39	kinase insert domain protein receptor	Mus musculus	64-70
32460635-5	2020	In this AuNP-PMS/FGF2 composite, PMS, playing as the high-active mimic of heparin/heparan sulfate (HS), is covalently anchored to AuNPs and bound with FGF2 on the surface of nanoparticles, forming a HS/FGF2 complex nanomimics to facilitate its binding to FGF receptor (FGFR) and promote high neural-inductive activity of mESCs.	Heparin	74-81	fibroblast growth factor 2	Mus musculus	151-155
32102014-0	2020	Potential and Limitations of the New P2Y12 Inhibitor, Cangrelor, in Preventing Heparin-Induced Platelet Aggregation During Cardiac Surgery: An In Vitro Study.	Heparin	79-86	purinergic receptor P2Y12	Homo sapiens	37-42
6800421-10	1982	The ability of heparin to induce precipitation of CIg while leaving most VIII:C activity in the supernatant plasma may be useful in the preparation of procoagulant-rich plasma subfractions, since VIII:C can subsequently be recovered in good yield by cryoprecipitation.	Heparin	15-22	cytochrome c oxidase subunit 8A	Homo sapiens	73-77
7059522-6	1982	In an activated partial thromboplastin time test system the anticoagulant activity of 1.0 mg S-Lim corresponded to about 40 iu of heparin.	Heparin	130-137	PDZ and LIM domain 5	Homo sapiens	95-98
32277030-6	2020	Examination of the promoter regions of all genes involved in heparin/heparan sulfate assembly uncovered a transcription factor-binding motif for ZNF263, a C2H2 zinc finger protein.	Heparin	61-68	zinc finger protein 263	Sus scrofa	145-151
32277030-7	2020	CRISPR-mediated targeting and siRNA knockdown of ZNF263 in mammalian cell lines and human primary cells led to dramatically increased expression levels of HS3ST1, a key enzyme involved in imparting anticoagulant activity to heparin, and HS3ST3A1, another glucosaminyl 3-O-sulfotransferase expressed in cells.	Heparin	224-231	heparan sulfate-glucosamine 3-sulfotransferase 1	Homo sapiens	155-161
30194803-10	2018	Results Mouse TFPI and human TFPI are similar in regard to: (i) the mechanisms for FVIIa/TF and FXa inhibition; (ii) TFPIalpha is a soluble form and TFPIbeta is glycosyl phosphatidyl inositol (GPI) membrane anchored; (iii) the predominant circulating form of TFPI in plasma is lipoprotein-associated; (iv) low levels of TFPIalpha circulate in plasma and increase following heparin treatment; and (v) TFPIalpha is the isoform in platelets.	Heparin	373-380	tissue factor pathway inhibitor	Homo sapiens	29-33
7314590-4	1981	Administration of heparin into the patients was responsible for an increase in the level of unsaturated phospholipids in HDL2 fraction (while they decreased in VLDL/as well as for a decrease in the ratio cholesterol/phospholipids.	Heparin	18-25	junctophilin 3	Homo sapiens	121-125
30273811-1	2018	Heparin-induced thrombocytopenia (HIT) is caused by antibodies targeting platelet factor 4 (PF4)/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	92-95
32344682-1	2020	Heparin-induced thrombocytopenia (HIT) is a prothrombotic immune drug reaction caused by platelet-activating antibodies that in most instances recognize platelet factor 4 (PF4)/polyanion complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	172-175
7261547-2	1981	Significant positive correlations were found between the lipoprotein lipase and hepatic lipase activities of post-heparin plasma samples and plasma high-density-lipoprotein (HDL) cholesterol concentrations in 21 children with hyperlipidaemia and six normal adult males.	Heparin	114-121	lipase C, hepatic type	Homo sapiens	80-94
32107314-9	2020	Of note, heparin increased the anti-inflammatory markers arginase 1 (ARG1) and interleukin-10 (IL-10) in murine BMDMs.	Heparin	9-16	arginase, liver	Mus musculus	57-67
32107314-9	2020	Of note, heparin increased the anti-inflammatory markers arginase 1 (ARG1) and interleukin-10 (IL-10) in murine BMDMs.	Heparin	9-16	arginase, liver	Mus musculus	69-73
32091872-3	2020	In this study, an innovative and efficient fibrin glue/fibronectin/heparin (FG/Fn/Hep)-based delivery system was developed for controlled release of BMP2.	Heparin	67-74	histocompatibility 51	Mus musculus	82-85
33435067-0	2018	Controlled Release of BMP-2 from a Heparin-Conjugated Strontium-Substituted Nanohydroxyapatite/Silk Fibroin Scaffold for Bone Regeneration.	Heparin	35-42	bone morphogenetic protein 2	Homo sapiens	22-27
33435067-1	2018	The objective of this study was to develop heparin-conjugated strontium-substituted hydroxyapatite/silk fibroin (Sr-nHAp/SF-Hep) scaffold loaded bone morphogenetic proteins-2 (BMP-2) with sustained release to improve bone regeneration.	Heparin	43-50	bone morphogenetic protein 2	Homo sapiens	145-174
33435067-1	2018	The objective of this study was to develop heparin-conjugated strontium-substituted hydroxyapatite/silk fibroin (Sr-nHAp/SF-Hep) scaffold loaded bone morphogenetic proteins-2 (BMP-2) with sustained release to improve bone regeneration.	Heparin	43-50	bone morphogenetic protein 2	Homo sapiens	176-181
6457413-2	1981	Heparin complexes with thrombin, plasmin, and trypsin.	Heparin	0-7	plasminogen	Homo sapiens	33-40
32026972-6	2020	CONCLUSIONS: The combination of CK and CKH assays could be useful to estimate factor VIII (FVIII) level when heparin concentration is low or without heparin; however, caution should be necessary for estimation of FVIII level by TEG under the effect of medium- or high-dose heparin.	Heparin	109-116	coagulation factor VIII	Homo sapiens	78-89
6457414-2	1981	The role of heparin in the ATIII inactivation of thrombin, plasmin, and trypsin.	Heparin	12-19	plasminogen	Homo sapiens	59-66
32026972-6	2020	CONCLUSIONS: The combination of CK and CKH assays could be useful to estimate factor VIII (FVIII) level when heparin concentration is low or without heparin; however, caution should be necessary for estimation of FVIII level by TEG under the effect of medium- or high-dose heparin.	Heparin	109-116	coagulation factor VIII	Homo sapiens	91-96
32026972-6	2020	CONCLUSIONS: The combination of CK and CKH assays could be useful to estimate factor VIII (FVIII) level when heparin concentration is low or without heparin; however, caution should be necessary for estimation of FVIII level by TEG under the effect of medium- or high-dose heparin.	Heparin	149-156	coagulation factor VIII	Homo sapiens	78-89
32026972-6	2020	CONCLUSIONS: The combination of CK and CKH assays could be useful to estimate factor VIII (FVIII) level when heparin concentration is low or without heparin; however, caution should be necessary for estimation of FVIII level by TEG under the effect of medium- or high-dose heparin.	Heparin	149-156	coagulation factor VIII	Homo sapiens	91-96
32026972-6	2020	CONCLUSIONS: The combination of CK and CKH assays could be useful to estimate factor VIII (FVIII) level when heparin concentration is low or without heparin; however, caution should be necessary for estimation of FVIII level by TEG under the effect of medium- or high-dose heparin.	Heparin	149-156	coagulation factor VIII	Homo sapiens	78-89
32026972-6	2020	CONCLUSIONS: The combination of CK and CKH assays could be useful to estimate factor VIII (FVIII) level when heparin concentration is low or without heparin; however, caution should be necessary for estimation of FVIII level by TEG under the effect of medium- or high-dose heparin.	Heparin	149-156	coagulation factor VIII	Homo sapiens	91-96
30078756-5	2018	We focus on the two areas of most interest to Bob at the time, namely controlled release of macromolecules from polymers, and removal of heparin in order to prevent uncontrolled bleeding during surgery.	Heparin	137-144	G protein-coupled receptor 15	Homo sapiens	46-49
29395816-8	2018	In blood samples obtained from cardiac surgical patients (n = 72), heparin prolonged the PT/INR with the laboratory assay, dry-hematology method with non heparin neutralization technology (DRI PT), Coaguchek XS (Roche Diagnostics, Basel, Switzerland), and Hemochron Jr. (Accriva Diagnostics, Edison, NJ), but DRI PT-S was not affected by heparin anticoagulation.	Heparin	67-74	6-pyruvoyltetrahydropterin synthase	Homo sapiens	313-317
7193783-0	1981	Interaction of heparin with the cytosol progesterone receptor from human mammary tumours: separate estimation of the 4 and 7 S binding components with a simple dextran-charcoal assay.	Heparin	15-22	progesterone receptor	Homo sapiens	40-61
29661682-0	2018	Absolute immature platelet counts in the setting of suspected heparin-induced thrombocytopenia may predict anti-PF4-heparin immunoassay testing results.	Heparin	62-69	platelet factor 4	Homo sapiens	112-115
29661682-1	2018	BACKGROUND: Heparin-induced-thrombocytopenia (HIT) is a disease mediated by antibodies to platelet factor 4 (PF4)-heparin complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	109-112
29661682-1	2018	BACKGROUND: Heparin-induced-thrombocytopenia (HIT) is a disease mediated by antibodies to platelet factor 4 (PF4)-heparin complexes.	Heparin	114-121	platelet factor 4	Homo sapiens	109-112
29661682-9	2018	An A-IPC of greater than 5 x 109/L characterized 80% of anti-PF4-heparin positive cases.	Heparin	65-72	platelet factor 4	Homo sapiens	61-64
30244713-1	2018	Heparin induced thrombocytopenia (HIT) is a serious adverse drug reaction caused by transient antibodies against platelet factor 4 (PF4)/heparin complexes, resulting in platelet activation and potentially fatal arterial and/or venous thrombosis.	Heparin	0-7	platelet factor 4	Homo sapiens	132-135
30244713-1	2018	Heparin induced thrombocytopenia (HIT) is a serious adverse drug reaction caused by transient antibodies against platelet factor 4 (PF4)/heparin complexes, resulting in platelet activation and potentially fatal arterial and/or venous thrombosis.	Heparin	137-144	platelet factor 4	Homo sapiens	132-135
31705871-1	2020	Heparin-induced thrombocytopenia (HIT) is an adverse immunological disorder caused by antibodies to platelet factor 4 (PF4)-heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	119-122
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	homeobox A10	Homo sapiens	202-208
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	homeobox A10	Homo sapiens	210-222
31922007-3	2020	We leveraged the strong affinity interactions between heparin microparticles (HMPs) and BMP-2 to improve protein delivery to bone defects.	Heparin	54-61	bone morphogenetic protein 2	Rattus norvegicus	88-93
31621093-1	2020	Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by platelet-activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	0-7	platelet factor 4	Homo sapiens	126-129
30061484-11	2018	Further, glycyrrhizin inhibited HMGB1 and HMGB1 A-box binding to heparin.	Heparin	65-72	high mobility group box 1	Homo sapiens	32-37
30061484-11	2018	Further, glycyrrhizin inhibited HMGB1 and HMGB1 A-box binding to heparin.	Heparin	65-72	high mobility group box 1	Homo sapiens	42-47
7451445-2	1981	The heparin-inhibitable lectin activity from adult chicken liver and embryonic chick pectoral muscle has been purified by gel filtration on Sepharose CL-2B followed by affinity chromatography on heparin-Sepharose.	Heparin	4-11	galectin 3	Gallus gallus	24-30
31904611-6	2020	On Bethesda inhibitor testing, FIX inhibition was detected at 1 U/ml UFH and 3 U/ml UFH for FVIII.	Heparin	84-87	coagulation factor VIII	Homo sapiens	92-97
31904611-11	2020	Inhibition of FVIII and FIX was detected at low ratios of protamine sulfate to UFH (below 0.4 : 1) and disappeared at higher ratios.	Heparin	79-82	coagulation factor VIII	Homo sapiens	14-19
31904611-12	2020	UFH and protamine sulfate, alone or in combination, impact factor activity and inhibitor testing for both FVIII and FIX.	Heparin	0-3	coagulation factor VIII	Homo sapiens	106-111
7451445-2	1981	The heparin-inhibitable lectin activity from adult chicken liver and embryonic chick pectoral muscle has been purified by gel filtration on Sepharose CL-2B followed by affinity chromatography on heparin-Sepharose.	Heparin	195-202	galectin 3	Gallus gallus	24-30
29325985-1	2018	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by platelet-activating antibodies that recognize platelet factor 4 (PF4)/heparin complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	159-162
7451445-6	1981	Agglutination activity of the lectin, tested with specially prepared rabbit erythrocytes, was very sensitive to heparin which inhibited 50% at concentrations of approximately 10(-5) mM.	Heparin	112-119	galectin 3	Gallus gallus	30-36
7451445-9	1981	Because of its properties, we operationally refer to this material as chicken heparin-lectin, recognizing that this does not necessarily indicate that it functionally interacts with heparin in vivo.	Heparin	78-85	galectin 3	Gallus gallus	86-92
33445317-0	2018	SEMA4D-heparin Complexes Immobilized on Titanium Surfaces Have Anticoagulant, Cell-Migration-Promoting, and Immunoregulatory Effects.	Heparin	7-14	semaphorin 4D	Homo sapiens	0-6
33445317-4	2018	The biocompatibility evaluation results indicated that the SEMA4D-heparin-modified surfaces displayed less platelet adhesion and activation, prolonged activated partial thromboplastin time (APTT), prothrombin time (PT) and thrombin time (TT) and reduced fibrinogen gamma chain (FGG) exposure and fibrinogen adhesion.	Heparin	66-73	semaphorin 4D	Homo sapiens	59-65
33445317-5	2018	Additionally, endothelial cells (ECs) showed improved adhesion density and proliferation activity on the SEMA4D-heparin-modified surfaces.	Heparin	112-119	semaphorin 4D	Homo sapiens	105-111
33445317-7	2018	The immunological tests revealed that the SEMA4D-heparin complexes had a positive immunomodulatory effect on macrophages and promoted macrophages polarization into M2 phenotypes.	Heparin	49-56	semaphorin 4D	Homo sapiens	42-48
33445317-8	2018	Overall, the results suggested that the SEMA4D-heparin complexes can be a potential therapeutic agent to promote tissue healing and accelerate in situ endothelialization with minimal side effects and positive immunomodulatory effect.	Heparin	47-54	semaphorin 4D	Homo sapiens	40-46
31817064-3	2019	Freezing of the CHI-HA-GA and PVA-Hep-GA mixture led to the formation of a non-stoichiometric PEC between oppositely charged groups of CHI and Hep, which caused further efficient immobilization of bone morphogenic protein 2 (BMP-2) possible due to electrostatic interactions.	Heparin	34-37	bone morphogenetic protein 2	Rattus norvegicus	197-223
31817064-3	2019	Freezing of the CHI-HA-GA and PVA-Hep-GA mixture led to the formation of a non-stoichiometric PEC between oppositely charged groups of CHI and Hep, which caused further efficient immobilization of bone morphogenic protein 2 (BMP-2) possible due to electrostatic interactions.	Heparin	34-37	bone morphogenetic protein 2	Rattus norvegicus	225-230
31817064-3	2019	Freezing of the CHI-HA-GA and PVA-Hep-GA mixture led to the formation of a non-stoichiometric PEC between oppositely charged groups of CHI and Hep, which caused further efficient immobilization of bone morphogenic protein 2 (BMP-2) possible due to electrostatic interactions.	Heparin	143-146	bone morphogenetic protein 2	Rattus norvegicus	197-223
31817064-3	2019	Freezing of the CHI-HA-GA and PVA-Hep-GA mixture led to the formation of a non-stoichiometric PEC between oppositely charged groups of CHI and Hep, which caused further efficient immobilization of bone morphogenic protein 2 (BMP-2) possible due to electrostatic interactions.	Heparin	143-146	bone morphogenetic protein 2	Rattus norvegicus	225-230
31824433-6	2019	Biological activities of IGFBP-2 which are independent of their abilities to bind to insulin-like growth factors (IGFs) are mediated by the heparin binding domain (HBD).	Heparin	140-147	insulin like growth factor binding protein 2	Homo sapiens	25-32
29501428-6	2018	The system was applied to a complex mixture of heparin/heparan sulfate oligosaccharides varying in chain length from dp3 to dp12 and more than 80 molecular compositions were identified by accurate mass measurement.	Heparin	47-54	APC regulator of WNT signaling pathway	Homo sapiens	117-120
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Heparin	54-61	plasminogen	Homo sapiens	126-133
29614814-5	2018	Recent studies using single-molecule force spectroscopy (SMFS)-based atomic force microscopy revealed detailed binding mechanisms of the interactions between platelet factor 4 (PF4) and heparins of different lengths in typical HIT.	Heparin	186-194	platelet factor 4	Homo sapiens	177-180
31737612-3	2019	In this study, we incorporated low-molecular-weight heparin (LMWH) into carboxymethyl chitosan-oxidized chondroitin sulfate (CMC-OCS) hydrogel for loading transforming growth factor-beta3 (TGF-beta3) as matrix of peripheral blood mesenchymal stem cells (PB-MSCs) to construct tissue-engineered cartilage.	Heparin	52-59	transforming growth factor beta 3	Homo sapiens	155-187
6798759-2	1981	Previously, we have reported that blood collected into heparin rather than into CPD anticoagulant results in higher starting levels of plasma F VIII:C activity.	Heparin	55-62	coagulation factor VIII	Homo sapiens	142-148
31737612-3	2019	In this study, we incorporated low-molecular-weight heparin (LMWH) into carboxymethyl chitosan-oxidized chondroitin sulfate (CMC-OCS) hydrogel for loading transforming growth factor-beta3 (TGF-beta3) as matrix of peripheral blood mesenchymal stem cells (PB-MSCs) to construct tissue-engineered cartilage.	Heparin	52-59	transforming growth factor beta 3	Homo sapiens	189-198
6988774-5	1980	However, heparin releases also other enzymes, particularly hepatic triglyceride lipase (HTGL).	Heparin	9-16	lipase C, hepatic type	Homo sapiens	59-86
31578149-4	2019	Herein, a heparin-immobilized fibroin hydrogel was fabricated to deliver FGF1 (human acidic fibroblast growth factor 1) on top of wound in rats with full-thickness skin excision by performing comprehensive preclinical studies to fully evaluate its safety and effectiveness.	Heparin	10-17	fibroin light chain	Bombyx mori	30-37
31284097-2	2019	In this study, a CD133+ EPC capture surface was fabricated by grafting CD133 antibody (a more specific EPC surface marker than CD34) and Arg-Glu-Asp-Val (REDV) peptideon the methacrylate-grafted hyaluronic acid (MA-HA) and heparin-hybridized (MA-HA&amp;Heparin) resisting layer.	Heparin	223-230	prominin 1	Homo sapiens	17-22
31284097-2	2019	In this study, a CD133+ EPC capture surface was fabricated by grafting CD133 antibody (a more specific EPC surface marker than CD34) and Arg-Glu-Asp-Val (REDV) peptideon the methacrylate-grafted hyaluronic acid (MA-HA) and heparin-hybridized (MA-HA&amp;Heparin) resisting layer.	Heparin	253-260	prominin 1	Homo sapiens	17-22
29305908-2	2018	Thus, changes in the amounts, structures, and chain lengths of heparan sulfate have profound effects on aspects of cell growth controlled by heparin-binding growth factors such as FGF2.	Heparin	141-148	fibroblast growth factor 2	Mus musculus	180-184
29663988-0	2018	[Unfractionated heparin inhibits the activation of endothelial cells by decreasing the degree of HOXA9 reduced expression].	Heparin	16-23	homeobox A9	Homo sapiens	97-102
29663988-1	2018	OBJECTIVE: To study unfractionated heparin (UFH) effect on the expression of HOXA9 in activation of human umbilical vein endothelial cells (HUVECs) induced by lipopolysaccharide (LPS).	Heparin	35-42	homeobox A9	Homo sapiens	77-82
6988774-5	1980	However, heparin releases also other enzymes, particularly hepatic triglyceride lipase (HTGL).	Heparin	9-16	lipase C, hepatic type	Homo sapiens	88-92
29663988-1	2018	OBJECTIVE: To study unfractionated heparin (UFH) effect on the expression of HOXA9 in activation of human umbilical vein endothelial cells (HUVECs) induced by lipopolysaccharide (LPS).	Heparin	44-47	homeobox A9	Homo sapiens	77-82
29663988-8	2018	UFH can inhibit the activation of endothelial cells by decreasing the degree of HOXA9 reduced expression.	Heparin	0-3	homeobox A9	Homo sapiens	80-85
6775267-3	1980	The crude antiserum was prepared by injecting milk lipoprotein lipase prepared by heparin Sepharose affinity chromatography.	Heparin	82-89	lipoprotein lipase	Bos taurus	51-69
29467192-3	2018	Heparin disrupts CXCL12-mediated sequestration of cells in the marrow.	Heparin	0-7	C-X-C motif chemokine ligand 12	Homo sapiens	17-23
31362339-5	2019	Extracellular IL-37 could either dimerize in the presence of heparin and lose biological activity, or be acted upon by proteases that can generate even more biologically active IL-37 forms.	Heparin	61-68	interleukin 37	Homo sapiens	14-19
31027908-5	2019	METHODS: A 3D gel based on heparin-conjugated collagen matrix capable of immobilizing recombinant human bone morphogenic protein 2 (BMP2) was synthesized.	Heparin	27-34	bone morphogenetic protein 2	Homo sapiens	104-130
31027908-5	2019	METHODS: A 3D gel based on heparin-conjugated collagen matrix capable of immobilizing recombinant human bone morphogenic protein 2 (BMP2) was synthesized.	Heparin	27-34	bone morphogenetic protein 2	Homo sapiens	132-136
31027908-9	2019	Investigation of the MSCs laden collagen-heparin hydrogels revealed their capability to provide spatiotemporal bioavailability of BMP2 while suppressing the matrix contraction over time.	Heparin	41-48	bone morphogenetic protein 2	Homo sapiens	130-134
29343861-4	2018	Cleavage by plasmin and application of either a positive or a negative NP bias results in nanopore signals corresponding either to the VEGF receptor recognition domain or to the heparin binding domain, accordingly.	Heparin	178-185	plasminogen	Homo sapiens	12-19
113062-2	1979	The results have been considered in relation to the heparin-induced liberation of diamine oxidase from tissues into the blood stream.	Heparin	52-59	amine oxidase, copper containing 1	Rattus norvegicus	82-97
29220362-7	2017	Our data strongly support the use of CTAD as anticoagulant for determining plasma concentrations of platelet-stored molecules, as anticoagulation with heparin or EDTA led to a 12.4- or 8.3-fold increase in plasma levels of PF4, respectively.	Heparin	151-158	platelet factor 4	Homo sapiens	223-226
29285085-6	2017	The in vivo data indicated that UFH preconditioning attenuated the decline in circulating activated protein C following LPS administration, and also reduced LPS-induced shedding of TM and EPCR.	Heparin	32-35	protein C receptor	Homo sapiens	188-192
30999216-10	2019	Blocking release of calcium from internal stores by loading cells with the IP3 receptor blocker heparin (1 mM) or the ryanodine receptor blocker dantrolene (20 muM) abolished both the calcium transients and the facilitation of evoked synaptic currents induced by dopamine.	Heparin	96-103	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	75-87
106967-0	1979	alpha-L-iduronidase, beta-D-glucuronidase, and 2-sulfo-L-iduronate 2-sulfatase: preparation and characterization of radioactive substrates from heparin.	Heparin	144-151	glucuronidase beta	Homo sapiens	21-78
29871549-3	2019	However, heparin has the unique drawback of triggering Heparin-PF4 (PF4) antibodies potentially leading to heparin-induced thrombocytopenia (HIT).	Heparin	9-16	platelet factor 4	Homo sapiens	55-66
29871549-3	2019	However, heparin has the unique drawback of triggering Heparin-PF4 (PF4) antibodies potentially leading to heparin-induced thrombocytopenia (HIT).	Heparin	9-16	platelet factor 4	Homo sapiens	63-66
100865-1	1978	Diamine oxidase (DAO) was purified from blood serum after intravenous heparin injection, from pregnancy blood serum and amniotic fluid.	Heparin	70-77	amine oxidase copper containing 1	Homo sapiens	0-15
31069988-1	2019	Heparin-induced thrombocytopenia (HIT) is a clinical-pathological disorder; thus, laboratory testing for the pathogenic platelet-activating antiplatelet factor 4 (PF4)/heparin antibodies is central for diagnosis.	Heparin	0-7	platelet factor 4	Homo sapiens	120-161
31069988-1	2019	Heparin-induced thrombocytopenia (HIT) is a clinical-pathological disorder; thus, laboratory testing for the pathogenic platelet-activating antiplatelet factor 4 (PF4)/heparin antibodies is central for diagnosis.	Heparin	0-7	platelet factor 4	Homo sapiens	163-166
33636847-4	2017	For patients with a high-titer anti-PF4-heparin antibody and who require exposure to heparin, therapeutic plasma exchange (TPE) has been used to remove the antibody.	Heparin	40-47	platelet factor 4	Homo sapiens	36-39
33636847-7	2017	RESULTS: We observed that a single round of plasma exchange led to greater reduction in platelet reactivity at heparin concentrations between 1 and 3 U/mL than at lower concentrations, consistent with the impression that heparin-PF4-antibody complexes form optimally within a limited heparin concentration range.	Heparin	221-228	platelet factor 4	Homo sapiens	229-232
33636847-7	2017	RESULTS: We observed that a single round of plasma exchange led to greater reduction in platelet reactivity at heparin concentrations between 1 and 3 U/mL than at lower concentrations, consistent with the impression that heparin-PF4-antibody complexes form optimally within a limited heparin concentration range.	Heparin	221-228	platelet factor 4	Homo sapiens	229-232
30660009-5	2019	The results showed that sustained release of GDF5 by the PEAD:heparin delivery system promoted hADSC differentiation to an NP-like phenotype in vitro.	Heparin	62-69	growth differentiation factor 5	Rattus norvegicus	45-49
28101973-5	2017	Subsequently, heparin-free collagen sponge scaffolds (C/F scaffold) and collagen sponge scaffolds cross-linked with 10 mug/ml heparin retained FGF-2 (C/H10/F scaffold), and were transplanted into rats with tracheal defects.	Heparin	126-133	fibroblast growth factor 2	Rattus norvegicus	143-148
100865-1	1978	Diamine oxidase (DAO) was purified from blood serum after intravenous heparin injection, from pregnancy blood serum and amniotic fluid.	Heparin	70-77	amine oxidase copper containing 1	Homo sapiens	17-20
149422-0	1978	[Importance of the fibrinogen-heparin complex in the fibrinolytic activity of the blood euglobulin fraction after the intravenous administration of thrombin or plasmin].	Heparin	30-37	plasminogen	Homo sapiens	160-167
28230633-14	2017	Interleukin-4 increased in heparin Ice group that was in comparison with TNF-alpha reduction.	Heparin	27-34	interleukin-4	Oryctolagus cuniculus	0-13
30916501-2	2019	BACKGROUND: The diagnosis of heparin-induced thrombocytopenia (HIT) requires clinical data and laboratory detection of platelet activating factor 4/heparin (PF4/H) antibodies by immunological or functional assays.	Heparin	29-36	platelet factor 4	Homo sapiens	157-162
621432-2	1978	PF-4 was iodinated, repurified by affinity chromatography on heparin-Sepharose, and incubated with rabbit antiserum and a source of unlabeled antigen.	Heparin	61-68	platelet factor 4	Homo sapiens	0-4
30573633-1	2019	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	0-7	platelet factor 4	Homo sapiens	96-99
30573633-3	2019	Moreover, heparin-exposed patients vary considerably with respect to the risk of PF4/heparin immunization and, among antibody-positive patients, the risk of subsequent "breakthrough" of clinical HIT with manifestation of thrombocytopenia.	Heparin	10-17	platelet factor 4	Homo sapiens	81-84
28571106-7	2017	Evaluation of the inflammatory response reveal less numbers of CD68+ macrophages in SDF-1 and SDF-1/heparin groups compared with the control group; whereas three groups show similar numbers of CD206+ macrophages.	Heparin	100-107	Cd68 molecule	Rattus norvegicus	63-67
413549-0	1977	Localization of histamine (diamine oxidase) in rat small intestinal mucosa: site of release by heparin.	Heparin	95-102	amine oxidase, copper containing 1	Rattus norvegicus	27-42
28877477-4	2017	Our results support a model whereby heparin competes with insulin for insulin receptor binding on AgRP neurons, and by doing so it inhibits FoxO1 activity to promote AgRP release and feeding.	Heparin	36-43	insulin receptor	Homo sapiens	70-86
29974515-10	2019	Heparin is protective against LPC cytotoxicity and might intervene steps between mitochondrial membrane potential drop/p38 activation and caspase 3 activation.	Heparin	0-7	mitogen-activated protein kinase 14	Mus musculus	119-122
993645-7	1976	In addition, heparinized samples with decreased factor VIII activity maintained their pretreatment factor VII activities after heparin removal.	Heparin	13-20	cytochrome c oxidase subunit 8A	Homo sapiens	55-59
30478722-0	2019	Increased risk of heparin induced thrombocytopenia and thrombosis in patients with essential thrombocythemia carrying the homozygous JAK2 V617F mutation.	Heparin	18-25	Janus kinase 2	Homo sapiens	133-137
30540167-1	2018	The polyanion heparin, which is frequently used in patients, complexes with the platelet-derived cationic chemokine platelet factor (PF4, CXCL4).	Heparin	14-21	platelet factor 4	Homo sapiens	133-136
30540167-1	2018	The polyanion heparin, which is frequently used in patients, complexes with the platelet-derived cationic chemokine platelet factor (PF4, CXCL4).	Heparin	14-21	platelet factor 4	Homo sapiens	138-143
30540167-2	2018	This results in the formation of anti-PF4/heparin antibodies (anti-PF4/H Abs).	Heparin	42-49	platelet factor 4	Homo sapiens	67-70
30540167-3	2018	Anti-PF4/H Abs are classified into three groups: (i) nonpathogenic Abs (group 1) with no clinical relevance; (ii) pathogenic heparin-dependent Abs (group 2), which activate platelets and can cause the severe adverse drug effect heparin-induced thrombocytopenia (HIT); and (iii) pathogenic autoimmune-HIT Abs (group 3), in which group 3 anti-PF4/H Abs causes a HIT-like autoimmune disease in the absence of heparin.	Heparin	125-132	platelet factor 4	Homo sapiens	5-10
30540167-3	2018	Anti-PF4/H Abs are classified into three groups: (i) nonpathogenic Abs (group 1) with no clinical relevance; (ii) pathogenic heparin-dependent Abs (group 2), which activate platelets and can cause the severe adverse drug effect heparin-induced thrombocytopenia (HIT); and (iii) pathogenic autoimmune-HIT Abs (group 3), in which group 3 anti-PF4/H Abs causes a HIT-like autoimmune disease in the absence of heparin.	Heparin	228-235	platelet factor 4	Homo sapiens	5-10
30540167-3	2018	Anti-PF4/H Abs are classified into three groups: (i) nonpathogenic Abs (group 1) with no clinical relevance; (ii) pathogenic heparin-dependent Abs (group 2), which activate platelets and can cause the severe adverse drug effect heparin-induced thrombocytopenia (HIT); and (iii) pathogenic autoimmune-HIT Abs (group 3), in which group 3 anti-PF4/H Abs causes a HIT-like autoimmune disease in the absence of heparin.	Heparin	228-235	platelet factor 4	Homo sapiens	5-10
27898513-0	2017	Inhibition of plasmin generation in plasma by heparin, low molecular weight heparin, and a covalent antithrombin-heparin complex.	Heparin	46-53	plasminogen	Homo sapiens	14-21
27898513-0	2017	Inhibition of plasmin generation in plasma by heparin, low molecular weight heparin, and a covalent antithrombin-heparin complex.	Heparin	76-83	plasminogen	Homo sapiens	14-21
28622439-5	2017	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a life-threatening drug reaction caused by antiplatelet factor 4/heparin (anti-PF4/H) antibodies.	Heparin	20-27	platelet factor 4	Homo sapiens	141-144
993645-9	1976	Following heparin adsorption on ECTEOLA-cellulose columns, factor VIII activity levels remained above 60 per cent during cardiopulmonary by-pass.	Heparin	10-17	cytochrome c oxidase subunit 8A	Homo sapiens	66-70
28198086-5	2017	We propose a communication hub between these two binding sites, which sheds new light on modulatory functions of Langerin-heparin interactions.	Heparin	122-129	CD207 molecule	Homo sapiens	113-121
30218657-0	2018	An automated method for measuring lipoprotein lipase and hepatic triglyceride lipase activities in post-heparin plasma.	Heparin	104-111	lipase C, hepatic type	Homo sapiens	57-84
996366-2	1976	Although heparin minimized premature kininogen consumption better than hexadimethrine bromide, both were ineffective when used in combination.	Heparin	9-16	kininogen 2-like 1	Rattus norvegicus	37-46
30218657-3	2018	METHODS: The automated kinetic colorimetric method was used for assaying LPL and HTGL activity in the post-heparin plasma using the natural long-chain fatty acid 2-diglyceride as a substrate.	Heparin	107-114	lipase C, hepatic type	Homo sapiens	81-85
30218657-9	2018	CONCLUSIONS: The L PL and HTGL activity assays are applicable to quantitating the LPL and HTGL activity in the post-heparin plasma.	Heparin	116-123	lipase C, hepatic type	Homo sapiens	26-30
30218657-9	2018	CONCLUSIONS: The L PL and HTGL activity assays are applicable to quantitating the LPL and HTGL activity in the post-heparin plasma.	Heparin	116-123	lipase C, hepatic type	Homo sapiens	90-94
28338419-4	2017	We designed an electrospun poly-e-caprolactone nanofiber mesh containing physically entrapped heparin microparticles, which have been previously demonstrated to bind and retain large amounts of BMP-2.	Heparin	94-101	bone morphogenetic protein 2	Rattus norvegicus	194-199
5445-14	1976	The immunoglobin G fraction from these antisera completely inhibited lipoprotein lipase eluted from heparin-Sepharose columns.	Heparin	100-107	lipoprotein lipase	Gallus gallus	69-87
30419766-1	2018	Heparin (H) anticoagulation in populations characterized by elevated platelet factor 4 (PF4) frequently elicits PF4/H antibodies, presenting a risk of heparin-induced thrombocytopenia.	Heparin	0-7	platelet factor 4	Homo sapiens	88-91
30419766-1	2018	Heparin (H) anticoagulation in populations characterized by elevated platelet factor 4 (PF4) frequently elicits PF4/H antibodies, presenting a risk of heparin-induced thrombocytopenia.	Heparin	0-7	platelet factor 4	Homo sapiens	112-115
30419766-1	2018	Heparin (H) anticoagulation in populations characterized by elevated platelet factor 4 (PF4) frequently elicits PF4/H antibodies, presenting a risk of heparin-induced thrombocytopenia.	Heparin	151-158	platelet factor 4	Homo sapiens	88-91
28346881-1	2017	Large multimolecular complexes of heparin with positively charged proteins such as platelet factor 4 (PF4) or protamine can initiate immune responses associated with heparin use in patients, including the most significant adverse event, heparin-induced thrombocytopenia (HIT).	Heparin	34-41	platelet factor 4	Homo sapiens	102-105
30419766-2	2018	Recent studies have shown that anti-PF4/H enzyme-linked immunosorbent assays (ELISAs) detect antibodies in individuals never exposed to heparin.	Heparin	136-143	platelet factor 4	Homo sapiens	36-39
28346881-1	2017	Large multimolecular complexes of heparin with positively charged proteins such as platelet factor 4 (PF4) or protamine can initiate immune responses associated with heparin use in patients, including the most significant adverse event, heparin-induced thrombocytopenia (HIT).	Heparin	166-173	platelet factor 4	Homo sapiens	102-105
1265048-1	1976	Lipolytic activity measured at pH 8.6 in bovine corpora lutea exhibited classical properties of lipoprotein lipase (LPL) in terms of serum and heparin stimulation and NaCl inhibition.	Heparin	143-150	lipoprotein lipase	Bos taurus	96-114
28346881-1	2017	Large multimolecular complexes of heparin with positively charged proteins such as platelet factor 4 (PF4) or protamine can initiate immune responses associated with heparin use in patients, including the most significant adverse event, heparin-induced thrombocytopenia (HIT).	Heparin	166-173	platelet factor 4	Homo sapiens	102-105
28346881-2	2017	Current evidence suggests that platelet-activating antibodies that recognize large multi-molecular complexes (300-700kDa) of PF4 bound to heparin cause HIT [1] and in very rare cases anti-protamine-heparin antibodies can induce thrombocytopenia [2].	Heparin	138-145	platelet factor 4	Homo sapiens	125-128
30419766-8	2018	In the future, determining whether PF4/H cross-reactive antibodies sensitize patients to respond adversely to heparin anticoagulation or predispose patients to other complications may be relevant to diabetes care.	Heparin	110-117	platelet factor 4	Homo sapiens	35-38
30269432-5	2018	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a major and potentially fatal consequence of antibodies produced against platelet factor 4 (PF4)-heparin complexes following heparin exposure.	Heparin	20-27	platelet factor 4	Homo sapiens	154-157
30269432-5	2018	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a major and potentially fatal consequence of antibodies produced against platelet factor 4 (PF4)-heparin complexes following heparin exposure.	Heparin	159-166	platelet factor 4	Homo sapiens	154-157
30269432-5	2018	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a major and potentially fatal consequence of antibodies produced against platelet factor 4 (PF4)-heparin complexes following heparin exposure.	Heparin	187-194	platelet factor 4	Homo sapiens	154-157
30096473-2	2018	In this study, quartz crystal microbalance and dissipation (QCM-D) provided a surface sensitive technique that enabled real-time monitoring of the adhesion and spreading response of endothelial cells (ECs) and macrophages (MAs) to soluble-semaphoring 4D (SEMA4D)/heparin modified substratum.	Heparin	263-270	semaphorin 4D	Homo sapiens	231-253
28242772-6	2017	Remarkably, protamine antagonist activity is fully reversed by heparin treatment both in vitro and in vivo Thus, our results demonstrate a new pharmacologic property of protamine-blockade of APJ-that could explain some adverse effects observed in protamine-treated patients.	Heparin	63-70	apelin receptor	Homo sapiens	191-194
28554992-6	2017	For LPL and HL, the use of heparin and low molecular weight heparin as anticoagulation during hemodialysis (HD) initiate a loss of these enzymes from their binding sites and degradation, causing a temporary dysregulation in triglyceride breakdown.	Heparin	27-34	lipase C, hepatic type	Homo sapiens	12-14
28554992-6	2017	For LPL and HL, the use of heparin and low molecular weight heparin as anticoagulation during hemodialysis (HD) initiate a loss of these enzymes from their binding sites and degradation, causing a temporary dysregulation in triglyceride breakdown.	Heparin	60-67	lipase C, hepatic type	Homo sapiens	12-14
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	interleukin 1 receptor associated kinase 1	Homo sapiens	162-167
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	MYD88 innate immune signal transduction adaptor	Homo sapiens	172-177
1265048-1	1976	Lipolytic activity measured at pH 8.6 in bovine corpora lutea exhibited classical properties of lipoprotein lipase (LPL) in terms of serum and heparin stimulation and NaCl inhibition.	Heparin	143-150	lipoprotein lipase	Bos taurus	116-119
1239282-0	1975	The hydrolytic and transacylation activity of the phospholipase A1 purified from human post-heparin plasma.	Heparin	92-99	lipase H	Homo sapiens	50-66
28271738-0	2017	Profile of Instrumentation Laboratory"s HemosIL  AcuStar HIT-Ab(PF4-H) assay for diagnosis of heparin-induced thrombocytopenia.	Heparin	94-101	platelet factor 4	Homo sapiens	64-67
30288870-2	2018	We hypothesized that an amino acid sequence mimicking the major heparin binding domain (HBD) of hHL will displace hHL from cell surfaces.	Heparin	64-71	hes family bHLH transcription factor 1	Homo sapiens	96-99
30288870-2	2018	We hypothesized that an amino acid sequence mimicking the major heparin binding domain (HBD) of hHL will displace hHL from cell surfaces.	Heparin	64-71	hes family bHLH transcription factor 1	Homo sapiens	114-117
30194803-10	2018	Results Mouse TFPI and human TFPI are similar in regard to: (i) the mechanisms for FVIIa/TF and FXa inhibition; (ii) TFPIalpha is a soluble form and TFPIbeta is glycosyl phosphatidyl inositol (GPI) membrane anchored; (iii) the predominant circulating form of TFPI in plasma is lipoprotein-associated; (iv) low levels of TFPIalpha circulate in plasma and increase following heparin treatment; and (v) TFPIalpha is the isoform in platelets.	Heparin	373-380	tissue factor pathway inhibitor	Homo sapiens	29-33
803847-6	1975	The interaction of PF4 with heparin resulted in the formation of a complex which migrated to the anode, as tested by immunoelectrophoresis.	Heparin	28-35	platelet factor 4	Homo sapiens	19-22
30077924-9	2018	These results suggested that Cellufine Sulfate was more effective than heparin-immobilized resins in purifying the highly sialylated alpha form of hAT for therapeutic applications.	Heparin	71-78	transmembrane serine protease 11D	Homo sapiens	147-150
28044236-10	2017	We found that VAP-1 concentration in patients dialyzed by using LMWH or UFH was similar.	Heparin	72-75	amine oxidase copper containing 3	Homo sapiens	14-19
4853047-0	1974	Lowering of kininogen in rat blood by adrenaline and its inhibition by sympatholytic agents, heparin and aspirin.	Heparin	93-100	kininogen 2-like 1	Rattus norvegicus	12-21
28391124-0	2017	Performance characteristics of an automated latex immunoturbidimetric assay [HemosIL  HIT-Ab(PF4-H)] for the diagnosis of immune heparin-induced thrombocytopenia.	Heparin	129-136	platelet factor 4	Homo sapiens	93-96
28391124-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by platelet-activating anti-PF4/heparin antibodies.	Heparin	12-19	platelet factor 4	Homo sapiens	119-122
30086574-8	2018	RESULTS/CONCLUSION:  The most striking changes were observed following heparin administration and were associated with the appearance of inactive forms of anti-thrombin and an increase in the plasma concentration of TFPI.	Heparin	71-78	tissue factor pathway inhibitor	Homo sapiens	216-220
4198195-0	1973	Response of plasma histaminase activity to small doses of heparin in normal subjects and patients with hyperlipoproteinemia.	Heparin	58-65	amine oxidase copper containing 1	Homo sapiens	19-30
29723924-2	2018	Immunization to platelet factor 4 (PF4)-heparin occurs early in life, before any heparin exposure.	Heparin	40-47	platelet factor 4	Homo sapiens	35-38
29723924-7	2018	Previous studies have shown immunity to PF4-heparin complexes occurs early in life, even before heparin exposure; however, the immunogenesis of HIT is not well characterized.	Heparin	44-51	platelet factor 4	Homo sapiens	40-43
29723924-15	2018	These findings further demonstrate cellular immune sensitization to PF4-heparin complexes occurs before heparin exposure, and suggests immune dysregulation can contribute to HIT.	Heparin	72-79	platelet factor 4	Homo sapiens	68-71
28193842-9	2017	mMCP-5 protein is therefore needed to target translated mMC-CPA to the secretory granule along with HP-containing serglycin proteoglycans.	Heparin	100-102	chymase 1, mast cell	Mus musculus	0-6
4198195-1	1973	The release of histaminase activity in plasma after small intravenous of heparin was studied in 85 normal subjects and patients.	Heparin	73-80	amine oxidase copper containing 1	Homo sapiens	15-26
4198195-2	1973	In normal subjects, plasma histaminase activity (basal level, 1.7+/-0.1 U/ml, mean +/-SEM) increased 1.6+/-0.2 U/ml after 10 U of heparin/kg, 8.5+/-2.4 U/ml after 20 U/kg, and 33+/-4.9 U/ml after 75 U/kg.	Heparin	130-137	amine oxidase copper containing 1	Homo sapiens	27-38
27878865-2	2017	The members of this subfamily, FGF19, FGF21 and FGF23, are characterized by their reduced binding affinity for heparin that enables them to be transported in the circulation and function in an endocrine manner.	Heparin	111-118	fibroblast growth factor 19	Homo sapiens	31-36
4198195-8	1973	In contrast, in 27 patients with other types of hyperlipoproteinemia in whom postheparin lipolytic activity was normal, the increase (2.4+/-0.6 U/ml) in plasma histaminase activity after 10 U heparin/kg was not significantly different from that of normal subjects.	Heparin	81-88	amine oxidase copper containing 1	Homo sapiens	160-171
28245630-4	2017	Using solution nuclear magnetic resonance (NMR) spectroscopy, we characterized the binding of CXCL7 monomer to the CXCR2 N-terminal domain (CXCR2Nd) that constitutes a critical docking site and to GAG heparin.	Heparin	201-208	pro-platelet basic protein	Homo sapiens	94-99
28245630-4	2017	Using solution nuclear magnetic resonance (NMR) spectroscopy, we characterized the binding of CXCL7 monomer to the CXCR2 N-terminal domain (CXCR2Nd) that constitutes a critical docking site and to GAG heparin.	Heparin	201-208	C-X-C motif chemokine receptor 2	Homo sapiens	115-120
29702734-0	2018	Heparin-dopamine functionalized graphene foam for sustained release of bone morphogenetic protein-2.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	71-99
29702734-5	2018	Importantly, the heparin-functionalized 3D GrF significantly improved the exogenous BMP2-induced osteogenic differentiation.	Heparin	17-24	bone morphogenetic protein 2	Homo sapiens	84-88
28931787-3	2018	These results strongly suggest that heparin induced MAB mobilization via HGF upregulation.	Heparin	36-43	hepatocyte growth factor	Homo sapiens	73-76
28931787-8	2018	We then examined patients undergoing cardiac catheterization and found that heparin significantly increased plasma HGF levels and the number of cMAB colonies in a dose-dependent manner.	Heparin	76-83	hepatocyte growth factor	Homo sapiens	115-118
4198195-9	1973	The reduced response of the plasma histaminase activity to heparin in patients with type I hyperlipoproteinemia did not appear to be due to the presence of lipemia or to an inhibitor of the enzyme in plasma.	Heparin	59-66	amine oxidase copper containing 1	Homo sapiens	35-46
28931787-10	2018	CONCLUSIONS: Human cMABs are mobilized by heparin injection during cardiac surgery or cardiac catheterization, presumably via HGF upregulation.	Heparin	42-49	hepatocyte growth factor	Homo sapiens	126-129
28698883-2	2017	Heparin-induced thrombocytopenia (HIT) is a thrombotic syndrome mediated by anti-platelet factor 4 (PF4)/heparin antibodies with undetermined significance for thrombosis in MPN.	Heparin	0-7	platelet factor 4	Homo sapiens	100-103
4198195-10	1973	These findings suggest that many patients with type I hyperlipoproteinemia may have deficient release of both lipolytic and histaminase activities into plasma after heparin administration.	Heparin	165-172	amine oxidase copper containing 1	Homo sapiens	124-135
5138478-0	1971	Heparin-induced release of lipase activity from perfused canine subcutaneous adipose tissue.	Heparin	0-7	pancreatic lipase related protein 1	Canis lupus familiaris	27-33
27758044-2	2017	Heparanase accomplishes this by degrading heparan sulfate which regulates the abundance and location of heparin-binding growth factors thereby influencing multiple signaling pathways that control gene expression, syndecan shedding and cell behavior.	Heparin	104-111	syndecan 1	Homo sapiens	213-221
29628468-1	2018	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	140-143
29628468-1	2018	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	140-143
4994826-0	1971	Heparin-induced increase of diamine oxidase in lymph and blood plasma of rat, guinea-pig and rabbit.	Heparin	0-7	amine oxidase, copper containing 1	Rattus norvegicus	28-43
29274508-0	2018	A Heparin Binding Motif Rich in Arginine and Lysine is the Functional Domain of YKL-40.	Heparin	2-9	chitinase 3 like 1	Homo sapiens	80-86
29274508-3	2018	YKL-40 harbors a consensus heparin-binding motif that consists of positively charged arginine (R) and lysine (K) (RRDK; residues 144-147); but they don"t bind to heparin.	Heparin	27-34	chitinase 3 like 1	Homo sapiens	0-6
29274508-5	2018	A short synthetic peptide spanning this KR-rich domain successfully competed with YKL-40 and blocked its ability to bind heparin.	Heparin	121-128	chitinase 3 like 1	Homo sapiens	82-88
27465274-4	2016	Recent descriptions of the crystal structure of the PF4/heparin complex, alongside other biophysical studies, have clarified the structural requirements for immunogenicity and heparin-dependency of antibody formation.	Heparin	56-63	platelet factor 4	Homo sapiens	52-55
27465274-4	2016	Recent descriptions of the crystal structure of the PF4/heparin complex, alongside other biophysical studies, have clarified the structural requirements for immunogenicity and heparin-dependency of antibody formation.	Heparin	176-183	platelet factor 4	Homo sapiens	52-55
29274508-7	2018	In addition, a neutralizing anti-YKL-40 antibody that targets these residues and prevents heparin binding impeded angiogenesis in vitro.	Heparin	90-97	chitinase 3 like 1	Homo sapiens	33-39
4958839-0	1966	Heparin-induced diamine oxidase increase in human blood plasma.	Heparin	0-7	amine oxidase copper containing 1	Homo sapiens	16-31
29274508-9	2018	These data reveal that the KR-rich heparin-binding motif is the functional heparin-binding domain of YKL-40.	Heparin	35-42	chitinase 3 like 1	Homo sapiens	101-107
29274508-9	2018	These data reveal that the KR-rich heparin-binding motif is the functional heparin-binding domain of YKL-40.	Heparin	75-82	chitinase 3 like 1	Homo sapiens	101-107
27487857-4	2016	Monocytes and endothelial cells bind PF4 with higher avidity than platelets and are more resistant to competitive removal of surface-bound PF4 in the presence of heparin.	Heparin	162-169	platelet factor 4	Homo sapiens	37-40
27487857-4	2016	Monocytes and endothelial cells bind PF4 with higher avidity than platelets and are more resistant to competitive removal of surface-bound PF4 in the presence of heparin.	Heparin	162-169	platelet factor 4	Homo sapiens	139-142
34048524-4	2021	In addition, fluorescence polarization (FP) and saturation transfer difference NMR (STD-NMR) experiments revealed that the synthesized CS-like derivatives were able to interact with midkine, a model heparin-binding growth factor, suggesting that the presence of the GlcA carboxylate groups is not essential for the binding.	Heparin	199-206	citrate synthase	Homo sapiens	135-137
27474590-0	2016	Magnetic field-responsive release of transforming growth factor beta 1 from heparin-modified alginate ferrogels.	Heparin	76-83	transforming growth factor, beta 1	Mus musculus	37-70
27474590-5	2016	To modulate the release of transforming growth factor beta 1 (TGF-beta1) under magnetic stimulation, alginate was chemically modified with heparin, as TGF-beta1 has a heparin-binding domain.	Heparin	139-146	transforming growth factor, beta 1	Mus musculus	27-60
27474590-5	2016	To modulate the release of transforming growth factor beta 1 (TGF-beta1) under magnetic stimulation, alginate was chemically modified with heparin, as TGF-beta1 has a heparin-binding domain.	Heparin	139-146	transforming growth factor, beta 1	Mus musculus	62-71
27474590-5	2016	To modulate the release of transforming growth factor beta 1 (TGF-beta1) under magnetic stimulation, alginate was chemically modified with heparin, as TGF-beta1 has a heparin-binding domain.	Heparin	139-146	transforming growth factor, beta 1	Mus musculus	151-160
29321335-8	2018	The association between serum HGF and primary outcome could be modified by heparin pre-treatment (Pinteraction=0.001), and a positive linear dose-response relationship between HGF and primary outcome was observed in patients without heparin pre-treatment (Plinearity&lt;0.001) but not in those with heparin pre-treatment.	Heparin	75-82	hepatocyte growth factor	Homo sapiens	30-33
29321335-8	2018	The association between serum HGF and primary outcome could be modified by heparin pre-treatment (Pinteraction=0.001), and a positive linear dose-response relationship between HGF and primary outcome was observed in patients without heparin pre-treatment (Plinearity&lt;0.001) but not in those with heparin pre-treatment.	Heparin	233-240	hepatocyte growth factor	Homo sapiens	176-179
29321335-8	2018	The association between serum HGF and primary outcome could be modified by heparin pre-treatment (Pinteraction=0.001), and a positive linear dose-response relationship between HGF and primary outcome was observed in patients without heparin pre-treatment (Plinearity&lt;0.001) but not in those with heparin pre-treatment.	Heparin	233-240	hepatocyte growth factor	Homo sapiens	176-179
29719300-0	2018	Unfractionated Heparin Alleviates Human Lung Endothelial Barrier Dysfunction Induced by High Mobility Group Box 1 Through Regulation of P38-GSK3beta-Snail Signaling Pathway.	Heparin	15-22	high mobility group box 1	Homo sapiens	88-113
29719300-0	2018	Unfractionated Heparin Alleviates Human Lung Endothelial Barrier Dysfunction Induced by High Mobility Group Box 1 Through Regulation of P38-GSK3beta-Snail Signaling Pathway.	Heparin	15-22	glycogen synthase kinase 3 beta	Homo sapiens	140-148
29719300-13	2018	In addition, we found that UFH was able to reverse the effect of HMGB1 on EndoMT and endothelial permeability through inhibition of p38 signaling in a dose-dependent manner.	Heparin	27-30	high mobility group box 1	Homo sapiens	65-70
29174344-7	2018	The HTGL ratio of the pre-heparin/post-heparin plasma concentration and sdLDL-C/LDL-C ratio were significantly greater in CAD patients than in non-CAD patients.	Heparin	26-33	lipase C, hepatic type	Homo sapiens	4-8
29174344-7	2018	The HTGL ratio of the pre-heparin/post-heparin plasma concentration and sdLDL-C/LDL-C ratio were significantly greater in CAD patients than in non-CAD patients.	Heparin	39-46	lipase C, hepatic type	Homo sapiens	4-8
33636847-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a hypercoagulable state caused by a transient antibody to heparin-bound platelet factor 4 (PF4).	Heparin	12-19	platelet factor 4	Homo sapiens	145-148
33636847-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a hypercoagulable state caused by a transient antibody to heparin-bound platelet factor 4 (PF4).	Heparin	112-119	platelet factor 4	Homo sapiens	145-148
27474590-5	2016	To modulate the release of transforming growth factor beta 1 (TGF-beta1) under magnetic stimulation, alginate was chemically modified with heparin, as TGF-beta1 has a heparin-binding domain.	Heparin	167-174	transforming growth factor, beta 1	Mus musculus	27-60
27474590-5	2016	To modulate the release of transforming growth factor beta 1 (TGF-beta1) under magnetic stimulation, alginate was chemically modified with heparin, as TGF-beta1 has a heparin-binding domain.	Heparin	167-174	transforming growth factor, beta 1	Mus musculus	62-71
27474590-5	2016	To modulate the release of transforming growth factor beta 1 (TGF-beta1) under magnetic stimulation, alginate was chemically modified with heparin, as TGF-beta1 has a heparin-binding domain.	Heparin	167-174	transforming growth factor, beta 1	Mus musculus	151-160
27474590-8	2016	Sustained release of TGF-beta1 from alginate-g-heparin ferrogels was achieved, and application of a magnetic field to the ferrogels regulated TGF-beta1 release, resultantly enhancing chondrogenic differentiation of ATDC5 cells, which were used as a model chondrogenic cell line.	Heparin	47-54	transforming growth factor, beta 1	Mus musculus	21-30
27706246-9	2016	Histone significantly induced 3 endothelial adhesion molecules expression, and promoted leukemic cell adhesion to endothelial cells, which was inhibited by histone inhibitors (heparin, polysialic acid, and activated protein C), neutralizing antibodies against these adhesion molecules, and a Toll like receptor(TLR)9 antagonist.	Heparin	176-183	toll like receptor 9	Homo sapiens	292-316
33915212-8	2021	Exploring further, our in-silico analysis indicated that the heparin interacts with post-translational glycoconjugates present on spike proteins.	Heparin	61-68	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	130-135
27694984-7	2016	Analysis of heparin binding of the main transglutaminases revealed that although the interaction between TG1 and HS is strong, the conformational heparin binding site of TG2 is not conserved, suggesting that TG2 has a unique interaction with HS within the family.	Heparin	12-19	transglutaminase 2	Rattus norvegicus	208-211
27694984-7	2016	Analysis of heparin binding of the main transglutaminases revealed that although the interaction between TG1 and HS is strong, the conformational heparin binding site of TG2 is not conserved, suggesting that TG2 has a unique interaction with HS within the family.	Heparin	146-153	transglutaminase 2	Rattus norvegicus	170-173
27694984-7	2016	Analysis of heparin binding of the main transglutaminases revealed that although the interaction between TG1 and HS is strong, the conformational heparin binding site of TG2 is not conserved, suggesting that TG2 has a unique interaction with HS within the family.	Heparin	146-153	transglutaminase 2	Rattus norvegicus	208-211
28846826-1	2017	Autoimmune heparin-induced thrombocytopenia (aHIT) indicates the presence in patients of anti-platelet factor 4 (PF4)-polyanion antibodies that are able to activate platelets strongly even in the absence of heparin (heparin-independent platelet activation).	Heparin	11-18	platelet factor 4	Homo sapiens	113-116
28846826-1	2017	Autoimmune heparin-induced thrombocytopenia (aHIT) indicates the presence in patients of anti-platelet factor 4 (PF4)-polyanion antibodies that are able to activate platelets strongly even in the absence of heparin (heparin-independent platelet activation).	Heparin	207-214	platelet factor 4	Homo sapiens	113-116
28846826-1	2017	Autoimmune heparin-induced thrombocytopenia (aHIT) indicates the presence in patients of anti-platelet factor 4 (PF4)-polyanion antibodies that are able to activate platelets strongly even in the absence of heparin (heparin-independent platelet activation).	Heparin	207-214	platelet factor 4	Homo sapiens	113-116
28846826-5	2017	Recent studies have implicated anti-PF4 antibodies that are able to bridge two PF4 tetramers even in the absence of heparin, probably facilitated by non-heparin platelet-associated polyanions (chondroitin sulfate and polyphosphates); nascent PF4-aHIT-IgG complexes recruit additional heparin-dependent HIT antibodies, leading to the formation of large multimolecular immune complexes and marked platelet activation.	Heparin	116-123	platelet factor 4	Homo sapiens	36-39
33915212-10	2021	Heparin-binding to the open conformation of spike structurally supports the state and may aid ACE2 binding as reported with cell surface-bound heparan sulfate.	Heparin	0-7	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	44-49
33915212-10	2021	Heparin-binding to the open conformation of spike structurally supports the state and may aid ACE2 binding as reported with cell surface-bound heparan sulfate.	Heparin	0-7	angiotensin converting enzyme 2	Homo sapiens	94-98
27338641-0	2016	Transferring the C-terminus of the chemokine CCL21 to CCL19 confers enhanced heparin binding.	Heparin	77-84	C-C motif chemokine ligand 21	Homo sapiens	45-50
33915212-11	2021	We also studied spike protein mutant variants" heparin interactions for possible resistance.	Heparin	47-54	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	16-21
27338641-0	2016	Transferring the C-terminus of the chemokine CCL21 to CCL19 confers enhanced heparin binding.	Heparin	77-84	C-C motif chemokine ligand 19	Homo sapiens	54-59
29046479-6	2017	LPL was released rapidly from chicken hearts with an infusion of heparin, consistent with LPL being located inside blood vessels.	Heparin	65-72	lipoprotein lipase	Gallus gallus	0-3
33915212-13	2021	Studies should be designed to exploit its nanomolar antiviral activity to formulate heparin as topical or inhalation-based formulations, particularly on exposed areas and sites of primary viremia e.g. ACE2 rich epithelia of the eye (conjunctiva/lids), nasal cavity, and mouth.	Heparin	84-91	angiotensin converting enzyme 2	Homo sapiens	201-205
28821136-5	2017	In addition, the selected depolymerized heparins inhibited high-mobility group protein B1 (HMGB-1) expression, prevented E-cadhesin from downregulation, and reduced fibroblasts accumulation in the mouse lung tissue.	Heparin	40-48	high mobility group box 1	Mus musculus	59-89
28821136-5	2017	In addition, the selected depolymerized heparins inhibited high-mobility group protein B1 (HMGB-1) expression, prevented E-cadhesin from downregulation, and reduced fibroblasts accumulation in the mouse lung tissue.	Heparin	40-48	high mobility group box 1	Mus musculus	91-97
27338641-6	2016	Deletion of this extended C-terminus reduces CCL21"s affinity for heparin and transferring the CCL21 C-terminus to CCL19 enhances heparin binding mainly through non-specific, electrostatic interactions.	Heparin	66-73	C-C motif chemokine ligand 21	Homo sapiens	45-50
27383886-5	2016	Recombinant human bone morphogenetic protein 2 (rhBMP-2) was bound to conjugated scaffolds by ionic interactions between the negatively charged SO42- clusters of heparin and positively charged amino acids of rhBMP-2.	Heparin	162-169	bone morphogenetic protein 2	Homo sapiens	18-46
33835769-4	2021	We used a standard enzyme-linked immunosorbent assay to detect platelet factor 4 (PF4)-heparin antibodies and a modified (PF4-enhanced) platelet-activation test to detect platelet-activating antibodies under various reaction conditions.	Heparin	87-94	platelet factor 4	Homo sapiens	82-85
27427828-7	2016	Gal-3 interacts with unmodified heparin, chondroitin sulfate-A (CSA), -B (CSB), and -C (CSC) as well as chondroitin sulfate proteoglycans (CSPGs).	Heparin	32-39	galectin 3	Homo sapiens	0-5
28936181-2	2017	Heparin binds specifically to TMEM184A and induces anti-proliferative signaling in vitro.	Heparin	0-7	transmembrane protein 184a	Danio rerio	30-38
33835769-5	2021	Included in this testing were samples from patients who had blood samples referred for investigation of vaccine-associated thrombotic events, with 28 testing positive on a screening PF4-heparin immunoassay.	Heparin	186-193	platelet factor 4	Homo sapiens	182-185
33835769-11	2021	All 28 patients who tested positive for antibodies against PF4-heparin tested positive on the platelet-activation assay in the presence of PF4 independent of heparin.	Heparin	63-70	platelet factor 4	Homo sapiens	59-62
28645809-3	2017	We incorporated BMP-2-binding heparin microparticles (HMPs) into a hydrogel scaffold to improve spatiotemporal control of BMP-2 delivery to large bone defects.	Heparin	30-37	bone morphogenetic protein 2	Homo sapiens	16-21
33835769-11	2021	All 28 patients who tested positive for antibodies against PF4-heparin tested positive on the platelet-activation assay in the presence of PF4 independent of heparin.	Heparin	63-70	platelet factor 4	Homo sapiens	139-142
28645809-3	2017	We incorporated BMP-2-binding heparin microparticles (HMPs) into a hydrogel scaffold to improve spatiotemporal control of BMP-2 delivery to large bone defects.	Heparin	30-37	bone morphogenetic protein 2	Homo sapiens	122-127
27113576-5	2016	Heparin immobilization improves the amount of VEGF retained by the construct, up to 3.6 fold, compared to untreated PCL scaffolds.	Heparin	0-7	vascular endothelial growth factor A	Gallus gallus	46-50
28645809-14	2017	Herein, we introduced heparin microparticles (HMPs) into a tissue engineered construct to increase in vivo retention of bone morphogenetic protein-2 (BMP-2) and enhance healing in femoral defects.	Heparin	22-29	bone morphogenetic protein 2	Homo sapiens	120-148
33835769-13	2021	Additional studies with PF4 or PF4-heparin affinity purified antibodies in 2 patients confirmed PF4-dependent platelet activation.	Heparin	35-42	platelet factor 4	Homo sapiens	31-34
33835769-13	2021	Additional studies with PF4 or PF4-heparin affinity purified antibodies in 2 patients confirmed PF4-dependent platelet activation.	Heparin	35-42	platelet factor 4	Homo sapiens	31-34
28645809-14	2017	Herein, we introduced heparin microparticles (HMPs) into a tissue engineered construct to increase in vivo retention of bone morphogenetic protein-2 (BMP-2) and enhance healing in femoral defects.	Heparin	22-29	bone morphogenetic protein 2	Homo sapiens	150-155
33835769-14	2021	CONCLUSIONS: Vaccination with ChAdOx1 nCov-19 can result in the rare development of immune thrombotic thrombocytopenia mediated by platelet-activating antibodies against PF4, which clinically mimics autoimmune heparin-induced thrombocytopenia.	Heparin	210-217	platelet factor 4	Homo sapiens	170-173
27898513-0	2017	Inhibition of plasmin generation in plasma by heparin, low molecular weight heparin, and a covalent antithrombin-heparin complex.	Heparin	76-83	plasminogen	Homo sapiens	14-21
27898513-4	2017	The aim of this study was to determine the effects of ATH, UFH, and LMWH on plasmin generation in plasma, under more physiological conditions.	Heparin	59-62	plasminogen	Homo sapiens	76-83
27062407-1	2016	Lipoprotein apheresis such as heparin-induced extracorporal LowDensityLipoprotein (LDL) Cholesterol precipitation (HELP) reduces apolipoprotein B-containing lipoproteins, most importantly low-density-lipoprotein (LDL), and lipoprotein (a) [Lp(a)].	Heparin	30-37	lipoprotein(a)	Homo sapiens	240-245
33561388-5	2021	Heparin or a chemically modified form of heparin without anticoagulant function inhibited the alarmin HMGB1-lipopolysaccharide (LPS) interaction and prevented the macrophage glycocalyx degradation by heparanase.	Heparin	0-7	high mobility group box 1	Homo sapiens	102-107
27417614-4	2016	Antepartum low molecular weight heparin combined with low-dose aspirin prophylaxis can cut the incidence of early onset PE-E and fetuses that are small for their gestational age in half.	Heparin	32-39	pregnancy-induced hypertension (pre-eclampsia, eclampsia, toxemia of pregnancy included)	Homo sapiens	120-124
27898513-7	2017	Plasmin generation was decreased in the presence of UFH and ATH, whereas LMWH had no effect.	Heparin	52-55	plasminogen	Homo sapiens	0-7
27898513-10	2017	Plasmin generation may be mildly inhibited by heparin-based anticoagulants; however, heparin-catalyzed antithrombin activity is not a major inhibitor of plasmin, as compared to its natural inhibitors alpha2-AP and alpha2-M.	Heparin	46-53	plasminogen	Homo sapiens	0-7
33561388-5	2021	Heparin or a chemically modified form of heparin without anticoagulant function inhibited the alarmin HMGB1-lipopolysaccharide (LPS) interaction and prevented the macrophage glycocalyx degradation by heparanase.	Heparin	41-48	high mobility group box 1	Homo sapiens	102-107
26928466-4	2016	In a second step, we took advantage of the heparin-binding domain of vascular endothelial growth factor (VEGF) and hepatocyte growth factor (HGF) to gain advanced re-endothelialization capabilities.	Heparin	43-50	hepatocyte growth factor	Homo sapiens	141-144
33385179-0	2021	Conformation-Crooking CXCL4 to Unravel Autoimmune Heparin-Induced Thrombocytopenia.	Heparin	50-57	platelet factor 4	Homo sapiens	22-27
27097314-3	2016	However, previous studies showed that the accumulation of two heparin-binding growth factors, Vascular Endothelial Cell Growth Factor-A (VEGF-A) and Fibroblast Growth Factor-2 (FGF-2), in combination with the viral protein Tat, can precipitate the progression of HIV-renal diseases.	Heparin	62-69	tyrosine aminotransferase	Homo sapiens	223-226
26774761-4	2016	Heparin-containing hydrogel particles sequestered growth factors Nodal and FGF-2, which are implicated in specifying pluripotent cells to definitive endoderm.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	75-80
26774761-5	2016	Mouse ESCs were encapsulated into heparin microgels with a single dose of Nodal and FGF-2, and expressed high levels of endoderm markers Sox17 and FoxA2 after 5 days.	Heparin	34-41	fibroblast growth factor 2	Mus musculus	84-89
27011914-1	2016	Exposure to heparin is associated with a high incidence of immunization against platelet factor 4 (PF4)/heparin complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	99-102
28688202-0	2017	Influence of Human Leukocyte Antigen (HLA) Alleles and Killer Cell Immunoglobulin-Like Receptors (KIR) Types on Heparin-Induced Thrombocytopenia (HIT).	Heparin	112-119	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 4	Homo sapiens	98-101
27273141-0	2017	Thromboelastography during coronary artery bypass grafting surgery of severe hemophilia A patient - the effect of heparin and protamine on factor VIII activity.	Heparin	114-121	coagulation factor VIII	Homo sapiens	139-150
27273141-7	2017	Data are compatible with in-vitro assays performed in our laboratory, showing that both heparin and protamine may impair measurable FVIII activity.	Heparin	88-95	coagulation factor VIII	Homo sapiens	132-137
28446364-2	2017	Heparin induced thrombocytopenia (HIT) is a rare but potentially fatal complication of heparin therapy that results from production of polyclonal antibodies to heparin in complex, usually with platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	212-215
27030175-3	2016	Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry.	Heparin	119-127	fibroblast growth factor 3	Homo sapiens	54-58
28446364-2	2017	Heparin induced thrombocytopenia (HIT) is a rare but potentially fatal complication of heparin therapy that results from production of polyclonal antibodies to heparin in complex, usually with platelet factor 4 (PF4).	Heparin	87-94	platelet factor 4	Homo sapiens	212-215
33197333-1	2021	Heparin and heparan sulfate (HS) are highly sulfated polysaccharides covalently bound to cell surface proteins, which directly interact with many extracellular proteins, including the transforming growth factor-beta (TGFbeta) family ligand antagonist, follistatin 288 (FS288).	Heparin	0-7	transforming growth factor alpha	Homo sapiens	217-224
28446364-2	2017	Heparin induced thrombocytopenia (HIT) is a rare but potentially fatal complication of heparin therapy that results from production of polyclonal antibodies to heparin in complex, usually with platelet factor 4 (PF4).	Heparin	160-167	platelet factor 4	Homo sapiens	212-215
27076245-1	2016	Heparin-induced thrombocytopenia (HIT) is a prothrombotic side effect of heparin therapy caused by HIT antibodies, i.e., anti-platelet factor 4 (PF4)/heparin IgG with platelet-activating properties.	Heparin	0-7	platelet factor 4	Homo sapiens	145-148
27076245-1	2016	Heparin-induced thrombocytopenia (HIT) is a prothrombotic side effect of heparin therapy caused by HIT antibodies, i.e., anti-platelet factor 4 (PF4)/heparin IgG with platelet-activating properties.	Heparin	73-80	platelet factor 4	Homo sapiens	145-148
28530237-2	2017	A subset of these antibodies may activate platelets after binding to PF4/heparin complexes, causing the prothrombotic adverse drug reaction heparin-induced thrombocytopenia (HIT).	Heparin	73-80	platelet factor 4	Homo sapiens	69-72
33400098-1	2021	A recent heparin shortage related to an outbreak of African Swine Flu in China led to substantial increase in the use of direct thrombin inhibitors (DTI) as an alternative.	Heparin	9-16	coagulation factor II, thrombin	Sus scrofa	128-136
26790955-5	2016	Moreover, kallistatin via its heparin-binding site antagonized Wnt3a-induced cancer cell proliferation and increased PPARgamma expression.	Heparin	30-37	Wnt family member 3A	Homo sapiens	63-68
32852122-9	2021	HMGB1 facilitated the proliferation of iNKT cells co-cultured with DCs and macrophages, which was found to be inhibited by heparin.	Heparin	123-130	high mobility group box 1	Homo sapiens	0-5
26999404-10	2016	Low molecular weight heparin (LMWH) was the favoured PTP agent in over 90% of respondents.	Heparin	21-28	protein tyrosine phosphatase receptor type U	Homo sapiens	53-56
28539836-5	2017	Here, we used a biodegradable coacervate, composed of heparin and polycation, to dominate the combined release of bFGF and NGF in a steady fashion.	Heparin	54-61	fibroblast growth factor 2	Rattus norvegicus	114-118
28539836-5	2017	Here, we used a biodegradable coacervate, composed of heparin and polycation, to dominate the combined release of bFGF and NGF in a steady fashion.	Heparin	54-61	nerve growth factor	Rattus norvegicus	123-126
28231509-3	2017	A factorial design of experiments study guided us to combine three complementary factors in one injection: tissue inhibitor of metalloproteinases-3 (TIMP-3) was embedded in a fibrin gel for signaling in the initial phase of the treatment, while basic fibroblast growth factor (FGF-2) and stromal cell-derived factor 1-alpha (SDF-1alpha) were embedded in heparin-based coacervates for sustained release and distributed within the same fibrin gel to exert their effects over a longer period.	Heparin	354-361	TIMP metallopeptidase inhibitor 3	Rattus norvegicus	149-155
33085589-1	2021	BACKGROUND: Serological assays for the diagnosis of heparin-induced thrombocytopenia (HIT) detect both platelet-activating and platelet non-activating anti-heparin/platelet factor 4 (PF4) antibodies and have therefore a limited positive predictive value.	Heparin	52-59	platelet factor 4	Homo sapiens	151-181
28087378-6	2017	The scaffolds were prepared from poly(lactic-co-glycolic acid), and BMP-7/TGF-beta3 were loaded as nanocomplexes with heparin and Tetronic 1107.	Heparin	118-125	transforming growth factor beta 3	Homo sapiens	74-83
26998625-8	2016	Attenuating intracellular calcium concentration with EGTA, heparin or procaine decreased POX-induced upregulation of calpain 1, calpain 2, caspase-12 and caspase-3, and reduced POX-induced cyt c release.	Heparin	59-66	calpain 1	Mus musculus	117-126
26998625-8	2016	Attenuating intracellular calcium concentration with EGTA, heparin or procaine decreased POX-induced upregulation of calpain 1, calpain 2, caspase-12 and caspase-3, and reduced POX-induced cyt c release.	Heparin	59-66	caspase 12	Mus musculus	139-149
33085589-1	2021	BACKGROUND: Serological assays for the diagnosis of heparin-induced thrombocytopenia (HIT) detect both platelet-activating and platelet non-activating anti-heparin/platelet factor 4 (PF4) antibodies and have therefore a limited positive predictive value.	Heparin	52-59	platelet factor 4	Homo sapiens	183-186
33324681-5	2020	In this study, we performed direct binding surface plasmon resonance (SPR) assay to characterize the kinetics of heparin binding to four recombinant murine PrP constructs including full length (M23-230), a deletion mutant lacking the four histidine-containing octapeptide repeats (M23-230 Delta59-90), the isolated N-terminal domain (M23-109), and the isolated C-terminal domain (M90-230).	Heparin	113-120	prion protein	Mus musculus	156-159
26474791-0	2015	Mode of heparin attachment to nanocrystalline hydroxyapatite affects its interaction with bone morphogenetic protein-2.	Heparin	8-15	bone morphogenetic protein 2	Homo sapiens	90-118
26474791-1	2015	Heparin has a high affinity for bone morphogenetic protein-2 (BMP-2), which is a key growth factor in bone regeneration.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	32-60
26474791-1	2015	Heparin has a high affinity for bone morphogenetic protein-2 (BMP-2), which is a key growth factor in bone regeneration.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	62-67
28249361-0	2017	Heparin-induced amyloid fibrillation of beta2 -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagram.	Heparin	0-7	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	40-45
26400659-1	2017	BACKGROUND: Previous studies have demonstrated optimized diagnostic accuracy in utilizing higher antiheparin-platelet factor 4 (PF4) enzyme-linked immunosorbent assay (ELISA) optical density (OD) thresholds for diagnosing heparin-induced thrombocytopenia (HIT).	Heparin	101-108	platelet factor 4	Homo sapiens	128-131
26474791-2	2015	The aim of this study was to investigate how the rate of release of BMP-2 was affected when adsorbed to nanosized hydroxyapatite (HAP) particles functionalized with heparin by different methods.	Heparin	165-172	bone morphogenetic protein 2	Homo sapiens	68-73
26474791-7	2015	Moreover, when heparin was adsorbed onto pure HAP, it was found that the BMP-2 released after 7 days was 5% (similar to that from unmodified HAP).	Heparin	15-22	bone morphogenetic protein 2	Homo sapiens	73-78
26474791-8	2015	This illustrates that by altering the mode of attachment of heparin to HAP the release profile and total release of BMP-2 can be manipulated.	Heparin	60-67	bone morphogenetic protein 2	Homo sapiens	116-121
26474791-9	2015	Importantly, the BMP-2 released from all the heparin particle types was found by the SMAD 1/5/8 phosphorylation assay to be biologically active.	Heparin	45-52	bone morphogenetic protein 2	Homo sapiens	17-22
26474791-9	2015	Importantly, the BMP-2 released from all the heparin particle types was found by the SMAD 1/5/8 phosphorylation assay to be biologically active.	Heparin	45-52	SMAD family member 1	Homo sapiens	85-93
33324681-6	2020	Additionally, we found the specific structural determinants required for GAG binding to the four PrP constructs with chemically defined derivatives of heparin and other GAGs by an SPR competition assay.	Heparin	151-158	prion protein	Mus musculus	97-100
26462137-3	2015	First, heparin-conjugated gelatin (HG) is synthesized, which provides binding domains for bone morphogenetic protein 2 (BMP2) to stabilize this growth factor, protect it from denaturation and proteolytic degradation, and subsequently prolong its sustained release.	Heparin	7-14	bone morphogenetic protein 2	Homo sapiens	90-118
26462137-3	2015	First, heparin-conjugated gelatin (HG) is synthesized, which provides binding domains for bone morphogenetic protein 2 (BMP2) to stabilize this growth factor, protect it from denaturation and proteolytic degradation, and subsequently prolong its sustained release.	Heparin	7-14	bone morphogenetic protein 2	Homo sapiens	120-124
34035190-3	2020	In order to make efficient use of bFGF, PCL electrospun fibrous membrane is firstly surface-coated by self-polymerization of dopamine, and followed by immobilization of heparin via covalent conjugation to the polydopamine (PDA) layer.	Heparin	169-176	fibroblast growth factor 2	Mus musculus	34-38
26462137-6	2015	BMP2 in the hierarchical microsphere is released in a multiple-controlled manner by the binding with heparin and encapsulation of the nanosphere and microsphere.	Heparin	101-108	bone morphogenetic protein 2	Homo sapiens	0-4
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	interleukin 4 induced 1	Homo sapiens	54-57
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	interleukin 4 induced 1	Homo sapiens	158-161
26643738-7	2015	CONCLUSIONS: Substituting bivalirudin for heparin conferred a tradeoff between bleeding and ST. Transradial access, adjunctive glycoprotein IIb/IIIa inhibitors, and potent P2Y12 inhibitors attenuated the bleeding advantage of bivalirudin over heparin but had no apparent effect on early ST. New approaches to reduce bleeding and ischemic complications during percutaneous coronary intervention warrant further investigation.	Heparin	243-250	purinergic receptor P2Y12	Homo sapiens	172-177
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	113-120	interleukin 4 induced 1	Homo sapiens	158-161
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	interleukin 4 induced 1	Homo sapiens	54-57
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	interleukin 4 induced 1	Homo sapiens	158-161
32653371-9	2020	Surface plasmon resonance (SPR) studies revealed that LAO showed an IC50 of 0.07 mg/mL inhibiting the binding of heparin to fibroblast growth factor 1 (FGF1) LAO inhibition of heparin binding to FGF2 fluctuated between 15% and 28%, suggesting that LAO inhibits A549 cell proliferation by selectively interacting with FGF1.	Heparin	176-183	interleukin 4 induced 1	Homo sapiens	158-161
26034014-2	2015	Here, basic fibroblast growth factor (bFGF) was immobilized on porous polymer materials using a mild and biologically safe three-step reaction: (1) modification with a novel surface-modification peptide (penta-lysine-mussel adhesive sequence, which reacts with various matrices), (2) electrostatic binding of heparin with introduced penta-lysine, and (3) biologically specific binding of bFGF to heparin.	Heparin	309-316	fibroblast growth factor 2	Mus musculus	6-36
33091948-2	2020	The target of the immune response is a cationic "self" protein, platelet factor 4 (PF4), rendered antigenic by heparin.	Heparin	111-118	platelet factor 4	Homo sapiens	64-81
26034014-2	2015	Here, basic fibroblast growth factor (bFGF) was immobilized on porous polymer materials using a mild and biologically safe three-step reaction: (1) modification with a novel surface-modification peptide (penta-lysine-mussel adhesive sequence, which reacts with various matrices), (2) electrostatic binding of heparin with introduced penta-lysine, and (3) biologically specific binding of bFGF to heparin.	Heparin	309-316	fibroblast growth factor 2	Mus musculus	38-42
26034014-2	2015	Here, basic fibroblast growth factor (bFGF) was immobilized on porous polymer materials using a mild and biologically safe three-step reaction: (1) modification with a novel surface-modification peptide (penta-lysine-mussel adhesive sequence, which reacts with various matrices), (2) electrostatic binding of heparin with introduced penta-lysine, and (3) biologically specific binding of bFGF to heparin.	Heparin	396-403	fibroblast growth factor 2	Mus musculus	6-36
26034014-6	2015	Direct physical coating of bFGF on PPS resulted in greater immobilization but lesser tissue integration than that after the three-step bFGF immobilization, indicating that heparin binds and enhances bFGF efficacy.	Heparin	172-179	fibroblast growth factor 2	Mus musculus	27-31
26034014-6	2015	Direct physical coating of bFGF on PPS resulted in greater immobilization but lesser tissue integration than that after the three-step bFGF immobilization, indicating that heparin binds and enhances bFGF efficacy.	Heparin	172-179	fibroblast growth factor 2	Mus musculus	135-139
26034014-6	2015	Direct physical coating of bFGF on PPS resulted in greater immobilization but lesser tissue integration than that after the three-step bFGF immobilization, indicating that heparin binds and enhances bFGF efficacy.	Heparin	172-179	fibroblast growth factor 2	Mus musculus	135-139
26276817-11	2015	These findings define new mechanisms through which FGF-2 and Ang-1* modulate the outcome of intestinal bleeding complications induced by PPS in mice and may have wider clinical implications for critically ill children treated with heparin-like drugs.	Heparin	231-238	fibroblast growth factor 2	Mus musculus	51-56
26291604-1	2015	BACKGROUND: Many patients exposed to heparin develop antibodies against platelet factor 4 (PF4) and heparin, yet only those antibodies that activate platelets cause heparin-induced thrombocytopenia (HIT).	Heparin	37-44	platelet factor 4	Homo sapiens	91-94
33091948-2	2020	The target of the immune response is a cationic "self" protein, platelet factor 4 (PF4), rendered antigenic by heparin.	Heparin	111-118	platelet factor 4	Homo sapiens	83-86
26291604-11	2015	CONCLUSIONS: A subset of heparin-treated patients produce subthreshold levels of platelet-activating anti-PF4/heparin antibodies that do not cause HIT.	Heparin	25-32	platelet factor 4	Homo sapiens	106-109
33091948-3	2020	A key problem is that only a minority of anti-PF4/polyanion antibodies induced by heparin are pathogenic, i.e., capable of causing platelet activation and thereby clinical HIT.	Heparin	82-89	platelet factor 4	Homo sapiens	46-49
33050376-0	2020	Structural Features and PF4 Functions that Occur in Heparin-Induced Thrombocytopenia (HIT) Complicated by COVID-19.	Heparin	52-59	platelet factor 4	Homo sapiens	24-27
25998703-0	2015	Heparin inhibits lipopolysaccharide-induced inflammation via inducing caveolin-1 and activating the p38/mitogen-activated protein kinase pathway in murine peritoneal macrophages.	Heparin	0-7	mitogen-activated protein kinase 14	Mus musculus	100-103
25998703-4	2015	The present study confirmed the anti-inflammatory effects of heparin in lipopolysaccharide (LPS)-induced murine peritoneal macrophages through decreasing the levels of the inflammatory cytokines tumor necrosis factor alpha (TNF-alpha), interleukin 6 (IL-6), IL-8 and IL-1beta.	Heparin	61-68	chemokine (C-X-C motif) ligand 15	Mus musculus	258-262
25998703-7	2015	Furthermore, following caveolin-1 silencing, the p38/mitogen-activated protein kinase (MAPK) pathway was still able to be activated by heparin, while the extracellular signal-regulated kinase and c-Jun N-terminal kinase pathways were inhibited.	Heparin	135-142	mitogen-activated protein kinase 14	Mus musculus	49-52
25998703-8	2015	In conclusion, these results suggested that heparin inhibits LPS-induced inflammation via inducing caveolin-1 and activating the p38/MAPK pathway in murine peritoneal macrophages.	Heparin	44-51	mitogen-activated protein kinase 14	Mus musculus	129-132
32351125-0	2020	Prophylactic low-molecular-weight heparin administration protected against severe acute pancreatitis partially by VEGF/Flt-1 signaling in a rat model.	Heparin	34-41	Fms related receptor tyrosine kinase 1	Rattus norvegicus	119-124
25998835-1	2015	OBJECTIVES: The objective of this study was to determine the differences in pregnancy associated plasma protein-A (PAPP-A) concentrations in heparin naive and heparin treated healthy men and non-pregnant women, to find a possible difference in different age groups, and to determine the response in PAPP-A concentration to repeated injections of unfractionated heparin.	Heparin	141-148	pappalysin 1	Homo sapiens	76-113
25998835-1	2015	OBJECTIVES: The objective of this study was to determine the differences in pregnancy associated plasma protein-A (PAPP-A) concentrations in heparin naive and heparin treated healthy men and non-pregnant women, to find a possible difference in different age groups, and to determine the response in PAPP-A concentration to repeated injections of unfractionated heparin.	Heparin	141-148	pappalysin 1	Homo sapiens	115-121
25998835-1	2015	OBJECTIVES: The objective of this study was to determine the differences in pregnancy associated plasma protein-A (PAPP-A) concentrations in heparin naive and heparin treated healthy men and non-pregnant women, to find a possible difference in different age groups, and to determine the response in PAPP-A concentration to repeated injections of unfractionated heparin.	Heparin	159-166	pappalysin 1	Homo sapiens	76-113
25998835-1	2015	OBJECTIVES: The objective of this study was to determine the differences in pregnancy associated plasma protein-A (PAPP-A) concentrations in heparin naive and heparin treated healthy men and non-pregnant women, to find a possible difference in different age groups, and to determine the response in PAPP-A concentration to repeated injections of unfractionated heparin.	Heparin	159-166	pappalysin 1	Homo sapiens	76-113
25998835-5	2015	RESULTS: Injection of heparin elicited increase in and rapid normalization of PAPP-A concentrations in all subjects.	Heparin	22-29	pappalysin 1	Homo sapiens	78-84
25998835-8	2015	Repeated injections of heparin caused additional peaks in PAPP-A concentration of about the same sizes as the first peak.	Heparin	23-30	pappalysin 1	Homo sapiens	58-64
25998835-12	2015	This result combined with the finding of equally sized peaks in PAPP-A concentration, and that all of this was found in healthy, non-pregnant individuals, suggests that heparin might compete for a binding-site on PAPP-A or with PAPP-A itself for a common receptor in healthy arterial vessels.	Heparin	169-176	pappalysin 1	Homo sapiens	64-70
25998835-12	2015	This result combined with the finding of equally sized peaks in PAPP-A concentration, and that all of this was found in healthy, non-pregnant individuals, suggests that heparin might compete for a binding-site on PAPP-A or with PAPP-A itself for a common receptor in healthy arterial vessels.	Heparin	169-176	pappalysin 1	Homo sapiens	213-219
25998835-12	2015	This result combined with the finding of equally sized peaks in PAPP-A concentration, and that all of this was found in healthy, non-pregnant individuals, suggests that heparin might compete for a binding-site on PAPP-A or with PAPP-A itself for a common receptor in healthy arterial vessels.	Heparin	169-176	pappalysin 1	Homo sapiens	213-219
32460635-5	2020	In this AuNP-PMS/FGF2 composite, PMS, playing as the high-active mimic of heparin/heparan sulfate (HS), is covalently anchored to AuNPs and bound with FGF2 on the surface of nanoparticles, forming a HS/FGF2 complex nanomimics to facilitate its binding to FGF receptor (FGFR) and promote high neural-inductive activity of mESCs.	Heparin	74-81	fibroblast growth factor 2	Mus musculus	17-21
32460635-5	2020	In this AuNP-PMS/FGF2 composite, PMS, playing as the high-active mimic of heparin/heparan sulfate (HS), is covalently anchored to AuNPs and bound with FGF2 on the surface of nanoparticles, forming a HS/FGF2 complex nanomimics to facilitate its binding to FGF receptor (FGFR) and promote high neural-inductive activity of mESCs.	Heparin	74-81	fibroblast growth factor 2	Mus musculus	151-155
25951824-5	2015	We fractionated DSPP-derived proteins from the dental pulp of developing porcine incisors using heparin chromatography.	Heparin	96-103	dentin sialophosphoprotein	Homo sapiens	16-20
32678978-6	2020	Using this technique in combination with molecular modeling also allows the role of heparin in destabilizing the ACE2/RBD association to be studied, providing critical information for understanding the molecular mechanism of its interference with the virus docking to the host cell receptor.	Heparin	84-91	angiotensin converting enzyme 2	Homo sapiens	113-117
25960020-4	2015	METHODS AND RESULTS: Using unlabeled and fluorescently-labeled antigen and/or labeled monoclonal antibody to PF4/heparin complexes (KKO), we show that PF4/heparin complexes are taken up by monocytes in a heparin-dependent manner and are internalized by human monocytes and dendritic cells, but not by neutrophils.	Heparin	113-120	platelet factor 4	Homo sapiens	151-154
25960020-4	2015	METHODS AND RESULTS: Using unlabeled and fluorescently-labeled antigen and/or labeled monoclonal antibody to PF4/heparin complexes (KKO), we show that PF4/heparin complexes are taken up by monocytes in a heparin-dependent manner and are internalized by human monocytes and dendritic cells, but not by neutrophils.	Heparin	155-162	platelet factor 4	Homo sapiens	109-112
25960020-4	2015	METHODS AND RESULTS: Using unlabeled and fluorescently-labeled antigen and/or labeled monoclonal antibody to PF4/heparin complexes (KKO), we show that PF4/heparin complexes are taken up by monocytes in a heparin-dependent manner and are internalized by human monocytes and dendritic cells, but not by neutrophils.	Heparin	155-162	platelet factor 4	Homo sapiens	109-112
25960020-9	2015	CONCLUSIONS: Taken together, these studies establish a distinct role for heparin in enhancing antigen uptake and activation of the initial steps in the cellular immune response to PF4-containing complexes.	Heparin	73-80	platelet factor 4	Homo sapiens	180-183
25926600-0	2015	Combination of 4Ts score and PF4/H-PaGIA for diagnosis and management of heparin-induced thrombocytopenia: prospective cohort study.	Heparin	73-80	platelet factor 4	Homo sapiens	29-32
25809312-1	2015	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies against complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	123-126
32678978-9	2020	The destabilizing effect of heparin is more pronounced in the case of the longer chains due to the electrostatic repulsion between the low-pI ACE2 and the heparin segments not accommodated on the RBD surface.	Heparin	28-35	angiotensin converting enzyme 2	Homo sapiens	142-146
25979342-5	2015	We defined interactions and structural requirements for heparin/HS interactions with VEGF receptor (VEGFR)-1, NRP-1, and VEGF165 in complex with VEGFR-2 and NRP-1.	Heparin	56-63	neuropilin 1	Homo sapiens	110-115
25979342-5	2015	We defined interactions and structural requirements for heparin/HS interactions with VEGF receptor (VEGFR)-1, NRP-1, and VEGF165 in complex with VEGFR-2 and NRP-1.	Heparin	56-63	neuropilin 1	Homo sapiens	157-162
25979342-7	2015	We further show that VEGF165, VEGFR-2, and monomeric NRP-1 bind weakly to heparin alone yet show synergistic binding to heparin when presented together in various combinations.	Heparin	74-81	neuropilin 1	Homo sapiens	53-58
25979342-7	2015	We further show that VEGF165, VEGFR-2, and monomeric NRP-1 bind weakly to heparin alone yet show synergistic binding to heparin when presented together in various combinations.	Heparin	120-127	neuropilin 1	Homo sapiens	53-58
32678978-10	2020	In addition to providing important mechanistic information on attenuation of the ACE2/RBD association by heparin, the study demonstrates the yet untapped potential of native MS coupled to gas-phase ion chemistry as a means of facilitating rational repurposing of the existing medicines for treating COVID-19.	Heparin	105-112	angiotensin converting enzyme 2	Homo sapiens	81-85
32577646-6	2020	Using this technique in combination with molecular modeling also allows the role of heparin in destabilizing the ACE2/RBD association to be studied, providing critical information for understanding the molecular mechanism of its interference with the virus docking to the host cell receptor.	Heparin	84-91	angiotensin converting enzyme 2	Homo sapiens	113-117
25864985-1	2015	BACKGROUND: We produced fibroblast growth factor (FGF)-2-containing low-molecular-weight heparin (Fragmin)/protamine nanoparticles (FGF-2 + F/P NPs).	Heparin	89-96	fibroblast growth factor 2	Rattus norvegicus	24-56
25864985-1	2015	BACKGROUND: We produced fibroblast growth factor (FGF)-2-containing low-molecular-weight heparin (Fragmin)/protamine nanoparticles (FGF-2 + F/P NPs).	Heparin	89-96	fibroblast growth factor 2	Rattus norvegicus	132-137
32577646-9	2020	The destabilizing effect of heparin is more pronounced in the case of the longer chains due to the electrostatic repulsion between the low-p I ACE2 and the heparin segments not accommodated on the RBD surface.	Heparin	28-35	angiotensin converting enzyme 2	Homo sapiens	143-147
32577646-10	2020	In addition to providing important mechanistic information on attenuation of the ACE2/RBD association by heparin, the study demonstrates the yet untapped potential of native MS coupled to gas-phase ion chemistry as a means of facilitating rational repurposing of the existing medicines for treating COVID-19.	Heparin	105-112	angiotensin converting enzyme 2	Homo sapiens	81-85
31943091-3	2020	This non-signal producing Met-HGF interaction can also be eliminated by addition of a heparin mimetic sucrose octasulphate (SOS).	Heparin	86-93	hepatocyte growth factor	Homo sapiens	30-33
25833002-4	2015	Heparin promoted the fibrillization of human islet amyloid polypeptide (IAPP) and enhanced its toxicity to INS-1 beta cells.	Heparin	0-7	islet amyloid polypeptide	Homo sapiens	72-76
32481593-2	2020	The binding of heparin on kallistatin has been shown to block the inhibition of KLK1 by kallistatin but the detailed molecular mechanism underlying this blockade is unclear.	Heparin	15-22	kallikrein 1	Homo sapiens	80-84
25736498-4	2015	BMP-2 was subsequently immobilized onto the mesh scaffolds via heparin, and released at a controlled rate.	Heparin	63-70	bone morphogenetic protein 2	Homo sapiens	0-5
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	58-65	kallikrein 1	Homo sapiens	279-283
25705961-2	2015	OBJECTIVE: This study evaluated a protamine-based polyelectrolyte complex (PEC) developed to use heparin in enhancing the biological activity of low-dose recombinant human bone morphogenetic protein-2 (rhBMP-2) in spinal fusion.	Heparin	97-104	bone morphogenetic protein 2	Homo sapiens	172-200
25705961-7	2015	Previous studies with poly-L-lysine (PLL) and heparin-based PEC carriers amplified the therapeutic efficacy of low-dose BMP-2.	Heparin	46-53	bone morphogenetic protein 2	Rattus norvegicus	120-125
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	58-65	kallikrein 1	Homo sapiens	403-407
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	58-65	kallikrein 1	Homo sapiens	403-407
25240785-5	2015	Activated mast cells systemically released heparin, which provided a negatively charged surface for factor XII autoactivation.	Heparin	43-50	coagulation factor XII (Hageman factor)	Mus musculus	100-110
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	236-243	kallikrein 1	Homo sapiens	279-283
25503805-1	2015	Heparin-induced thrombocytopenia (HIT) is an unpredictable, potentially catastrophic adverse effect of heparin treatment resulting from an immune response to platelet factor 4 (PF4)/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	177-180
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	236-243	kallikrein 1	Homo sapiens	403-407
25503805-1	2015	Heparin-induced thrombocytopenia (HIT) is an unpredictable, potentially catastrophic adverse effect of heparin treatment resulting from an immune response to platelet factor 4 (PF4)/heparin complexes.	Heparin	103-110	platelet factor 4	Homo sapiens	177-180
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	236-243	kallikrein 1	Homo sapiens	403-407
25595736-5	2015	Lastly, mice with B cells lacking CD40, a B-cell costimulatory molecule that helps T-cell-dependent B-cell responses, displayed a marked reduction of PF4/heparin-specific antibody production following PF4/heparin challenge.	Heparin	154-161	CD40 antigen	Mus musculus	34-38
32481593-7	2020	Taken together, these data indicate that heparin controls the specificity of kallistatin, such that kinin generation by KLK1 within the microcirculation will be locally protected by the binding of kallistatin to the heparin-like glycosaminoglycans of the endothelium.	Heparin	41-48	kallikrein 1	Homo sapiens	120-124
32379796-13	2020	Dynamic light scattering revealed the rPF4 oligomerization into of larger complexes of approximately 100-1200 nm in size following heparin supplementation, implying proper protein folding and tetramerization.	Heparin	131-138	platelet factor 4	Rattus norvegicus	38-42
25498652-3	2015	Derivatives of heparin involving the periodate cleavage of 2,3 vicinal diols in non-sulfated uronate residues (glycol-split) and replacement of N-sulphamido- with N-acetamido- groups in glucosamine residues, capable of inhibiting neutrophil elastase activity in vitro, while exhibiting attenuated anticoagulant properties, have been identified and characterised.	Heparin	15-22	elastase, neutrophil expressed	Homo sapiens	230-249
32187531-5	2020	Our binding analyses further revealed that glycosaminoglycans, heparin and heparan sulfate, are ligands for OTK and thus may play a role in the Sema1a-PlexA axon guidance system.	Heparin	63-70	off-track	Drosophila melanogaster	108-111
25489725-0	2015	PAPP-A and IGFBP-4 fragment levels in patients with ST-elevation myocardial infarction treated with heparin and PCI.	Heparin	100-107	pappalysin 1	Homo sapiens	0-6
25489725-2	2015	Unfortunately, administration of heparin to patients with ACS increases circulating PAPP-A, probably by a detachment of PAPP-A from cell surfaces, inducing a considerable bias when using PAPP-A as a biomarker.	Heparin	33-40	pappalysin 1	Homo sapiens	84-90
25489725-2	2015	Unfortunately, administration of heparin to patients with ACS increases circulating PAPP-A, probably by a detachment of PAPP-A from cell surfaces, inducing a considerable bias when using PAPP-A as a biomarker.	Heparin	33-40	pappalysin 1	Homo sapiens	120-126
25489725-2	2015	Unfortunately, administration of heparin to patients with ACS increases circulating PAPP-A, probably by a detachment of PAPP-A from cell surfaces, inducing a considerable bias when using PAPP-A as a biomarker.	Heparin	33-40	pappalysin 1	Homo sapiens	120-126
32328108-4	2020	The heparin-PF4 immune complex leads to activation of platelets, monocytes, and endothelial cells which release procoagulant proteins and tissue factor with subsequent blood coagulation activation.	Heparin	4-11	platelet factor 4	Homo sapiens	12-15
25562836-0	2015	Heparin inhibits the inflammatory response induced by LPS and HMGB1 by blocking the binding of HMGB1 to the surface of macrophages.	Heparin	0-7	high mobility group box 1	Mus musculus	62-67
25562836-0	2015	Heparin inhibits the inflammatory response induced by LPS and HMGB1 by blocking the binding of HMGB1 to the surface of macrophages.	Heparin	0-7	high mobility group box 1	Mus musculus	95-100
25562836-3	2015	This study investigated the influence of heparin on LPS+HMGB1-mediated inflammatory responses in cultured macrophages and a murine sepsis model.	Heparin	41-48	high mobility group box 1	Mus musculus	56-61
25562836-6	2015	Heparin blocked the binding of HMGB1 to the surface of macrophages, and suppressed the phosphorylation of p38 and ERK1/2, but not JNK; TNF-alpha secretion was also decreased.	Heparin	0-7	high mobility group box 1	Mus musculus	31-36
27734602-4	2017	It results from an autoantibody directed against endogenous platelet factor 4 (PF4) in complex with heparin, which activates platelets and can cause catastrophic arterial and venous thromboses.	Heparin	100-107	platelet factor 4	Homo sapiens	79-82
27899064-5	2017	We also found that heparin inhibited both GDF5 binding to cell surface HS and GDF5-induced induction of Smad 1/5/8 signaling.	Heparin	19-26	SMAD family member 1	Homo sapiens	104-112
25562836-6	2015	Heparin blocked the binding of HMGB1 to the surface of macrophages, and suppressed the phosphorylation of p38 and ERK1/2, but not JNK; TNF-alpha secretion was also decreased.	Heparin	0-7	mitogen-activated protein kinase 14	Mus musculus	106-109
32337112-3	2020	The pathophysiological basis of HIT results from the formation of an immunocomplex consisting of an auto-antibody against platelet factor 4 (PF4) - heparin complex, which binds to the surface of platelets and monocytes, provoking their activation by cross-linking FcgIIA receptors.	Heparin	148-155	platelet factor 4	Homo sapiens	141-144
25562836-6	2015	Heparin blocked the binding of HMGB1 to the surface of macrophages, and suppressed the phosphorylation of p38 and ERK1/2, but not JNK; TNF-alpha secretion was also decreased.	Heparin	0-7	mitogen-activated protein kinase 3	Mus musculus	114-120
28221043-6	2017	111In-FGF-2 had affinity for the low-molecular-weight heparin enoxaparin identical to that of unlabeled FGF-2 (Kd: 0.6 +- 0.07 muM and 0.33 +- 0.03 muM, respectively) as assessed by isothermal titration calorimetry.	Heparin	54-61	fibroblast growth factor 2	Mus musculus	6-11
32308382-7	2020	Peptide 12, which is located in the heparin-binding site of FGF-2, or protein-conjugated VLPs presented the most significant effects on the suppression of TC-1 tumor growth.	Heparin	36-43	fibroblast growth factor 2	Mus musculus	60-65
28344423-2	2017	Hemodialysis patients may develop anti-platelet factor 4/heparin antibody (PF4-H Ab) because of heparin treatment in dialysis.	Heparin	57-64	platelet factor 4	Homo sapiens	75-78
27318178-5	2017	Defining the interaction partners of SCP is fundamental to evaluate if its pharmacological side effects can be as harmful as those from heparin.	Heparin	136-143	urocortin 3	Homo sapiens	37-40
25569517-2	2015	Heparin, a natural polydisperse sulfated glycosaminoglycan, is known to allosterically modulate plasmin activity.	Heparin	0-7	plasminogen	Homo sapiens	96-103
25130770-7	2015	We further showed that HCII could up-regulate cancer cell migration through the activation of PI3K, which acts upstream of Rac1 and Cdc42, and this effect could be blocked by heparin.	Heparin	175-182	serpin family D member 1	Homo sapiens	23-27
25130770-7	2015	We further showed that HCII could up-regulate cancer cell migration through the activation of PI3K, which acts upstream of Rac1 and Cdc42, and this effect could be blocked by heparin.	Heparin	175-182	cell division cycle 42	Homo sapiens	132-137
25130770-8	2015	We suggest that HCII is a novel metastasis enhancer and may be used as a prognostic predictor for heparin treatment in NSCLC.	Heparin	98-105	serpin family D member 1	Homo sapiens	16-20
25002339-9	2015	This study confirms that testing for anti-PF4/H IgG antibodies should be restricted to ICU-patients who develop a platelet count decrease of &gt;50 % that begins after day four of heparin treatment (which may have started before ICU admission).	Heparin	180-187	platelet factor 4	Homo sapiens	42-47
27585400-2	2017	We reported that 2-O, 3-O desulfated heparin (ODSH) inhibits the release of HMGB1 from murine macrophages triggered by neutrophil elastase both in vivo and in vitro.	Heparin	37-44	high mobility group box 1	Mus musculus	76-81
32182331-10	2020	Heparin downregulates hepcidin, and reduces TGF-beta2-mediated increase in ferritin and ROS.	Heparin	0-7	hepcidin antimicrobial peptide	Bos taurus	22-30
31115719-5	2020	Here, BMP-2 concentration increased systematically with incorporation of Hep, and higher concentrations were achieved by covalent conjugation.	Heparin	73-76	bone morphogenetic protein 2	Homo sapiens	6-11
27714919-5	2017	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a prothrombotic response to heparin therapy with platelet-activating, anti-platelet factor 4 (PF4)/heparin antibodies leading to thrombocytopenia associated with thromboembolism.	Heparin	20-27	platelet factor 4	Homo sapiens	132-154
27714919-5	2017	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a prothrombotic response to heparin therapy with platelet-activating, anti-platelet factor 4 (PF4)/heparin antibodies leading to thrombocytopenia associated with thromboembolism.	Heparin	20-27	platelet factor 4	Homo sapiens	156-159
27714919-5	2017	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a prothrombotic response to heparin therapy with platelet-activating, anti-platelet factor 4 (PF4)/heparin antibodies leading to thrombocytopenia associated with thromboembolism.	Heparin	90-97	platelet factor 4	Homo sapiens	132-154
27714919-5	2017	SUMMARY: Background Heparin-induced thrombocytopenia (HIT) is a prothrombotic response to heparin therapy with platelet-activating, anti-platelet factor 4 (PF4)/heparin antibodies leading to thrombocytopenia associated with thromboembolism.	Heparin	90-97	platelet factor 4	Homo sapiens	156-159
26502466-1	2015	Heparin induced thrombocytopenia (HIT) is an immune-mediated adverse reaction characterized by thrombocytopenia and paradoxical arterial or venous thrombosis, due to the formation IgG antibodies directed to a multimolecular complex of heparin-platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	235-260
26502466-1	2015	Heparin induced thrombocytopenia (HIT) is an immune-mediated adverse reaction characterized by thrombocytopenia and paradoxical arterial or venous thrombosis, due to the formation IgG antibodies directed to a multimolecular complex of heparin-platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	262-265
31658420-6	2020	Furthermore, several allosteric plasmin inhibitors based on heparin mimetics have been developed.	Heparin	60-67	plasminogen	Homo sapiens	32-39
25466847-1	2015	INTRODUCTION: Since heparin-induced thrombocytopenia (HIT), caused by the generation of antibodies against platelet factor 4 (PF4)/heparin complexes (HIT antibodies), may induce serious complications due to thrombosis, a prompt diagnosis is desirable.	Heparin	20-27	platelet factor 4	Homo sapiens	126-129
25466847-5	2015	MATERIALS AND METHODS: A murine monoclonal antibody (HIT-MoAb) against PF4/heparin complexes was used as an alternative to human HIT antibodies.	Heparin	75-82	platelet factor 4	Homo sapiens	71-74
28744338-5	2017	Likewise, kallistatin through the heparin-binding site inhibits TGF-beta-induced miR-21 synthesis and oxidative stress in endothelial cells, resulting in inhibition of endothelial-mesenchymal transition, a process contributing to fibrosis and cancer.	Heparin	34-41	microRNA 21a	Mus musculus	81-87
31944769-7	2020	The impact of storage buffer, storage period, lyophilization, and temperature on the size of PF4 and PF4/heparin (H) complexes were assessed by dynamic light scattering (DLS), while enzyme immunoassay (EIA) was used to test binding of anti-PF4/H antibodies (aPF4/H Abs) to PF4/H complexes.	Heparin	105-112	platelet factor 4	Homo sapiens	101-104
27728816-5	2016	Heparin in the gel protects FGF2 from proteolytic degradation and allows it to be released over time with preserved bioactivity.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	28-32
25263872-0	2014	Improving osteoblast functions and bone formation upon BMP-2 immobilization on titanium modified with heparin.	Heparin	102-109	bone morphogenetic protein 2	Homo sapiens	55-60
31944769-7	2020	The impact of storage buffer, storage period, lyophilization, and temperature on the size of PF4 and PF4/heparin (H) complexes were assessed by dynamic light scattering (DLS), while enzyme immunoassay (EIA) was used to test binding of anti-PF4/H antibodies (aPF4/H Abs) to PF4/H complexes.	Heparin	105-112	platelet factor 4	Homo sapiens	101-104
25263872-1	2014	The aim of this study was to develop bone morphogenetic protein-2 (BMP-2) immobilization on titanium (Ti) modified by heparin for improving osteoblast function in vitro and bone formation in vivo.	Heparin	118-125	bone morphogenetic protein 2	Homo sapiens	37-65
29296696-1	2016	Heparin-induced thrombocytopenia (HIT) is a thrombotic disorder initiated by antibodies to complexes between platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	128-131
25263872-1	2014	The aim of this study was to develop bone morphogenetic protein-2 (BMP-2) immobilization on titanium (Ti) modified by heparin for improving osteoblast function in vitro and bone formation in vivo.	Heparin	118-125	bone morphogenetic protein 2	Homo sapiens	67-72
29296696-1	2016	Heparin-induced thrombocytopenia (HIT) is a thrombotic disorder initiated by antibodies to complexes between platelet factor 4 (PF4) and heparin.	Heparin	137-144	platelet factor 4	Homo sapiens	128-131
31944769-7	2020	The impact of storage buffer, storage period, lyophilization, and temperature on the size of PF4 and PF4/heparin (H) complexes were assessed by dynamic light scattering (DLS), while enzyme immunoassay (EIA) was used to test binding of anti-PF4/H antibodies (aPF4/H Abs) to PF4/H complexes.	Heparin	105-112	platelet factor 4	Homo sapiens	101-104
29296696-9	2016	These studies suggest that thrombin- or immune complex-mediated release of endogenous antigenic PF4/polyphosphate complexes from platelets may augment the prothrombotic risk of HIT and perpetuate the risk of thrombosis after heparin has been discontinued.	Heparin	225-232	platelet factor 4	Homo sapiens	96-99
27566697-3	2016	Aims of the present study are (1) to evaluate a possible role of low-molecular-weight-heparins (LMWHs) in the modulation of the expression of TF, TFPI, TFPI2 and VEGF in placentae from thrombophilic women and (2) to study the possible role of endothelium in the placental expression of markers involved in haemostasis and angiogenesis.	Heparin	86-94	tissue factor pathway inhibitor	Homo sapiens	146-150
25263872-6	2014	In conclusion, BMP-2 immobilized Ti modified heparin implants seemed to be a suitable delivery system for BMP-2 to improve osteoblast functions and new bone formation at the defect area around an implant.	Heparin	45-52	bone morphogenetic protein 2	Homo sapiens	15-20
25263872-6	2014	In conclusion, BMP-2 immobilized Ti modified heparin implants seemed to be a suitable delivery system for BMP-2 to improve osteoblast functions and new bone formation at the defect area around an implant.	Heparin	45-52	bone morphogenetic protein 2	Homo sapiens	106-111
25183015-8	2014	CXCL4 (in association with heparin treatment) and MPO declined over 6 hours during ACS.	Heparin	27-34	platelet factor 4	Homo sapiens	0-5
32512680-6	2016	HIGHLIGHT: We fractionated DSPP-derived proteins from the dental pulp of developing porcine incisors using heparin chromatography.	Heparin	107-114	dentin sialophosphoprotein	Homo sapiens	27-31
31573759-12	2020	CONCLUSIONS: We provide a template for characterizing interactions of newly developed heparin-based anticoagulant drugs with proteins, especially PF4 and the resulting potential antigenicity.	Heparin	86-93	platelet factor 4	Homo sapiens	146-149
25196151-5	2014	Pharmacological manipulations of signaling gradients using heparin and dextran sulfate showed that pattern organizing centers correspond precisely with WntA, wingless, Wnt6, and Wnt10 expression patterns, thus suggesting a role for Wnt signaling in color pattern induction.	Heparin	59-66	Wnt family member 6	Homo sapiens	168-172
32036969-7	2020	The gene ontology terms of DEG were highly enriched in heparin binding (9 genes including COMP, CTGF, and IMPG2), glycosaminoglycan binding (10 genes including PCOLCE, POSTN, and RSPO3), and response to estradiol and ion transport (AREG, RAMP3, SFRP1, and SSTR1).	Heparin	55-62	cartilage oligomeric matrix protein	Gallus gallus	90-94
25196151-5	2014	Pharmacological manipulations of signaling gradients using heparin and dextran sulfate showed that pattern organizing centers correspond precisely with WntA, wingless, Wnt6, and Wnt10 expression patterns, thus suggesting a role for Wnt signaling in color pattern induction.	Heparin	59-66	Wnt family member 6	Homo sapiens	152-155
25100742-3	2014	Activation of the FcgammaRIIa receptor leads to immune-mediated thrombosis, which is often life threatening in patients undergoing heparin-induced thrombocytopenia or sepsis.	Heparin	131-138	Fc gamma receptor IIa	Homo sapiens	18-29
27572115-0	2016	Heparin regulates B6FS cell motility through a FAK/actin cytoskeleton axis.	Heparin	0-7	protein tyrosine kinase 2	Homo sapiens	47-50
27895229-5	2016	We found that the ability of PECAM-1 to stimulate cell migration, promote filopodia formation and trigger Cdc42 activation were lost if PECAM-1-dependent homophilic or heparin/GAG-dependent heterophilic ligand binding was disabled.	Heparin	168-175	platelet/endothelial cell adhesion molecule 1	Mus musculus	29-36
27895229-5	2016	We found that the ability of PECAM-1 to stimulate cell migration, promote filopodia formation and trigger Cdc42 activation were lost if PECAM-1-dependent homophilic or heparin/GAG-dependent heterophilic ligand binding was disabled.	Heparin	168-175	cell division cycle 42	Mus musculus	106-111
32306341-2	2020	ZG16p binds to mannose via the well-conserved GXXXD loop among mJRLs and sulfated glycosaminoglycans (e.g., heparin and heparan sulfate) via the basic patch of molecular surface.	Heparin	108-115	zymogen granule protein 16	Rattus norvegicus	0-5
31575433-2	2020	It is mediated by antibodies that recognize neoepitopes on platelet factor 4 (PF4)/heparin complexes.	Heparin	83-90	platelet factor 4	Homo sapiens	78-81
27658429-1	2016	The antigen in heparin-induced thrombocytopenia (HIT) is expressed on platelet factor 4 (PF4) when PF4 complexes with polyanions.	Heparin	15-22	platelet factor 4	Homo sapiens	89-92
27658429-1	2016	The antigen in heparin-induced thrombocytopenia (HIT) is expressed on platelet factor 4 (PF4) when PF4 complexes with polyanions.	Heparin	15-22	platelet factor 4	Homo sapiens	99-102
27412887-1	2016	Heparin-induced thrombocytopenia is a prothrombotic disorder caused by antibodies to platelet factor 4 (PF4)/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	104-107
24845712-7	2014	RESULTS: OPG concentrations were significantly lower (p&lt;0.0001) in serum (1015+-357 pg/mL) than in all plasma samples (1314+-448 pg/mL in EDTA, 1209+-417 pg/mL in heparin and 1260+-498 pg/mL in citrate).	Heparin	166-173	TNF receptor superfamily member 11b	Homo sapiens	9-12
31575433-4	2020	Since many patients develop antibodies in response to heparin, but only a few of them generate anti-PF4/heparin antibodies capable of activating platelets which consequently cause clinical complications, the performance of serologic assays is not enough to diagnose HIT.	Heparin	104-111	platelet factor 4	Homo sapiens	100-103
27412887-4	2016	In healthy donors, PF4/heparin complexes bind preferentially to B cells (&gt;90% of B cells bind to PF4/heparin in vitro) relative to neutrophils, monocytes, or T cells.	Heparin	23-30	platelet factor 4	Homo sapiens	19-22
24881028-0	2014	Heparin microparticle effects on presentation and bioactivity of bone morphogenetic protein-2.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	65-93
27412887-4	2016	In healthy donors, PF4/heparin complexes bind preferentially to B cells (&gt;90% of B cells bind to PF4/heparin in vitro) relative to neutrophils, monocytes, or T cells.	Heparin	23-30	platelet factor 4	Homo sapiens	100-103
31642823-5	2019	The specific binding of HSPG with bFGF protein was demonstrated, which was about 6-fold stronger than the binding of bFGF with heparin.	Heparin	127-134	fibroblast growth factor 2	Rattus norvegicus	34-38
27412887-4	2016	In healthy donors, PF4/heparin complexes bind preferentially to B cells (&gt;90% of B cells bind to PF4/heparin in vitro) relative to neutrophils, monocytes, or T cells.	Heparin	104-111	platelet factor 4	Homo sapiens	19-22
27412887-5	2016	Binding of PF4 to B cells is heparin dependent, and PF4/heparin complexes are found on circulating B cells from some, but not all, patients receiving heparin.	Heparin	29-36	platelet factor 4	Homo sapiens	11-14
24881028-8	2014	In summary, our results suggest that heparin microparticles stably retain large amounts of bioactive BMP-2 for prolonged periods of time, and that presentation of BMP-2 via heparin microparticles can elicit cell responses comparable to soluble BMP-2 treatment.	Heparin	37-44	bone morphogenetic protein 2	Homo sapiens	101-106
24881028-8	2014	In summary, our results suggest that heparin microparticles stably retain large amounts of bioactive BMP-2 for prolonged periods of time, and that presentation of BMP-2 via heparin microparticles can elicit cell responses comparable to soluble BMP-2 treatment.	Heparin	173-180	bone morphogenetic protein 2	Homo sapiens	163-168
24881028-8	2014	In summary, our results suggest that heparin microparticles stably retain large amounts of bioactive BMP-2 for prolonged periods of time, and that presentation of BMP-2 via heparin microparticles can elicit cell responses comparable to soluble BMP-2 treatment.	Heparin	173-180	bone morphogenetic protein 2	Homo sapiens	163-168
27412887-5	2016	Binding of PF4 to B cells is heparin dependent, and PF4/heparin complexes are found on circulating B cells from some, but not all, patients receiving heparin.	Heparin	56-63	platelet factor 4	Homo sapiens	11-14
27412887-5	2016	Binding of PF4 to B cells is heparin dependent, and PF4/heparin complexes are found on circulating B cells from some, but not all, patients receiving heparin.	Heparin	56-63	platelet factor 4	Homo sapiens	52-55
27412887-5	2016	Binding of PF4 to B cells is heparin dependent, and PF4/heparin complexes are found on circulating B cells from some, but not all, patients receiving heparin.	Heparin	56-63	platelet factor 4	Homo sapiens	11-14
27412887-5	2016	Binding of PF4 to B cells is heparin dependent, and PF4/heparin complexes are found on circulating B cells from some, but not all, patients receiving heparin.	Heparin	56-63	platelet factor 4	Homo sapiens	52-55
27412887-8	2016	Binding of PF4/heparin complexes to B cells is mediated through the interaction between complement and complement receptor 2 (CR2 [CD21]).	Heparin	15-22	platelet factor 4	Homo sapiens	11-14
27301751-1	2016	Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma.	Heparin	15-22	serpin family D member 1	Homo sapiens	92-96
27301751-1	2016	Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma.	Heparin	24-27	serpin family D member 1	Homo sapiens	92-96
27599556-7	2016	Heparin also decreased the TNF-alpha-induced mRNA and protein expression levels of IL-6, IL-8, TNF-alpha and cyclin D1 in a dose-dependent manner.	Heparin	0-7	cyclin D1	Homo sapiens	109-118
27599556-10	2016	In conclusion, the results of the present study revealed that heparin inhibited the TNF-alpha-induced proliferation, cytokine production, expression of cyclin D1 and activation of NF-kappaB signaling in FLSs, indicating the therapeutic potential of heparin in the treatment of RA.	Heparin	62-69	cyclin D1	Homo sapiens	152-161
27599556-10	2016	In conclusion, the results of the present study revealed that heparin inhibited the TNF-alpha-induced proliferation, cytokine production, expression of cyclin D1 and activation of NF-kappaB signaling in FLSs, indicating the therapeutic potential of heparin in the treatment of RA.	Heparin	249-256	cyclin D1	Homo sapiens	152-161
27564657-5	2016	METHODS: TAFI activation by thrombin or plasmin was studied in the presence of physiological anionic molecules (polyphosphate, heparin, hyaluronan, DNA and dermatan sulfate) and the non-physiological sodium dodecyl sulfate (SDS).	Heparin	127-134	carboxypeptidase B2	Homo sapiens	9-13
24850085-8	2014	Cell attachment to peptides G1EF1, G1EF2, G2EF1, G3EF4, and G5EF4 was inhibited by heparin, and peptides G1EF1, G1EF2, and G2EF1 specifically bound to syndecan-overexpressing cells.	Heparin	83-90	syndecan 1	Homo sapiens	151-159
27564657-7	2016	RESULTS: Unfractioned heparin, calcium-saturated polyphosphate with an average chain length of 100 monomers (Ca-PolyP100) and SDS significantly enhanced TAFI activation by thrombin and plasmin.	Heparin	22-29	carboxypeptidase B2	Homo sapiens	153-157
24357546-5	2014	Heparin increased gene expression of chain initiation and modification enzymes including EXT1 and NDST1, as well as core proteins SDC2 and GPC6.	Heparin	0-7	exostosin glycosyltransferase 1	Homo sapiens	89-93
27564657-7	2016	RESULTS: Unfractioned heparin, calcium-saturated polyphosphate with an average chain length of 100 monomers (Ca-PolyP100) and SDS significantly enhanced TAFI activation by thrombin and plasmin.	Heparin	22-29	plasminogen	Homo sapiens	185-192
31642823-5	2019	The specific binding of HSPG with bFGF protein was demonstrated, which was about 6-fold stronger than the binding of bFGF with heparin.	Heparin	127-134	fibroblast growth factor 2	Rattus norvegicus	117-121
24357546-5	2014	Heparin increased gene expression of chain initiation and modification enzymes including EXT1 and NDST1, as well as core proteins SDC2 and GPC6.	Heparin	0-7	glypican 6	Homo sapiens	139-143
33455219-5	2019	The most promising variants hCXCL12 K24/K27/R41/R47A and hCXCL12 Q48K were used for release studies from starPEG-heparin-hydrogels.	Heparin	113-120	C-X-C motif chemokine ligand 12	Homo sapiens	28-35
24832898-6	2014	In the presence of heparin, a well-known activator of FGF signaling, cystic morphology with lumen expansion was observed in cultures containing FGF1, FGF7, or FGF10, but growth arrest was observed in cultures containing FGF2 or FGF9.	Heparin	19-26	fibroblast growth factor 2	Mus musculus	220-224
24463147-5	2014	In contrast, "acoustic" mass, calculated from quartz crystal micro balance with dissipation monitoring, showed the lowest mass and dissipation values for CS2.6 (highest sulfation degree) multilayers indicating formation of stiffer layers compared to heparin and CS1.6 layers which led to higher mass and dissipation values.	Heparin	250-257	calsyntenin 2	Mus musculus	154-157
26905366-0	2016	A Novel PF4-Dependent Platelet Activation Assay Identifies Patients Likely to Have Heparin-Induced Thrombocytopenia/Thrombosis.	Heparin	83-90	platelet factor 4	Homo sapiens	8-11
26905366-1	2016	BACKGROUND: Almost without exception, patients with heparin-induced thrombocytopenia/thrombosis (HIT) have antibodies that recognize platelet factor 4 (PF4) in a complex with heparin; however, many heparin-treated patients without HIT are also antibody-positive.	Heparin	52-59	platelet factor 4	Homo sapiens	152-155
26905366-1	2016	BACKGROUND: Almost without exception, patients with heparin-induced thrombocytopenia/thrombosis (HIT) have antibodies that recognize platelet factor 4 (PF4) in a complex with heparin; however, many heparin-treated patients without HIT are also antibody-positive.	Heparin	175-182	platelet factor 4	Homo sapiens	152-155
26905366-1	2016	BACKGROUND: Almost without exception, patients with heparin-induced thrombocytopenia/thrombosis (HIT) have antibodies that recognize platelet factor 4 (PF4) in a complex with heparin; however, many heparin-treated patients without HIT are also antibody-positive.	Heparin	175-182	platelet factor 4	Homo sapiens	152-155
31215255-1	2019	Objective: Heparanase (HPA) is an endo-beta-D-glucuronidase capable of degrading heparin sulphate (HS) and heparin side chains.	Heparin	107-114	glucuronidase beta	Homo sapiens	39-59
31220752-1	2019	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize platelet factor 4/heparin (PF4/hep)-complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	137-144
27380556-5	2016	HIT has features of both B-cell and T-cell immune responses; uptake of PF4/heparin complexes into macrophages ("macropinocytosis") facilitates the anti-PF4/heparin immune response.	Heparin	75-82	platelet factor 4	Homo sapiens	152-155
27380556-5	2016	HIT has features of both B-cell and T-cell immune responses; uptake of PF4/heparin complexes into macrophages ("macropinocytosis") facilitates the anti-PF4/heparin immune response.	Heparin	156-163	platelet factor 4	Homo sapiens	71-74
27380556-7	2016	Sometimes, HIT antibodies recognize PF4 bound to (platelet-associated) chondroitin sulfate, explaining how HIT might occur without concurrent or recent heparin (delayed-onset HIT, "spontaneous HIT syndrome").	Heparin	152-159	platelet factor 4	Homo sapiens	36-39
32261381-4	2014	Then, the DA-g-HepLP and DA-g-Hep are used to prepare surface coated heparin-mimicking substrates; the polyethersulfone (PES) dialysis membrane is chosen as the model substrate.	Heparin	69-76	dystroglycan 1	Homo sapiens	10-14
31441407-0	2019	[Effect of unfractionated heparin on high mobility group box 1-mediated expression of vascular endothelial cadherin].	Heparin	26-33	high mobility group box 1	Homo sapiens	37-62
25343675-2	2014	This review summarizes the current knowledge of plasma PAPP-A in relation to nonpregnant individuals focusing on patients with ACS, discusses its use as a possible biomarker for diagnosis and prognosis in ACS, briefly describes the challenges in different assay technologies and describes the effect of heparin administration on PAPP-A concentrations in plasma.	Heparin	303-310	pappalysin 1	Homo sapiens	55-61
25374012-1	2014	Heparin-induced thrombocytopenia (HIT) is a life and limb-threatening thrombotic complication of heparin, which is the result of platelet activation by anti-PF4/heparin antibodies.	Heparin	0-7	platelet factor 4	Homo sapiens	157-160
25374012-1	2014	Heparin-induced thrombocytopenia (HIT) is a life and limb-threatening thrombotic complication of heparin, which is the result of platelet activation by anti-PF4/heparin antibodies.	Heparin	97-104	platelet factor 4	Homo sapiens	157-160
27558507-1	2016	BACKGROUND: Heparin-induced thrombocytopenia is caused by antibodies (Abs) specific to platelet factor 4 (PF4)/heparin complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	106-109
27558507-11	2016	The heparin-binding affinity of the circulating PF4 was similar between RA patients and OA patients; however, the IgG fractions isolated from the sera of RA patients contained PF4 more frequently (69.2 %) than those from OA patients (10.2 %).	Heparin	4-11	platelet factor 4	Homo sapiens	48-51
27143444-0	2016	Specific inhibition of secreted NRG1 types I-II by heparin enhances Schwann Cell myelination.	Heparin	51-58	neuregulin 1	Mus musculus	32-36
27143444-6	2016	The myelin promoting activity of heparin results from specific inhibition of the soluble immunoglobulin (Ig)-containing isoforms of neuregulin 1 (i.e., NRG1 types I and II) that negatively regulates myelination.	Heparin	33-40	neuregulin 1	Mus musculus	152-156
31441407-1	2019	OBJECTIVE: To observe the damage of high mobility group box 1 (HMGB1) on human umbilical vein endothelial cell (HUVEC) barrier permeability and the protective effect of unfractionated heparin (UFH), and to explore the down-regulated protection effect mechanism of UFH on HMGB1-mediated vascular endothelial cadherin (VE-cadherin) expression.	Heparin	264-267	high mobility group box 1	Homo sapiens	36-61
26966871-1	2016	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is a drug-mediated, prothrombotic disorder caused by immunization against platelet factor 4 (PF4) after complex formation with heparin or other polyanions.	Heparin	14-21	platelet factor 4	Homo sapiens	146-149
24002822-5	2014	Several genes, including those encoding granule proteases and enzymes involved in heparin biosynthesis, were downregulated in Hdc(-/-) peritoneal mast cells.	Heparin	82-89	histidine decarboxylase	Mus musculus	126-129
31441407-1	2019	OBJECTIVE: To observe the damage of high mobility group box 1 (HMGB1) on human umbilical vein endothelial cell (HUVEC) barrier permeability and the protective effect of unfractionated heparin (UFH), and to explore the down-regulated protection effect mechanism of UFH on HMGB1-mediated vascular endothelial cadherin (VE-cadherin) expression.	Heparin	264-267	high mobility group box 1	Homo sapiens	63-68
26966871-1	2016	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is a drug-mediated, prothrombotic disorder caused by immunization against platelet factor 4 (PF4) after complex formation with heparin or other polyanions.	Heparin	180-187	platelet factor 4	Homo sapiens	146-149
31205102-8	2019	RESULTS: Of the 89 subjects included, 22 (24.7%) were positive for anti-PF4/heparin antibody.	Heparin	76-83	platelet factor 4	Homo sapiens	72-75
27013193-9	2016	Moreover, growth of tumor xenografts by Hpa2-overexpressing cells was unaffected by administration of a mAb that targets the heparin-binding domain of Hpa2, implying that Hpa2 function does not rely on heparanase or heparan sulfate.	Heparin	125-132	heparanase 2 (inactive)	Homo sapiens	151-155
27013193-9	2016	Moreover, growth of tumor xenografts by Hpa2-overexpressing cells was unaffected by administration of a mAb that targets the heparin-binding domain of Hpa2, implying that Hpa2 function does not rely on heparanase or heparan sulfate.	Heparin	125-132	heparanase 2 (inactive)	Homo sapiens	151-155
31074986-0	2019	On the Process of Discovering Leads That Target the Heparin-Binding Site of Neutrophil Elastase in the Sputum of Cystic Fibrosis Patients.	Heparin	52-59	elastase, neutrophil expressed	Homo sapiens	76-95
26890038-2	2016	To target human metastatic breast cancer as well as improving patient compliance, we developed an orally active low molecular weight heparin (LMWH)-taurocholate conjugated with tetrameric deoxycholic acid, namely LHTD4, which followed by physical complexation with a synthetic bile acid enhancer, DCK.	Heparin	133-140	deoxycytidine kinase	Homo sapiens	297-300
31074986-3	2019	We reasoned that allosteric agents targeting the heparin-binding site of neutrophil elastase would offer a therapeutic paradigm.	Heparin	49-56	elastase, neutrophil expressed	Homo sapiens	73-92
30565254-9	2019	BMP-2 and OC mRNA expressions were significantly higher in cells exposed to heparin than control group after 1 day (P &lt; 0.05).	Heparin	76-83	bone morphogenetic protein 2	Homo sapiens	0-5
30565254-10	2019	CONCLUSIONS: Heparin was biocompatible in hDPCs, induced osteogenic bioactivity and enhanced mRNA expression of osteo/odontogenic markers BMP-2 and OC.	Heparin	13-20	bone morphogenetic protein 2	Homo sapiens	138-143
31139717-5	2019	Here, we report the discovery of a specific, glycomimetic Langerin ligand employing a heparin-inspired design strategy and structural characterization by NMR spectroscopy and molecular docking.	Heparin	86-93	CD207 molecule	Homo sapiens	58-66
26607136-2	2016	Both TFPI and FXa interact with several plasma proteins (e. g. prothrombin, FV/FVa, protein S) and non-proteinaceous compounds (e. g. phospholipids, heparin).	Heparin	149-156	tissue factor pathway inhibitor	Homo sapiens	5-9
26607136-6	2016	Unfractionated heparin at concentrations (0.2-1 U/ml) enhanced FXa inhibition by TFPI ~8-fold, but impaired inhibition at concentrations &gt; 1 U/ml.	Heparin	15-22	tissue factor pathway inhibitor	Homo sapiens	81-85
26839156-11	2016	HL activity (mean +- standard deviation [SD], mumol free fatty acid/mL post-heparin plasma.h)-9.83 +- 4.25 versus 9.92 +- 5.20, p = 0.707-and sdLDL levels (mg/dL)-23.1 +- 10.7 versus 22.6 +- 8.4, p = 0.83-were similar.	Heparin	76-83	lipase C, hepatic type	Homo sapiens	0-2
30894640-5	2019	SH and HE influenced MMP2 and TIMP3 protein levels and MMP2 activity.	Heparin	7-9	matrix metallopeptidase 2	Homo sapiens	21-25
30894640-5	2019	SH and HE influenced MMP2 and TIMP3 protein levels and MMP2 activity.	Heparin	7-9	matrix metallopeptidase 2	Homo sapiens	55-59
30442678-7	2019	Def++ mice were resistant to thromboprophylaxis with heparin.	Heparin	53-60	UTP25 small subunit processome component	Mus musculus	0-3
26659923-1	2016	Platelet-activating antibodies, which recognize platelet factor 4 (PF4)/heparin complexes, induce spontaneous heparin-induced thrombocytopenia (HIT) syndrome or fondaparinux-associated HIT without exposure to unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	110-117	platelet factor 4	Homo sapiens	67-70
26659923-1	2016	Platelet-activating antibodies, which recognize platelet factor 4 (PF4)/heparin complexes, induce spontaneous heparin-induced thrombocytopenia (HIT) syndrome or fondaparinux-associated HIT without exposure to unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	110-117	platelet factor 4	Homo sapiens	67-70
26659923-1	2016	Platelet-activating antibodies, which recognize platelet factor 4 (PF4)/heparin complexes, induce spontaneous heparin-induced thrombocytopenia (HIT) syndrome or fondaparinux-associated HIT without exposure to unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	233-236	platelet factor 4	Homo sapiens	67-70
26659923-1	2016	Platelet-activating antibodies, which recognize platelet factor 4 (PF4)/heparin complexes, induce spontaneous heparin-induced thrombocytopenia (HIT) syndrome or fondaparinux-associated HIT without exposure to unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH).	Heparin	110-117	platelet factor 4	Homo sapiens	67-70
26955355-2	2015	Heparins seem to act by interfering with BMP6 signaling pathways that control the expression of liver hepcidin, causing the suppression of SMAD1/5/8 phosphorylation.	Heparin	0-8	SMAD family member 1	Homo sapiens	139-146
26494902-4	2016	Here, we treated 6-week-old mdx mice for 4 weeks with the clinically used anticoagulant drug heparin known to activate p38 mitogen-activated protein kinase, and determined the impact of this pharmacological intervention on the dystrophic phenotype.	Heparin	93-100	mitogen-activated protein kinase 14	Mus musculus	119-122
26613641-12	2016	PCC with low or no heparin shortened the lag phase (p&lt;0.01), whereas 1 heparin containing PCC prolonged the lag phase by 66% (p&lt;0.01).	Heparin	74-81	crystallin gamma D	Homo sapiens	93-96
26613641-15	2016	Patients with an implanted left ventricular assist device and anticoagulated with vitamin-K antagonists could benefit from the use of PCC with low heparin content when surgery or bleeding requires emergency reversal.	Heparin	147-154	crystallin gamma D	Homo sapiens	134-137
30205243-2	2018	Glycosaminoglycan (GAG) sugars are known to enhance BMP activity in vitro and in vivo; here the interactions of BMP-2 with various glycosaminoglycan classes were compared and shown to be selective for heparin over other comparable saccharides.	Heparin	201-208	bone morphogenetic protein 2	Homo sapiens	112-117
26898225-12	2016	A heparin-free APCC better corrected an in vitro albumin-induced dilutional coagulopathy than a four-factor PCC, despite of blocking heparin with protamine.	Heparin	2-9	crystallin gamma D	Homo sapiens	16-19
33429678-10	2015	Heparin-functionalized GelNB (i.e., GelNB-Hep) hydrogels were able to sequester and slowly release hepatocyte growth factor (HGF) in vitro.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	99-123
33429678-10	2015	Heparin-functionalized GelNB (i.e., GelNB-Hep) hydrogels were able to sequester and slowly release hepatocyte growth factor (HGF) in vitro.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	125-128
26370927-0	2015	Controlled dual delivery of fibroblast growth factor-2 and Interleukin-10 by heparin-based coacervate synergistically enhances ischemic heart repair.	Heparin	77-84	fibroblast growth factor 2	Mus musculus	28-54
26370927-3	2015	We investigated the bioactivity and therapeutic potential of an injectable, heparin-based coacervate co-delivering an angiogenic factor, fibroblast growth factor-2 (FGF2), and an anti-inflammatory cytokine, Interleukin-10 (IL-10) in a spatially and temporally controlled manner.	Heparin	76-83	fibroblast growth factor 2	Mus musculus	137-163
30205243-3	2018	The minimal chain lengths and specific sulfate moieties required for heparin-derived oligosaccharide binding to BMP-2, and the ability of such oligosaccharides to promote BMP-2-induced osteogenic differentiation in vitro were then determined.	Heparin	69-76	bone morphogenetic protein 2	Homo sapiens	112-117
26370927-3	2015	We investigated the bioactivity and therapeutic potential of an injectable, heparin-based coacervate co-delivering an angiogenic factor, fibroblast growth factor-2 (FGF2), and an anti-inflammatory cytokine, Interleukin-10 (IL-10) in a spatially and temporally controlled manner.	Heparin	76-83	fibroblast growth factor 2	Mus musculus	165-169
26034014-2	2015	Here, basic fibroblast growth factor (bFGF) was immobilized on porous polymer materials using a mild and biologically safe three-step reaction: (1) modification with a novel surface-modification peptide (penta-lysine-mussel adhesive sequence, which reacts with various matrices), (2) electrostatic binding of heparin with introduced penta-lysine, and (3) biologically specific binding of bFGF to heparin.	Heparin	396-403	fibroblast growth factor 2	Mus musculus	38-42
30205243-3	2018	The minimal chain lengths and specific sulfate moieties required for heparin-derived oligosaccharide binding to BMP-2, and the ability of such oligosaccharides to promote BMP-2-induced osteogenic differentiation in vitro were then determined.	Heparin	69-76	bone morphogenetic protein 2	Homo sapiens	171-176
30205243-4	2018	BMP-2 could bind to heparin hexasaccharides (dp6) and octasaccharides (dp8), but decasaccharides (dp10) were the minimum chain length required for both efficient binding of BMP-2 and consequent heparin-dependent cell responses.	Heparin	20-27	bone morphogenetic protein 2	Homo sapiens	0-5
30160040-2	2018	This study aims to maintain the long-term controlled release of bFGF by utilizing a collagen/heparin bi-affinity multilayer delivery system (CHBMDS), which is fabricated by the alternate deposition of negatively charged heparin, positively charged collagen, and CBD-bFGF (a collagen-binding domain [CBD] was fused into the native bFGF) via specific or electrostatic interaction.	Heparin	93-100	fibroblast growth factor 2	Rattus norvegicus	64-68
26580551-8	2015	Heparin partially removed microparticle-bound protein C inhibitor, supporting our assumption that protein C inhibitor is bound via phospholipids.	Heparin	0-7	serpin family A member 5	Homo sapiens	46-65
26580551-8	2015	Heparin partially removed microparticle-bound protein C inhibitor, supporting our assumption that protein C inhibitor is bound via phospholipids.	Heparin	0-7	serpin family A member 5	Homo sapiens	98-117
30299938-4	2018	Herein, we report a novel nanocomposite prepared by heparin-mediated cross-linking of urokinase with magnetite nanoparticles (MNPs@uPA).	Heparin	52-59	plasminogen activator, urokinase	Rattus norvegicus	131-134
26231738-0	2015	Fabrication of a BMP-2-immobilized porous microsphere modified by heparin for bone tissue engineering.	Heparin	66-73	bone morphogenetic protein 2	Homo sapiens	17-22
26231738-1	2015	The purpose of this study was to fabricate BMP-2-immobilized porous poly(lactide-co-glycolide) (PLGA) microspheres (PMS) modified with heparin for bone regeneration.	Heparin	135-142	bone morphogenetic protein 2	Homo sapiens	43-48
30648066-1	2018	Heparin-induced thrombocytopenia (HIT) is an adverse reaction to the administration of heparin due to the activation of the platelets by the immunoglobulin G (IgG) antibody-platelet factor 4 (PF4)/heparin immune complex.	Heparin	0-7	platelet factor 4	Homo sapiens	192-195
26160844-5	2015	Intravenous injection of such heparin derivatives (with cancer cells pre-treated with galectin-3 followed by 3 subcutaneous injections of the derivatives) abolished the circulating galectin-3-mediated increase in lung metastasis of human melanoma and colon cancer cells in nude mice.	Heparin	30-37	galectin 3	Homo sapiens	181-191
26160844-6	2015	Structural analysis using nuclear magnetic resonance and synchrotron radiation circular dichroism spectroscopies showed that the modified heparin derivatives bind to the galectin-3 carbohydrate-recognition domain.	Heparin	138-145	galectin 3	Homo sapiens	170-180
26160844-7	2015	Thus, these chemically modified, non-anticoagulant, low-sulfated heparin derivatives are potent galectin-3 binding inhibitors with substantial potential as anti-metastasis/cancer drugs.	Heparin	65-72	galectin 3	Homo sapiens	96-106
25959412-9	2015	Moreover, luciferase reporter assays, inhibitor experiments and gene expression analyses revealed that heparin had putative permissive effects on osteogenic signaling via the BMP pathway and reduced the mRNA expression of the Wnt pathway inhibitors dickkopf 1 (DKK1) and sclerostin (SOST).	Heparin	103-110	dickkopf WNT signaling pathway inhibitor 1	Homo sapiens	249-259
25959412-9	2015	Moreover, luciferase reporter assays, inhibitor experiments and gene expression analyses revealed that heparin had putative permissive effects on osteogenic signaling via the BMP pathway and reduced the mRNA expression of the Wnt pathway inhibitors dickkopf 1 (DKK1) and sclerostin (SOST).	Heparin	103-110	dickkopf WNT signaling pathway inhibitor 1	Homo sapiens	261-265
26198856-1	2015	BACKGROUND: Heparin therapy may induce anti-platelet factor 4/heparin antibody (PF4-H Ab).	Heparin	12-19	platelet factor 4	Homo sapiens	80-83
26198856-2	2015	Hemodialysis patients receive scheduled heparin and are at a risk of developing PF4-H Ab.	Heparin	40-47	platelet factor 4	Homo sapiens	80-83
24325177-8	2014	Additionally, PAPP-A is known to interact with heparin, which may diminish its potential utility in every day clinical life.	Heparin	47-54	pappalysin 1	Homo sapiens	14-20
24266905-1	2014	BACKGROUND: We tested the hypothesis that heparin administration prior to the emergence of tissue factor (TF) would increase plasma TF pathway inhibitor (TFPI) and attenuate TF-mediated thrombin generation during simulated cardiopulmonary bypass (CPB).	Heparin	42-49	tissue factor pathway inhibitor	Homo sapiens	132-152
24266905-1	2014	BACKGROUND: We tested the hypothesis that heparin administration prior to the emergence of tissue factor (TF) would increase plasma TF pathway inhibitor (TFPI) and attenuate TF-mediated thrombin generation during simulated cardiopulmonary bypass (CPB).	Heparin	42-49	tissue factor pathway inhibitor	Homo sapiens	154-158
24266905-4	2014	In the two TFPI boost groups, 50 U/kg of heparin was given to the donors intravenously five minutes before donation to boost plasma TFPI levels.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	11-15
24266905-4	2014	In the two TFPI boost groups, 50 U/kg of heparin was given to the donors intravenously five minutes before donation to boost plasma TFPI levels.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	132-136
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	tissue factor pathway inhibitor	Homo sapiens	20-24
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	tissue factor pathway inhibitor	Homo sapiens	114-118
24266905-10	2014	CONCLUSIONS: Heparin-induced TFPI elevation attenuates TF-mediated thrombin generation.	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	29-33
26524358-6	2015	RESULTS: TLR3 expression, and not expression of TLR 7 or TLR8,was significantly increased in heparin-treated DCs as compared to levels detected in the DCs without heparin treatment (t =2.849,P less than 0.05;t =3.027,P less than 0.05).	Heparin	93-100	toll like receptor 3	Homo sapiens	9-13
26524358-6	2015	RESULTS: TLR3 expression, and not expression of TLR 7 or TLR8,was significantly increased in heparin-treated DCs as compared to levels detected in the DCs without heparin treatment (t =2.849,P less than 0.05;t =3.027,P less than 0.05).	Heparin	163-170	toll like receptor 3	Homo sapiens	9-13
30648066-1	2018	Heparin-induced thrombocytopenia (HIT) is an adverse reaction to the administration of heparin due to the activation of the platelets by the immunoglobulin G (IgG) antibody-platelet factor 4 (PF4)/heparin immune complex.	Heparin	87-94	platelet factor 4	Homo sapiens	192-195
25998835-0	2015	The effect of heparin on pregnancy associated plasma protein-A concentration in healthy, non-pregnant individuals.	Heparin	14-21	pappalysin 1	Homo sapiens	25-62
23939423-9	2013	The ER IP3 receptor antagonist heparin blocked this release, indicating that the receptor is required for activity.	Heparin	31-38	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	7-19
30218780-8	2018	Notably, heparin could reinforce the recognition between rhBMP-2 and its receptors (BMPRs) whereas weaken its binding to its antagonist Noggin.	Heparin	9-16	noggin	Homo sapiens	136-142
29753267-1	2018	We have previously shown that the heterodimeric cytokine interleukin-12, and the homodimer of its larger subunit p40, both bind to heparin and heparan sulfate with relatively high affinity.	Heparin	131-138	interleukin 9	Homo sapiens	113-116
24278373-9	2013	Only 6.39 +- 1.22% of labeled antibody dissociated from IONPs in heparin-treated whole blood over 4 h. The binding affinity of PECAM-1 antibody (KD) was 32 nM with a maximal binding (Bmax) of 17 x 10(5) antibody molecules/cell.	Heparin	65-72	platelet and endothelial cell adhesion molecule 1	Homo sapiens	127-134
24167632-3	2013	To lower its effective dose, we precomplexed BMP-2 with the glycosaminoglycans (GAGs) dermatan sulfate (DS) or heparin (HP), prior to loading it into a hyaluronic acid (HA) hydrogel.	Heparin	111-118	bone morphogenetic protein 2	Rattus norvegicus	45-50
25702768-8	2015	Heparin (Sdc1 analogue) and SB203580 (a p38 MAPK inhibitor), instead of insulin, alleviated Sdc1 destruction and HPSE overexpression, and effectively prevented against the reductions of tight junctions and the abnormality of intestinal permeability in HG conditions.	Heparin	0-7	syndecan 1	Mus musculus	9-13
25702768-8	2015	Heparin (Sdc1 analogue) and SB203580 (a p38 MAPK inhibitor), instead of insulin, alleviated Sdc1 destruction and HPSE overexpression, and effectively prevented against the reductions of tight junctions and the abnormality of intestinal permeability in HG conditions.	Heparin	0-7	syndecan 1	Mus musculus	92-96
25517543-4	2015	In this study, we investigate the uptake kinetics of recombinant porcine OAS1 and show that it is rapidly and efficiently internalized in a manner that can be blocked by heparin.	Heparin	170-177	2'-5'-oligoadenylate synthetase 1	Homo sapiens	73-77
25517543-5	2015	Heparin, furthermore, abolishes the antiviral activity of OAS1, demonstrating the requirement of the intracellular localization of OAS1 to inhibit the virus.	Heparin	0-7	2'-5'-oligoadenylate synthetase 1	Homo sapiens	58-62
24167632-3	2013	To lower its effective dose, we precomplexed BMP-2 with the glycosaminoglycans (GAGs) dermatan sulfate (DS) or heparin (HP), prior to loading it into a hyaluronic acid (HA) hydrogel.	Heparin	120-122	bone morphogenetic protein 2	Rattus norvegicus	45-50
29753267-3	2018	Human interleukin-12 and p40 homodimer show indistinguishable binding profiles with a panel of heparin derivatives, but that of murine interleukin-12 is distinct.	Heparin	95-102	interleukin 9	Homo sapiens	25-28
25517543-5	2015	Heparin, furthermore, abolishes the antiviral activity of OAS1, demonstrating the requirement of the intracellular localization of OAS1 to inhibit the virus.	Heparin	0-7	2'-5'-oligoadenylate synthetase 1	Homo sapiens	131-135
29753267-5	2018	Moreover the essential role of the carboxyterminal D3 domain in heparin binding is established by the failure of a truncated construct of the p40 subunit lacking this domain to bind.	Heparin	64-71	interleukin 9	Homo sapiens	142-145
29753267-8	2018	Thus overall the binding of IL-12 via its p40 subunit to heparin-related polysaccharides of the extracellular matrix appears to be functionally important since it has been conserved across mammalian species despite this structural divergence.	Heparin	57-64	interleukin 9	Homo sapiens	42-45
30248108-7	2018	We found differential affinities of CXCL1, CXCL2 and CCL2 for HS in isolated mGEnC-1 glycocalyx, heparan sulfate from bovine kidney or low molecular weight heparin in competition ELISAs using mGEnC-1 as a substrate, indicating that chemokine binding is affected by the domain structure of the different HS preparations.	Heparin	156-163	growth-regulated protein homolog gamma	Bos taurus	43-48
25711986-10	2015	In fact, CE results confirmed the inductory effect of the sulfated sugars heparin and heparan sulfate on tau hyperphosphorylation, probably because of the exposition of new sites phosphorylatable by GSK3beta.	Heparin	74-81	glycogen synthase kinase 3 beta	Homo sapiens	199-207
25489725-8	2015	RESULTS: Plasma PAPP-A was strongly elevated upon STEMI, UFH-administration and PCI with mean concentrations (95%-confidence interval) pre-PCI, post-PCI, day 1, and day 2 of 13.0 (11.2;15.2), 14.8 (13.1;16.8), 1.03 (0.90;1.18), and 1.08 (0.92;1.28) mug/L, respectively (p&lt;0.0001).	Heparin	57-60	pappalysin 1	Homo sapiens	16-22
25239670-4	2015	RESULTS: LPL activity and concentration in the post-heparin plasma exhibited a significant inverse correlation with TG, RLP-C, RLP-TG, and RLP particle size estimated as RLP-TG/RLP-C ratio and sdLDL-C, and positively correlated with HDL-C. HTGL was only inversely correlated with HDL-C. LPL concentration in the pre-heparin plasma was also inversely correlated with the RLP-TG/RLP-C ratio and other lipoprotein parameters.	Heparin	52-59	lipase C, hepatic type	Homo sapiens	240-244
23715906-6	2013	All patients had fasted for at least 6 h and were given unfractionated heparin (50 IU/kg) intravenously to reduce the physiological (18)F-FDG uptake in the myocardium.	Heparin	71-78	single-strand-selective monofunctional uracil-DNA glycosylase 1	Homo sapiens	138-141
24273488-7	2013	CONCLUSION: Heparin can significantly enhance the stimulating effects of a combination of TPO, SCF, FL, IL-6, and IL-11 supplemented with autologous serum on CFU-MK, MK, and platelet production from CB CD34+ cells.	Heparin	12-19	fms related receptor tyrosine kinase 3 ligand	Homo sapiens	100-102
23939434-6	2013	Heparin or insulin significantly prevented the increase in heparanase but decreased perlecan mRNA while heparin, but not insulin, prevented the decrease in syndecan mRNA in HG treated cells.	Heparin	104-111	syndecan 1	Homo sapiens	156-164
23939434-8	2013	Heparin may protect endothelium from HG injury by reducing heparanase and increasing syndecan while insulin inhibits heparanase expression.	Heparin	0-7	syndecan 1	Homo sapiens	85-93
23939434-9	2013	Effects with insulin plus heparin suggest interference in transcriptional regulation of heparanase and syndecan genes.	Heparin	26-33	syndecan 1	Homo sapiens	103-111
23951310-7	2013	We show that CCL18 selectivity displaces heparin bound chemokines, and that chemokines from all four chemokine sub-classes displace cell bound CCL18.	Heparin	41-48	C-C motif chemokine ligand 18	Homo sapiens	13-18
25416968-8	2015	Our results demonstrate that increased FVIII concentration shortens APTT under therapeutic doses of UFH, and that APTT thus underestimates the anticoagulant effect of UFH in pregnant women, mainly due to the increased FVIII concentration.	Heparin	100-103	coagulation factor VIII	Homo sapiens	39-44
25416968-8	2015	Our results demonstrate that increased FVIII concentration shortens APTT under therapeutic doses of UFH, and that APTT thus underestimates the anticoagulant effect of UFH in pregnant women, mainly due to the increased FVIII concentration.	Heparin	167-170	coagulation factor VIII	Homo sapiens	218-223
29723037-3	2018	Recent studies from our laboratory revealed that heparin treatment of mdx mice activates p38 MAPK, leading to an upregulation of utrophin A expression and improvements in the dystrophic phenotype.	Heparin	49-56	mitogen-activated protein kinase 14	Mus musculus	89-97
23830968-7	2013	These results show that PF4/LPS complex is immunogenic and can elicit cross-reacting antibodies against PF4/Heparin, providing an explanation for the presence of these antibodies in individuals, who were never been exposed to heparin before.	Heparin	226-233	platelet factor 4	Homo sapiens	24-27
30172259-0	2018	Sulfated non-anticoagulant heparin blocks Th2-induced asthma by modulating the IL-4/signal transducer and activator of transcription 6/Janus kinase 1 pathway.	Heparin	27-34	signal transducer and activator of transcription 6	Mus musculus	84-134
23874391-0	2013	Low molecular weight heparin relieves experimental colitis in mice by downregulating IL-1beta and inhibiting syndecan-1 shedding in the intestinal mucosa.	Heparin	21-28	syndecan 1	Mus musculus	109-119
24764177-0	2015	Controlled release of BMP-2 using a heparin-conjugated carrier system reduces in vivo adipose tissue formation.	Heparin	36-43	bone morphogenetic protein 2	Homo sapiens	22-27
32261927-8	2015	The primary amine groups of the PDAM/HD coating could be used to effectively immobilize biomolecules containing carboxylic groups such as heparin.	Heparin	138-145	TP73 antisense RNA 1	Homo sapiens	32-36
30172259-0	2018	Sulfated non-anticoagulant heparin blocks Th2-induced asthma by modulating the IL-4/signal transducer and activator of transcription 6/Janus kinase 1 pathway.	Heparin	27-34	Janus kinase 1	Mus musculus	135-149
26495958-8	2015	In contrast, in normal HBE-1 cells, fully sulfated heparin significantly suppressed only ERK signaling, COX-2 gene expression at 12 hours, and CXCL-8 gene expression at 6 and 12 hours, while desulfated heparin had no significant effects on LPS-stimulated signaling or on gene or protein expression.	Heparin	51-58	hemoglobin subunit epsilon 1	Homo sapiens	23-28
23673861-1	2013	The tight electrostatic binding of the chemokine platelet factor 4 (PF4) to polyanions induces heparin-induced thrombocytopenia, a prothrombotic adverse drug reaction caused by immunoglobulin G directed against PF4/polyanion complexes.	Heparin	95-102	platelet factor 4	Homo sapiens	68-71
30233568-5	2018	All CXCL12 forms had a similar binding affinity for heparin, the G protein-coupled chemokine receptor CXCR4 and the atypical chemokine receptor ACKR3.	Heparin	52-59	C-X-C motif chemokine ligand 12	Homo sapiens	4-10
23673861-1	2013	The tight electrostatic binding of the chemokine platelet factor 4 (PF4) to polyanions induces heparin-induced thrombocytopenia, a prothrombotic adverse drug reaction caused by immunoglobulin G directed against PF4/polyanion complexes.	Heparin	95-102	platelet factor 4	Homo sapiens	211-214
23673861-4	2013	Aptamers were shown by circular dichroism spectroscopy to induce structural changes in PF4 that resemble those induced by heparin.	Heparin	122-129	platelet factor 4	Homo sapiens	87-90
23673861-5	2013	Moreover, heparin-induced anti-human-PF4/heparin antibodies cross-reacted with human PF4/nucleic acid and PF4/aptamer complexes, as shown by an enzyme immunoassay and a functional platelet activation assay.	Heparin	10-17	platelet factor 4	Homo sapiens	37-40
23673861-5	2013	Moreover, heparin-induced anti-human-PF4/heparin antibodies cross-reacted with human PF4/nucleic acid and PF4/aptamer complexes, as shown by an enzyme immunoassay and a functional platelet activation assay.	Heparin	10-17	platelet factor 4	Homo sapiens	85-88
23673861-5	2013	Moreover, heparin-induced anti-human-PF4/heparin antibodies cross-reacted with human PF4/nucleic acid and PF4/aptamer complexes, as shown by an enzyme immunoassay and a functional platelet activation assay.	Heparin	10-17	platelet factor 4	Homo sapiens	85-88
25434537-9	2014	Plate factor 4( PF4) antibody against heparin in her blood examination was found, and HIT II was diagnosed.	Heparin	38-45	platelet factor 4	Homo sapiens	16-19
29903912-3	2018	Our hypothesis is that variants of heparin, which potently inhibit NE but are not anticoagulant, would help restore the protease-antiprotease balance in CF.	Heparin	35-42	elastase, neutrophil expressed	Homo sapiens	67-69
25023776-0	2014	Unfractionated heparin suppresses lipopolysaccharide-induced monocyte chemoattractant protein-1 expression in human microvascular endothelial cells by blocking Kruppel-like factor 5 and nuclear factor-kappaB pathway.	Heparin	15-22	Kruppel like factor 5	Homo sapiens	160-181
25023776-9	2014	UFH inhibited LPS-induced Kruppel-like factor 5 (KLF-5) mRNA and protein levels.	Heparin	0-3	Kruppel like factor 5	Homo sapiens	26-47
29903912-5	2018	Using sputa from CF patients and an NE activity assay, we found that heparins are ineffective if used in the absence of dornase.	Heparin	69-77	elastase, neutrophil expressed	Homo sapiens	36-38
25023776-9	2014	UFH inhibited LPS-induced Kruppel-like factor 5 (KLF-5) mRNA and protein levels.	Heparin	0-3	Kruppel like factor 5	Homo sapiens	49-54
25023776-12	2014	These results demonstrate that interfering with KLF-5 mediated NF-kappaB activation might contribute to the inhibitory effects of chemokines and monocytes migration by UFH in LPS-stimulated HPMECs.	Heparin	168-171	Kruppel like factor 5	Homo sapiens	48-53
25034023-3	2014	We demonstrate the presence of heparin/heparan sulfate binding sites in fibrillin-2 and -3.	Heparin	31-38	fibrillin 2	Homo sapiens	72-90
29505875-0	2018	The smaller heparin fragments bind non-specifically through the IAPP sequence: An in silico study.	Heparin	12-19	islet amyloid polypeptide	Homo sapiens	64-68
24708339-8	2014	Since binding to glycosaminoglycans (GAG) modulates the function of CXCL12, binding to heparin was analyzed.	Heparin	87-94	C-X-C motif chemokine ligand 12	Homo sapiens	68-74
29505875-3	2018	In the autopsy of TIIDM patients, IAPP rich amyloid plaques are found containing different components of extracellular matrix (ECM), including heparin.	Heparin	143-150	islet amyloid polypeptide	Homo sapiens	34-38
29505875-4	2018	For a positively charged IAPP, interaction with heparin which has accessible high density negatively charged functional groups is anticipated to moderate the fibrillation kinetics.	Heparin	48-55	islet amyloid polypeptide	Homo sapiens	25-29
25024924-0	2014	Characterisation of the interaction of neuropilin-1 with heparin and a heparan sulfate mimetic library of heparin-derived sugars.	Heparin	57-64	neuropilin 1	Homo sapiens	39-51
29505875-5	2018	Hence, the heparin has shown to affect the amyloidogenicity and cytotoxicity of IAPP depending upon its polymer length; short polymer inhibited the amyloidogenicity and longer fragment enhanced the propensity.	Heparin	11-18	islet amyloid polypeptide	Homo sapiens	80-84
25024924-0	2014	Characterisation of the interaction of neuropilin-1 with heparin and a heparan sulfate mimetic library of heparin-derived sugars.	Heparin	106-113	neuropilin 1	Homo sapiens	39-51
25024924-9	2014	Unusually, NRP-1 bound both highly sulfated and completely desulfated stretches of heparin and exhibited a complex pattern of preferences for chemically modified heparins possessing one or two sulfate groups, e.g., it bound heparin with just a 6-O sulfate group better than heparin with any two of N-sulfate, 6-O sulfate and 2-O sulfate.	Heparin	83-90	neuropilin 1	Homo sapiens	11-16
29505875-6	2018	Here using docking and molecular dynamic (MD) simulations studies, the work investigates key interactions between IAPP and different heparin fragments, those are likely involved in moderating IAPP fibrillation kinetics in presence of different length heparin fragments.	Heparin	133-140	islet amyloid polypeptide	Homo sapiens	114-118
25024924-9	2014	Unusually, NRP-1 bound both highly sulfated and completely desulfated stretches of heparin and exhibited a complex pattern of preferences for chemically modified heparins possessing one or two sulfate groups, e.g., it bound heparin with just a 6-O sulfate group better than heparin with any two of N-sulfate, 6-O sulfate and 2-O sulfate.	Heparin	162-170	neuropilin 1	Homo sapiens	11-16
25024924-9	2014	Unusually, NRP-1 bound both highly sulfated and completely desulfated stretches of heparin and exhibited a complex pattern of preferences for chemically modified heparins possessing one or two sulfate groups, e.g., it bound heparin with just a 6-O sulfate group better than heparin with any two of N-sulfate, 6-O sulfate and 2-O sulfate.	Heparin	162-169	neuropilin 1	Homo sapiens	11-16
29505875-6	2018	Here using docking and molecular dynamic (MD) simulations studies, the work investigates key interactions between IAPP and different heparin fragments, those are likely involved in moderating IAPP fibrillation kinetics in presence of different length heparin fragments.	Heparin	251-258	islet amyloid polypeptide	Homo sapiens	114-118
25024924-9	2014	Unusually, NRP-1 bound both highly sulfated and completely desulfated stretches of heparin and exhibited a complex pattern of preferences for chemically modified heparins possessing one or two sulfate groups, e.g., it bound heparin with just a 6-O sulfate group better than heparin with any two of N-sulfate, 6-O sulfate and 2-O sulfate.	Heparin	162-169	neuropilin 1	Homo sapiens	11-16
29734651-5	2018	Our data show that the hyperacetylation of Tau by p300 histone acetyltransferase (HAT) disfavors LLPS, inhibits heparin-induced aggregation, and impedes access to LLPS-initiated microtubule assembly.	Heparin	112-119	E1A binding protein p300	Homo sapiens	50-54
24720634-8	2014	Consequently, BMP-2 was immobilized on the coatings by the electrostatic attraction between CS, heparin, and BMP-2.	Heparin	96-103	bone morphogenetic protein 2	Oryctolagus cuniculus	14-19
29597024-3	2018	In this work, we developed a hydrogel surface that can mimic heparin to stabilize BMP-2 and to enhance osteogenesis by introducing heparin-mimicking sulfonated molecules such as poly-vinylsulfonic acid (PVSA) or poly-4-styrenesulfonic acid (PSS), into photo-crosslinkable hydrogel.	Heparin	61-68	bone morphogenetic protein 2	Homo sapiens	82-87
29597024-5	2018	The heparin-mimicking sulfonated hydrogels were effective to bind BMP-2 compared to unmodified MeGC hydrogel and significantly enhanced osteogenic differentiation of encapsulated bone marrow stromal cells (BMSCs) without the addition of exogenous BMP-2.	Heparin	4-11	bone morphogenetic protein 2	Homo sapiens	66-71
24750676-1	2014	Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction and prothrombotic disorder caused by immunization against platelet factor 4 (PF4) after complex formation with heparin or other polyanions.	Heparin	0-7	platelet factor 4	Homo sapiens	144-147
24750676-1	2014	Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction and prothrombotic disorder caused by immunization against platelet factor 4 (PF4) after complex formation with heparin or other polyanions.	Heparin	178-185	platelet factor 4	Homo sapiens	144-147
29597024-5	2018	The heparin-mimicking sulfonated hydrogels were effective to bind BMP-2 compared to unmodified MeGC hydrogel and significantly enhanced osteogenic differentiation of encapsulated bone marrow stromal cells (BMSCs) without the addition of exogenous BMP-2.	Heparin	4-11	bone morphogenetic protein 2	Homo sapiens	247-252
24750676-2	2014	After antibody binding to PF4/heparin complexes, HIT antibodies are capable of intravascular platelet activation by cross-linking Fc gamma receptor IIa (FcgammaRIIa) on the platelet surface leading to a platelet count decrease and/or thrombosis.	Heparin	30-37	Fc gamma receptor IIa	Homo sapiens	130-151
29597024-9	2018	This study demonstrates a novel hydrogel platform that mimics a natural protector of BMPs, heparin, to sequester and stabilize BMP-2 for increased osteoinductive signaling.	Heparin	91-98	bone morphogenetic protein 2	Homo sapiens	127-132
24750676-2	2014	After antibody binding to PF4/heparin complexes, HIT antibodies are capable of intravascular platelet activation by cross-linking Fc gamma receptor IIa (FcgammaRIIa) on the platelet surface leading to a platelet count decrease and/or thrombosis.	Heparin	30-37	Fc gamma receptor IIa	Homo sapiens	153-164
29409830-3	2018	Heparin administration protected mice from cerulein-induced AP and prevented Fib-gammaD formation.	Heparin	0-7	fibrinogen alpha chain	Mus musculus	77-80
29172900-1	2018	Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction characterized by IgG antibodies bound to complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	140-143
24269522-9	2014	DHA dilated resistance pulmonary arteries in a dose-dependent manner in hypoxic or normoxic solution, and the effects of DHA were abolished after pre-treatment with heparin (100 mug/ml), a 1,4,5-triphosphate (IP3) receptor (IP3R) inhibitor or iberiotoxin (100 nmol/L), a specific inhibitor of BKCa channel.	Heparin	165-172	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	209-222
24269522-9	2014	DHA dilated resistance pulmonary arteries in a dose-dependent manner in hypoxic or normoxic solution, and the effects of DHA were abolished after pre-treatment with heparin (100 mug/ml), a 1,4,5-triphosphate (IP3) receptor (IP3R) inhibitor or iberiotoxin (100 nmol/L), a specific inhibitor of BKCa channel.	Heparin	165-172	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	224-228
24629593-6	2014	After sperm treatment with heparin to promote capacitation, the percentage of cells with E1-pattern (56 +- 12%) significantly decreased; concomitantly, the percentage of spermatozoa depicting an E-cadherin staining pattern similar to E1-pattern but showing a signal loss in the acrosomal cap (E2-pattern: 40 +- 11%) increased.	Heparin	27-34	cadherin 1	Bos taurus	195-205
23104956-7	2014	Plasma OPG levels expressly changed during both enoxaparin (chi(2) analysis of variance [ANOVA] = 31.13, P &lt; .016) and UFH (chi(2) ANOVA = 8.26, P = .016) anticoagulation, and its increment at T10 and T180 was significantly different between both the heparins.	Heparin	254-262	TNF receptor superfamily member 11b	Homo sapiens	7-10
29172900-11	2018	Absorbance readings from the anti-PF4/heparin EIA using platelet-derived and rhPF4 were highly correlated (n = 194; r = 0.9545, p &lt; 0.0001); and functional release of serotonin in the PF4-SRA induced by anti-PF4/heparin antibodies was similar to either platelet-derived or rhPF4 and heparin (r = 0.9597, p &lt; 0.0001).	Heparin	38-45	platelet factor 4	Homo sapiens	79-82
29172900-11	2018	Absorbance readings from the anti-PF4/heparin EIA using platelet-derived and rhPF4 were highly correlated (n = 194; r = 0.9545, p &lt; 0.0001); and functional release of serotonin in the PF4-SRA induced by anti-PF4/heparin antibodies was similar to either platelet-derived or rhPF4 and heparin (r = 0.9597, p &lt; 0.0001).	Heparin	38-45	platelet factor 4	Homo sapiens	79-82
29559750-15	2018	Recommendations were written in the three following areas 1) Heparin dosing and monitoring for initiation and maintenance of CPB, 2) Heparin contraindications and heparin alternatives, 3) Reversal of anticoagulation during cardiac operations.	Heparin	61-68	carboxypeptidase B2	Homo sapiens	125-131
24667603-6	2014	In C57BL/6 mouse aortae, phenylephrine-induced contraction was partially inhibited by either IP3 receptor antagonist heparin or PKC inhibitor GFX, and the combined treatment with heparin and GFX abolished the contraction.	Heparin	117-124	inositol 1,4,5-triphosphate receptor 3	Mus musculus	93-105
29346400-8	2018	In defibrinated, recalcified plasma, on the contrary, heparin is able to reduce CXCL5 and CXCL7 release from platelets by thrombin inhibition.	Heparin	54-61	pro-platelet basic protein	Homo sapiens	90-95
23981347-1	2014	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is a life-threatening condition, in which the anticoagulant heparin, platelet factor 4 (PF4), and platelet-activating antibodies form complexes with prothrombotic properties.	Heparin	14-21	platelet factor 4	Homo sapiens	141-144
29022213-7	2018	Ten patients, among those with JAK 2 V617F mutation after a median of 10 days from heparin treatment presented a platelet drop, new thrombotic events and in 10/10 cases heparin-related antibodies were found.	Heparin	83-90	Janus kinase 2	Homo sapiens	31-36
24525311-0	2014	Low molecular weight heparin-induced increase in chylomicron-remnants clearance, is associated with decreased plasma TNF-alpha level and increased hepatic lipase activity.	Heparin	21-28	lipase C, hepatic type	Homo sapiens	147-161
24641672-0	2014	Heparin binding VEGF isoforms attenuate hyperoxic embryonic lung growth retardation via a FLK1-neuropilin-1-PKC dependent pathway.	Heparin	0-7	neuropilin 1	Homo sapiens	95-107
29022213-7	2018	Ten patients, among those with JAK 2 V617F mutation after a median of 10 days from heparin treatment presented a platelet drop, new thrombotic events and in 10/10 cases heparin-related antibodies were found.	Heparin	169-176	Janus kinase 2	Homo sapiens	31-36
28712066-1	2017	Antibodies against the chemokine platelet factor 4 (PF4) in complex with heparin cause the prothrombotic adverse drug reaction heparin-induced thrombocytopenia (HIT).	Heparin	73-80	platelet factor 4	Homo sapiens	52-55
24046088-4	2014	HIV-1 gp120 prefers heparin and heparan sulfate (with at least 16 monomers in length) over chondroitin and dermatan.	Heparin	20-27	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	6-11
28712066-1	2017	Antibodies against the chemokine platelet factor 4 (PF4) in complex with heparin cause the prothrombotic adverse drug reaction heparin-induced thrombocytopenia (HIT).	Heparin	127-134	platelet factor 4	Homo sapiens	52-55
28712066-5	2017	At physiological conditions (pH 7.4, 150 mM NaCl), non-pathogenic antibodies bound to PF4/heparin complexes with weaker binding forces than pathogenic ones.	Heparin	90-97	platelet factor 4	Homo sapiens	86-89
23941573-5	2014	Recombinant hBMP4 protein was purified by SP Sepharose and heparin affinity chromatography.	Heparin	59-66	bone morphogenetic protein 4	Homo sapiens	12-17
28903994-1	2017	Heparin can induce the formation of antibodies against a heparin complex with a platelet factor 4 (PF4), leading to platelet activation and the development of heparin-induced thrombocytopaenia (HIT).	Heparin	0-7	platelet factor 4	Homo sapiens	99-102
24326668-10	2014	Overexpression of Hs3st1 in MST-10H cells resulted in a change in the composition of heparan sulfate (HS)/HP and CS/dermatan sulfate (DS) glycosaminoglycans.	Heparin	106-108	heparan sulfate (glucosamine) 3-O-sulfotransferase 1	Mus musculus	18-24
29117741-13	2017	A possible mechanism for the decline in beta-TG concentration may be adherence of this heparin-binding protein to the heparin-coated dialysis membrane.	Heparin	87-94	pro-platelet basic protein	Homo sapiens	40-47
24627836-0	2014	Controlled release of nerve growth factor from heparin-conjugated fibrin gel within the nerve growth factor-delivering implant.	Heparin	47-54	nerve growth factor	Rattus norvegicus	22-41
24627836-0	2014	Controlled release of nerve growth factor from heparin-conjugated fibrin gel within the nerve growth factor-delivering implant.	Heparin	47-54	nerve growth factor	Rattus norvegicus	88-107
24627836-2	2014	In this study, we loaded the NGF-bound heparin-conjugated fibrin (HCF) gel in the NGF-delivering implants and analyzed the time-dependent release of NGF and its bioactivity to evaluate the clinical effectiveness.	Heparin	39-46	nerve growth factor	Rattus norvegicus	29-32
24627836-2	2014	In this study, we loaded the NGF-bound heparin-conjugated fibrin (HCF) gel in the NGF-delivering implants and analyzed the time-dependent release of NGF and its bioactivity to evaluate the clinical effectiveness.	Heparin	39-46	nerve growth factor	Rattus norvegicus	82-85
24627836-2	2014	In this study, we loaded the NGF-bound heparin-conjugated fibrin (HCF) gel in the NGF-delivering implants and analyzed the time-dependent release of NGF and its bioactivity to evaluate the clinical effectiveness.	Heparin	39-46	nerve growth factor	Rattus norvegicus	82-85
29149067-0	2017	The HMGB1/RAGE Pro-Inflammatory Axis in the Human Placenta: Modulating Effect of Low Molecular Weight Heparin.	Heparin	102-109	high mobility group box 1	Homo sapiens	4-9
24316520-6	2014	Of the identified proteins, 14 are not previously shown to be heparin-binding, such as the low concentration proteins lipocalin-1 and tropomyosin and a hitherto not detected protein in plasma, zinc finger protein 483.	Heparin	62-69	lipocalin 1	Homo sapiens	118-129
24316520-6	2014	Of the identified proteins, 14 are not previously shown to be heparin-binding, such as the low concentration proteins lipocalin-1 and tropomyosin and a hitherto not detected protein in plasma, zinc finger protein 483.	Heparin	62-69	zinc finger protein 483	Homo sapiens	193-216
24942999-0	2014	A comparison of the effects of nifedipine, verapamil, and low-molecular-weight heparin on SLIGRL-NH2-induced calcium influx through proteinase-activated receptor 2 activation.	Heparin	79-86	F2R like trypsin receptor 1	Homo sapiens	132-163
24942999-3	2014	AIMS: In this study, we investigated the effects of nifedipine, verapamil, and low-molecular-weight heparin (LMWH) on SLIGRL-NH2-induced PAR2-mediated calcium mobilization within cells.	Heparin	100-107	F2R like trypsin receptor 1	Homo sapiens	137-141
24246163-0	2014	Non-transient "self-sustaining" heparin-induced thrombocytopenia: 4-year persistence of a platelet-activating PF4/heparin-antibody status without heparin exposure.	Heparin	32-39	platelet factor 4	Homo sapiens	110-113
23884221-0	2013	Effect of routine heparins treatment in acute coronary syndrome on serum pregnancy-associated plasma protein a concentration.	Heparin	18-26	pappalysin 1	Homo sapiens	73-110
23884221-2	2013	Serum PAPP-A concentrations are affected by unfractionated heparin (UFH) in ACS population, and we tried to investigate the time profile of effects of routine heparins treatment on serum PAPP-A concentrations in ACS population thoroughly and give advice to sample collection of related study.	Heparin	59-66	pappalysin 1	Homo sapiens	6-12
23884221-2	2013	Serum PAPP-A concentrations are affected by unfractionated heparin (UFH) in ACS population, and we tried to investigate the time profile of effects of routine heparins treatment on serum PAPP-A concentrations in ACS population thoroughly and give advice to sample collection of related study.	Heparin	68-71	pappalysin 1	Homo sapiens	6-12
23884221-2	2013	Serum PAPP-A concentrations are affected by unfractionated heparin (UFH) in ACS population, and we tried to investigate the time profile of effects of routine heparins treatment on serum PAPP-A concentrations in ACS population thoroughly and give advice to sample collection of related study.	Heparin	159-167	pappalysin 1	Homo sapiens	187-193
23884221-7	2013	In group B, there was a rapid and intense increase after intravenous heparin injection (13.1 to 49.3 mIU/L, P&lt;0.05), and a new PAPP-A peak was induced by additional heparin administration.	Heparin	168-175	pappalysin 1	Homo sapiens	130-136
23884221-8	2013	CONCLUSIONS: Heparins-induced increase in serum PAPP-A concentration lasted until 48h after drug use was discontinued.	Heparin	13-21	pappalysin 1	Homo sapiens	48-54
23523386-3	2013	Functionally, N domain is part of the HGF/SF high affinity binding site for MET and also the main HGF/SF binding site for heparin.	Heparin	122-129	hepatocyte growth factor	Homo sapiens	38-44
23523386-3	2013	Functionally, N domain is part of the HGF/SF high affinity binding site for MET and also the main HGF/SF binding site for heparin.	Heparin	122-129	hepatocyte growth factor	Homo sapiens	98-104
29149067-2	2017	Moreover, we investigated, in physiological placental tissue, the ability of Low Molecular Weight Heparin (LMWH) to modify HMGB1 structural conformation thus inhibiting RAGE binding and HMGB1/RAGE axis inflammatory activity.	Heparin	98-105	high mobility group box 1	Homo sapiens	123-128
23641914-7	2013	Heparin binds directly with the growth factor bone morphogenetic protein-2 and helps to retain its activity.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	46-74
24097975-1	2013	Heparin-induced thrombocytopenia (HIT) is a thrombotic complication of heparin therapy mediated by antibodies to complexes between platelet factor 4 (PF4) and heparin or cellular glycosaminoglycans.	Heparin	0-7	platelet factor 4	Homo sapiens	150-153
29149067-2	2017	Moreover, we investigated, in physiological placental tissue, the ability of Low Molecular Weight Heparin (LMWH) to modify HMGB1 structural conformation thus inhibiting RAGE binding and HMGB1/RAGE axis inflammatory activity.	Heparin	98-105	high mobility group box 1	Homo sapiens	186-191
24097975-1	2013	Heparin-induced thrombocytopenia (HIT) is a thrombotic complication of heparin therapy mediated by antibodies to complexes between platelet factor 4 (PF4) and heparin or cellular glycosaminoglycans.	Heparin	71-78	platelet factor 4	Homo sapiens	150-153
24097975-5	2013	To mimic the effect of heparin in bringing PF4 complexes into proximity, we chemically cross-linked PF4 tetramers using glutaraldehyde.	Heparin	23-30	platelet factor 4	Homo sapiens	43-46
28118750-3	2017	The aim of this work was to study the complexes that human PF4 forms with heparins from various species, such as porcine, bovine, and ovine; heparins from various organs, such as mucosa and lung; and different low-molecular-weight heparins (LMWHs) at several stoichiometric ratios to evaluate their sizes and charges by photo correlation spectroscopy and zeta potential measurements.	Heparin	74-82	platelet factor 4	Homo sapiens	59-62
23987380-2	2013	The Ti substrates were initially modified by chemical grafting poly-L-lysine (PLL) using condensing agent, followed by immobilizing the heparin/BMP-2 complex to the PLL-grafted Ti substrate via electrostatic interactions.	Heparin	136-143	bone morphogenetic protein 2	Homo sapiens	144-149
23498894-1	2013	Heparin-functionalized poly(N-isopropylacrylamide-co-2-carboxyisopropylacrylamide) [P(IPAAm-co-CIPAAm)] grafted surface was designed for the switching of cell growth/detachment, achieved by the regulation of affinity binding between basic fibroblast growth factor (bFGF) and immobilized heparin through the temperature-dependent conformational change of grafted P(IPAAm-co-CIPAAm) chains.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	233-263
23498894-1	2013	Heparin-functionalized poly(N-isopropylacrylamide-co-2-carboxyisopropylacrylamide) [P(IPAAm-co-CIPAAm)] grafted surface was designed for the switching of cell growth/detachment, achieved by the regulation of affinity binding between basic fibroblast growth factor (bFGF) and immobilized heparin through the temperature-dependent conformational change of grafted P(IPAAm-co-CIPAAm) chains.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	265-269
28118750-3	2017	The aim of this work was to study the complexes that human PF4 forms with heparins from various species, such as porcine, bovine, and ovine; heparins from various organs, such as mucosa and lung; and different low-molecular-weight heparins (LMWHs) at several stoichiometric ratios to evaluate their sizes and charges by photo correlation spectroscopy and zeta potential measurements.	Heparin	141-149	platelet factor 4	Homo sapiens	59-62
28118750-3	2017	The aim of this work was to study the complexes that human PF4 forms with heparins from various species, such as porcine, bovine, and ovine; heparins from various organs, such as mucosa and lung; and different low-molecular-weight heparins (LMWHs) at several stoichiometric ratios to evaluate their sizes and charges by photo correlation spectroscopy and zeta potential measurements.	Heparin	141-149	platelet factor 4	Homo sapiens	59-62
23714311-1	2013	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder caused by antibodies to platelet factor 4/heparin (PF4/H) complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	118-123
22752790-3	2013	The extracellular D2 domain of the FGFR4 receptor contains a heparin binding site and the main interaction site with the fibroblast growth factor.	Heparin	61-68	fibroblast growth factor receptor 4	Homo sapiens	35-40
28771917-14	2017	Two regions (Asp-7 to Thr-15 and Ala-32 to Thr-38) therefore appeared important for the binding of 5B9 and KKO on PF4 modified by heparin.	Heparin	130-137	platelet factor 4	Homo sapiens	114-117
23876263-1	2013	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) results from antibodies to PF4/heparin complexes and clinical diagnosis is difficult.	Heparin	14-21	platelet factor 4	Homo sapiens	80-83
23467042-6	2013	Heparin was covalently crosslinked to the chitosan scaffolds using genipin, which bound fibroblast growth factor-2 (FGF-2) with high affinity while retaining its biological activity.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	88-114
23467042-6	2013	Heparin was covalently crosslinked to the chitosan scaffolds using genipin, which bound fibroblast growth factor-2 (FGF-2) with high affinity while retaining its biological activity.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	116-121
23498894-2	2013	At 37  C, bFGF-bound heparin-thermoresponsive surfaces were able to hold the two- to three-fold number of mouse fibroblast (NIH/3T3) cells than both bFGF-physisorbed surface and PIPAAm surface with soluble bFGF after a 3-day cultivation.	Heparin	21-28	fibroblast growth factor 2	Mus musculus	10-14
23551961-0	2013	FcgammaRIIa proteolysis as a diagnostic biomarker for heparin-induced thrombocytopenia.	Heparin	54-61	Fc gamma receptor IIa	Homo sapiens	0-11
23551961-10	2013	RESULTS: Only HIT patient samples (20/20) caused heparin-dependent FcgammaRIIa proteolysis, similar to what was shown by the SRA.	Heparin	49-56	Fc gamma receptor IIa	Homo sapiens	67-78
23551961-12	2013	Among nine additional samples that tested indeterminate in the SRA, FcgammaRIIa proteolysis resolved five samples that had a positive anti-PF4/heparin EIA result; three had no FcgammaRIIa proteolysis, and two were shown to have heparin-dependent FcgammaRIIa proteolysis CONCLUSIONS: This study suggests that heparin-dependent FcgammaRIIa proteolysis is at least as specific as the SRA for the diagnosis of HIT.	Heparin	143-150	Fc gamma receptor IIa	Homo sapiens	68-79
23447529-8	2013	Furthermore, the binding of ligands (glycyrrhizin and heparin) to HMGB1 significantly modulated the oxidation kinetics.	Heparin	54-61	high mobility group box 1	Homo sapiens	66-71
23268358-0	2013	Heparin inhibits angiotensin II-induced vasoconstriction on isolated mouse mesenteric resistance arteries through Rho-A- and PKA-dependent pathways.	Heparin	0-7	ras homolog family member A	Mus musculus	114-119
23268358-4	2013	We hypothesized that heparin may offset Ang II-induced vasoconstriction on mesenteric resistance arteries through modulating the Rho-A/Rho kinase pathway.	Heparin	21-28	ras homolog family member A	Mus musculus	129-134
23498894-2	2013	At 37  C, bFGF-bound heparin-thermoresponsive surfaces were able to hold the two- to three-fold number of mouse fibroblast (NIH/3T3) cells than both bFGF-physisorbed surface and PIPAAm surface with soluble bFGF after a 3-day cultivation.	Heparin	21-28	fibroblast growth factor 2	Mus musculus	149-153
23498894-2	2013	At 37  C, bFGF-bound heparin-thermoresponsive surfaces were able to hold the two- to three-fold number of mouse fibroblast (NIH/3T3) cells than both bFGF-physisorbed surface and PIPAAm surface with soluble bFGF after a 3-day cultivation.	Heparin	21-28	fibroblast growth factor 2	Mus musculus	149-153
23498894-3	2013	Bound bFGF via heparin on shrunken grafted P(IPAAm-co-CIPAAm) chains at 37  C was able to reinforce the formation and stabilization of bFGF-FGF receptor complex, although the activity of physisorbed bFGF on PIPAAm-grafted surfaces was decreased by non-specific and randomly oriented adsorption.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	6-10
23268358-8	2013	The combined effect of Ang II with heparin was almost abolished by a specific Rho kinase inhibitor Y27632.	Heparin	35-42	angiogenin, ribonuclease, RNase A family, 5	Mus musculus	23-26
28870205-7	2017	Meanwhile, CCN2 was able to enhance malignant phenotype of HCC cells in a dose-dependent manner through binding with LRP6; and knock-down of LRP6 expression, perturbation of HSPGs, co-incubation of CCN2 with LMWH could significantly block the adhesion of CCN2 to LRP6.	Heparin	208-212	cellular communication network factor 2	Homo sapiens	11-15
23268358-9	2013	Ang II stimulated Rho-A activation and myosin light chain phosphorylation, both responses were antagonized by heparin.	Heparin	110-117	ras homolog family member A	Mus musculus	18-23
23268358-12	2013	We conclude that heparin inhibits Ang II-induced vasoconstriction through Rho-A/Rho kinase- and cGMP/PKA-dependent pathways.	Heparin	17-24	ras homolog family member A	Mus musculus	74-79
23341458-6	2013	N-terminal sequencing indicated that pro-BMP-2 was cleaved by FSAP at the canonical PC cleavage site, giving rise to mature BMP-2 (Arg(282) Gln(283)), as well as in the N-terminal heparin binding region of mature BMP-2, generating a truncated mature BMP-2 peptide (Arg(289) Lys(290)).	Heparin	180-187	bone morphogenetic protein 2	Homo sapiens	41-46
23498894-3	2013	Bound bFGF via heparin on shrunken grafted P(IPAAm-co-CIPAAm) chains at 37  C was able to reinforce the formation and stabilization of bFGF-FGF receptor complex, although the activity of physisorbed bFGF on PIPAAm-grafted surfaces was decreased by non-specific and randomly oriented adsorption.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	135-139
23498894-3	2013	Bound bFGF via heparin on shrunken grafted P(IPAAm-co-CIPAAm) chains at 37  C was able to reinforce the formation and stabilization of bFGF-FGF receptor complex, although the activity of physisorbed bFGF on PIPAAm-grafted surfaces was decreased by non-specific and randomly oriented adsorption.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	135-139
23498894-4	2013	At 20  C, the cultured NIH/3T3 cell sheet with bFGF detached from heparin-functionalized thermoresponsive surface.	Heparin	66-73	fibroblast growth factor 2	Mus musculus	47-51
23498894-5	2013	The release of bFGF from the surfaces was induced by reducing the affinity binding between bFGF and immobilized-heparin due to increasing the mobility of the swollen grafted P(IPAAm-co-CIPAAm) chains.	Heparin	112-119	fibroblast growth factor 2	Mus musculus	15-19
23371442-1	2013	Diamine oxidase (DAO) was purified to homogeneity from human seminal plasma by consecutive chromatographic fractionation on heparin-sepharose, phenyl-sepharose, CIM-QA, and Superdex 200.	Heparin	124-131	amine oxidase copper containing 1	Homo sapiens	0-15
28870205-8	2017	LMWH enhanced the therapeutic effect of oxaliplatin on HCC with a high CCN2 expression.	Heparin	0-4	cellular communication network factor 2	Homo sapiens	71-75
23371442-1	2013	Diamine oxidase (DAO) was purified to homogeneity from human seminal plasma by consecutive chromatographic fractionation on heparin-sepharose, phenyl-sepharose, CIM-QA, and Superdex 200.	Heparin	124-131	amine oxidase copper containing 1	Homo sapiens	17-20
28870205-10	2017	Heparin in combination with chemotherapy has a synergic effect and could be a treatment choice for HCCs with a high CCN2 expression.	Heparin	0-7	cellular communication network factor 2	Homo sapiens	116-120
26860978-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe side effect of heparin treatment caused by platelet activating IgG antibodies generated against the platelet factor 4 (PF4)-heparin complex.	Heparin	12-19	platelet factor 4	Homo sapiens	182-185
23769097-3	2013	Administration of heparin can lead to heparin-induced thrombocytopenia (HIT) type II, mainly through heparin/platelet factor 4 (PF4) antibodies.	Heparin	18-25	platelet factor 4	Homo sapiens	101-126
23769097-3	2013	Administration of heparin can lead to heparin-induced thrombocytopenia (HIT) type II, mainly through heparin/platelet factor 4 (PF4) antibodies.	Heparin	18-25	platelet factor 4	Homo sapiens	128-131
23769097-3	2013	Administration of heparin can lead to heparin-induced thrombocytopenia (HIT) type II, mainly through heparin/platelet factor 4 (PF4) antibodies.	Heparin	38-45	platelet factor 4	Homo sapiens	101-126
23769097-3	2013	Administration of heparin can lead to heparin-induced thrombocytopenia (HIT) type II, mainly through heparin/platelet factor 4 (PF4) antibodies.	Heparin	38-45	platelet factor 4	Homo sapiens	128-131
23769097-13	2013	The physical relationship between the PF4-positive thrombi and the heparin-coated surface suggests that onset of HIT II could be influenced by the immobilized heparin coating.	Heparin	67-74	platelet factor 4	Homo sapiens	38-41
23769097-13	2013	The physical relationship between the PF4-positive thrombi and the heparin-coated surface suggests that onset of HIT II could be influenced by the immobilized heparin coating.	Heparin	159-166	platelet factor 4	Homo sapiens	38-41
23395667-5	2013	bFGF was released slowly because of its high affinity to the heparin while the significantly higher release of the non-specific binding EGF was controlled by diffusion only.	Heparin	61-68	fibroblast growth factor 2	Mus musculus	0-4
23064887-5	2013	Furthermore, in the presence of hepatic sGAGs or heparin, nanomolar hFGF19 activates mFGFR4, even in the absence of co-expressed mKLB.	Heparin	49-56	fibroblast growth factor 19	Homo sapiens	68-74
23627055-7	2013	Finally, the adhesion abilities of K562 on M210B4 and HS5 are changed by adding heparin into culture medium, which demonstrates the specificity of the adhesion.	Heparin	80-87	hemoglobin, activating region	Mus musculus	54-57
23135410-0	2013	Evaluation of collagen/heparin coated TCP/HA granules for long-term delivery of BMP-2.	Heparin	23-30	bone morphogenetic protein 2	Homo sapiens	80-85
23135410-4	2013	We covalently attached heparin to a cross-linked collagen type I coated tricalciumphosphate/hydroxyapatite (TCP/HA) bone substitute and subsequently loaded it with BMP-2.	Heparin	23-30	bone morphogenetic protein 2	Homo sapiens	164-169
26860978-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe side effect of heparin treatment caused by platelet activating IgG antibodies generated against the platelet factor 4 (PF4)-heparin complex.	Heparin	78-85	platelet factor 4	Homo sapiens	182-185
23148226-3	2013	We found that co-administration of heparin, a common treatment for myocardial infarction, abrogated the protective effect of CXCL12 in an ex vivo rat heart model for myocardial infarction.	Heparin	35-42	C-X-C motif chemokine ligand 12	Rattus norvegicus	125-131
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	0-7	serpin family A member 10	Homo sapiens	22-25
23148226-5	2013	However, complications from heparin-induced CXCL12 oligomerization and studies using very short oligosaccharides have led to inconsistent conclusions as to the residues involved, the orientation of the binding site, and whether it overlaps with the CXCR4 N-terminal site.	Heparin	28-35	C-X-C motif chemokine ligand 12	Rattus norvegicus	44-50
23148226-7	2013	Biophysical and mutagenic analyses reveal a CXCL12/heparin interaction surface that lies perpendicular to the dimer interface, does not involve the chemokine N terminus, and partially overlaps with the CXCR4-binding site.	Heparin	51-58	C-X-C motif chemokine ligand 12	Rattus norvegicus	44-50
23148226-8	2013	We further demonstrate that heparin-mediated enzymatic protection results from the promotion of dimerization rather than direct heparin binding to the CXCL12 N terminus.	Heparin	28-35	C-X-C motif chemokine ligand 12	Rattus norvegicus	151-157
23907946-2	2013	We studied the effects of unfractionated heparin (UFH) vs. enoxaparin vs. sulodexide on the levels and gene expression of osteoprotegerin (OPG), Receptor Activator of Nuclear Factor kB Ligand (RANKL) and von Willebrand factor (vWF) in Human Umbilical Vein Endothelial Cells (HUVEC) culture.	Heparin	41-48	TNF receptor superfamily member 11b	Homo sapiens	122-137
23907946-2	2013	We studied the effects of unfractionated heparin (UFH) vs. enoxaparin vs. sulodexide on the levels and gene expression of osteoprotegerin (OPG), Receptor Activator of Nuclear Factor kB Ligand (RANKL) and von Willebrand factor (vWF) in Human Umbilical Vein Endothelial Cells (HUVEC) culture.	Heparin	50-53	TNF receptor superfamily member 11b	Homo sapiens	122-137
23907946-7	2013	Already the lowest concentration of UFH caused 2.5-fold increase in OPG gene expression while higher UFH concentrations substantially increased RANKL mRNA level.	Heparin	36-39	TNF receptor superfamily member 11b	Homo sapiens	68-71
23907946-10	2013	Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis.	Heparin	14-21	TNF receptor superfamily member 11b	Homo sapiens	79-82
23907946-10	2013	Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis.	Heparin	31-34	TNF receptor superfamily member 11b	Homo sapiens	79-82
23646121-1	2013	BACKGROUND: Heparin-induced thrombocytopenia is an immune response mediated by anti-PF4/heparin antibody, which is clinically characterized by thrombocytopenia and thromboembolic events.	Heparin	12-19	platelet factor 4	Homo sapiens	84-87
23462864-0	2013	Reversible binding and quantification of heparin and chondroitin sulfate in water using redox-stable biferrocenylene SAMs.	Heparin	41-48	methionine adenosyltransferase 1A	Homo sapiens	117-121
23462864-2	2013	The resulting SAMs with their extraordinary stability in the monocationic state were used to detect and quantify heparin (3-300 x 10(-5) g L(-1) = 0.003-0.3 U mL(-1)) and chondroitin sulfate (3-250 x 10(-5) g L(-1)) in aqueous buffer by cyclic voltammetry, square wave voltammetry and surface plasmon resonance.	Heparin	113-120	methionine adenosyltransferase 1A	Homo sapiens	14-18
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	0-7	serpin family A member 10	Homo sapiens	46-49
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	0-7	serpin family A member 10	Homo sapiens	46-49
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	0-7	serpin family A member 10	Homo sapiens	46-49
22942185-1	2012	The positively charged chemokine platelet factor 4 (PF4) forms immunogenic complexes with heparin and other polyanions.	Heparin	90-97	platelet factor 4	Homo sapiens	52-55
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	98-105	serpin family A member 10	Homo sapiens	22-25
22942185-3	2012	PF4 also binds to bacteria, thereby exposing the same neoantigen(s) as with heparin.	Heparin	76-83	platelet factor 4	Homo sapiens	0-3
23261567-1	2013	A heparin-conjugated biodegradable polymer was synthesized by direct coupling of heparin to poly(L-lactide-co-e-caprolactone) (PLCL) and was manufactured into lotus-leaf-like structured films.	Heparin	2-9	phospholipase C like 1 (inactive)	Homo sapiens	127-131
23261567-2	2013	We evaluated whether lotus-leaf-like structured heparin-conjugated PLCL (LH-PLCL) could be applied to blood vessel tissue engineering.	Heparin	48-55	phospholipase C like 1 (inactive)	Homo sapiens	67-71
22942185-8	2012	Interactions of PF4 with Gram-negative bacteria, where only the lipid A part of LPS is exposed, induce epitopes on PF4 resembling those on PF4/heparin complexes as shown by binding of human anti-PF4/heparin antibodies.	Heparin	143-150	platelet factor 4	Homo sapiens	16-19
23261567-2	2013	We evaluated whether lotus-leaf-like structured heparin-conjugated PLCL (LH-PLCL) could be applied to blood vessel tissue engineering.	Heparin	48-55	phospholipase C like 1 (inactive)	Homo sapiens	76-80
23261567-5	2013	The concentration of conjugated heparin was 0.14 mug/mg H-PLCL, and the contact angle with the lotus-leaf-like surface was approximately 120 .	Heparin	32-39	phospholipase C like 1 (inactive)	Homo sapiens	58-62
23216710-1	2013	BACKGROUND: Anti-PF4/heparin antibodies are frequently generated after coronary artery bypass grafting (CABG) surgery, with platelet-activating IgG implicated in heparin-induced thrombocytopenia (HIT).	Heparin	21-28	platelet factor 4	Homo sapiens	17-20
23216710-3	2013	OBJECTIVES: To determine in post-CABG patients whether thromboprophylaxis using fondaparinux vs. unfractionated heparin (UFH) reduces the frequency of anti-PF4/heparin antibodies, and whether anti-PF4/heparin antibodies are associated with early graft occlusion.	Heparin	121-124	platelet factor 4	Homo sapiens	156-159
22924876-4	2012	We have developed a technique that can quickly fabricate (~40 min) such 3D gradients by simultaneously electrospinning polycaprolactone (PCL) fibers, encapsulating gradient amount of bFGF (stabilized by heparin) into poly(lactide-co-glycolide) (PLGA) microspheres, and electrospraying the microspheres into PCL fibers.	Heparin	203-210	fibroblast growth factor 2	Mus musculus	183-187
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	98-105	serpin family A member 10	Homo sapiens	46-49
22821930-0	2012	Heparin disrupts the CXCR4/SDF-1 axis and impairs the functional capacity of bone marrow-derived mononuclear cells used for cardiovascular repair.	Heparin	0-7	chemokine (C-X-C motif) ligand 12	Mus musculus	27-32
22821930-5	2012	METHODS AND RESULTS: Heparin, but not bivalirudin profoundly and dose-dependently inhibited basal and stromal cell-derived factor 1 (SDF-1)-induced BMC migration.	Heparin	21-28	chemokine (C-X-C motif) ligand 12	Mus musculus	102-131
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	98-105	serpin family A member 10	Homo sapiens	46-49
22821930-5	2012	METHODS AND RESULTS: Heparin, but not bivalirudin profoundly and dose-dependently inhibited basal and stromal cell-derived factor 1 (SDF-1)-induced BMC migration.	Heparin	21-28	chemokine (C-X-C motif) ligand 12	Mus musculus	133-138
22821930-6	2012	Incubation of BMCs with 20 U/mL heparin for 30 minutes abrogated SDF-1-induced BMC invasion (16+-8% of control; P&lt;0.01), whereas no effects on apoptosis or colony formation were observed (80+-33% and 100+-44% of control, respectively).	Heparin	32-39	chemokine (C-X-C motif) ligand 12	Mus musculus	65-70
23320987-6	2013	Cell-associated TFPI was detected after phosphatidylinositol-phospholipase C (PI-PLC) and heparin treatment by flow cytometry, immunofluorescence, and Western blotting.	Heparin	90-97	tissue factor pathway inhibitor	Homo sapiens	16-20
28717005-7	2017	Heparin protected the ZPI-PZ complex and free ZPI from inactivation, suggesting that blocking the heparin-binding site on ZPI interferes with ZPI binding to lipid or to PZ.	Heparin	98-105	serpin family A member 10	Homo sapiens	46-49
22821930-9	2012	Mechanistically, heparin binds to both, the chemoattractant SDF-1 and its receptor, chemokine receptor 4 (CXCR4), blocking CXCR4 internalization as well as SDF-1/CXCR4 signaling after SDF-1 stimulation.	Heparin	17-24	chemokine (C-X-C motif) ligand 12	Mus musculus	60-104
22821930-9	2012	Mechanistically, heparin binds to both, the chemoattractant SDF-1 and its receptor, chemokine receptor 4 (CXCR4), blocking CXCR4 internalization as well as SDF-1/CXCR4 signaling after SDF-1 stimulation.	Heparin	17-24	chemokine (C-X-C motif) ligand 12	Mus musculus	60-65
28869736-5	2017	GST tag was cleaved with thrombin, and a crude SOD2 recombinant protein (25 kDa) was obtained and further purified by heparin affinity chromatography.	Heparin	118-125	superoxide dismutase 2	Homo sapiens	47-51
22821930-9	2012	Mechanistically, heparin binds to both, the chemoattractant SDF-1 and its receptor, chemokine receptor 4 (CXCR4), blocking CXCR4 internalization as well as SDF-1/CXCR4 signaling after SDF-1 stimulation.	Heparin	17-24	chemokine (C-X-C motif) ligand 12	Mus musculus	156-161
22821930-10	2012	CONCLUSIONS: Heparin blocks SDF-1/CXCR4 signaling by binding to the ligand as well as the receptor, thereby interfering with migration and homing of BMCs.	Heparin	13-20	chemokine (C-X-C motif) ligand 12	Mus musculus	28-33
23099062-3	2013	We report here on a synthetic biomimetic strategy that emulates biological BMP-2 signaling through the use of peptide amphiphile nanofibers designed to bind heparin.	Heparin	157-164	bone morphogenetic protein 2	Rattus norvegicus	75-80
22972991-4	2012	The extracellular protease, neuropsin, cleaved mature NRG-1 (comprising the extracellular domain of the NRG-1) at three newly identified sites to remove the heparin-binding domain of NRG-1.	Heparin	157-164	opsin 5	Mus musculus	28-37
28725494-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a life and limb-threatening condition caused by the binding of platelet-activating antibodies (IgG) to multimolecular platelet factor 4 (PF4)/heparin complexes because of heparin exposure.	Heparin	12-19	platelet factor 4	Homo sapiens	191-194
22972991-4	2012	The extracellular protease, neuropsin, cleaved mature NRG-1 (comprising the extracellular domain of the NRG-1) at three newly identified sites to remove the heparin-binding domain of NRG-1.	Heparin	157-164	neuregulin 1	Mus musculus	54-59
22972991-4	2012	The extracellular protease, neuropsin, cleaved mature NRG-1 (comprising the extracellular domain of the NRG-1) at three newly identified sites to remove the heparin-binding domain of NRG-1.	Heparin	157-164	neuregulin 1	Mus musculus	104-109
22972991-4	2012	The extracellular protease, neuropsin, cleaved mature NRG-1 (comprising the extracellular domain of the NRG-1) at three newly identified sites to remove the heparin-binding domain of NRG-1.	Heparin	157-164	neuregulin 1	Mus musculus	104-109
22972991-7	2012	Moreover, neuropsin knock-out mice exhibited impairments in Schaffer collateral early phase long-term potentiation, and application of the recombinant NRG-1 lacking heparin-binding activity reversed the effects through the activation of ErbB4 and GABA(A) receptors.	Heparin	165-172	neuregulin 1	Mus musculus	151-156
24319250-1	2013	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder caused by antibodies that recognize complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	135-138
24307297-6	2013	Furthermore, we found that fibroblast growth factor-2 (FGF-2) with heparin induced miPS cell differentiation into neuronal cells, both in an adherent monolayer and in embryoid body suspension culture.	Heparin	67-74	fibroblast growth factor 2	Mus musculus	27-53
28725494-1	2017	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a life and limb-threatening condition caused by the binding of platelet-activating antibodies (IgG) to multimolecular platelet factor 4 (PF4)/heparin complexes because of heparin exposure.	Heparin	196-203	platelet factor 4	Homo sapiens	191-194
24307297-6	2013	Furthermore, we found that fibroblast growth factor-2 (FGF-2) with heparin induced miPS cell differentiation into neuronal cells, both in an adherent monolayer and in embryoid body suspension culture.	Heparin	67-74	fibroblast growth factor 2	Mus musculus	55-60
22687758-0	2012	Hyaluronic acid-based hydrogels functionalized with heparin that support controlled release of bioactive BMP-2.	Heparin	52-59	bone morphogenetic protein 2	Rattus norvegicus	105-110
22687758-2	2012	Heparin (HP), a highly sulfated glycosaminoglycan (GAG) that avidly binds BMP-2, has inherent biological properties that may circumvent these limitations.	Heparin	0-7	bone morphogenetic protein 2	Rattus norvegicus	74-79
22687758-2	2012	Heparin (HP), a highly sulfated glycosaminoglycan (GAG) that avidly binds BMP-2, has inherent biological properties that may circumvent these limitations.	Heparin	9-11	bone morphogenetic protein 2	Rattus norvegicus	74-79
22687758-7	2012	Importantly, the inclusion of a small amount of heparin (0.3% w/w) attenuated release of BMP-2 and sustained its osteogenic activity for up to 28 days.	Heparin	48-55	bone morphogenetic protein 2	Rattus norvegicus	89-94
22687758-8	2012	In contrast, hydrogels lacking heparin released more BMP-2 initially but were unable to maintain BMP-2 activity at later time points.	Heparin	31-38	bone morphogenetic protein 2	Rattus norvegicus	53-58
22718864-7	2012	RESULTS: Heparin-dependent anti-PF4 antibodies were detected in 11 SLE (9%) and 2 primary ITP (3%) patients, but at much lower levels than in HIT patients.	Heparin	9-16	platelet factor 4	Homo sapiens	32-35
23047829-5	2013	A pharmacokinetic model including plasma and liver compartments was constructed, incorporating both high- and low-affinity receptors for association and subsequent endocytosis of HGF because HGF is eliminated via specific receptor c-Met and heparin-like substance.	Heparin	241-248	hepatocyte growth factor	Homo sapiens	179-182
23047829-5	2013	A pharmacokinetic model including plasma and liver compartments was constructed, incorporating both high- and low-affinity receptors for association and subsequent endocytosis of HGF because HGF is eliminated via specific receptor c-Met and heparin-like substance.	Heparin	241-248	hepatocyte growth factor	Homo sapiens	191-194
22718864-12	2012	Heparin-dependent anti-PF4 antibodies were associated with thrombocytopenia and IgM aCLs (P = 0.007 for both comparisons), while heparin-independent anti-PF4 antibody levels were correlated with SLE disease activity index (P = 0.0005).	Heparin	129-136	platelet factor 4	Homo sapiens	154-157
28703769-5	2017	The observation that heparan sulfate did not, and heparin only moderately, altered CXCL10-induced T cell chemotaxis in vitro may be explained by a combination of protection against proteolytic inactivation and altered receptor interaction as observed in calcium assays.	Heparin	50-57	chemokine (C-X-C motif) ligand 10	Mus musculus	83-89
22634073-0	2012	A novel, biased-like SDF-1 derivative acts synergistically with starPEG-based heparin hydrogels and improves eEPC migration in vitro.	Heparin	78-85	C-X-C motif chemokine ligand 12	Homo sapiens	21-26
23437253-3	2013	Size-exclusion chromatography shows that full length SMOC-1 as well as its C-terminal EC domain alone bind heparin and heparan sulfate, but not the related chondroitin sulfate or dermatan sulfate glycosaminoglycans.	Heparin	107-114	SPARC related modular calcium binding 1	Homo sapiens	53-59
23437253-4	2013	Intrinsic tryptophan fluorescence measurements were used to quantify the binding of heparin to full length SMOC-1 and the EC domain alone.	Heparin	84-91	SPARC related modular calcium binding 1	Homo sapiens	107-113
23437253-8	2013	Heparin-binding impaired mutants failed to support S1EC-mediated cell adhesion and together with the observation that S1EC in complex with soluble heparin attenuated cell adhesion we conclude that a functional and accessible S1EC heparin-binding site mediates adhesion of epithelial cells to SMOC-1.	Heparin	230-237	SPARC related modular calcium binding 1	Homo sapiens	292-298
27975162-3	2017	In our previous studies we have shown the inhibitory effects of heparin on Hepatocyte Growth Factor (HGF)-induced invasion and migration in hepatocellular carcinoma (HCC) cells.	Heparin	64-71	hepatocyte growth factor	Homo sapiens	75-99
27975162-3	2017	In our previous studies we have shown the inhibitory effects of heparin on Hepatocyte Growth Factor (HGF)-induced invasion and migration in hepatocellular carcinoma (HCC) cells.	Heparin	64-71	hepatocyte growth factor	Homo sapiens	101-104
22938543-10	2012	BNP levels were higher in anteroseptal allocation of AMI compared to inferior allocation (835.80 pg/ml vs 243.03 pg/ml, p&lt; 0.001) and in patients who were treated with heparin compared to fibrinolitic therapy (507.885 pg/ml vs 354.73 pg/ml, p&lt; 0.05).	Heparin	171-178	natriuretic peptide B	Homo sapiens	0-3
27975162-4	2017	In this study, we showed the differential effects of heparin on the behaviors of HCC cells based on the presence or absence of HGF.	Heparin	53-60	hepatocyte growth factor	Homo sapiens	127-130
23853587-6	2013	According to SPR analysis, the affinity of BAD-1 for heparin is 33 nM+-14 nM.	Heparin	53-60	sepiapterin reductase	Homo sapiens	13-16
27975162-5	2017	In the absence of HGF, heparin activated HGF/c-Met signaling and promoted motility and invasion in HCC cells.	Heparin	23-30	hepatocyte growth factor	Homo sapiens	41-44
27975162-6	2017	Heparin treatment led to c-Met receptor dimerization and activated c-Met signaling in an HGF independent manner.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	89-92
28374939-5	2017	SUMMARY: Background There are conflicting data on whether the IgG-specific or polyspecific antiplatelet factor 4/heparin (PF4/H) enzyme-linked immunosorbent assay (ELISA) is preferred for the laboratory diagnosis of heparin-induced thrombocytopenia (HIT).	Heparin	113-120	platelet factor 4	Homo sapiens	122-162
22859690-1	2012	BACKGROUND: Platelet factor 4 (PF4) is released by activated platelets and has a strong affinity for heparin.	Heparin	101-108	platelet factor 4	Homo sapiens	31-34
22859690-2	2012	Recombinant PF4 (rPF4) has been previously considered as an alternative to protamine for heparin reversal.	Heparin	89-96	platelet factor 4	Homo sapiens	12-15
22859690-2	2012	Recombinant PF4 (rPF4) has been previously considered as an alternative to protamine for heparin reversal.	Heparin	89-96	platelet factor 4	Rattus norvegicus	17-21
22859690-3	2012	However, it has been demonstrated that antibodies directed against the PF4/heparin moiety are important in the pathophysiologic development of heparin-induced thrombocytopenia, a prothrombotic complication for which cardiac bypass patients are at increased risk.	Heparin	75-82	platelet factor 4	Homo sapiens	71-74
22657385-2	2012	FGF2 protected by heparin and bovine serum albumin was loaded into the microcapsules by a coprecipitation-based layer-by-layer encapsulation method.	Heparin	18-25	fibroblast growth factor 2	Mus musculus	0-4
22302637-0	2012	Apparent heparin resistance in a patient with infective  endocarditis secondary to elevated factor VIII levels.	Heparin	9-16	cytochrome c oxidase subunit 8A	Homo sapiens	99-103
22859690-8	2012	RESULTS: Heparin reversal was successful by 10 minutes after administration of rPF4 as measured by ACT in all 16 patients.	Heparin	9-16	platelet factor 4	Rattus norvegicus	79-83
22302637-5	2012	We hereby report an unusual case of heparin resistance due to increased factor VIII levels in an elderly male with infective endocarditis.	Heparin	36-43	cytochrome c oxidase subunit 8A	Homo sapiens	79-83
28416511-1	2017	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	140-143
22395770-0	2012	High positive predictive value of PAPP-A for acute coronary syndrome diagnosis in heparin-naive patients.	Heparin	82-89	pappalysin 1	Homo sapiens	34-40
22395770-3	2012	Therefore, the aim of our study was to ascertain the diagnostic significance of PAPP-A in heparin-naive patients and compare it with (TnI).	Heparin	90-97	pappalysin 1	Homo sapiens	80-86
22395770-10	2012	PAPP-A levels were an independent predictor of ACS diagnosis in heparin-naive patients.	Heparin	64-71	pappalysin 1	Homo sapiens	0-6
22540147-0	2012	Characterization of the heparin-binding site of the protein z-dependent protease inhibitor.	Heparin	24-31	serpin family A member 10	Homo sapiens	52-90
22859690-11	2012	CONCLUSIONS: Our case series demonstrates that heparin anticoagulation was effectively reversed by the administration of rPF4 without serious complications.	Heparin	47-54	platelet factor 4	Rattus norvegicus	121-125
22824487-2	2012	In this paper we report our predictions of the likely heparin binding sites for BMP-2 and 14.	Heparin	54-61	bone morphogenetic protein 2	Homo sapiens	80-85
22824487-3	2012	The N-terminal sequences upstream of TGF-beta-type cysteine-knot domains in BMP-2, 7 and 14 contain the basic residues arginine and lysine, which are key components of the heparin/HS-binding sites, with these residues being highly non-conserved.	Heparin	172-179	bone morphogenetic protein 2	Homo sapiens	76-81
22824487-7	2012	Histidines were found to play a role in the interactions of BMP-2 with heparin; however, a pK(a) analysis suggests that histidines are likely not protonated.	Heparin	71-78	bone morphogenetic protein 2	Homo sapiens	60-65
22824487-8	2012	This is indicative that interactions of BMP-2 with heparin do not require acidic pH.	Heparin	51-58	bone morphogenetic protein 2	Homo sapiens	40-45
22672269-11	2012	Interestingly, intraperitoneally administered HARP decreased the anticoagulant activity of heparin and of OTR4120 in mice.	Heparin	91-98	pleiotrophin	Mus musculus	46-50
22540147-1	2012	High-molecular weight heparins promote the protein Z-dependent protease inhibitor (ZPI) inhibition of factors Xa (FXa) and XIa (FXIa) by a template mechanism.	Heparin	22-30	serpin family A member 10	Homo sapiens	51-81
22540147-1	2012	High-molecular weight heparins promote the protein Z-dependent protease inhibitor (ZPI) inhibition of factors Xa (FXa) and XIa (FXIa) by a template mechanism.	Heparin	22-30	serpin family A member 10	Homo sapiens	83-86
22540147-2	2012	To map the heparin-binding site of ZPI, the role of basic residues of the D-helix (residues Lys-113, Lys-116, and Lys-125) in the interaction with heparin was evaluated by either substituting these residues with Ala (ZPI-3A) or replacing the D-helix with the corresponding loop of the non-heparin-binding serpin alpha(1)-proteinase inhibitor (ZPI-D-helix(alpha1-PI)).	Heparin	11-18	serpin family A member 10	Homo sapiens	35-38
22963465-8	2012	We observed that heparin mimetic peptide nanofibers demonstrate better binding profiles to VEGF, hepatocyte growth factor (HGF), and fibroblast growth factor-2 (FGF-2) than control peptide nanofibers.	Heparin	17-24	fibroblast growth factor 2	Rattus norvegicus	133-159
28416511-1	2017	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	140-143
22963465-8	2012	We observed that heparin mimetic peptide nanofibers demonstrate better binding profiles to VEGF, hepatocyte growth factor (HGF), and fibroblast growth factor-2 (FGF-2) than control peptide nanofibers.	Heparin	17-24	fibroblast growth factor 2	Rattus norvegicus	161-166
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	41-48	serpin family A member 10	Homo sapiens	150-153
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	41-48	serpin family A member 10	Homo sapiens	182-185
28279966-10	2017	Finally, we demonstrate that VWF susceptibility to plasmin proteolysis at K1491-R1492 is modulated by local N-linked glycan expression within A1A2A3, and specifically inhibited by heparin binding to the A1 domain.	Heparin	180-187	plasminogen	Homo sapiens	51-58
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	41-48	serpin family A member 10	Homo sapiens	182-185
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	41-48	serpin family A member 10	Homo sapiens	182-185
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	88-95	serpin family A member 10	Homo sapiens	150-153
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	88-95	serpin family A member 10	Homo sapiens	182-185
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	88-95	serpin family A member 10	Homo sapiens	182-185
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	88-95	serpin family A member 10	Homo sapiens	182-185
22540147-6	2012	Consistent with a template mechanism for heparin cofactor action, ZPI-CD-helix(alpha1-PI) inhibition of a FXa mutant containing a mutation in the heparin-binding site (FXa-R240A) was minimally affected by heparin.	Heparin	41-48	serpin family A member 10	Homo sapiens	66-69
22540147-6	2012	Consistent with a template mechanism for heparin cofactor action, ZPI-CD-helix(alpha1-PI) inhibition of a FXa mutant containing a mutation in the heparin-binding site (FXa-R240A) was minimally affected by heparin.	Heparin	146-153	serpin family A member 10	Homo sapiens	66-69
22540147-6	2012	Consistent with a template mechanism for heparin cofactor action, ZPI-CD-helix(alpha1-PI) inhibition of a FXa mutant containing a mutation in the heparin-binding site (FXa-R240A) was minimally affected by heparin.	Heparin	146-153	serpin family A member 10	Homo sapiens	66-69
22540147-7	2012	A significant decrease (~2-5-fold) in the heparin template effect was also observed for the inhibition of FXIa by ZPI mutants.	Heparin	42-49	serpin family A member 10	Homo sapiens	114-117
23407680-3	2012	In this study the mature part of human bone morphogenetic protein-7 (BMP-7) was engineered through substitution of the BMP-7 N-terminal sequence by heparin-binding site of BMP-2.	Heparin	148-155	bone morphogenetic protein 2	Homo sapiens	172-177
23040778-11	2012	UFH could exert protective effects by inhibiting expression of MMP-2 and MMP-9 in serum and lung tissue, in both mRNA and protein expression.	Heparin	0-3	matrix metallopeptidase 2	Rattus norvegicus	63-68
22540147-8	2012	Interestingly, ZPI derivatives exhibited a markedly elevated stoichiometry of inhibition with FXIa in the absence of heparin.	Heparin	117-124	serpin family A member 10	Homo sapiens	15-18
22540147-9	2012	These results suggest that basic residues of both helices C and D of ZPI interact with heparin to modulate the inhibitory function of the serpin.	Heparin	87-94	serpin family A member 10	Homo sapiens	69-72
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	18-25	p21 (RAC1) activated kinase 1	Homo sapiens	97-119
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	18-25	p21 (RAC1) activated kinase 1	Homo sapiens	121-125
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	18-25	p21 (RAC1) activated kinase 1	Homo sapiens	212-216
22759380-4	2012	In vitro maturation of cumulus oocyte complexes in the presence of exogenous heparin, which antagonizes HSPG signaling, prevented cumulus expansion and blocked the induction of cumulus-specific matrix genes, Has2 and Tnfaip6, whereas conversely, the mural granulosa-specific genes, Lhcgr and Cyp11a1, were strongly up-regulated.	Heparin	77-84	hyaluronan synthase 2	Homo sapiens	208-212
22759380-5	2012	Heparin also blocked phosphorylation of SMAD2.	Heparin	0-7	SMAD family member 2	Homo sapiens	40-45
22859710-1	2012	Antiplatelet factor 4 (PF4) antibodies have an important role in the most frequent drug-induced immune disorder, heparin-induced thrombocytopenia (HIT).	Heparin	113-120	platelet factor 4	Homo sapiens	23-26
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	177-184	p21 (RAC1) activated kinase 1	Homo sapiens	97-119
28188826-5	2017	The untagged TET2 enzyme was purified using cation exchange and heparin sepharose chromatography.	Heparin	64-71	tet methylcytosine dioxygenase 2	Homo sapiens	13-17
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	177-184	p21 (RAC1) activated kinase 1	Homo sapiens	121-125
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	177-184	p21 (RAC1) activated kinase 1	Homo sapiens	212-216
22285427-9	2012	These results suggest that the mechanism of hASC adhesion to MBP-bFGF immobilized on a PS substrate is mediated by a specific interaction between bFGF and heparin, and that the adhesion mechanism might provide an insight into the design of biomaterials to control the fate of stem cells.	Heparin	155-162	myelin basic protein	Homo sapiens	61-64
22504297-5	2012	Furthermore, rat embryonic fibroblasts (REFs) plated on fibronectin fragments lacking the heparin-binding domain that interacts with syndecan-4 showed much lower RhoA activation than that in cells plated on full-length fibronectin, indicating that RhoA is involved in syndecan-4-mediated cell adhesion signaling.	Heparin	90-97	syndecan 4	Rattus norvegicus	133-143
22504297-5	2012	Furthermore, rat embryonic fibroblasts (REFs) plated on fibronectin fragments lacking the heparin-binding domain that interacts with syndecan-4 showed much lower RhoA activation than that in cells plated on full-length fibronectin, indicating that RhoA is involved in syndecan-4-mediated cell adhesion signaling.	Heparin	90-97	syndecan 4	Rattus norvegicus	268-278
28297651-5	2017	Using a heparin-immobilized chip, SPR revealed that tau K18 and K19 bind heparin with a KD of 0.2 and 70 muM, respectively.	Heparin	8-15	keratin 19	Homo sapiens	64-67
23606934-1	2012	Heparin-induced thrombocytopenia (HIT) is a drug-mediated, prothrombotic disorder caused by immunization against platelet factor 4 (PF4) after complex formation with heparin or other polyanions.	Heparin	0-7	platelet factor 4	Homo sapiens	132-135
23606934-1	2012	Heparin-induced thrombocytopenia (HIT) is a drug-mediated, prothrombotic disorder caused by immunization against platelet factor 4 (PF4) after complex formation with heparin or other polyanions.	Heparin	166-173	platelet factor 4	Homo sapiens	132-135
23606934-2	2012	After their binding to PF4/heparin complexes on the platelet surface, HIT antibodies are capable of intravascular platelet activation by cross-linking Fcgamma receptor IIA leading to a platelet count decrease and/or thrombosis.	Heparin	27-34	Fc gamma receptor IIa	Homo sapiens	151-171
22475438-3	2012	Resulting antibodies against these PF4/heparin complexes can activate platelets via the platelet FcgammaIIa receptor, leading to thrombin generation and thus to the paradox of a prothrombotic state despite thrombocytopenia and application of heparin.	Heparin	39-46	platelet factor 4	Homo sapiens	35-38
22475438-3	2012	Resulting antibodies against these PF4/heparin complexes can activate platelets via the platelet FcgammaIIa receptor, leading to thrombin generation and thus to the paradox of a prothrombotic state despite thrombocytopenia and application of heparin.	Heparin	242-249	platelet factor 4	Homo sapiens	35-38
22223757-0	2012	Significance of heparin binding to basic residues in homologous to the amino terminus of hepatoma-derived growth factor and related proteins.	Heparin	16-23	heparin binding growth factor	Homo sapiens	89-119
28297651-5	2017	Using a heparin-immobilized chip, SPR revealed that tau K18 and K19 bind heparin with a KD of 0.2 and 70 muM, respectively.	Heparin	73-80	keratin 19	Homo sapiens	64-67
22223757-4	2012	With the HDGF HATH domain used as a model, residue K19 was the most critical basic residue in molecular recognition and protein internalization, and with its proximal proline-tryptophan-tryptophan-proline motif, coordinated a conformational change when binding to the heparin fragment.	Heparin	268-275	heparin binding growth factor	Homo sapiens	9-13
28297651-9	2017	NMR showed the largest chemical-shift perturbation (CSP) in R2 in tau K18, which was absent in K19, revealing differential binding sites in K18 and K19 to heparin.	Heparin	155-162	keratin 19	Homo sapiens	95-98
22953684-6	2012	RESULTS: The immunoassays revealed that heparin-preloaded PG-incubated matrices showed a sustained release of 56.28 pg/ml bFGF and 30.66 ng/ml TGF-beta1 after 24 h. Dynamic culture induced oMSC invasion in growth factor-loaded matrices.	Heparin	40-47	fibroblast growth factor 2	Ovis aries	122-126
28297651-9	2017	NMR showed the largest chemical-shift perturbation (CSP) in R2 in tau K18, which was absent in K19, revealing differential binding sites in K18 and K19 to heparin.	Heparin	155-162	keratin 19	Homo sapiens	148-151
22953684-6	2012	RESULTS: The immunoassays revealed that heparin-preloaded PG-incubated matrices showed a sustained release of 56.28 pg/ml bFGF and 30.66 ng/ml TGF-beta1 after 24 h. Dynamic culture induced oMSC invasion in growth factor-loaded matrices.	Heparin	40-47	transforming growth factor beta-1 proprotein	Ovis aries	143-152
28104757-5	2017	We determined that residues involved in heparin/HS binding, while not necessary for BMP antagonism, merge with the heparin/HS-binding epitope of BMP2.	Heparin	40-47	bone morphogenetic protein 2	Homo sapiens	145-149
22669117-17	2012	Heparin 25 and 125 mug/mL decreased the protein expression of vimentin and 14-3-3 zeta/delta and the mRNA expression of alpha(v)-integrin.	Heparin	0-7	integrin alpha V	Mus musculus	120-137
22669117-20	2012	CONCLUSION: Heparin inhibited PC-3M cell proliferation in vitro and B16-F10-luc-G5 cells metastasis in nude mice by inhibition of vimentin, 14-3-3 zeta/delta, and alpha(v)-integrin expression.	Heparin	12-19	integrin alpha V	Mus musculus	163-180
22234620-1	2012	BACKGROUND: The frequency of heparin-induced platelet antibodies (H/PF4 antibodies) following heparin exposure during percutaneous intervention with stent implantation is unknown.	Heparin	29-36	platelet factor 4	Homo sapiens	68-71
22234620-1	2012	BACKGROUND: The frequency of heparin-induced platelet antibodies (H/PF4 antibodies) following heparin exposure during percutaneous intervention with stent implantation is unknown.	Heparin	94-101	platelet factor 4	Homo sapiens	68-71
22371501-5	2012	Moreover, GSPP competitively inhibited bFGF binding to heparin/heparan sulfate via direct binding to bFGF.	Heparin	55-62	fibroblast growth factor 2	Mus musculus	39-43
22371501-5	2012	Moreover, GSPP competitively inhibited bFGF binding to heparin/heparan sulfate via direct binding to bFGF.	Heparin	55-62	fibroblast growth factor 2	Mus musculus	101-105
22038266-1	2012	AIM: Anti-platelet factor 4/heparin complex antibodies (anti-PF4/heparin Ab) have been found to cause heparin-induced thrombocytopenia (HIT), a clinical syndrome thrombocytopenia and thrombosis.	Heparin	28-35	platelet factor 4	Homo sapiens	61-64
28104757-7	2017	Overall, the present study shows that the Grem2 heparin/HS and BMP-binding epitopes are unique and independent, where, interestingly, the Grem2-BMP2 complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope.	Heparin	48-55	bone morphogenetic protein 2	Homo sapiens	144-148
21898414-10	2012	In conclusion, the heparin-induced up-regulation of HSPG expression is associated with the phosphorylation of focal adhesion proteins and Ras/Raf/MEK/ERK MAP and Ca(2+) /NO pathways.	Heparin	19-26	zinc fingers and homeoboxes 2	Homo sapiens	142-145
28253327-6	2017	The effect of heparin administration on OPG levels was studied in 20 patients referred to elective coronary angiography.	Heparin	14-21	TNF receptor superfamily member 11b	Homo sapiens	40-43
22394597-2	2012	Patients with HIT develop autoantibodies to the platelet factor 4 (PF4)/heparin complex, which is termed the HIT Ab complex.	Heparin	72-79	platelet factor 4	Homo sapiens	67-70
21688265-2	2012	This study examined the effect of the heparin-binding growth factor midkine (MK) on hypoxia-induced apoptosis and related signal pathways in mouse embryonic stem cells (mESCs).	Heparin	38-45	midkine	Mus musculus	68-75
22682144-1	2012	Platelet factor 4 (CXCL4-PF4) is a chemokine that binds to and neutralizes heparin and other negatively charged proteoglycans, but is also involved in angiogenesis and cancer development.	Heparin	75-82	platelet factor 4	Homo sapiens	19-24
22682144-1	2012	Platelet factor 4 (CXCL4-PF4) is a chemokine that binds to and neutralizes heparin and other negatively charged proteoglycans, but is also involved in angiogenesis and cancer development.	Heparin	75-82	platelet factor 4	Homo sapiens	25-28
28253327-13	2017	A 77% increase in OPG levels following heparin administration was found in patients undergoing elective coronary angiography.	Heparin	39-46	TNF receptor superfamily member 11b	Homo sapiens	18-21
22682144-2	2012	In some patients exposed to heparin, antibodies are generated against the CXCL-PF4/heparin complex that may activate platelets and coagulation and lead to thrombocytopenia and arterial or venous thrombosis, a condition commonly named heparin induced thrombocytopenia (HIT).	Heparin	28-35	platelet factor 4	Homo sapiens	79-82
22431632-0	2012	Dissecting the substrate recognition of 3-O-sulfotransferase for the biosynthesis of anticoagulant heparin.	Heparin	99-106	heparan sulfate-glucosamine 3-sulfotransferase 1	Homo sapiens	40-60
22682144-2	2012	In some patients exposed to heparin, antibodies are generated against the CXCL-PF4/heparin complex that may activate platelets and coagulation and lead to thrombocytopenia and arterial or venous thrombosis, a condition commonly named heparin induced thrombocytopenia (HIT).	Heparin	83-90	platelet factor 4	Homo sapiens	79-82
28253327-15	2017	The use of OPG as a biomarker in STEMI patients seems to be limited by a strong association with age, confounding effect of heparin administration, and little additive value to established biomarkers.	Heparin	124-131	TNF receptor superfamily member 11b	Homo sapiens	11-14
22682144-2	2012	In some patients exposed to heparin, antibodies are generated against the CXCL-PF4/heparin complex that may activate platelets and coagulation and lead to thrombocytopenia and arterial or venous thrombosis, a condition commonly named heparin induced thrombocytopenia (HIT).	Heparin	83-90	platelet factor 4	Homo sapiens	79-82
22431632-4	2012	3-OST isoform 1 (3-OST-1) is the key enzyme for the biosynthesis of anticoagulant heparin.	Heparin	82-89	heparan sulfate-glucosamine 3-sulfotransferase 1	Homo sapiens	0-15
22431632-4	2012	3-OST isoform 1 (3-OST-1) is the key enzyme for the biosynthesis of anticoagulant heparin.	Heparin	82-89	heparan sulfate-glucosamine 3-sulfotransferase 1	Homo sapiens	17-24
28218620-1	2017	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder initiated by antibodies against complexes between human platelet factor 4 (hPF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	142-146
21688265-2	2012	This study examined the effect of the heparin-binding growth factor midkine (MK) on hypoxia-induced apoptosis and related signal pathways in mouse embryonic stem cells (mESCs).	Heparin	38-45	midkine	Mus musculus	77-79
22850051-7	2012	PAPP-A levels can be influenced by various chemicals and drugs, among them mainly heparin.	Heparin	82-89	pappalysin 1	Homo sapiens	0-6
28218620-4	2017	hPF4 released from platelets predominantly bound to peri-injury endothelium and formed HIT antigenic complexes that were dissociated by heparin.	Heparin	136-143	platelet factor 4	Homo sapiens	0-4
22206940-8	2012	These studies demonstrate that binding of HCII to the thrombin heparin complex is dramatically enhanced compared with heparin binding alone and that exosite I is still available for ligand or HCII binding when both heparin binding sites on thrombin are saturated.	Heparin	63-70	serpin family D member 1	Homo sapiens	42-46
22382479-5	2012	During hospitalization, the patient received heparin, and her platelet count dropped to 12,000 cells/muL 13 days after the initiation of heparin.	Heparin	137-144	tripartite motif containing 37	Homo sapiens	101-104
28053085-10	2017	Finally, heparin non-specifically binds at the YKL-40 surface, as predicted from structural studies.	Heparin	9-16	chitinase 3 like 1	Homo sapiens	47-53
22049520-0	2012	Heparin-induced thrombocytopenia: in vitro studies on the interaction of dabigatran, rivaroxaban, and low-sulfated heparin, with platelet factor 4 and anti-PF4/heparin antibodies.	Heparin	115-122	platelet factor 4	Homo sapiens	156-159
22333045-7	2012	There was a significant difference (p &lt; 0.05) in the mean channel fluorescence intensity (MFI) of mCD14 on neutrophils in whole blood samples anticoagulated with HEPARIN (MFI = 64.77) in comparison with those in whole blood samples anticoagulated with either EDTA (MFI = 38.25) or CITRATE (MFI = 43.7).	Heparin	165-172	CD14 antigen	Mus musculus	101-106
22333045-8	2012	The MFI of mCD14 on monocytes in whole blood samples anticoagulted with HEPARIN (MFI = 206.90) was significantly higher than the MFI in whole blood samples anticoagulated with EDTA (MFI = 149.37) but similar to that with CITRATE (MFI = 162.55).	Heparin	72-79	CD14 antigen	Mus musculus	11-16
22333045-10	2012	However, MFI of mCD14 on monocytes was about 3.2-folds (HEPARIN), 3.9-folds (EDTA) or 3.7 folds (CITRATE) higher than those on neutrophils.	Heparin	56-63	CD14 antigen	Mus musculus	16-21
22333045-13	2012	CONCLUSION: From these results, it is suggested that sodium heparin should be the preferred anticoagulant for use in the reliable quantification of the surface expression of mCD14.	Heparin	53-67	CD14 antigen	Mus musculus	174-179
22302552-0	2012	Levels of heparin-releasable TFPI are increased in first-ever lacunar stroke patients.	Heparin	10-17	tissue factor pathway inhibitor	Homo sapiens	29-33
22302552-5	2012	Heparin-releasable free FL TFPI was determined in a random subset of 17 patients and 15 controls.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	27-31
22302552-8	2012	However, levels of heparin-releasable free FL TFPI were higher in patients than in controls.	Heparin	19-26	tissue factor pathway inhibitor	Homo sapiens	46-50
22302552-9	2012	CONCLUSIONS: Although ambient plasma levels of total TFPI were not different in subtypes of LS, the increased levels of heparin-releasable TFPI in patients suggest a role of endothelial activation in the pathogenesis of LS.	Heparin	120-127	tissue factor pathway inhibitor	Homo sapiens	139-143
22308278-1	2012	In this issue of Blood, Krauel and colleagues identify two potential off-label treatments(rivaroxaban, dabigatran) for heparin-induced thrombocytopenia (HIT),and also outline aHIT prevention strategy through disrupting PF4/heparin complexes with low-sulfated heparin; the former approach will be easy to implement, the latter much harder:but potentially more worthwhile	Heparin	119-126	platelet factor 4	Homo sapiens	219-222
27979781-2	2017	It also functions as an activating ligand of the vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2), and binds strongly to the sulfated polysaccharide, heparin.	Heparin	163-170	kinase insert domain protein receptor	Mus musculus	49-101
22209849-6	2012	Using an endoplasmic reticulum (ER)-Ca(2+) mobilizer (thapsigargin) and an ER-IP3R antagonist (heparin), results revealed ER as a major source of [Ca(2+)](c) which led to the activation of calpain and caspase12, and cleavage of fodrin.	Heparin	95-102	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	78-82
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	dual oxidase 1	Homo sapiens	113-118
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	dual oxidase 1	Homo sapiens	170-175
21984036-11	2012	Heparin can decrease the level of Duox1, ROS production and block the PMA-induced activation of EGFR, thus inhibiting the overexpression of mucin MUC5AC in a dose-dependent manner.	Heparin	0-7	dual oxidase 1	Homo sapiens	34-39
22075045-11	2012	CONCLUSION: Higher levels of anti-PF4/heparin antibody are associated with increased thrombosis risk among patients with clinically suspected heparin-induced thrombocytopenia and might have clinical utility for prediction of true heparin-induced thrombocytopenia and the development of thrombosis.	Heparin	38-45	platelet factor 4	Homo sapiens	34-37
22075045-11	2012	CONCLUSION: Higher levels of anti-PF4/heparin antibody are associated with increased thrombosis risk among patients with clinically suspected heparin-induced thrombocytopenia and might have clinical utility for prediction of true heparin-induced thrombocytopenia and the development of thrombosis.	Heparin	142-149	platelet factor 4	Homo sapiens	34-37
27979781-2	2017	It also functions as an activating ligand of the vascular endothelial growth factor (VEGF) receptor 2 (VEGFR2), and binds strongly to the sulfated polysaccharide, heparin.	Heparin	163-170	kinase insert domain protein receptor	Mus musculus	103-109
23047095-4	2012	The purified His-PF4 protein was further identified by cleavage with enterokinase and MS, and its heparin-neutralizing activity was determined by colony formation assay.	Heparin	98-105	platelet factor 4	Homo sapiens	17-20
28082743-9	2017	The uptake of ASC-derived artificial nanovesicles was inhibited by heparin, which is a competitive inhibitor of heparan sulfate proteoglycan that is associated with FGF2 signaling.	Heparin	67-74	fibroblast growth factor 2	Mus musculus	165-169
21746763-0	2012	Computational analyses of the catalytic and heparin-binding sites and their interactions with glycosaminoglycans in glycoside hydrolase family 79 endo-beta-D-glucuronidase (heparanase).	Heparin	44-51	glucuronidase beta	Homo sapiens	151-171
23308316-1	2012	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction caused by antibodies to the heparin/platelet factor 4 (PF4) complexes.	Heparin	14-21	platelet factor 4	Homo sapiens	109-134
23308316-1	2012	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction caused by antibodies to the heparin/platelet factor 4 (PF4) complexes.	Heparin	14-21	platelet factor 4	Homo sapiens	136-139
23308316-5	2012	Heparin-PF4 antibodies were detected by both Heparin-induced platelet activation test (HIPA) and Heparin platelet induced antibodies enzyme immunoassay.	Heparin	0-7	platelet factor 4	Homo sapiens	8-11
27922061-5	2016	The bFGF-ASC complex was further encapsulated into a heparin modified poloxamer (HP) solution to prepare atemperature-sensitive hydrogel (bFGF-ASC-HP).	Heparin	53-60	fibroblast growth factor 2	Rattus norvegicus	4-8
22723979-8	2012	The SI (stoichiometry of inhibition) value for the inhibition of EP by PCI was 10.8 in the absence and 17.9 in the presence of UFH (10 U/ml).	Heparin	127-130	transmembrane serine protease 15	Homo sapiens	65-67
22082515-2	2011	Heparin-induced thrombocytopenia (HIT) explains thrombocytopenia in only approximately 1/100 critically ill patients; also, only 1 or 2 in 10 ICU patients with a positive PF4-dependent enzyme immunoassay has "true" HIT.	Heparin	0-7	platelet factor 4	Homo sapiens	171-174
22243931-6	2012	Taken together, these data indicate that the heparin bound bFGF-coated and DEX-loaded PLGA microsphere constructs is an effective bioactive scaffold for the regeneration of NP tissue.	Heparin	45-52	fibroblast growth factor 2	Rattus norvegicus	59-63
27913490-3	2016	Recent basic scientific studies have advanced our understanding of disease pathogenesis through studies of the PF4/heparin structure, immune mechanisms, and cellular basis of thrombosis.	Heparin	115-122	platelet factor 4	Homo sapiens	111-114
22261751-8	2012	RESULTS: Exogenous FGF-10 inhibited branching and induced cystic lung growth only in cultures containing heparin.	Heparin	105-112	fibroblast growth factor 10	Rattus norvegicus	19-25
22261751-11	2012	CONCLUSIONS: Unlike FGF-7, FGF-10 effects on lung branching morphogenesis are heparin-dependent.	Heparin	78-85	fibroblast growth factor 10	Rattus norvegicus	27-33
23133647-6	2012	Here, we show that the corresponding region of fibrillin-2 binds heparin very poorly, highlighting a novel functional difference between the two isoforms.	Heparin	65-72	fibrillin 2	Homo sapiens	47-58
21875394-2	2011	It requires the combination of clinical data with the detection of antibodies directed against platelet factor 4 (PF4) in complex with polyanions (PA) such as heparin.	Heparin	159-166	platelet factor 4	Homo sapiens	114-117
21710996-2	2011	Prior to mineralization, chitosan and heparin were covalently immobilized onto the surface of the fibers to accelerate the nucleation of bone-like HAp crystals.	Heparin	38-45	reticulon 3	Homo sapiens	147-150
21671895-7	2011	Anti-PF4/H Abs were detected by ELISA in 22 cases (12 8%) in the heparin group.	Heparin	65-72	platelet factor 4	Homo sapiens	5-8
22912725-0	2012	Heparin inhibits Hepatocyte Growth Factor induced motility and invasion of hepatocellular carcinoma cells through early growth response protein 1.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	17-41
22912725-4	2012	However, the role of heparin in the regulation of HGF signaling remains controversial and the effects of heparin on HGF-induced biological responses during hepatocarcinogenesis is not yet defined.	Heparin	105-112	hepatocyte growth factor	Homo sapiens	116-119
22912725-5	2012	In this study we determined the effects of heparin on HGF-induced activities of HCC cells and the underlying molecular mechanisms.	Heparin	43-50	hepatocyte growth factor	Homo sapiens	54-57
22912725-6	2012	Here, we report for the first time that heparin inhibits HGF-induced adhesion, motility and invasion of HCC cells.	Heparin	40-47	hepatocyte growth factor	Homo sapiens	57-60
22912725-7	2012	In addition, heparin reduced HGF-induced activation of c-Met and MAPK in a dose-dependent manner, as well as decreased transcriptional activation and expression of Early growth response factor 1 (Egr1).	Heparin	13-20	hepatocyte growth factor	Homo sapiens	29-32
22912725-8	2012	HGF-induced MMP-2 and MMP-9 activation, and MT1-MMP expression, also were inhibited by heparin.	Heparin	87-94	hepatocyte growth factor	Homo sapiens	0-3
22912725-8	2012	HGF-induced MMP-2 and MMP-9 activation, and MT1-MMP expression, also were inhibited by heparin.	Heparin	87-94	matrix metallopeptidase 2	Homo sapiens	12-17
27697839-8	2016	We further show that heparin-derived dodecasaccharide is able to induce dimerization of OPG monomers with a stoichiometry of 1:1.	Heparin	21-28	TNF receptor superfamily member 11b	Homo sapiens	88-91
22066556-2	2011	Of these, we have previously developed heparin-conjugated PLGA nanospheres (HCPN) as a long-term delivery system for BMP-2.	Heparin	39-46	bone morphogenetic protein 2	Oryctolagus cuniculus	117-122
21773727-9	2011	A solution competition SPR study was performed to test the ability of different O-acylated LMWHP derivatives to inhibit fibroblast growth factor (FGF) 1 and FGF2 binding to surface-immobilized heparin.	Heparin	193-200	fibroblast growth factor 1	Bos taurus	120-152
21652703-15	2011	The interaction of PEDF with collagen I was specifically competed with by heparin but not by chondroitin sulfate-C or hyaluronan.	Heparin	74-81	serpin family F member 1	Homo sapiens	19-23
27739168-3	2016	In this work, the protein transduction ability of a novel CPP (termed HBP) derived from the heparin-binding domain of HB-EGF was evaluated.	Heparin	92-99	heme binding protein 1	Homo sapiens	70-73
21565207-9	2011	The cellular uptake of MafA PTD can be completely blocked by heparin, whereas cytochalasin D and amiloride were partially effective in blocking the PTD-EGFP protein entry.	Heparin	61-68	MAF bZIP transcription factor A	Rattus norvegicus	23-27
21939260-0	2011	Biophysical investigations on the interaction of the major bovine seminal plasma protein, PDC-109, with heparin.	Heparin	104-111	seminal plasma protein PDC-109	Bos taurus	66-97
21939260-1	2011	PDC-109, the major bovine seminal plasma protein, binds to sperm plasma membrane and modulates capacitation in the presence of heparin.	Heparin	127-134	seminal plasma protein PDC-109	Bos taurus	0-7
21939260-1	2011	PDC-109, the major bovine seminal plasma protein, binds to sperm plasma membrane and modulates capacitation in the presence of heparin.	Heparin	127-134	seminal plasma protein PDC-109	Bos taurus	26-48
21939260-2	2011	In view of this, the PDC-109/heparin interaction has been investigated employing various biophysical approaches.	Heparin	29-36	seminal plasma protein PDC-109	Bos taurus	21-28
27779234-8	2016	Recombinant C-termini of ADAMTS10 and ADAMTS6, both of which induce focal adhesions, bind heparin and syndecan-4.	Heparin	90-97	ADAM metallopeptidase with thrombospondin type 1 motif 10	Homo sapiens	25-33
21939260-3	2011	Isothermal titration calorimetric studies yielded the association constant and changes in enthalpy and entropy for the interaction at 25  C (pH 7.4) as 1.92 (+-0.2) x 10(5) M(-1), 18.6 (+-1.6) kcal M(-1), and 86.5 (+-5.1) cal M(-1) K(-1), respectively, whereas differential scanning calorimetric studies indicated that heparin binding results in a significant increase in the thermal stability of PDC-109.	Heparin	319-326	seminal plasma protein PDC-109	Bos taurus	397-404
21939260-5	2011	Circular dichroism spectroscopic studies indicated that PDC-109 retains its conformational features even up to 70-75  C in the presence of heparin, whereas the native protein unfolds at about 55  C. Atomic force microscopic studies demonstrated that large oligomeric structures are formed upon binding of PDC-109 to heparin, indicating an increase in the local density of the protein, which may be relevant to the ability of heparin to potentiate PDC-109 induced sperm capacitation.	Heparin	139-146	seminal plasma protein PDC-109	Bos taurus	56-63
21939260-5	2011	Circular dichroism spectroscopic studies indicated that PDC-109 retains its conformational features even up to 70-75  C in the presence of heparin, whereas the native protein unfolds at about 55  C. Atomic force microscopic studies demonstrated that large oligomeric structures are formed upon binding of PDC-109 to heparin, indicating an increase in the local density of the protein, which may be relevant to the ability of heparin to potentiate PDC-109 induced sperm capacitation.	Heparin	316-323	seminal plasma protein PDC-109	Bos taurus	56-63
21939260-5	2011	Circular dichroism spectroscopic studies indicated that PDC-109 retains its conformational features even up to 70-75  C in the presence of heparin, whereas the native protein unfolds at about 55  C. Atomic force microscopic studies demonstrated that large oligomeric structures are formed upon binding of PDC-109 to heparin, indicating an increase in the local density of the protein, which may be relevant to the ability of heparin to potentiate PDC-109 induced sperm capacitation.	Heparin	316-323	seminal plasma protein PDC-109	Bos taurus	56-63
21829356-8	2011	We further showed that heparin inhibited the binding of CX3CL1 by the SECRET domain and the SECRET domain inhibited RAW264.7 cell migration induced by CX3CL1.	Heparin	23-30	chemokine (C-X3-C motif) ligand 1	Mus musculus	56-62
21829356-8	2011	We further showed that heparin inhibited the binding of CX3CL1 by the SECRET domain and the SECRET domain inhibited RAW264.7 cell migration induced by CX3CL1.	Heparin	23-30	chemokine (C-X3-C motif) ligand 1	Mus musculus	151-157
27380556-1	2016	PURPOSE OF REVIEW: The purpose of this review is to summarize recent findings on heparin-induced thrombocytopenia (HIT), a prothrombotic disorder caused by platelet-activating IgG targeting platelet factor 4 (PF4)/polyanion complexes.	Heparin	81-88	platelet factor 4	Homo sapiens	209-212
21802135-9	2011	Excellent chondrogenic nature of the heparin-based hydrogel might be associated with the hydrogel characteristic that can secure endogenous growth factors secreted from chondrocytes, which then can promote the chondrogenesis, as suggested by the detection of TGF-beta1 in both in vitro and in vivo cell/hydrogel constructs.	Heparin	37-44	transforming growth factor, beta 1	Mus musculus	259-268
27380556-5	2016	HIT has features of both B-cell and T-cell immune responses; uptake of PF4/heparin complexes into macrophages ("macropinocytosis") facilitates the anti-PF4/heparin immune response.	Heparin	75-82	platelet factor 4	Homo sapiens	71-74
22340251-4	2011	The laboratory test for heparin-induced thrombocytopenia (HIT) specific antibodies (heparin-platelet factor, PF4) was positive.	Heparin	24-31	platelet factor 4	Homo sapiens	109-112
21805439-6	2011	In particular, HCII binds many glycosaminoglycans (GAGs) such as heparin and heparin sulfate as well as several different polyanions to enhance its inhibition of thrombin.	Heparin	65-72	serpin family D member 1	Homo sapiens	15-19
21518912-9	2011	In support of this idea, a chicken LPL (cLPL)-specific monoclonal antibody, xCAL 1-11 (epitope, cLPL amino acids 416-435), blocks cLPL binding to GPIHBP1 but not to heparin.	Heparin	165-172	lipoprotein lipase	Gallus gallus	35-38
21343305-6	2011	We demonstrate that VEGF-C binds to heparan sulfate purified from primary lymphatic endothelia, and activation of lymphatic endothelial Erk1/2 in response to VEGF-C is reduced by interference with heparin or pretreatment of cells with heparinase, which destroys heparan sulfate.	Heparin	197-204	mitogen-activated protein kinase 3	Mus musculus	136-142
27585207-5	2016	Self-assembled PECs have been fabricated to provide better control of BMP-2/NELL-1 delivery via heparin binding and further potentiate growth factor bioactivity by enhancing in vivo stability.	Heparin	96-103	bone morphogenetic protein 2	Homo sapiens	70-75
22345625-3	2011	We asked whether levels of antibody to heparin-platelet factor 4 (PF4) complex were differentially present in unfractionated heparin (UFH) versus Enoxaparin, following hip fracture and whether one particular subtype of antibodies was more prevalent.	Heparin	39-46	platelet factor 4	Homo sapiens	66-69
22345625-3	2011	We asked whether levels of antibody to heparin-platelet factor 4 (PF4) complex were differentially present in unfractionated heparin (UFH) versus Enoxaparin, following hip fracture and whether one particular subtype of antibodies was more prevalent.	Heparin	134-137	platelet factor 4	Homo sapiens	39-64
22345625-3	2011	We asked whether levels of antibody to heparin-platelet factor 4 (PF4) complex were differentially present in unfractionated heparin (UFH) versus Enoxaparin, following hip fracture and whether one particular subtype of antibodies was more prevalent.	Heparin	134-137	platelet factor 4	Homo sapiens	66-69
22345625-5	2011	The prevalence of antiheparin-PF4 antibodies was higher in the UFH group especially on postoperative day 7.	Heparin	63-66	platelet factor 4	Homo sapiens	30-33
22345625-6	2011	Patients treated with UFH showed a greater prevalence of antiheparin-PF4 antibodies and a greater prevalence of immunoglobulin G (IgG) subtype.	Heparin	22-25	platelet factor 4	Homo sapiens	69-72
22345625-8	2011	When comparing low-molecular-weight heparin (LMWH) with UFH, the incidence of new antiheparin-PF4 antibody production is higher in patients treated with UFH.	Heparin	36-43	platelet factor 4	Homo sapiens	94-97
20558775-0	2011	Heparin inhibits pulmonary artery smooth muscle cell proliferation through guanine nucleotide exchange factor-H1/RhoA/Rho kinase/p27.	Heparin	0-7	ras homolog family member A	Mus musculus	113-117
26377606-3	2016	The aim of this study was to characterize the fluctuations in the levels of natural anticoagulants, particularly TFPI, in the course of sepsis and to find out their association with the anticoagulant action of the low-molecular-weight heparin enoxaparin.	Heparin	235-242	tissue factor pathway inhibitor	Homo sapiens	113-117
21220417-0	2011	Heparin is a major activator of the anticoagulant serpin, protein Z-dependent protease inhibitor.	Heparin	0-7	serpin family A member 10	Homo sapiens	66-96
21220417-2	2011	Here we provide evidence that, in addition to the established cofactors, protein Z, lipid, and calcium, heparin is an important cofactor of ZPI anticoagulant function.	Heparin	104-111	serpin family A member 10	Homo sapiens	140-143
21220417-3	2011	Heparin produced 20-100-fold accelerations of ZPI reactions with factor Xa and factor XIa to yield second order rate constants approaching the physiologically significant diffusion limit (k(a) = 10(6) to 10(7) M(-1) s(-1)).	Heparin	0-7	serpin family A member 10	Homo sapiens	46-49
21220417-4	2011	The dependence of heparin accelerating effects on heparin concentration was bell-shaped for ZPI reactions with both factors Xa and XIa, consistent with a template-bridging mechanism of heparin rate enhancement.	Heparin	18-25	serpin family A member 10	Homo sapiens	92-95
21220417-4	2011	The dependence of heparin accelerating effects on heparin concentration was bell-shaped for ZPI reactions with both factors Xa and XIa, consistent with a template-bridging mechanism of heparin rate enhancement.	Heparin	50-57	serpin family A member 10	Homo sapiens	92-95
21220417-4	2011	The dependence of heparin accelerating effects on heparin concentration was bell-shaped for ZPI reactions with both factors Xa and XIa, consistent with a template-bridging mechanism of heparin rate enhancement.	Heparin	50-57	serpin family A member 10	Homo sapiens	92-95
21220417-5	2011	Maximal accelerations of ZPI-factor Xa reactions required calcium, which augmented the heparin acceleration by relieving Gla domain inhibition as previously shown for heparin bridging of the antithrombin-factor Xa reaction.	Heparin	87-94	serpin family A member 10	Homo sapiens	25-28
22345625-8	2011	When comparing low-molecular-weight heparin (LMWH) with UFH, the incidence of new antiheparin-PF4 antibody production is higher in patients treated with UFH.	Heparin	56-59	platelet factor 4	Homo sapiens	94-97
22345625-8	2011	When comparing low-molecular-weight heparin (LMWH) with UFH, the incidence of new antiheparin-PF4 antibody production is higher in patients treated with UFH.	Heparin	153-156	platelet factor 4	Homo sapiens	94-97
21719530-7	2011	In the study group (XPC), unfractionated heparin was embedded in the PC matrix of the oxygenator and arterial line filter.	Heparin	41-48	XPC complex subunit, DNA damage recognition and repair factor	Homo sapiens	20-23
21220417-6	2011	Heparin acceleration of both ZPI-protease reactions was optimal at heparin concentrations and heparin chain lengths comparable with those that produce physiologically significant rate enhancements of other serpin-protease reactions.	Heparin	0-7	serpin family A member 10	Homo sapiens	29-32
27125765-2	2016	Herein, a multifunctional self-assembled nanosystem consisting of amphiphilic c(RGDyK)-functionalized low-molecular-weight heparin-gambogic acid conjugate (cRHG) is developed, using c(RGDyK) peptide as alphav beta3 integrin targeting moiety to realize a double-targeted delivery to both tumor cells and angiogenic vasculature.	Heparin	123-130	calcium channel, voltage-dependent, beta 3 subunit	Mus musculus	209-214
21220417-6	2011	Heparin acceleration of both ZPI-protease reactions was optimal at heparin concentrations and heparin chain lengths comparable with those that produce physiologically significant rate enhancements of other serpin-protease reactions.	Heparin	67-74	serpin family A member 10	Homo sapiens	29-32
21220417-6	2011	Heparin acceleration of both ZPI-protease reactions was optimal at heparin concentrations and heparin chain lengths comparable with those that produce physiologically significant rate enhancements of other serpin-protease reactions.	Heparin	94-101	serpin family A member 10	Homo sapiens	29-32
21220417-7	2011	Protein Z binding to ZPI minimally affected heparin rate enhancements, indicating that heparin binds to a distinct site on ZPI and activates ZPI in its physiologically relevant complex with protein Z.	Heparin	87-94	serpin family A member 10	Homo sapiens	21-24
21220417-7	2011	Protein Z binding to ZPI minimally affected heparin rate enhancements, indicating that heparin binds to a distinct site on ZPI and activates ZPI in its physiologically relevant complex with protein Z.	Heparin	87-94	serpin family A member 10	Homo sapiens	123-126
21220417-7	2011	Protein Z binding to ZPI minimally affected heparin rate enhancements, indicating that heparin binds to a distinct site on ZPI and activates ZPI in its physiologically relevant complex with protein Z.	Heparin	87-94	serpin family A member 10	Homo sapiens	123-126
21360640-0	2011	Heparin plays a key regulatory role via a p53/FAK-dependent signaling in melanoma cell adhesion and migration.	Heparin	0-7	protein tyrosine kinase 2	Homo sapiens	46-49
21360640-4	2011	Cell treatment with heparin caused a marked downregulation in FAK expression (P &lt;= 0.01).	Heparin	20-27	protein tyrosine kinase 2	Homo sapiens	62-65
20659908-0	2011	Effects of unfractioned heparin and low-molecular-weight heparin on osteoprotegerin and RANKL plasma levels in haemodialysis patients.	Heparin	24-31	TNF receptor superfamily member 11b	Homo sapiens	68-83
21204619-7	2011	Given that the efficiency and selectivity of BMP4-induced TE depended on medium components, we developed a basal medium containing insulin and heparin.	Heparin	143-150	bone morphogenetic protein 4	Homo sapiens	45-49
21249364-8	2011	In conclusion, regulating SDF1 gradients with heparin-containing hydrogels may offer valuable options to direct site-specific migration of HSPC.	Heparin	46-53	C-X-C motif chemokine ligand 12	Homo sapiens	26-30
21600196-9	2011	In addition, a variety of known UB branching morphogens (i.e., pleiotrophin, heregulin, FGF1 and GDNF) were found to have a higher affinity for 6-O sulfated heparin providing additional support for the notion that this HS modification is important for robust UB branching morphogenesis.	Heparin	157-164	pleiotrophin	Mus musculus	63-75
21600196-9	2011	In addition, a variety of known UB branching morphogens (i.e., pleiotrophin, heregulin, FGF1 and GDNF) were found to have a higher affinity for 6-O sulfated heparin providing additional support for the notion that this HS modification is important for robust UB branching morphogenesis.	Heparin	157-164	neuregulin 1	Mus musculus	77-86
21600196-9	2011	In addition, a variety of known UB branching morphogens (i.e., pleiotrophin, heregulin, FGF1 and GDNF) were found to have a higher affinity for 6-O sulfated heparin providing additional support for the notion that this HS modification is important for robust UB branching morphogenesis.	Heparin	157-164	glial cell line derived neurotrophic factor	Mus musculus	97-101
20659908-0	2011	Effects of unfractioned heparin and low-molecular-weight heparin on osteoprotegerin and RANKL plasma levels in haemodialysis patients.	Heparin	57-64	TNF receptor superfamily member 11b	Homo sapiens	68-83
20659908-1	2011	BACKGROUND: This randomized crossover study investigated the effects of unfractioned heparin (UFH) and low-molecular-weight heparin (LMWH) on intra- and post-dialytic blood levels of osteoprotegerin (OPG), receptor activator of nuclear factor kappa B ligand (RANKL) and inflammatory cytokines.	Heparin	85-92	TNF receptor superfamily member 11b	Homo sapiens	183-198
20659908-1	2011	BACKGROUND: This randomized crossover study investigated the effects of unfractioned heparin (UFH) and low-molecular-weight heparin (LMWH) on intra- and post-dialytic blood levels of osteoprotegerin (OPG), receptor activator of nuclear factor kappa B ligand (RANKL) and inflammatory cytokines.	Heparin	124-131	TNF receptor superfamily member 11b	Homo sapiens	183-198
27098389-0	2016	Is Heparin Effective for the Controlled Delivery of High-Dose Bone Morphogenetic Protein-2?	Heparin	3-10	bone morphogenetic protein 2	Homo sapiens	62-90
20659908-11	2011	When we analysed the changes in OPG levels over time, we found that the administration of heparin, regardless of the type, determined an increase in circulating OPG with a zenith at 15 min (T1), with a return back to the baseline levels within the 24th hour post-infusion.	Heparin	90-97	TNF receptor superfamily member 11b	Homo sapiens	32-35
20659908-11	2011	When we analysed the changes in OPG levels over time, we found that the administration of heparin, regardless of the type, determined an increase in circulating OPG with a zenith at 15 min (T1), with a return back to the baseline levels within the 24th hour post-infusion.	Heparin	90-97	TNF receptor superfamily member 11b	Homo sapiens	161-164
21653700-3	2011	Here we report that hFGF19 at picomolar levels require sulfated glycosaminoglycans (sGAGs), such as heparan sulfate, heparin, and chondroitin sulfates, for its signaling via human FGFR4 in the presence of human betaKlotho.	Heparin	117-124	fibroblast growth factor 19	Homo sapiens	20-26
21653700-5	2011	At nanomolar levels, in contrast, hFGF19 activates all types of human FGFRs, i.e. FGFR1c, FGFR2c, FGFR3c, and FGFR4 in the co-presence of betaKlotho and heparin and activates FGFR4 even in the absence of betaKlotho.	Heparin	153-160	fibroblast growth factor 19	Homo sapiens	34-40
27098389-1	2016	Sustained release of bone morphogenetic protein (BMP)-2 by heparin-contained biomaterials is advantageous for bone tissue regeneration using low-dose BMP-2.	Heparin	59-66	bone morphogenetic protein 2	Homo sapiens	21-55
27098389-1	2016	Sustained release of bone morphogenetic protein (BMP)-2 by heparin-contained biomaterials is advantageous for bone tissue regeneration using low-dose BMP-2.	Heparin	59-66	bone morphogenetic protein 2	Homo sapiens	150-155
21261941-7	2011	The seroconversion incidence of IgG-class PF4/heparin antibodies was higher in patients receiving UFH (32.7%) compared to those receiving LMWH (9.5%) or fondaparinux (14.8%).	Heparin	98-101	platelet factor 4	Homo sapiens	42-45
21118381-1	2011	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a rare complication of heparin therapy resulting from antibody production to platelet factor 4 and heparin complexes (H-PF4).	Heparin	12-19	platelet factor 4	Homo sapiens	174-177
27098389-3	2016	This study aimed to evaluate the efficacy of a heparin-conjugated collagen sponge (HCS) with high-dose BMP-2 delivery by investigating in vivo initial osteogenic regulation and bone healing over 12 weeks in comparison with that of an absorbable collagen sponge (ACS).	Heparin	47-54	bone morphogenetic protein 2	Homo sapiens	103-108
21118381-1	2011	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a rare complication of heparin therapy resulting from antibody production to platelet factor 4 and heparin complexes (H-PF4).	Heparin	77-84	platelet factor 4	Homo sapiens	174-177
27110777-0	2016	Unfractionated Heparin Promotes Osteoclast Formation in Vitro by Inhibiting Osteoprotegerin Activity.	Heparin	15-22	TNF receptor superfamily member 11b	Homo sapiens	76-91
21296407-0	2011	Cell affinity for bFGF immobilized heparin-containing poly(lactide-co-glycolide) scaffolds.	Heparin	35-42	fibroblast growth factor 2	Mus musculus	18-22
21296407-1	2011	In order to effectively and uniformly immobilize basic fibroblast growth factor (bFGF) to thick PLGA scaffold, the heparin-conjugated PLGA (H-PLGA) was synthesized at the first by reaction between heparin and a low molecular weight PLGA.	Heparin	115-122	fibroblast growth factor 2	Mus musculus	49-79
21296407-1	2011	In order to effectively and uniformly immobilize basic fibroblast growth factor (bFGF) to thick PLGA scaffold, the heparin-conjugated PLGA (H-PLGA) was synthesized at the first by reaction between heparin and a low molecular weight PLGA.	Heparin	115-122	fibroblast growth factor 2	Mus musculus	81-85
21223602-8	2011	The C-terminal half bound to the peptide more strongly than the N-terminal half, and heparin inhibited midkine from binding to the peptide.	Heparin	85-92	midkine	Mus musculus	103-110
21467643-0	2011	Down-regulation of vascular endothelial growth factor and up-regulation of pigment epithelium derived factor make low molecular weight heparin-endostatin and polyethylene glycol-endostatin potential candidates for anti-angiogenesis drug.	Heparin	135-142	collagen type XVIII alpha 1 chain a	Danio rerio	143-153
27110777-5	2016	According to previous studies, heparin could bind specifically to OPG and inhibit its activity, so we hypothesized that this might be a possible mechanism of heparin activity.	Heparin	31-38	TNF receptor superfamily member 11b	Homo sapiens	66-69
21076280-12	2011	Further consideration of precipitating events in these individuals merits further investigation and may lead to valuable insight into the pathophysiology of heparin-independent PF4-related thrombocytopenia and thrombosis.	Heparin	157-164	platelet factor 4	Homo sapiens	177-180
21448669-2	2011	We hypothesized that a slow-degrading heparin-incorporated hyaluronan (HA) hydrogel can preserve BMP-2; while an arterio-venous (A-V) loop can support axial vascularization to provide nutrition for a bio-artificial bone graft.	Heparin	38-45	bone morphogenetic protein 2	Rattus norvegicus	97-102
20977482-1	2011	BACKGROUND: Heparin-induced thrombocytopenia and thrombosis (HITT) is characterized by thrombocytopenia due to the formation of antibodies against heparin : platelet factor 4 (PF4) complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	176-179
21987113-8	2011	Flow cytometric analysis using anti-CD14 (monocyte marker) and anti-CD83 (mature DC marker) revealed that expression of CD14 decreased in MCM plus heparin-treated DC, and the expression of CD83 was increased when heparin and MCM used as a maturation factor.	Heparin	147-154	CD14 molecule	Homo sapiens	36-40
27110777-5	2016	According to previous studies, heparin could bind specifically to OPG and inhibit its activity, so we hypothesized that this might be a possible mechanism of heparin activity.	Heparin	158-165	TNF receptor superfamily member 11b	Homo sapiens	66-69
21987113-8	2011	Flow cytometric analysis using anti-CD14 (monocyte marker) and anti-CD83 (mature DC marker) revealed that expression of CD14 decreased in MCM plus heparin-treated DC, and the expression of CD83 was increased when heparin and MCM used as a maturation factor.	Heparin	147-154	CD14 molecule	Homo sapiens	120-124
27110777-10	2016	These results strongly suggest that heparin promotes osteocyte-modulated osteoclastogenesis in vitro, at least partially, through inhibiting OPG activity.	Heparin	36-43	TNF receptor superfamily member 11b	Homo sapiens	141-144
21731773-0	2011	Mechanism of heparin acceleration of tissue inhibitor of metalloproteases-1 (TIMP-1) degradation by the human neutrophil elastase.	Heparin	13-20	elastase, neutrophil expressed	Homo sapiens	110-129
21346090-1	2011	Fibroblast growth factor 21 (FGF21) was originally identified as a member of the FGF family in homology studies and is a member of the endocrine FGF subfamily that lacks heparin binding domains and is released into the circulation.	Heparin	170-177	fibroblast growth factor 21	Mus musculus	0-27
21346090-1	2011	Fibroblast growth factor 21 (FGF21) was originally identified as a member of the FGF family in homology studies and is a member of the endocrine FGF subfamily that lacks heparin binding domains and is released into the circulation.	Heparin	170-177	fibroblast growth factor 21	Mus musculus	29-34
21731773-1	2011	Heparin has been shown to regulate human neutrophil elastase (HNE) activity.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	41-60
26852939-2	2016	We here demonstrate that binding of the chemokine-like inflammatory cytokine macrophage migration inhibitory factor (MIF) to epithelial lung and breast tumor cell lines A549 and MDA-MB231 is sensitive to enzymatic digestion of heparan sulphate chains and competitive inhibition with heparin.	Heparin	283-290	macrophage migration inhibitory factor	Homo sapiens	77-115
21731773-1	2011	Heparin has been shown to regulate human neutrophil elastase (HNE) activity.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	62-65
21731773-2	2011	We have assessed the regulatory effect of heparin on Tissue Inhibitor of Metalloproteases-1 [TIMP-1] hydrolysis by HNE employing the recombinant form of TIMP-1 and correlated FRET-peptides comprising the TIMP-1 cleavage site.	Heparin	42-49	elastase, neutrophil expressed	Homo sapiens	115-118
21731773-3	2011	Heparin accelerates 2.5-fold TIMP-1 hydrolysis by HNE.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	50-53
21731773-7	2011	The presence of heparin induces a dramatic effect in the pre-steady-state behavior of HNE.	Heparin	16-23	elastase, neutrophil expressed	Homo sapiens	86-89
21731773-8	2011	Heparin induces transient lag phase kinetics in HNE cleavage of the FRET-peptide substrate.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	48-51
21731773-12	2011	Heparin shifts the HNE pH activity profile to the right, allowing HNE to be active at alkaline pH.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	19-22
21731773-12	2011	Heparin shifts the HNE pH activity profile to the right, allowing HNE to be active at alkaline pH.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	66-69
21731773-13	2011	Molecular docking and kinetic analysis suggest that heparin induces conformational changes in HNE structure.	Heparin	52-59	elastase, neutrophil expressed	Homo sapiens	94-97
21140191-0	2011	Skin regeneration with fibroblast growth factor 2 released from heparin-conjugated fibrin.	Heparin	64-71	fibroblast growth factor 2	Mus musculus	23-49
26852939-2	2016	We here demonstrate that binding of the chemokine-like inflammatory cytokine macrophage migration inhibitory factor (MIF) to epithelial lung and breast tumor cell lines A549 and MDA-MB231 is sensitive to enzymatic digestion of heparan sulphate chains and competitive inhibition with heparin.	Heparin	283-290	macrophage migration inhibitory factor	Homo sapiens	117-120
21731773-14	2011	Here, we are showing for the first time that heparin is able to accelerate the hydrolysis of TIMP-1 by HNE.	Heparin	45-52	elastase, neutrophil expressed	Homo sapiens	103-106
26852939-3	2016	Moreover, MIF interaction with heparin was confirmed by chromatography and a structural comparison indicated a possible heparin binding site.	Heparin	31-38	macrophage migration inhibitory factor	Homo sapiens	10-13
26852939-3	2016	Moreover, MIF interaction with heparin was confirmed by chromatography and a structural comparison indicated a possible heparin binding site.	Heparin	120-127	macrophage migration inhibitory factor	Homo sapiens	10-13
20936359-2	2011	In ulcerative colitis patients, decreased Sdc1 expression was observed and Sdc1 analogue heparin could improve the disease course.	Heparin	89-96	syndecan 1	Homo sapiens	75-79
20936359-11	2011	Inhibited Sdc1 ectodomain shedding was detected in the heparin+DSS group compared to the DSS group.	Heparin	55-62	syndecan 1	Mus musculus	10-14
26852939-8	2016	These MIF-induced responses were abrogated by heparin or by silencing of syndecan-1.	Heparin	46-53	macrophage migration inhibitory factor	Homo sapiens	6-9
21162606-10	2010	The peak activity for the TFPI effect was earlier than the anti-Xa effect, at 1-2 h, and lasted for 6-12 h. Bemiparin thus has good antithrombotic activity and a better pharmacological profile than unfractionated heparin.	Heparin	213-220	tissue factor pathway inhibitor	Homo sapiens	26-30
27042064-0	2016	Sustained dual release of placental growth factor-2 and bone morphogenic protein-2 from heparin-based nanocomplexes for direct osteogenesis.	Heparin	88-95	bone morphogenetic protein 2	Homo sapiens	56-82
21480334-9	2011	Heparin did not directly interfere with FasL-induced apoptosis in isolated hepatocytes, and heparin-treated mice survived the FasL-induced liver injury longer compared with heparin-untreated animals.	Heparin	92-99	Fas ligand (TNF superfamily, member 6)	Mus musculus	126-130
21480334-12	2011	Heparin provides a potential therapeutic modality, because it not only prevents extensive FasL-related liver injury but also limits the extent of injury if given at early stages of injury exposure.	Heparin	0-7	Fas ligand (TNF superfamily, member 6)	Mus musculus	90-94
21220417-8	2011	Taken together, these results suggest that whereas protein Z, lipid, and calcium cofactors promote ZPI inhibition of membrane-associated factor Xa, heparin activates ZPI to inhibit free factor Xa as well as factor XIa and therefore may play a physiologically and pharmacologically important role in ZPI anticoagulant function.	Heparin	148-155	serpin family A member 10	Homo sapiens	166-169
21220417-8	2011	Taken together, these results suggest that whereas protein Z, lipid, and calcium cofactors promote ZPI inhibition of membrane-associated factor Xa, heparin activates ZPI to inhibit free factor Xa as well as factor XIa and therefore may play a physiologically and pharmacologically important role in ZPI anticoagulant function.	Heparin	148-155	serpin family A member 10	Homo sapiens	166-169
21329668-1	2011	Natural cytotoxicity receptor 1 (NCR1, NKp46) binds to heparin and heparan sulfate; however, other natural ligands for NKp46 have yet to be elucidated.	Heparin	55-62	natural cytotoxicity triggering receptor 1	Homo sapiens	0-31
21329668-1	2011	Natural cytotoxicity receptor 1 (NCR1, NKp46) binds to heparin and heparan sulfate; however, other natural ligands for NKp46 have yet to be elucidated.	Heparin	55-62	natural cytotoxicity triggering receptor 1	Homo sapiens	33-37
26930499-7	2016	All antibodies were found to bind with high affinity to two epitopes at the heparin binding site of A27, toward either the N- or C-terminal of the crucial KKEP-segment of A27.	Heparin	76-83	immunoglobulin kappa variable 3-20	Homo sapiens	100-103
21329668-1	2011	Natural cytotoxicity receptor 1 (NCR1, NKp46) binds to heparin and heparan sulfate; however, other natural ligands for NKp46 have yet to be elucidated.	Heparin	55-62	natural cytotoxicity triggering receptor 1	Homo sapiens	39-44
21329668-3	2011	NKp46-H6 directly bound to plates coated with heparin- and heparan sulfate-conjugated bovine serum albumin with K(d) values of 770 and 850 nM, respectively.	Heparin	46-53	natural cytotoxicity triggering receptor 1	Homo sapiens	0-5
21329668-4	2011	The binding of NKp46-H6 to heparin-BSA was suppressed by soluble heparin, herparan sulfate, fucoidan, lambda-carrageenan, and dextran sulfate, but not by 2-O-, 6-O-, and N-desulfated heparin.	Heparin	27-34	natural cytotoxicity triggering receptor 1	Homo sapiens	15-20
21329668-4	2011	The binding of NKp46-H6 to heparin-BSA was suppressed by soluble heparin, herparan sulfate, fucoidan, lambda-carrageenan, and dextran sulfate, but not by 2-O-, 6-O-, and N-desulfated heparin.	Heparin	65-72	natural cytotoxicity triggering receptor 1	Homo sapiens	15-20
26930499-7	2016	All antibodies were found to bind with high affinity to two epitopes at the heparin binding site of A27, toward either the N- or C-terminal of the crucial KKEP-segment of A27.	Heparin	76-83	immunoglobulin kappa variable 3-20	Homo sapiens	171-174
21257720-0	2011	SST0001, a chemically modified heparin, inhibits myeloma growth and angiogenesis via disruption of the heparanase/syndecan-1 axis.	Heparin	31-38	syndecan 1	Homo sapiens	114-124
26607136-12	2016	Direct FXa inhibition by TFPI is modulated by physiological concentrations prothrombin, FV, FVa, protein S, phospholipids and heparin indicating the importance of these modulators for the in vivo anticoagulant activity of TFPI.	Heparin	126-133	tissue factor pathway inhibitor	Homo sapiens	25-29
26581031-10	2016	In diluted prothrombin and activated factor X (FXa)-induced clotting assays, TPP2009 dose-dependently reduced the anticoagulant effect of heparin in non-hemophilic and FVIII-deficient human plasma, with half-maximal effective concentrations (EC50 ) of 10.5 nm and 4.7 nm, respectively.	Heparin	138-145	coagulation factor VIII	Homo sapiens	168-173
21349432-6	2011	Ablation of factor XII or kinin B2 receptors abolished heparin-induced skin edema and protected mice from allergen-activated mast cell-driven leakage.	Heparin	55-62	coagulation factor XII (Hageman factor)	Mus musculus	12-22
21349432-6	2011	Ablation of factor XII or kinin B2 receptors abolished heparin-induced skin edema and protected mice from allergen-activated mast cell-driven leakage.	Heparin	55-62	bradykinin receptor, beta 2	Mus musculus	26-34
21349432-7	2011	In contrast, heparin and activated mast cells induced excessive edema in mice deficient in the major inhibitor of factor XII, C1 esterase inhibitor.	Heparin	13-20	coagulation factor XII (Hageman factor)	Mus musculus	114-124
26553567-3	2016	Heparin followed by gelatin affinity chromatography was used for purification of BSP1 from bovine seminal vesicle fluid.	Heparin	0-7	seminal plasma protein PDC-109	Bos taurus	81-85
26553567-10	2016	Embryo development was higher (P &lt; 0.05) after treatment with 20 mug/mL BSP1 (35.6 +- 2.5%) and 40 mug/mL (41.1 +- 2%) than after incubations with heparin (24.7 +- 3.2%) or without heparin (27.3 +- 1.6%).	Heparin	150-157	seminal plasma protein PDC-109	Bos taurus	75-79
21142149-3	2011	In the present work, light scattering, fluorescence, circular dichroism, and nuclear magnetic resonance (NMR) spectroscopy were used to describe the chemical and physical properties of the murine recombinant PrP 23-231 interaction with low molecular weight heparin (LMWHep) at pH 7.4 and 5.5.	Heparin	257-264	prion protein	Mus musculus	208-211
26553567-10	2016	Embryo development was higher (P &lt; 0.05) after treatment with 20 mug/mL BSP1 (35.6 +- 2.5%) and 40 mug/mL (41.1 +- 2%) than after incubations with heparin (24.7 +- 3.2%) or without heparin (27.3 +- 1.6%).	Heparin	184-191	seminal plasma protein PDC-109	Bos taurus	75-79
27576282-2	2016	Heparin-induced thrombocytopenia (HIT) is an immune-mediated adverse reaction due to antibodies to a multimolecular complex of heparin and platelet factor 4 (PF4) characterized by moderate thrombocytopenia and paradoxical arterial or venous thrombosis.	Heparin	0-7	platelet factor 4	Homo sapiens	158-161
21212510-0	2011	Binding affinities of NKG2D and CD94 to sialyl Lewis X-expressing N-glycans and heparin.	Heparin	80-87	killer cell lectin like receptor K1	Homo sapiens	22-27
21212510-1	2011	Lectin-like receptors natural killer group 2D (NKG2D) and CD94 on natural killer (NK) cells bind to alpha2,3-NeuAc-containing N-glycans and heparin/heparan sulfate (HS).	Heparin	140-147	killer cell lectin like receptor K1	Homo sapiens	47-52
26306634-6	2015	In cell-based assays, heparin, 2-O-, 6-O- and N-desulfated re-N-acetylated heparin and oligosaccharides 14-24 saccharides (dp14-24) in length all increased the phosphorylation of mothers against decapentaplegic homolog 2 (SMAD2) after 6 h of stimulation with TGF-beta1.	Heparin	22-29	SMAD family member 2	Homo sapiens	179-220
26306634-6	2015	In cell-based assays, heparin, 2-O-, 6-O- and N-desulfated re-N-acetylated heparin and oligosaccharides 14-24 saccharides (dp14-24) in length all increased the phosphorylation of mothers against decapentaplegic homolog 2 (SMAD2) after 6 h of stimulation with TGF-beta1.	Heparin	22-29	SMAD family member 2	Homo sapiens	222-227
21239863-1	2011	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction caused by antibodies to the heparin/platelet factor 4 (PF4) complex, resulting in thrombocytopenia and prothrombotic state.	Heparin	12-19	platelet factor 4	Homo sapiens	107-132
21239863-1	2011	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is an adverse drug reaction caused by antibodies to the heparin/platelet factor 4 (PF4) complex, resulting in thrombocytopenia and prothrombotic state.	Heparin	12-19	platelet factor 4	Homo sapiens	134-137
26306634-6	2015	In cell-based assays, heparin, 2-O-, 6-O- and N-desulfated re-N-acetylated heparin and oligosaccharides 14-24 saccharides (dp14-24) in length all increased the phosphorylation of mothers against decapentaplegic homolog 2 (SMAD2) after 6 h of stimulation with TGF-beta1.	Heparin	75-82	SMAD family member 2	Homo sapiens	179-220
20674748-6	2011	The 15 kDa granulysin is purified using a HiTrap Heparin column and a Resource S column.	Heparin	49-56	granulysin	Homo sapiens	11-21
21048103-6	2010	GRP94.NTD surface binding was markedly suppressed after treatment of MEF cell lines with heparin, sodium chlorate, or heparinase II, demonstrating that heparin sulfate proteoglycans can function in GRP94.NTD surface binding.	Heparin	89-96	heat shock protein 90, beta (Grp94), member 1	Mus musculus	0-5
21048103-6	2010	GRP94.NTD surface binding was markedly suppressed after treatment of MEF cell lines with heparin, sodium chlorate, or heparinase II, demonstrating that heparin sulfate proteoglycans can function in GRP94.NTD surface binding.	Heparin	89-96	heat shock protein 90, beta (Grp94), member 1	Mus musculus	198-203
26306634-6	2015	In cell-based assays, heparin, 2-O-, 6-O- and N-desulfated re-N-acetylated heparin and oligosaccharides 14-24 saccharides (dp14-24) in length all increased the phosphorylation of mothers against decapentaplegic homolog 2 (SMAD2) after 6 h of stimulation with TGF-beta1.	Heparin	75-82	SMAD family member 2	Homo sapiens	222-227
26640392-2	2015	There is mounting evidence supporting a positive correlation between definitive heparin-induced thrombocytopenia and optical density (OD) positivity from the widely available anti-platelet factor 4 enzyme-linked immunosorbent assays (PF4 ELISAs).	Heparin	80-87	platelet factor 4	Homo sapiens	234-237
20959660-1	2010	Platelet factor 4 (PF4)/heparin antibody, typically associated with heparin therapy, is reported in some heparin-naive people.	Heparin	24-31	platelet factor 4	Homo sapiens	0-17
20959660-1	2010	Platelet factor 4 (PF4)/heparin antibody, typically associated with heparin therapy, is reported in some heparin-naive people.	Heparin	68-75	platelet factor 4	Homo sapiens	0-17
20959660-1	2010	Platelet factor 4 (PF4)/heparin antibody, typically associated with heparin therapy, is reported in some heparin-naive people.	Heparin	68-75	platelet factor 4	Homo sapiens	19-22
26497525-6	2015	Finally, we present some new data investigating whether levels of the extracellular ligand-binding region of platelet glycoprotein VI which is rapidly shed upon engagement of platelet FcgammaRIIa by autoantibodies, can report on the presence of pathological anti-heparin/platelet factor 4 immune complexes and thus identify patients with pathological autoantibodies who are at the greatest risk of developing life-threatening thrombosis in the setting of heparin-induced thrombocytopenia.	Heparin	263-270	Fc gamma receptor IIa	Homo sapiens	184-195
20725964-0	2010	Beneficial effects of granulocyte-colony stimulating factor on small-diameter heparin immobilized decellularized vascular graft.	Heparin	78-85	colony stimulating factor 3	Rattus norvegicus	22-59
26177601-11	2015	UFH+-GPI significantly increased the odds of MI vs LMWHs, of ST vs UFH+GPI, and of MB vs bivalirudin.	Heparin	0-3	glucose-6-phosphate isomerase	Homo sapiens	5-8
20679343-9	2010	Because the regular incorporation of negative charges by GSK3beta leads to a potential parallel between phospho-Tau and heparin, we investigated its interaction with the heparin/low density lipoprotein receptor binding domain of human apolipoprotein E.	Heparin	120-127	glycogen synthase kinase 3 alpha	Homo sapiens	57-65
20679343-9	2010	Because the regular incorporation of negative charges by GSK3beta leads to a potential parallel between phospho-Tau and heparin, we investigated its interaction with the heparin/low density lipoprotein receptor binding domain of human apolipoprotein E.	Heparin	170-177	glycogen synthase kinase 3 alpha	Homo sapiens	57-65
20823601-2	2010	Heparin/heparan sulfate (HS) is required for FGF2 signaling but heparin mimics either promotes or inhibits FGF2 signaling.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	45-49
26177601-11	2015	UFH+-GPI significantly increased the odds of MI vs LMWHs, of ST vs UFH+GPI, and of MB vs bivalirudin.	Heparin	0-3	glucose-6-phosphate isomerase	Homo sapiens	67-74
20823601-2	2010	Heparin/heparan sulfate (HS) is required for FGF2 signaling but heparin mimics either promotes or inhibits FGF2 signaling.	Heparin	64-71	fibroblast growth factor 2	Mus musculus	107-111
20823601-3	2010	To take advantage such properties of heparin mimics, a series of N-heteroaroyl aminosaccharide derivatives were designed and synthesized as FGF2 signaling modulators.	Heparin	37-44	fibroblast growth factor 2	Mus musculus	140-144
26522454-8	2015	The latter function is modulated by two distinct heparin-binding domains of IGFBP-2 which are lacking in IGFBP-1.	Heparin	49-56	insulin like growth factor binding protein 2	Homo sapiens	76-83
20696992-7	2010	Finally, preincubation of monocytes with soluble heparin abrogated Ang-1 binding to monocytes and migration, and partially prevented Ang-1 binding to human umbilical endothelial cells.	Heparin	49-56	angiopoietin 1	Homo sapiens	67-72
26160844-0	2015	Chemically modified, non-anticoagulant heparin derivatives are potent galectin-3 binding inhibitors and inhibit circulating galectin-3-promoted metastasis.	Heparin	39-46	galectin 3	Homo sapiens	70-80
20696992-7	2010	Finally, preincubation of monocytes with soluble heparin abrogated Ang-1 binding to monocytes and migration, and partially prevented Ang-1 binding to human umbilical endothelial cells.	Heparin	49-56	angiopoietin 1	Homo sapiens	133-138
26160844-0	2015	Chemically modified, non-anticoagulant heparin derivatives are potent galectin-3 binding inhibitors and inhibit circulating galectin-3-promoted metastasis.	Heparin	39-46	galectin 3	Homo sapiens	124-134
26160844-2	2015	Here we show that 2- or 6-de-O-sulfated, N-acetylated heparin derivatives are galectin-3 binding inhibitors.	Heparin	54-61	galectin 3	Homo sapiens	78-88
26160844-3	2015	These chemically modified heparin derivatives inhibited galectin-3-ligand binding and abolished galectin-3-mediated cancer cell-endothelial adhesion and angiogenesis.	Heparin	26-33	galectin 3	Homo sapiens	56-66
26160844-3	2015	These chemically modified heparin derivatives inhibited galectin-3-ligand binding and abolished galectin-3-mediated cancer cell-endothelial adhesion and angiogenesis.	Heparin	26-33	galectin 3	Homo sapiens	96-106
26160844-5	2015	Intravenous injection of such heparin derivatives (with cancer cells pre-treated with galectin-3 followed by 3 subcutaneous injections of the derivatives) abolished the circulating galectin-3-mediated increase in lung metastasis of human melanoma and colon cancer cells in nude mice.	Heparin	30-37	galectin 3	Homo sapiens	86-96
26045608-8	2015	In particular, blockage of thrombin exosites with compounds specific for exosite I (hirudin and HD1 aptamer) or exosite II (heparin and HD22 aptamer) impaired the COMP-thrombin interaction, indicating a 2-site binding mechanism.	Heparin	124-131	cartilage oligomeric matrix protein	Mus musculus	163-167
25667200-6	2015	Downregulation of the messenger RNA of trophoblast EPCR occurred when trophoblasts were challenged with tumor necrosis factor alpha, and it could be prevented by unfractionated heparin but not by low-molecular-weight heparin at therapeutic doses.	Heparin	177-184	protein C receptor	Homo sapiens	51-55
20626620-0	2010	Heparin-induced thrombocytopenia: towards standardization of platelet factor 4/heparin antigen tests.	Heparin	0-7	platelet factor 4	Homo sapiens	61-78
20626620-4	2010	PATIENTS/METHODS: Using quantile regression we determined the 97.5th percentile of PF4/heparin-immunoglobulin G (IgG) EIA reactivities in non-heparin-treated individuals [blood donors (n = 935)] and patients before heparin therapy (n = 1207).	Heparin	87-94	platelet factor 4	Homo sapiens	83-86
20626620-4	2010	PATIENTS/METHODS: Using quantile regression we determined the 97.5th percentile of PF4/heparin-immunoglobulin G (IgG) EIA reactivities in non-heparin-treated individuals [blood donors (n = 935)] and patients before heparin therapy (n = 1207).	Heparin	142-149	platelet factor 4	Homo sapiens	83-86
20547765-4	2010	Our study now shows that the osteogenic activity of Wnt3a is cooperatively stimulated through physical interactions with exogenous heparin.	Heparin	131-138	Wnt family member 3A	Homo sapiens	52-57
20547765-5	2010	N-Sulfation and to a lesser extent O-sulfation of heparin contribute to the physical binding and optimal co-stimulation of Wnt3a.	Heparin	50-57	Wnt family member 3A	Homo sapiens	123-128
20547765-6	2010	Wnt3a-heparin signaling synergistically increases osteoblast differentiation with minimal effects on cell proliferation.	Heparin	6-13	Wnt family member 3A	Homo sapiens	0-5
20547765-7	2010	Thus, heparin selectively reduces the effective dose of Wnt3a needed to elicit osteogenic, but not mitogenic responses.	Heparin	6-13	Wnt family member 3A	Homo sapiens	56-61
20691844-1	2010	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is caused by anti-platelet factor 4/heparin (PF4/H) immunoglobulin (Ig) G antibodies, which activate platelets.	Heparin	12-19	platelet factor 4	Homo sapiens	96-101
26041143-0	2015	Heparin-conjugated alginate multilayered microspheres for controlled release of bFGF.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	80-84
20552727-7	2010	Delivery of FGF2 and VEGF in conjunction with the HBPA/heparin nanofibers also induced a significant amount of islet endothelial cell sprouting from the islets into a peptide amphiphile 3-D matrix.	Heparin	55-62	fibroblast growth factor 2	Mus musculus	12-16
26041143-1	2015	In order to effectively immobilize and control release of basic fibroblast growth factor (bFGF) from alginate microspheres, heparin-conjugated alginate (H-Alg) was first synthesized by covalent binding.	Heparin	124-131	fibroblast growth factor 2	Mus musculus	58-88
26041143-1	2015	In order to effectively immobilize and control release of basic fibroblast growth factor (bFGF) from alginate microspheres, heparin-conjugated alginate (H-Alg) was first synthesized by covalent binding.	Heparin	124-131	fibroblast growth factor 2	Mus musculus	90-94
19627396-6	2010	Accordingly, the peptide hampers the binding of FGF2 to Chinese Hamster ovary cells overexpressing the tyrosine-kinase FGF receptor-1 (FGFR1) and to recombinant FGFR1 immobilized to a BIAcore sensorchip without affecting heparin interaction.	Heparin	221-228	fibroblast growth factor 2	Cricetulus griseus	48-52
25765490-5	2015	Treatment with the IP3R antagonist heparin prevented mechanical allodynia with no effect on thermal response.	Heparin	35-42	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	19-23
20432446-0	2010	Low-concentration heparin suppresses ionomycin-activated CAMK-II/EGF receptor- and ERK-mediated signaling in mesangial cells.	Heparin	18-25	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	57-64
24663337-7	2015	CXCL4-induced up-regulation of both MMP7 and S100A8 was curbed in the presence of heparin, which binds to CXCL4 and glycosaminoglycans, most likely representing the macrophage receptor for CXCL4.	Heparin	82-89	platelet factor 4	Homo sapiens	0-5
20596760-11	2010	Furthermore, heparin was incorporated in order to accomplish sustained delivery of a growth factor of interest namely, bone morphogenetic proteins (BMP-2).	Heparin	13-20	bone morphogenetic protein 2	Homo sapiens	148-153
24663337-7	2015	CXCL4-induced up-regulation of both MMP7 and S100A8 was curbed in the presence of heparin, which binds to CXCL4 and glycosaminoglycans, most likely representing the macrophage receptor for CXCL4.	Heparin	82-89	S100 calcium binding protein A8	Homo sapiens	45-51
24663337-7	2015	CXCL4-induced up-regulation of both MMP7 and S100A8 was curbed in the presence of heparin, which binds to CXCL4 and glycosaminoglycans, most likely representing the macrophage receptor for CXCL4.	Heparin	82-89	platelet factor 4	Homo sapiens	106-111
24663337-7	2015	CXCL4-induced up-regulation of both MMP7 and S100A8 was curbed in the presence of heparin, which binds to CXCL4 and glycosaminoglycans, most likely representing the macrophage receptor for CXCL4.	Heparin	82-89	platelet factor 4	Homo sapiens	106-111
25604035-3	2015	The unpredictable occurrence and the mechanism of this atypical immune response to PF4:heparin complexes are poorly understood.	Heparin	87-94	platelet factor 4	Homo sapiens	83-86
19911252-1	2010	Heparin-platelet factor 4 (PF4) antibodies mediate heparin-induced thrombocytopenia (HIT) and, irrespective of thrombocytopenia, are associated with poorer outcomes in some patients.	Heparin	51-58	platelet factor 4	Homo sapiens	0-25
19911252-1	2010	Heparin-platelet factor 4 (PF4) antibodies mediate heparin-induced thrombocytopenia (HIT) and, irrespective of thrombocytopenia, are associated with poorer outcomes in some patients.	Heparin	51-58	platelet factor 4	Homo sapiens	27-30
25604035-7	2015	RESULTS: PF4:heparin complexes caused release of the biomarker interleukin 8 in whole blood, and the level of response varied with the stoichiometric ratio of PF4 to heparin.	Heparin	13-20	platelet factor 4	Homo sapiens	9-12
25604035-7	2015	RESULTS: PF4:heparin complexes caused release of the biomarker interleukin 8 in whole blood, and the level of response varied with the stoichiometric ratio of PF4 to heparin.	Heparin	13-20	platelet factor 4	Homo sapiens	159-162
25604035-7	2015	RESULTS: PF4:heparin complexes caused release of the biomarker interleukin 8 in whole blood, and the level of response varied with the stoichiometric ratio of PF4 to heparin.	Heparin	166-173	platelet factor 4	Homo sapiens	9-12
25562836-8	2015	Heparin reduced lethality in mice exposed to LPS+HMGB1.	Heparin	0-7	high mobility group box 1	Mus musculus	49-54
20398703-4	2010	Surface plasmon resonance (SPR) experiments revealed that BSA-Tat-NLS binds to the HSPG analogue heparin.	Heparin	97-104	tyrosine aminotransferase	Homo sapiens	58-69
25562836-9	2015	To conclude, heparin inhibited LPS-induced HMGB1-amplified inflammatory responses by blocking HMGB1 binding to macrophage surfaces.	Heparin	13-20	high mobility group box 1	Mus musculus	43-48
25562836-9	2015	To conclude, heparin inhibited LPS-induced HMGB1-amplified inflammatory responses by blocking HMGB1 binding to macrophage surfaces.	Heparin	13-20	high mobility group box 1	Mus musculus	94-99
25562836-10	2015	Heparin could be used therapeutically as an effective inhibitor of HMGB1-associated inflammation.	Heparin	0-7	high mobility group box 1	Mus musculus	67-72
25324455-1	2015	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is caused by platelet activating antibodies that recognize platelet factor 4/heparin (PF4/H) complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	137-142
19853891-10	2010	CONCLUSION: A positive family history of VTE, carriership of the prothrombin mutation and elevated FVIII or Hcy levels were significantly associated with failure to prevent VTE by heparin therapy following ATSCI.	Heparin	180-187	coagulation factor VIII	Homo sapiens	99-104
20335795-3	2010	It is well known that the cationic portion of HMGB1 binds to heparin, which has abundant sulfates in its structure.	Heparin	61-68	high mobility group box 1	Homo sapiens	46-51
25404732-3	2015	Translocation of shed syndecan-1 (sSDC1) to the nucleus was blocked by addition of exogenous heparin or heparan sulfate, pretreatment of conditioned medium with heparinase III, or growth of cells in sodium chlorate, indicating that sulfated heparan sulfate chains are required for nuclear translocation.	Heparin	93-100	syndecan 1	Homo sapiens	22-32
20053992-1	2010	Inactivation of thrombin (T) by the serpins heparin cofactor II (HCII) and antithrombin (AT) is accelerated by a heparin template between the serpin and thrombin exosite II.	Heparin	44-51	serpin family D member 1	Homo sapiens	65-69
19959490-8	2010	Topical administration of both the MPS and heparin ointments resulted in no measurable anticoagulant effects in the primate model; however, MPS produced a concentration-dependent release of TFPI antigen and a functional activity that was stronger than the effects observed with heparin.	Heparin	278-285	tissue factor pathway inhibitor	Homo sapiens	190-194
20039931-7	2010	CD40 ligand expression on platelets was significantly reduced following PCI with HD-tirofiban and either UFH or enoxaparin.	Heparin	105-108	CD40 molecule	Homo sapiens	0-4
20880110-2	2010	This study explores the UFH-dependent tissue factor pathway inhibitor (TFPI) release in children compared to previously published data in adults.	Heparin	24-27	tissue factor pathway inhibitor	Homo sapiens	71-75
20880110-5	2010	This study demonstrated that, whilst the immediate release of TFPI post-UFH was similar in children compared to adults, TFPI release in children remained increased and consistent for a significantly longer period post-UFH administration compared to adults.	Heparin	72-75	tissue factor pathway inhibitor	Homo sapiens	62-66
20880110-7	2010	The prolonged TFPI-mediated anticoagulant levels observed in children administered UFH may contribute to the increased rate of major bleeding reported in children compared to adults.	Heparin	83-86	tissue factor pathway inhibitor	Homo sapiens	14-18
20880110-8	2010	Furthermore, we postulate that this sustained UFH-dependent increase in TFPI levels in children may influence the binding of UFH to competitive plasma proteins, such as those involved in the immunological response to UFH associated with heparin-induced thrombocytopenia.	Heparin	46-49	tissue factor pathway inhibitor	Homo sapiens	72-76
20880110-8	2010	Furthermore, we postulate that this sustained UFH-dependent increase in TFPI levels in children may influence the binding of UFH to competitive plasma proteins, such as those involved in the immunological response to UFH associated with heparin-induced thrombocytopenia.	Heparin	125-128	tissue factor pathway inhibitor	Homo sapiens	72-76
20880110-8	2010	Furthermore, we postulate that this sustained UFH-dependent increase in TFPI levels in children may influence the binding of UFH to competitive plasma proteins, such as those involved in the immunological response to UFH associated with heparin-induced thrombocytopenia.	Heparin	125-128	tissue factor pathway inhibitor	Homo sapiens	72-76
20880110-8	2010	Furthermore, we postulate that this sustained UFH-dependent increase in TFPI levels in children may influence the binding of UFH to competitive plasma proteins, such as those involved in the immunological response to UFH associated with heparin-induced thrombocytopenia.	Heparin	237-244	tissue factor pathway inhibitor	Homo sapiens	72-76
26328426-0	2015	Preparation of Low Molecular Weight Heparin by Microwave Discharge Electrodeless Lamp/TiO2 Photo-Catalytic Reaction.	Heparin	36-43	lysosomal associated membrane protein 3	Homo sapiens	81-85
21068538-1	2010	BACKGROUND: The addition of glycoprotein IIb/IIIa inhibitors (GPIs) to heparin in percutaneous coronary intervention (PCI) procedures has been demonstrated to reduce ischemic complications; however, GPI use is known to increase the risk of bleeding events, which are linked to increased mortality, longer hospital length of stay, greater medical resource utilization, and increased costs.	Heparin	71-78	glucose-6-phosphate isomerase	Homo sapiens	62-65
19733222-6	2010	Through its heparin binding domain, OPG is also able to bind proteoglycans present in the bone matrix.	Heparin	12-19	TNF receptor superfamily member 11b	Homo sapiens	36-39
32262010-6	2014	The existence of heparin made the nanogel achieve a high loading efficiency of BMP-2, and the vectoring delivery of BMP-2 could be easily controlled by the external magnetic field.	Heparin	17-24	bone morphogenetic protein 2	Homo sapiens	79-84
20482984-0	2010	Heparin-binding-affinity-based delivery systems releasing nerve growth factor enhance sciatic nerve regeneration.	Heparin	0-7	nerve growth factor	Rattus norvegicus	58-77
20638238-7	2010	Of note PF4/heparin complexes are also immunogenic triggering the production of anti-PF4/heparin antibodies which activate also platelets (the so-called "heparin-induced thrombocytopenia and thrombosis syndrome", HITT).	Heparin	12-19	platelet factor 4	Homo sapiens	8-11
32262010-6	2014	The existence of heparin made the nanogel achieve a high loading efficiency of BMP-2, and the vectoring delivery of BMP-2 could be easily controlled by the external magnetic field.	Heparin	17-24	bone morphogenetic protein 2	Homo sapiens	116-121
20638238-7	2010	Of note PF4/heparin complexes are also immunogenic triggering the production of anti-PF4/heparin antibodies which activate also platelets (the so-called "heparin-induced thrombocytopenia and thrombosis syndrome", HITT).	Heparin	12-19	platelet factor 4	Homo sapiens	85-88
20638238-7	2010	Of note PF4/heparin complexes are also immunogenic triggering the production of anti-PF4/heparin antibodies which activate also platelets (the so-called "heparin-induced thrombocytopenia and thrombosis syndrome", HITT).	Heparin	89-96	platelet factor 4	Homo sapiens	8-11
19897001-8	2010	Site-directed mutagenesis within the heparin-binding domain (HBD) of NGF abolished ATP-binding and the neuroprotective effect.	Heparin	37-44	nerve growth factor	Rattus norvegicus	69-72
32262010-7	2014	In vitro cytotoxicity tests demonstrated that incorporation of BMP-2 into this biopolymer nanogel through binding with heparin showed high efficiency to promote MG-63 cells" viabilities, in particular under a magnetic field, which suggested a promising future for cartilage and bone regeneration applications.	Heparin	119-126	bone morphogenetic protein 2	Homo sapiens	63-68
25150299-3	2014	Understanding why the endogenous protein PF4 becomes immunogenic when complexing with heparin is important for the development of other negatively charged drugs and may also hint toward more general mechanisms underlying the induction of autoantibodies to other proteins.	Heparin	86-93	platelet factor 4	Homo sapiens	41-44
19329263-10	2009	The effect of heparin on capacitation dependent protein tyrosine phosphorylation was also analyzed, finding a decrease in p32 phosphorylation in the presence of heparin.	Heparin	14-21	complement C1q binding protein	Homo sapiens	122-125
19329263-10	2009	The effect of heparin on capacitation dependent protein tyrosine phosphorylation was also analyzed, finding a decrease in p32 phosphorylation in the presence of heparin.	Heparin	161-168	complement C1q binding protein	Homo sapiens	122-125
20688114-2	2010	The physical properties of self-assembled heparin-Pluronic (HP) nanogels incorporating RNase A (HPR nanogels) were characterized by dynamic light scattering (DLS), xi-potential, and transmission electron microscopy (TEM).	Heparin	42-49	haptoglobin-related protein	Homo sapiens	96-99
25150299-4	2014	By circular dichroism spectroscopy, atomic force microscopy, and isothermal titration calorimetry we characterized the interaction of PF4 with unfractionated heparin (UFH), its 16-, 8-, and 6-mer subfractions, low-molecular-weight heparin (LMWH), and the pentasaccharide fondaparinux.	Heparin	158-165	platelet factor 4	Homo sapiens	134-137
25150299-4	2014	By circular dichroism spectroscopy, atomic force microscopy, and isothermal titration calorimetry we characterized the interaction of PF4 with unfractionated heparin (UFH), its 16-, 8-, and 6-mer subfractions, low-molecular-weight heparin (LMWH), and the pentasaccharide fondaparinux.	Heparin	167-170	platelet factor 4	Homo sapiens	134-137
20504805-5	2010	The surface-modification improved the wettability of scaffolds and provided specific binding site between conjugated heparin and the growth factor recombinant human bone morphogenetic protein-2 (rhBMP-2).	Heparin	117-124	bone morphogenetic protein 2	Homo sapiens	165-193
25150299-4	2014	By circular dichroism spectroscopy, atomic force microscopy, and isothermal titration calorimetry we characterized the interaction of PF4 with unfractionated heparin (UFH), its 16-, 8-, and 6-mer subfractions, low-molecular-weight heparin (LMWH), and the pentasaccharide fondaparinux.	Heparin	231-238	platelet factor 4	Homo sapiens	134-137
20621352-2	2010	Receptor-mediated osteoblastic differentiation by bone morphogenetic protein (BMP)-4 and supportive function of its heparin binding has been proposed, direct role of the heparin binding site of BMP-4 on osteogenesis has not yet been fully investigated.	Heparin	170-177	bone morphogenetic protein 4	Homo sapiens	194-199
20621352-4	2010	Herein, we synthesized a peptide sequence corresponding to residues 15-24 of BMP-4 (HBD, RKKNPNCRRH), as potential heparin binding sequence.	Heparin	115-122	bone morphogenetic protein 4	Homo sapiens	77-82
18985789-2	2009	The transforming growth factor beta (TGF beta) proteins, which have been shown to bind to heparin, have been well established to induce chondrogenic differentiation in chondrocytes.	Heparin	90-97	transforming growth factor, beta 1	Mus musculus	37-45
18985789-3	2009	In this study, we assessed the effects of heparin on the TGF beta-3 activities in rabbit chondrocytes embedded in thermoreversible hydrogel.	Heparin	42-49	transforming growth factor, beta 1	Mus musculus	57-65
18985789-10	2009	These data indicate the potential use of heparin-binding TGF beta-3 for the reconstruction of neocartilage formation.	Heparin	41-48	transforming growth factor, beta 1	Mus musculus	57-65
25117899-0	2014	NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding.	Heparin	100-107	heparin binding growth factor	Homo sapiens	79-83
25117899-4	2014	We used the H2CN NMR pulse sequence to detect heparin binding through the side-chain resonances Hepsilon-Cepsilon-Nzeta of Lys and Hdelta-Cdelta-Nepsilon of Arg in the two proteins of hepatoma-derived growth factor (HDGF) and basic fibroblast growth factor (FGF2).	Heparin	46-53	heparin binding growth factor	Homo sapiens	184-214
21083474-2	2010	Heparin-induced thrombocytopenia (HIT) is an antibody-mediated prothrombotic disorder triggered by PF4-binding polyanions, usually heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	99-102
21083474-2	2010	Heparin-induced thrombocytopenia (HIT) is an antibody-mediated prothrombotic disorder triggered by PF4-binding polyanions, usually heparin.	Heparin	131-138	platelet factor 4	Homo sapiens	99-102
20079161-13	2009	The lung tissue levels of phospho-ERK1/2 and phospho-P38 MAPK expressions were markedly higher in the ALI group than in the normal control group, AT-III treatment group and heparin treatment group respectively.	Heparin	173-180	mitogen activated protein kinase 3	Rattus norvegicus	34-40
25117899-4	2014	We used the H2CN NMR pulse sequence to detect heparin binding through the side-chain resonances Hepsilon-Cepsilon-Nzeta of Lys and Hdelta-Cdelta-Nepsilon of Arg in the two proteins of hepatoma-derived growth factor (HDGF) and basic fibroblast growth factor (FGF2).	Heparin	46-53	heparin binding growth factor	Homo sapiens	216-220
20079161-13	2009	The lung tissue levels of phospho-ERK1/2 and phospho-P38 MAPK expressions were markedly higher in the ALI group than in the normal control group, AT-III treatment group and heparin treatment group respectively.	Heparin	173-180	mitogen activated protein kinase 14	Rattus norvegicus	53-56
20079161-13	2009	The lung tissue levels of phospho-ERK1/2 and phospho-P38 MAPK expressions were markedly higher in the ALI group than in the normal control group, AT-III treatment group and heparin treatment group respectively.	Heparin	173-180	mitogen activated protein kinase 3	Rattus norvegicus	57-61
24934306-0	2014	Optimal condition of heparin-conjugated fibrin with bone morphogenetic protein-2 for spinal fusion in a rabbit model.	Heparin	21-28	bone morphogenetic protein 2	Oryctolagus cuniculus	52-80
20137277-13	2009	The lung tissue levels of phospho-ERK1/2 and phospho-P38 MAPK expressions of heparin treatment group were markedly higher than those of normal control group, whereas markedly lower than those of ALI group.	Heparin	77-84	mitogen activated protein kinase 3	Rattus norvegicus	57-61
19893601-5	2009	The heparin-dependent induction of angiogenesis by HMGB1 was accompanied by increases in the expression of tumor necrosis factor-alpha (TNF-alpha) and vascular endothelial growth factor-A120 (VEGF-A120).	Heparin	4-11	high mobility group box 1	Mus musculus	51-56
19893601-6	2009	It is likely that the dependence of the angiogenic activity of HMGB1 on heparin was due to the efficiency of the diffusion of the HMGB1-heparin complex from matrigel to the surrounding areas.	Heparin	72-79	high mobility group box 1	Mus musculus	63-68
19893601-6	2009	It is likely that the dependence of the angiogenic activity of HMGB1 on heparin was due to the efficiency of the diffusion of the HMGB1-heparin complex from matrigel to the surrounding areas.	Heparin	72-79	high mobility group box 1	Mus musculus	130-135
21063505-4	2010	In a recent paper, data are provided that CCN5 (wisp2), which lacks the carboxy-terminal heparin-binding domain shared by the other CCN proteins, may act as a dominant-negative protein to suppress CCN2-mediated fibrogenesis.	Heparin	89-96	cellular communication network factor 5	Homo sapiens	42-46
21063505-4	2010	In a recent paper, data are provided that CCN5 (wisp2), which lacks the carboxy-terminal heparin-binding domain shared by the other CCN proteins, may act as a dominant-negative protein to suppress CCN2-mediated fibrogenesis.	Heparin	89-96	cellular communication network factor 5	Homo sapiens	48-53
21063505-4	2010	In a recent paper, data are provided that CCN5 (wisp2), which lacks the carboxy-terminal heparin-binding domain shared by the other CCN proteins, may act as a dominant-negative protein to suppress CCN2-mediated fibrogenesis.	Heparin	89-96	cellular communication network factor 2	Homo sapiens	197-201
19893601-6	2009	It is likely that the dependence of the angiogenic activity of HMGB1 on heparin was due to the efficiency of the diffusion of the HMGB1-heparin complex from matrigel to the surrounding areas.	Heparin	136-143	high mobility group box 1	Mus musculus	63-68
19893601-6	2009	It is likely that the dependence of the angiogenic activity of HMGB1 on heparin was due to the efficiency of the diffusion of the HMGB1-heparin complex from matrigel to the surrounding areas.	Heparin	136-143	high mobility group box 1	Mus musculus	130-135
25062563-0	2014	Heparin attenuates HMGB1 expression in arterial tissue subjected to limb ischemia/reperfusion.	Heparin	0-7	high mobility group box 1	Homo sapiens	19-24
19893601-8	2009	The presence of heparin also inhibited the degradation of HMGB1 by plasmin in vitro.	Heparin	16-23	high mobility group box 1	Mus musculus	58-63
19893601-9	2009	Taken together, these results suggested that HMGB1 in complex with heparin possesses remarkable angiogenic activity, probably through the induction of TNF-alpha and VEGF-A120.	Heparin	67-74	high mobility group box 1	Mus musculus	45-50
20508160-1	2010	The diagnosis of heparin-induced thrombocytopenia (HIT) requires detection of antibodies to the heparin/platelet factor 4 (PF4) complexes via enzyme-linked immunosorbent assay.	Heparin	17-24	platelet factor 4	Homo sapiens	96-121
20508160-1	2010	The diagnosis of heparin-induced thrombocytopenia (HIT) requires detection of antibodies to the heparin/platelet factor 4 (PF4) complexes via enzyme-linked immunosorbent assay.	Heparin	17-24	platelet factor 4	Homo sapiens	123-126
24628114-5	2014	KEY RESULTS: Functional analyses showed that heparin was a competitive antagonist of all IP3R subtypes with different affinities for each (IP3R3 &gt; IP3R1 &gt;= IP3R2).	Heparin	45-52	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	139-144
20592020-1	2010	Tissue factor pathway inhibitor (TFPI) inhibits tissue factor-induced coagulation, but may, via its C terminus, also modulate cell surface, heparin, and lipopolysaccharide interactions as well as participate in growth inhibition.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	0-31
20592020-1	2010	Tissue factor pathway inhibitor (TFPI) inhibits tissue factor-induced coagulation, but may, via its C terminus, also modulate cell surface, heparin, and lipopolysaccharide interactions as well as participate in growth inhibition.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	33-37
20699357-4	2010	Blocking alpha5beta1 integrin or supplementing cultures with heparin, which both inhibited microfibril assembly, disrupted LTBP-1 deposition and enhanced Smad2 phosphorylation.	Heparin	61-68	SMAD family member 2	Homo sapiens	154-159
19709740-3	2009	Heparin inhibited SMC proliferation and up-regulated expression of contractile SMC phenotype markers, including smooth muscle alpha-actin, calponin, and SM-22alpha, in a dose-dependent fashion (6 microg/ml to 3.2mg/ml).	Heparin	0-7	transgelin	Homo sapiens	153-163
19555665-0	2009	NKG2D and CD94 bind to heparin and sulfate-containing polysaccharides.	Heparin	23-30	killer cell lectin like receptor K1	Homo sapiens	0-5
19555665-6	2009	Mutagenesis revealed that (152)Y and (199)Y of NKG2D and (144)F, (160)N, and (166)C of CD94 were critical for binding to heparin-BSA.	Heparin	121-128	killer cell lectin like receptor K1	Homo sapiens	47-52
19555665-7	2009	The present manuscript provides the first evidence that NKG2D and CD94 bind to heparin and sulfate-containing polysaccharides.	Heparin	79-86	killer cell lectin like receptor K1	Homo sapiens	56-61
20547765-8	2010	Mechanistically, Wnt3a-heparin signaling strongly activates the phosphoinositide 3-kinase/Akt pathway and requires the bone-related transcription factor RUNX2 to stimulate alkaline phosphatase activity, which parallels canonical beta-catenin signaling.	Heparin	23-30	Wnt family member 3A	Homo sapiens	17-22
24844576-5	2014	It is caused by heparin-dependent, platelet-activating antibodies that identifies a self-protein, PF4, bound to heparin that results in an antibody formation.	Heparin	16-23	platelet factor 4	Homo sapiens	98-101
20547765-9	2010	Collectively, our findings establish the osteo-inductive potential of a heparin-mediated Wnt3a-phosphoinositide 3-kinase/Akt-RUNX2 signaling network and suggest that heparan sulfate supplementation may selectively reduce the therapeutic doses of peptide factors required to promote bone formation.	Heparin	72-79	Wnt family member 3A	Homo sapiens	89-94
20547770-0	2010	Influence of heparin mimetics on assembly of the FGF.FGFR4 signaling complex.	Heparin	13-20	fibroblast growth factor receptor 4	Homo sapiens	53-58
20432446-1	2010	Heparin and endogenous heparinoids inhibit the proliferation of smooth muscle cells, including renal mesangial cells; multiple effects on signaling pathways are well established, including effects on PKC, Erk, and CaMK-II.	Heparin	0-7	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	214-221
20432446-6	2010	Our data support a mechanism whereby heparin acts at the cell surface to suppress downstream targets of CaMK-II, including EGFR, leading in turn to a decrease in Erk- (but not c-Src-) dependent induction of c-fos.	Heparin	37-44	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	104-111
20445443-1	2010	Earlier studies of addition of naturally sulfated polysaccharides including unfractionated heparin showed a significant enhancement of the in-vitro activation of glutamic plasminogen (Glu-Plg) by tissue plasminogen activator (t-PA) or urokinase plasminogen activator (u-PA).	Heparin	91-98	plasminogen	Homo sapiens	188-191
20445443-6	2010	In-vitro studies were conducted on comparing the effect of oversulfated chondroitin-6-sulfate (S-2) with native compound (N-2) and unfractionated heparin in enhancing the activation of Glu-Plg by t-PA or u-PA using 0.05 mol/l Tris buffer (pH 7.3) containing 0.9% of NaCl.	Heparin	146-153	plasminogen	Homo sapiens	189-192
19552638-1	2009	BACKGROUND: Antibodies to complexes of heparin and platelet factor 4 (PF4) are capable of causing heparin-induced thrombocytopenia (HIT).	Heparin	39-46	platelet factor 4	Homo sapiens	70-73
24844576-5	2014	It is caused by heparin-dependent, platelet-activating antibodies that identifies a self-protein, PF4, bound to heparin that results in an antibody formation.	Heparin	112-119	platelet factor 4	Homo sapiens	98-101
24657949-0	2014	Intracellular delivery of desulfated heparin with bile acid conjugation alleviates T cell-mediated inflammatory arthritis via inhibition of RhoA-dependent transcellular diapedesis.	Heparin	37-44	ras homolog family member A	Mus musculus	140-144
19736157-4	2009	UFH released tissue factor pathway inhibitor (TFPI) during and immediately after PCI while bivalirudin (irrespective of GP IIb/IIIa) did not.	Heparin	0-3	tissue factor pathway inhibitor	Homo sapiens	13-44
19736157-4	2009	UFH released tissue factor pathway inhibitor (TFPI) during and immediately after PCI while bivalirudin (irrespective of GP IIb/IIIa) did not.	Heparin	0-3	tissue factor pathway inhibitor	Homo sapiens	46-50
24657949-9	2014	Thus, intracellular heparin exerts anti-inflammatory effects through the inhibition of RhoA-dependent transendothelial recruitment of T cells and may have applications in the treatment of chronic inflammatory arthritis.	Heparin	20-27	ras homolog family member A	Mus musculus	87-91
24467264-9	2014	In cultured endothelial cells, human kallistatin via its heparin-binding site inhibited HMGB1-induced nuclear factor-kappaB activation and inflammatory gene expression.	Heparin	57-64	high mobility group box 1	Homo sapiens	88-93
18465825-4	2009	The ratio of peptide to heparin was found to modulate the rate of GDNF release.	Heparin	24-31	glial cell derived neurotrophic factor	Gallus gallus	66-70
19359419-6	2009	In this study, we demonstrate that anti-HARE antibodies specifically block the uptake of LMWH and UFH by isolated rat liver SECs and by human 293 cells expressing recombinant human HARE (hHARE).	Heparin	98-101	stabilin 2	Rattus norvegicus	40-44
24655923-8	2014	More importantly, we show, for the first time, that the AMPK pathway is activated in platelets of patients undergoing major cardiac surgery, in a heparin-sensitive manner.	Heparin	146-153	protein kinase AMP-activated catalytic subunit alpha 1	Homo sapiens	56-60
19359419-8	2009	Rat liver SECs or cells expressing the recombinant 190-kDa HARE isoform internalized both UFH and LMWH, and both heparins cross-compete with each other, suggesting that they share the same binding sites.	Heparin	90-93	stabilin 2	Rattus norvegicus	59-63
19359419-8	2009	Rat liver SECs or cells expressing the recombinant 190-kDa HARE isoform internalized both UFH and LMWH, and both heparins cross-compete with each other, suggesting that they share the same binding sites.	Heparin	113-121	stabilin 2	Rattus norvegicus	59-63
24655935-1	2014	BACKGROUND: Heparin, the standard perioperative anticoagulant for the prevention of graft vessel thrombosis in patients undergoing liver transplantation (LT), binds to the chemokine platelet factor 4 (PF4).	Heparin	12-19	platelet factor 4	Homo sapiens	201-204
24655935-2	2014	Antibodies that are formed against the resulting PF4/heparin complexes can induce heparin-induced thrombocytopenia.	Heparin	53-60	platelet factor 4	Homo sapiens	49-52
19254961-2	2009	Exogenous heparin polymer and some octasaccharides inhibited FGF-2-induced phosphorylation both of FGFR-1 and of extracellular signal-regulated kinase (ERK1/2) in Chinese hamster ovary (CHO)-K1 cells transfected with FGFR-1, which present HS on their cell surface.	Heparin	10-17	fibroblast growth factor 2	Cricetulus griseus	61-66
19254961-6	2009	In CHO-677 cells deficient in HS biosynthesis, heparin enhanced FGF-2-induced phosphorylation of ERK1/2.	Heparin	47-54	fibroblast growth factor 2	Cricetulus griseus	64-69
19144981-1	2009	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize PF4/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	98-101
24655935-4	2014	OBJECTIVES: To investigate the immune response against PF4/heparin complexes in patients undergoing LT.	Heparin	59-66	platelet factor 4	Homo sapiens	55-58
24735539-0	2014	A mutation in the heparin-binding site of noggin as a novel mechanism of proximal symphalangism and conductive hearing loss.	Heparin	18-25	noggin	Homo sapiens	42-48
19281736-2	2009	Our study aimed to establish the prevalence of heparin-induced antibodies (HIA), otherwise known as platelet factor 4 (PF4) antibodies, and their relationship to thrombocytopenia and thrombotic events in a group of predominantly African-American hemodialysis patients over 12 months.	Heparin	47-54	platelet factor 4	Homo sapiens	119-122
19218095-6	2009	Increasing concentrations (0-200 ng/mL) of various TFPI in the presence of low heparin concentrations (0.1 IU/mL) prolonged lag time and decreased ETP by 25% to 75% with the most prominent effect promoted by glycosylated full-length TFPI.	Heparin	79-86	tissue factor pathway inhibitor	Homo sapiens	51-55
19218095-11	2009	The C-terminal region and, to a lesser extent, glycosylation of the TFPI molecule were essential for its anticoagulant function in the absence and presence of heparin.	Heparin	159-166	tissue factor pathway inhibitor	Homo sapiens	68-72
24735539-4	2014	In this study, we investigated a Japanese pedigree with SYM1 and conductive hearing loss and found that it carried a novel heterozygous missense mutation of NOG (c.406C&gt;T; p.R136C) affecting the heparin-binding site of noggin.	Heparin	198-205	noggin	Homo sapiens	56-60
24735539-4	2014	In this study, we investigated a Japanese pedigree with SYM1 and conductive hearing loss and found that it carried a novel heterozygous missense mutation of NOG (c.406C&gt;T; p.R136C) affecting the heparin-binding site of noggin.	Heparin	198-205	noggin	Homo sapiens	157-160
24735539-4	2014	In this study, we investigated a Japanese pedigree with SYM1 and conductive hearing loss and found that it carried a novel heterozygous missense mutation of NOG (c.406C&gt;T; p.R136C) affecting the heparin-binding site of noggin.	Heparin	198-205	noggin	Homo sapiens	222-228
24735539-5	2014	As no mutations of the heparin-binding site of noggin have previously been reported, we investigated the crystal structure of wild-type noggin to investigate molecular mechanism of the p.R136C mutation.	Heparin	23-30	noggin	Homo sapiens	47-53
24735539-7	2014	An in silico docking analysis showed that one of the salt bridges between noggin and heparin disappeared following the replacement of the arginine with a non-charged cysteine.	Heparin	85-92	noggin	Homo sapiens	74-80
19140680-0	2009	Heparin enhances the inhibition of factor Xa by protein C inhibitor in the presence but not in the absence of Ca2+.	Heparin	0-7	serpin family A member 5	Homo sapiens	48-67
24452831-3	2014	We embedded biotinylated water-soluble quantum dots into polyethylene glycol (PEG)-coated micropatterned arrays and functionalised them via streptavidin to bind biotinylated ligands, here biotinylated-PF4/heparin complexes.	Heparin	205-212	platelet factor 4	Homo sapiens	201-204
24497640-6	2014	Co-immunoprecipitation studies show that PECAM-1 Galphaq/11 binding is dramatically decreased by competitive inhibition with heparin, pharmacological inhibition with the HS antagonist surfen, and enzymatic removal of HS chains with heparinase III treatment as well as by site-directed mutagenesis of basic residues within the extracellular domain of PECAM-1.	Heparin	125-132	platelet and endothelial cell adhesion molecule 1	Homo sapiens	41-48
19154117-8	2009	Mutant competition and heparin trapping experiments reveal that UvsW is extremely processive during ATP-driven translocation with a half-life on the order of several minutes.	Heparin	23-30	UvsW helicase	Escherichia phage T4	64-68
19196184-0	2009	Natural cytotoxicity receptors NKp30, NKp44 and NKp46 bind to different heparan sulfate/heparin sequences.	Heparin	88-95	natural cytotoxicity triggering receptor 1	Homo sapiens	48-53
24627550-1	2014	In this issue of Blood, Poli et al demonstrate that heparin analogs engineered to minimize their anticoagulant properties can potently downregulate hepcidin production in vitro and in vivo, and may potentially be used to treat the anemia of inflammation.	Heparin	52-59	DNA polymerase iota	Homo sapiens	24-28
18990693-9	2009	Molecular modeling shows a structural disruption in the region of RCP that corresponds to the KCP-heparin-binding site.	Heparin	98-105	CGRP receptor component	Homo sapiens	66-69
24595027-4	2014	We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site.	Heparin	159-166	nucleolin	Homo sapiens	22-31
22914811-4	2014	RESULTS: Preoperative heparin pretreatment increased the antiheparin/PF4 antibody IgG levels (P &lt; .01), while the administration of heparin further increased this levels (P &lt; .01).	Heparin	22-29	platelet factor 4	Rattus norvegicus	69-72
19731406-1	2009	PURPOSE: Anticoagulant tissue factor pathway inhibitor (TFPI) is released from its endothelial stores by heparin, which may lead to its untoward depletion.	Heparin	105-112	tissue factor pathway inhibitor	Homo sapiens	23-54
19731406-1	2009	PURPOSE: Anticoagulant tissue factor pathway inhibitor (TFPI) is released from its endothelial stores by heparin, which may lead to its untoward depletion.	Heparin	105-112	tissue factor pathway inhibitor	Homo sapiens	56-60
18845532-5	2008	After an injection of heparin, we reasoned that LPL bound to GPIHBP1 in capillaries would be released very quickly, and we hypothesized that the kinetics of LPL entry into the plasma would differ in Gpihbp1(-/-) and control mice.	Heparin	22-29	GPI-anchored HDL-binding protein 1	Mus musculus	61-68
22914811-4	2014	RESULTS: Preoperative heparin pretreatment increased the antiheparin/PF4 antibody IgG levels (P &lt; .01), while the administration of heparin further increased this levels (P &lt; .01).	Heparin	61-68	platelet factor 4	Rattus norvegicus	69-72
18845532-7	2008	In contrast, plasma LPL levels in Gpihbp1(-/-) mice were much lower 1 min after heparin and increased slowly over 15 min.	Heparin	80-87	GPI-anchored HDL-binding protein 1	Mus musculus	34-41
22499338-8	2014	We identified osterix as the key transcription factor responsible for the enhanced bone matrix deposition observed on hyaluronic acid, heparin and chondroitin-6-sulphate.	Heparin	135-142	Sp7 transcription factor	Homo sapiens	14-21
18845532-11	2008	The differences in LPL release after intravenous heparin and Intralipid strongly suggest that GPIHBP1 represents an important binding site for LPL in vivo.	Heparin	49-56	GPI-anchored HDL-binding protein 1	Mus musculus	94-101
18845535-2	2008	We have solved the GDNF(2).GFR alpha 1(2) complex structure at 2.35 A resolution in the presence of a heparin mimic, sucrose octasulfate.	Heparin	102-109	GDNF family receptor alpha 1	Homo sapiens	27-38
18926810-4	2008	RESULTS: The levels and zymography of MMP-2 did not show significant changes among all samples, and during time- and dose-dependent heparin treatments.	Heparin	132-139	matrix metallopeptidase 2	Homo sapiens	38-43
18926810-6	2008	Addition of heparin allowed also the displacement of MMP-2 prodomain, favouring zymogen activation.	Heparin	12-19	matrix metallopeptidase 2	Homo sapiens	53-58
24253450-7	2014	Doxorubicin cytoxicity, which was enhanced by heparin treatment of MCF-7 cells, was found to be under the control of one of the major non-ABC transporter proteins, lung resistance protein (LRP).	Heparin	46-53	major vault protein	Homo sapiens	164-187
18773185-7	2008	Heparin, a potent G-coupled protein kinase 2 inhibitor, was found to abolish ERM protein phosphorylation and cortical F-actin ring formation in Ang II-treated podocytes, indicating that phosphorylated ERM proteins are the cytoskeletal effector in AT1R signaling.	Heparin	0-7	angiotensin II receptor, type 1a	Rattus norvegicus	247-251
24253450-7	2014	Doxorubicin cytoxicity, which was enhanced by heparin treatment of MCF-7 cells, was found to be under the control of one of the major non-ABC transporter proteins, lung resistance protein (LRP).	Heparin	46-53	major vault protein	Homo sapiens	189-192
17982734-8	2008	CONCLUSIONS: Heparin-PF4 ELISA optical density values increase with increasing probability of heparin induced thrombocytopenia.	Heparin	94-101	platelet factor 4	Homo sapiens	21-24
24985584-4	2014	We hypothesized that heparin might inhibit burn-induced apoptosis in the spleen via suppression of the IL-1 pathway.	Heparin	21-28	interleukin 1 complex	Mus musculus	103-107
19226055-1	2008	Heparin-induced thrombocytopenia is a serious complication during antithromboembolic prophylaxis caused by anti-heparin/platelet factor 4 (PF4) complex antibodies.	Heparin	0-7	platelet factor 4	Homo sapiens	139-142
24985584-13	2014	CONCLUSION: Heparin inhibits burn-induced apoptosis of the spleen cells by suppressing IL-1 expression in mice.	Heparin	12-19	interleukin 1 complex	Mus musculus	87-91
23904295-4	2013	The virulence factor Int1 contained the most putative heparin-binding motifs (n = 5); peptides encompassing 2 of 5 motifs bound to heparin-Sepharose.	Heparin	54-61	Wnt family member 1	Rattus norvegicus	21-25
18954601-2	2008	CXCL7 is heparin binding, has heparanase activity, and is a ligand to CXCR2, a G-protein-linked receptor.	Heparin	9-16	pro-platelet basic protein	Homo sapiens	0-5
18713736-8	2008	Finally, mutation of the positively charged heparin-binding domains within LPL and apolipoprotein AV abolished the ability of these proteins to bind to GPIHBP1.	Heparin	44-51	glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1	Cricetulus griseus	152-159
23904295-4	2013	The virulence factor Int1 contained the most putative heparin-binding motifs (n = 5); peptides encompassing 2 of 5 motifs bound to heparin-Sepharose.	Heparin	131-138	Wnt family member 1	Rattus norvegicus	21-25
24127555-5	2013	KIR2DL4 was found to directly interact with HS/heparin, and the D0 domain of KIR2DL4 was essential for this interaction.	Heparin	47-54	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 4	Homo sapiens	0-7
18841292-1	2008	Laboratory testing for heparin-induced thrombocytopenia (HIT) includes the highly sensitive, though less specific, heparin/platelet factor 4 (PF4) ELISA.	Heparin	23-30	platelet factor 4	Homo sapiens	115-140
18841292-1	2008	Laboratory testing for heparin-induced thrombocytopenia (HIT) includes the highly sensitive, though less specific, heparin/platelet factor 4 (PF4) ELISA.	Heparin	23-30	platelet factor 4	Homo sapiens	142-145
24127555-5	2013	KIR2DL4 was found to directly interact with HS/heparin, and the D0 domain of KIR2DL4 was essential for this interaction.	Heparin	47-54	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 4	Homo sapiens	77-84
24127555-6	2013	Accordingly, exogenous HS/heparin can regulate cytokine production by KIR2DL4-expressing NK cells and HEK293T cells (HEK293T-2DL4), and induces differential localization of KIR2DL4 to rab5(+) and rab7(+) endosomes, thus leading to downregulation of cytokine production and degradation of the receptor.	Heparin	26-33	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 4	Homo sapiens	70-77
18449905-0	2008	Heparin inhibits BMP-2 osteogenic bioactivity by binding to both BMP-2 and BMP receptor.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	17-22
18449905-0	2008	Heparin inhibits BMP-2 osteogenic bioactivity by binding to both BMP-2 and BMP receptor.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	65-70
18449905-3	2008	In the present study, we examined whether heparin has the effects on osteoblast differentiation induced by BMP-2 in vitro and also elucidated the precise mechanism by which heparin regulates bone metabolism induced by this molecule.	Heparin	42-49	bone morphogenetic protein 2	Homo sapiens	107-112
24127555-6	2013	Accordingly, exogenous HS/heparin can regulate cytokine production by KIR2DL4-expressing NK cells and HEK293T cells (HEK293T-2DL4), and induces differential localization of KIR2DL4 to rab5(+) and rab7(+) endosomes, thus leading to downregulation of cytokine production and degradation of the receptor.	Heparin	26-33	killer cell immunoglobulin like receptor, two Ig domains and long cytoplasmic tail 4	Homo sapiens	173-180
18449905-4	2008	Our results showed that heparin inhibited alkaline phosphatase (ALP) activity and mineralization in osteoblastic cells cultured with BMP-2.	Heparin	24-31	bone morphogenetic protein 2	Homo sapiens	133-138
18449905-5	2008	Heparin was found to suppress the mRNA expressions of osterix, Runx2, ALP and osteocalcin, as well as phosphorylation of Smad1/5/8 and p38 MAPK.	Heparin	0-7	Sp7 transcription factor	Homo sapiens	54-61
24127555-6	2013	Accordingly, exogenous HS/heparin can regulate cytokine production by KIR2DL4-expressing NK cells and HEK293T cells (HEK293T-2DL4), and induces differential localization of KIR2DL4 to rab5(+) and rab7(+) endosomes, thus leading to downregulation of cytokine production and degradation of the receptor.	Heparin	26-33	RAB7B, member RAS oncogene family	Homo sapiens	196-200
23813781-1	2013	STUDY OBJECTIVE: To evaluate whether using an immunoglobulin G (IgG)-specific platelet factor 4 (PF4) test reduces the rate of positive PF4 results and has an impact on prescribing practices of nonheparin anticoagulants (direct thrombin inhibitors and fondaparinux) in patients assessed for heparin-induced thrombocytopenia (HIT).	Heparin	197-204	platelet factor 4	Homo sapiens	97-100
20632253-3	2010	As a heparin-binding tetramer, recombinant PF4 interferes with several steps of endothelial cell proliferation, migration, and angiogenesis, regulates apoptotic death through activation of distinct signal transduction pathways, inhibits growth factor receptor binding, amplifies the inflammatory response of natural killer cells through regulation of cytokines production, and induces and maintains a nonspecific immune response to cancer cells.	Heparin	5-12	platelet factor 4	Homo sapiens	43-46
23703622-1	2013	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is diagnosed using clinical criteria and detection of platelet-activating anti-platelet factor 4/heparin (anti-PF4/H) antibodies, usually through a surrogate enzyme-linked immunosorbent assay (ELISA).	Heparin	12-19	platelet factor 4	Homo sapiens	162-167
20136400-0	2010	Delivery of basic fibroblast growth factor using heparin-conjugated fibrin for therapeutic angiogenesis.	Heparin	49-56	fibroblast growth factor 2	Mus musculus	12-42
20136400-1	2010	Heparin-conjugated fibrin (HCF, a mixture of heparin-conjugated fibrinogen and thrombin) was developed as an injectable carrier for long-term delivery of fibroblast growth factor 2 (FGF2), and the therapeutic potential of the HCF system was investigated by evaluating neovascularization in a mouse hind limb ischemia model.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	154-180
20136400-1	2010	Heparin-conjugated fibrin (HCF, a mixture of heparin-conjugated fibrinogen and thrombin) was developed as an injectable carrier for long-term delivery of fibroblast growth factor 2 (FGF2), and the therapeutic potential of the HCF system was investigated by evaluating neovascularization in a mouse hind limb ischemia model.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	182-186
24065103-5	2013	Furthermore, in silico computer modeling and in vitro binding assays suggest critical roles for the following basic amino acids located within heparin binding regions (HBRs) of EDN 34QRRCKN39 (HBR1), 65NKTRKN70 (HBR2), and 113NRDQRRD119 (HBR3) and in particular Arg35, Arg36, and Arg38 within HBR1, and Arg114 and Arg117 within HBR3.	Heparin	143-150	ribonuclease A family member 2	Homo sapiens	177-180
20299390-1	2010	Heparin/platelet factor 4 (H:PF4) antibodies are the causative agent in heparin-induced thrombocytopenia (HIT).	Heparin	72-79	platelet factor 4	Homo sapiens	29-32
20206875-5	2010	This article explains the important role of PF4 released during platelet activation with the administration of heparin in the pathogenesis of thrombocytopenia and thrombosis in HIT.	Heparin	111-118	platelet factor 4	Homo sapiens	44-47
23575223-8	2013	In pre-clinical studies, treatment of mdx mice with heparin, an activator of p38, causes a pronounced increase in utrophin A in diaphragm muscle fibers.	Heparin	52-59	mitogen-activated protein kinase 14	Mus musculus	77-80
20004006-5	2010	This review will focus on PF4 and its potential roles in hemostasis/thrombosis and the underlying pathways by which PF4 may be especially important in such pathologic thrombotic states as heparin-induced thrombocytopenia (HIT) and septic shock.	Heparin	188-195	platelet factor 4	Homo sapiens	26-29
20004006-5	2010	This review will focus on PF4 and its potential roles in hemostasis/thrombosis and the underlying pathways by which PF4 may be especially important in such pathologic thrombotic states as heparin-induced thrombocytopenia (HIT) and septic shock.	Heparin	188-195	platelet factor 4	Homo sapiens	116-119
23847186-1	2013	In this issue of Blood, Jaax and colleagues show that heparin-PF4 antibodies cross-reacted with nucleic acid (NA)-PF4 complexes and induced platelet activation, suggesting that NA-PF4 can potentially cause a heparin-induced thrombocytopenia (HIT)-like prothrombotic disorder.	Heparin	54-61	platelet factor 4	Homo sapiens	62-65
20079824-5	2010	Additionally, POX up-regulated caspase-12 expression in a dose-dependent manner, and pre-treatment with EGTA, heparin or procaine significantly inhibited POX-induced increase of caspase-12 expression.	Heparin	110-117	caspase 12	Mus musculus	31-41
20079824-5	2010	Additionally, POX up-regulated caspase-12 expression in a dose-dependent manner, and pre-treatment with EGTA, heparin or procaine significantly inhibited POX-induced increase of caspase-12 expression.	Heparin	110-117	caspase 12	Mus musculus	178-188
19965682-2	2010	The combined effect of type of surgery (major vs minor) and heparin on this prothrombotic immune reaction to platelet factor 4 (PF4)/heparin was analyzed.	Heparin	60-67	platelet factor 4	Homo sapiens	128-131
23847186-1	2013	In this issue of Blood, Jaax and colleagues show that heparin-PF4 antibodies cross-reacted with nucleic acid (NA)-PF4 complexes and induced platelet activation, suggesting that NA-PF4 can potentially cause a heparin-induced thrombocytopenia (HIT)-like prothrombotic disorder.	Heparin	54-61	platelet factor 4	Homo sapiens	114-117
23847186-1	2013	In this issue of Blood, Jaax and colleagues show that heparin-PF4 antibodies cross-reacted with nucleic acid (NA)-PF4 complexes and induced platelet activation, suggesting that NA-PF4 can potentially cause a heparin-induced thrombocytopenia (HIT)-like prothrombotic disorder.	Heparin	54-61	platelet factor 4	Homo sapiens	114-117
23737512-1	2013	OBJECTIVE: To report a case in which there was a lack of activated partial thromboplastin time (aPTT) correlation with plasma argatroban concentrations in a patient with elevated factor VIII levels who was diagnosed with heparin-induced thrombocytopenia (HIT).	Heparin	221-228	cytochrome c oxidase subunit 8A	Homo sapiens	186-190
20113257-0	2010	Is heparin plasma suitable for the determination of B-type natriuretic peptide on the Beckman-Coulter Access 2?	Heparin	3-10	natriuretic peptide B	Homo sapiens	52-78
20113257-1	2010	BACKGROUND: The use of heparin as an alternative to EDTA in the production of plasma samples is of particular interest for B-type natriuretic peptide (BNP) measurements.	Heparin	23-30	natriuretic peptide B	Homo sapiens	123-149
20113257-1	2010	BACKGROUND: The use of heparin as an alternative to EDTA in the production of plasma samples is of particular interest for B-type natriuretic peptide (BNP) measurements.	Heparin	23-30	natriuretic peptide B	Homo sapiens	151-154
20113257-3	2010	The goal of this study was to determine the feasibility of measuring BNP using heparin plasma instead of EDTA plasma with the Access 2 system (Beckman-Coulter).	Heparin	79-86	natriuretic peptide B	Homo sapiens	69-72
20113257-4	2010	METHODS: BNP was determined in heparin plasma and EDTA plasma from 24 patients within 1 h of blood collection.	Heparin	31-38	natriuretic peptide B	Homo sapiens	9-12
23562456-4	2013	The putative YKL-40 ligands are thought to be carbohydrate structures, since it is capable of binding chitin, chito-oligosaccharides and heparin.	Heparin	137-144	chitinase 3 like 1	Homo sapiens	13-19
20113257-6	2010	RESULTS: At H(0), the observed BNP concentrations in heparin plasma were much higher (mean values 65% higher) than those in EDTA plasma.	Heparin	53-60	natriuretic peptide B	Homo sapiens	31-34
20113257-8	2010	BNP stability decreased over time in heparin plasma: immunoreactivity decreased approximately by 30% during the first 2 h and by 60% after 8 h. CONCLUSIONS: Heparin plasma does not seem to be a suitable alternative to EDTA plasma for measurement of BNP using the Access 2 system, even if measurements are performed immediately after blood sampling.	Heparin	37-44	natriuretic peptide B	Homo sapiens	0-3
23551961-12	2013	Among nine additional samples that tested indeterminate in the SRA, FcgammaRIIa proteolysis resolved five samples that had a positive anti-PF4/heparin EIA result; three had no FcgammaRIIa proteolysis, and two were shown to have heparin-dependent FcgammaRIIa proteolysis CONCLUSIONS: This study suggests that heparin-dependent FcgammaRIIa proteolysis is at least as specific as the SRA for the diagnosis of HIT.	Heparin	228-235	Fc gamma receptor IIa	Homo sapiens	68-79
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	32-39	C-X-C motif chemokine ligand 12	Rattus norvegicus	64-70
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	32-39	C-X-C motif chemokine ligand 12	Rattus norvegicus	109-115
23888776-7	2013	Substitution of the Bone morphogenetic protein-7 N-terminus by the heparin-binding site of Bone morphogenetic protein-2 was carried out to increase the heparin binding capacity of the novel protein.	Heparin	67-74	bone morphogenetic protein 2	Homo sapiens	91-119
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	187-194	C-X-C motif chemokine ligand 12	Rattus norvegicus	64-70
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	187-194	C-X-C motif chemokine ligand 12	Rattus norvegicus	109-115
23888776-7	2013	Substitution of the Bone morphogenetic protein-7 N-terminus by the heparin-binding site of Bone morphogenetic protein-2 was carried out to increase the heparin binding capacity of the novel protein.	Heparin	152-159	bone morphogenetic protein 2	Homo sapiens	91-119
23561460-0	2013	Emphasis on the Role of PF4 in the Incidence, Pathophysiology and Treatment of Heparin Induced Thrombocytopenia.	Heparin	79-86	platelet factor 4	Homo sapiens	24-27
20387539-9	2010	Generation of Slit2 and Ext 1 compound mutants caused disturbed activity of Slit proteins, heparin/heparan sulfate-binding chemorepulsive guidance factors.	Heparin	91-98	exostosin glycosyltransferase 1	Homo sapiens	24-29
19845689-6	2010	Furthermore, heparin inhibited cyclin-dependent kinase inhibitor p21(WAF1/CIP1) and p53 tumour suppressor gene and protein expression up to 2-fold or 1.8-fold, respectively, and stimulated cyclin D1 expression up to 1.8-fold, in these cell lines through a p38-mediated mechanism.	Heparin	13-20	cyclin D1	Homo sapiens	189-198
19965971-9	2010	Patients who received heparin and aspirin had significantly higher live birth rate (RR 1.301; 95% CI 1.040, 1.629) than aspirin alone, with the number needed to achieve one live birth being 5.6.	Heparin	22-29	ribonucleotide reductase catalytic subunit M1	Homo sapiens	84-88
19910578-7	2010	The CXCL4 effect was entirely neutralized by heparin, which bound CXCL4 and prevented CXCL4 surface binding to monocytes.	Heparin	45-52	platelet factor 4	Homo sapiens	4-9
19910578-7	2010	The CXCL4 effect was entirely neutralized by heparin, which bound CXCL4 and prevented CXCL4 surface binding to monocytes.	Heparin	45-52	platelet factor 4	Homo sapiens	66-71
19910578-7	2010	The CXCL4 effect was entirely neutralized by heparin, which bound CXCL4 and prevented CXCL4 surface binding to monocytes.	Heparin	45-52	platelet factor 4	Homo sapiens	66-71
23561460-1	2013	Heparin Induced Thrombocytopenia (HIT) is caused by antibodies that recognize platelet factor 4 (PF4) associated with polyanionic glycosaminoglycan drugs or displayed on vascular cell membranes.	Heparin	0-7	platelet factor 4	Homo sapiens	97-100
23561460-2	2013	These antibodies are elicited by multimolecular complexes that can occur when heparin is administered in clinical settings associated with abundant PF4.	Heparin	78-85	platelet factor 4	Homo sapiens	148-151
20059332-1	2010	Heparin-induced thrombocytopenia (HIT) is an immune-mediated hypercoagulable disorder caused by antibodies to platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	129-132
23561460-3	2013	Heparin binding alters native PF4 and elicits immune recognition and response.	Heparin	0-7	platelet factor 4	Homo sapiens	30-33
23305841-1	2013	BACKGROUND: Heparin-induced thrombocytopenia (HIT) develops as a result of platelet (PLT) activation by anti-platelet factor 4 (PF4)/heparin complex antibodies.	Heparin	12-19	platelet factor 4	Homo sapiens	128-131
20139591-2	2010	Bovine 18 kDa lactophorin was purified by heparin affinity chromatography from cow"s milk whey.	Heparin	42-49	glycosylation dependent cell adhesion molecule 1	Bos taurus	14-25
23351665-1	2013	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize platelet factor 4/heparin (PF4/hep) complexes.	Heparin	12-19	platelet factor 4	Homo sapiens	137-144
20369319-1	2010	Heparin-induced thrombocytopenia (HIT) is a potentially life-threatening adverse drug reaction that may develop in certain patients exposed to heparin and is caused by antibodies with specificity for chemokine CXCL4 (formerly known as platelet factor 4)/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	210-215
20369319-1	2010	Heparin-induced thrombocytopenia (HIT) is a potentially life-threatening adverse drug reaction that may develop in certain patients exposed to heparin and is caused by antibodies with specificity for chemokine CXCL4 (formerly known as platelet factor 4)/heparin complexes.	Heparin	143-150	platelet factor 4	Homo sapiens	210-215
23223449-9	2013	These observations suggest that both HS6ST-1 and HS6ST-2 are involved in 6-O-sulfation of heparin and that the proper packaging and storage of tryptase, carboxypeptidase-A, and chymase may be regulated differently by the 6-O-sulfate residues in heparin.	Heparin	90-97	heparan sulfate 6-O-sulfotransferase 1	Mus musculus	37-44
19819167-11	2010	CONCLUSIONS: This series demonstrates that short-term re-exposure to heparin during urgent CPB for heart transplantation or MCSD placement is safe despite the presence of thrombocytopenia and Hep/PF4 antibodies.	Heparin	69-76	platelet factor 4	Homo sapiens	196-199
23223449-9	2013	These observations suggest that both HS6ST-1 and HS6ST-2 are involved in 6-O-sulfation of heparin and that the proper packaging and storage of tryptase, carboxypeptidase-A, and chymase may be regulated differently by the 6-O-sulfate residues in heparin.	Heparin	245-252	heparan sulfate 6-O-sulfotransferase 1	Mus musculus	37-44
23211448-0	2013	The effect of a heparin-based coacervate of fibroblast growth factor-2 on scarring in the infarcted myocardium.	Heparin	16-23	fibroblast growth factor 2	Mus musculus	44-70
23284011-7	2013	Concomitant Intralipid/heparin infusion, which caused a reduction of insulin sensitivity by 40% (P &lt; .0001), resulted in a marked increase in serum visfatin (P &lt; .0001), which was already observed after 2 hours of FFAs increase (P &lt; .0001).	Heparin	23-30	nicotinamide phosphoribosyltransferase	Homo sapiens	151-159
20652010-3	2010	The chemokine CXCL7 binds heparin and the G-protein-linked receptor CXCR2.	Heparin	26-33	pro-platelet basic protein	Homo sapiens	14-19
23284011-8	2013	Serum visfatin during the clamp study after 2 and 6 hours of Intralipid/heparin infusion was significantly higher than respective values during the clamp study without the elevation of FFAs (both P &lt; .0001).	Heparin	72-79	nicotinamide phosphoribosyltransferase	Homo sapiens	6-14
19709391-1	2010	BACKGROUND: The anti-platelet factor 4 (PF4)/heparin immune response, which underlies heparin-induced thrombocytopenia (HIT), has several atypical features: relatively rapid onset even without previous heparin exposure, lack of immune anamnesis, and transience of antibody production.	Heparin	45-52	platelet factor 4	Homo sapiens	16-38
23284011-9	2013	The increase in serum visfatin during Intralipid/heparin infusion was positively related to body weight (r = 0.54, P = .016) and gamma-glutamyltransferase activity (r = 0.56, P = .011).	Heparin	49-56	nicotinamide phosphoribosyltransferase	Homo sapiens	22-30
19709391-1	2010	BACKGROUND: The anti-platelet factor 4 (PF4)/heparin immune response, which underlies heparin-induced thrombocytopenia (HIT), has several atypical features: relatively rapid onset even without previous heparin exposure, lack of immune anamnesis, and transience of antibody production.	Heparin	45-52	platelet factor 4	Homo sapiens	40-43
19709391-1	2010	BACKGROUND: The anti-platelet factor 4 (PF4)/heparin immune response, which underlies heparin-induced thrombocytopenia (HIT), has several atypical features: relatively rapid onset even without previous heparin exposure, lack of immune anamnesis, and transience of antibody production.	Heparin	86-93	platelet factor 4	Homo sapiens	16-38
22894570-1	2013	In this study, we tested the hypothesis that a surface functionalization delivery platform incorporating heparin onto strontium alginate microbeads surfaces would convert this "naive carriers" into "mini-reservoirs" for localized in vivo delivery of recombinant human bone morphogenetic protein-2 (rhBMP-2) that will induce functional bone regeneration.	Heparin	105-112	bone morphogenetic protein 2	Homo sapiens	268-296
19709391-1	2010	BACKGROUND: The anti-platelet factor 4 (PF4)/heparin immune response, which underlies heparin-induced thrombocytopenia (HIT), has several atypical features: relatively rapid onset even without previous heparin exposure, lack of immune anamnesis, and transience of antibody production.	Heparin	86-93	platelet factor 4	Homo sapiens	40-43
19709391-3	2010	The PF4-containing antigen complexes were attached to microtiter plates via a spacer, rather than using nitrocellulose, and the final reaction enzyme substrate was added in melted agarose which, after rapid hardening, localized color development of enzyme-tagged anti-immunoglobulin G (IgG) probes to single PF4/heparin-specific B cells.	Heparin	312-319	platelet factor 4	Homo sapiens	4-7
19877579-0	2009	The heparin binding motif of endostatin mediates its interaction with receptor nucleolin.	Heparin	4-11	nucleolin	Homo sapiens	79-88
19877579-3	2009	To define the exact role of the heparin binding motif in mediating the interaction between endostatin and its receptor nucleolin, up to six arginine residues (R155, R158, R184, R270, R193, and R194) located in the heparin binding motif of endostatin were substituted by alanine to make double, quadruple, or hexad point mutations, respectively.	Heparin	32-39	nucleolin	Homo sapiens	119-128
19877579-4	2009	Contributions of the heparin binding motif to both the interaction with nucleolin and the biological activities of endostatin were investigated from in vitro to in vivo.	Heparin	21-28	nucleolin	Homo sapiens	72-81
19877579-5	2009	Here we show that Arg to Ala point mutagenesis of the heparin binding motif does not interrupt the folding of endostatin but significantly impairs the interaction between endostatin and nucleolin.	Heparin	54-61	nucleolin	Homo sapiens	186-195
19877579-7	2009	Taken together, the present study demonstrates that the arginine clusters in the heparin binding motif of endostatin significantly contribute to its interaction with receptor nucleolin and mediate the antiangiogenic and antitumor activities of endostatin.	Heparin	81-88	nucleolin	Homo sapiens	175-184
23073152-7	2013	The best tripartite fusion was identified as MBP-(EAAAK)(3)-GFP-(GGGGS)(3)-HepA, which shows potential to facilitate the production of HepA and its application in industrial preparation of low molecular weight heparin.	Heparin	210-217	myelin basic protein	Homo sapiens	45-48
19695308-7	2009	The pre-incubation of HeLa cells with heparin or with anti-heparan sulfate antibodies or with beta-d-xyloside inhibited SDF-1/CXCL12-mediated cell invasion.	Heparin	38-45	C-X-C motif chemokine ligand 12	Homo sapiens	120-125
19695308-7	2009	The pre-incubation of HeLa cells with heparin or with anti-heparan sulfate antibodies or with beta-d-xyloside inhibited SDF-1/CXCL12-mediated cell invasion.	Heparin	38-45	C-X-C motif chemokine ligand 12	Homo sapiens	126-132
19961422-7	2009	Therefore, admixtures of MMPs can be efficiently eliminated from CP preparations by chromatography on heparin-Sepharose as proposed previously.	Heparin	102-109	matrix metallopeptidase 2	Homo sapiens	25-29
24772670-4	2013	Earlier, it was considered that the anticoagulant activities of these two marine glycans were driven mainly by a catalytic serpin-dependent mechanism likewise the mammalian heparins.	Heparin	173-181	serpin-ZX	Cucumis sativus	123-129
19782617-7	2009	CONCLUSIONS: Bone formation was stimulated around the apatite-covered titanium coated with BMP-2/heparin, which may be useful in improving implant therapy.	Heparin	97-104	bone morphogenetic protein 2	Rattus norvegicus	91-96
24151519-6	2013	Heparin treatment of B/W mice reduced the in vivo expression of CCR2, IL1 beta , and TLR7 compared to untreated B/W mice.	Heparin	0-7	chemokine (C-C motif) receptor 2	Mus musculus	64-68
19786011-0	2009	Histidine-rich glycoprotein inhibited high mobility group box 1 in complex with heparin-induced angiogenesis in matrigel plug assay.	Heparin	80-87	high mobility group box 1	Homo sapiens	38-63
19786011-3	2009	Additionally, we reported that high mobility group box 1 (HMGB1) in complex with heparin induces angiogenesis; therefore, we examined the effect of HRG on heparin-dependent HMGB1-induced angiogenesis in the present study.	Heparin	81-88	high mobility group box 1	Homo sapiens	58-63
19786011-3	2009	Additionally, we reported that high mobility group box 1 (HMGB1) in complex with heparin induces angiogenesis; therefore, we examined the effect of HRG on heparin-dependent HMGB1-induced angiogenesis in the present study.	Heparin	155-162	high mobility group box 1	Homo sapiens	58-63
19786011-3	2009	Additionally, we reported that high mobility group box 1 (HMGB1) in complex with heparin induces angiogenesis; therefore, we examined the effect of HRG on heparin-dependent HMGB1-induced angiogenesis in the present study.	Heparin	155-162	high mobility group box 1	Homo sapiens	173-178
19786011-4	2009	HRG completely inhibited angiogenesis induced by HMGB1 in complex with heparin.	Heparin	71-78	high mobility group box 1	Homo sapiens	49-54
19786011-5	2009	HRG inhibited the diffusion of a complex of HMGB1 with heparin from matrigel into surrounding tissue.	Heparin	55-62	high mobility group box 1	Homo sapiens	44-49
19786011-6	2009	HRG also competed with HMGB1 for heparin binding in vitro.	Heparin	33-40	high mobility group box 1	Homo sapiens	23-28
18519572-3	2008	Recently, we have shown that heparin specifically inhibits the APC-mediated cleavage at Arg506 and stimulates cleavage at Arg306.	Heparin	29-36	APC regulator of WNT signaling pathway	Homo sapiens	63-66
18519572-4	2008	Three-dimensional molecular models of APC docked at the Arg306 and Arg506 cleavage sites in FVa have identified several FVa amino acids that may be important for FVa inactivation by APC in the absence and presence of heparin.	Heparin	217-224	APC regulator of WNT signaling pathway	Homo sapiens	38-41
18519572-7	2008	With this, we have now demonstrated that a cluster of basic residues in FVa comprising Lys320, Arg321, and Arg400 is required for the heparin-mediated stimulation of cleavage at Arg306 by APC.	Heparin	134-141	APC regulator of WNT signaling pathway	Homo sapiens	188-191
23546723-1	2013	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating immunoglobulin (Ig) G antibodies that recognize multimolecular complexes of platelet factor 4 (PF4) bound to heparin or other polyanions.	Heparin	0-7	platelet factor 4	Homo sapiens	167-170
18633011-0	2008	Urgent cardiac surgery in a patient with a remote history of heparin-induced thrombocytopenia: use of the anti-PF4/heparin ELISA confirmatory test.	Heparin	61-68	platelet factor 4	Homo sapiens	111-114
19251947-7	2009	Surface plasmon resonance analysis revealed that NE binding to HS (equilibrium dissociation constant, approximately 14 nM) could be outcompeted by heparin variants.	Heparin	147-154	elastase, neutrophil expressed	Homo sapiens	49-51
23546723-1	2013	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating immunoglobulin (Ig) G antibodies that recognize multimolecular complexes of platelet factor 4 (PF4) bound to heparin or other polyanions.	Heparin	181-188	platelet factor 4	Homo sapiens	167-170
22793995-1	2013	Heparin-induced thrombocytopenia (HIT) is a severe complication of heparin therapy, characterized by thrombocytopenia and an increased risk for thrombotic complications secondary to the formation of IgG antibodies (Ab), recognizing a complex of heparin (H) and PF4.	Heparin	0-7	platelet factor 4	Homo sapiens	261-264
19805913-9	2009	Abundant syndecan-1 on wild-type murine hepatocytes exhibited saturable binding of VLDL and inhibition by heparin and facilitated degradation of VLDL.	Heparin	106-113	syndecan 1	Mus musculus	9-19
18489711-1	2008	BACKGROUND: Many laboratories test for heparin-induced thrombocytopenia (HIT) using a PF4-dependent enzyme-immunoassay (EIA).	Heparin	39-46	platelet factor 4	Homo sapiens	86-89
18549262-12	2008	In summary, we describe heparin affinity fractionation enrichment (HAFE) as a prefractionation tool for the study of the human primary tissue proteome and the discovery of PSB7, PRDX1, and SRP9 up-regulation as candidate biomarkers of colon cancer.	Heparin	24-31	signal recognition particle 9	Homo sapiens	189-193
22993391-9	2012	We recently have identified platelet polyphosphate (an inorganic polymer) and mast cell heparin as in vivo FXII activators with implications on the initiation of thrombosis and edema during hypersensitivity reactions.	Heparin	88-95	coagulation factor XII (Hageman factor)	Mus musculus	107-111
18544901-5	2008	Application of IP(3) caused GFP-IP(3)R3 clustering in permeabilized cells, and the response was completely inhibited by heparin, a competitive inhibitor of IP(3)R.	Heparin	120-127	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	28-39
18544901-5	2008	Application of IP(3) caused GFP-IP(3)R3 clustering in permeabilized cells, and the response was completely inhibited by heparin, a competitive inhibitor of IP(3)R.	Heparin	120-127	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	32-38
18327914-4	2008	Here, the possibility that heparin and heparan sulfate (HS) are ligands for PECAM-1 was reinvestigated.	Heparin	27-34	platelet and endothelial cell adhesion molecule 1	Homo sapiens	76-83
18327914-11	2008	Heparin oligosaccharides inhibited Flag-PECAM-1 from binding immobilized heparin, with certain structures having greater inhibitory activity than others.	Heparin	73-80	platelet and endothelial cell adhesion molecule 1	Homo sapiens	40-47
18327914-13	2008	PECAM-1 does bind heparin/HS but by a site that is distinct from that required for homophilic binding.	Heparin	18-25	platelet and endothelial cell adhesion molecule 1	Homo sapiens	0-7
19936054-3	2009	We show that heparin displaces PrP(C) from rafts and promotes its endocytosis, suggesting that heparin competes with an endogenous raft-resident HSPG for binding to PrP(C).	Heparin	13-20	prion protein	Mus musculus	31-37
19936054-3	2009	We show that heparin displaces PrP(C) from rafts and promotes its endocytosis, suggesting that heparin competes with an endogenous raft-resident HSPG for binding to PrP(C).	Heparin	13-20	prion protein	Mus musculus	165-171
19936054-3	2009	We show that heparin displaces PrP(C) from rafts and promotes its endocytosis, suggesting that heparin competes with an endogenous raft-resident HSPG for binding to PrP(C).	Heparin	95-102	prion protein	Mus musculus	31-37
19936054-3	2009	We show that heparin displaces PrP(C) from rafts and promotes its endocytosis, suggesting that heparin competes with an endogenous raft-resident HSPG for binding to PrP(C).	Heparin	95-102	prion protein	Mus musculus	165-171
19936054-4	2009	We then utilised a transmembrane-anchored form of PrP (PrP-TM), which is targeted to rafts solely by its N-terminal domain, to show that both heparin and phosphatidylinositol-specific phospholipase C can inhibit its association with detergent-resistant rafts, implying that a GPI-anchored HSPG targets PrP(C) to rafts.	Heparin	142-149	prion protein	Mus musculus	50-53
19893601-0	2009	High mobility group box 1 complexed with heparin induced angiogenesis in a matrigel plug assay.	Heparin	41-48	high mobility group box 1	Mus musculus	0-25
19560816-0	2009	A star-PEG-heparin hydrogel platform to aid cell replacement therapies for neurodegenerative diseases.	Heparin	11-18	activation induced cytidine deaminase	Homo sapiens	40-43
22206708-1	2012	Protein C inhibitor was purified from human plasma by use of a dermatan sulfate or heparin column, followed by hydroxyapatite, gel filtration and ion exchange columns.	Heparin	83-90	serpin family A member 5	Homo sapiens	0-19
20092760-8	2009	Low molecular weight heparin and heparin were both available to anticoagualte;but dosage required in patients with FAP was much higher than that of SAP (P &lt; 0.05).	Heparin	21-28	fibroblast activation protein alpha	Homo sapiens	115-118
20092760-8	2009	Low molecular weight heparin and heparin were both available to anticoagualte;but dosage required in patients with FAP was much higher than that of SAP (P &lt; 0.05).	Heparin	33-40	fibroblast activation protein alpha	Homo sapiens	115-118
18325345-5	2008	NaPaC completely inhibited the heparin binding to VEGF165, NRP-1 and VEGFR2.	Heparin	31-38	neuropilin 1	Homo sapiens	59-64
18325345-7	2008	These results suggested that heparin binding sites of VEGFR2 and NRP-1 were different from those of VEGF165.	Heparin	29-36	neuropilin 1	Homo sapiens	65-70
22999213-0	2012	Daily administration of low molecular weight heparin increases Hepatocyte Growth Factor serum levels in gynaecological patients: pharmacokinetic parameters and clinical implications.	Heparin	45-52	hepatocyte growth factor	Homo sapiens	63-87
18291250-2	2008	In an unpredictable fashion, as many as approximately 17% of patients treated with unfractionated heparin (UFH) and approximately 8% treated with low-molecular-weight heparin (LMWH) subsequently develop the anti-heparin-PF4 antibodies that mediate heparin-induced thrombocytopenia and thrombosis (HIT).	Heparin	98-105	platelet factor 4	Homo sapiens	220-223
18291250-2	2008	In an unpredictable fashion, as many as approximately 17% of patients treated with unfractionated heparin (UFH) and approximately 8% treated with low-molecular-weight heparin (LMWH) subsequently develop the anti-heparin-PF4 antibodies that mediate heparin-induced thrombocytopenia and thrombosis (HIT).	Heparin	107-110	platelet factor 4	Homo sapiens	220-223
18291250-2	2008	In an unpredictable fashion, as many as approximately 17% of patients treated with unfractionated heparin (UFH) and approximately 8% treated with low-molecular-weight heparin (LMWH) subsequently develop the anti-heparin-PF4 antibodies that mediate heparin-induced thrombocytopenia and thrombosis (HIT).	Heparin	167-174	platelet factor 4	Homo sapiens	220-223
18291250-2	2008	In an unpredictable fashion, as many as approximately 17% of patients treated with unfractionated heparin (UFH) and approximately 8% treated with low-molecular-weight heparin (LMWH) subsequently develop the anti-heparin-PF4 antibodies that mediate heparin-induced thrombocytopenia and thrombosis (HIT).	Heparin	167-174	platelet factor 4	Homo sapiens	220-223
19470522-2	2009	By using glycan microarray analysis and other assays, we found that human C21orf63 interacts with heparin and to a lesser extent with heparan sulphate.	Heparin	98-105	eva-1 homolog C	Homo sapiens	74-82
19470522-3	2009	The C-terminal galactose-binding lectin domain of C21orf63 is necessary for heparin binding.	Heparin	76-83	eva-1 homolog C	Homo sapiens	50-58
19470522-4	2009	The inability of other human proteins with galactose-binding lectin domains to interact with heparin suggests that heparin binding is a unique property of C21orf63.	Heparin	115-122	eva-1 homolog C	Homo sapiens	155-163
18302088-1	2008	Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by platelet-activating antibodies that recognize multimolecular complexes of platelet factor 4 (PF4) bound to heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	175-178
22679243-1	2012	Antibodies to the heparin/platelet factor 4 complex (heparin/PF4) are linked to the pathogenesis of heparin-induced thrombocytopenia (HIT) and to the thrombotic complications.	Heparin	18-25	platelet factor 4	Homo sapiens	61-64
18302088-1	2008	Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by platelet-activating antibodies that recognize multimolecular complexes of platelet factor 4 (PF4) bound to heparin.	Heparin	189-196	platelet factor 4	Homo sapiens	175-178
19950764-1	2009	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is an acquired, prothrombotic disorder, caused by antibodies to a complex of heparin and platelet factor 4 (PF4) that activates platelets, resulting in the release of procoagulant microparticles, thrombocytopenia occurrence, generation of thrombin, and frequent thromboses.	Heparin	14-21	platelet factor 4	Homo sapiens	161-164
22677127-0	2012	Polymorphisms of protein tyrosine phosphatase CD148 influence FcgammaRIIA-dependent platelet activation and the risk of heparin-induced thrombocytopenia.	Heparin	120-127	protein tyrosine phosphatase receptor type J	Homo sapiens	46-51
19706524-5	2009	We show that betaKlotho was essential for FGF19 interaction with FGFRs 1c, 2c, and 3c, but FGF19 was able to interact directly with FGFR4 in the absence of betaKlotho in a heparin-dependent manner.	Heparin	172-179	fibroblast growth factor receptor 4	Mus musculus	132-137
19625657-8	2009	Interestingly, CXCL4 did not act as a direct enzyme inhibitor, but destabilized active tetrameric beta-tryptase by antagonizing the heparin component required for the integrity of the tetramer.	Heparin	132-139	platelet factor 4	Homo sapiens	15-20
19727205-9	2009	These results suggested that heparin"s anti-inflammatory effects can be partly explained by its blocking of the interaction between HMGB1 or S100A12 and RAGE.	Heparin	29-36	high mobility group box 1	Homo sapiens	132-137
22677127-1	2012	Heparin-induced thrombocytopenia (HIT) is due primarily to IgG antibodies specific to platelet factor 4/heparin complexes (PF4/Hs) that activate platelets via FcgammaRIIA.	Heparin	0-7	platelet factor 4	Homo sapiens	123-129
19482851-1	2009	BACKGROUND: Antibodies to the heparin/platelet factor 4 (PF4) complex are linked to the pathogenesis of heparin-induced thrombocytopenia type II, and to the thrombotic complications associated with this syndrome.	Heparin	30-37	platelet factor 4	Homo sapiens	57-60
22577175-5	2012	Heparin increased the avidity of KKO binding to PF4 without affecting RTO, but it did not increase total binding or binding to nontetrameric PF4(K50E).	Heparin	0-7	platelet factor 4	Homo sapiens	48-51
19172319-6	2009	The modeled structure also shows specific structural differences between AT3 and ZPI in the heparin-binding and flexible N-terminal tail regions.	Heparin	92-99	serpin family A member 10	Homo sapiens	81-84
22641378-0	2012	Improving the specificity of the PF4 ELISA in diagnosing heparin-induced thrombocytopenia.	Heparin	57-64	platelet factor 4	Homo sapiens	33-36
19411282-6	2009	As an example, translation efficiency mediated by heparin-binding epidermal growth factor 3-untranslated region was increased 3-fold in liver cancer cells compared with normal hepatocytes, whereas stability of an mRNA containing a portion of Cyclin D1 3-untranslated region was increased more than 2-fold in HepG2 cells compared with normal hepatocytes.	Heparin	50-57	cyclin D1	Homo sapiens	242-251
22739141-1	2012	Heparins have been reported to cause elevations in serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) but have not been associated with clinically significant liver injury.	Heparin	0-8	glutamic--pyruvic transaminase	Homo sapiens	57-81
22330023-11	2012	JNK and p38 MAPK were activated under heparin in TA and SOL of WT (P &lt; 0.05) but not in muscles of tlr2 and tlr4 mice.	Heparin	38-45	mitogen-activated protein kinase 14	Mus musculus	8-16
19034645-4	2009	The assay is applicable to a wide variety of heparin/HS-binding proteins of diverse structure and function (e.g., FGF-1, FGF-2, VEGF, IL-8, MCP-2, ATIII, PF4) and to ligands of varying molecular weight and degree of sulfation (e.g., heparin, PI-88, sucrose octasulfate, naphthalene trisulfonate) and is thus well suited for the rapid screening of ligands in drug discovery applications.	Heparin	45-52	platelet factor 4	Homo sapiens	154-157
22285427-5	2012	Human adipose-derived stem cell (hASC) adhesion to MBP-bFGF immobilized on a PS surface (PS-MBP-bFGF) was inhibited by heparin.	Heparin	119-126	myelin basic protein	Homo sapiens	51-54
22285427-5	2012	Human adipose-derived stem cell (hASC) adhesion to MBP-bFGF immobilized on a PS surface (PS-MBP-bFGF) was inhibited by heparin.	Heparin	119-126	myelin basic protein	Homo sapiens	92-95
21080209-0	2012	Modulating the interaction of CXCR4 and CXCL12 by low-molecular-weight heparin inhibits hepatic metastasis of colon cancer.	Heparin	71-78	C-X-C motif chemokine ligand 12	Homo sapiens	40-46
19158842-7	2009	Characterization of the plasmin-derived 97 kDa fragment with domain-specific collagen XVII antibodies, heparin binding and N-glycosylation studies indicates that the N-terminus is located approximately at AA 515 and the C-terminus N-terminally from AA 1,421.	Heparin	103-110	plasminogen	Homo sapiens	24-31
22302099-6	2012	Accordingly, KIN59 inhibited the binding of FGF2 to FGF receptor-1 (FGFR1), thus preventing the formation of productive heparan sulphate proteoglycan/FGF2/FGFR1 ternary complexes, without affecting heparin interaction.	Heparin	198-205	fibroblast growth factor 2	Mus musculus	44-48
19325014-0	2009	Intravenous administration of low molecular weight and unfractionated heparin elicits a rapid increase in serum pregnancy-associated plasma protein A.	Heparin	70-77	pappalysin 1	Homo sapiens	112-149
19325014-2	2009	Because low molecular weight heparin (LMWH) and unfractionated heparin (UFH) are commonly used in these cases, we analyzed the effects of intravenous administration of these heparins on serum PAPP-A concentrations.	Heparin	174-182	pappalysin 1	Homo sapiens	192-198
19325014-8	2009	RESULTS: A rapid increase in total PAPP-A (median, 25-fold) was seen in all patients within 5 min of administration for both LMWH and UFH boluses.	Heparin	134-137	pappalysin 1	Homo sapiens	35-41
19325014-11	2009	Repeated heparin boluses induced a new PAPP-A release.	Heparin	9-16	pappalysin 1	Homo sapiens	39-45
22302099-6	2012	Accordingly, KIN59 inhibited the binding of FGF2 to FGF receptor-1 (FGFR1), thus preventing the formation of productive heparan sulphate proteoglycan/FGF2/FGFR1 ternary complexes, without affecting heparin interaction.	Heparin	198-205	fibroblast growth factor receptor 1	Mus musculus	52-66
19325014-13	2009	CONCLUSIONS: Intravenous administration of heparin induces an intense and rapid increase in free PAPP-A in the serum.	Heparin	43-50	pappalysin 1	Homo sapiens	97-103
22302099-6	2012	Accordingly, KIN59 inhibited the binding of FGF2 to FGF receptor-1 (FGFR1), thus preventing the formation of productive heparan sulphate proteoglycan/FGF2/FGFR1 ternary complexes, without affecting heparin interaction.	Heparin	198-205	fibroblast growth factor receptor 1	Mus musculus	68-73
22088491-1	2012	Heparin-induced thrombocytopenia (HIT) is a pathophysiological syndrome caused by platelet-activating antibodies that recognize PF4/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	128-131
19670563-2	2009	Like heparin-induced thrombocytopenia, it is associated with the presence of anti-PF4 antibodies.	Heparin	5-12	platelet factor 4	Homo sapiens	82-85
22088491-1	2012	Heparin-induced thrombocytopenia (HIT) is a pathophysiological syndrome caused by platelet-activating antibodies that recognize PF4/heparin complexes.	Heparin	132-139	platelet factor 4	Homo sapiens	128-131
19195682-2	2009	To address the hypothesis of a calcium-dependent template mechanism in LMWH activity, we compared the ability of the heparin neutralising agent Platelet Factor 4 (PF4) to inhibit various therapeutic LMWH in a kinetic assay.	Heparin	117-124	platelet factor 4	Homo sapiens	163-166
19195682-7	2009	Instead, increasing enzyme concentration reversed the negative effect of heparin-bound AT on PF4-dependent neutralization.	Heparin	73-80	platelet factor 4	Homo sapiens	93-96
22239992-1	2012	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) results from an atypical immune response with synthesis of IgG antibodies (Abs) to platelet factor 4/heparin complexes (PF4/H), and probably involves both B and T cells.	Heparin	14-21	platelet factor 4	Homo sapiens	173-178
19195682-8	2009	Inhibition of thrombin by heparin was also neutralized by PF4, albeit to a higher extent than the fXa-AT reaction.	Heparin	26-33	platelet factor 4	Homo sapiens	58-61
19195682-9	2009	Altogether, these results suggested that an interaction of PF4 with protease mediated the association of PF4 to the heparin chain.	Heparin	116-123	platelet factor 4	Homo sapiens	59-62
19195682-9	2009	Altogether, these results suggested that an interaction of PF4 with protease mediated the association of PF4 to the heparin chain.	Heparin	116-123	platelet factor 4	Homo sapiens	105-108
18243369-1	2009	We determined change in serum hepatocyte growth factor (HGF), one of the most potent angiogenic factors, after intravenous infusion of heparin in children and reported successful improvement of cardiac ischemia after regular intravenous heparin infusion in an infant with ischemic heart disease (IHD) caused by Kawasaki disease (KD).	Heparin	135-142	hepatocyte growth factor	Homo sapiens	30-54
18243369-1	2009	We determined change in serum hepatocyte growth factor (HGF), one of the most potent angiogenic factors, after intravenous infusion of heparin in children and reported successful improvement of cardiac ischemia after regular intravenous heparin infusion in an infant with ischemic heart disease (IHD) caused by Kawasaki disease (KD).	Heparin	135-142	hepatocyte growth factor	Homo sapiens	56-59
18243369-1	2009	We determined change in serum hepatocyte growth factor (HGF), one of the most potent angiogenic factors, after intravenous infusion of heparin in children and reported successful improvement of cardiac ischemia after regular intravenous heparin infusion in an infant with ischemic heart disease (IHD) caused by Kawasaki disease (KD).	Heparin	237-244	hepatocyte growth factor	Homo sapiens	30-54
18243369-1	2009	We determined change in serum hepatocyte growth factor (HGF), one of the most potent angiogenic factors, after intravenous infusion of heparin in children and reported successful improvement of cardiac ischemia after regular intravenous heparin infusion in an infant with ischemic heart disease (IHD) caused by Kawasaki disease (KD).	Heparin	237-244	hepatocyte growth factor	Homo sapiens	56-59
18243369-2	2009	Intravenous infusion of 50 units/kg of heparin significantly increased serum HGF from 0.8+/-0.6 to 8.4+/-3.4 at 5 min, 8.3+/-2.5 at 30 min, and 4.9+/-1.5 ng/ml at 60 min, respectively.	Heparin	39-46	hepatocyte growth factor	Homo sapiens	77-80
18243369-5	2009	In conclusion, regular heparin infusion alone can improve myocardial ischemia caused by KD, probably due to facilitated production of HGF.	Heparin	23-30	hepatocyte growth factor	Homo sapiens	134-137
22318669-0	2012	Disruption of PF4/H multimolecular complex formation with a minimally anticoagulant heparin (ODSH).	Heparin	84-91	platelet factor 4	Homo sapiens	14-17
19329916-0	2009	PEPE II--a multicenter study with an end-point heparin-bonded expanded polytetrafluoroethylene vascular graft for above and below knee bypass surgery: determinants of patency.	Heparin	47-54	peptidase E	Homo sapiens	0-4
18261960-6	2008	Studies of cultured endothelial cells and human placenta have demonstrated that TFPI associates with the cell surface through a glycosyl phosphatidyinositol (GPI)-anchor in a manner that is not dependent on GAGs or altered by heparin.	Heparin	226-233	tissue factor pathway inhibitor	Homo sapiens	80-84
22318669-1	2012	Recent studies have shown that ultra-large complexes (ULCs) of platelet factor 4 (PF4) and heparin (H) play an essential role in the pathogenesis of heparin-induced thrombocytopenia (HIT), an immune-mediated disorder caused by PF4/H antibodies.	Heparin	91-98	platelet factor 4	Homo sapiens	227-230
22318669-3	2012	We tested a minimally anticoagulant compound (2-O, 3-O desulfated heparin, ODSH) with preserved charge to disrupt PF4/H complex formation and immunogenicity.	Heparin	66-73	platelet factor 4	Homo sapiens	114-117
18234290-2	2009	We aimed to investigate the effect of UFH and enoxaparin on plasma levels of prothrombin fragment 1+2 (PF 1+2) and thrombin/antithrombin complex (TAT) as markers of intravascular thrombogenesis during HD.	Heparin	38-41	PHD finger protein 12	Homo sapiens	103-107
18234290-6	2009	PF 1+2 significantly decreased during both UFH (chi(2) ANOVA=9.82, P=0.007) and enoxaparin (chi(2) ANOVA=29.40, P&lt;10(-6)) anticoagulated HD, while over-HD TAT levels changes differed depending on the type of heparin.	Heparin	211-218	PHD finger protein 12	Homo sapiens	0-4
22318669-6	2012	When ODSH and unfractionated heparin (UFH) are mixed at equimolar concentrations, we show that there is a negligible effect on amount of protamine required for heparin neutralisation and reduced immunogenicity of PF4/UFH in the presence of ODSH.	Heparin	38-41	platelet factor 4	Homo sapiens	213-220
18234290-7	2009	The switch from enoxaparin to UFH treatment was connected with a significantly higher PF 1+2 after 10 and 180 min as well as higher TAT concentration after 180 min of HD.	Heparin	30-33	PHD finger protein 12	Homo sapiens	86-101
18234290-8	2009	Only during enoxaparin anticoagulated HD 34% PF 1+2 decrease and TAT levels after 180 min of HD was closely associated with heparin dosage.	Heparin	124-131	PHD finger protein 12	Homo sapiens	45-49
18158320-5	2008	There are two putative heparin-binding domains (HBDs) within the OPN molecule, which may bind both heparin and heparin-like glycosaminoglycans such as syndecan.	Heparin	23-30	secreted phosphoprotein 1	Mus musculus	65-68
22235124-1	2012	The mouse and human TPSB2 and TPSAB1 genes encode tetramer-forming tryptases stored in the secretory granules of mast cells (MCs) ionically bound to heparin-containing serglycin proteoglycans.	Heparin	149-156	tryptase beta 2	Homo sapiens	20-25
22067544-0	2012	Incidence of isolated heparin-induced thrombocytopenia and risk of thrombosis by IgG-specific anti-PF4/heparin ELISA.	Heparin	22-29	platelet factor 4	Homo sapiens	99-102
17848620-9	2008	Activation of both pathways was observed with immunoglobulin from patients with heparin-induced thrombocytopenia (HIT), suggesting novel mechanisms for platelet dysfunction by FcgammaRIIa after immunologic insult.	Heparin	80-87	Fc gamma receptor IIa	Homo sapiens	176-187
20008202-1	2009	Heparin-induced thrombocytopenia (HIT) is an immune-mediated disorder caused by the development of antibodies to platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	132-135
20008202-5	2009	A more rapid drop in the platelet count can occur in patients who have been recently exposed to heparin (within the preceding 3 months), due to preformed anti-heparin/PF4 antibodies.	Heparin	96-103	platelet factor 4	Homo sapiens	167-170
22238310-7	2012	We found that treatment of syndecan 1-transduced cells (expressing increased HS) with heparinase, a heparin-degradative enzyme, reduced HTLV-1 susceptibility without affecting the expression levels of HS chains.	Heparin	86-93	syndecan 1	Homo sapiens	27-37
19925286-0	2009	Hepatocyte growth factor/activin A/follistatin system activation during hemodialysis with different low molecular weight heparins.	Heparin	121-129	hepatocyte growth factor	Homo sapiens	0-24
19925286-1	2009	Hepatocyte growth factor (HGF), activin A (Act A), and follistatin (FS) compose an organotrophic system; interestingly it is modified by heparin.	Heparin	137-144	hepatocyte growth factor	Homo sapiens	0-24
19925286-1	2009	Hepatocyte growth factor (HGF), activin A (Act A), and follistatin (FS) compose an organotrophic system; interestingly it is modified by heparin.	Heparin	137-144	hepatocyte growth factor	Homo sapiens	26-29
18468239-5	2008	Heparin, one of the soluble glycosaminoglycans (GAGs), inhibited PDX-1 internalization, while chondroitin sulfate A, B, and C caused only very limited inhibition.	Heparin	0-7	pancreatic and duodenal homeobox 1	Homo sapiens	65-70
22194593-0	2012	Heparin-induced leukocytosis requires 6-O-sulfation and is caused by blockade of selectin- and CXCL12 protein-mediated leukocyte trafficking in mice.	Heparin	0-7	chemokine (C-X-C motif) ligand 12	Mus musculus	95-101
19081843-15	2008	IGFBP-2 mutants with altered IGF binding-, RGD-, and heparin-binding sites were generated and their actions examined.	Heparin	53-60	insulin-like growth factor binding protein 2a	Danio rerio	0-7
18262226-1	2008	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize platelet factor 4 (PF4)/heparin complexes.	Heparin	14-21	platelet factor 4	Homo sapiens	131-134
18262226-1	2008	INTRODUCTION: Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize platelet factor 4 (PF4)/heparin complexes.	Heparin	136-143	platelet factor 4	Homo sapiens	131-134
18262226-5	2008	MATERIALS AND METHODS: By photon correlation spectroscopy we determined the concentrations at which UFH, LMWH, and fondaparinux form complexes optimally with PF4.	Heparin	100-103	platelet factor 4	Homo sapiens	158-161
18262226-8	2008	Thus, immunization should occur more often in situations with major rather than minor platelet activation, and--for a given degree of platelet activation (PF4 availability)--as: prophylactic-dose UFH&gt;therapeutic-dose UFH&gt;prophylactic-dose LMWH, fondaparinux&gt;therapeutic-dose LMWH.	Heparin	196-199	platelet factor 4	Homo sapiens	155-158
17854853-3	2007	In the present study, a unique LAO from Agkistrodon blomhoffii ussurensis snake venom named ABU-LAO was purified by Heparin-Sepharose FF chromatography followed by an ion-exchange chromatography procedure.	Heparin	116-123	interleukin 4 induced 1	Homo sapiens	31-34
17854853-3	2007	In the present study, a unique LAO from Agkistrodon blomhoffii ussurensis snake venom named ABU-LAO was purified by Heparin-Sepharose FF chromatography followed by an ion-exchange chromatography procedure.	Heparin	116-123	interleukin 4 induced 1	Homo sapiens	96-99
19002046-2	2008	Direct thrombin inhibitors and heparin enhance fibrinolysis by inhibition of activation of thrombin activatable fibrinolysis inhibitor (TAFI); however, the role played by other thrombin-activated proteins [e.g., factor XIII (FXIII)] in fibrinolysis remained to be elucidated.	Heparin	31-38	carboxypeptidase B2	Homo sapiens	91-134
19002046-2	2008	Direct thrombin inhibitors and heparin enhance fibrinolysis by inhibition of activation of thrombin activatable fibrinolysis inhibitor (TAFI); however, the role played by other thrombin-activated proteins [e.g., factor XIII (FXIII)] in fibrinolysis remained to be elucidated.	Heparin	31-38	carboxypeptidase B2	Homo sapiens	136-140
18803278-1	2008	Heparin-induced thrombocytopenia (HIT) is a prothrombotic condition caused by platelet-activating antibodies that react with platelet factor 4 (PF4)/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	144-147
18490020-0	2008	Osteoprotegerin released from the vascular wall by heparin mainly derives from vascular smooth muscle cells.	Heparin	51-58	TNF receptor superfamily member 11b	Homo sapiens	0-15
17870532-0	2007	Novel heparin/heparan sulfate mimics as inhibitors of HGF/SF-induced MET activation.	Heparin	6-13	hepatocyte growth factor	Homo sapiens	54-60
22194593-8	2012	We conclude that heparin-induced leukocytosis requires glucosamine 6-O-sulfation and is caused by blockade of L-selectin-, P-selectin-, and CXCL12-mediated leukocyte trafficking.	Heparin	17-24	C-X-C motif chemokine ligand 12	Homo sapiens	140-146
19216269-11	2008	CONCLUSION: These findings demonstrate that heparin enhanced BMP-2-induced osteogenesis on apatite-coated titanium without the loss of BMP-2 activity.	Heparin	44-51	bone morphogenetic protein 2	Homo sapiens	61-66
22206940-1	2012	Thrombin inactivation by heparin cofactor II (HCII) is accelerated by ternary complex formation with heparin.	Heparin	25-32	serpin family D member 1	Homo sapiens	46-50
21948871-7	2012	Affinity chromatography demonstrated that ZG16p binds most strongly to heparin among the zymogen granule proteins.	Heparin	71-78	zymogen granule protein 16	Rattus norvegicus	42-47
18773307-0	2008	Enhancement of ectopic bone formation by bone morphogenetic protein-2 delivery using heparin-conjugated PLGA nanoparticles with transplantation of bone marrow-derived mesenchymal stem cells.	Heparin	85-92	bone morphogenetic protein 2	Homo sapiens	41-69
18773307-1	2008	This study was performed to determine if a combination of previously undifferentiated bone marrow-derived mesenchymal stem cells (BMMSCs) and exogenous bone morphogenetic protein-2 (BMP-2) delivered via heparin-conjugated PLGA nanoparticles (HCPNs) would extensively regenerate bone in vivo.	Heparin	203-210	bone morphogenetic protein 2	Homo sapiens	152-180
18773307-1	2008	This study was performed to determine if a combination of previously undifferentiated bone marrow-derived mesenchymal stem cells (BMMSCs) and exogenous bone morphogenetic protein-2 (BMP-2) delivered via heparin-conjugated PLGA nanoparticles (HCPNs) would extensively regenerate bone in vivo.	Heparin	203-210	bone morphogenetic protein 2	Homo sapiens	182-187
18669635-2	2008	An unprocessed monomeric N-terminal fragment (PF1) induced a very high heparin binding response, indicating heparin-mediated multimerization.	Heparin	71-78	PHD finger protein 12	Homo sapiens	46-49
18669635-2	2008	An unprocessed monomeric N-terminal fragment (PF1) induced a very high heparin binding response, indicating heparin-mediated multimerization.	Heparin	108-115	PHD finger protein 12	Homo sapiens	46-49
17916391-6	2007	This DNA-binding protein was sequentially purified using DEAE-Sephacel, heparin-Sepharose, DNA Affinity, and gel filtration chromatography.	Heparin	72-79	zinc finger protein 763	Homo sapiens	5-24
17928217-3	2007	Hybrid chondroitin/dermatan sulfate chains are also involved in formation of the neural network by capturing and presenting heparin-binding growth factors like basic fibroblast growth factor, pleiotrophin, and hepatocyte growth factor to stem cells or neuronal cells.	Heparin	124-131	hepatocyte growth factor	Homo sapiens	210-234
18669635-3	2008	Using PF1 deletion and short fragments, a heparin binding site was localized within the domain encoded by exon 7 after the first hybrid domain.	Heparin	42-49	PHD finger protein 12	Homo sapiens	6-9
21948871-8	2012	Site-directed mutational analysis revealed that the basic amino acid residues located in two putative carbohydrate-binding sites (CBSs) of ZG16p, which were found in association with the crystal structure of BanLec, are responsible for the recognition of heparin.	Heparin	255-262	zymogen granule protein 16	Rattus norvegicus	139-144
22005328-0	2012	Enhanced osteogenic activity of bone morphogenetic protein-2 by 2-O-desulfated heparin.	Heparin	79-86	bone morphogenetic protein 2	Rattus norvegicus	32-60
17623663-7	2007	Actually, MMP-2 was found to exhibit a strong binding ability to heparin, the dissociation constant value being 62 nM.	Heparin	65-72	matrix metallopeptidase 2	Homo sapiens	10-15
22005328-8	2012	These findings demonstrated that the 2-O-DS derivative of heparin has a synergistic effect on the in vitro and in vivo osteogenic activity of BMP-2.	Heparin	58-65	bone morphogenetic protein 2	Rattus norvegicus	142-147
22339638-4	2012	The SNP-derived activation was more pronounced when purified ADA2 was preincubated with heparin and different proteins as an experimental model of the protein environment in vivo.	Heparin	88-95	adenosine deaminase 2	Homo sapiens	61-65
17726466-3	2007	Radioligand competition binding assays were performed using a range of heparin oligosaccharides to compete with polymeric heparin or heparan sulphate binding to I(125) CXCL12.	Heparin	71-78	C-X-C motif chemokine ligand 12	Homo sapiens	168-174
22701303-8	2012	Both PEDF forms were glycosylated, bound to heparin, and had identical patterns by limited proteolysis.	Heparin	44-51	serpin family F member 1	Homo sapiens	5-9
17557914-5	2007	Compounds (heparin and CRM-197) that specifically interfere with HB-EGF signaling eliminated OxyHb-induced K(V) suppression, suggesting that HB-EGF is the EGFR ligand involved in this pathway.	Heparin	11-18	proheparin-binding EGF-like growth factor	Oryctolagus cuniculus	65-71
17557914-5	2007	Compounds (heparin and CRM-197) that specifically interfere with HB-EGF signaling eliminated OxyHb-induced K(V) suppression, suggesting that HB-EGF is the EGFR ligand involved in this pathway.	Heparin	11-18	proheparin-binding EGF-like growth factor	Oryctolagus cuniculus	141-147
17896955-7	2007	There is increasing evidence that platelet factor 4 (PF4) displaced from endothelial cells, heparan sulphate or directly from the platelets, binds to heparin molecule to form an immunogenic complex.	Heparin	150-157	platelet factor 4	Homo sapiens	53-56
17896955-15	2007	However, the introduction of sensitive ELISA tests to measure anti-heparin/PF4 antibodies has showed the immuno-conversion in an higher number of patients treated with heparin such as the incidence of anti-heparin/PF4 exceeds the incidence of the disease.	Heparin	67-74	platelet factor 4	Homo sapiens	214-217
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	dual oxidase 1	Homo sapiens	101-106
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	dual oxidase 1	Homo sapiens	152-157
17475322-6	2007	Next, heparin-functionalized hydrogel cell substrates were polymerized from vinyl-modified precursors and rendered adhesive through incorporation of RGDS peptide.	Heparin	6-13	ral guanine nucleotide dissociation stimulator	Homo sapiens	149-153
22261751-0	2012	Exogenous fibroblast growth factor-10 induces cystic lung development with altered target gene expression in the presence of heparin in cultures of embryonic rat lung.	Heparin	125-132	fibroblast growth factor 10	Rattus norvegicus	10-37
22912725-8	2012	HGF-induced MMP-2 and MMP-9 activation, and MT1-MMP expression, also were inhibited by heparin.	Heparin	87-94	matrix metallopeptidase 14	Homo sapiens	44-51
17363729-4	2007	However, preincubation of OPG with heparin abrogated its proadhesive activity, whereas pretreatment of endothelial cells with chondroitinase plus heparinases significantly decreased the proadhesive activity of OPG.	Heparin	35-42	TNF receptor superfamily member 11b	Homo sapiens	26-29
22912725-11	2012	Our results suggest that Egr1 activates HGF-induced cell invasion through the regulation of MMPs in HCC cells and heparin inhibits HGF-induced cellular invasion via the downregulation of Egr1.	Heparin	114-121	hepatocyte growth factor	Homo sapiens	131-134
22912725-12	2012	Therefore, heparin treatment might be a therapeutic approach to inhibit invasion and metastasis of HCC, especially for patients with active HGF/c-Met signaling.	Heparin	11-18	hepatocyte growth factor	Homo sapiens	140-143
22328880-0	2011	Influence of concomitant heparin administration on pregnancy-associated plasma protein-A levels in acute coronary syndrome with ST segment elevation.	Heparin	25-32	pappalysin 1	Homo sapiens	51-88
17580283-1	2007	Heparin-induced thrombocytopenia is a life threatening thrombotic disorder caused by antibodies to platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	118-121
22328880-3	2011	RESULTS: Heparin caused a high PAPP-A increase in ACS-STE patients, in all patients with heparin without ACS and angiographic signs of significant atherosclerosis.	Heparin	9-16	pappalysin 1	Homo sapiens	31-37
22328880-8	2011	CONCLUSIONS: The diagnostic validity of PAPP-A can be verified only within the 1(st) h after clinical onset of ACS before heparin administration, the prognostic value in heparinized patients not earlier than 12 h after the last heparin application, if ACT is normal and serious clinical concomitant complications are eliminated.	Heparin	122-129	pappalysin 1	Homo sapiens	40-46
17452490-3	2007	Surface plasmon resonance revealed that SSAPs inhibit with a competitive mechanism of action the binding of Tat and gp120 to surface-immobilized heparin, an experimental condition that resembles binding to cellular HSPGs.	Heparin	145-152	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	116-121
22328880-8	2011	CONCLUSIONS: The diagnostic validity of PAPP-A can be verified only within the 1(st) h after clinical onset of ACS before heparin administration, the prognostic value in heparinized patients not earlier than 12 h after the last heparin application, if ACT is normal and serious clinical concomitant complications are eliminated.	Heparin	170-177	pappalysin 1	Homo sapiens	40-46
17452490-6	2007	Here, we identified two classes of gp120 receptors expressed on endothelial cells, one of which was consistent with an HSPG-binding, low-affinity/high-capacity receptor that is inhibited by free heparin.	Heparin	195-202	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	35-40
21979237-1	2011	Heparin-induced thrombocytopenia (HIT) is an adverse complication of heparin caused by HIT antibodies (abs) that recognise platelet factor 4-heparin (PF4/hep) complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	150-157
17507826-0	2007	PF4 ENHANCED assay for the diagnosis of heparin-induced thrombocytopenia in complex medical and surgical patients.	Heparin	40-47	platelet factor 4	Homo sapiens	0-3
21979237-1	2011	Heparin-induced thrombocytopenia (HIT) is an adverse complication of heparin caused by HIT antibodies (abs) that recognise platelet factor 4-heparin (PF4/hep) complexes.	Heparin	69-76	platelet factor 4	Homo sapiens	150-157
17507826-1	2007	OBJECTIVE: To evaluate the sensitivity and specificity of the PF4 ENHANCED (GTI Diagnostics, Waukesha, WI) enzyme-linked immunosorbent assay for heparin-induced thrombocytopenia using the carbon-14 serotonin-release assay as the reference method.	Heparin	145-152	platelet factor 4	Homo sapiens	62-65
21772054-1	2011	Heparin-induced thrombocytopenia (HIT) is caused by antibodies that recognize complexes between platelet factor 4 (PF4) and heparin or glycosaminoglycan side chains.	Heparin	0-7	platelet factor 4	Homo sapiens	115-118
17456194-7	2007	The second-order rate constants (m(-1) min(-1)) of the reaction between HGFA and PCI in the presence or absence of heparin (10 U mL(-1)) were 4.3 x 10(6) and 4.0 x 10(6), respectively.	Heparin	115-122	serpin family A member 5	Homo sapiens	81-84
17456194-9	2007	Exogenous HGFA added to normal human plasma formed a complex with plasma PCI, and this complex formation was competitively inhibited by APC in the presence of heparin, but very weakly in the absence of heparin.	Heparin	159-166	serpin family A member 5	Homo sapiens	73-76
21772054-1	2011	Heparin-induced thrombocytopenia (HIT) is caused by antibodies that recognize complexes between platelet factor 4 (PF4) and heparin or glycosaminoglycan side chains.	Heparin	124-131	platelet factor 4	Homo sapiens	115-118
21772054-6	2011	This observation and the finding that the effect of heparin on aPC generation depends on the concentration of PF4 suggest similarity between PF4/CS complexes and those that bind HIT antibodies.	Heparin	52-59	platelet factor 4	Homo sapiens	110-113
17893639-3	2007	These antibodies recognize a "self protein", platelet factor 4 (PF4), bound to heparin.	Heparin	79-86	platelet factor 4	Homo sapiens	64-67
21772054-6	2011	This observation and the finding that the effect of heparin on aPC generation depends on the concentration of PF4 suggest similarity between PF4/CS complexes and those that bind HIT antibodies.	Heparin	52-59	platelet factor 4	Homo sapiens	141-147
21620439-1	2011	BACKGROUND: IgG-specific anti-PF4/heparin enzyme-immunoassays (EIAs) are sensitive but not specific for platelet-activating antibodies, the cause of heparin-induced thrombocytopenia (HIT).	Heparin	34-41	platelet factor 4	Homo sapiens	30-33
17332248-1	2007	Protein C inhibitor (PCI) is a serpin with affinity for heparin and phosphatidylethanolamine (PE).	Heparin	56-63	serpin family A member 5	Homo sapiens	0-19
17537154-1	2007	BACKGROUND: The T allele of the hepatic lipase (HL) C-480T polymorphism was previously found to be associated with lower post-heparin plasma HL activity, atherosclerosis and risk of coronary artery disease.	Heparin	126-133	lipase C, hepatic type	Homo sapiens	32-46
21788507-0	2011	Hypoxia triggers a proangiogenic pathway involving cancer cell microvesicles and PAR-2-mediated heparin-binding EGF signaling in endothelial cells.	Heparin	96-103	F2R like trypsin receptor 1	Homo sapiens	81-86
17317686-1	2007	We previously reported that heparin post-transcriptionally stimulates the production of hepatocyte growth factor (HGF).	Heparin	28-35	hepatocyte growth factor	Homo sapiens	114-117
17317686-2	2007	In this study, we addressed the size-dependency of heparin fragments on the HGF-inducing activity aiming to obtain fragments without antiblood coagulant activity.	Heparin	51-58	hepatocyte growth factor	Homo sapiens	76-79
21788507-5	2011	Inhibition of HB-EGF by antibody neutralization or heparin treatment efficiently counteracted PAR-2-mediated activation of hypoxic ECs.	Heparin	51-58	F2R like trypsin receptor 1	Homo sapiens	94-99
17317686-8	2007	The lack of N-sulfation in heparin markedly reduced HGF-inducing activity, whereas 2-O-desulfation or 6-O-desulation had a lesser influence.	Heparin	27-34	hepatocyte growth factor	Homo sapiens	52-55
21593136-5	2011	The data indicate that at low concentrations, soluble heparin modulates CXCR4/CXCL12 interaction and at high concentrations, abrogates binding.	Heparin	54-61	C-X-C motif chemokine ligand 12	Homo sapiens	78-84
17405859-0	2007	Structural basis for ligand and heparin binding to neuropilin B domains.	Heparin	32-39	neuropilin 1	Homo sapiens	51-61
17405859-6	2007	These results provide a detailed picture of interactions at the core of the Nrp signaling complex and establish a molecular basis for the synergistic effects of heparin on Nrp-mediated signaling.	Heparin	161-168	neuropilin 1	Homo sapiens	76-79
17405859-6	2007	These results provide a detailed picture of interactions at the core of the Nrp signaling complex and establish a molecular basis for the synergistic effects of heparin on Nrp-mediated signaling.	Heparin	161-168	neuropilin 1	Homo sapiens	172-175
20558775-5	2011	We found that: (1) hypoxia increased ROCK expression in mice and PASMCs; (2) overexpression of RhoA diminished the inhibitory effect of heparin on PASMC proliferation and down-regulated p27 expression; and (3) overexpression of GEF-H1 negated heparin inhibition of PASMC proliferation, which was accompanied by increased GTP-RhoA and decreased p27.	Heparin	136-143	ras homolog family member A	Mus musculus	95-99
20558775-5	2011	We found that: (1) hypoxia increased ROCK expression in mice and PASMCs; (2) overexpression of RhoA diminished the inhibitory effect of heparin on PASMC proliferation and down-regulated p27 expression; and (3) overexpression of GEF-H1 negated heparin inhibition of PASMC proliferation, which was accompanied by increased GTP-RhoA and decreased p27.	Heparin	136-143	ras homolog family member A	Mus musculus	325-329
20558775-5	2011	We found that: (1) hypoxia increased ROCK expression in mice and PASMCs; (2) overexpression of RhoA diminished the inhibitory effect of heparin on PASMC proliferation and down-regulated p27 expression; and (3) overexpression of GEF-H1 negated heparin inhibition of PASMC proliferation, which was accompanied by increased GTP-RhoA and decreased p27.	Heparin	243-250	ras homolog family member A	Mus musculus	95-99
16750851-3	2007	Therefore, we investigated the hypothesis that low-molecular weight heparin (LMWH) might regulate in vitro trophoblast invasiveness and placental production of matrix metalloproteinases (MMPs) and tissue inhibitors (TIMPs).	Heparin	68-75	matrix metallopeptidase 2	Homo sapiens	187-191
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	78-85	ras homolog family member A	Mus musculus	33-37
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	ras homolog family member A	Mus musculus	33-37
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	ras homolog family member A	Mus musculus	190-194
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	ras homolog family member A	Mus musculus	190-194
21480334-7	2011	The observed intrahepatic IC raised the possibility that heparin therapy may ameliorate FasL-mediated liver injury.	Heparin	57-64	Fas ligand (TNF superfamily, member 6)	Mus musculus	88-92
17202143-0	2007	Heparin binding induces a conformational change in pigment epithelium-derived factor.	Heparin	0-7	serpin family F member 1	Homo sapiens	51-84
21480334-8	2011	Notably, heparin administration in mice 4 hours before or up to 2 hours after FasL injection resulted in a dramatic reduction of liver injury-including liver hemorrhage, serum alanine aminotransferase, caspase activation, and liver apoptosis-compared with heparin-untreated mice.	Heparin	9-16	Fas ligand (TNF superfamily, member 6)	Mus musculus	78-82
21480334-8	2011	Notably, heparin administration in mice 4 hours before or up to 2 hours after FasL injection resulted in a dramatic reduction of liver injury-including liver hemorrhage, serum alanine aminotransferase, caspase activation, and liver apoptosis-compared with heparin-untreated mice.	Heparin	256-263	Fas ligand (TNF superfamily, member 6)	Mus musculus	78-82
21232785-1	2011	BACKGROUND: The in vitro demonstration of antibodies against platelet factor-4/heparin (PF4/hep) complexes is an important contribution to the diagnosis of heparin-induced thrombocytopenia (HIT).	Heparin	79-86	platelet factor 4	Homo sapiens	88-95
17276943-1	2007	Heparin-induced thrombocytopenia (HIT) is a complication caused by antibodies directed to the heparin-platelet factor 4 (PF4) complex with a seemingly paradoxical high risk of thrombosis.	Heparin	0-7	platelet factor 4	Homo sapiens	94-119
17276943-1	2007	Heparin-induced thrombocytopenia (HIT) is a complication caused by antibodies directed to the heparin-platelet factor 4 (PF4) complex with a seemingly paradoxical high risk of thrombosis.	Heparin	0-7	platelet factor 4	Homo sapiens	121-124
17332302-8	2007	RESULTS: Unfractionated heparin and the low-molecular-weight heparin tinzaparin inhibited receptor ligation and the response of CXCR4-expressing Chinese hamster ovary cells and human breast cancer cell lines to CXCL12.	Heparin	24-31	C-X-C chemokine receptor type 4	Cricetulus griseus	128-133
17332302-8	2007	RESULTS: Unfractionated heparin and the low-molecular-weight heparin tinzaparin inhibited receptor ligation and the response of CXCR4-expressing Chinese hamster ovary cells and human breast cancer cell lines to CXCL12.	Heparin	24-31	C-X-C motif chemokine ligand 12	Homo sapiens	211-217
21185276-6	2011	Patients and volunteers experiencing ischemic events without atherosclerotic lesions only had elevated PAPP-A when treated with heparin.	Heparin	128-135	pappalysin 1	Homo sapiens	103-109
17332302-8	2007	RESULTS: Unfractionated heparin and the low-molecular-weight heparin tinzaparin inhibited receptor ligation and the response of CXCR4-expressing Chinese hamster ovary cells and human breast cancer cell lines to CXCL12.	Heparin	61-68	C-X-C chemokine receptor type 4	Cricetulus griseus	128-133
17332302-8	2007	RESULTS: Unfractionated heparin and the low-molecular-weight heparin tinzaparin inhibited receptor ligation and the response of CXCR4-expressing Chinese hamster ovary cells and human breast cancer cell lines to CXCL12.	Heparin	61-68	C-X-C motif chemokine ligand 12	Homo sapiens	211-217
17332302-9	2007	Heparin also removed CXCL12 from its normal site of expression on the surface of parenchymal cells in the murine lung.	Heparin	0-7	chemokine (C-X-C motif) ligand 12	Mus musculus	21-27
17257990-1	2007	BACKGROUND: The coronary artery bypass grafting (CABG) heparin-induced thrombocytopenia thrombosis syndrome (HITTS) on- and off-pump safety and efficacy (CHOOSE-ON) trial was designed as a safety and efficacy trial of bivalirudin for use in anticoagulation during cardiopulmonary bypass (CPB) in patients with confirmed or suspected HIT and (or) antiplatelet factor 4/heparin (anti-PF4/H) antibodies.	Heparin	55-62	platelet factor 4	Homo sapiens	382-385
17143873-6	2007	FGFR1beta bound FGF-2 with three-fourfold higher affinity than FGFR1alpha both in the presence and absence of heparin.	Heparin	110-117	fibroblast growth factor 2	Cricetulus griseus	16-21
21185276-7	2011	When tissue from normal artery wall was incubated with heparin, PAPP-A was eluted.	Heparin	55-62	pappalysin 1	Homo sapiens	64-70
17143873-7	2007	Heparin increased affinity of both receptor isoforms for FGF-2 approximately four-fivefold.	Heparin	0-7	fibroblast growth factor 2	Cricetulus griseus	57-62
21185276-9	2011	CONCLUSION: Elevation of PAPP-A in patients with acute coronary syndromes seems to be caused by heparin induced release of PAPP-A from the arterial wall and not due to excretion from vulnerable plaques.	Heparin	96-103	pappalysin 1	Homo sapiens	25-31
21185276-9	2011	CONCLUSION: Elevation of PAPP-A in patients with acute coronary syndromes seems to be caused by heparin induced release of PAPP-A from the arterial wall and not due to excretion from vulnerable plaques.	Heparin	96-103	pappalysin 1	Homo sapiens	123-129
21386996-0	2011	PKCalpha and PKCdelta regulate ADAM17-mediated ectodomain shedding of heparin binding-EGF through separate pathways.	Heparin	70-77	protein kinase C delta	Homo sapiens	13-21
18688288-6	2007	By introducing a heparin functionality into the gel to sequester and localize the hMSC-produced BMP2, the osteogenic differentiation of hMSCs was further augmented over fluvastatin delivery alone.	Heparin	17-24	bone morphogenetic protein 2	Homo sapiens	96-100
21095260-0	2011	Heparin changes the conformation of high-mobility group protein 1 and decreases its affinity toward receptor for advanced glycation endproducts in vitro.	Heparin	0-7	high mobility group box 1	Mus musculus	36-65
17150202-4	2007	RESULTS: MMPs are released by platelets or leukocytes during platelet activation or sampling process, thus leading to artificially higher MMP-9 levels in serum compared with citrate, heparin, or EDTA plasma samples, independently of TBDC.	Heparin	183-190	matrix metallopeptidase 2	Homo sapiens	9-13
21095260-3	2011	Since HMGB1 also exhibits heparin-binding activity, we investigated whether heparin interferes with HMGB1/RAGE interaction and prevents the cytokine activity.	Heparin	76-83	high mobility group box 1	Mus musculus	100-105
21095260-5	2011	After treatment of HMGB1 with different concentrations of heparin (0, 50, 100 and 1000 U/L), the fluorescence peak values of HMGB1 increased and the emission wavelength showed red shifts; further, the secondary structure of HMGB1 showed a marked change in that the content of beta-pleated sheet reduced while that of alpha-helix increased.	Heparin	58-65	high mobility group box 1	Mus musculus	19-24
21095260-5	2011	After treatment of HMGB1 with different concentrations of heparin (0, 50, 100 and 1000 U/L), the fluorescence peak values of HMGB1 increased and the emission wavelength showed red shifts; further, the secondary structure of HMGB1 showed a marked change in that the content of beta-pleated sheet reduced while that of alpha-helix increased.	Heparin	58-65	high mobility group box 1	Mus musculus	125-130
17495447-0	2007	Prospective trial of combined therapy with heparin/warfarin and renin-angiotensin system inhibitors in progressive IgA nephropathy.	Heparin	43-50	IGAN1	Homo sapiens	115-130
21095260-5	2011	After treatment of HMGB1 with different concentrations of heparin (0, 50, 100 and 1000 U/L), the fluorescence peak values of HMGB1 increased and the emission wavelength showed red shifts; further, the secondary structure of HMGB1 showed a marked change in that the content of beta-pleated sheet reduced while that of alpha-helix increased.	Heparin	58-65	high mobility group box 1	Mus musculus	125-130
17495447-1	2007	We previously reported that a combined therapy with heparin/warfarin and renin-angiotensin system (RAS) inhibitors dramatically reduces proteinuria for prolonged periods in advanced IgA nephropathy (IgAN).	Heparin	52-59	IGAN1	Homo sapiens	182-197
17495447-1	2007	We previously reported that a combined therapy with heparin/warfarin and renin-angiotensin system (RAS) inhibitors dramatically reduces proteinuria for prolonged periods in advanced IgA nephropathy (IgAN).	Heparin	52-59	IGAN1	Homo sapiens	199-203
17495447-11	2007	These results indicate that our combined therapy with heparin/warfarin and RAS inhibitors can inhibit the progressive decline in renal function Combined Heparin/Warfarin and RAS Inhibitors in Progressive IgAN 115 of patients with progressive IgAN through its marked antiproteinuric and anti-inflammatory effects.	Heparin	54-61	IGAN1	Homo sapiens	204-208
17495447-11	2007	These results indicate that our combined therapy with heparin/warfarin and RAS inhibitors can inhibit the progressive decline in renal function Combined Heparin/Warfarin and RAS Inhibitors in Progressive IgAN 115 of patients with progressive IgAN through its marked antiproteinuric and anti-inflammatory effects.	Heparin	54-61	IGAN1	Homo sapiens	242-246
17495447-11	2007	These results indicate that our combined therapy with heparin/warfarin and RAS inhibitors can inhibit the progressive decline in renal function Combined Heparin/Warfarin and RAS Inhibitors in Progressive IgAN 115 of patients with progressive IgAN through its marked antiproteinuric and anti-inflammatory effects.	Heparin	153-160	IGAN1	Homo sapiens	204-208
21095260-8	2011	The amount of HMGB1 and RAGE bound forms reduced after treatment with heparin.	Heparin	70-77	high mobility group box 1	Mus musculus	14-19
17495447-11	2007	These results indicate that our combined therapy with heparin/warfarin and RAS inhibitors can inhibit the progressive decline in renal function Combined Heparin/Warfarin and RAS Inhibitors in Progressive IgAN 115 of patients with progressive IgAN through its marked antiproteinuric and anti-inflammatory effects.	Heparin	153-160	IGAN1	Homo sapiens	242-246
21095260-10	2011	In conclusion, heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE by changing the conformation of HMGB1.	Heparin	15-22	high mobility group box 1	Mus musculus	40-45
21095260-10	2011	In conclusion, heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE by changing the conformation of HMGB1.	Heparin	15-22	high mobility group box 1	Mus musculus	73-78
18716314-1	2008	Low-molecular-weight heparins (LMWHs) differ considerably in their influence on clotting tests and release of tissue factor pathway inhibitor (TFPI).	Heparin	21-29	tissue factor pathway inhibitor	Homo sapiens	110-141
18716314-1	2008	Low-molecular-weight heparins (LMWHs) differ considerably in their influence on clotting tests and release of tissue factor pathway inhibitor (TFPI).	Heparin	21-29	tissue factor pathway inhibitor	Homo sapiens	143-147
18449905-5	2008	Heparin was found to suppress the mRNA expressions of osterix, Runx2, ALP and osteocalcin, as well as phosphorylation of Smad1/5/8 and p38 MAPK.	Heparin	0-7	SMAD family member 1	Homo sapiens	121-130
18449905-6	2008	Further, heparin bound to both BMP-2 and BMP receptor (BMPR).	Heparin	9-16	bone morphogenetic protein 2	Homo sapiens	31-36
18449905-7	2008	These results suggest that heparin suppresses BMP-2-BMPR binding, and inhibits BMP-2 osteogenic activity in vitro.	Heparin	27-34	bone morphogenetic protein 2	Homo sapiens	46-51
18449905-7	2008	These results suggest that heparin suppresses BMP-2-BMPR binding, and inhibits BMP-2 osteogenic activity in vitro.	Heparin	27-34	bone morphogenetic protein 2	Homo sapiens	79-84
18715996-5	2008	Among the ephrins tested, including ephrin-A1, -A2, -A5, -B1, and -B2, only ephrin-A3 binds heparin or heparan sulfate.	Heparin	92-99	ephrin A3	Mus musculus	76-85
17244320-0	2007	Therapeutic angiogenesis induced by controlled release of fibroblast growth factor-2 from injectable chitosan/non-anticoagulant heparin hydrogel in a rat hindlimb ischemia model.	Heparin	128-135	fibroblast growth factor 2	Rattus norvegicus	58-84
17088546-3	2006	We demonstrate here that the N-terminal coiled-coil domain of Angptl-4 binds transiently to LPL and that the interaction results in conversion of the enzyme from catalytically active dimers to inactive, but still folded, monomers with decreased affinity for heparin.	Heparin	258-265	angiopoietin-like 4	Rattus norvegicus	62-70
21095260-10	2011	In conclusion, heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE by changing the conformation of HMGB1.	Heparin	15-22	high mobility group box 1	Mus musculus	73-78
21360640-8	2011	In conclusion, the results of this study clearly demonstrate that the action of heparin in the regulation of melanoma cell adhesion and migration involves a p53/FAK/signaling pathway, which may be of importance in molecular targeted therapy of the disease.	Heparin	80-87	protein tyrosine kinase 2	Homo sapiens	161-164
16940054-3	2006	Treatment with recombinant neprilysin, but not enzymatically inactive neprilysin, resulted in a slight increase in basic fibroblast growth factor electrophoretic mobility from proteolytic cleavage between amino acids Leu-135 and Gly-136, which was inhibited by the neutral endopeptidase inhibitor CGS24592 and heparin.	Heparin	310-317	membrane metallo endopeptidase	Mus musculus	27-37
21094153-0	2011	Studies on the effects of heparin products on pregnancy-associated plasma protein A.	Heparin	26-33	pappalysin 1	Homo sapiens	46-83
16794256-7	2006	In contrast, SP-B mRNA abundance was increased by heparin in a dose- and sulfation-dependent manner when used in combination with FGF-1.	Heparin	50-57	surfactant protein B	Homo sapiens	13-17
19378419-10	2008	Soluble heparin and K252a, an inhibitor of Trk, blocked CTGF-induced production of the above chemokines and the activation of the above signaling proteins.	Heparin	8-15	neurotrophic receptor tyrosine kinase 1	Homo sapiens	43-46
21094153-1	2011	BACKGROUND: Intravenous low molecular weight (LMWH) and unfractionated heparin (UFH) increase the circulating concentrations of pregnancy-associated plasma protein A (PAPP-A), a novel cardiac risk marker, in haemodialysis and coronary angiography patients.	Heparin	46-50	pappalysin 1	Homo sapiens	128-165
21094153-1	2011	BACKGROUND: Intravenous low molecular weight (LMWH) and unfractionated heparin (UFH) increase the circulating concentrations of pregnancy-associated plasma protein A (PAPP-A), a novel cardiac risk marker, in haemodialysis and coronary angiography patients.	Heparin	46-50	pappalysin 1	Homo sapiens	167-173
18455220-8	2008	EDN release was also induced by lysine-coated beads with cytokines (67.1 ng/100 microL) and blocked by heparin.	Heparin	103-110	ribonuclease A family member 2	Homo sapiens	0-3
16873726-1	2006	OBJECTIVE: Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by antibodies that recognize positively charged platelet factor 4 (PF4), bound to the polyanion, heparin.	Heparin	11-18	platelet factor 4	Homo sapiens	157-160
21094153-1	2011	BACKGROUND: Intravenous low molecular weight (LMWH) and unfractionated heparin (UFH) increase the circulating concentrations of pregnancy-associated plasma protein A (PAPP-A), a novel cardiac risk marker, in haemodialysis and coronary angiography patients.	Heparin	71-78	pappalysin 1	Homo sapiens	128-165
16873726-1	2006	OBJECTIVE: Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by antibodies that recognize positively charged platelet factor 4 (PF4), bound to the polyanion, heparin.	Heparin	187-194	platelet factor 4	Homo sapiens	157-160
16873726-4	2006	To better understand these findings, we analyzed the molecular structure of the complexes formed between PF4 and UFH, LMWH, or fondaparinux.	Heparin	113-116	platelet factor 4	Homo sapiens	105-108
21094153-1	2011	BACKGROUND: Intravenous low molecular weight (LMWH) and unfractionated heparin (UFH) increase the circulating concentrations of pregnancy-associated plasma protein A (PAPP-A), a novel cardiac risk marker, in haemodialysis and coronary angiography patients.	Heparin	71-78	pappalysin 1	Homo sapiens	167-173
16873726-5	2006	METHODS AND RESULTS: By atomic force microscopy and photon correlation spectroscopy, we show that with any of the 3 polyanions, but in the order, UFH&gt;LMWH&gt;&gt;fondaparinux--PF4 forms clusters in which PF4 tetramers become closely apposed, and to which anti-PF4/heparin antibodies bind.	Heparin	146-149	platelet factor 4	Homo sapiens	179-182
16873726-5	2006	METHODS AND RESULTS: By atomic force microscopy and photon correlation spectroscopy, we show that with any of the 3 polyanions, but in the order, UFH&gt;LMWH&gt;&gt;fondaparinux--PF4 forms clusters in which PF4 tetramers become closely apposed, and to which anti-PF4/heparin antibodies bind.	Heparin	146-149	platelet factor 4	Homo sapiens	207-210
19051709-4	2008	Heparin, in the affected individual binds with platelet factor 4 (PF-4) and forms a highly antigenic Heparin PF-4 complex which leads to the generation of specific IgG Heparin PF4 antibodies (also called HIT antibodies).	Heparin	0-7	platelet factor 4	Homo sapiens	66-70
19051709-4	2008	Heparin, in the affected individual binds with platelet factor 4 (PF-4) and forms a highly antigenic Heparin PF-4 complex which leads to the generation of specific IgG Heparin PF4 antibodies (also called HIT antibodies).	Heparin	0-7	platelet factor 4	Homo sapiens	109-113
21094153-1	2011	BACKGROUND: Intravenous low molecular weight (LMWH) and unfractionated heparin (UFH) increase the circulating concentrations of pregnancy-associated plasma protein A (PAPP-A), a novel cardiac risk marker, in haemodialysis and coronary angiography patients.	Heparin	80-83	pappalysin 1	Homo sapiens	128-165
16982928-6	2006	Finally, simultaneous cell incubation with the polyanion molecules, poly-L-glutamic acid or heparin, restored MMP-1 gene expression but incompletely inhibited MBP- and EPO-induced transcriptional effects as well as endothelin-1 and PDGF-AB release, suggesting that cationic proteins act partially through their cationic charge.	Heparin	92-99	myelin basic protein	Homo sapiens	159-162
21094153-1	2011	BACKGROUND: Intravenous low molecular weight (LMWH) and unfractionated heparin (UFH) increase the circulating concentrations of pregnancy-associated plasma protein A (PAPP-A), a novel cardiac risk marker, in haemodialysis and coronary angiography patients.	Heparin	80-83	pappalysin 1	Homo sapiens	167-173
16940188-6	2006	We confirmed previous reports that heparin inhibits the IFN-gamma-dependent production of CXCR3 chemokine ligands using atherosclerotic coronary arteries in organ culture.	Heparin	35-42	C-X-C motif chemokine receptor 3	Homo sapiens	90-95
16940188-7	2006	In addition to prolonged treatment decreasing chemokine secretion, heparin rapidly displaced membrane-associated IP-10 from cultured endothelial cells that did not express CXCR3 and reduced the IP-10-dependent transendothelial migration of T helper cells under conditions of venular shear stress.	Heparin	67-74	C-X-C motif chemokine receptor 3	Homo sapiens	172-177
16940188-10	2006	Disruption of CXCR3+ Th1 cell trafficking to arteriosclerotic arteries may contribute to the therapeutic efficacy of heparin in inflammatory arterial diseases, and nonanticoagulant heparin derivatives may represent a novel antiinflammatory strategy.	Heparin	117-124	C-X-C motif chemokine receptor 3	Homo sapiens	14-19
18589060-1	2008	BACKGROUND: Antibodies against the "self" protein, platelet factor 4 (PF4), bound to heparin-the cause of immune heparin-induced thrombocytopenia-are believed invariably to be triggered by preceding heparin therapy.	Heparin	85-92	platelet factor 4	Homo sapiens	70-73
21094153-4	2011	The interaction between heparin products and free PAPP-A was studied with gel filtration.	Heparin	24-31	pappalysin 1	Homo sapiens	50-56
18160611-0	2008	Further insight into the heparin-releasable and glycosylphosphatidylinositol-lipid--anchored forms of tissue factor pathway inhibitor.	Heparin	25-32	tissue factor pathway inhibitor	Homo sapiens	102-133
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	44-51	TNF receptor superfamily member 11b	Homo sapiens	31-34
18160611-1	2008	The release of tissue factor pathway inhibitor (TFPI) from human umbilical vein endothelial cells (HUVECs) was investigated using heparin and phospholipase C. The experiment included incubating HUVECs with 0, 1, or 10 U/mL heparin diluted in Dulbecco Modified Eagle"s Medium plus 5% fetal calf serum for 1 or 24 hours.	Heparin	130-137	tissue factor pathway inhibitor	Homo sapiens	15-46
21094153-5	2011	RESULTS: After intravenous UFH and LMWH free PAPP-A increased significantly but bivalirudin had no effect.	Heparin	35-39	pappalysin 1	Homo sapiens	45-51
18160611-1	2008	The release of tissue factor pathway inhibitor (TFPI) from human umbilical vein endothelial cells (HUVECs) was investigated using heparin and phospholipase C. The experiment included incubating HUVECs with 0, 1, or 10 U/mL heparin diluted in Dulbecco Modified Eagle"s Medium plus 5% fetal calf serum for 1 or 24 hours.	Heparin	130-137	tissue factor pathway inhibitor	Homo sapiens	48-52
18160611-1	2008	The release of tissue factor pathway inhibitor (TFPI) from human umbilical vein endothelial cells (HUVECs) was investigated using heparin and phospholipase C. The experiment included incubating HUVECs with 0, 1, or 10 U/mL heparin diluted in Dulbecco Modified Eagle"s Medium plus 5% fetal calf serum for 1 or 24 hours.	Heparin	223-230	tissue factor pathway inhibitor	Homo sapiens	15-46
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	44-51	TNF receptor superfamily member 11b	Homo sapiens	118-121
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	44-51	TNF receptor superfamily member 11b	Homo sapiens	118-121
18160611-1	2008	The release of tissue factor pathway inhibitor (TFPI) from human umbilical vein endothelial cells (HUVECs) was investigated using heparin and phospholipase C. The experiment included incubating HUVECs with 0, 1, or 10 U/mL heparin diluted in Dulbecco Modified Eagle"s Medium plus 5% fetal calf serum for 1 or 24 hours.	Heparin	223-230	tissue factor pathway inhibitor	Homo sapiens	48-52
21094153-6	2011	After LMWH bolus in haemodialysis patients 85% of free PAPP-A was cleared with a half-life of 13.1 min and the rest with a half-life of 96.6 min.	Heparin	6-10	pappalysin 1	Homo sapiens	55-61
18160611-4	2008	Sequential treatment of HUVECs with phospholipase C and heparin was performed, and a trend was observed where GPI-anchored TFPI levels were increased after 1 hour of pretreatment with heparin but were decreased after 24 hours.	Heparin	56-63	tissue factor pathway inhibitor	Homo sapiens	123-127
18160611-4	2008	Sequential treatment of HUVECs with phospholipase C and heparin was performed, and a trend was observed where GPI-anchored TFPI levels were increased after 1 hour of pretreatment with heparin but were decreased after 24 hours.	Heparin	184-191	tissue factor pathway inhibitor	Homo sapiens	123-127
21094153-7	2011	Subcutaneous LMWH led to lower and slower free PAPP-A elevation.	Heparin	13-17	pappalysin 1	Homo sapiens	47-53
18160611-5	2008	Serum is a requirement for the heparin-dependent release of TFPI from HUVECs.	Heparin	31-38	tissue factor pathway inhibitor	Homo sapiens	60-64
16890321-2	2006	In the investigations reported here, a heparin-binding, coiled-coil peptide, PF4 ZIP, was employed to mediate the assembly of heparinized polymers.	Heparin	39-46	platelet factor 4	Homo sapiens	77-80
18160611-6	2008	Heparin pretreatment of HUVECs may affect levels of GPI anchored TFPI in a time and dose-dependent manner.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	65-69
16890321-4	2006	Results from these experiments indicate that PF4 ZIP demonstrates a higher heparin-binding affinity and heparin association rate when compared to the heparin-binding domains of antithrombin III (ATIII) and heparin-interacting protein (HIP).	Heparin	75-82	platelet factor 4	Homo sapiens	45-48
21094153-8	2011	PAPP-A extracted from plaque tissues was in free form and extraction was strongly enhanced by LMWH.	Heparin	94-98	pappalysin 1	Homo sapiens	0-6
21094153-9	2011	Heparin products increased the molecular size of free PAPP-A.	Heparin	0-7	pappalysin 1	Homo sapiens	54-60
21094153-10	2011	CONCLUSIONS: The heparin-induced PAPP-A elevation is seen in various patients and should be taken into account when PAPP-A is studied as a biomarker.	Heparin	17-24	pappalysin 1	Homo sapiens	33-39
16828079-7	2006	Our results indicate that shedding of heparin-binding-EGF, transactivation of EGF receptors plays a more general role in alpha1B-adrenoceptor phosphorylation than previously anticipated.	Heparin	38-45	epidermal growth factor like 1	Rattus norvegicus	54-57
21094153-10	2011	CONCLUSIONS: The heparin-induced PAPP-A elevation is seen in various patients and should be taken into account when PAPP-A is studied as a biomarker.	Heparin	17-24	pappalysin 1	Homo sapiens	116-122
16828079-7	2006	Our results indicate that shedding of heparin-binding-EGF, transactivation of EGF receptors plays a more general role in alpha1B-adrenoceptor phosphorylation than previously anticipated.	Heparin	38-45	epidermal growth factor like 1	Rattus norvegicus	78-81
16828079-7	2006	Our results indicate that shedding of heparin-binding-EGF, transactivation of EGF receptors plays a more general role in alpha1B-adrenoceptor phosphorylation than previously anticipated.	Heparin	38-45	adrenoceptor alpha 1B	Rattus norvegicus	121-141
18313401-1	2008	In this study, heparin-conjugated poly(l-lactide-co-glycolide) (PLGA) nanospheres (HCPNs) suspended in fibrin gel (group 1) were developed for a long-term delivery of BMP-2, and then used to address the hypothesis that a long-term delivery of BMP-2 would enhance ectopic bone formation compared to a short-term delivery at an equivalent dose.	Heparin	15-22	bone morphogenetic protein 2	Rattus norvegicus	167-172
18313401-1	2008	In this study, heparin-conjugated poly(l-lactide-co-glycolide) (PLGA) nanospheres (HCPNs) suspended in fibrin gel (group 1) were developed for a long-term delivery of BMP-2, and then used to address the hypothesis that a long-term delivery of BMP-2 would enhance ectopic bone formation compared to a short-term delivery at an equivalent dose.	Heparin	15-22	bone morphogenetic protein 2	Rattus norvegicus	243-248
18380923-3	2008	Heparin stimulates production of hepatocyte growth factor (HGF), which has key roles in tissue regeneration.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	33-57
18380923-3	2008	Heparin stimulates production of hepatocyte growth factor (HGF), which has key roles in tissue regeneration.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	59-62
16699957-0	2006	The apoptotic endonuclease DFF40/CAD is inhibited by RNA, heparin and other polyanions.	Heparin	58-65	DNA fragmentation factor subunit beta	Homo sapiens	27-32
20959601-1	2011	A clinically important adverse drug reaction, heparin-induced thrombocytopenia (HIT), is induced by antibodies specific for complexes of the chemokine platelet factor 4 (PF4) and the polyanion heparin.	Heparin	46-53	platelet factor 4	Homo sapiens	170-173
16699957-3	2006	In addition, other anionic polymers, like poly-glutamic acid and heparin also inhibit DFF40/CAD, the latter one being highly effective at nanomolar concentrations.	Heparin	65-72	DNA fragmentation factor subunit beta	Homo sapiens	86-91
18380923-5	2008	This induction of HGF by heparin or fucoidan and their oligosaccharide derivates occurs primarily at the level of translation, probably via the same mechanism.	Heparin	25-32	hepatocyte growth factor	Homo sapiens	18-21
20959601-2	2011	Even heparin-naive patients can generate anti-PF4/heparin IgG as early as day 4 of heparin treatment, suggesting preimmunization by antigens mimicking PF4/heparin complexes.	Heparin	5-12	platelet factor 4	Homo sapiens	46-49
18426686-2	2008	HIT is mainly caused by immunoglobulin G (IgG) class among anti-heparin/platelet factor 4 antibodies that bind to epitopes on platelet factor 4 (PF4) released from activated platelets that developed when it forms complexes with heparin.	Heparin	64-71	platelet factor 4	Homo sapiens	145-148
16858650-5	2006	The bFGF loaded PLGA-heparin microspheres were tested for in vitro release and in vivo angiogenic activity.	Heparin	21-28	fibroblast growth factor 2	Mus musculus	4-8
20959601-2	2011	Even heparin-naive patients can generate anti-PF4/heparin IgG as early as day 4 of heparin treatment, suggesting preimmunization by antigens mimicking PF4/heparin complexes.	Heparin	5-12	platelet factor 4	Homo sapiens	151-154
16858650-8	2006	PLGA-heparin microspheres released out bFGF in a more sustained manner with a smaller extent of initial burst than PLGA microspheres, indicating that surface immobilized heparin controlled the release rate of bFGF.	Heparin	5-12	fibroblast growth factor 2	Mus musculus	39-43
16858650-8	2006	PLGA-heparin microspheres released out bFGF in a more sustained manner with a smaller extent of initial burst than PLGA microspheres, indicating that surface immobilized heparin controlled the release rate of bFGF.	Heparin	5-12	fibroblast growth factor 2	Mus musculus	209-213
20959601-3	2011	These antibodies probably result from bacterial infections, as (1) PF4 bound charge-dependently to various bacteria, (2) human heparin-induced anti-PF4/heparin antibodies cross-reacted with PF4-coated Staphylococcus aureus and Escherichia coli, and (3) mice developed anti-PF4/heparin antibodies during polymicrobial sepsis without heparin application.	Heparin	127-134	platelet factor 4	Homo sapiens	67-70
16858650-9	2006	Subcutaneous implantation of bFGF loaded PLGA-heparin microspheres in mice significantly induced the formation of new vascular microvessels.	Heparin	46-53	fibroblast growth factor 2	Mus musculus	29-33
18039685-0	2008	Biochemical characterization of phospholipids, sulfatide and heparin as potent stimulators for autophosphorylation of GSK-3beta and the GSK-3beta-mediated phosphorylation of myelin basic protein in vitro.	Heparin	61-68	glycogen synthase kinase 3 beta	Homo sapiens	118-127
16858650-11	2006	bFGF loaded PLGA-HP microspheres showed sustained release profiles of bFGF in vitro, demonstrating reversible and specific binding of bFGF to immobilized heparin.	Heparin	154-161	fibroblast growth factor 2	Mus musculus	0-4
20959601-3	2011	These antibodies probably result from bacterial infections, as (1) PF4 bound charge-dependently to various bacteria, (2) human heparin-induced anti-PF4/heparin antibodies cross-reacted with PF4-coated Staphylococcus aureus and Escherichia coli, and (3) mice developed anti-PF4/heparin antibodies during polymicrobial sepsis without heparin application.	Heparin	127-134	platelet factor 4	Homo sapiens	148-151
18039685-0	2008	Biochemical characterization of phospholipids, sulfatide and heparin as potent stimulators for autophosphorylation of GSK-3beta and the GSK-3beta-mediated phosphorylation of myelin basic protein in vitro.	Heparin	61-68	glycogen synthase kinase 3 beta	Homo sapiens	136-145
18039685-0	2008	Biochemical characterization of phospholipids, sulfatide and heparin as potent stimulators for autophosphorylation of GSK-3beta and the GSK-3beta-mediated phosphorylation of myelin basic protein in vitro.	Heparin	61-68	myelin basic protein	Homo sapiens	174-194
20959601-3	2011	These antibodies probably result from bacterial infections, as (1) PF4 bound charge-dependently to various bacteria, (2) human heparin-induced anti-PF4/heparin antibodies cross-reacted with PF4-coated Staphylococcus aureus and Escherichia coli, and (3) mice developed anti-PF4/heparin antibodies during polymicrobial sepsis without heparin application.	Heparin	127-134	platelet factor 4	Homo sapiens	148-151
18039685-1	2008	The stimulatory effects of SH (sulfatide and heparin) and two phospholipids (PI and PS) on autophosphorylation of GSK-3beta and the GSK-3beta-mediated phosphorylation of myelin basic protein (MBP) and two synthetic MBP peptides (M86 and M156) were comparatively examined in vitro.	Heparin	45-52	glycogen synthase kinase 3 beta	Homo sapiens	114-123
18039685-1	2008	The stimulatory effects of SH (sulfatide and heparin) and two phospholipids (PI and PS) on autophosphorylation of GSK-3beta and the GSK-3beta-mediated phosphorylation of myelin basic protein (MBP) and two synthetic MBP peptides (M86 and M156) were comparatively examined in vitro.	Heparin	45-52	glycogen synthase kinase 3 beta	Homo sapiens	132-141
20959601-6	2011	The same antigenic epitopes are expressed when pharmacologic heparin binds to platelets augmenting formation of PF4 complexes.	Heparin	61-68	platelet factor 4	Homo sapiens	112-115
18039685-2	2008	It was found that (i) both PI and SH highly stimulated the GSK-3beta-mediated phosphorylation of MBP, but not glycogen synthase, and two MBP peptides through their direct binding to these substrates and (ii) both PI and heparin, as compared with sulfatide, highly stimulated autophosphorylation of GSK-3beta.	Heparin	220-227	glycogen synthase kinase 3 beta	Homo sapiens	59-68
18039685-2	2008	It was found that (i) both PI and SH highly stimulated the GSK-3beta-mediated phosphorylation of MBP, but not glycogen synthase, and two MBP peptides through their direct binding to these substrates and (ii) both PI and heparin, as compared with sulfatide, highly stimulated autophosphorylation of GSK-3beta.	Heparin	220-227	myelin basic protein	Homo sapiens	97-100
20980681-2	2011	We found that CXCL4L1 has lower affinity for heparin and chondroitin sulfate-E than platelet factor-4 (CXCL4) and showed that CXCL10 and CXCL4L1 could displace each other on microvascular endothelial cells.	Heparin	45-52	platelet factor 4	Homo sapiens	14-19
18039685-4	2008	Under our experimental condition, similar stimulatory effects of PI and heparin were observed with the GSK-3beta-mediated phosphorylation of tau protein (TP) in vitro.	Heparin	72-79	glycogen synthase kinase 3 beta	Homo sapiens	103-112
19003601-5	2008	CHI3L1 is a nonhydrolytic member of the human chitinase family that binds chitin tightly and heparin at lower affinity.	Heparin	93-100	chitinase 3 like 1	Homo sapiens	0-6
16169188-1	2006	The low affinity receptor for immunoglobulin G, FcgammaRIIA, is expressed in human platelets, mediates heparin-induced thrombocytopenia and participates to platelet activation induced by von Willebrand factor.	Heparin	103-110	Fc gamma receptor IIa	Homo sapiens	48-59
16730571-8	2006	RESULTS: Compared with unmodified plasma, heparin significantly prolonged R and essentially reduced MTG and MG to the limits of detection in an activity-dependent fashion.	Heparin	42-49	serine protease 3	Homo sapiens	100-103
21041299-6	2011	To block the inhibitory effects of PF4 on TAFI activation, heparin derivatives were tested for their ability to retain high affinity binding to PF4 despite having greatly diminished anticoagulant activity.	Heparin	59-66	platelet factor 4	Homo sapiens	144-147
16628723-2	2006	We prospectively investigated the prevalence of heparin-induced platelet-reactive antibodies in a cohort of 38 pediatric hemodialysis patients, by means of heparin/platelet factor 4 (H/PF4) ELISA and heparin-induced platelet activation assay (HIPA).	Heparin	48-55	platelet factor 4	Homo sapiens	185-188
16628723-10	2006	In conclusion, heparin induces the transient production of anti-H/PF4 antibodies in children undergoing hemodialysis, but other abnormalities probably contribute to hypercoagulability.	Heparin	15-22	platelet factor 4	Homo sapiens	66-69
19343162-1	2008	BACKGROUND: Clinical studies have clearly revealed that low-molecular-weight heparins (LMWHs) are an effective alternative to unfractionated heparin in the therapy of acute coronary syndrome (ACS); however, data on the comparison of different LMWHs are sparse.	Heparin	77-85	acyl-CoA synthetase long chain family member 3	Homo sapiens	192-195
19343162-1	2008	BACKGROUND: Clinical studies have clearly revealed that low-molecular-weight heparins (LMWHs) are an effective alternative to unfractionated heparin in the therapy of acute coronary syndrome (ACS); however, data on the comparison of different LMWHs are sparse.	Heparin	77-84	acyl-CoA synthetase long chain family member 3	Homo sapiens	192-195
20925654-6	2011	These amino acids, when introduced in the non-heparin-binding ephrin-B1, conferred the heparin-binding property.	Heparin	46-53	ephrin B1	Homo sapiens	62-71
19099244-3	2008	Heparin affinity chromatography is an easy step that provides a major enrichment, particularly for sFRP-1 and sFRP-2.	Heparin	0-7	secreted frizzled related protein 1	Homo sapiens	99-105
17580326-9	2007	This demonstrates that both F105 and F119 interact with cell-surface heparan sulfate proteoglycans, suggesting that FGF-2 has two heparin binding sites.	Heparin	130-137	fibroblast growth factor 2	Mus musculus	116-121
17699253-1	2006	A previous trial showed that treatment of children with severe IgA nephropathy (IgAN) using prednisolone, azathioprine, heparin-warfarin, and dipyridamole for 2 yr early in the course of disease reduced the severity of immunologic renal injury and prevented any increase in the percentage of sclerosed glomeruli.	Heparin	120-127	IGAN1	Homo sapiens	63-78
17699253-1	2006	A previous trial showed that treatment of children with severe IgA nephropathy (IgAN) using prednisolone, azathioprine, heparin-warfarin, and dipyridamole for 2 yr early in the course of disease reduced the severity of immunologic renal injury and prevented any increase in the percentage of sclerosed glomeruli.	Heparin	120-127	IGAN1	Homo sapiens	80-84
20925654-6	2011	These amino acids, when introduced in the non-heparin-binding ephrin-B1, conferred the heparin-binding property.	Heparin	87-94	ephrin B1	Homo sapiens	62-71
20880582-3	2011	BMP-2 was then immobilized on the heparin-grafted Ti surfaces.	Heparin	34-41	bone morphogenetic protein 2	Homo sapiens	0-5
16466367-1	2006	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is usually caused by anti-platelet factor 4 (PF4)/heparin antibodies, leading to intravascular platelet activation.	Heparin	12-19	platelet factor 4	Homo sapiens	96-99
17722079-1	2007	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize platelet factor 4//heparin (PF4/H) complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	126-131
20946474-5	2011	However, we recently demonstrated that co-expression of MT1-MMP and HB-EGF in gastric carcinoma cells leads to cleavage of HB-EGF within its N-terminal heparin-binding region, converting it into a potent heparin-independent growth factor.	Heparin	152-159	matrix metallopeptidase 14	Homo sapiens	56-63
17936096-6	2007	Interestingly, the natural substrate HS did not cause a secondary structural change in the enzyme, whereas heparin and chondroitin sulfate did, both of which also exhibited similar high affinity binding to 3-OST-3A compared to HS as detected by isothermal fluorescence titrations.	Heparin	107-114	heparan sulfate-glucosamine 3-sulfotransferase 3A1	Homo sapiens	206-214
16304054-5	2006	Heparin is not required for HIT antibody binding but shifts the concentration of PF4 needed for optimal surface antigenicity to higher levels.	Heparin	0-7	platelet factor 4	Homo sapiens	81-84
16146647-0	2006	Long-term and zero-order release of basic fibroblast growth factor from heparin-conjugated poly(L-lactide-co-glycolide) nanospheres and fibrin gel.	Heparin	72-79	fibroblast growth factor 2	Mus musculus	36-66
16146647-2	2006	In this study, novel heparin-conjugated poly(L-lactide-co-glycolide) (PLGA) nanospheres (HCPNs) were developed for long-term, zero-order delivery of bFGF.	Heparin	21-28	fibroblast growth factor 2	Mus musculus	149-153
20970218-7	2011	Heparin acted at 2 distinct steps of osteoclastogenesis from human CD14(+) cells: first, heparin strongly decreased the adherence of osteoclast precursors, and secondly inhibited osteoclasts to spread and to be active.	Heparin	0-7	CD14 molecule	Homo sapiens	67-71
16520718-0	2006	Inhibitory effect of C-reactive protein on the release of tissue factor pathway inhibitor from human endothelial cells: reversal by low molecular weight heparin.	Heparin	153-160	tissue factor pathway inhibitor	Homo sapiens	58-89
16520718-1	2006	AIM: The effects of C-reactive protein (CRP) and low molecular weight heparin (LMWH) on the release of tissue factor pathway inhibitor (TFPI) from human umbilical vein endothelial cells (HUVECs) were examined.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	103-134
16520718-1	2006	AIM: The effects of C-reactive protein (CRP) and low molecular weight heparin (LMWH) on the release of tissue factor pathway inhibitor (TFPI) from human umbilical vein endothelial cells (HUVECs) were examined.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	136-140
17717051-5	2007	The cellular uptake of Pax4 PTD can be completely blocked by heparin, whereas cytochalasin D and amiloride were partially effective in blocking the Pax4 protein entry.	Heparin	61-68	paired box 4	Homo sapiens	23-27
17699512-0	2007	Binding between the integrin alphaXbeta2 (CD11c/CD18) and heparin.	Heparin	58-65	integrin subunit alpha X	Homo sapiens	42-47
17699512-2	2007	Heparin, a highly sulfated polymer of uronic acids and glucosamine, binds strongly to the integrin receptor alphaXbeta2 (p150,95, CD11c/CD18).	Heparin	0-7	integrin subunit alpha X	Homo sapiens	130-135
22160026-1	2011	Heparin-induced thrombocytopenia (HIT) is a prothrombotic drug reaction caused by platelet-activating IgG antibodies that recognize platelet factor 4 (PF4)/polyanion complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	151-154
17632078-5	2007	Moreover, heparin-binding fractions obtained from serum also stimulated osteoblastic differentiation in the presence of BMP-4.	Heparin	10-17	bone morphogenetic protein 4	Homo sapiens	120-125
17662276-8	2007	5-Amino-2-NMS binds to the heparin-binding site of FGF1 and FGF2 and thus may be a promising substance for the local treatment of retinal neovascularization.	Heparin	27-34	fibroblast growth factor 2	Mus musculus	60-64
17611187-7	2007	RESULTS: Both forms of heparin significantly reduced HGF-induced invasion in the SGHPL-4 cell line.	Heparin	23-30	hepatocyte growth factor	Homo sapiens	53-56
16520718-8	2006	The amount of endothelial TFPI released was dependent on the heparin molecular weight distribution, with minimal effect at 3000 Da and maximum at 8000 to 12,000 Da.	Heparin	61-68	tissue factor pathway inhibitor	Homo sapiens	26-30
16225459-8	2006	Moreover, we investigated the location of the heparin-binding site of human XT-I using the truncated mutants.	Heparin	46-53	xylosyltransferase 1	Homo sapiens	76-80
16225459-10	2006	The effect of heparin or UDP on the XT-I activity of all mutants was not significantly different from that of the wild-type.	Heparin	14-21	xylosyltransferase 1	Homo sapiens	36-40
16461305-8	2006	Both heparins increased TFPI antigen release in HMEC-1 and HUVEC.	Heparin	5-13	tissue factor pathway inhibitor	Homo sapiens	24-28
22160026-2	2011	Platelet activation assays, such as the serotonin-release assay, are superior to PF4-dependent immunoassays in discerning which heparin-induced antibodies are clinically relevant.	Heparin	128-135	platelet factor 4	Homo sapiens	81-84
21506142-5	2011	We report two patients with HIT who underwent successful CPB with heparin anticoagulation following plasma exchange (PE) to reduce heparin/PF4 antibody titers.	Heparin	66-73	platelet factor 4	Homo sapiens	139-142
16310171-4	2006	A non-linear relationship was found between degree of sulfation and binding affinity or enzyme inhibition properties, showing a composite correlation between heparin charge density and interference with EL/CatG activity.	Heparin	158-165	elastase, neutrophil expressed	Homo sapiens	203-205
18481204-3	2007	CCN5 is a secreted heparin- and estrogen-regulated matricellular protein that inhibits vertebrate smooth muscle cell proliferation and motility.	Heparin	19-26	cellular communication network factor 5	Mus musculus	0-4
16955639-9	2006	Heparin plasma is an attractive alternative to the established EDTA samples which can be used for BNP determination.	Heparin	0-7	natriuretic peptide B	Homo sapiens	98-101
20852126-1	2010	The immune response in heparin-induced thrombocytopenia is initiated by and directed to large multimolecular complexes of platelet factor 4 (PF4) and heparin (H).	Heparin	23-30	platelet factor 4	Homo sapiens	141-144
16955639-10	2006	This flexibility allows the simultaneous determination of CK, CK-MB, cTnI and BNP on a single heparin specimen, which facilitates blood collection for clinicians and nursing staff in an emergency unit.	Heparin	94-101	natriuretic peptide B	Homo sapiens	78-81
15869786-8	2006	HCII-IIa complexes of all P1 variants were stable in the absence of heparin, but those of the L444K and L444R variants released active IIa over time with heparin.	Heparin	68-75	serpin family D member 1	Homo sapiens	0-4
15869786-8	2006	HCII-IIa complexes of all P1 variants were stable in the absence of heparin, but those of the L444K and L444R variants released active IIa over time with heparin.	Heparin	154-161	serpin family D member 1	Homo sapiens	0-4
17500071-2	2007	sFRP-1 and Wnts are heparin-binding proteins, and their interaction can be stabilized by heparin in vitro.	Heparin	20-27	secreted frizzled related protein 1	Homo sapiens	0-6
17500071-3	2007	Here we report that heparin can specifically enhance recombinant sFRP-1 accumulation in a cell type-specific manner.	Heparin	20-27	secreted frizzled related protein 1	Homo sapiens	65-71
17500071-5	2007	Interestingly, further investigation uncovers that heparin can also affect the post-translational modification of sFRP-1.	Heparin	51-58	secreted frizzled related protein 1	Homo sapiens	114-120
15869786-11	2006	This is the first description of HCII-IIa complexes of transient stability forming in the absence of heparin, and may explain the extent to which the reactive centre loop of HCII differs from that of AT.	Heparin	101-108	serpin family D member 1	Homo sapiens	33-37
21058638-1	2010	Heparin and heparan sulfate mediated basic fibroblast growth factor (bFGF) signaling plays an important role in skeletal muscle homeostasis by maintaining a balance between proliferation and differentiation of muscle progenitor cells.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	69-73
16215261-8	2005	We showed that dimerization of OPG results from noncovalent interactions mediated by the death domains and to a lesser extent by a C-terminal heparin-binding region.	Heparin	142-149	TNF receptor superfamily member 11b	Homo sapiens	31-34
17524524-3	2007	Binding to heparin-acrylic beads was markedly reduced when lysine in position 134 of bFGF was replaced by alanine.	Heparin	11-18	fibroblast growth factor 2	Rattus norvegicus	85-89
17524524-7	2007	In conclusion, lysine at position 134 of bFGF is essential for bFGF to bind heparin, then to interact with its receptor and, subsequently, to protect neurons against damage.	Heparin	76-83	fibroblast growth factor 2	Rattus norvegicus	41-45
17524524-7	2007	In conclusion, lysine at position 134 of bFGF is essential for bFGF to bind heparin, then to interact with its receptor and, subsequently, to protect neurons against damage.	Heparin	76-83	fibroblast growth factor 2	Rattus norvegicus	63-67
20688960-2	2010	Because interactions with glycosaminoglycans play a crucial role in chemokines activity, we determined the binding parameters of CXCL4 and CXCL4L1 for heparin, heparan sulfate, and chondroitin sulfate B.	Heparin	151-158	platelet factor 4	Homo sapiens	129-134
17388803-4	2007	In models of arterial injury, FXII or FXI null mice are protected from formation of platelet rich occlusive thrombi to a degree similar to that seen in FIX deficient mice (a model for the severe bleeding disorder hemophilia B) or to wild type mice treated with high dose heparin.	Heparin	271-278	coagulation factor XII (Hageman factor)	Mus musculus	30-34
16280424-4	2005	RESULTS: Intravenous infusion of heparin plus the lipid emulsion reduced peripheral T cell membrane fluidity and altered lipid raft organization, both of which were associated with reduced T cell proliferation after stimulation with CD3 plus CD28.	Heparin	33-40	CD28 molecule	Homo sapiens	242-246
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Heparin	63-70	serpin family D member 1	Homo sapiens	84-88
16105849-8	2005	CONCLUSION: Our results demonstrate that in patients, without heparin pre-treatment, referred for PCR, a high serum level of HGF is an independent predictor of clinical events during follow-up and is correlated with other surrogate measures of the activity of atherosclerosis.	Heparin	62-69	hepatocyte growth factor	Homo sapiens	125-128
17339340-3	2007	Here, we present the crystal structures of FGF19 alone and FGF23 in complex with sucrose octasulfate, a disaccharide chemically related to heparin.	Heparin	139-146	fibroblast growth factor 19	Homo sapiens	43-48
17339340-4	2007	The conformation of the heparin-binding region between beta strands 10 and 12 in FGF19 and FGF23 diverges completely from the common conformation adopted by paracrine-acting FGFs.	Heparin	24-31	fibroblast growth factor 19	Homo sapiens	81-86
17339340-5	2007	A cleft between this region and the beta1-beta2 loop, the other heparin-binding region, precludes direct interaction between heparin/heparan sulfate and backbone atoms of FGF19/23.	Heparin	64-71	fibroblast growth factor 19	Homo sapiens	171-176
17339340-5	2007	A cleft between this region and the beta1-beta2 loop, the other heparin-binding region, precludes direct interaction between heparin/heparan sulfate and backbone atoms of FGF19/23.	Heparin	125-132	fibroblast growth factor 19	Homo sapiens	171-176
17339340-7	2007	Klotho/betaKlotho have evolved as a compensatory mechanism for the poor ability of heparin/heparan sulfate to promote binding of FGF19, -21, and -23 to their cognate receptors.	Heparin	83-90	fibroblast growth factor 19	Homo sapiens	129-134
17460090-7	2007	These opposing effects on Ca2+ signals were both mediated by an increase in intracellular inositol 1,4,5-trisphosphate (IP3) levels, because they were blocked by heparin, an IP3 receptor antagonist, and reproduced by photolytic application of IP3.	Heparin	162-169	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	174-186
16351577-8	2005	This finding suggests the possibility for modeling of ex vivo establishment of correlation between plasma activity of FVIII and needed doses of heparin for appropriate management of heparin therapy.	Heparin	144-151	coagulation factor VIII	Homo sapiens	118-123
16351577-8	2005	This finding suggests the possibility for modeling of ex vivo establishment of correlation between plasma activity of FVIII and needed doses of heparin for appropriate management of heparin therapy.	Heparin	182-189	coagulation factor VIII	Homo sapiens	118-123
15936726-5	2005	Furthermore, we could demonstrate that the XT-I interacts strongly with heparin and that this glycosaminoglycan is a predominantly non-competitive inhibitor of the enzyme using the fragment bFGF (1-24) as xylose acceptor.	Heparin	72-79	xylosyltransferase 1	Homo sapiens	43-47
20975989-9	2010	In vitro assays demonstrated that the ocular fluid or soluble heparan sulfate or heparin inhibited the binding of VEGF-A and immobilized heparin or VEGF receptor 2 but not VEGF receptor 1.	Heparin	81-88	kinase insert domain protein receptor	Mus musculus	148-163
16004450-7	2005	Heparin-TBA (mixing ratio: 1, 5, and 10 wt % to PLCL), soluble in HFIP, was co-electrospun with PLCL to form a fabric.	Heparin	0-7	phospholipase C like 1 (inactive)	Homo sapiens	48-52
16004450-7	2005	Heparin-TBA (mixing ratio: 1, 5, and 10 wt % to PLCL), soluble in HFIP, was co-electrospun with PLCL to form a fabric.	Heparin	0-7	phospholipase C like 1 (inactive)	Homo sapiens	96-100
16004450-8	2005	TEM observation showed that heparin-TBA formed as a dispersed phase in a PLCL nanofiber.	Heparin	28-35	phospholipase C like 1 (inactive)	Homo sapiens	73-77
16004450-10	2005	The potential biomedical application of co-electrospun PLCL with type I collagen or heparin-TBA was discussed.	Heparin	84-91	phospholipase C like 1 (inactive)	Homo sapiens	55-59
17039513-5	2007	In this study, the ability of a novel platelet GPIIb/IIIa antagonist, a free acid form of roxifiban (XV459), to block platelet activation/aggregation in response to highly characterized heparin-PF4 antibody-positive plasma/heparin was examined using light transmittance aggregometry, serotonin release, and (125)I-fibrinogen binding assays to human platelets.	Heparin	186-193	platelet factor 4	Homo sapiens	194-197
20200993-1	2010	Midkine (Mdk) and pleiotrophin (Ptn) comprise a family of heparin-binding growth factors known primarily for their effects on neuronal cells.	Heparin	58-65	midkine	Mus musculus	0-7
17117469-5	2007	The addition of heparin to fibrin gel decreased the rate of NGF release from the fibrin gel.	Heparin	16-23	nerve growth factor	Rattus norvegicus	60-63
17258198-1	2007	Heparin influences numerous pleiotropic growth factors, including hepatocyte growth factor (HGF), partially by their release from endothelial and extracellular matrix stores.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	66-90
17258198-1	2007	Heparin influences numerous pleiotropic growth factors, including hepatocyte growth factor (HGF), partially by their release from endothelial and extracellular matrix stores.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	92-95
15882850-3	2005	The results thus obtained indicated that ESP and Lowdin charges gave the better results in heparin simulations, followed by Mulliken charges, and that the minimum-energy conformation of IdoA can be different from that observed by NMR spectroscopy by less than 1 Angstrom.	Heparin	91-98	protein tyrosine phosphatase receptor type V, pseudogene	Homo sapiens	41-44
15943814-6	2005	Interleukin-1beta (IL-1beta) alone, or in synergy with FGF-2/heparin strongly induced the gene in 3T3 fibroblasts.	Heparin	61-68	fibroblast growth factor 2	Mus musculus	55-60
20200993-1	2010	Midkine (Mdk) and pleiotrophin (Ptn) comprise a family of heparin-binding growth factors known primarily for their effects on neuronal cells.	Heparin	58-65	midkine	Mus musculus	9-12
15943814-11	2005	FGF-2-/heparin-induced, but not IL-1beta-induced responses were significantly suppressed by TGF-beta, possibly mediated by decreased mRNA stability.	Heparin	7-14	fibroblast growth factor 2	Mus musculus	0-5
20200993-1	2010	Midkine (Mdk) and pleiotrophin (Ptn) comprise a family of heparin-binding growth factors known primarily for their effects on neuronal cells.	Heparin	58-65	pleiotrophin	Mus musculus	18-30
20200993-1	2010	Midkine (Mdk) and pleiotrophin (Ptn) comprise a family of heparin-binding growth factors known primarily for their effects on neuronal cells.	Heparin	58-65	pleiotrophin	Mus musculus	32-35
17349901-1	2007	BACKGROUND: Patients with heparin-platelet factor 4 (PF4) antibodies, particularly platelet-activating ones, are at risk for heparin-induced thrombocytopenia if administered heparin.	Heparin	26-33	platelet factor 4	Homo sapiens	53-56
20547342-6	2010	In 2D collagen gel cultures, albumin synthesis of around 15 microg/well/day was detected and maintained for more than 18 days on HGF/heparin-immobilized collagen gels.	Heparin	133-140	hepatocyte growth factor	Homo sapiens	129-132
17349901-1	2007	BACKGROUND: Patients with heparin-platelet factor 4 (PF4) antibodies, particularly platelet-activating ones, are at risk for heparin-induced thrombocytopenia if administered heparin.	Heparin	125-132	platelet factor 4	Homo sapiens	26-51
17349901-1	2007	BACKGROUND: Patients with heparin-platelet factor 4 (PF4) antibodies, particularly platelet-activating ones, are at risk for heparin-induced thrombocytopenia if administered heparin.	Heparin	125-132	platelet factor 4	Homo sapiens	53-56
15910290-1	2005	Heparin-induced thrombocytopenia (HIT) is an adverse immune-mediated drug reaction in which antibodies are generated usually towards complexes of the soluble platelet protein platelet-factor-4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	175-192
20547342-9	2010	Taken together, the HGF/heparin-immobilized collagen system was effective for albumin synthesis by hepatocytes in both 2D film cultures and 3D gel cultures, and therefore shows good potential for tissue engineering use.	Heparin	24-31	hepatocyte growth factor	Homo sapiens	20-23
15784180-10	2005	On the other hand, DTL-A binding to heparin was effectively inhibited by dextran sulfate, fucoidan, whereas BSM showed insignificantly inhibitory effect.	Heparin	36-43	denticleless E3 ubiquitin protein ligase homolog	Homo sapiens	19-22
15784180-11	2005	DTL-A binding to heparin was not inhibited by D-GlcNAc and D-GalNAc.	Heparin	17-24	denticleless E3 ubiquitin protein ligase homolog	Homo sapiens	0-3
20587521-6	2010	MT1-MMP additionally cleaves HB-EGF and removes the NH(2)-terminal 20 amino acids that are important for binding heparin.	Heparin	113-120	matrix metallopeptidase 14	Homo sapiens	0-7
15945439-3	2005	The authors report the first case of a spontaneous spinal SDH occurring in conjunction with low-molecular-weight heparin use in a patient with a history of spinal radiotherapy.	Heparin	113-120	serine dehydratase	Homo sapiens	58-61
15731113-0	2005	Regulation of vascular smooth muscle proliferation by heparin: inhibition of cyclin-dependent kinase 2 activity by p27(kip1).	Heparin	54-61	cyclin dependent kinase 2	Homo sapiens	77-102
15731113-5	2005	Our results indicate that the heparin-induced block in G(1) to S phase transition is imposed by p27(kip1)-mediated inhibition of cyclin-dependent kinase 2 activity.	Heparin	30-37	cyclin dependent kinase 2	Homo sapiens	129-154
15731113-7	2005	We present evidence that heparin causes stabilization of p27(kip1) protein during G(1) phase and thereby prevents activation of cyclin-dependent kinase 2.	Heparin	25-32	cyclin dependent kinase 2	Homo sapiens	128-153
15748704-1	2005	Effect of unfractionated heparin (UFH), described as a cell-impermeant IP3 receptor antagonist, was studied on the capacitive Ca(2+) entry in non-permeabilized, intact cells, measuring the intracellular Ca(2+) levels using fluorescence microplate technique.	Heparin	34-37	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	71-83
17352757-1	2007	We describe synthetic extracellular matrix (sECM) hydrogel films composed of co-crosslinked thiolated derivatives of chondroitin 6-sulfate (CS) and heparin (HP) for controlled-release delivery of basic fibroblast growth factor (bFGF) to full-thickness wounds in genetically diabetic (db/db) mice.	Heparin	157-159	fibroblast growth factor 2	Mus musculus	196-226
17352757-1	2007	We describe synthetic extracellular matrix (sECM) hydrogel films composed of co-crosslinked thiolated derivatives of chondroitin 6-sulfate (CS) and heparin (HP) for controlled-release delivery of basic fibroblast growth factor (bFGF) to full-thickness wounds in genetically diabetic (db/db) mice.	Heparin	157-159	fibroblast growth factor 2	Mus musculus	228-232
17376263-5	2007	Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI.	Heparin	43-50	tissue factor pathway inhibitor	Homo sapiens	147-151
17376263-5	2007	Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI.	Heparin	75-82	tissue factor pathway inhibitor	Homo sapiens	147-151
17109210-4	2007	RESULTS: Heparin-DOCA inhibited capillary-like tubular structures of endothelial cells and bFGF-induced neovascularizations in Matrigel plug assays.	Heparin	9-16	fibroblast growth factor 2	Mus musculus	91-95
17109210-5	2007	Signaling experiments showed that heparin-DOCA significantly inhibited angiogenesis by suppressing the phosphorylation of FGFR and its downstream signal pathways (ERK and p38 MAPK activities).	Heparin	34-41	mitogen-activated protein kinase 14	Mus musculus	171-179
17109210-8	2007	CONCLUSION: Heparin-DOCA derivative exerted a significant antitumoral effect by inhibiting angiogenesis resulting from the disruption of FGF/FGFR and its downstream signal pathways, and could be applied to treat various angiogenic diseases.	Heparin	12-19	fibroblast growth factor 2	Mus musculus	137-140
16824584-0	2007	Molecular weight dependent tissue factor pathway inhibitor release by heparin and heparin oligosaccharides.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	27-58
19338998-12	2010	The expression of alpha-smooth muscle actin, Ras homology (Rho) A, Rho-associated coiled-coil-forming protein kinase (ROCK)-I, and ROCK-II was down-regulated by heparin administration.	Heparin	161-168	Rho associated coiled-coil containing protein kinase 1	Homo sapiens	67-125
16824584-1	2007	Heparin and low molecular weight heparins exert their vascular effects by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	85-116
16824584-1	2007	Heparin and low molecular weight heparins exert their vascular effects by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	118-122
16824584-1	2007	Heparin and low molecular weight heparins exert their vascular effects by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	33-41	tissue factor pathway inhibitor	Homo sapiens	85-116
16824584-1	2007	Heparin and low molecular weight heparins exert their vascular effects by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	33-41	tissue factor pathway inhibitor	Homo sapiens	118-122
16824584-2	2007	We compared the influence of molecular weight on the TFPI release by heparin and its fractions in a non-human primate model.	Heparin	69-76	tissue factor pathway inhibitor	Homo sapiens	53-57
16919311-2	2007	In this study we examined the in vitro effects of heparin and other glycosaminoglycans on TFPI mRNA-expression in cultivated human endothelial (Ea.hy 926) and in chondrosarcoma (SW 1353) cells.	Heparin	50-57	tissue factor pathway inhibitor	Homo sapiens	90-94
15755289-1	2005	Cardiopulmonary bypass (CPB) induces the release of platelet factor 4 (PF4) and patients are at risk of heparin-induced thrombocytopenia (HIT).	Heparin	104-111	platelet factor 4	Homo sapiens	71-74
15720347-8	2005	Unfractionated heparin and low molecular weight heparin (4 studies) were equally effective POR 1.01 (95% CI 0.67-1.52).	Heparin	15-22	ADP ribosylation factor interacting protein 2	Homo sapiens	91-96
15720347-8	2005	Unfractionated heparin and low molecular weight heparin (4 studies) were equally effective POR 1.01 (95% CI 0.67-1.52).	Heparin	48-55	ADP ribosylation factor interacting protein 2	Homo sapiens	91-96
16919311-6	2007	RESULTS: Stimulation of Ea.hy 926 cells with unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH) caused a time- and dose-dependent upregulation of TFPI-mRNA expression with LMWH showing the stronger effect.	Heparin	60-67	tissue factor pathway inhibitor	Homo sapiens	163-167
19338998-12	2010	The expression of alpha-smooth muscle actin, Ras homology (Rho) A, Rho-associated coiled-coil-forming protein kinase (ROCK)-I, and ROCK-II was down-regulated by heparin administration.	Heparin	161-168	Rho associated coiled-coil containing protein kinase 2	Homo sapiens	131-138
16919311-6	2007	RESULTS: Stimulation of Ea.hy 926 cells with unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH) caused a time- and dose-dependent upregulation of TFPI-mRNA expression with LMWH showing the stronger effect.	Heparin	69-72	tissue factor pathway inhibitor	Homo sapiens	163-167
16919311-6	2007	RESULTS: Stimulation of Ea.hy 926 cells with unfractionated heparin (UFH) or low-molecular-weight heparin (LMWH) caused a time- and dose-dependent upregulation of TFPI-mRNA expression with LMWH showing the stronger effect.	Heparin	98-105	tissue factor pathway inhibitor	Homo sapiens	163-167
20382221-10	2010	LTBP-2 was found to interact strongly in a heparin-inhibitable manner with cell surface HSPG syndecan-4, but showed no interaction with recombinant syndecan-2.	Heparin	43-50	syndecan 4	Homo sapiens	93-103
16919311-10	2007	As a conclusion, the determined heparin-induced upregulation of TFPI-mRNA expression can be considered a major component of the modulation of the anticoagulant properties of the endothelium.	Heparin	32-39	tissue factor pathway inhibitor	Homo sapiens	64-68
15578661-3	2005	As an alternative means of inhibition, we used heparin to mask the dystroglycan binding site of the laminin-1, known to overlap with heparin binding sites.	Heparin	47-54	dystroglycan 1	Homo sapiens	67-79
20230412-4	2010	This "apparent heparin resistance" is commonly due to high levels of factor VIII (FVIII).	Heparin	15-22	coagulation factor VIII	Homo sapiens	69-80
15699163-0	2005	Heparin binds to lipopolysaccharide (LPS)-binding protein, facilitates the transfer of LPS to CD14, and enhances LPS-induced activation of peripheral blood monocytes.	Heparin	0-7	CD14 molecule	Homo sapiens	94-98
15699163-5	2005	Using a fluorescence-based assay, we showed that clinically used heparin preparations significantly enhance the ability of LBP to catalytically disaggregate and transfer LPS to CD14, the LPS receptor.	Heparin	65-72	CD14 molecule	Homo sapiens	177-181
15620916-4	2005	Of these 144 patients, 41 underwent also a third procedure and were screened before each procedure for presence of antiheparin-PF4 antibodies and for clinical signs of heparin-induced thrombocytopenia.	Heparin	119-126	platelet factor 4	Homo sapiens	127-130
15620916-12	2005	In antiheparin-PF4 antibody positive patients, the complete avoidance of heparin can be achieved and may account for an uneventful perioperative course.	Heparin	7-14	platelet factor 4	Homo sapiens	15-18
17034986-1	2006	Heparin-induced thrombocytopenia (HIT) is a dangerous complication of heparin therapy caused by an antibody against heparin/Platelet Factor 4 (PF4) complex.	Heparin	0-7	platelet factor 4	Homo sapiens	116-141
17034986-1	2006	Heparin-induced thrombocytopenia (HIT) is a dangerous complication of heparin therapy caused by an antibody against heparin/Platelet Factor 4 (PF4) complex.	Heparin	0-7	platelet factor 4	Homo sapiens	143-146
17034986-1	2006	Heparin-induced thrombocytopenia (HIT) is a dangerous complication of heparin therapy caused by an antibody against heparin/Platelet Factor 4 (PF4) complex.	Heparin	70-77	platelet factor 4	Homo sapiens	116-141
17034986-1	2006	Heparin-induced thrombocytopenia (HIT) is a dangerous complication of heparin therapy caused by an antibody against heparin/Platelet Factor 4 (PF4) complex.	Heparin	70-77	platelet factor 4	Homo sapiens	143-146
16873726-5	2006	METHODS AND RESULTS: By atomic force microscopy and photon correlation spectroscopy, we show that with any of the 3 polyanions, but in the order, UFH&gt;LMWH&gt;&gt;fondaparinux--PF4 forms clusters in which PF4 tetramers become closely apposed, and to which anti-PF4/heparin antibodies bind.	Heparin	146-149	platelet factor 4	Homo sapiens	207-210
16805860-5	2006	Heparin did not affect A3-mediated binding of VWF and DeltaA1-VWF, but inhibited binding to horse tendon collagen of GST-A1 and DeltaA3-VWF.	Heparin	0-7	glutathione S-transferase alpha 1	Equus caballus	117-123
20230412-4	2010	This "apparent heparin resistance" is commonly due to high levels of factor VIII (FVIII).	Heparin	15-22	coagulation factor VIII	Homo sapiens	82-87
15635159-5	2005	However, heparin, dextran sulfate and hyaluronan stimulated the release of heparan sulfate PGs rather than chondroitin/dermatan sulfate PGs, whereas the release of both types of PGs was strongly stimulated by Na-SP.	Heparin	9-16	nuclear autoantigenic sperm protein	Bos taurus	209-214
20230412-6	2010	We hypothesized that at high FVIII levels, the heparin resistance encountered may be genuine rather than apparent and that higher doses of heparin may indeed be needed for an equivalent anticoagulant effect.	Heparin	47-54	coagulation factor VIII	Homo sapiens	29-34
16754660-0	2006	Heparin potentiates the in vivo ectopic bone formation induced by bone morphogenetic protein-2.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	66-94
20334464-9	2010	This patient had an elevated thyroxine level of 32.5 microg/dl, which suggested that an increased factor VIII level was the probable mechanism of heparin resistance.	Heparin	146-153	cytochrome c oxidase subunit 8A	Homo sapiens	105-109
16754660-6	2006	Heparin enhanced BMP-2-induced gene expression and Smad1/5/8 phosphorylation at 24 h and thereafter, although not within 12 h. Heparitinase treatment did not affect the response of cells to BMP-2.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	17-22
16754660-6	2006	Heparin enhanced BMP-2-induced gene expression and Smad1/5/8 phosphorylation at 24 h and thereafter, although not within 12 h. Heparitinase treatment did not affect the response of cells to BMP-2.	Heparin	0-7	SMAD family member 1	Homo sapiens	51-58
16754660-7	2006	In the presence of heparin, degradation of BMP-2 was blocked, and the half-life of BMP-2 in the culture medium was prolonged by nearly 20-fold.	Heparin	19-26	bone morphogenetic protein 2	Homo sapiens	43-48
16754660-7	2006	In the presence of heparin, degradation of BMP-2 was blocked, and the half-life of BMP-2 in the culture medium was prolonged by nearly 20-fold.	Heparin	19-26	bone morphogenetic protein 2	Homo sapiens	83-88
16754660-9	2006	Furthermore, simultaneous administration of BMP-2 and heparin in vivo dose-dependently induced larger amounts of mineralized bone tissue compared with BMP-2 alone.	Heparin	54-61	bone morphogenetic protein 2	Homo sapiens	151-156
15678271-0	2005	Comparative tissue factor pathway inhibitor release potential of heparins.	Heparin	65-73	tissue factor pathway inhibitor	Homo sapiens	12-43
15678271-1	2005	Tissue factor pathway inhibitor (TFPI) is released following the administration of unfractionated heparin, low-molecular-weight heparins, defibrotide and PI-88.	Heparin	98-105	tissue factor pathway inhibitor	Homo sapiens	0-31
15678271-1	2005	Tissue factor pathway inhibitor (TFPI) is released following the administration of unfractionated heparin, low-molecular-weight heparins, defibrotide and PI-88.	Heparin	98-105	tissue factor pathway inhibitor	Homo sapiens	33-37
15678271-1	2005	Tissue factor pathway inhibitor (TFPI) is released following the administration of unfractionated heparin, low-molecular-weight heparins, defibrotide and PI-88.	Heparin	128-136	tissue factor pathway inhibitor	Homo sapiens	0-31
15678271-1	2005	Tissue factor pathway inhibitor (TFPI) is released following the administration of unfractionated heparin, low-molecular-weight heparins, defibrotide and PI-88.	Heparin	128-136	tissue factor pathway inhibitor	Homo sapiens	33-37
15678271-4	2005	Following the administration of 1 mg/kg of heparin, gammaparin, and C3, the functional levels of TFPI at 5 minutes were 2.40, 2.56, and 1.08 U/mL and the corresponding TFPI immunologic levels were 4.3-, 4.0-, and 2.1-fold, increased, respectively, over the baseline value.	Heparin	43-50	tissue factor pathway inhibitor	Homo sapiens	97-101
15678271-4	2005	Following the administration of 1 mg/kg of heparin, gammaparin, and C3, the functional levels of TFPI at 5 minutes were 2.40, 2.56, and 1.08 U/mL and the corresponding TFPI immunologic levels were 4.3-, 4.0-, and 2.1-fold, increased, respectively, over the baseline value.	Heparin	43-50	tissue factor pathway inhibitor	Homo sapiens	168-172
15678271-5	2005	From these results, it can be concluded that heparin and gammaparin produced similar levels of TFPI release.	Heparin	45-52	tissue factor pathway inhibitor	Homo sapiens	95-99
16673389-0	2006	Controlled release of fibroblast growth factor-2 from an injectable 6-O-desulfated heparin hydrogel and subsequent effect on in vivo vascularization.	Heparin	83-90	fibroblast growth factor 2	Rattus norvegicus	22-48
16673389-1	2006	We prepared a 6-O-desulfated (DS-) heparin (Hep) hydrogel as an excellent carrier for the controlled release of Hep-binding growth factors, such as fibroblast growth factor (FGF)-2.	Heparin	44-47	fibroblast growth factor 2	Rattus norvegicus	148-180
19886733-0	2010	Heparin-conjugated fibrin as an injectable system for sustained delivery of bone morphogenetic protein-2.	Heparin	0-7	bone morphogenetic protein 2	Rattus norvegicus	76-104
16858650-1	2006	PURPOSE: Heparin immobilized porous poly(D,L-lactic-co-glycolic acid) (PLGA) microspheres were prepared for sustained release of basic fibroblast growth factor (bFGF) to induce angiogenesis.	Heparin	9-16	fibroblast growth factor 2	Mus musculus	129-159
16858650-1	2006	PURPOSE: Heparin immobilized porous poly(D,L-lactic-co-glycolic acid) (PLGA) microspheres were prepared for sustained release of basic fibroblast growth factor (bFGF) to induce angiogenesis.	Heparin	9-16	fibroblast growth factor 2	Mus musculus	161-165
16858650-4	2006	bFGF was loaded into the heparin functionalized (PLGA-heparin) microspheres by a simple dipping method.	Heparin	25-32	fibroblast growth factor 2	Mus musculus	0-4
16819821-0	2006	Zinc ions induce the unfolding and self-association of boar spermadhesin PSP-I, a protein with a single CUB domain architecture, and promote its binding to heparin.	Heparin	156-163	major seminal plasma glycoprotein PSP-I	Sus scrofa	73-78
16819821-7	2006	Thus, the modulation of the structural organization and heparin-binding ability of PSP-I by Zn2+ might be a physiological phenomenon in seminal plasma.	Heparin	56-63	major seminal plasma glycoprotein PSP-I	Sus scrofa	83-88
16709175-5	2006	Thus the presence of heparin increases the potency of HGF/SF in experiments with cells in culture leading to elevated downstream signalling effects and, although not vital for the Met-HGF/SF interaction, heparin or heparan sulphate is essential for the activity of certain isoforms of HGF/SF, such as NK1 and NK2.	Heparin	21-28	hepatocyte growth factor	Homo sapiens	54-60
16170812-3	2005	HIT is related to the presence of heparin-induced antibodies (HIA), which show specificity for the PF4-heparin (PF4-H) complex.	Heparin	34-41	platelet factor 4	Homo sapiens	99-102
16170812-3	2005	HIT is related to the presence of heparin-induced antibodies (HIA), which show specificity for the PF4-heparin (PF4-H) complex.	Heparin	34-41	platelet factor 4	Homo sapiens	112-115
16772737-1	2005	Synergism between low-molecular-weight heparin and low doses of unfractionated heparin (UH) enhancing anti-factor Xa activity and the release of tissue factor pathway inhibitor was observed.	Heparin	39-46	tissue factor pathway inhibitor	Rattus norvegicus	145-176
16772737-1	2005	Synergism between low-molecular-weight heparin and low doses of unfractionated heparin (UH) enhancing anti-factor Xa activity and the release of tissue factor pathway inhibitor was observed.	Heparin	79-86	tissue factor pathway inhibitor	Rattus norvegicus	145-176
15604266-4	2004	Using endostatin mutants lacking either of these two sites, we show that inhibition of fibroblast growth factor-2-induced angiogenesis in the chicken chorioallantoic membrane requires both heparin-binding sites.	Heparin	189-196	fibroblast growth factor 2	Gallus gallus	87-113
19886733-2	2010	We developed an injectable system for long-term delivery of BMP-2 by covalently conjugating heparin to fibrinogen.	Heparin	92-99	bone morphogenetic protein 2	Rattus norvegicus	60-65
16554020-0	2006	Mapping the heparin-binding domain of human hepatic lipase.	Heparin	12-19	lipase C, hepatic type	Homo sapiens	44-58
19931120-6	2010	Heparin-independent platelet activation was attenuated when SRA-positive specimens were retested after platelets were incubated 45 minutes at 37 degrees C. Surface PF4 expression was diminished on the rested platelets, compared to the same platelets labeled immediately after handling.	Heparin	0-7	platelet factor 4	Homo sapiens	164-167
16554020-4	2006	In the present study, we have used a systematic approach to map the heparin-binding regions of human HL by utilizing peptide arrays spanning the complete sequence of the mature protein.	Heparin	68-75	lipase C, hepatic type	Homo sapiens	101-103
15681807-4	2004	VCP is a multifunctional anti-inflammatory protein that can inhibit both pathways of complement activation and bind heparin.	Heparin	116-123	valosin containing protein	Homo sapiens	0-3
19944086-3	2010	Aim of this study was to evaluate the use of heparin plasma sample for BNP determination.	Heparin	45-52	natriuretic peptide B	Homo sapiens	71-74
15815878-6	2004	In a multiple logistic regression model that included inflammatory markers and clinical risk factors, antibody to PF4/heparin was a strong predictor of 30 day MI (odds ratio: 9.0; 95% confidence intervals 2.1-38.6; p &lt; 0.01), with IL-6 being the only other predictor (odds ratio: 1.1; 95% confidence intervals 1.0-1.2; p = 0.03).	Heparin	118-125	platelet factor 4	Homo sapiens	114-117
15815878-12	2004	In a multiple logistic regression model, antibody to PF4/heparin was a predictor of 30 day MI (odds ratio: 9.0; 95% CI: 2.1-38.6; p &lt; 0.01).	Heparin	57-64	platelet factor 4	Homo sapiens	53-56
15815881-4	2004	Compared to control, increases in TFPI were seen with both unfractionated heparin (182% higher, p &lt; 0.001) and enoxaparin (194% higher, p &lt; 0.001).	Heparin	74-81	tissue factor pathway inhibitor	Homo sapiens	34-38
22993547-7	2010	Western blot analysis showed that the CD31 protein was induced in PDL cells upon treatment with both heparin and FGF-2 for 3 weeks.	Heparin	101-108	platelet and endothelial cell adhesion molecule 1	Homo sapiens	38-42
15526371-8	2004	The hexasaccharide with Mr of 1,806, produced by depolymerizing heparin with beta-elimination method, had the strongest inhibitory effect on the secretion of IL-5.	Heparin	64-71	interleukin 5	Homo sapiens	158-162
20050998-2	2010	Antibodies recognize PF4/heparin complexes formed at optimal stoichiometric molar ratios.	Heparin	25-32	platelet factor 4	Homo sapiens	21-24
15371417-5	2004	Rapid kinetics of heparin binding indicate an induced fit mechanism that involves a conformational change in HCII.	Heparin	18-25	serpin family D member 1	Homo sapiens	109-113
15371417-6	2004	Thus, HCII binds to heparin in a manner analogous to the interaction of AT with low affinity heparin.	Heparin	20-27	serpin family D member 1	Homo sapiens	6-10
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Heparin	29-36	serpin family D member 1	Homo sapiens	74-78
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Heparin	99-106	serpin family D member 1	Homo sapiens	74-78
15371417-8	2004	We conclude that the heparin-binding mechanism of HCII is closely analogous to that of AT and that the induced fit mechanism suggests the potential design or discovery of specific HCII agonists.	Heparin	21-28	serpin family D member 1	Homo sapiens	50-54
15371417-8	2004	We conclude that the heparin-binding mechanism of HCII is closely analogous to that of AT and that the induced fit mechanism suggests the potential design or discovery of specific HCII agonists.	Heparin	21-28	serpin family D member 1	Homo sapiens	180-184
14764524-7	2004	However, the same amount of heparin paradoxically normalized thrombus formation in the hPF4(+) animals, although these animals were anticoagulated systemically.	Heparin	28-35	platelet factor 4	Homo sapiens	87-91
20008145-11	2010	The modification of missing Sdc1 function by heparin analogues may emerge as a promising anti-inflammatory approach.	Heparin	45-52	syndecan 1	Mus musculus	28-32
19858217-0	2009	A turn-like structure "KKPE" segment mediates the specific binding of viral protein A27 to heparin and heparan sulfate on cell surfaces.	Heparin	91-98	immunoglobulin kappa variable 3-20	Homo sapiens	84-87
15500441-4	2004	ERp29 was purified 4800-fold in non-denaturing conditions exploiting an unusual affinity for heparin.	Heparin	93-100	endoplasmic reticulum protein 29	Rattus norvegicus	0-5
15468163-10	2004	The results implicate RhoA for a role in regulating SMC phenotype and further show that activation of Rho by heparin and thrombin correlates with the ability of these factors to promote the contractile phenotype.	Heparin	109-116	transforming protein RhoA	Oryctolagus cuniculus	22-26
19858217-1	2009	Vaccinia viral envelope protein A27 (110 amino acids) specifically interacts with heparin (HP) or heparan sulfate (HS) proteoglycans for cell surface attachment.	Heparin	82-89	immunoglobulin kappa variable 3-20	Homo sapiens	32-35
15549170-3	2004	Current studies support a model whereby AT(1)R-dependent transactivation of EGFRs on cardiomyocytes involves stimulation of membrane-bound metalloproteases, which in turn cleave EGFR ligands such as heparin-binding EGF from a plasma membrane-associated precursor.	Heparin	199-206	angiotensin II receptor type 1	Homo sapiens	40-46
19858217-1	2009	Vaccinia viral envelope protein A27 (110 amino acids) specifically interacts with heparin (HP) or heparan sulfate (HS) proteoglycans for cell surface attachment.	Heparin	91-93	immunoglobulin kappa variable 3-20	Homo sapiens	32-35
15570242-6	2004	Similar dose-dependent mobilization of TFPI and lipoprotein lipase (LPL), another glucosaminoglycan (GAG)-anchored protein of the endothelial membrane, was observed after both subcutaneous and intravenous administration of heparins.	Heparin	223-231	tissue factor pathway inhibitor	Homo sapiens	39-43
15570242-7	2004	However, UFH induced a more efficient release of both TFPI and LPL into plasma than did LMWH at equivalent anti-Xa levels, indicating molecular-weight dependence of the release reactions.	Heparin	9-12	tissue factor pathway inhibitor	Homo sapiens	54-58
19858217-9	2009	We conclude that a turn-like structure introduced by the KKPE segment in vaccinia viral envelope protein A27 is responsible for its specific binding to HP and to HS on cell surfaces.	Heparin	152-154	immunoglobulin kappa variable 3-20	Homo sapiens	105-108
15570242-10	2004	UFH and LMWH treatment reduced renal clearance of TFPI compared with the control regimen.	Heparin	0-3	tissue factor pathway inhibitor	Homo sapiens	50-54
15570242-11	2004	Our findings suggest that displacement of TFPI from the endothelial-surface GAG is the main mechanism for TFPI release during heparin treatment in vivo and that differential urinary excretion of TFPI is not the explanation for selective depletion of TFPI during UFH treatment.	Heparin	126-133	tissue factor pathway inhibitor	Homo sapiens	42-46
19966216-4	2009	In this study we demonstrate that PDGF-AA binds directly to fibronectin and that this association is greatly enhanced by heparin.	Heparin	121-128	fibronectin 1 S homeolog	Xenopus laevis	60-71
15292258-0	2004	Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV.	Heparin	16-23	C-X-C motif chemokine ligand 12	Homo sapiens	49-78
15292258-0	2004	Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV.	Heparin	16-23	C-X-C motif chemokine ligand 12	Homo sapiens	80-85
15292258-0	2004	Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV.	Heparin	16-23	C-X-C motif chemokine ligand 12	Homo sapiens	87-93
15292258-5	2004	We report here that heparin and HS specifically prevent the processing of SDF-1 by DPP IV expressed by Caco-2 cells.	Heparin	20-27	C-X-C motif chemokine ligand 12	Homo sapiens	74-79
19675100-4	2009	We studied the effect of different monosaccharide derivatives, featuring the main characteristics of heparin and heparan sulphate (HS) building blocks, on the aggregation kinetics of human muscle acylphosphatase (mAcP), a useful model protein for these studies.	Heparin	101-108	vitamin A enhanced cleft palate	Mus musculus	213-217
15230691-0	2004	Effect of intravenous heparin on serum levels of endostatin, VEGF and HGF: author"s reply.	Heparin	22-29	hepatocyte growth factor	Homo sapiens	70-73
15230692-0	2004	Effect of intravenous heparin on serum levels of endostatin, VEGF and HGF.	Heparin	22-29	hepatocyte growth factor	Homo sapiens	70-73
15368365-6	2004	Second, a negatively charged resin (heparin) was used, which retained small amounts of NAP-2 (a very acidic polypeptide) and topoisomerase I.	Heparin	36-43	nucleosome assembly protein 1 like 4	Homo sapiens	87-92
19675100-5	2009	We observed that while heparin and HS changed the mAcP aggregation kinetic profile, the monosaccharide derivatives had no effect, whatever their concentration could be and both when they are studied separately or in combination.	Heparin	23-30	vitamin A enhanced cleft palate	Mus musculus	50-54
19675100-8	2009	We propose a model in which heparin and HS promote mAcP aggregation through a scaffolding-based mechanism, in which the regularly spaced sulphate moieties of the polymer interact with mAcP molecules increasing their local concentration and facilitating their orientation.	Heparin	28-35	vitamin A enhanced cleft palate	Mus musculus	51-55
19675100-8	2009	We propose a model in which heparin and HS promote mAcP aggregation through a scaffolding-based mechanism, in which the regularly spaced sulphate moieties of the polymer interact with mAcP molecules increasing their local concentration and facilitating their orientation.	Heparin	28-35	vitamin A enhanced cleft palate	Mus musculus	184-188
20019810-5	2009	The antimicrobial activity of PCI is located to the heparin-binding site of the protein and a peptide spanning this region was found to mimic the antimicrobial activity of PCI, without causing lysis or membrane destruction of eukaryotic cells.	Heparin	52-59	serpin family A member 5	Homo sapiens	30-33
15374620-7	2004	Heparin-sepharose (100 mM NaCl eluate)-purified preparation contained the MMP-2/TIMP-2 complex.	Heparin	0-7	matrix metallopeptidase 2	Bos taurus	74-79
20019810-5	2009	The antimicrobial activity of PCI is located to the heparin-binding site of the protein and a peptide spanning this region was found to mimic the antimicrobial activity of PCI, without causing lysis or membrane destruction of eukaryotic cells.	Heparin	52-59	serpin family A member 5	Homo sapiens	172-175
19664613-0	2009	Development of a real-time PCR detection method for a FCGR2A polymorphism in the LightCycler and application in the heparin-induced thrombocytopenia syndrome.	Heparin	116-123	Fc gamma receptor IIa	Homo sapiens	54-60
15182231-1	2004	We have previously shown that the LG4 (laminin G-like) domain of the laminin alpha4 chain is responsible for the significantly higher affinity of the alpha4 chain to heparin than found for other alpha chains [Yamaguchi, Yamashita, Mori, Okazaki, Nomizu, Beck and Kitagawa (2000) J. Biol.	Heparin	166-173	laminin subunit alpha 4	Homo sapiens	69-83
20101991-0	2009	[Analysis of the impact of heparin on the affinity of high mobility group box-1 protein and the receptor of advanced glycation end products by surface plasmon resonance technology].	Heparin	27-34	high mobility group box 1	Homo sapiens	54-79
15351861-0	2004	Inhibition of endothelial cell tube formation by the low molecular weight heparin, tinzaparin, is mediated by tissue factor pathway inhibitor.	Heparin	74-81	tissue factor pathway inhibitor	Homo sapiens	110-141
20101991-1	2009	To investigate the affinity constants of heparin with high mobility group protein 1(HMGB1) and HMGB1 with the receptor of advanced glycation end products (RAGE) and to analyze the impact of heparin on the affinity of HMGB1 and RAGE, the standard BIAcore amine coupling chemistry protocol using EDC and NHS was employed for immobilizing.	Heparin	41-48	high mobility group box 1	Homo sapiens	84-89
20101991-3	2009	Binding analysis was used to investigate the impact of heparin on the affinity of HMGB1 and RAGE.	Heparin	55-62	high mobility group box 1	Homo sapiens	82-87
15218077-6	2004	This CICR did not involve inositol 1,4,5-trisphosphate (IP(3)) receptors (IP(3)Rs) because it was resistant to heparin.	Heparin	111-118	corepressor interacting with RBPJ, 1	Mus musculus	5-9
20101991-7	2009	The highest concentration of 10 000 u x L(-1) of heparin in this experiment did not reach the saturation with HMGB1.	Heparin	49-56	high mobility group box 1	Homo sapiens	110-115
15264226-7	2004	UH-treated rats showed smaller infarctions than rats treated with vehicle, as well as higher IL-10 plasma levels and HO-1 brain expression and lower endothelial VCAM-1 induction.	Heparin	0-2	vascular cell adhesion molecule 1	Rattus norvegicus	161-167
20101991-8	2009	After 50 mg x L(-1) of HMGB1 was mixed with heparin of 50, 100, 1 000, 10 000 u x L(-1), the combining amount of HMGB1 and RAGE declined from 100 to 50 RU.	Heparin	44-51	high mobility group box 1	Homo sapiens	23-28
20101991-8	2009	After 50 mg x L(-1) of HMGB1 was mixed with heparin of 50, 100, 1 000, 10 000 u x L(-1), the combining amount of HMGB1 and RAGE declined from 100 to 50 RU.	Heparin	44-51	high mobility group box 1	Homo sapiens	113-118
15178681-7	2004	Moreover, we show that the IL-26 protein binds to heparin, is released from the cell surface, and can be functionally inhibited by heparin.	Heparin	50-57	interleukin 26	Homo sapiens	27-32
20101991-10	2009	It was concluded that heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE.	Heparin	22-29	high mobility group box 1	Homo sapiens	47-52
15178681-7	2004	Moreover, we show that the IL-26 protein binds to heparin, is released from the cell surface, and can be functionally inhibited by heparin.	Heparin	131-138	interleukin 26	Homo sapiens	27-32
20101991-10	2009	It was concluded that heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE.	Heparin	22-29	high mobility group box 1	Homo sapiens	80-85
19712047-10	2009	However, both intact and plasmin-cleaved HRG enhanced the binding of plasminogen to heparin-coated surfaces to a similar extent.	Heparin	84-91	plasminogen	Homo sapiens	25-32
15219850-5	2004	Inhibitors of matrix metalloproteinase and heparin bound-EGF prevented the CaR-mediated increases of pERK and PTHrP, consistent with a "triple-membrane-spanning signaling" requirement for transactivation of the EGFR by the CaR.	Heparin	43-50	parathyroid hormone like hormone	Homo sapiens	110-115
14966081-2	2004	Heparin, a model for sulfated components of basement membrane matrices, is known to inhibit fibroblast growth factor (FGF)-2-stimulated DNA synthesis as well as gene expression of FGF-2 and its receptor in AT2 cells.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	180-185
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	fibroblast growth factor 2	Rattus norvegicus	36-41
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	mitogen activated protein kinase kinase 1	Rattus norvegicus	114-120
19712047-11	2009	Furthermore, the presence of heparin, Zn2+ or acidic pH was found to protect HRG from plasmin cleavage.	Heparin	29-36	plasminogen	Homo sapiens	86-93
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	mitogen activated protein kinase 3	Rattus norvegicus	123-126
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	mitogen activated protein kinase 3	Rattus norvegicus	165-169
20137277-15	2009	CONCLUSION: Heparin markedly inhibits the expressions of phospho-ERK1/2 and phospho-P38 MAPK, down-regulates the inflammatory reaction, attenuates the endothelial permeability of pulmonary vasculature and significantly improves endotoxin-induced lung injury in rats.	Heparin	12-19	mitogen activated protein kinase 3	Rattus norvegicus	88-92
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	mitogen activated protein kinase 3	Rattus norvegicus	170-176
14966081-6	2004	FGF-2-stimulated signaling was more sensitive to heparin"s effects than was signaling stimulated by FGF-1.	Heparin	49-56	fibroblast growth factor 2	Rattus norvegicus	0-5
14966081-7	2004	Heparin had an additive effect on the reduced [(3)H]thymidine incorporation in FGF-2-treated AT2 cells caused by inhibition of the MEK/ERK pathway by the MEK inhibitor PD-98059.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	79-84
19615368-0	2009	Heparin-binding determinants of GDNF reduce its tissue distribution but are beneficial for the protection of nigral dopaminergic neurons.	Heparin	0-7	glial cell derived neurotrophic factor	Rattus norvegicus	32-36
15186946-9	2004	Moreover, pre-incubation of FGF-2 with heparin prior to injection restored SMC replication to the levels present in injured vessels treated with buffer alone (P &lt; 0.01).	Heparin	39-46	fibroblast growth factor 2	Rattus norvegicus	28-33
19615368-4	2009	We assessed the importance of heparin-binding determinants in the neuroprotective effects of GDNF in the 6-OHDA rat model of Parkinson"s disease.	Heparin	30-37	glial cell derived neurotrophic factor	Rattus norvegicus	93-97
15367830-3	2004	Heparin rapidly induces the release of HGF into the circulation, and HGF is a major factor involved in heparin-induced angiogenesis.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	39-42
15367830-3	2004	Heparin rapidly induces the release of HGF into the circulation, and HGF is a major factor involved in heparin-induced angiogenesis.	Heparin	103-110	hepatocyte growth factor	Homo sapiens	69-72
19422442-0	2009	Prospective evaluation of PF4/heparin immunoassays for the diagnosis of heparin-induced thrombocytopenia.	Heparin	72-79	platelet factor 4	Homo sapiens	26-29
15282657-7	2004	In a multiple logistic regression model that included inflammatory markers and clinical risk factors, antibodies to PF4/heparin were a strong predictor of 30-day MI (odds ratio, 9.0; 95% confidence intervals, 2.1 to 38.6; p &lt; 0.01), with IL-6 being the only other predictor (odds ratio, 1.1; 95% confidence intervals, 1.0 to 1.2; p = 0.03).	Heparin	120-127	platelet factor 4	Homo sapiens	116-119
15282660-3	2004	Although the complete physiologic role of PF4 is unknown, it is highly effective for the neutralization of heparin anticoagulation.	Heparin	107-114	platelet factor 4	Homo sapiens	42-45
15282660-5	2004	In the first open-label, phase 1 human study, patients received rPF4 in doses of 0.5, 1.0, 2.5, or 5.0 mg/kg over 3 minutes to reverse heparin anticoagulation after diagnostic cardiac catheterization.	Heparin	135-142	platelet factor 4	Rattus norvegicus	64-68
15282660-6	2004	There were no important hemodynamic changes and the rPF4 was highly effective in neutralizing heparin.	Heparin	94-101	platelet factor 4	Rattus norvegicus	52-56
15282661-8	2004	In cardiovascular disease, PF4 may possibly intervene in collateral vessel formation, plaque neovascularization, heparin-induced thrombocytopenia and stent endothelialization.	Heparin	113-120	platelet factor 4	Homo sapiens	27-30
19422442-1	2009	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is an adverse complication of heparin caused by HIT antibodies that recognize platelet factor 4-heparin (PF4/hep) complexes leading to platelet activation.	Heparin	12-19	platelet factor 4	Homo sapiens	156-163
15051888-6	2004	Furthermore, QSulf1 can produce enzymatically modified soluble heparin that acts as a potent inhibitor of FGF2-induced angiogenesis in the chicken embryo.	Heparin	63-70	fibroblast growth factor 2	Gallus gallus	106-110
19422442-1	2009	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is an adverse complication of heparin caused by HIT antibodies that recognize platelet factor 4-heparin (PF4/hep) complexes leading to platelet activation.	Heparin	81-88	platelet factor 4	Homo sapiens	156-163
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Heparin	6-13	pappalysin 1	Homo sapiens	176-182
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Heparin	188-195	pappalysin 1	Homo sapiens	176-182
19540379-0	2009	Heparin/PF4 antibodies formation after heparin treatment: temporal aspects and long-term follow-up.	Heparin	39-46	platelet factor 4	Homo sapiens	8-11
15066178-11	2004	Furthermore, when acidic residues of the homologous proteinase PAPP-A2 (Asp1547, Glu1555 and Glu1567) were introduced into the corresponding positions in the sequence of PAPP-A, located in each of the three basic clusters of CCP3, binding to heparin was strongly impaired and cell surface binding was abrogated.	Heparin	242-249	pappalysin 2	Homo sapiens	63-70
15066178-11	2004	Furthermore, when acidic residues of the homologous proteinase PAPP-A2 (Asp1547, Glu1555 and Glu1567) were introduced into the corresponding positions in the sequence of PAPP-A, located in each of the three basic clusters of CCP3, binding to heparin was strongly impaired and cell surface binding was abrogated.	Heparin	242-249	pappalysin 1	Homo sapiens	63-69
19565481-1	2009	OBJECTIVE: We have previously identified in articular cartilage an abundant pool of the heparin-binding growth factor, fibroblast growth factor 2 (FGF-2), which is bound to the pericellular matrix heparan sulfate proteoglycan, perlecan.	Heparin	88-95	fibroblast growth factor 2	Mus musculus	119-145
15045531-1	2004	BACKGROUND: The alteration of the N-terminal amino acid sequence of BMP-2 allows modification of heparin binding of the new protein.	Heparin	97-104	bone morphogenetic protein 2	Homo sapiens	68-73
19565481-1	2009	OBJECTIVE: We have previously identified in articular cartilage an abundant pool of the heparin-binding growth factor, fibroblast growth factor 2 (FGF-2), which is bound to the pericellular matrix heparan sulfate proteoglycan, perlecan.	Heparin	88-95	fibroblast growth factor 2	Mus musculus	147-152
19291166-1	2009	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe complication of heparin therapy that can be associated with arterial or venous thrombosis and is caused by antibodies against platelet factor 4 (PF4)-heparin complex.	Heparin	12-19	platelet factor 4	Homo sapiens	208-211
14744997-4	2004	In living mice, mesoangioblasts injected into the femoral artery migrate close to HMGB1-loaded heparin-Sepharose beads implanted in healthy muscle, but are unresponsive to control beads.	Heparin	95-102	high mobility group box 1	Mus musculus	82-87
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	serpin family D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	serpin family D member 1	Homo sapiens	305-309
15063833-0	2004	Continuous administration of heparin in patients with deep vein thrombosis can increase plasma levels of diamine oxidase.	Heparin	29-36	amine oxidase copper containing 1	Homo sapiens	105-120
19291166-1	2009	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a severe complication of heparin therapy that can be associated with arterial or venous thrombosis and is caused by antibodies against platelet factor 4 (PF4)-heparin complex.	Heparin	79-86	platelet factor 4	Homo sapiens	208-211
15063833-2	2004	Especially the antiinflammatory and immunoregulatory properties of heparin may be associated with its ability to release the histamine-degrading enzyme diamine oxidase (DAO) from tissue-bound sites into the circulation.	Heparin	67-74	amine oxidase copper containing 1	Homo sapiens	152-167
19291166-5	2009	METHODS: Antibodies against PF4-heparin complex were assayed by particle gel immunoassay (PaGIA), or enzyme immunoassay (EIA) with or without an excess of heparin.	Heparin	32-39	platelet factor 4	Homo sapiens	28-31
15063833-2	2004	Especially the antiinflammatory and immunoregulatory properties of heparin may be associated with its ability to release the histamine-degrading enzyme diamine oxidase (DAO) from tissue-bound sites into the circulation.	Heparin	67-74	amine oxidase copper containing 1	Homo sapiens	169-172
15063833-3	2004	Whereas DAO activity is at the limits of detection in normal human plasma, the application of heparin leads to a significant increase of plasma DAO activity.	Heparin	94-101	amine oxidase copper containing 1	Homo sapiens	144-147
16631722-0	2006	Temporal aspects of anti-heparin-PF4 antibodies in heparin-induced thrombocytopenia.	Heparin	25-32	platelet factor 4	Homo sapiens	33-36
15063833-5	2004	To investigate DAO release during continuous heparin infusion, 28 patients with deep vein thrombosis (DVT) undergoing heparin therapy were analyzed.	Heparin	45-52	amine oxidase copper containing 1	Homo sapiens	15-18
19291166-10	2009	All 24 samples that were positive for PF4-heparin complex by EIA IgG were also positive for EIA IgG in the presence of heparin excess, and all were negative by the HIPA and heparin-induced platelet aggregation tests.	Heparin	42-49	platelet factor 4	Homo sapiens	38-41
15063833-9	2004	This study shows, for the first time, that continuous heparin infusion can lead to DAO release and that individuals exhibit considerable differences in their release response.	Heparin	54-61	amine oxidase copper containing 1	Homo sapiens	83-86
19291166-10	2009	All 24 samples that were positive for PF4-heparin complex by EIA IgG were also positive for EIA IgG in the presence of heparin excess, and all were negative by the HIPA and heparin-induced platelet aggregation tests.	Heparin	119-126	platelet factor 4	Homo sapiens	38-41
15063833-10	2004	Although the significance of heparin-induced DAO release needs further clarification, our results indicate that postheparin plasma DAO activity could be an interesting parameter correlated with idiopathic DVT.	Heparin	29-36	amine oxidase copper containing 1	Homo sapiens	45-48
19291166-11	2009	CONCLUSION: A large proportion of patients with APS and/or SLE give false-positive HIT antigen test results that are presumably related to autoantibodies against PF4, which can be distinguished from true HIT antibodies by EIA for PF4-heparin complexes tested with heparin excess, and by functional assays.	Heparin	234-241	platelet factor 4	Homo sapiens	162-165
19630810-4	2009	HIT is caused by antibodies that recognize the platelet chemokine, Platelet Factor 4 (PF4), complexed to heparin or to cellular glycosaminoglycans (GAGs).	Heparin	105-112	platelet factor 4	Homo sapiens	67-84
14624766-4	2003	In the presence of IGF-II, IGFBP-2 bound with high affinity to heparin-Sepharose, but not to type I collagen, fibronectin, or laminin.	Heparin	63-70	insulin like growth factor binding protein 2	Homo sapiens	27-34
14624766-5	2003	Furthermore, heparin and heparan sulfate, but not chondroitin sulfate, inhibited IGFBP-2/IGF-II binding to ECM.	Heparin	13-20	insulin like growth factor binding protein 2	Homo sapiens	81-88
16689752-3	2006	Upon heparin infusion during cardiopulmonary bypass (CPB), a heparin releasable pool of endothelial associated TFPI circulates in plasma.	Heparin	5-12	tissue factor pathway inhibitor	Homo sapiens	111-115
16689752-3	2006	Upon heparin infusion during cardiopulmonary bypass (CPB), a heparin releasable pool of endothelial associated TFPI circulates in plasma.	Heparin	61-68	tissue factor pathway inhibitor	Homo sapiens	111-115
16689752-4	2006	Following protamine neutralization of heparin, the plasma TFPI level decreases, but does not return completely to baseline, suggesting that during CPB a fraction of the plasma TFPI becomes heparin-independent.	Heparin	38-45	tissue factor pathway inhibitor	Homo sapiens	58-62
16689752-4	2006	Following protamine neutralization of heparin, the plasma TFPI level decreases, but does not return completely to baseline, suggesting that during CPB a fraction of the plasma TFPI becomes heparin-independent.	Heparin	38-45	tissue factor pathway inhibitor	Homo sapiens	176-180
16689752-11	2006	RESULTS: The ELISA and Western blot data indicated that an increase in full-length TFPI accounted for most of the heparin releasable TFPI.	Heparin	114-121	tissue factor pathway inhibitor	Homo sapiens	83-87
16689752-11	2006	RESULTS: The ELISA and Western blot data indicated that an increase in full-length TFPI accounted for most of the heparin releasable TFPI.	Heparin	114-121	tissue factor pathway inhibitor	Homo sapiens	133-137
16689752-12	2006	Following heparin neutralization with protamine, the full-length TFPI antigen returned to baseline levels while the free TFPI antigen and the total plasma TFPI activity remained elevated.	Heparin	10-17	tissue factor pathway inhibitor	Homo sapiens	65-69
16689752-16	2006	CONCLUSIONS: During CPB the full-length form of TFPI is the predominant form in plasma because of its prompt release from the endothelial surface following heparin administration.	Heparin	156-163	tissue factor pathway inhibitor	Homo sapiens	48-52
16689752-17	2006	Upon heparin neutralization with protamine, full-length TFPI redistributes back to the endothelial surface.	Heparin	5-12	tissue factor pathway inhibitor	Homo sapiens	56-60
19630810-4	2009	HIT is caused by antibodies that recognize the platelet chemokine, Platelet Factor 4 (PF4), complexed to heparin or to cellular glycosaminoglycans (GAGs).	Heparin	105-112	platelet factor 4	Homo sapiens	86-89
16567403-4	2006	To determine the mPrP-aptamer binding region, we performed protein-deletion-mutant analysis and competition-binding analysis using heparin.	Heparin	131-138	prion protein	Mus musculus	17-21
19630810-7	2009	Heparin removes cell surface-bound PF4 in most individuals, but removal is incomplete in those with high pre-exposure surface-bound PF4 levels.	Heparin	0-7	platelet factor 4	Homo sapiens	35-38
19630810-7	2009	Heparin removes cell surface-bound PF4 in most individuals, but removal is incomplete in those with high pre-exposure surface-bound PF4 levels.	Heparin	0-7	platelet factor 4	Homo sapiens	132-135
19425605-1	2009	HDL acts much like heparin to liberate hepatic lipase (HL) from cell surface proteoglycans and stimulate triglyceride clearance.	Heparin	19-26	lipase C, hepatic type	Homo sapiens	39-53
16445278-5	2006	Addition of heparin or IP(3)R antibody blocked the IP(3)-induced Ca(2+) releases, indicating the release of Ca(2+) through the IP(3)R/Ca(2+) channels.	Heparin	12-19	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	127-133
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	113-120	C-X-C motif chemokine ligand 12	Homo sapiens	83-88
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	113-120	C-C motif chemokine ligand 21	Homo sapiens	93-96
19425605-1	2009	HDL acts much like heparin to liberate hepatic lipase (HL) from cell surface proteoglycans and stimulate triglyceride clearance.	Heparin	19-26	lipase C, hepatic type	Homo sapiens	55-57
19567201-4	2009	Moreover, specific inhibitors, such as staurosporine, H89 and heparin, inhibited internalization of CCR9, which indicated a role of protein kinase C (PKC) and G protein-coupled kinase 2 (GRK2), respectively.	Heparin	62-69	C-C motif chemokine receptor 9	Homo sapiens	100-104
19369870-4	2009	The pattern of lipoprotein lipase (LPL) release into the plasma after an intravenous injection of heparin is abnormal in Gpihbp1-deficient mice, suggesting that GPIHBP1 plays a direct role in binding LPL within the tissues of mice.	Heparin	98-105	GPI-anchored HDL-binding protein 1	Mus musculus	121-128
17113870-5	2006	Sulf-1 and Sulf-2 have been cloned and identified as sulfatases that release sulfate groups on the C-6 position of GlcNAc residue from an internal subdomain in intact heparin.	Heparin	167-174	extracellular sulfatase Sulf-2	Cricetulus griseus	11-17
19369870-4	2009	The pattern of lipoprotein lipase (LPL) release into the plasma after an intravenous injection of heparin is abnormal in Gpihbp1-deficient mice, suggesting that GPIHBP1 plays a direct role in binding LPL within the tissues of mice.	Heparin	98-105	GPI-anchored HDL-binding protein 1	Mus musculus	161-168
19195684-1	2009	UNLABELLED: Heparin-induced thrombocytopenia (HIT) results from development of an antibody to a complex of heparin and platelet factor 4 (PF4) resulting in thrombocytopenia and a prothrombotic state with serious clinical consequences.	Heparin	12-19	platelet factor 4	Homo sapiens	138-141
16902310-1	2006	Heparin-induced thrombocytopenia (HIT) is a syndrome caused by platelet-activating antibodies that recognize complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	141-144
16902310-11	2006	Antibodies against the PF4-heparin complex were detected with a combination of a "quick test" and an enzyme-linked immunosorbent assay test.	Heparin	27-34	platelet factor 4	Homo sapiens	23-26
19249255-1	2009	In this manuscript we report the binding affinity between two model proteins, human serum albumin (HSA) and ribonuclease A (RNase A), and negatively charged polyelectrolytes, two different heparin fractions and dextran sulfate, by means of partial filling and affinity capillary electrophoresis.	Heparin	189-196	ribonuclease A family member 1, pancreatic	Homo sapiens	108-122
16462666-5	2006	Thrombocytosis associated with heparin is probably explained by the latter"s potentiation of megakaryocytopoiesis, in particular, by inhibition of platelet factor 4 (PF4).	Heparin	31-38	platelet factor 4	Homo sapiens	166-169
19249255-1	2009	In this manuscript we report the binding affinity between two model proteins, human serum albumin (HSA) and ribonuclease A (RNase A), and negatively charged polyelectrolytes, two different heparin fractions and dextran sulfate, by means of partial filling and affinity capillary electrophoresis.	Heparin	189-196	ribonuclease A family member 1, pancreatic	Homo sapiens	124-131
19249435-0	2009	Heparin/PF4 antibodies formation after heparin treatment: temporal aspects and long-term follow-up.	Heparin	39-46	platelet factor 4	Homo sapiens	8-11
16317389-6	2005	Heparin, a heparan sulfate analog, inhibited internalization of S. bovis, S. agalactiae, S. pyogenes, and S. aureus by HT-29 enterocytes (prominent syndecan-1 expression), but not Caco-2 enterocytes (relatively low syndecan-1 expression).	Heparin	0-7	syndecan 1	Homo sapiens	148-158
16317389-6	2005	Heparin, a heparan sulfate analog, inhibited internalization of S. bovis, S. agalactiae, S. pyogenes, and S. aureus by HT-29 enterocytes (prominent syndecan-1 expression), but not Caco-2 enterocytes (relatively low syndecan-1 expression).	Heparin	0-7	syndecan 1	Homo sapiens	215-225
16262248-0	2005	Characterization of the heparin/heparan sulfate binding site of the natural cytotoxicity receptor NKp46.	Heparin	24-31	natural cytotoxicity triggering receptor 1	Homo sapiens	98-103
16262248-5	2005	On the basis of both the electrostatic potential map and comparison to the heparin binding site on human fibronectin, we predicted a continuous region containing the basic amino acids K133, R136, H139, R142, and K146 to be involved in NKp46 binding to heparan sulfate.	Heparin	75-82	natural cytotoxicity triggering receptor 1	Homo sapiens	235-240
16262248-7	2005	The minimal length of the heparin/heparan sulfate epitope recognized by NKp46 was eight saccharides as predicted from the structure and proven by testing heparin oligomers.	Heparin	26-33	natural cytotoxicity triggering receptor 1	Homo sapiens	72-77
16262248-7	2005	The minimal length of the heparin/heparan sulfate epitope recognized by NKp46 was eight saccharides as predicted from the structure and proven by testing heparin oligomers.	Heparin	154-161	natural cytotoxicity triggering receptor 1	Homo sapiens	72-77
19249435-1	2009	BACKGROUND: Heparin-induced thrombocytopenia is characterized by the presence of heparin-induced antibodies against heparin/platelet factor-4 (PF4) complex and paradoxical thrombosis.	Heparin	12-19	platelet factor 4	Homo sapiens	116-141
16262248-8	2005	Testing selectively monodesulfated heparin oligomers emphasized the specific contributions of O-sulfation, N-sulfation, and N-acetylation to epitope recognition by NKp46.	Heparin	35-42	natural cytotoxicity triggering receptor 1	Homo sapiens	164-169
19249435-1	2009	BACKGROUND: Heparin-induced thrombocytopenia is characterized by the presence of heparin-induced antibodies against heparin/platelet factor-4 (PF4) complex and paradoxical thrombosis.	Heparin	12-19	platelet factor 4	Homo sapiens	143-146
19249435-1	2009	BACKGROUND: Heparin-induced thrombocytopenia is characterized by the presence of heparin-induced antibodies against heparin/platelet factor-4 (PF4) complex and paradoxical thrombosis.	Heparin	81-88	platelet factor 4	Homo sapiens	116-141
19249435-1	2009	BACKGROUND: Heparin-induced thrombocytopenia is characterized by the presence of heparin-induced antibodies against heparin/platelet factor-4 (PF4) complex and paradoxical thrombosis.	Heparin	81-88	platelet factor 4	Homo sapiens	143-146
19249435-3	2009	The aim of this study was to evaluate the time course of heparin/PF4 antibodies in patients exposed to heparin.	Heparin	57-64	platelet factor 4	Homo sapiens	65-68
16266050-4	2005	METHODS: Platinum coils were prepared by successive coatings with cationic polyethyleneimine and anionic heparin and then TNC or basic fibroblast growth factor (bFGF) was immobilized by affinity binding to the heparin.	Heparin	210-217	fibroblast growth factor 2	Rattus norvegicus	129-159
19285275-10	2009	As heparins are strong inhibitors of heparanase, in view of the effect of heparanase on the TF/TFPI pathway, the role of anticoagulant activity of heparin may potentially be expanded.	Heparin	3-11	tissue factor pathway inhibitor	Homo sapiens	95-99
16266050-4	2005	METHODS: Platinum coils were prepared by successive coatings with cationic polyethyleneimine and anionic heparin and then TNC or basic fibroblast growth factor (bFGF) was immobilized by affinity binding to the heparin.	Heparin	210-217	fibroblast growth factor 2	Rattus norvegicus	161-165
16125968-5	2005	Identification of GPR30 as a Gs-coupled 7TM receptor that triggers release of heparin-binding EGF establishes its role in cell signaling cascades initiated by estrogens, and explains their capacity to activate second messengers and promote EGF-like effects.	Heparin	78-85	cholinergic receptor muscarinic 2	Homo sapiens	40-52
19285275-10	2009	As heparins are strong inhibitors of heparanase, in view of the effect of heparanase on the TF/TFPI pathway, the role of anticoagulant activity of heparin may potentially be expanded.	Heparin	3-10	tissue factor pathway inhibitor	Homo sapiens	95-99
19309011-5	2009	1x10(3) kDa, which were mainly attributed to the presence of the complexes of complement C4b and C4b-binding protein in heparin-plasma and their absence in EDTA-plasma.	Heparin	120-127	complement C4B (Chido blood group)	Homo sapiens	78-92
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	25-32	complement factor B	Homo sapiens	124-143
16102727-7	2005	A mutant of the heparin-binding site of PEDF (Hep-mut PEDF) suppressed tumor growth.	Heparin	16-23	serpin family F member 1	Homo sapiens	40-44
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	49-56	complement factor B	Homo sapiens	124-143
16102727-7	2005	A mutant of the heparin-binding site of PEDF (Hep-mut PEDF) suppressed tumor growth.	Heparin	16-23	serpin family F member 1	Homo sapiens	54-58
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	49-56	complement factor B	Homo sapiens	124-143
19309011-7	2009	The 2-DE pattern of high-heparin-plasma (0.50 mg heparin/mL blood) showed pI changes of three plasma proteins, fibronectin, complement factor B, and pre-alpha-inhibitor when compared with that of heparin-plasma, suggesting the interactions between heparin and the proteins.	Heparin	49-56	complement factor B	Homo sapiens	124-143
19150337-1	2009	Platelet Factor 4 (PF4) prevents inhibition of blood coagulation proteases by heparin via formation of a putative enzyme-PF4 complex.	Heparin	78-85	platelet factor 4	Homo sapiens	19-22
16079143-3	2005	Inhibition studies in both the presence and absence of PZ revealed that Arg-143, Lys-147, and Arg-154 of the autolysis loop and Lys-96, Lys-169, and Lys-236 of the heparin binding exosite are required for recognition of ZPI, with Arg-143 being essential for the interaction.	Heparin	164-171	serpin family A member 10	Homo sapiens	220-223
19150337-1	2009	Platelet Factor 4 (PF4) prevents inhibition of blood coagulation proteases by heparin via formation of a putative enzyme-PF4 complex.	Heparin	78-85	platelet factor 4	Homo sapiens	121-124
19150337-6	2009	These findings suggest that PF4 in the presence of heparin is an allosteric effector of the prothrombinase complex.	Heparin	51-58	platelet factor 4	Homo sapiens	28-31
16127194-6	2005	In all patients, HGF levels increased more than 4-fold of the basal level at 30 min after heparin injection.	Heparin	90-97	hepatocyte growth factor	Homo sapiens	17-20
19154352-0	2009	Murine serum nucleases--contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1l3).	Heparin	59-66	deoxyribonuclease 1-like 3	Mus musculus	99-112
19154352-0	2009	Murine serum nucleases--contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1l3).	Heparin	59-66	deoxyribonuclease 1-like 3	Mus musculus	114-122
16040252-6	2005	Conserved residues at the N-terminus, helix d (hD), and helix A (hA) of PEDF form a structure similar to the heparin-binding groove of other serpins.	Heparin	109-116	serpin family F member 1	Homo sapiens	72-76
16190367-6	2005	We investigated the roles of endogenous tPA and MMPs in hemorrhagic cerebral infarction associated with heparin.	Heparin	104-111	plasminogen activator, tissue	Mus musculus	40-43
16190367-6	2005	We investigated the roles of endogenous tPA and MMPs in hemorrhagic cerebral infarction associated with heparin.	Heparin	104-111	matrix metallopeptidase 9	Mus musculus	48-52
16190367-8	2005	Heparin administration increased tPA activity and its mRNA expression in WT.	Heparin	0-7	plasminogen activator, tissue	Mus musculus	33-36
16190367-10	2005	Our findings suggest that endogenous tPA plays an important role in heparin-produced cerebral hemorrhage via MMP9 induction and activation.	Heparin	68-75	plasminogen activator, tissue	Mus musculus	37-40
16190367-10	2005	Our findings suggest that endogenous tPA plays an important role in heparin-produced cerebral hemorrhage via MMP9 induction and activation.	Heparin	68-75	matrix metallopeptidase 9	Mus musculus	109-113
19101225-4	2009	The purposes of the present study were to evaluate in-hospital levels of PAPP-A compared with other circulating biomarkers in patients with acute myocardial infarctions and to explore the potential impact of concomitant heparin administration on PAPP-A levels in an animal experiment.	Heparin	220-227	pappalysin 1	Homo sapiens	246-252
15917224-6	2005	We also show that heparin can modify another property of the Link module, i.e. its potentiation of the anti-plasmin activity of inter-alpha-inhibitor (IalphaI).	Heparin	18-25	plasminogen	Homo sapiens	108-115
15917224-9	2005	Changes in plasmin activity have been observed previously at sites of TSG-6 expression, and the results presented here suggest that TSG-6 is likely to contribute to matrix remodeling, at least in part, through down-regulation of the protease network, especially in locations containing heparin/heparan sulfate proteoglycans.	Heparin	286-293	plasminogen	Homo sapiens	11-18
19101225-12	2009	In the animal experiment, concomitant heparin administration resulted in increased levels of PAPP-A and delayed clearance of PAPP-A from the circulation.	Heparin	38-45	pappalysin 1	Homo sapiens	93-99
15878877-8	2005	ApoA-V enrichment enhanced binding of apoC-II-deficient chylomicrons and VLDL to heparin-coated chips.	Heparin	81-88	apolipoprotein C2	Homo sapiens	38-45
15989807-7	2005	Heparin, C5 and adenosine did not induce any histamine release at concentrations tested, but heparin enhanced histamine release induced by C5a and substance P. CONCLUSION: Trypsin, anti-IgE, CI, FMLP, C5a and substance P can induce histamine release from baosophils, but PAR-2 agonist can not.	Heparin	93-100	F2R like trypsin receptor 1	Homo sapiens	271-276
19101225-12	2009	In the animal experiment, concomitant heparin administration resulted in increased levels of PAPP-A and delayed clearance of PAPP-A from the circulation.	Heparin	38-45	pappalysin 1	Homo sapiens	125-131
15910290-1	2005	Heparin-induced thrombocytopenia (HIT) is an adverse immune-mediated drug reaction in which antibodies are generated usually towards complexes of the soluble platelet protein platelet-factor-4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	194-197
19101225-13	2009	In conclusion, PAPP-A is markedly elevated in the earliest hours after the onset of symptoms in patients with STEMIs treated with heparin and primary percutaneous coronary intervention, and in animal studies, heparin administration is associated with a significant increase in PAPP-A levels, presumably because of the detachment of PAPP-A from the vessel wall.	Heparin	130-137	pappalysin 1	Homo sapiens	15-21
19101225-13	2009	In conclusion, PAPP-A is markedly elevated in the earliest hours after the onset of symptoms in patients with STEMIs treated with heparin and primary percutaneous coronary intervention, and in animal studies, heparin administration is associated with a significant increase in PAPP-A levels, presumably because of the detachment of PAPP-A from the vessel wall.	Heparin	209-216	pappalysin 1	Homo sapiens	15-21
19101225-13	2009	In conclusion, PAPP-A is markedly elevated in the earliest hours after the onset of symptoms in patients with STEMIs treated with heparin and primary percutaneous coronary intervention, and in animal studies, heparin administration is associated with a significant increase in PAPP-A levels, presumably because of the detachment of PAPP-A from the vessel wall.	Heparin	209-216	pappalysin 1	Homo sapiens	277-283
19101225-13	2009	In conclusion, PAPP-A is markedly elevated in the earliest hours after the onset of symptoms in patients with STEMIs treated with heparin and primary percutaneous coronary intervention, and in animal studies, heparin administration is associated with a significant increase in PAPP-A levels, presumably because of the detachment of PAPP-A from the vessel wall.	Heparin	209-216	pappalysin 1	Homo sapiens	277-283
15823034-2	2005	The C-terminal globular domain (G domain) of the laminin alpha4 chain was previously found to be critical for heparin binding and cell attachment activity.	Heparin	110-117	laminin subunit alpha 4	Rattus norvegicus	49-63
19101225-14	2009	If future studies confirm that concomitant heparin administration also increases PAPP-A levels in humans, the prognostic role of PAPP-A in patients with STEMIs needs to be reevaluated.	Heparin	43-50	pappalysin 1	Homo sapiens	81-87
19101225-14	2009	If future studies confirm that concomitant heparin administration also increases PAPP-A levels in humans, the prognostic role of PAPP-A in patients with STEMIs needs to be reevaluated.	Heparin	43-50	pappalysin 1	Homo sapiens	129-135
18286621-1	2009	In the present study, we explored the binding capacity of synthetic heparin-like dextran derivatives to recombinant human bone morphogenetic protein 2 (BMP-2), a heparin-binding osteoinductive growth factor.	Heparin	68-75	bone morphogenetic protein 2	Homo sapiens	122-150
15741341-0	2005	The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin.	Heparin	115-122	C-X-C motif chemokine ligand 12	Homo sapiens	33-62
15741341-0	2005	The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin.	Heparin	115-122	C-X-C motif chemokine ligand 12	Homo sapiens	64-71
16104364-5	2005	(1) Infused heparin neutralizes a portion of excess surface PF4, directly enhancing local thrombosis.	Heparin	12-19	platelet factor 4	Homo sapiens	60-63
16104364-6	2005	(2) The excess PF4 is mobilized into PF4/heparin complexes that stimulates HIT antibody production.	Heparin	41-48	platelet factor 4	Homo sapiens	15-18
16104364-7	2005	(3) The remaining PF4 complexed to heparanoids and heparin on the vascular surfaces now bind to these HIT antibodies and through surface Fc gammaRII receptors leads to more platelet activation and removal, thrombus formation, and inflammation.	Heparin	51-58	platelet factor 4	Homo sapiens	18-21
18286621-1	2009	In the present study, we explored the binding capacity of synthetic heparin-like dextran derivatives to recombinant human bone morphogenetic protein 2 (BMP-2), a heparin-binding osteoinductive growth factor.	Heparin	68-75	bone morphogenetic protein 2	Homo sapiens	152-157
16104365-1	2005	Heparin-induced thrombocytopenia (HIT) type II is an immune mediated reaction in which pathologic antibodies develop to a complex composed of heparin and the platelet-derived alpha granule protein, platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	217-220
18286621-1	2009	In the present study, we explored the binding capacity of synthetic heparin-like dextran derivatives to recombinant human bone morphogenetic protein 2 (BMP-2), a heparin-binding osteoinductive growth factor.	Heparin	162-169	bone morphogenetic protein 2	Homo sapiens	122-150
15876997-0	2005	Pharmacodynamic effects of low molecular weight heparin in obese subjects following subcutaneous administration of 75 IU/kg on plasma tissue factor pathway inhibitor and nitric oxide.	Heparin	48-55	tissue factor pathway inhibitor	Homo sapiens	134-165
15876997-1	2005	AIM: Pharmacodynamic effects of the low molecular weight heparin tinzaparin on plasma levels of tissue factor pathway inhibitor (TFPI) and nitric oxide (NO) were compared in obese subjects, as well as in normal healthy controls.	Heparin	57-64	tissue factor pathway inhibitor	Homo sapiens	96-127
15522881-5	2005	CLAC displays features characteristic of a collagen protein, e.g. it forms a partly protease-resistant triple-helical structure, exhibits an intermediate affinity for heparin, and is glycosylated.	Heparin	167-174	collagen type XXV alpha 1 chain	Homo sapiens	0-4
14727038-0	2003	[Prevention of thromboembolism in trauma surgery by dose adjustment of low molecular weight heparin depending on levels of TAT and D-dimer].	Heparin	92-99	tyrosine aminotransferase	Homo sapiens	123-126
15620727-0	2005	Heparin recovers AT1 receptor and its intracellular signal transduction in cultured vascular smooth muscle cells.	Heparin	0-7	angiotensin II receptor type 1	Homo sapiens	17-20
14636425-0	2003	CCN5 modulates the antiproliferative effect of heparin and regulates cell motility in vascular smooth muscle cells.	Heparin	47-54	cellular communication network factor 5	Homo sapiens	0-4
18286621-1	2009	In the present study, we explored the binding capacity of synthetic heparin-like dextran derivatives to recombinant human bone morphogenetic protein 2 (BMP-2), a heparin-binding osteoinductive growth factor.	Heparin	162-169	bone morphogenetic protein 2	Homo sapiens	152-157
14636425-6	2003	RESULTS: Using RNA interference (RNAi), we first demonstrate that CCN5 is required for the antiproliferative effect of heparin in VSMC.	Heparin	119-126	cellular communication network factor 5	Homo sapiens	66-70
15620727-3	2005	The present study demonstrated that heparin recovered Ang receptors and differentiation markers, such as desmin, SM-22 and smooth muscle alpha-actin in VSMCs at the ninth passage.	Heparin	36-43	transgelin	Homo sapiens	113-118
18286621-7	2009	Like heparin, DMCB sustained the biological activity of the growth factor; this result suggests that the formation of the BMP-2/DMCB complex may protect the protein from being inactivated.	Heparin	5-12	bone morphogenetic protein 2	Homo sapiens	122-127
15829109-5	2005	This release can be completely blocked by heparin, a well-known antagonist of IP3 receptor, indicating a direct activation of IP3 receptor on endoplasmic reticulum (ER) membrane by H2O2.	Heparin	42-49	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	78-90
14575696-8	2003	It is proposed that PF4 inhibited the sequence of events recapitulated in the template mechanism describing heparin-dependent inhibition of fXa.	Heparin	108-115	platelet factor 4	Homo sapiens	20-23
18796439-4	2009	METHODS: Crossover design was used to evaluate sodium citrate and heparin-supplemented Gambrosol Trio (2.5% glucose) in 28 stable outpatients from the PD unit.	Heparin	66-73	trio Rho guanine nucleotide exchange factor	Homo sapiens	97-101
12912996-7	2003	The biological activity of BMP-2, which was evaluated using a BMP-responsive reporter gene expression, was prolonged in the presence of heparin.	Heparin	136-143	bone morphogenetic protein 2	Homo sapiens	27-32
15829109-5	2005	This release can be completely blocked by heparin, a well-known antagonist of IP3 receptor, indicating a direct activation of IP3 receptor on endoplasmic reticulum (ER) membrane by H2O2.	Heparin	42-49	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	126-138
15668190-0	2005	Potentiation of platelet aggregation by heparin in human whole blood is attenuated by P2Y12 and P2Y1 antagonists but not aspirin.	Heparin	40-47	purinergic receptor P2Y12	Homo sapiens	86-91
19016244-6	2008	Analyses of associations between SOD genotypes and levels of plasma SOD activity demonstrated that SOD2 Ala16Val, a dimorphism leading to substitution in the mitochondrial targeting sequence of SOD2, significantly influences plasma SOD2 activity, and that SOD3 Arg231Gly, leading to substitution in the heparin-binding domain of SOD3, significantly influences plasma total SOD activity.	Heparin	303-310	superoxide dismutase 2	Homo sapiens	99-103
15491618-0	2004	Solution structure and heparin interaction of human hepatoma-derived growth factor.	Heparin	23-30	heparin binding growth factor	Homo sapiens	52-82
12837131-2	2003	In the present study, we identify a new heparin-binding region in fibrillin-2 between exons 18 and 24.	Heparin	40-47	fibrillin 2	Homo sapiens	66-77
14528000-4	2003	The MET ectodomain, which behaves as a rod-shaped monomer with a large Stokes radius in solution, binds HGF/SF in the absence or presence of heparin, and forms a stable HGF/SF-heparin-MET complex with 1:1:1 stoichiometry.	Heparin	176-183	hepatocyte growth factor	Homo sapiens	169-175
19016244-6	2008	Analyses of associations between SOD genotypes and levels of plasma SOD activity demonstrated that SOD2 Ala16Val, a dimorphism leading to substitution in the mitochondrial targeting sequence of SOD2, significantly influences plasma SOD2 activity, and that SOD3 Arg231Gly, leading to substitution in the heparin-binding domain of SOD3, significantly influences plasma total SOD activity.	Heparin	303-310	superoxide dismutase 2	Homo sapiens	194-198
19016244-6	2008	Analyses of associations between SOD genotypes and levels of plasma SOD activity demonstrated that SOD2 Ala16Val, a dimorphism leading to substitution in the mitochondrial targeting sequence of SOD2, significantly influences plasma SOD2 activity, and that SOD3 Arg231Gly, leading to substitution in the heparin-binding domain of SOD3, significantly influences plasma total SOD activity.	Heparin	303-310	superoxide dismutase 2	Homo sapiens	194-198
18796646-0	2008	Sulfated oligosaccharides (heparin and fucoidan) binding and dimerization of stromal cell-derived factor-1 (SDF-1/CXCL 12) are coupled as evidenced by affinity CE-MS analysis.	Heparin	27-34	C-X-C motif chemokine ligand 12	Homo sapiens	77-106
12963372-0	2003	Distinct requirements for heparin and alpha-dystroglycan binding revealed by structure-based mutagenesis of the laminin alpha2 LG4-LG5 domain pair.	Heparin	26-33	laminin subunit alpha 2	Homo sapiens	112-126
15726889-1	2004	Native Fucoidan and unfractionated heparin enhanced by 6-fold the in vitro activation of human glutamic plasminogen (Glu-Plg) by tissue plasminogen activator (t-PA) using 0.05M Tris buffer pH 7.4, while sulfated fucoidan inhibited the activation under these conditions.	Heparin	35-42	plasminogen	Homo sapiens	121-124
15726889-5	2004	The results showed that heparin interacted with Glu-Plg while native fucoidan and sulfated fucoidan interacted with t-PA.	Heparin	24-31	plasminogen	Homo sapiens	52-55
15726889-6	2004	Studies were also conducted on the effect of the two fucoidans and heparin on the activation of Glu-Plg by t-PA using 0.05M Tris buffer pH 7.4 containing 0.1 M NaCl.	Heparin	67-74	plasminogen	Homo sapiens	100-103
12963372-3	2003	We have used site-directed mutagenesis and in vitro binding assays to map the binding sites on the laminin alpha2 chain LG4-LG5 domain pair for alpha-DG, heparin and sulfatides.	Heparin	154-161	laminin subunit alpha 2	Homo sapiens	99-113
18796646-0	2008	Sulfated oligosaccharides (heparin and fucoidan) binding and dimerization of stromal cell-derived factor-1 (SDF-1/CXCL 12) are coupled as evidenced by affinity CE-MS analysis.	Heparin	27-34	C-X-C motif chemokine ligand 12	Homo sapiens	108-113
18796646-0	2008	Sulfated oligosaccharides (heparin and fucoidan) binding and dimerization of stromal cell-derived factor-1 (SDF-1/CXCL 12) are coupled as evidenced by affinity CE-MS analysis.	Heparin	27-34	C-X-C motif chemokine ligand 12	Homo sapiens	114-121
12941044-6	2003	SR121903 displaced PF4-bound heparin, whereas SanOrg123781 did not, underlining the importance of the charge of the molecule for the interaction with PF4.	Heparin	29-36	platelet factor 4	Homo sapiens	19-22
12922167-2	2003	Other activities arise from VCP"s ability to strongly bind heparin.	Heparin	59-66	valosin containing protein	Homo sapiens	28-31
12922167-3	2003	To map regions within VCP involved in binding complement and heparin experimentally, surface plasmon resonance (SPR) and recombinantly expressed VCP (rVCP) constructs were employed.	Heparin	61-68	valosin containing protein	Homo sapiens	22-25
15223307-8	2004	treatment with heparin, an IP(3) receptor antagonist, prevented the increase of pain threshold induced by the investigated compound, analgesia that was restored by co-administration of D-myo-inositol.	Heparin	15-22	inositol 1,4,5-triphosphate receptor 3	Mus musculus	27-41
15223308-5	2004	In mice undergoing treatment with LiCl, which impairs phosphatidylinositol synthesis, or treatment with heparin, an IP(3)-receptor antagonist, the hyperalgesia induced by the H(1)-receptor agonist remained unchanged.	Heparin	104-111	inositol 1,4,5-triphosphate receptor 3	Mus musculus	116-130
15205701-0	2004	[Release of hepatocyte growth factor mediated by heparin].	Heparin	49-56	hepatocyte growth factor	Homo sapiens	12-36
15205701-1	2004	OBJECTIVE: To observe the effects of sodium heparin and low molecular weight heparin on the release of plasma hepatocyte growth factor (HGF) in senior coronary heart disease patients.	Heparin	37-51	hepatocyte growth factor	Homo sapiens	110-134
15205701-1	2004	OBJECTIVE: To observe the effects of sodium heparin and low molecular weight heparin on the release of plasma hepatocyte growth factor (HGF) in senior coronary heart disease patients.	Heparin	37-51	hepatocyte growth factor	Homo sapiens	136-139
18983520-1	2008	BACKGROUND: Treatment of heparin-induced thrombocytopenia (HIT), a disorder in which anti-platelet factor 4 (PF4)-heparin antibodies cause platelet activation and hypercoagulability, requires alternative (non-heparin) anticoagulation.	Heparin	25-32	platelet factor 4	Homo sapiens	109-112
15205701-1	2004	OBJECTIVE: To observe the effects of sodium heparin and low molecular weight heparin on the release of plasma hepatocyte growth factor (HGF) in senior coronary heart disease patients.	Heparin	44-51	hepatocyte growth factor	Homo sapiens	110-134
15205701-1	2004	OBJECTIVE: To observe the effects of sodium heparin and low molecular weight heparin on the release of plasma hepatocyte growth factor (HGF) in senior coronary heart disease patients.	Heparin	44-51	hepatocyte growth factor	Homo sapiens	136-139
15205701-4	2004	RESULTS: Plasma HGF was increased rapidly and significantly after intravenous injection of sodium heparin, reaching its peak level (about 48 fold) after approximately 10 minutes.	Heparin	91-105	hepatocyte growth factor	Homo sapiens	16-19
15205701-5	2004	Plasma HGF was also increased rapidly and significantly after subcutaneous injection of sodium heparin and LMWH, reaching its peak level (about 4 and 5 fold in sodium heparin and LMWH respectively) after approximately 2-3 hours.	Heparin	88-102	hepatocyte growth factor	Homo sapiens	7-10
15205701-5	2004	Plasma HGF was also increased rapidly and significantly after subcutaneous injection of sodium heparin and LMWH, reaching its peak level (about 4 and 5 fold in sodium heparin and LMWH respectively) after approximately 2-3 hours.	Heparin	160-174	hepatocyte growth factor	Homo sapiens	7-10
15205701-6	2004	CONCLUSION: The rise of plasma HGF after heparin treatment suggests that heparin has some other biological effects in addition to its anticoagulant property through HGF.	Heparin	41-48	hepatocyte growth factor	Homo sapiens	31-34
12882838-8	2003	The inhibitory effect of PF4 on CD1a expression was reversed by 50 U/ml heparin.	Heparin	72-79	platelet factor 4	Homo sapiens	25-28
12882838-8	2003	The inhibitory effect of PF4 on CD1a expression was reversed by 50 U/ml heparin.	Heparin	72-79	CD1a molecule	Homo sapiens	32-36
18805795-8	2008	Competition assays showed that PEDF can bind heparin and HA simultaneously.	Heparin	45-52	serpin family F member 1	Homo sapiens	31-35
12754204-8	2003	Heparin inhibition of endogenous inositol trisphosphate receptors (IP3R) had little effect on intracellular Ca2+ handling or viability.	Heparin	0-7	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	67-71
12689334-0	2003	Interaction of the 268-282 region of glycoprotein Ibalpha with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII.	Heparin	67-74	coagulation factor VIII	Homo sapiens	134-145
12689334-2	2003	Full FVIII activation requires cleavage at Arg(372), a process involving the alpha-thrombin exosite-II; referred to as heparin-binding site (HBS).	Heparin	119-126	coagulation factor VIII	Homo sapiens	5-10
15044471-6	2004	In addition, ACP binds soluble heparin specifically in inhibition and dot blot assays.	Heparin	31-38	NADH:ubiquinone oxidoreductase subunit AB1	Homo sapiens	13-16
18791163-3	2008	Short-term use of unfractionated heparin (UFH) for CPB, with restriction of UFH to the surgery itself, is safe and effective in patients with a history of HIT who test negative for antiplatelet factor 4 (PF4)/heparin antibodies.	Heparin	33-40	platelet factor 4	Homo sapiens	204-207
15144459-14	2004	CONCLUSION: Data indicate that anti-thrombin III affects eosinophil motility via the effects of its heparin-binding site on cell surface syndecan-4.	Heparin	100-107	syndecan 4	Homo sapiens	137-147
12856386-1	2003	Low molecular weight heparins (LMWHs) stimulate the release of endothelial tissue factor pathway inhibitor (TFPI).	Heparin	21-29	tissue factor pathway inhibitor	Homo sapiens	75-106
12856386-1	2003	Low molecular weight heparins (LMWHs) stimulate the release of endothelial tissue factor pathway inhibitor (TFPI).	Heparin	21-29	tissue factor pathway inhibitor	Homo sapiens	108-112
18791163-3	2008	Short-term use of unfractionated heparin (UFH) for CPB, with restriction of UFH to the surgery itself, is safe and effective in patients with a history of HIT who test negative for antiplatelet factor 4 (PF4)/heparin antibodies.	Heparin	42-45	platelet factor 4	Homo sapiens	204-207
12684510-0	2003	Two different heparin-binding domains in the triple-helical domain of ColQ, the collagen tail subunit of synaptic acetylcholinesterase.	Heparin	14-21	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	70-74
15151481-3	2004	Three European clinical trials, designated Heparin-Associated Thrombocytopenia (HAT)-1, -2 and -3, demonstrated the efficacy and safety of lepirudin in the prevention and treatment of thrombosis in patients with antibody-confirmed heparin-induced thrombocytopenia.	Heparin	231-238	histone acetyltransferase 1	Homo sapiens	43-97
12684510-2	2003	To get insights about this function, the interaction of ColQ with heparin was analyzed.	Heparin	66-73	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	56-60
18652856-8	2008	The chemically constructed TAT-ASNase conjugates not only were able to translocate into the MOLT-4 cells and elicit the cytotoxic effects, but also this PTD-mediated intracellular drug uptake could be regulated (with on/off control) by the addition of heparin and protamine.	Heparin	252-259	asparaginase	Homo sapiens	31-37
12684510-3	2003	For this, heparin affinity chromatography of the complete oligomeric enzyme carrying different mutations in ColQ was performed.	Heparin	10-17	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	108-112
12684510-4	2003	Results demonstrate that only the two predicted heparin-binding domains present in the collagen domain of ColQ are responsible for heparin interaction.	Heparin	48-55	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	106-110
12684510-4	2003	Results demonstrate that only the two predicted heparin-binding domains present in the collagen domain of ColQ are responsible for heparin interaction.	Heparin	131-138	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	106-110
12684510-7	2003	Thus, ColQ possesses two heparin-binding domains with different properties that may have non-redundant functions.	Heparin	25-32	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	6-10
12889827-3	2003	When beta-glucuronidase (GUS) reporter gene activity was evaluated in heparin-treated (0.6%), 14-month old callus following microprojectile bombardment, GUS activity increased 1000-fold compared to equivalent aged untreated Penn A4 callus.	Heparin	70-77	glucuronidase beta	Homo sapiens	5-23
12889827-3	2003	When beta-glucuronidase (GUS) reporter gene activity was evaluated in heparin-treated (0.6%), 14-month old callus following microprojectile bombardment, GUS activity increased 1000-fold compared to equivalent aged untreated Penn A4 callus.	Heparin	70-77	glucuronidase beta	Homo sapiens	25-28
12889827-3	2003	When beta-glucuronidase (GUS) reporter gene activity was evaluated in heparin-treated (0.6%), 14-month old callus following microprojectile bombardment, GUS activity increased 1000-fold compared to equivalent aged untreated Penn A4 callus.	Heparin	70-77	glucuronidase beta	Homo sapiens	153-156
14963717-8	2004	In contrast, the mitogenic effects of the platelet-derived and the heparin-binding epidermal growth factors were dependent on p44/p42 MAPK activation and independent of activation of p38 MAPK.	Heparin	67-74	interferon induced protein 44	Homo sapiens	126-129
15209550-7	2004	The PMNE concentration was significantly lower in the OPCAB group and the heparin-coated group as compared to the PMEA-coated group both at the end of CPB and 4 hours after CPB.	Heparin	74-81	elastase, neutrophil expressed	Homo sapiens	4-8
14630814-4	2004	Heparin administration increased tPA activity and its mRNA expression at 6 and 12 hours after MCAO in the ischemic hemispheres of WT mice.	Heparin	0-7	plasminogen activator, tissue	Mus musculus	33-36
14630814-6	2004	We also observed an exacerbation of matrix metalloproteinase (MMP) 9 expression at the mRNA level and its conversion to an active form after heparin administration in the ischemic hemisphere in WT mice but not in tPA KO mice.	Heparin	141-148	matrix metallopeptidase 9	Mus musculus	36-68
14630814-8	2004	These findings suggest that endogenous tPA, through the enhancement of MMP 9 expression and proteolytic activation, plays an essential role in the pathogenesis of heparin-produced cerebral hemorrhage.	Heparin	163-170	plasminogen activator, tissue	Mus musculus	39-42
14630814-8	2004	These findings suggest that endogenous tPA, through the enhancement of MMP 9 expression and proteolytic activation, plays an essential role in the pathogenesis of heparin-produced cerebral hemorrhage.	Heparin	163-170	matrix metallopeptidase 9	Mus musculus	71-76
12801846-1	2003	BACKGROUND AND OBJECTIVES: Unfractionated heparin and low molecular weight heparins exert their anticoagulant effect by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	42-49	tissue factor pathway inhibitor	Homo sapiens	131-162
18664596-2	2008	Four hours of insulin infusion (4.8 mU.kg(-1).min(-1)) without or with lipid-heparin infusion (to produce insulin resistance) decreased hepatic MMP-2 mRNA (by RT-PCR), pro-MMP-2, MMP-2, MMP-9, and MT1-MMP (all by Western blots) and the gelatinolytic activity of MMP-2 (by gelatin zymography) by approximately 60-80%.	Heparin	77-84	matrix metallopeptidase 2	Rattus norvegicus	144-149
12801846-1	2003	BACKGROUND AND OBJECTIVES: Unfractionated heparin and low molecular weight heparins exert their anticoagulant effect by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	42-49	tissue factor pathway inhibitor	Homo sapiens	164-168
12801846-1	2003	BACKGROUND AND OBJECTIVES: Unfractionated heparin and low molecular weight heparins exert their anticoagulant effect by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	75-83	tissue factor pathway inhibitor	Homo sapiens	131-162
12801846-1	2003	BACKGROUND AND OBJECTIVES: Unfractionated heparin and low molecular weight heparins exert their anticoagulant effect by mobilizing tissue factor pathway inhibitor (TFPI) from the vascular endothelium into the blood circulation.	Heparin	75-83	tissue factor pathway inhibitor	Homo sapiens	164-168
12801846-8	2003	With long periods of incubation (24-48h), both unfractionated heparin and enoxaparin significantly increased TFPI release (control vs. unfractionated heparin, p&lt;0.05-0.001; control vs. enoxaparin, p&lt;0.01-0.001) and also reduced the release of vWF in the culture medium, though no variations in endothelial cell procoagulant activity or TF content were observed.	Heparin	62-69	tissue factor pathway inhibitor	Homo sapiens	109-113
14981145-3	2004	As leiomyomas are benign neoplasias of smooth muscle cells, we sought to understand the regulation of uterine smooth muscle cell mitogenesis by CCN5, a growth arrest-specific gene in vascular smooth muscle cells which is induced and maintained by heparin treatment.	Heparin	247-254	cellular communication network factor 5	Homo sapiens	144-148
14981145-5	2004	Surprisingly, we show that even though CCN5 is induced by heparin in vascular smooth muscle cells, treatment with heparin does not induce CCN5 expression in human uterine smooth muscle cells.	Heparin	58-65	cellular communication network factor 5	Homo sapiens	39-43
18566753-15	2008	Immunoblotting with this antibody showed that heparin and 4,5,6,7-tetrabromobenzotriazole (TBB), known CK2 inhibitors, inhibited in vitro phosphorylation of Cdc37 on Ser13 by CK2 holoenzyme or CK2alpha, confirming the specificity of the antibody to detect CK2 activity.	Heparin	46-53	cell division cycle 37, HSP90 cochaperone	Homo sapiens	157-162
15030181-0	2004	Differential prevalence of anti-heparin-PF4 immunoglobulin subtypes in patients treated with clivarin and heparin: implications in the HIT pathogenesis.	Heparin	32-39	platelet factor 4	Homo sapiens	40-43
12571234-3	2003	In this study, we performed an extensive mutational analysis to identify the CXCR3 and heparin binding sites of murine IP-10.	Heparin	87-94	chemokine (C-X-C motif) ligand 10	Mus musculus	119-124
12571234-5	2003	Double mutations neutralizing adjacent basic residues at the C terminus did not lead to a significant reduction in heparin binding, indicating that the main heparin binding site of IP-10 is not along the C-terminal alpha helix.	Heparin	157-164	chemokine (C-X-C motif) ligand 10	Mus musculus	181-186
12571234-10	2003	CXCR3 expressing GAG-deficient Chinese hamster ovary cells revealed that GAG binding was not required for IP-10 binding and signaling through CXCR3, which suggests that the CXCR3 and heparin binding sites of IP-10 are partially overlapping.	Heparin	183-190	chemokine (C-X-C motif) ligand 10	Mus musculus	208-213
14995994-6	2004	Heparin enhanced plasmin generation by both rt-PA and ru-PA.	Heparin	0-7	plasminogen	Homo sapiens	17-24
19378419-10	2008	Soluble heparin and K252a, an inhibitor of Trk, blocked CTGF-induced production of the above chemokines and the activation of the above signaling proteins.	Heparin	8-15	cellular communication network factor 2	Homo sapiens	56-60
15078125-2	2004	Although AT and HCII are structural homologs, only heparin binds to AT, and HCII has different binding sites for heparin and dermatan sulfate.	Heparin	113-120	serpin family D member 1	Homo sapiens	76-80
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Heparin	28-35	serpin family D member 1	Homo sapiens	141-145
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Heparin	167-174	serpin family D member 1	Homo sapiens	141-145
15078125-6	2004	Whereas it inactivates the binding site for AT causing a drop of the anticoagulant activity, it enhances the HCII-associated activity of both heparin and dermatan sulfate.	Heparin	142-149	serpin family D member 1	Homo sapiens	109-113
12736633-5	2003	In mice undergoing treatment with LiCl, which impairs phosphatidylinositol synthesis, or treatment with heparin, an IP(3) receptor antagonist, the antinociception induced by physostigmine and oxotremorine was dose-dependently antagonized.	Heparin	104-111	inositol 1,4,5-triphosphate receptor 3	Mus musculus	116-130
12877576-2	2003	Heparin and 6-AH inhibited streptokinase-mediated activation of Glu-Plg using 10 mM Tris-HCl buffer pH 7.4.	Heparin	0-7	plasminogen	Homo sapiens	68-71
12877576-4	2003	Increasing the ionic strength of Tris-HCl buffer from 10 to 50 mM or addition of 50-150 mM of NaCl to 50 mM Tris-HCl pH 7.4 inhibited the activation of Glu-Plg by streptokinase while decreasing the % inhibition by heparin over the control samples.	Heparin	214-221	plasminogen	Homo sapiens	156-159
12877576-5	2003	Double reciprocal plot of the activation of Glu-Plg by streptokinase using 50 mM Tris-HCl pH 7.4 containing 100 mM NaCl showed that the addition of heparin lowered Vmax by 50% without affecting Km.	Heparin	148-155	plasminogen	Homo sapiens	48-51
12877576-6	2003	To determine whether the inhibitory effect of heparin was specifically directed towards Glu-Plg or streptokinase, the ratios of the initial rate of plasmin generation in the presence of heparin over the controls were plotted against the inverse of the volume fraction of Glu-Plg or streptokinase after serial dilutions.	Heparin	46-53	plasminogen	Homo sapiens	92-95
15557744-9	2004	These results suggest that, although p37-0 may become a substrate for the heparin-sensitive protein kinase (PK) in vitro, only p37-1 is a substrate for p40 production catalyzed by heparin-sensitive PK in animal cells, and staurosporine-sensitive PK is involved in the production of more phosphorylated forms of p37, but not in p37-1 production from p37-0.	Heparin	74-81	nucleoporin 37	Homo sapiens	37-40
19051709-4	2008	Heparin, in the affected individual binds with platelet factor 4 (PF-4) and forms a highly antigenic Heparin PF-4 complex which leads to the generation of specific IgG Heparin PF4 antibodies (also called HIT antibodies).	Heparin	0-7	platelet factor 4	Homo sapiens	176-179
18346949-7	2008	Within 96 h, 17.0+/-0.1 and 10.1+/-0.2% of the used BMP-2 was released from non-modified and heparinized Ecopore/collagen, respectively, indicating that the heparin modification retarded BMP-2 release.	Heparin	93-100	bone morphogenetic protein 2	Oryctolagus cuniculus	52-57
14500581-5	2003	Intracellular application of the IP3 receptor antagonist heparin abolished fNT-induced electrical activity.	Heparin	57-64	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	33-45
12674336-4	2003	To mimic activated signaling by mutated FGF receptors, we used heparin acrylic beads to deliver FGF ligands to mouse calvaria and demonstrated increased Msx2, Runx2, Bsp, and Osteocalcin gene expression, decreased cell proliferation, and suture obliteration and fusion.	Heparin	63-70	msh homeobox 2	Mus musculus	153-157
12734405-6	2003	In addition to binding complement, VCP also binds to heparin.	Heparin	53-60	valosin containing protein	Homo sapiens	35-38
18317699-2	2008	BMP-2 released from heparin-conjugated poly(lactic-co-glycolic acid) (HCPLGA) scaffolds stimulates osteogenic differentiation of cultured BMMSCs.	Heparin	20-27	bone morphogenetic protein 2	Homo sapiens	0-5
12641447-4	2003	By utilizing residue-specific chemical modification and site-directed mutagenesis techniques, we revealed that the acidic amino acid residues on PEDF (Asp(255), Asp(257), and Asp(299)) are critical to collagen binding, and three clustered basic amino acid residues (Arg(145), Lys(146), and Arg(148)) are necessary for heparin binding.	Heparin	318-325	serpin family F member 1	Homo sapiens	145-149
12579570-11	2003	Furthermore, addition of heparin with either FGF-1 or FGF-2 into the hydrogel resulted in a significantly enhanced and prolonged vascularization effect.	Heparin	25-32	fibroblast growth factor 2	Mus musculus	54-59
12579570-12	2003	These results indicate that the controlled release of biologically active FGF-1 and FGF-2 with heparin is caused by biodegradation of the chitosan hydrogel, and subsequent induction of vascularization.	Heparin	95-102	fibroblast growth factor 2	Mus musculus	84-89
14574072-0	2003	Plasmin-mediated proteolysis of vascular endothelial cell heparin releasable tissue factor pathway inhibitor.	Heparin	58-65	plasminogen	Homo sapiens	0-7
14652650-13	2003	From our results, we can conclude that endotoxin-induced adhesion of leukocytes to endothelium can be reversed by ligation of syndecan-4 with antithrombin"s heparin-binding site and interferences with stress response signaling events in endothelium.	Heparin	157-164	syndecan 4	Homo sapiens	126-136
12912996-2	2003	In the present study, we examined the effects of heparin on the BMP activities in C2C12 myoblasts.	Heparin	49-56	bone morphogenetic protein 2	Homo sapiens	64-67
12912996-3	2003	Heparin dose dependently enhanced the osteoblast differentiation induced by not only homodimers of BMP-2 or BMP-4 but also heterodimers of BMP-2/6 or BMP-2/7.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	99-104
12912996-3	2003	Heparin dose dependently enhanced the osteoblast differentiation induced by not only homodimers of BMP-2 or BMP-4 but also heterodimers of BMP-2/6 or BMP-2/7.	Heparin	0-7	bone morphogenetic protein 4	Homo sapiens	108-113
12912996-3	2003	Heparin dose dependently enhanced the osteoblast differentiation induced by not only homodimers of BMP-2 or BMP-4 but also heterodimers of BMP-2/6 or BMP-2/7.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	139-146
12912996-3	2003	Heparin dose dependently enhanced the osteoblast differentiation induced by not only homodimers of BMP-2 or BMP-4 but also heterodimers of BMP-2/6 or BMP-2/7.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	139-144
12912996-5	2003	Heparan sulfate and dextran sulfate also enhanced the BMP-2 activity, although the chemically desulfated heparin-derivatives have lost this stimulatory capacity.	Heparin	105-112	bone morphogenetic protein 2	Homo sapiens	54-59
12912996-6	2003	Heparin dose-dependently suppressed the accumulation of BMP-2 from the culture media into the cell layer or BMPR-IA, and retained a large amount of BMP-2 in the culture media.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	56-61
14574072-0	2003	Plasmin-mediated proteolysis of vascular endothelial cell heparin releasable tissue factor pathway inhibitor.	Heparin	58-65	tissue factor pathway inhibitor	Homo sapiens	77-108
14574072-3	2003	METHODS/RESULTS: Human umbilical vein endothelial cells (HUVEC) were incubated with unfractionated heparin (1.5 U/ml) (to provoke tissue factor pathway inhibitor [TFPI] release) followed by the addition of varying concentrations of alteplase (recombinant tissue plasminogen activator), plasminogen, their combination or plasmin alone.	Heparin	99-106	tissue factor pathway inhibitor	Homo sapiens	130-161
12578541-5	2003	CTGF was exported from DB1 cells as early as 5 min after synthesis and all isoforms were readily purified from conditioned medium by sequential steps of heparin affinity, cation exchange, and reverse-phase chromatography.	Heparin	153-160	cellular communication network factor 2	Homo sapiens	0-4
12912996-6	2003	Heparin dose-dependently suppressed the accumulation of BMP-2 from the culture media into the cell layer or BMPR-IA, and retained a large amount of BMP-2 in the culture media.	Heparin	0-7	bone morphogenetic protein 2	Homo sapiens	148-153
14563580-5	2003	RESULTS: Adverse events, including reocclusion of the recanalized infarct-related coronary artery and major or minor hemorrhagic complications, occurred more frequently in the heparin group (4 of 10 cases) than in the APC group (none of 9 cases) (p = 0.033).	Heparin	176-183	APC regulator of WNT signaling pathway	Homo sapiens	218-221
14563580-6	2003	In the heparin group, plasma PAI activity (IU/ml, median value [range]) was increased continuously from 8 to 24 h after thrombolysis and peaked at 24 h (30.9 [11.3 to 38.5]); on the other hand, it was not increased in the APC group at 24 h after thrombolysis (11.3 [0.0 to 31.0], p &lt; 0.01 vs. heparin group).	Heparin	7-14	APC regulator of WNT signaling pathway	Homo sapiens	222-225
18344410-10	2008	Lipase activity detected in a 1.6 M NaCl-eluted fraction from a heparin-Sepharose column was enhanced by adding purified apoC-II in a dose-dependent manner, whereas that eluted by 0.8 M NaCl was not.	Heparin	64-71	apolipoprotein C2	Homo sapiens	121-128
12885773-4	2003	The presence of heparin, which inhibits laminin interactions, prevents recruitment of Rac1.	Heparin	16-23	ras-related C3 botulinum toxin substrate 1	Oryctolagus cuniculus	86-90
12535616-8	2003	Similarly, PC6A is also able to bind to heparin, whereas soluble furin does not.	Heparin	40-47	proprotein convertase subtilisin/kexin type 5	Homo sapiens	11-15
12537186-4	2003	We therefore undertook a randomized, prospective study of heparin-PF4 antibody formation in patients undergoing first-time CABG given intraoperative bovine or porcine heparin.	Heparin	58-65	platelet factor 4	Homo sapiens	66-69
18388325-5	2008	The IP(3)-induced I(Cat) and [Ca(2+)](i) elevation were attenuated by cation channel (Gd(3+), 2-APB) and IP(3) receptor (xestospongin C, heparin, 2-APB) blockers.	Heparin	137-144	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	105-119
12519315-0	2003	Tissue factor pathway inhibitor (TFPI) release after heparin stimulation is increased in Type 1 diabetic patients with albuminuria.	Heparin	53-60	tissue factor pathway inhibitor	Homo sapiens	0-31
12519315-0	2003	Tissue factor pathway inhibitor (TFPI) release after heparin stimulation is increased in Type 1 diabetic patients with albuminuria.	Heparin	53-60	tissue factor pathway inhibitor	Homo sapiens	33-37
12889008-5	2003	Because the modulation of heparin on monocyte activation could be mediated by its binding via CD14, the main LPS receptor on monocytes, we then studied the binding of LPS and heparin to leukocytes from human blood and to Chinese hamster ovary cells transfected with the human CD14 gene.	Heparin	26-33	CD14 molecule	Homo sapiens	94-98
12889008-10	2003	heparin inhibits the binding of LPS to cells via a CD14-independent pathway.	Heparin	0-7	CD14 molecule	Homo sapiens	51-55
12519315-1	2003	AIMS: To study heparin-stimulated TFPI release in relation to complications in Type 1 diabetic patients.	Heparin	15-22	tissue factor pathway inhibitor	Homo sapiens	34-38
18341586-6	2008	Furthermore, the antibacterial and antifungal activities of trappin-2 were sensitive to NaCl and heparin, demonstrating that its mechanism of action is most probably dependent on its cationic nature.	Heparin	97-104	peptidase inhibitor 3	Homo sapiens	60-69
12519315-8	2003	At all time points after heparin administration, TFPI activity in group III was significantly higher than in group I.	Heparin	25-32	tissue factor pathway inhibitor	Homo sapiens	49-53
12519315-9	2003	TFPI activity was also higher in group III than in group II 5-30 min post-heparin.	Heparin	74-81	tissue factor pathway inhibitor	Homo sapiens	0-4
12519315-13	2003	The increase in heparin-stimulated TFPI release in patients with albuminuria is higher than in patients with retinopathy or without complications.	Heparin	16-23	tissue factor pathway inhibitor	Homo sapiens	35-39
12799194-2	2003	We have studied the mechanism whereby heparin directs FGF-2-induced FGF receptor-1 (FGFR-1) signal transduction.	Heparin	38-45	fibroblast growth factor 2	Cricetulus griseus	54-59
12799194-8	2003	Our data imply that tyrosine 463 is phosphorylated and able to transduce signals in response to FGF-2 treatment alone; furthermore, we suggest that FGFR-1 dimerization/kinase activation is stabilized by heparin.	Heparin	203-210	fibroblast growth factor 2	Cricetulus griseus	96-101
12626395-5	2003	We also show that heparin at low concentrations protects GDNF from proteolytic modification by an endoprotease and also promotes the binding of GDNF to its receptor polypeptide, GFRalpha1.	Heparin	18-25	GDNF family receptor alpha 1	Homo sapiens	178-187
18216069-4	2008	MMP-9, exhibiting high affinity to heparin, was demonstrated to be condensed on tips of cellular podia.	Heparin	35-42	matrix metallopeptidase 9	Mus musculus	0-5
12893029-13	2003	The concentration of TFPI was significantly increased following incubation with thrombin and heparin in a dose- and time-dependent manner, although the amount of TFPI mRNA was not changed.	Heparin	93-100	tissue factor pathway inhibitor	Homo sapiens	21-25
12893029-15	2003	Thrombin and heparin stimulated TFPI secretion from PTEC.	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	32-36
12893029-17	2003	The augmentation of TFPI secretion by heparin may play an important role in the modulation of anticoagulant properties of PTEC.	Heparin	38-45	tissue factor pathway inhibitor	Homo sapiens	20-24
12529676-5	2003	Competition experiments showed that 125I-SDF-1 alpha binding to the BMEC cell line 4LHBMEC was inhibited by heparins, heparan sulfate (HS) intestinal mucosa, chondroitin and dermatan sulfate (CS/DS), but not by HS bovine kidney.	Heparin	108-116	C-X-C motif chemokine ligand 12	Homo sapiens	41-46
18230614-5	2008	In BaF3/FGFR2b cells, heparin with at least 10 saccharides and 6-O-, 2-O-, and N-sulfates were required for maximal proliferation.	Heparin	22-29	fibroblast growth factor receptor 2	Mus musculus	8-13
12587674-0	2003	Muscle reinnervation and IGF-I synthesis are affected by exposure to heparin: an effect partially antagonized by anti-growth hormone-releasing hormone.	Heparin	69-76	growth hormone releasing hormone	Rattus norvegicus	118-150
12519080-4	2003	We previously described that the synthetic heparin-binding peptide/III5 (HBP/III5) (WTPPRAQITGYRLTVGLTRR, repeat III5) binds heparin and mediates cell adhesion via chondroitin sulphate proteoglycans.	Heparin	43-50	heme binding protein 1	Homo sapiens	73-81
12519080-4	2003	We previously described that the synthetic heparin-binding peptide/III5 (HBP/III5) (WTPPRAQITGYRLTVGLTRR, repeat III5) binds heparin and mediates cell adhesion via chondroitin sulphate proteoglycans.	Heparin	125-132	heme binding protein 1	Homo sapiens	73-81
18156631-12	2008	This discrepancy is most likely due to selective inhibition of full-length ADAMTS-4 by heparin, particularly for cleavage at the Glu373-Ala374 bond.	Heparin	87-94	ADAM metallopeptidase with thrombospondin type 1 motif 4	Homo sapiens	75-83
12646274-9	2003	The other basic residues on the N terminus, Arg 5, Lys 29, and Arg 31, also contribute to heparin binding by presenting an additional cationic motif.	Heparin	90-97	activity regulated cytoskeleton associated protein	Homo sapiens	63-69
12877576-1	2003	Studies were conducted on the effect of heparin or 6-aminohexanoic acid (6-AH) on the activation of glutamic plasminogen (Glu-Plg) by streptokinase in the presence of different concentrations of buffer, NaCl and divalent cations.	Heparin	40-47	plasminogen	Homo sapiens	126-129
12662405-5	2003	RESULTS: From the mean results from ten patients it was shown that use of heparin plasma resulted in a statistically significant reduction in levels of PAPP-A and that EDTA plasma reduced the levels of PAPP-A dramatically.	Heparin	74-81	pappalysin 1	Homo sapiens	152-158
12509979-2	2003	The p68 subunit is expressed, in the absence of induction, and use of a heparin-Sepharose column produces substantially pure protein.	Heparin	72-79	GATA zinc finger domain containing 2B	Homo sapiens	4-7
12535302-5	2003	Heparin binds to PF4, resulting in a conformational change in the molecule that exposes neo-epitopes that act as immunogens.	Heparin	0-7	platelet factor 4	Homo sapiens	17-20
12381729-4	2002	We have now prepared three different truncated rPAI-1 proteins and demonstrate that PAI-1 conformations control the release of heparin-binding vascular endothelial growth factor (VEGF) isoforms.	Heparin	127-134	vascular endothelial growth factor A	Gallus gallus	179-183
18083224-0	2008	The effect of crosslinking heparin to demineralized bone matrix on mechanical strength and specific binding to human bone morphogenetic protein-2.	Heparin	27-34	bone morphogenetic protein 2	Homo sapiens	117-145
12429572-15	2002	Inositol 1,4,5-triphosphate IP3 receptor inhibitor heparin reduced ACh-induced contraction.	Heparin	51-58	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	28-40
12384988-5	2002	In a similar manner as NH, the modified heparins were capable of inhibiting activation of ERK1 and 2 and DNA synthesis induced by FCS and hbEGF whereas the modified heparins potentiated the mitogenic effect of bFGF and no compound affected PDGF BB-induced ERK activity and SMC growth.	Heparin	40-48	mitogen activated protein kinase 3	Rattus norvegicus	90-100
12645717-8	2003	CONCLUSIONS: The use of a fully heparin-coated system, a centrifugal pump, and a closed circuit during CPB in children (10 kg or less) leads to a lower degree of complement activation and PMN elastase release compared with a conventional system.	Heparin	32-39	elastase, neutrophil expressed	Homo sapiens	188-200
12624625-2	2003	Heparin caused a dose-dependent increase in plasma TFPI concentrations in both arms (ANOVA, p &lt;0.0001).	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	51-55
12624625-3	2003	Estimated net forearm TFPI release was 7 +/- 16, 29 +/- 20 and 138 +/- 72 ng/100 mL tissue/min during 10, 30 and 100 IU/min of heparin respectively (ANOVA, p &lt;0.0001).	Heparin	127-134	tissue factor pathway inhibitor	Homo sapiens	22-26
12624625-4	2003	Compared to the systemic circulation, the forearm sensitivity to heparin induced TFPI release was 3.6-fold lower (166 +/- 67 ng/IU vs. 596 +/- 252 ng/IU: t-test, p = 0.004).	Heparin	65-72	tissue factor pathway inhibitor	Homo sapiens	81-85
12384988-5	2002	In a similar manner as NH, the modified heparins were capable of inhibiting activation of ERK1 and 2 and DNA synthesis induced by FCS and hbEGF whereas the modified heparins potentiated the mitogenic effect of bFGF and no compound affected PDGF BB-induced ERK activity and SMC growth.	Heparin	165-173	fibroblast growth factor 2	Rattus norvegicus	210-214
18083224-3	2008	Here, we crosslinked heparin to DBM to increase its BMP-2 binding ability.	Heparin	21-28	bone morphogenetic protein 2	Homo sapiens	52-57
18645924-10	2008	As heparins are strong inhibitors of heparanase, in view of the effect of heparanase on TF/TFPI pathway, the role of heparins" anticoagulant activity may potentially be expanded.	Heparin	3-11	tissue factor pathway inhibitor	Homo sapiens	91-95
12186633-2	2002	We found that recombinant human PrP (rPrP) binds GAGs including chondroitin sulphate A, chondroitin sulphate B, hyaluronic acid, and heparin.	Heparin	133-140	prion protein	Rattus norvegicus	37-41
12186633-5	2002	rPrP binds heparin strongest, and the binding is inhibited by certain heparin analogues, including heparin disaccharide and sulphate-containing monosaccharides, but not by acetylated heparin.	Heparin	11-18	prion protein	Rattus norvegicus	0-4
12186633-5	2002	rPrP binds heparin strongest, and the binding is inhibited by certain heparin analogues, including heparin disaccharide and sulphate-containing monosaccharides, but not by acetylated heparin.	Heparin	70-77	prion protein	Rattus norvegicus	0-4
12186633-5	2002	rPrP binds heparin strongest, and the binding is inhibited by certain heparin analogues, including heparin disaccharide and sulphate-containing monosaccharides, but not by acetylated heparin.	Heparin	70-77	prion protein	Rattus norvegicus	0-4
12186633-8	2002	We further demonstrated that while both wild-type PrPC and an octapeptide-repeat-deleted mutant PrP produced by transfected cells bound heparin at the cell surface, the PrP N-terminal deletion mutant and non-transfectant control failed to bind heparin.	Heparin	136-143	prion protein	Rattus norvegicus	96-99
12186633-8	2002	We further demonstrated that while both wild-type PrPC and an octapeptide-repeat-deleted mutant PrP produced by transfected cells bound heparin at the cell surface, the PrP N-terminal deletion mutant and non-transfectant control failed to bind heparin.	Heparin	244-251	prion protein	Rattus norvegicus	96-99
12904124-6	2003	Despite these risks, the benefits of GPI therapy in addition to conventional treatment, such as aspirin and heparin, should be considered for these high-risk patients.	Heparin	108-115	glucose-6-phosphate isomerase	Homo sapiens	37-40
14693175-6	2003	Next, since Coamatic( Heparin contains dextran sulfate (DXS) to reduce the influence of heparin antagonists such as platelet factor 4 (PF4), whereas Rotachrom Heparin does not, we hypothesized that the dextran sulfate contained in the reagent might explain this discrepancy.	Heparin	22-29	platelet factor 4	Homo sapiens	135-138
14693175-6	2003	Next, since Coamatic( Heparin contains dextran sulfate (DXS) to reduce the influence of heparin antagonists such as platelet factor 4 (PF4), whereas Rotachrom Heparin does not, we hypothesized that the dextran sulfate contained in the reagent might explain this discrepancy.	Heparin	88-95	platelet factor 4	Homo sapiens	135-138
18686880-8	2008	Despite the complex therapy including higher doses of a low-molecular-weight heparin, ischemization of the whole left upper extremity and distal part of right shank and foot occurred.	Heparin	77-84	SH3 and multiple ankyrin repeat domains 2	Homo sapiens	159-164
12221095-9	2002	The kinetic constants k(a), k(d), and K(d) suggested that MK, PTN, FGF-16, FGF-18, and HB-EGF bound strongly to CS-E, in comparable degrees to the binding to Hep, whereas the intensity of binding of FGF-2 and FGF-10 toward CS-E was lower than that for Hep.	Heparin	158-161	pleiotrophin	Rattus norvegicus	62-65
18925524-0	2008	Elevated hepatocyte growth factor levels at the beginning of high-flux hemodialysis are due to heparin administration.	Heparin	95-102	hepatocyte growth factor	Homo sapiens	9-33
12213822-2	2002	Human heparanase is an endo-beta-d-glucuronidase that degrades heparan sulfate/heparin and has been implicated in a variety of biological processes, such as inflammation, tumor angiogenesis, and metastasis.	Heparin	79-86	glucuronidase beta	Homo sapiens	28-48
12370176-5	2002	Heparin and heparan sulfate, but not dermatan or chondroitin sulfate, effectively compete for PAPP-A surface binding, and because incubation of cells with heparinase abrogated PAPP-A adhesion, binding is probably mediated by a cell surface heparan sulfate proteoglycan.	Heparin	0-7	pappalysin 1	Homo sapiens	94-100
12370176-5	2002	Heparin and heparan sulfate, but not dermatan or chondroitin sulfate, effectively compete for PAPP-A surface binding, and because incubation of cells with heparinase abrogated PAPP-A adhesion, binding is probably mediated by a cell surface heparan sulfate proteoglycan.	Heparin	0-7	pappalysin 1	Homo sapiens	176-182
12492611-0	2002	Quantification of heparin-induced TFPI release: a maximum release at low heparin dose.	Heparin	18-25	tissue factor pathway inhibitor	Homo sapiens	34-38
12492611-0	2002	Quantification of heparin-induced TFPI release: a maximum release at low heparin dose.	Heparin	73-80	tissue factor pathway inhibitor	Homo sapiens	34-38
12492611-1	2002	AIMS: Heparin releases tissue factor pathway inhibitor (TFPI) from the endothelium and this release may decrease after repeated high dose heparin administration.	Heparin	138-145	tissue factor pathway inhibitor	Homo sapiens	23-54
12492611-1	2002	AIMS: Heparin releases tissue factor pathway inhibitor (TFPI) from the endothelium and this release may decrease after repeated high dose heparin administration.	Heparin	138-145	tissue factor pathway inhibitor	Homo sapiens	56-60
12492611-8	2002	The relationship between heparin concentration (anti-IIa activity) and TFPI concentration followed a maximum effect model and a clockwise loop (proteresis) was observed.	Heparin	25-32	tissue factor pathway inhibitor	Homo sapiens	71-75
12492611-9	2002	The TFPI release rate rapidly increased to maximum of 200 +/- 45 micro g min-1 after 17.5 min heparin infusion but did not increase further although heparin concentrations further doubled.	Heparin	94-101	tissue factor pathway inhibitor	Homo sapiens	4-8
12492611-11	2002	CONCLUSIONS: Our application of concentration-effect models and pharmacokinetic principles to these haemostatic variables showed that endothelial TFPI release has a maximum that is already reached at low heparin dose, corresponding with an anti-IIa activity of 0.08 IU ml-1.	Heparin	204-211	tissue factor pathway inhibitor	Homo sapiens	146-150
12492611-13	2002	These findings may be of importance for the heparin dose used in conditions such as unstable angina, in which the favourable effects of heparin have been ascribed to its ability to release TFPI.	Heparin	44-51	tissue factor pathway inhibitor	Homo sapiens	189-193
12492611-13	2002	These findings may be of importance for the heparin dose used in conditions such as unstable angina, in which the favourable effects of heparin have been ascribed to its ability to release TFPI.	Heparin	136-143	tissue factor pathway inhibitor	Homo sapiens	189-193
12372763-6	2002	CaMK but not PKA signaling is suppressed by low concentrations of heparin.	Heparin	66-73	calcium/calmodulin dependent protein kinase IV	Homo sapiens	0-4
12391192-8	2002	Finally, biosensor-based binding kinetic analysis revealed that IFN-kappa, like IFN-beta, binds strongly to heparin (K(d): 2.1 nM), suggesting that the cytokine can be retained close to the local site of production.	Heparin	108-115	interferon beta 1	Homo sapiens	80-88
18037384-0	2007	Heparin enhances the furin cleavage of HIV-1 gp160 peptides.	Heparin	0-7	furin, paired basic amino acid cleaving enzyme	Homo sapiens	21-26
12417924-3	2002	Association on the single nucleotide polymorphisms (SNPs) in the HL gene to post-heparin plasma HL activity and the plasma HDL-cholesterol concentration have been investigated thoroughly, but to date, little is known about th is in Chinese.	Heparin	81-88	lipase C, hepatic type	Homo sapiens	65-67
12417924-3	2002	Association on the single nucleotide polymorphisms (SNPs) in the HL gene to post-heparin plasma HL activity and the plasma HDL-cholesterol concentration have been investigated thoroughly, but to date, little is known about th is in Chinese.	Heparin	81-88	lipase C, hepatic type	Homo sapiens	96-98
18037384-0	2007	Heparin enhances the furin cleavage of HIV-1 gp160 peptides.	Heparin	0-7	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	45-50
18037384-4	2007	Our data support the hypothesis of a direct binding of heparin with site1 and site2, allowing selective exposure/accessibility of the REKR sequence, which is only then optimally cleaved by furin.	Heparin	55-62	furin, paired basic amino acid cleaving enzyme	Homo sapiens	189-194
12379743-6	2002	HIV-1- or gp120-induced apoptosis of rat myocytes through a mitochondrion-controlled pathway, which was inhibited by heparin, AOP-RANTES, or pertussis toxin, suggesting that cardiomyocyte apoptosis is induced by signaling through chemokine receptors.	Heparin	117-124	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	10-15
17879163-3	2007	Here we report that an altered matrix, consisting of a mutated, nonfunctional high-affinity heparin-binding domain and the V region of fibronectin (V+H-), induced anoikis in human SCC cells; this response was blocked by inhibitors of caspase-8 and caspase-3.	Heparin	92-99	caspase 8	Homo sapiens	234-243
17879163-8	2007	These findings provide evidence that mutations in the high-affinity heparin-binding domain in association with the V region of fibronectin, or altered fibronectin matrices, induce anoikis in human SCC cells by modulating integrin alpha v-mediated phosphorylation of FAK and ERK.	Heparin	68-75	protein tyrosine kinase 2	Homo sapiens	266-269
12130633-4	2002	Previously, we identified heparin-binding sites in the C-terminal globular domain (G domain) of the laminin alpha 4 chain.	Heparin	26-33	laminin subunit alpha 4	Homo sapiens	100-121
17761776-5	2007	An IP(3)-dependent increase of [Ca(2+)](Nuc) was still observed after pretreatment with tetracaine to block Ca(2+) release from ryanodine receptors (RyRs), and the effect of IP(3) was partially reversed or prevented by the IP(3)R blockers heparin and 2-APB.	Heparin	239-246	nucleobindin 1	Homo sapiens	40-43
19649227-3	2002	It has been previously demonstrated that heparin displaces active basic fibroblast growth factor (bFGF) from the lumenal surface of blood vessels.	Heparin	41-48	fibroblast growth factor 2	Rattus norvegicus	66-96
19649227-3	2002	It has been previously demonstrated that heparin displaces active basic fibroblast growth factor (bFGF) from the lumenal surface of blood vessels.	Heparin	41-48	fibroblast growth factor 2	Rattus norvegicus	98-102
17711860-5	2007	In addition, heparin further enhanced the effects of both alphaKlotho and betaKlotho in FGF19 signaling and interaction experiments.	Heparin	13-20	fibroblast growth factor 19	Homo sapiens	88-93
19649227-4	2002	Sequestration of the displaced bFGF by injured areas of the vessel wall is inhibited in the presence of a synthetic nonsulphated heparin-mimicking polyanionic compound (RG-13577).	Heparin	129-136	fibroblast growth factor 2	Rattus norvegicus	31-35
17429586-1	2007	About 0.1-2% of patients receiving heparin develop heparin-induced thrombocytopenia type II (HIT II) which is caused by antibodies directed against heparin-platelet factor 4 (PF4) complexes.	Heparin	35-42	platelet factor 4	Homo sapiens	148-173
12084721-6	2002	Heparin or heparan sulfate displaces FGF3 from binding sites on the cell surface inhibiting the growth of DMI cells and reverts the transformed phenotype ().	Heparin	0-7	fibroblast growth factor 3	Mus musculus	37-41
12084721-7	2002	However, the presence of heparin is necessary to induce a mitogenic response in NIH3T3 cells when stimulated with soluble purified mouse FGF3.	Heparin	25-32	fibroblast growth factor 3	Mus musculus	137-141
17429586-1	2007	About 0.1-2% of patients receiving heparin develop heparin-induced thrombocytopenia type II (HIT II) which is caused by antibodies directed against heparin-platelet factor 4 (PF4) complexes.	Heparin	35-42	platelet factor 4	Homo sapiens	175-178
12173939-2	2002	Heparin activates FGF2 by favoring formation of ternary complexes with its cellular receptors (FGFRs).	Heparin	0-7	fibroblast growth factor 2	Gallus gallus	18-22
17429586-1	2007	About 0.1-2% of patients receiving heparin develop heparin-induced thrombocytopenia type II (HIT II) which is caused by antibodies directed against heparin-platelet factor 4 (PF4) complexes.	Heparin	51-58	platelet factor 4	Homo sapiens	148-173
12173939-7	2002	However, it fully retains the FGF2-binding ability of the original heparin, as shown by its capacity to protect FGF2 from trypsin cleavage and to prevent the formation of heparan sulfate proteoglycan (HSPG)/FGF2/FGFR1 ternary complexes.	Heparin	67-74	fibroblast growth factor 2	Gallus gallus	30-34
12173939-7	2002	However, it fully retains the FGF2-binding ability of the original heparin, as shown by its capacity to protect FGF2 from trypsin cleavage and to prevent the formation of heparan sulfate proteoglycan (HSPG)/FGF2/FGFR1 ternary complexes.	Heparin	67-74	fibroblast growth factor 2	Gallus gallus	112-116
12173939-7	2002	However, it fully retains the FGF2-binding ability of the original heparin, as shown by its capacity to protect FGF2 from trypsin cleavage and to prevent the formation of heparan sulfate proteoglycan (HSPG)/FGF2/FGFR1 ternary complexes.	Heparin	67-74	fibroblast growth factor 2	Gallus gallus	112-116
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Heparin	26-33	serpin family D member 1	Homo sapiens	47-51
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Heparin	116-123	serpin family D member 1	Homo sapiens	69-73
17429586-1	2007	About 0.1-2% of patients receiving heparin develop heparin-induced thrombocytopenia type II (HIT II) which is caused by antibodies directed against heparin-platelet factor 4 (PF4) complexes.	Heparin	51-58	platelet factor 4	Homo sapiens	175-178
17604871-1	2007	As an efficient sustained release system of BMP-2, a functional nanoparticle-hydrogel complex, composed of heparin-functionalized nanoparticles and fibrin gel, was developed and used as a bone graft.	Heparin	107-114	bone morphogenetic protein 2	Rattus norvegicus	44-49
12072492-3	2002	Heparin blocked the binding of both Env-deficient and amphotropic MLV (MLV-A) particles to NIH 3T3 fibroblasts, CHO cells which lack the amphotropic retroviral receptor Pit-2, and CHO cells transfected with Pit-2 (CHO-Pit-2).	Heparin	0-7	sodium-dependent phosphate transporter 2	Cricetulus griseus	169-174
12072492-3	2002	Heparin blocked the binding of both Env-deficient and amphotropic MLV (MLV-A) particles to NIH 3T3 fibroblasts, CHO cells which lack the amphotropic retroviral receptor Pit-2, and CHO cells transfected with Pit-2 (CHO-Pit-2).	Heparin	0-7	sodium-dependent phosphate transporter 2	Cricetulus griseus	207-212
12072492-3	2002	Heparin blocked the binding of both Env-deficient and amphotropic MLV (MLV-A) particles to NIH 3T3 fibroblasts, CHO cells which lack the amphotropic retroviral receptor Pit-2, and CHO cells transfected with Pit-2 (CHO-Pit-2).	Heparin	0-7	sodium-dependent phosphate transporter 2	Cricetulus griseus	214-223
17488345-1	2007	INTRODUCTION: Platelet-activating antiplatelet factor 4/heparin (anti-PF4/heparin) antibodies are the major cause of heparin-induced thrombocytopenia (HIT).	Heparin	56-63	platelet factor 4	Homo sapiens	70-73
12063117-0	2002	Effect of heparin chain length on the interaction with tissue factor pathway inhibitor (TFPI).	Heparin	10-17	tissue factor pathway inhibitor	Homo sapiens	55-86
12063117-0	2002	Effect of heparin chain length on the interaction with tissue factor pathway inhibitor (TFPI).	Heparin	10-17	tissue factor pathway inhibitor	Homo sapiens	88-92
12063117-2	2002	In order to elucidate the minimal size of heparin chain required for the interaction with TFPI, we prepared a series of heparin-derived oligosaccharides with tailored chain length ranged from disaccharide to eicosasaccharide after the successive treatments of heparin, including partial N-desulphation, deaminative cleavage with nitrous acid and gel-filtration.	Heparin	42-49	tissue factor pathway inhibitor	Homo sapiens	90-94
12063117-2	2002	In order to elucidate the minimal size of heparin chain required for the interaction with TFPI, we prepared a series of heparin-derived oligosaccharides with tailored chain length ranged from disaccharide to eicosasaccharide after the successive treatments of heparin, including partial N-desulphation, deaminative cleavage with nitrous acid and gel-filtration.	Heparin	120-127	tissue factor pathway inhibitor	Homo sapiens	90-94
17500071-6	2007	We demonstrate that sFRP-1 is post-translationally modified by tyrosine sulfation at tyrosines 34 and 36, which is inhibited by the treatment of heparin.	Heparin	145-152	secreted frizzled related protein 1	Homo sapiens	20-26
17500071-7	2007	The results suggest that accumulation of sFRP-1 induced by heparin is in part due to the relative stabilization of unsulfated sFRP-1 and the direct stabilization by heparin.	Heparin	59-66	secreted frizzled related protein 1	Homo sapiens	41-47
12071876-0	2002	Heparin-induced thrombocytopenia: detection of antiheparin/PF4 antibodies by means of heparin/PF4-coated beads and flow cytometry.	Heparin	0-7	platelet factor 4	Homo sapiens	59-62
17500071-7	2007	The results suggest that accumulation of sFRP-1 induced by heparin is in part due to the relative stabilization of unsulfated sFRP-1 and the direct stabilization by heparin.	Heparin	59-66	secreted frizzled related protein 1	Homo sapiens	126-132
12071876-0	2002	Heparin-induced thrombocytopenia: detection of antiheparin/PF4 antibodies by means of heparin/PF4-coated beads and flow cytometry.	Heparin	0-7	platelet factor 4	Homo sapiens	94-97
17500071-7	2007	The results suggest that accumulation of sFRP-1 induced by heparin is in part due to the relative stabilization of unsulfated sFRP-1 and the direct stabilization by heparin.	Heparin	165-172	secreted frizzled related protein 1	Homo sapiens	41-47
17500071-8	2007	The study has revealed a multifaceted regulation on sFRP-1 protein by heparin.	Heparin	70-77	secreted frizzled related protein 1	Homo sapiens	52-58
17452490-0	2007	Heparin-mimicking sulfonic acid polymers as multitarget inhibitors of human immunodeficiency virus type 1 Tat and gp120 proteins.	Heparin	0-7	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	114-119
17507826-8	2007	CONCLUSION: Because of its high sensitivity, we believe the PF4 ENHANCED enzyme-linked immunosorbent assay should be used to identify heparin-induced thrombocytopenia in patients with multiple potential causes of thrombocytopenia, although false-positive results will not be uncommon.	Heparin	134-141	platelet factor 4	Homo sapiens	60-63
11994010-3	2002	Similarly, PCI inhibited mutants with identical or improved second-order rate constants (k(2)) in the absence of heparin.	Heparin	113-120	serpin family A member 5	Homo sapiens	11-14
11994010-4	2002	However, the heparin-catalyzed inhibition of mutants by PCI was impaired approximately 10-fold.	Heparin	13-20	serpin family A member 5	Homo sapiens	56-59
17598007-0	2007	Heparin induces mobilization of osteoprotegerin into the circulation.	Heparin	0-7	TNF receptor superfamily member 11b	Homo sapiens	32-47
12108544-1	2002	Heparin-deficient mice, generated by gene targeting of N-deacetylase/N-sulfotransferase-2 (NDST-2), display severe mast cell defects, including an absence of stored mast cell proteases.	Heparin	0-7	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	55-89
12108544-1	2002	Heparin-deficient mice, generated by gene targeting of N-deacetylase/N-sulfotransferase-2 (NDST-2), display severe mast cell defects, including an absence of stored mast cell proteases.	Heparin	0-7	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	91-97
12108544-3	2002	Here we show that NDST-2+/+ bone marrow-derived mast cells cultured in the presence of IL-3 synthesise, in addition to highly sulphated chondroitin sulphate (CS), small amounts of equally highly sulphated heparin-like polysaccharide.	Heparin	205-212	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	18-24
12390693-3	2002	Purification of rhES was performed with heparin affinity chromatography.	Heparin	40-47	RASD family member 2	Homo sapiens	16-20
17598007-3	2007	The objective was to investigate the effect of unfractionated heparin (UFH) and lowmolecular-weight heparin (LMWH; dalteparin) on plasma levels of OPG.	Heparin	62-69	TNF receptor superfamily member 11b	Homo sapiens	147-150
12021535-0	2002	Effect of intraperitoneal administration of low-molecular-weight heparin on plasma tissue factor pathway inhibitor levels in CAPD patients.	Heparin	65-72	tissue factor pathway inhibitor	Homo sapiens	83-114
17598007-3	2007	The objective was to investigate the effect of unfractionated heparin (UFH) and lowmolecular-weight heparin (LMWH; dalteparin) on plasma levels of OPG.	Heparin	71-74	TNF receptor superfamily member 11b	Homo sapiens	147-150
17598007-3	2007	The objective was to investigate the effect of unfractionated heparin (UFH) and lowmolecular-weight heparin (LMWH; dalteparin) on plasma levels of OPG.	Heparin	100-107	TNF receptor superfamily member 11b	Homo sapiens	147-150
17598007-5	2007	UFH boluses of 5,000 IU were given 4 and 24 hours after cessation of regimens A and B. Bolus injection of UFH iv caused a prompt increase in plasma OPG from 0.68 ng/ml (SD = 0.09) to 1.13 ng/ml (SD = 0.30) (p = 0.003) which declined during the continuous UFH infusion and reached baseline values after 8 hours (regime A).	Heparin	0-3	TNF receptor superfamily member 11b	Homo sapiens	148-151
11832488-7	2002	These results suggest the essential roles of DEXT3, its human ortholog EXTL3, and the C. elegans ortholog rib-2 in the biosynthesis of heparan sulfate and heparin, if present, in the respective organisms.	Heparin	155-162	brother of tout-velu	Drosophila melanogaster	45-50
17598007-5	2007	UFH boluses of 5,000 IU were given 4 and 24 hours after cessation of regimens A and B. Bolus injection of UFH iv caused a prompt increase in plasma OPG from 0.68 ng/ml (SD = 0.09) to 1.13 ng/ml (SD = 0.30) (p = 0.003) which declined during the continuous UFH infusion and reached baseline values after 8 hours (regime A).	Heparin	106-109	TNF receptor superfamily member 11b	Homo sapiens	148-151
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	102-109	MET proto-oncogene, receptor tyrosine kinase	Rattus norvegicus	38-53
17598007-5	2007	UFH boluses of 5,000 IU were given 4 and 24 hours after cessation of regimens A and B. Bolus injection of UFH iv caused a prompt increase in plasma OPG from 0.68 ng/ml (SD = 0.09) to 1.13 ng/ml (SD = 0.30) (p = 0.003) which declined during the continuous UFH infusion and reached baseline values after 8 hours (regime A).	Heparin	106-109	TNF receptor superfamily member 11b	Homo sapiens	148-151
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	102-109	MET proto-oncogene, receptor tyrosine kinase	Rattus norvegicus	55-60
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	169-176	MET proto-oncogene, receptor tyrosine kinase	Rattus norvegicus	38-53
17598007-8	2007	We conclude that UFH causes a more pronounced vascular mobilization of OPG than LMWH, indicating that UFH has a higher affinity for OPG than LMWH.	Heparin	17-20	TNF receptor superfamily member 11b	Homo sapiens	71-74
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	169-176	MET proto-oncogene, receptor tyrosine kinase	Rattus norvegicus	55-60
17598007-8	2007	We conclude that UFH causes a more pronounced vascular mobilization of OPG than LMWH, indicating that UFH has a higher affinity for OPG than LMWH.	Heparin	17-20	TNF receptor superfamily member 11b	Homo sapiens	132-135
17598007-8	2007	We conclude that UFH causes a more pronounced vascular mobilization of OPG than LMWH, indicating that UFH has a higher affinity for OPG than LMWH.	Heparin	102-105	TNF receptor superfamily member 11b	Homo sapiens	71-74
17598007-8	2007	We conclude that UFH causes a more pronounced vascular mobilization of OPG than LMWH, indicating that UFH has a higher affinity for OPG than LMWH.	Heparin	102-105	TNF receptor superfamily member 11b	Homo sapiens	132-135
17544586-5	2007	Both increases in ERK1/2 phosphorylation are also inhibited by GM 6001 (a metalloproteinase inhibitor, preventing "shedding" of growth factors), by AG 1478 (a receptor tyrosine kinase inhibitor, preventing epidermal growth factor [EGF] receptor activation), and also partly by heparin (inactivating heparin-binding epidermal growth factor [HB-EGF]), suggesting transactivation of epidermal growth factor receptors (EGFR).	Heparin	277-284	mitogen-activated protein kinase 3	Mus musculus	18-24
11983216-6	2002	The success of the assay is dependent on the use of heparin, an anionic molecule, which neutralizes the positive charge on the highly cationic MBP.	Heparin	52-59	myelin basic protein	Homo sapiens	143-146
17339423-1	2007	The heparan sulfate (HS) proteoglycan, syndecan-1, plays a major role in multiple myeloma (MM) by concentrating heparin-binding growth factors on the surface of MM cells (MMCs).	Heparin	112-119	syndecan 1	Homo sapiens	39-49
11917058-11	2002	CONCLUSION: Serum HGF levels in HD patients are determined by inflammatory conditions such as viral hepatitis and CVD, increase in response to rHuEpo treatment, and may be influenced by type and dose of heparin used during HD procedures.	Heparin	203-210	hepatocyte growth factor	Homo sapiens	18-21
17350678-0	2007	Enhancement of ectopic bone formation by bone morphogenetic protein-2 released from a heparin-conjugated poly(L-lactic-co-glycolic acid) scaffold.	Heparin	86-93	bone morphogenetic protein 2	Homo sapiens	41-69
11741940-1	2002	Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin.	Heparin	227-234	secreted frizzled related protein 1	Homo sapiens	0-35
17350678-2	2007	We found the amount of heparin conjugated to the PLGA scaffolds could be increased up to 3.2-fold by using scaffolds made from star-shaped PLGA, as compared to scaffolds made from linear PLGA, and that the release of BMP-2 from the HP-PLGA scaffold was sustained for at least 14 days in vitro.	Heparin	23-30	bone morphogenetic protein 2	Homo sapiens	217-222
11741940-1	2002	Secreted Frizzled-related protein-1 (sFRP-1), a soluble protein that binds to Wnts and modulates Wnt signaling, contains an N-terminal domain homologous to the putative Wnt-binding site of Frizzled (Fz domain) and a C-terminal heparin-binding domain with weak homology to netrin.	Heparin	227-234	secreted frizzled related protein 1	Homo sapiens	37-43
11741940-6	2002	This latter set of assignments provides experimental verification of one of the disulfide patterns proposed for netrin (NTR) modules and thereby supports the prediction that the C-terminal heparin-binding domain of sFRP-1 is an NTR-type domain.	Heparin	189-196	secreted frizzled related protein 1	Homo sapiens	215-221
11830470-7	2002	Therefore, the binding of KKO to a series of mouse/human PF4 chimeras complexed with heparin was examined.	Heparin	85-92	platelet factor 4	Homo sapiens	57-60
11830470-13	2002	These studies further help to define a portion of the PF4 tetramer to which self-reactive antibodies develop in patients exposed to heparin.	Heparin	132-139	platelet factor 4	Homo sapiens	54-57
11857048-7	2002	Heparin-induced activities of LPL or HL or the response of serum total or LDL-C to the reduced fat diet did not differ between the groups.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	37-39
17785064-1	2007	OBJECTIVE: To investigate the effect of unfitrate heparin (UFH) and low molecular weight heparin (LMWH) on the expression of serum hepatocyte growth factor (HGF) during percutaneous coronary intervention (PCI).	Heparin	50-57	hepatocyte growth factor	Homo sapiens	131-155
11809731-2	2002	HIT is mediated by antibodies directed mostly to epitope(s) formed by complexes between heparin or other anionic mucopolysaccharides and platelet factor 4 (PF4).	Heparin	88-95	platelet factor 4	Homo sapiens	156-159
11711550-0	2002	Heparin inhibits the binding of beta 2-glycoprotein I to phospholipids and promotes the plasmin-mediated inactivation of this blood protein.	Heparin	0-7	plasminogen	Homo sapiens	88-95
11711550-10	2002	Surprisingly, heparin at concentrations that can be achieved in vivo during anticoagulation therapy greatly enhances the plasmin-mediated cleavage of the Lys(317)-Thr(318) site in beta2-GPI.	Heparin	14-21	plasminogen	Homo sapiens	121-128
12438521-8	2002	The CRP-associated increase in infarct size was ameliorated by pretreatment with heparin (n = 7; infarct size 33 +/- 3%; CRP, 2.3 +/- 0.3 mg/dl; P &lt; 0.05) or N-acetylheparin (n = 7; infarct size 23 +/- 4%; CRP, 3.1 +/- 0.5 mg/dl; P &lt; 0.05).	Heparin	81-88	C-reactive protein	Oryctolagus cuniculus	4-7
12438521-8	2002	The CRP-associated increase in infarct size was ameliorated by pretreatment with heparin (n = 7; infarct size 33 +/- 3%; CRP, 2.3 +/- 0.3 mg/dl; P &lt; 0.05) or N-acetylheparin (n = 7; infarct size 23 +/- 4%; CRP, 3.1 +/- 0.5 mg/dl; P &lt; 0.05).	Heparin	81-88	C-reactive protein	Oryctolagus cuniculus	121-124
12438521-8	2002	The CRP-associated increase in infarct size was ameliorated by pretreatment with heparin (n = 7; infarct size 33 +/- 3%; CRP, 2.3 +/- 0.3 mg/dl; P &lt; 0.05) or N-acetylheparin (n = 7; infarct size 23 +/- 4%; CRP, 3.1 +/- 0.5 mg/dl; P &lt; 0.05).	Heparin	81-88	C-reactive protein	Oryctolagus cuniculus	121-124
12351414-7	2002	The results suggest a novel biologic mechanism for the bone disease associated with MM and that treatment of the bone disease with OPG lacking the heparin-binding domain should be considered.	Heparin	147-154	TNF receptor superfamily member 11b	Homo sapiens	131-134
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	neuropilin 1	Homo sapiens	4-16
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	neuropilin 1	Homo sapiens	18-22
17785064-1	2007	OBJECTIVE: To investigate the effect of unfitrate heparin (UFH) and low molecular weight heparin (LMWH) on the expression of serum hepatocyte growth factor (HGF) during percutaneous coronary intervention (PCI).	Heparin	50-57	hepatocyte growth factor	Homo sapiens	157-160
17785064-1	2007	OBJECTIVE: To investigate the effect of unfitrate heparin (UFH) and low molecular weight heparin (LMWH) on the expression of serum hepatocyte growth factor (HGF) during percutaneous coronary intervention (PCI).	Heparin	89-96	hepatocyte growth factor	Homo sapiens	131-155
17785064-1	2007	OBJECTIVE: To investigate the effect of unfitrate heparin (UFH) and low molecular weight heparin (LMWH) on the expression of serum hepatocyte growth factor (HGF) during percutaneous coronary intervention (PCI).	Heparin	89-96	hepatocyte growth factor	Homo sapiens	157-160
17298301-3	2007	The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRalpha1 (GDNF family receptor alpha1), and heparin-bound GDNF is able to bind GFRalpha1 simultaneously.	Heparin	4-11	GDNF family receptor alpha 1	Homo sapiens	129-156
11827173-15	2001	Transfection of cells with CK2alphaE75E76 results in a CK2 activity of extracts that is 90% resistant to heparin demonstrating that a very large proportion of the CK2 activity is derived from the expression of the exogenous mutant.	Heparin	105-112	casein kinase 2 beta S homeolog	Xenopus laevis	27-30
11827173-15	2001	Transfection of cells with CK2alphaE75E76 results in a CK2 activity of extracts that is 90% resistant to heparin demonstrating that a very large proportion of the CK2 activity is derived from the expression of the exogenous mutant.	Heparin	105-112	casein kinase 2 beta S homeolog	Xenopus laevis	55-58
12423248-2	2002	The heparin-resistant binding of [125I]bFGF to TM-BBB4 cells was found to be time-, temperature-, osmolarity- and concentration-dependent.	Heparin	4-11	fibroblast growth factor 2	Mus musculus	39-43
12423248-4	2002	The heparin-resistant binding of [125I]bFGF to TM-BBB4 was significantly inhibited by a cationic polypeptide poly-L-lysine (300 micro m), and compounds which contain a sulfate moiety, e.g. heparin and chondroitin sulfate-B (each 10 micro g/mL).	Heparin	4-11	fibroblast growth factor 2	Mus musculus	39-43
12423248-4	2002	The heparin-resistant binding of [125I]bFGF to TM-BBB4 was significantly inhibited by a cationic polypeptide poly-L-lysine (300 micro m), and compounds which contain a sulfate moiety, e.g. heparin and chondroitin sulfate-B (each 10 micro g/mL).	Heparin	189-196	fibroblast growth factor 2	Mus musculus	39-43
12423248-5	2002	Moreover, the heparin-resistant binding of [125I]bFGF in TM-BBB4 cells was significantly reduced by 50% following treatment with sodium chlorate, suggesting the loss of perlecan (a core protein of heparan sulfate proteoglycan, HSPG) from the extracellular matrix of the cells.	Heparin	14-21	fibroblast growth factor 2	Mus musculus	49-53
17298301-3	2007	The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRalpha1 (GDNF family receptor alpha1), and heparin-bound GDNF is able to bind GFRalpha1 simultaneously.	Heparin	4-11	GDNF family receptor alpha 1	Homo sapiens	198-207
17298301-3	2007	The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRalpha1 (GDNF family receptor alpha1), and heparin-bound GDNF is able to bind GFRalpha1 simultaneously.	Heparin	163-170	GDNF family receptor alpha 1	Homo sapiens	129-156
17298301-3	2007	The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRalpha1 (GDNF family receptor alpha1), and heparin-bound GDNF is able to bind GFRalpha1 simultaneously.	Heparin	163-170	GDNF family receptor alpha 1	Homo sapiens	198-207
17298301-6	2007	Heparin neither inhibits nor potentiates GDNF-GFRalpha1 interaction, and the extracellular domain of GFRalpha1 does not bind to heparin itself, precluding heparin cross-bridging of cytokine and receptor polypeptides.	Heparin	155-162	GDNF family receptor alpha 1	Homo sapiens	101-110
11597998-1	2001	NK1 is a splice variant of the polypeptide growth factor HGF/SF, which consists of the N-terminal (N) and first kringle (K) domain and requires heparan sulfate or soluble heparin for activity.	Heparin	171-178	hepatocyte growth factor	Homo sapiens	57-63
17314405-5	2007	Gamma2sa bound to syndecan-1, and this binding, as well as its cell adhesion activity, was blocked by heparin.	Heparin	102-109	syndecan 1	Homo sapiens	18-28
11685038-11	2001	The present study shows that PF4 is essential for platelet aggregation triggered by the antibodies related to HIT in the presence of heparin.	Heparin	133-140	platelet factor 4	Homo sapiens	29-32
11685038-12	2001	The concentration of PF4 that is available to bind with heparin or with the HIT-related antibodies is critical for platelet aggregation induced by HIT antibodies.	Heparin	56-63	platelet factor 4	Homo sapiens	21-24
11606310-17	2001	Our results indicate that glycosylation of PAR(2) and heparin-inhibition of PAR(2) activation by tryptase could provide novel mechanisms for regulating receptor activation by tryptase and possibly other proteases.	Heparin	54-61	F2R like trypsin receptor 1	Homo sapiens	76-82
11571649-8	2001	Likewise, tyrosine phosphorylation of VEGF receptors, MAPK activity and PI3-kinase activity were all several-fold higher in cells seeded on fibronectin or in the presence of heparin as compared to cells exposed to VEGF alone.	Heparin	174-181	peptidase inhibitor 3	Homo sapiens	72-75
11340591-0	2001	Sustained release of basic fibroblast growth factor and angiogenesis in a novel covalently crosslinked gel of heparin and alginate.	Heparin	110-117	fibroblast growth factor 2	Rattus norvegicus	21-51
12714831-0	2002	Comparative effects of unfractionated heparin and low molecular weight heparin on vascular endothelial cell tissue factor pathway inhibitor release: a model for assessing intrinsic thromboresistance.	Heparin	38-45	tissue factor pathway inhibitor	Homo sapiens	108-139
12714831-0	2002	Comparative effects of unfractionated heparin and low molecular weight heparin on vascular endothelial cell tissue factor pathway inhibitor release: a model for assessing intrinsic thromboresistance.	Heparin	71-78	tissue factor pathway inhibitor	Homo sapiens	108-139
12714831-1	2002	OBJECTIVES: The purpose of our study was to characterize tissue factor pathway inhibitor (TFPI) release from human vascular endothelial cells following daily exposure to varying concentrations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	211-218	tissue factor pathway inhibitor	Homo sapiens	57-88
12714831-1	2002	OBJECTIVES: The purpose of our study was to characterize tissue factor pathway inhibitor (TFPI) release from human vascular endothelial cells following daily exposure to varying concentrations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	211-218	tissue factor pathway inhibitor	Homo sapiens	90-94
12714831-1	2002	OBJECTIVES: The purpose of our study was to characterize tissue factor pathway inhibitor (TFPI) release from human vascular endothelial cells following daily exposure to varying concentrations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	220-223	tissue factor pathway inhibitor	Homo sapiens	57-88
12714831-1	2002	OBJECTIVES: The purpose of our study was to characterize tissue factor pathway inhibitor (TFPI) release from human vascular endothelial cells following daily exposure to varying concentrations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	250-257	tissue factor pathway inhibitor	Homo sapiens	57-88
12714831-1	2002	OBJECTIVES: The purpose of our study was to characterize tissue factor pathway inhibitor (TFPI) release from human vascular endothelial cells following daily exposure to varying concentrations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	250-257	tissue factor pathway inhibitor	Homo sapiens	90-94
12714831-12	2002	The differing effects of UFH and LMWH on vascular endothelial cell TFPI synthesis, release and reserve with prolonged administration require further investigation.	Heparin	25-28	tissue factor pathway inhibitor	Homo sapiens	67-71
12145273-5	2002	Pathol., in press) by our laboratory show an inhibitory effect of heparin on CaMK II phosphorylation and activity.	Heparin	66-73	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	77-84
17270212-0	2007	PWWP module of human hepatoma-derived growth factor forms a domain-swapped dimer with much higher affinity for heparin.	Heparin	111-118	heparin binding growth factor	Homo sapiens	21-51
12204897-7	2002	Total protein, cell number, and FGF-2 protein expression and mRNA of FGF-1, -2, and FGF receptor-2 detected by reverse transcriptase-polymerase chain reaction were decreased by heparin.	Heparin	177-184	fibroblast growth factor 2	Rattus norvegicus	32-37
12223528-2	2002	This ability was retained even while PF4 was bound to heparin.	Heparin	54-61	platelet factor 4	Homo sapiens	37-40
11692908-6	2001	Diagnosis of heparin-induced thrombocytopenia was confirmed by positivity of anti-heparin-PF4 antibodies.	Heparin	13-20	platelet factor 4	Homo sapiens	90-93
17380220-0	2007	Effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells.	Heparin	11-18	matrix metallopeptidase 2	Rattus norvegicus	75-101
11449373-0	2001	IgM and stromal cell-associated heparan sulfate/heparin as complement-independent ligands for CD19.	Heparin	48-55	CD19 antigen	Mus musculus	94-98
11390981-1	2001	The tumor suppressors EXT1 and EXT2 are associated with hereditary multiple exostoses and encode bifunctional glycosyltransferases essential for chain polymerization of heparan sulfate (HS) and its analog, heparin (Hep).	Heparin	206-213	exostosin glycosyltransferase 1	Homo sapiens	22-26
11390981-1	2001	The tumor suppressors EXT1 and EXT2 are associated with hereditary multiple exostoses and encode bifunctional glycosyltransferases essential for chain polymerization of heparan sulfate (HS) and its analog, heparin (Hep).	Heparin	215-218	exostosin glycosyltransferase 1	Homo sapiens	22-26
13679659-4	2002	HIT type II is an immune-mediated reaction towards neo-antigen on PF4, which is platelet factor 4 (PF4) that is exposed upon binding to heparins.	Heparin	136-144	platelet factor 4	Homo sapiens	66-69
13679659-4	2002	HIT type II is an immune-mediated reaction towards neo-antigen on PF4, which is platelet factor 4 (PF4) that is exposed upon binding to heparins.	Heparin	136-144	platelet factor 4	Homo sapiens	99-102
12173939-9	2002	Accordingly, it was more effective than heparin in inhibiting the mitogenic activity exerted by FGF2 in cultured endothelial cells.	Heparin	40-47	fibroblast growth factor 2	Gallus gallus	96-100
17380220-1	2007	OBJECTIVE: To study the effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells.	Heparin	35-42	matrix metallopeptidase 2	Rattus norvegicus	99-125
11145957-6	2001	An N-terminal human pro-IAPP fragment (residues 1-30) was retained by both heparin-agarose and heparan sulfate-Sepharose, eluting at 0.18 m NaCl at pH 7.5.	Heparin	75-82	islet amyloid polypeptide	Homo sapiens	24-28
11145957-8	2001	At pH 5.5, the affinity of the wild-type peptide for heparin/heparan sulfate was increased, implying a role for histidine residues at positions 6 and 28 of pro-IAPP.	Heparin	53-60	islet amyloid polypeptide	Homo sapiens	160-164
17380220-1	2007	OBJECTIVE: To study the effects of heparin on the production of homocysteine-induced extracellular matrix metalloproteinase-2 (MMP-2) in cultured rat vascular smooth muscle cells.	Heparin	35-42	matrix metallopeptidase 2	Rattus norvegicus	127-132
12195701-1	2002	Heparin has been proposed to enhance thrombolysis by inhibiting thrombin-dependent generation of activated TAFI (thrombin activatable fibrinolysis inhibitor), a carboxypeptidase that inhibits fibrinolysis.	Heparin	0-7	carboxypeptidase B2	Homo sapiens	107-111
12195701-1	2002	Heparin has been proposed to enhance thrombolysis by inhibiting thrombin-dependent generation of activated TAFI (thrombin activatable fibrinolysis inhibitor), a carboxypeptidase that inhibits fibrinolysis.	Heparin	0-7	carboxypeptidase B2	Homo sapiens	113-156
12094292-5	2002	The inhibitory activity of Na-SP was the strongest when compared to that of heparan sulfate, heparin, dextran sulfate, dermatan sulfate, chondroitin sulfate A/C and hyaluronan.	Heparin	93-100	nuclear autoantigenic sperm protein	Bos taurus	27-32
11279105-9	2001	An exonuclease competition assay was designed using heparin as a nonsubstrate inhibitor with a series of partial duplex DNAs to delineate the substrate structure preferences for 3" nucleotide excision by Trex1 and TREX2.	Heparin	52-59	three prime repair exonuclease 1	Homo sapiens	204-209
11389981-7	2001	In addition, PLG with free acid end groups appeared to retard the initial release of rhVEGF by associating with it through ionic interactions at the positively charged heparin binding domain.	Heparin	168-175	plasminogen	Homo sapiens	13-16
17380220-4	2007	Increased production of MMP-2 induced by homocysteine was reduced by the extracellular addition of heparin in a dose-dependent manner.	Heparin	99-106	matrix metallopeptidase 2	Rattus norvegicus	24-29
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	135-142	serpin family D member 1	Homo sapiens	31-35
17380220-5	2007	Production of MMP-2 with various treatment regimens for 72 h was greater than for 24 h and 48 h. CONCLUSIONS: Extracellular addition of heparin decreased homocysteine-induced MMP-2 secretion.	Heparin	136-143	matrix metallopeptidase 2	Rattus norvegicus	14-19
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	201-208	serpin family D member 1	Homo sapiens	31-35
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	201-208	serpin family D member 1	Homo sapiens	31-35
17380220-5	2007	Production of MMP-2 with various treatment regimens for 72 h was greater than for 24 h and 48 h. CONCLUSIONS: Extracellular addition of heparin decreased homocysteine-induced MMP-2 secretion.	Heparin	136-143	matrix metallopeptidase 2	Rattus norvegicus	175-180
17352757-1	2007	We describe synthetic extracellular matrix (sECM) hydrogel films composed of co-crosslinked thiolated derivatives of chondroitin 6-sulfate (CS) and heparin (HP) for controlled-release delivery of basic fibroblast growth factor (bFGF) to full-thickness wounds in genetically diabetic (db/db) mice.	Heparin	148-155	fibroblast growth factor 2	Mus musculus	196-226
11858944-11	2002	R-PIA-induced contraction of esophageal muscle cells was inhibited by IP(3) receptor antagonist heparin, which suggests that the contraction of esophageal smooth muscle cells is dependent on phosphatidylinositol-specific phospholipase (PI-PLC) and IP(3).	Heparin	96-103	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	70-84
17285619-2	2007	HIT is caused by IgG antibodies that bind to epitopes on platelet factor 4 (PF4) released from activated platelets that develop when it forms complexes with heparin.	Heparin	157-164	platelet factor 4	Homo sapiens	76-79
11858944-11	2002	R-PIA-induced contraction of esophageal muscle cells was inhibited by IP(3) receptor antagonist heparin, which suggests that the contraction of esophageal smooth muscle cells is dependent on phosphatidylinositol-specific phospholipase (PI-PLC) and IP(3).	Heparin	96-103	phospholipase C beta 1	Homo sapiens	236-242
11914002-5	2002	The pathophysiology of HIT has been characterized: immune complexes of IgG and heparin in association with a small platelet peptide, platelet factor 4 (PF4), activate platelets by binding to the Fc receptors (FcR) and releasing procoagulant-active, platelet-derived microparticles.	Heparin	79-86	platelet factor 4	Homo sapiens	152-155
17285619-11	2007	High doses of heparin, as used in CPB, or protamine, which competes with PF4 for heparin, disrupts antigen formation and prevents thrombocytopenia induced by HIT antibody.	Heparin	14-21	platelet factor 4	Homo sapiens	73-76
17285619-11	2007	High doses of heparin, as used in CPB, or protamine, which competes with PF4 for heparin, disrupts antigen formation and prevents thrombocytopenia induced by HIT antibody.	Heparin	81-88	platelet factor 4	Homo sapiens	73-76
17335986-0	2007	Anti-metastatic activity of heparin is probably associated with modulation of SDF-1-CXCR4 axis.	Heparin	28-35	C-X-C motif chemokine ligand 12	Homo sapiens	78-83
11922273-4	2002	Heparin dramatically increased the HGF level and it declined to the normal range 18h after heparin injection.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	35-38
11922273-4	2002	Heparin dramatically increased the HGF level and it declined to the normal range 18h after heparin injection.	Heparin	91-98	hepatocyte growth factor	Homo sapiens	35-38
17259344-8	2007	These biological effects of SDF-1 were strongly inhibited by the CXCR4 antagonist AMD3100, by a glycosaminoglycan, heparin, as well as by beta-D-xyloside treatment of the cells, or by c-jun NH(2)-terminal kinase/stress-activated protein kinase inhibitor.	Heparin	115-122	C-X-C motif chemokine ligand 12	Homo sapiens	28-33
11911943-2	2002	In this report, we have firstly expressed in stably transfected MDCK II cells a range of truncation mutants lacking up to 78% of the C-terminus of TSP1; these studies indicate that the N-terminal region containing the heparin binding domain is sufficient for basolateral targeting of TSP1.	Heparin	218-225	thrombospondin 1	Canis lupus familiaris	147-151
17098277-3	2007	Hemodialysis patients are repeatedly exposed to heparin and are at risk for developing PF4-H antibodies.	Heparin	48-55	platelet factor 4	Homo sapiens	87-90
11911943-2	2002	In this report, we have firstly expressed in stably transfected MDCK II cells a range of truncation mutants lacking up to 78% of the C-terminus of TSP1; these studies indicate that the N-terminal region containing the heparin binding domain is sufficient for basolateral targeting of TSP1.	Heparin	218-225	thrombospondin 1	Canis lupus familiaris	284-288
17098277-12	2007	CONCLUSIONS: Hemodialysis with repeated exposure to unfractionated heparin was associated with a moderately elevated prevalence of PF4-H antibodies.	Heparin	67-74	platelet factor 4	Homo sapiens	131-134
11804978-2	2002	In addition, TFPI-1 is released from microvascular endothelial cells after treatment with heparin and thereby contributes to its antithrombotic properties.	Heparin	90-97	tissue factor pathway inhibitor	Homo sapiens	13-19
17020769-0	2006	Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2).	Heparin	24-31	insulin like growth factor binding protein 2	Homo sapiens	68-112
11958801-2	2002	Antibodies to heparin-platelet factor 4 (PF4) complexes have been observed in patient with heparin-induced thrombocytopenia (HIT) syndrome.	Heparin	14-21	platelet factor 4	Homo sapiens	41-44
11958801-7	2002	In 50 normal human serum (NHS) samples, only two were positive for IgG, but 33 were positive for IgM, indicating a potential humoral response to the heparin-PF4 complex prior to heparin administration.	Heparin	149-156	platelet factor 4	Homo sapiens	157-160
17020769-0	2006	Structure, dynamics and heparin binding of the C-terminal domain of insulin-like growth factor-binding protein-2 (IGFBP-2).	Heparin	24-31	insulin like growth factor binding protein 2	Homo sapiens	114-121
11835336-1	2002	Heparin-induced thrombocytopenia (HIT), characterized by the formation of antibodies to a complex of platelet factor 4 (PF4) and heparin, is a well-recognized risk factor for thromboembolic complications.	Heparin	0-7	platelet factor 4	Homo sapiens	120-123
11893078-6	2002	Removal of heparin chains from the various matrices by pretreatment of the ECM with heparinase resulted in reduction of glucose-6-phosphatase and DPP IV in adult hepatocytes.	Heparin	11-18	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	120-141
17082614-4	2006	Although monomeric IP-10 had reduced binding affinity for CXCR3 and heparin, it was able to induce in vitro chemotaxis of activated T cells with the same efficacy as wild-type IP-10.	Heparin	68-75	chemokine (C-X-C motif) ligand 10	Mus musculus	19-24
11748111-1	2001	BACKGROUND: In animal models, heparin delivered as a continuous intravenous infusion or via frequent (BID) subcutaneous dosing inhibits neointimal hyperplasia after balloon injury or stent implantation.	Heparin	30-37	BH3-interacting domain death agonist	Oryctolagus cuniculus	102-105
11748111-9	2001	After balloon injury, both intravenous (0.3 mg/kg per hour) and oral heparin (90 mg/kg BID) effectively inhibited neointimal hyperplasia (0.11+/-0.02 and 0.09+/-0.07 mm(2), respectively, versus 0.16+/-0.06 mm(2) in control; P&lt;0.05).	Heparin	69-76	BH3-interacting domain death agonist	Oryctolagus cuniculus	87-90
11748111-10	2001	After stent implantation, intravenous administration of heparin (0.3 mg/kg per hour) effectively inhibited neointimal growth (0.35+/-0.05 mm(2) versus 0.51+/-0.09 mm(2) in control; P&lt;0.05), but oral heparin at 90 mg/kg BID and 180 mg/kg BID (0.48+/-0.04 and 0.49+/-0.08 mm(2), respectively; P=NS versus control) did not.	Heparin	56-63	BH3-interacting domain death agonist	Oryctolagus cuniculus	222-225
11748111-10	2001	After stent implantation, intravenous administration of heparin (0.3 mg/kg per hour) effectively inhibited neointimal growth (0.35+/-0.05 mm(2) versus 0.51+/-0.09 mm(2) in control; P&lt;0.05), but oral heparin at 90 mg/kg BID and 180 mg/kg BID (0.48+/-0.04 and 0.49+/-0.08 mm(2), respectively; P=NS versus control) did not.	Heparin	56-63	BH3-interacting domain death agonist	Oryctolagus cuniculus	240-243
16967044-3	2006	The effects of Tat on CD127 expression could be blocked with anti-Tat monoclonal antibodies or by preincubating Tat with heparin.	Heparin	121-128	interleukin 7 receptor	Homo sapiens	22-27
11903489-4	2001	For comparison, LPL and HL activities were measured in pre- and post-heparin plasma from fed and 24-h-fasted guinea pigs.	Heparin	69-76	lipoprotein lipase	Cavia porcellus	16-19
17008164-2	2006	It is caused by platelet-activating IgG antibodies that recognize multimolecular complexes of platelet factor 4 (PF4) bound to heparin or certain other polyanions.	Heparin	127-134	platelet factor 4	Homo sapiens	113-116
11748593-6	2001	This, however, was not due to an increase in affinity of IGFBP-3 for heparin at reduced pH although both heparinase III treatment and heparin addition reduced IGFBP-3 enhancement of IGF-I binding.	Heparin	105-112	insulin like growth factor 1	Sus scrofa	182-187
17008164-3	2006	Although an immune response to PF4/heparin associated with heparin treatment is very common, clinical HIT occurs only among the minority of patients whose antibodies are capable of strongly activating platelets.	Heparin	59-66	platelet factor 4	Homo sapiens	31-34
11772296-9	2001	TFPI can be administered exogenously in high doses to suppress TF-mediated effects, alternatively high amounts of TFPI can be released from intravascular stores by other drugs, such as heparin and low molecular weight heparins (LMWH).	Heparin	185-192	tissue factor pathway inhibitor	Homo sapiens	114-118
16771712-5	2006	In contrast, TIMP-3 is demonstrated to inhibit ADAMTS-2 in vitro with apparent Ki values of 160 and 602 nM, in the presence of heparin or without respectively; and TIMP-3 is shown to inhibit procollagen processing by cells.	Heparin	127-134	ADAM metallopeptidase with thrombospondin type 1 motif 2	Homo sapiens	47-55
11772296-9	2001	TFPI can be administered exogenously in high doses to suppress TF-mediated effects, alternatively high amounts of TFPI can be released from intravascular stores by other drugs, such as heparin and low molecular weight heparins (LMWH).	Heparin	218-226	tissue factor pathway inhibitor	Homo sapiens	0-4
11772296-9	2001	TFPI can be administered exogenously in high doses to suppress TF-mediated effects, alternatively high amounts of TFPI can be released from intravascular stores by other drugs, such as heparin and low molecular weight heparins (LMWH).	Heparin	218-226	tissue factor pathway inhibitor	Homo sapiens	114-118
11678646-2	2001	Since such sequences are present in the heparin-binding angiogenic cytokines, including hepatocyte growth factor (HGF), we have postulated that such small peptides may have biological activity.	Heparin	40-47	hepatocyte growth factor	Homo sapiens	88-112
16627026-7	2006	Three sutures specimens were treated with FGF2-soaked heparin acrylic beads to induce accelerated mineralization and premature suture closure.	Heparin	54-61	fibroblast growth factor 2	Mus musculus	42-46
11678646-2	2001	Since such sequences are present in the heparin-binding angiogenic cytokines, including hepatocyte growth factor (HGF), we have postulated that such small peptides may have biological activity.	Heparin	40-47	hepatocyte growth factor	Homo sapiens	114-117
11514538-1	2001	We have previously shown that carboxymethyl dextran benzylamide (CMDB7), a heparin-like molecule, inhibits the growth of tumors xenografted in nude mice, angiogenesis, and metastasis by altering the binding of angiogenic growth factors, including platelet-derived growth factor, transforming growth factor beta, and fibroblast growth factor 2, to their specific receptors.	Heparin	75-82	fibroblast growth factor 2	Mus musculus	316-342
11304894-6	2001	Greater systemic exposure was observed when heparin was administered closer to rFGF-2 infusion, consistent with slower clearance of heparin/rFGF-2 complexes.	Heparin	44-51	fibroblast growth factor 2	Rattus norvegicus	140-146
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	127-134	TNF receptor superfamily member 11b	Homo sapiens	31-34
11473122-4	2001	O-Sulfated and N,O-sulfated K5 derivatives with a low degree and a high degree of sulfation compete with heparin for binding to 125I-FGF2 with different potency.	Heparin	105-112	fibroblast growth factor 2	Cricetulus griseus	133-137
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	127-134	TNF receptor superfamily member 11b	Homo sapiens	118-121
11330545-3	2001	Recently, VCP has been shown to bind to heparin, and this property contributes to separate functions, making the molecule a multifunctional protein.	Heparin	40-47	valosin containing protein	Homo sapiens	10-13
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	127-134	TNF receptor superfamily member 11b	Homo sapiens	118-121
16828054-7	2006	The results demonstrated that sulfation is essential in the OPG-blocking function of GAGs since a totally desulfated heparin loses its capacity to bind and to block OPG binding to RANKL.	Heparin	117-124	TNF receptor superfamily member 11b	Homo sapiens	60-63
16828054-7	2006	The results demonstrated that sulfation is essential in the OPG-blocking function of GAGs since a totally desulfated heparin loses its capacity to bind and to block OPG binding to RANKL.	Heparin	117-124	TNF receptor superfamily member 11b	Homo sapiens	165-168
11182220-2	2001	Heparin induced thrombocytopenia (HIT) is associated with an antibody response in which the immunogen is a self-protein, platelet factor 4 (PF4), modified by an external agent, heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	140-143
11182220-2	2001	Heparin induced thrombocytopenia (HIT) is associated with an antibody response in which the immunogen is a self-protein, platelet factor 4 (PF4), modified by an external agent, heparin.	Heparin	177-184	platelet factor 4	Homo sapiens	140-143
11182220-4	2001	We identify here, a subset of T cells derived from a subject with severe HIT, which were expanded preferentially in 14-day in vitro cultures specifically in the presence of PF4:heparin complexes.	Heparin	177-184	platelet factor 4	Homo sapiens	173-176
11549250-6	2001	Data suggest that antithrombin regulates neutrophil migration via effects of its heparin-binding site on cell surface syndecan-4.	Heparin	81-88	syndecan 4	Homo sapiens	118-128
11527417-6	2001	These data show that a heparin-binding site is present in the C-terminal end of the chicken collagen XII sequence and strongly suggest that proteolytic processing in the NC1 domain can occur in vivo and regulate the interactive properties of collagen XII.	Heparin	23-30	collagen type XII alpha 1 chain	Gallus gallus	92-104
11527417-6	2001	These data show that a heparin-binding site is present in the C-terminal end of the chicken collagen XII sequence and strongly suggest that proteolytic processing in the NC1 domain can occur in vivo and regulate the interactive properties of collagen XII.	Heparin	23-30	collagen type XII alpha 1 chain	Gallus gallus	242-254
16890321-4	2006	Results from these experiments indicate that PF4 ZIP demonstrates a higher heparin-binding affinity and heparin association rate when compared to the heparin-binding domains of antithrombin III (ATIII) and heparin-interacting protein (HIP).	Heparin	104-111	platelet factor 4	Homo sapiens	45-48
11174738-3	2001	The two most commonly used heparin-coated systems are the Carmeda BioActive Surface (Medtronic Inc, Minneapolis, Minn) and the Duraflo II coating (Baxter Healthcare Corp, Bentley Laboratories Division, Irvine, Calif).	Heparin	27-34	CCR4-NOT transcription complex subunit 8	Homo sapiens	210-215
16890321-4	2006	Results from these experiments indicate that PF4 ZIP demonstrates a higher heparin-binding affinity and heparin association rate when compared to the heparin-binding domains of antithrombin III (ATIII) and heparin-interacting protein (HIP).	Heparin	104-111	platelet factor 4	Homo sapiens	45-48
16890321-5	2006	Viscoelastic hydrogels were formed upon the association of PF4 ZIP-functionalized star poly(ethylene glycol) (PEG-PF4 ZIP) with low-molecular-weight heparin-functionalized star PEG (PEG-LMWH).	Heparin	149-156	platelet factor 4	Homo sapiens	114-117
11560562-10	2001	Inhibition of ADP-and collagen-induced aggregation tended to be attenuated by treatment with UFH (e.g. ADP-induced aggregation at 0.25 h after ABC + ASA alone =13 +/- 4%; after coadministration with UFH = 40 +/- 26%).	Heparin	93-96	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	143-146
16860036-1	2006	A substantial proportion of patients who undergo cardiac catheterization develop antibodies directed against the heparin/platelet factor 4 (PF4) complex after the procedure, which have been implicated in the pathogenesis of heparin-induced thrombocytopenia.	Heparin	113-120	platelet factor 4	Homo sapiens	140-143
11583326-1	2001	We compare the relative activities of surface-bound and fluid-phase thrombin and their inhibition by heparin and Intimatan, a novel heparin cofactor II (HCII) agonist.	Heparin	101-108	serpin family D member 1	Homo sapiens	132-151
11583326-1	2001	We compare the relative activities of surface-bound and fluid-phase thrombin and their inhibition by heparin and Intimatan, a novel heparin cofactor II (HCII) agonist.	Heparin	101-108	serpin family D member 1	Homo sapiens	153-157
11229821-2	2001	Free TFPI is the most potent and important type, because it is released from endothelial cells following an injection of heparin, or as a result of pathological stimuli.	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	5-9
16866356-0	2006	New insights into the inhibition of human neutrophil elastase by heparin.	Heparin	65-72	elastase, neutrophil expressed	Homo sapiens	42-61
28452441-3	2001	Given stoichiometric concentrations of heparin and platelet factor 4 (PF4), heparin may induce conformational changes in the PF4 molecule, rendering it antigenic.	Heparin	39-46	platelet factor 4	Homo sapiens	125-128
28452441-3	2001	Given stoichiometric concentrations of heparin and platelet factor 4 (PF4), heparin may induce conformational changes in the PF4 molecule, rendering it antigenic.	Heparin	76-83	platelet factor 4	Homo sapiens	70-73
28452441-3	2001	Given stoichiometric concentrations of heparin and platelet factor 4 (PF4), heparin may induce conformational changes in the PF4 molecule, rendering it antigenic.	Heparin	76-83	platelet factor 4	Homo sapiens	125-128
11395520-9	2001	Finally, heparin, which has affinity for PS-PLA(1), completely blocked the stimulatory effect of the enzyme.	Heparin	9-16	phospholipase A1 member A	Rattus norvegicus	41-50
16866356-3	2006	To gain insight into this complex process of heparin and heparan sulfate regulation of elastases, an experimental study was undertaken to resolve the mechanism and structural requirements of heparin inhibition of human neutrophil elastase (HNE).	Heparin	191-198	elastase, neutrophil expressed	Homo sapiens	219-238
16709175-6	2006	Here, we summarize the progress made in understanding the interaction between heparin and heparan sulphate and NK1, NK2 and HGF/SF and we discuss their role in HGF/SF-Met signalling.	Heparin	78-85	hepatocyte growth factor	Homo sapiens	124-130
11415432-0	2001	Characterization of Sp17: a ubiquitous three domain protein that binds heparin.	Heparin	71-78	sperm autoantigenic protein 17	Mus musculus	20-24
11436975-3	2001	In the presence of basic fibroblast growth factor (bFGF), the growth of NIH3T3 cells was enhanced only in the heparin-immobilized regions.	Heparin	110-117	fibroblast growth factor 2	Mus musculus	19-49
16709187-8	2006	More recently, we and others have been investigating the heparin/heparan sulphate-binding properties of BMP-7, which is a representative of a distinct BMP subgroup from that of BMPs -2 and -4.	Heparin	57-64	bone morphogenetic protein 2	Homo sapiens	104-107
11436975-3	2001	In the presence of basic fibroblast growth factor (bFGF), the growth of NIH3T3 cells was enhanced only in the heparin-immobilized regions.	Heparin	110-117	fibroblast growth factor 2	Mus musculus	51-55
11415432-3	2001	In the present study, we report that Sp17"s central domain (amino acids 61-117), spanning exon 3, is critical for heparin binding.	Heparin	114-121	sperm autoantigenic protein 17	Mus musculus	37-41
11415432-7	2001	Sp17"s central domain, which is necessary for heparin binding, exhibits the greatest sequence divergence of all three domains.	Heparin	46-53	sperm autoantigenic protein 17	Mus musculus	0-4
11436975-4	2001	This result indicated that gradient-micropattern-immobilized heparin activated bFGF for cell growth.	Heparin	61-68	fibroblast growth factor 2	Mus musculus	79-83
16500040-6	2006	The results indicate that the MUC1 SEA domain originated from heparin sulfate proteoglycan of basement membrane (HSPG2; perlecan), an inducer of tumor cell growth.	Heparin	62-69	mucin 1, cell surface associated	Homo sapiens	30-34
11436975-7	2001	Although a high density (a region having short gap length) of immobilized heparin suppressed the cell growth in the absence of bFGF, it enhanced cell growth in the presence of bFGF.	Heparin	74-81	fibroblast growth factor 2	Mus musculus	127-131
11272097-7	2001	Tg endocytosis via megalin is facilitated by the interaction of Tg with cell surface heparan sulfate proteoglycans, which occurs via a carboxyl terminal heparin binding site of Tg functionally related with a major megalin binding site.	Heparin	153-160	thyroglobulin	Homo sapiens	0-2
11272097-7	2001	Tg endocytosis via megalin is facilitated by the interaction of Tg with cell surface heparan sulfate proteoglycans, which occurs via a carboxyl terminal heparin binding site of Tg functionally related with a major megalin binding site.	Heparin	153-160	LDL receptor related protein 2	Homo sapiens	19-26
11272097-7	2001	Tg endocytosis via megalin is facilitated by the interaction of Tg with cell surface heparan sulfate proteoglycans, which occurs via a carboxyl terminal heparin binding site of Tg functionally related with a major megalin binding site.	Heparin	153-160	thyroglobulin	Homo sapiens	64-66
11272097-7	2001	Tg endocytosis via megalin is facilitated by the interaction of Tg with cell surface heparan sulfate proteoglycans, which occurs via a carboxyl terminal heparin binding site of Tg functionally related with a major megalin binding site.	Heparin	153-160	thyroglobulin	Homo sapiens	64-66
11272097-7	2001	Tg endocytosis via megalin is facilitated by the interaction of Tg with cell surface heparan sulfate proteoglycans, which occurs via a carboxyl terminal heparin binding site of Tg functionally related with a major megalin binding site.	Heparin	153-160	LDL receptor related protein 2	Homo sapiens	214-221
11451924-9	2001	Heparin as low as 0.01 mg/mL significantly downregulated expression of TGF-beta(1) and FGF-1-stimulated FGF-2 and FGFR-1.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	104-109
11433225-2	2001	Platelet-activating, heparin-induced antibodies characteristic of HIT are thought to be specific for complexes formed between platelet factor 4 (PF4) and heparin, and such complexes are routinely used for antibody detection.	Heparin	21-28	platelet factor 4	Homo sapiens	145-148
11433225-2	2001	Platelet-activating, heparin-induced antibodies characteristic of HIT are thought to be specific for complexes formed between platelet factor 4 (PF4) and heparin, and such complexes are routinely used for antibody detection.	Heparin	154-161	platelet factor 4	Homo sapiens	145-148
11433225-3	2001	We studied the binding of HIT antibodies to PF4 complexed with heparin fractions of uniform molecular size or linear polyanions other than heparin and found that many compounds other than heparin form complexes with PF4 that are suitable for antibody detection, provided they carry strong negative charges spaced about 0.5 nm apart along the molecular backbone and are of sufficient length to span about 40% of the circumference of the PF4 tetramer.	Heparin	63-70	platelet factor 4	Homo sapiens	44-47
11113279-1	2000	The effect of four sulfated polyvinylalcohol-acrylate copolymers and heparin on plasminogen activation and on plasmin activity is studied.	Heparin	69-76	plasminogen	Homo sapiens	80-87
11316800-0	2001	Structural and energetic characteristics of the heparin-binding site in antithrombotic protein C. Human activated protein C (APC) is a key component of a natural anticoagulant system that regulates blood coagulation.	Heparin	48-55	APC regulator of WNT signaling pathway	Homo sapiens	125-128
16424390-1	2006	Neuropilin-1 (Npn-1) is a receptor shared by class 3 semaphorins and heparin-binding forms of vascular endothelial growth factor (VEGF), protein families that regulate endothelial and neuronal-cell function.	Heparin	69-76	neuropilin 1	Homo sapiens	0-12
11316800-1	2001	In vivo, the catalytic activity of APC is regulated by two serpins, alpha1-antitrypsin and the protein C inhibitor (PCI), the inhibition by the latter being stimulated by heparin.	Heparin	171-178	APC regulator of WNT signaling pathway	Homo sapiens	35-38
11316800-1	2001	In vivo, the catalytic activity of APC is regulated by two serpins, alpha1-antitrypsin and the protein C inhibitor (PCI), the inhibition by the latter being stimulated by heparin.	Heparin	171-178	serpin family A member 5	Homo sapiens	95-114
11316800-2	2001	We have identified a heparin-binding site in the serine protease domain of APC and characterized the energetic basis of the interaction with heparin.	Heparin	21-28	APC regulator of WNT signaling pathway	Homo sapiens	75-78
11316800-2	2001	We have identified a heparin-binding site in the serine protease domain of APC and characterized the energetic basis of the interaction with heparin.	Heparin	141-148	APC regulator of WNT signaling pathway	Homo sapiens	75-78
11316800-3	2001	According to the counter-ion condensation theory, the binding of heparin to APC is 66% ionic in nature and comprises four to six net ionic interactions.	Heparin	65-72	APC regulator of WNT signaling pathway	Homo sapiens	76-79
11316800-4	2001	To localize the heparin-binding site, five recombinant APC variants containing amino acid exchanges in loops 37, 60, and 70 (chymotrypsinogen numbering) were created.	Heparin	16-23	APC regulator of WNT signaling pathway	Homo sapiens	55-58
11316800-6	2001	The functional consequence was loss in heparin-induced stimulation of APC inhibition by PCI, whereas the PCI-induced APC inhibition in the absence of heparin was enhanced.	Heparin	39-46	APC regulator of WNT signaling pathway	Homo sapiens	70-73
11316800-8	2001	The heparin-binding site of APC was also shown to interact with heparan sulfate, albeit with lower affinity.	Heparin	4-11	APC regulator of WNT signaling pathway	Homo sapiens	28-31
11316800-9	2001	In conclusion, we have characterized and spatially localized the functionally important heparin/heparan sulfate-binding site of APC.	Heparin	88-95	APC regulator of WNT signaling pathway	Homo sapiens	128-131
11798537-9	2000	CONCLUSION: TGF-beta1, EGF and bFGF may play an important role in the airway wall and pulmonary arteriole structure remodeling in COPD, the intervention against TGF-beta1 and long term inhalation of heparin mat be helpful for the inhibition of airway wall remodeling in human COPD and worth of further observation.	Heparin	199-206	epidermal growth factor like 1	Rattus norvegicus	23-26
10922378-8	2000	Binding experiments done in the presence of heparin and with altered forms of TFPI suggest that the basic C-terminal region of TFPI is required for TSP-1 binding.	Heparin	44-51	tissue factor pathway inhibitor	Homo sapiens	127-131
16424390-1	2006	Neuropilin-1 (Npn-1) is a receptor shared by class 3 semaphorins and heparin-binding forms of vascular endothelial growth factor (VEGF), protein families that regulate endothelial and neuronal-cell function.	Heparin	69-76	neuropilin 1	Homo sapiens	14-19
16314835-5	2006	These fragments also inhibited Erk1/2 kinase activation induced by soluble heparin-binding EGF and AR.	Heparin	75-82	mitogen-activated protein kinase 3	Mus musculus	31-37
10900194-2	2000	The present results show that glycosaminoglycans such as heparin, heparan sulfate, chondroitin sulfates A, B, and C, and sulfated compounds such as suramin and pentosan efficiently extract TIMP-3 from the postpartum rat uterus.	Heparin	57-64	TIMP metallopeptidase inhibitor 3	Rattus norvegicus	189-195
11018749-12	2000	Collectively, these findings suggest that intercellular d/tPRP targeting is mediated through associations with heparin-containing molecules which help direct d/tPRP to specific interactions with eosinophils within the uterus and with the labyrinthine compartment of the chorioallantoic placenta.	Heparin	111-118	prolactin family 8, subfamily a, member 2	Mus musculus	56-62
11304529-3	2001	Here we demonstrate that the heparin analog pentosan polysulfate (PPS) inhibits the interaction of glutathione S-transferase (GST)-Tat protein with heparin immobilized to a BIAcore sensor chip.	Heparin	29-36	tyrosine aminotransferase	Homo sapiens	131-134
11304529-3	2001	Here we demonstrate that the heparin analog pentosan polysulfate (PPS) inhibits the interaction of glutathione S-transferase (GST)-Tat protein with heparin immobilized to a BIAcore sensor chip.	Heparin	148-155	tyrosine aminotransferase	Homo sapiens	131-134
11255190-7	2001	Matrices preloaded with bFGF also demonstrated good biocompatibility, especially in combination with higher amounts of immobilized heparin.	Heparin	131-138	fibroblast growth factor 2	Rattus norvegicus	24-28
11371192-5	2001	Our results indicate that the heparin binding site, defined as the 40s loop, is only marginally involved in CCR5 binding and activation, but largely overlaps the CCR1 and CCR3 binding and activation domain in RANTES.	Heparin	30-37	C-C chemokine receptor type 5	Cricetulus griseus	108-112
11145957-5	2001	This possibility was tested using affinity chromatography by applying synthetic fragments of pro-IAPP to heparin-agarose and heparan sulfate-Sepharose.	Heparin	105-112	islet amyloid polypeptide	Homo sapiens	97-101
11018749-12	2000	Collectively, these findings suggest that intercellular d/tPRP targeting is mediated through associations with heparin-containing molecules which help direct d/tPRP to specific interactions with eosinophils within the uterus and with the labyrinthine compartment of the chorioallantoic placenta.	Heparin	111-118	prolactin family 8, subfamily a, member 2	Mus musculus	158-164
11034411-1	2000	We herein demonstrate that mast cells express all known members of the group II subfamily of secretory phospholipase A2 (sPLA2) isozymes, and those having heparin affinity markedly enhance the exocytotic response.	Heparin	155-162	phospholipase A2 group IIA	Rattus norvegicus	93-119
11034411-2	2000	Rat mastocytoma RBL-2H3 cells transfected with heparin-binding (sPLA2-IIA, -V, and -IID), but not heparin-nonbinding (sPLA2-IIC), enzymes released more granule-associated markers (beta-hexosaminidase and histamine) than mock- or cytosolic PLA2alpha (cPLA2alpha)-transfected cells after stimulation with IgE and Ag.	Heparin	47-54	phospholipase A2 group IIA	Rattus norvegicus	64-69
16304054-0	2006	Role of platelet surface PF4 antigenic complexes in heparin-induced thrombocytopenia pathogenesis: diagnostic and therapeutic implications.	Heparin	52-59	platelet factor 4	Homo sapiens	25-28
11034411-3	2000	Site-directed mutagenesis of sPLA2-IIA and -V revealed that both the catalytic and heparin-binding domains are essential for this function.	Heparin	83-90	phospholipase A2 group IIA	Rattus norvegicus	29-34
11342428-4	2001	Because N-deacetylase/N-sulfotransferase 2 (NDST-2) is essential for the synthesis of heparin, the amount of NDST-2 messenger RNA (mRNA) was compared among cultured mast cells (CMCs) of +/+, mi/mi, and tg/tg genotypes.	Heparin	86-93	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	8-42
16304054-1	2006	Heparin-induced thrombocytopenia (HIT) antibodies recognize complexes between heparin and platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	109-112
11342428-4	2001	Because N-deacetylase/N-sulfotransferase 2 (NDST-2) is essential for the synthesis of heparin, the amount of NDST-2 messenger RNA (mRNA) was compared among cultured mast cells (CMCs) of +/+, mi/mi, and tg/tg genotypes.	Heparin	86-93	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	44-50
16304054-8	2006	Therapeutic interventions in this model using high-dose heparin or protamine sulfate support the pathogenic role of surface PF4 antigenic complexes in the etiology of HIT.	Heparin	56-63	platelet factor 4	Homo sapiens	124-127
10889187-3	2000	In vitro, these biopolymers were able to protect various heparin-binding growth factors against proteolytic degradation as well as to inhibit the enzymatic activity of neutrophil elastase.	Heparin	57-64	elastase, neutrophil expressed	Homo sapiens	168-187
16304054-9	2006	We believe that this focus on surface PF4 advances our understanding of the pathogenesis of HIT, suggests ways to identify patients at high risk to develop HIT upon heparin exposure, and offers new therapeutic strategies.	Heparin	165-172	platelet factor 4	Homo sapiens	38-41
16449539-7	2006	DISCUSSION: During active HIT, when thrombocytopenia and heparin-PF4 antibodies are present, heparin therapy must be avoided.	Heparin	57-64	platelet factor 4	Homo sapiens	65-68
10842181-6	2000	The affinity of VEGF165 for the NP-1 ECD was greatly enhanced either by increasing the density of immobilized NP-1 (K(d) = 113 nm) or by the addition of heparin (K(d) = 25 nm).	Heparin	153-160	neuropilin 1	Homo sapiens	32-36
11333985-5	2001	Newborn mice deficient in syndecan-1 resist P. aeruginosa lung infection but become susceptible when given purified syndecan-1 ectodomains or heparin, but not when given ectodomain core protein, indicating that the ectodomain"s heparan sulphate chains are the effectors.	Heparin	142-149	syndecan 1	Mus musculus	26-36
10816596-4	2000	In the presence of FGF-2, FGFR-1 kinase and subsequent mitogen-activated protein kinase Erk2 activities were augmented in a dose-dependent manner, whereas high concentrations of heparin resulted in decreased activity.	Heparin	178-185	fibroblast growth factor 2	Gallus gallus	19-24
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	177-184	C-X-C motif chemokine ligand 12	Homo sapiens	83-88
10816596-6	2000	The N- and 2-O-sulfate groups of heparin were essential for binding to FGF-2, whereas stimulation of FGFR-1 and Erk2 kinases by FGF-2 also required the presence of 6-O-sulfate groups.	Heparin	33-40	fibroblast growth factor 2	Gallus gallus	71-76
10816596-8	2000	Selectively 6-O-desulfated heparin, which binds to FGF-2 but fails to bind the receptor, decreased FGF-2-induced proliferation of CHO677 cells, presumably by displacing intact heparin.	Heparin	27-34	fibroblast growth factor 2	Gallus gallus	51-56
11134040-12	2001	In addition, FGFR3DeltaAB responds to FGF1 at lower concentrations of heparin than FGFR3 does.	Heparin	70-77	fibroblast growth factor receptor 3	Mus musculus	13-18
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	177-184	C-C motif chemokine ligand 21	Homo sapiens	93-96
10816596-8	2000	Selectively 6-O-desulfated heparin, which binds to FGF-2 but fails to bind the receptor, decreased FGF-2-induced proliferation of CHO677 cells, presumably by displacing intact heparin.	Heparin	27-34	fibroblast growth factor 2	Gallus gallus	99-104
10816596-8	2000	Selectively 6-O-desulfated heparin, which binds to FGF-2 but fails to bind the receptor, decreased FGF-2-induced proliferation of CHO677 cells, presumably by displacing intact heparin.	Heparin	176-183	fibroblast growth factor 2	Gallus gallus	99-104
17162545-6	2006	Accumulating data on the safety of PCI with low-dose unfractionated heparin is pointed out.	Heparin	68-75	serpin family A member 5	Homo sapiens	35-38
10816596-11	2000	Preventing complex formation by modified heparin preparations may allow regulation of FGF-2 functions, such as induction of angiogenesis.	Heparin	41-48	fibroblast growth factor 2	Gallus gallus	86-91
11290444-6	2001	The TN-like protein from macaque, horse and cat serum bound heparin and showed the same dependence on Ca2+ for interaction with the monoclonal antibodies as human TN.	Heparin	60-67	C-type lectin domain family 3 member B	Homo sapiens	4-6
16614797-3	2006	The fibroblast growth factor (FGF)-2 molecules retained in the chitosan hydrogel and in an injectable chitosan/IO(4)-heparin hydrogel remain biologically active, and were gradually released from the hydrogels as they biodegraded in vivo.	Heparin	117-124	fibroblast growth factor 2	Mus musculus	4-36
11262187-8	2001	We have previously shown that overexpression of syndecan-1 heparan sulfate proteoglycan renders S115 cells insensitive to testosterone and now demonstrate that this effect can be overcome by sodium chlorate treatment in combination with exogenous heparin.	Heparin	247-254	syndecan 1	Mus musculus	48-58
11599124-9	2001	Furthermore, heparin and HS inhibited ET-1-induced activation of extracellular signal-regulated kinase (ERK) and phosphorylation of Elk-1, which is one of the TCFs.	Heparin	13-20	ETS transcription factor ELK1	Rattus norvegicus	132-137
11599124-10	2001	These results indicate that heparin and HS inhibited ET-1-induced ERK activation, resulting in suppression of Elk-1 phosphorylation, and lead to inhibition of c-fos gene expression through SRF-independent manner.	Heparin	28-35	ETS transcription factor ELK1	Rattus norvegicus	110-115
11281725-3	2001	In order to sort out functional Ets-1-binding sites among those present in gene promoters, we constructed an expression vector and designed a purification protocol for the production of the 440-amino-acid form of mouse Ets-1, based on heparin-Sepharose affinity and anion-exchange chromatographies.	Heparin	235-242	E26 avian leukemia oncogene 1, 5' domain	Mus musculus	219-224
10845910-2	2000	In a rat model, intravenous administration of APC markedly reduced I/R-induced renal dysfunction and histological changes, whereas intravenous administration of dansyl glutamylglycylarginyl chloromethyl ketone-treated factor Xa (DEGR-FXa; active-site-blocked factor Xa), heparin or diisopropyl fluorophosphate-treated APC (DIP-APC; inactive derivative of ARC) had no effect.	Heparin	271-278	APC regulator of WNT signaling pathway	Rattus norvegicus	46-49
10898311-1	2000	BACKGROUND/AIMS: YKL-40, a mammalian member of the chitinase family, is a lectin that binds heparin and chitin.	Heparin	92-99	chitinase 3 like 1	Homo sapiens	17-23
10864991-0	2000	Heparin-induced coagulopathy associated with staphylococcal protein A immunoadsorption treatment columns: an in vitro and in vivo analysis.	Heparin	0-7	surfactant protein A1	Homo sapiens	45-69
10864991-1	2000	BACKGROUND: The staphylococcal protein A (SPA) column used to treat refractory autoimmune and alloimmune thrombocytopenia and rheumatoid arthritis patients is primed with heparin to prevent possible fibrin clot formation when the patient"s plasma is passed through the column.	Heparin	171-178	surfactant protein A1	Homo sapiens	16-40
16411606-2	2006	Gelatin- or heparin-immobilized agarose beads were prepared and HGF interaction with them was evaluated by Scatchard binding assay.	Heparin	12-19	hepatocyte growth factor	Homo sapiens	64-67
10864991-1	2000	BACKGROUND: The staphylococcal protein A (SPA) column used to treat refractory autoimmune and alloimmune thrombocytopenia and rheumatoid arthritis patients is primed with heparin to prevent possible fibrin clot formation when the patient"s plasma is passed through the column.	Heparin	171-178	surfactant protein A1	Homo sapiens	42-45
10864991-3	2000	This observation led to in vivo and in vitro analysis of the kinetics of heparin elution from the SPA column.	Heparin	73-80	surfactant protein A1	Homo sapiens	98-101
10864991-5	2000	In addition, two in vitro analyses were performed with FFP for heparin elution from the SPA column.	Heparin	63-70	surfactant protein A1	Homo sapiens	88-91
11121409-5	2001	Heparinase/heparinitase treatment of the basolateral cell surface or addition of heparin to the basolateral medium decreased the movement of LPL.	Heparin	11-18	lipoprotein lipase	Bos taurus	141-144
16411606-3	2006	The dissociation constant of HGF with the acidic gelatin was about 2-3 orders of magnitude higher than that of heparin.	Heparin	111-118	hepatocyte growth factor	Homo sapiens	29-32
10864991-6	2000	RESULTS: The in vivo studies showed the presence of 0.3 to 1.5 U per mL of heparin in patients" plasma at the end of the SPA column treatments that corresponded with the prolonged aPTTs.	Heparin	75-82	surfactant protein A1	Homo sapiens	121-124
16855345-2	2006	HIT results from a platelet-activating immune response triggered by the interaction of heparin with a specific platelet protein, platelet factor 4 (PF4).	Heparin	87-94	platelet factor 4	Homo sapiens	148-151
10864991-9	2000	CONCLUSION: Patients undergoing SPA column treatments, especially those with thrombocytopenia, may be at increased risk of bleeding as a result of the presence of a significant amount of heparin in their circulation during the entire period of SPA column treatment.	Heparin	187-194	surfactant protein A1	Homo sapiens	32-35
10896252-3	2000	and administration of unfractionated heparin (UFH) in vivo causes a prompt mobilization of TFPI into the circulation.	Heparin	37-44	tissue factor pathway inhibitor	Homo sapiens	91-95
10896252-3	2000	and administration of unfractionated heparin (UFH) in vivo causes a prompt mobilization of TFPI into the circulation.	Heparin	46-49	tissue factor pathway inhibitor	Homo sapiens	91-95
10896252-4	2000	The present study was conducted to investigate how UFH affected the synthesis, secretion and anticoagulant potency of TFPI in endothelial cells in vitro.	Heparin	51-54	tissue factor pathway inhibitor	Homo sapiens	118-122
10896252-6	2000	Stimulation of ECV304 cells with UFH caused a prompt dose-dependent (0-5 IU UFH/ml) release of TFPI to the medium accompanied by no change of TFPI at the surface membrane assessed by immunocytochemical methods.	Heparin	33-36	tissue factor pathway inhibitor	Homo sapiens	95-99
10896252-8	2000	Stimulation of ECV304 cells for 24 hrs with various concentrations of UFH caused a dose-dependent increase of TFPI in the medium (6.2-29.6 ng/10(6) cells within the concentration range 0-10 IU/ml).	Heparin	70-73	tissue factor pathway inhibitor	Homo sapiens	110-114
11113133-7	2001	Addition of heparin, which competes for the binding of TSP2 to LRP coreceptor proteoglycans, inhibited adhesion of control but not TSP2-null cells, and a blocking antibody to LRP as well as the LRP inhibitor, receptor-associated protein, also inhibited adhesion and increased MMP2 levels only in control fibroblasts.	Heparin	12-19	thrombospondin 2	Mus musculus	55-59
11311219-6	2001	BNP and NT-BNP were stable for &lt; 24 hours when stored in EDTA or heparin at room temperature.	Heparin	68-75	natriuretic peptide B	Homo sapiens	0-3
11311219-6	2001	BNP and NT-BNP were stable for &lt; 24 hours when stored in EDTA or heparin at room temperature.	Heparin	68-75	natriuretic peptide B	Homo sapiens	11-14
10896252-10	2000	Long-term incubation of ECV304 cells with 5.0 IU/ml UFH caused a 5-10 fold increase in the TFPI concentration accumulated in the medium over 48 hrs.	Heparin	52-55	tissue factor pathway inhibitor	Homo sapiens	91-95
16855347-1	2006	The peculiar pathogenesis of heparin-induced thrombocytopenia (HIT), involving a "self" antigen-platelet factor 4 (PF4) bound to heparin-and resulting antibody-mediated platelet activation, is a model for thrombosis triggered by drug-induced autoimmunity.	Heparin	29-36	platelet factor 4	Homo sapiens	115-118
10896252-12	2000	The procoagulant activity of the cells was downregulated by 36% and the contribution of TFPI to the anticoagulant potency of ECV304 cells was moderately increased after 24 hrs heparin stimulation.	Heparin	176-183	tissue factor pathway inhibitor	Homo sapiens	88-92
16855347-1	2006	The peculiar pathogenesis of heparin-induced thrombocytopenia (HIT), involving a "self" antigen-platelet factor 4 (PF4) bound to heparin-and resulting antibody-mediated platelet activation, is a model for thrombosis triggered by drug-induced autoimmunity.	Heparin	129-136	platelet factor 4	Homo sapiens	115-118
16499440-11	2006	In the presence of HGF, the level of albumin secretion in AL/GC/heparin sponges was markedly elevated compared to that in AL/GC sponges.	Heparin	64-71	hepatocyte growth factor	Homo sapiens	19-22
10848821-1	2000	Antibodies to heparin platelet factor 4 (H-PF4) complexes were purified from the plasma of three patients with heparin-induced thrombocytopenia (HIT) using affinity chromatography.	Heparin	14-21	platelet factor 4	Homo sapiens	43-46
10848821-8	2000	Using [14C]-serotonin release assays, the antibodies developed in the three patients and exhibiting the strongest ability to activate platelets with heparin were those having the highest affinity to H-PF4.	Heparin	149-156	platelet factor 4	Homo sapiens	201-204
10736564-1	2000	Among the members of the fibroblast growth factor receptor family the FGFR4 has demonstrated strong dependence on heparin-like material for its activation by fibroblast growth factors.	Heparin	114-121	fibroblast growth factor receptor 4	Homo sapiens	70-75
10736564-4	2000	Pure FGFR4ed was tested for FGF- and heparin-binding by covalent crosslinking experiments and by biosensor analysis.	Heparin	37-44	fibroblast growth factor receptor 4	Homo sapiens	5-10
10736564-5	2000	In solution, FGFR4ed formed complexes with acidic FGF (FGF-1) and basic FGF (FGF-2), both in the presence and absence of heparin.	Heparin	121-128	fibroblast growth factor receptor 4	Homo sapiens	13-18
11170730-0	2001	Heparin coinfusion during convection-enhanced delivery (CED) increases the distribution of the glial-derived neurotrophic factor (GDNF) ligand family in rat striatum and enhances the pharmacological activity of neurturin.	Heparin	0-7	glial cell derived neurotrophic factor	Rattus norvegicus	95-128
11170730-0	2001	Heparin coinfusion during convection-enhanced delivery (CED) increases the distribution of the glial-derived neurotrophic factor (GDNF) ligand family in rat striatum and enhances the pharmacological activity of neurturin.	Heparin	0-7	glial cell derived neurotrophic factor	Rattus norvegicus	130-134
11170730-4	2001	Heparin coinfusion significantly enhanced the V(d) of GDNF and GDNF-homologous trophic factors, probably by binding and blocking heparin-binding sites in the extracellular matrix.	Heparin	0-7	glial cell derived neurotrophic factor	Rattus norvegicus	54-58
11170730-4	2001	Heparin coinfusion significantly enhanced the V(d) of GDNF and GDNF-homologous trophic factors, probably by binding and blocking heparin-binding sites in the extracellular matrix.	Heparin	0-7	glial cell derived neurotrophic factor	Rattus norvegicus	63-67
11170730-4	2001	Heparin coinfusion significantly enhanced the V(d) of GDNF and GDNF-homologous trophic factors, probably by binding and blocking heparin-binding sites in the extracellular matrix.	Heparin	129-136	glial cell derived neurotrophic factor	Rattus norvegicus	54-58
11170730-4	2001	Heparin coinfusion significantly enhanced the V(d) of GDNF and GDNF-homologous trophic factors, probably by binding and blocking heparin-binding sites in the extracellular matrix.	Heparin	129-136	glial cell derived neurotrophic factor	Rattus norvegicus	63-67
11035040-2	2001	We have previously generated a mouse strain with a defect in its heparin biosynthesis by targeting the gene for N-deacetylase/N-sulfotransferase-2 (NDST-2).	Heparin	65-72	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	112-146
11035040-2	2001	We have previously generated a mouse strain with a defect in its heparin biosynthesis by targeting the gene for N-deacetylase/N-sulfotransferase-2 (NDST-2).	Heparin	65-72	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	148-154
11035040-10	2001	Further experiments showed that the degradation of fibronectin observed in cell cultures from NDST-2(+/+) mice was catalyzed by mast cell chymase in a strongly heparin-dependent manner.	Heparin	160-167	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	94-100
11035040-10	2001	Further experiments showed that the degradation of fibronectin observed in cell cultures from NDST-2(+/+) mice was catalyzed by mast cell chymase in a strongly heparin-dependent manner.	Heparin	160-167	chymase 1, mast cell	Mus musculus	138-145
16109780-1	2005	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating IgG antibodies that recognize platelet factor 4 (PF4) bound to heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	121-124
11806242-5	2001	CM from 293-VEGF183 cells treated with heparin or plasmin induced about a twofold increase in cell numbers and stimulated MAPK phosphorylation in HUVECs as compared with CM from untreated 293-VEGF183 cells or from heparin- or plasmin-treated 293 cells containing the vector alone.	Heparin	39-46	plasminogen	Homo sapiens	226-233
11806242-5	2001	CM from 293-VEGF183 cells treated with heparin or plasmin induced about a twofold increase in cell numbers and stimulated MAPK phosphorylation in HUVECs as compared with CM from untreated 293-VEGF183 cells or from heparin- or plasmin-treated 293 cells containing the vector alone.	Heparin	214-221	plasminogen	Homo sapiens	50-57
10779780-4	2000	Three of these sites are involved in binding C3b and regulating complement activation; others bind to sialic acid and/or heparin and are responsible for host recognition.	Heparin	121-128	endogenous retrovirus group K member 3	Homo sapiens	45-48
10805884-10	2000	Heparin at 5 U/mL enhanced EC proliferation at the VEGF dose of 100 ng/mL as compared wtih no heparin (P &lt;.001), but not at the VEGF dose of 1000 ng/mL, which likely represents a maximal response.	Heparin	0-7	PDGF- and VEGF-related factor 1	Drosophila melanogaster	51-55
16109780-1	2005	Heparin-induced thrombocytopenia (HIT) is caused by platelet-activating IgG antibodies that recognize platelet factor 4 (PF4) bound to heparin.	Heparin	135-142	platelet factor 4	Homo sapiens	121-124
10727403-0	2000	Biosynthesis of heparin/heparan sulphate: mechanism of epimerization of glucuronyl C-5.	Heparin	16-23	complement C5	Bos taurus	83-86
11307751-2	2001	Heparin thins sputum by decreasing the mucin molecule amino group negative charge, altering its intermolecular hydrogen bonding, and ionically shielding its polyionic moieties.	Heparin	0-7	LOC100508689	Homo sapiens	39-44
10727403-1	2000	In the biosynthesis of heparin and heparan sulphate, D-glucuronic acid residues are converted into L-iduronic acid (IdoA) units by C-5 epimerization, at the polymer level.	Heparin	23-30	complement C5	Bos taurus	131-134
16109780-2	2005	Immunogenicity of heparins differs in that unfractionated heparin (UFH) induces more anti-PF4/heparin antibodies than low-molecular-weight heparin (LMWH) and UFH also causes more HIT.	Heparin	18-26	platelet factor 4	Homo sapiens	90-93
16109780-2	2005	Immunogenicity of heparins differs in that unfractionated heparin (UFH) induces more anti-PF4/heparin antibodies than low-molecular-weight heparin (LMWH) and UFH also causes more HIT.	Heparin	18-25	platelet factor 4	Homo sapiens	90-93
16109780-2	2005	Immunogenicity of heparins differs in that unfractionated heparin (UFH) induces more anti-PF4/heparin antibodies than low-molecular-weight heparin (LMWH) and UFH also causes more HIT.	Heparin	67-70	platelet factor 4	Homo sapiens	90-93
16109780-2	2005	Immunogenicity of heparins differs in that unfractionated heparin (UFH) induces more anti-PF4/heparin antibodies than low-molecular-weight heparin (LMWH) and UFH also causes more HIT.	Heparin	58-65	platelet factor 4	Homo sapiens	90-93
16404704-4	2005	Decreased levels of PF4 and anaphylatoxin C5a (p&lt;0.05) as well as terminal complement complex demonstrated improved hemocompatibility after anticoagulation with heparin in contrast to hirudin.	Heparin	164-171	platelet factor 4	Homo sapiens	20-23
10722718-5	2000	Pro-alpha3(V) is shown to be closely related to the alpha1(V) precursor, pro-alpha1(V), but with marked differences in N-propeptide sequences, and collagenous domain features that provide insights into the low melting temperature of alpha1(V)alpha2(V)alpha3(V) heterotrimers, lack of heparin binding by alpha3(V) chains and the possibility that alpha1(V)alpha2(V)alpha3(V) heterotrimers are incorporated into heterotypic fibrils.	Heparin	284-291	collagen type V alpha 3 chain	Homo sapiens	0-13
10722718-5	2000	Pro-alpha3(V) is shown to be closely related to the alpha1(V) precursor, pro-alpha1(V), but with marked differences in N-propeptide sequences, and collagenous domain features that provide insights into the low melting temperature of alpha1(V)alpha2(V)alpha3(V) heterotrimers, lack of heparin binding by alpha3(V) chains and the possibility that alpha1(V)alpha2(V)alpha3(V) heterotrimers are incorporated into heterotypic fibrils.	Heparin	284-291	collagen type V alpha 3 chain	Homo sapiens	4-13
10706134-4	2000	We tested epidermal growth factor (EGF), transforming growth factor alpha, betacellulin, heparin-binding EGF, and amphiregulin and measured expression of gelatinases MMP-9 and MMP-2 in an established squamous carcinoma cell line (Detroit-562) and in two cell lines newly derived from patients with head and neck cancers (SIHN-005A and SIHN-006).	Heparin	89-96	matrix metallopeptidase 2	Homo sapiens	176-181
10956644-6	2000	In the presence of heparin, CTAP-III was unable to insert sphingomyelin into the peripheral blood lymphocytes.	Heparin	19-26	pro-platelet basic protein	Homo sapiens	28-36
11156724-0	2000	Low-molecular-weight heparin therapy in percutaneous coronary intervention: the NICE 1 and NICE 4 trials.	Heparin	21-28	cysteine rich C-terminal 1	Homo sapiens	80-86
11150580-2	2000	Heparin is known to exert its antithrombotic effects by accelerating the effect of antithrombin (AT) and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation from vascular endothelium.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	119-150
11150580-2	2000	Heparin is known to exert its antithrombotic effects by accelerating the effect of antithrombin (AT) and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation from vascular endothelium.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	152-156
10688118-9	2000	In heparinized plasma, the radioactivity shifted from a 30- to 50-kDa complex to a 150-kDa complex and to a free ligand, because the binding of heparin with IGFBPs decreased its affinity for IGF-I.	Heparin	3-10	insulin-like growth factor 1	Mus musculus	191-196
11150580-10	2000	The present study shows that the FVIIa assay is sensitive to TFPI and AT, especially during heparin treatment, and thereby indicates that the heparin-induced decrease in FVIIa is affected by interactions between TFPI and AT with the FVIIa assay.	Heparin	92-99	tissue factor pathway inhibitor	Homo sapiens	61-65
16310517-1	2005	Heparin-induced thrombocytopenia (HIT) is usually caused by platelet-activating antibodies of immunoglobulin G class that recognize platelet factor-4 (PF4) bound to heparin or certain other polyanions.	Heparin	0-7	platelet factor 4	Homo sapiens	151-154
11150580-10	2000	The present study shows that the FVIIa assay is sensitive to TFPI and AT, especially during heparin treatment, and thereby indicates that the heparin-induced decrease in FVIIa is affected by interactions between TFPI and AT with the FVIIa assay.	Heparin	142-149	tissue factor pathway inhibitor	Homo sapiens	61-65
11150580-10	2000	The present study shows that the FVIIa assay is sensitive to TFPI and AT, especially during heparin treatment, and thereby indicates that the heparin-induced decrease in FVIIa is affected by interactions between TFPI and AT with the FVIIa assay.	Heparin	142-149	tissue factor pathway inhibitor	Homo sapiens	212-216
10938877-2	2000	Heparin-induced thrombocytopenia is caused by the formation of antibodies that bind to specific complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	128-131
10634807-1	2000	Apolipoprotein E (apoE) and lipoprotein lipase (LPL), key proteins in the regulation of lipoprotein metabolism, bind with high affinity to heparin and cell-surface heparan sulfate proteoglycan (HSPG).	Heparin	139-146	apolipoprotein E	Cricetulus griseus	0-16
16310517-1	2005	Heparin-induced thrombocytopenia (HIT) is usually caused by platelet-activating antibodies of immunoglobulin G class that recognize platelet factor-4 (PF4) bound to heparin or certain other polyanions.	Heparin	165-172	platelet factor 4	Homo sapiens	151-154
10634807-1	2000	Apolipoprotein E (apoE) and lipoprotein lipase (LPL), key proteins in the regulation of lipoprotein metabolism, bind with high affinity to heparin and cell-surface heparan sulfate proteoglycan (HSPG).	Heparin	139-146	apolipoprotein E	Cricetulus griseus	18-22
11063092-1	2000	Biological active compounds such as insulin, heparin, progesterone and labeled-LH were entrapped in glutaraldehyde cross-linked bovine serum albumin (BSA) and human serum albumin (HAS) microspheres.	Heparin	45-52	albumin	Mus musculus	135-148
16245931-0	2005	Eosinophil-granule major basic protein, a C-type lectin, binds heparin.	Heparin	63-70	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	0-38
11049983-8	2000	Heparin (0.2 U/mL) enhances the rate (t(1/2) = 25 seconds vs 50 seconds) and the extent (99% vs 93% at 30 minutes) of factor XIa inhibition by ZPI.	Heparin	0-7	serpin family A member 10	Homo sapiens	143-146
10570220-9	2000	We have previously shown that gp120 of X4 strain HIV-1LAI presents specific carbohydrate-binding properties for mannosylated derivatives, including mannan, and for GAGs including heparin.	Heparin	179-186	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	30-35
16245931-4	2005	We also provide direct evidence of binding of EMBP to heparin and heparin disaccharide by surface plasmon resonance.	Heparin	54-61	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	46-50
16245931-5	2005	We propose that the sugars recognized by EMBP are likely to be proteoglycans such as heparin, leading to new interpretations for EMBP function.	Heparin	85-92	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	41-45
16245931-5	2005	We propose that the sugars recognized by EMBP are likely to be proteoglycans such as heparin, leading to new interpretations for EMBP function.	Heparin	85-92	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	129-133
10646636-9	2000	Heparin injection 1 hr later released &lt;10% of the original bovine LPL, further indicating its rapid systemic clearance, inactivation, or degradation as well as its ineffectiveness as a viable therapeutic alternative for complete LPL deficiency.	Heparin	0-7	lipoprotein lipase	Bos taurus	69-72
11131269-3	2000	Because heparin, which is routinely used during hemodialysis, increases circulating hHGF concentration in humans, circulating hHGF may be involved in hemodialysis hypotension via increased NO production.	Heparin	8-15	hepatocyte growth factor	Homo sapiens	84-88
16170576-1	2005	BACKGROUND: Modification of the heparin binding site by alteration of the amino acid sequence of bone morphogenetic protein-2 (BMP-2) results in a change in the local retention time.	Heparin	32-39	bone morphogenetic protein 2	Rattus norvegicus	97-125
11131269-3	2000	Because heparin, which is routinely used during hemodialysis, increases circulating hHGF concentration in humans, circulating hHGF may be involved in hemodialysis hypotension via increased NO production.	Heparin	8-15	hepatocyte growth factor	Homo sapiens	126-130
11034601-6	2000	This interaction with HGF is highly selective since the HSPGs did not bind the chemokine stromal cell-derived factor (SDF)-1 alpha, even though the affinities of HGF and SDF-1alpha for heparin are similar.	Heparin	185-192	hepatocyte growth factor	Homo sapiens	22-25
11034601-6	2000	This interaction with HGF is highly selective since the HSPGs did not bind the chemokine stromal cell-derived factor (SDF)-1 alpha, even though the affinities of HGF and SDF-1alpha for heparin are similar.	Heparin	185-192	hepatocyte growth factor	Homo sapiens	162-165
10993828-5	2000	The enhancing activity of MK was completely suppressed by heparin at 600 ng/ml but not by the other compounds.	Heparin	58-65	midkine	Bos taurus	26-28
10574918-3	1999	Thrombin inhibition by rHCII-CHis(6) was increased &gt;2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin.	Heparin	94-101	serpin family D member 1	Homo sapiens	24-28
10574918-3	1999	Thrombin inhibition by rHCII-CHis(6) was increased &gt;2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin.	Heparin	177-184	serpin family D member 1	Homo sapiens	24-28
10630505-0	1999	Expression of syndecan-1 in inflammatory bowel disease and a possible mechanism of heparin therapy.	Heparin	83-90	syndecan 1	Homo sapiens	14-24
10630505-2	1999	The purpose of this study was to investigate the hypothesis that heparin functions as a coreceptor molecule for basic fibroblast growth factor, a role usually performed by heparan sulfate chains on syndecan-1.	Heparin	65-72	syndecan 1	Homo sapiens	198-208
10630505-8	1999	The present data show that heparin may substitute the loss of functional activity of syndecan-1 in the binding of basic fibroblast growth factor.	Heparin	27-34	syndecan 1	Homo sapiens	85-95
10613650-17	1999	Thus by enhancing lipase activity, full length TFPI may facilitate hydrolysis of triglyceride and concomitantly lower factor VII coagulant activity as demonstrated earlier, particularly after heparin injection when both TFPI and LPL are released in circulation.	Heparin	192-199	tissue factor pathway inhibitor	Bos taurus	47-51
10613653-8	1999	Further, increased synthesis of TFPI initially led to the saturation of heparin-releasable binding sites.	Heparin	72-79	tissue factor pathway inhibitor	Homo sapiens	32-36
10613653-9	1999	TFPI-Ag was detected by Western blotting, 35S-metabolic labeling and activity assays on the conditioned media, heparin-released material from cells, and in cell lysates.	Heparin	111-118	tissue factor pathway inhibitor	Homo sapiens	0-4
10982357-13	2000	The O-sulfate groups of heparin were found to be more important for interaction with gB-1 than gB-2.	Heparin	24-31	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	95-99
16170576-1	2005	BACKGROUND: Modification of the heparin binding site by alteration of the amino acid sequence of bone morphogenetic protein-2 (BMP-2) results in a change in the local retention time.	Heparin	32-39	bone morphogenetic protein 2	Rattus norvegicus	127-132
16170576-8	2005	CONCLUSION: Increased heparin binding capacity enhances osteogenic activity of BMP-2 in vivo.	Heparin	22-29	bone morphogenetic protein 2	Rattus norvegicus	79-84
16286530-4	2005	RESEARCH METHODS AND PROCEDURES: LPL and HL activities were determined in post-heparin plasma in a sample of 197 men and 209 women, 60 to 87 years of age.	Heparin	79-86	lipase C, hepatic type	Homo sapiens	41-43
10971306-0	2000	Heparin-mediated selective release of hepatocyte growth factor in humans.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	38-62
10555961-0	1999	Identification and dynamics of a heparin-binding site in hepatocyte growth factor.	Heparin	33-40	hepatocyte growth factor	Homo sapiens	57-81
10555961-1	1999	Hepatocyte growth factor (HGF) is a heparin-binding, multipotent growth factor that transduces a wide range of biological signals, including mitogenesis, motogenesis, and morphogenesis.	Heparin	36-43	hepatocyte growth factor	Homo sapiens	0-24
10555961-1	1999	Hepatocyte growth factor (HGF) is a heparin-binding, multipotent growth factor that transduces a wide range of biological signals, including mitogenesis, motogenesis, and morphogenesis.	Heparin	36-43	hepatocyte growth factor	Homo sapiens	26-29
10555961-2	1999	Heparin or closely related heparan sulfate has profound effects on HGF signaling.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	67-70
16086578-5	2005	We report the structure of suramin, in complex with the heparin-binding site of vaccinia virus complement control protein (VCP), which interacts with heparin in a geometrically similar manner to many FGFs.	Heparin	56-63	valosin containing protein	Homo sapiens	123-126
10555961-3	1999	A heparin-binding site in the N-terminal (N) domain of HGF was proposed on the basis of the clustering of surface positive charges [Zhou, H., Mazzulla, M. J., Kaufman, J. D., Stahl, S. J., Wingfield, P. T., Rubin, J. S., Bottaro, D. P., and Byrd, R. A.	Heparin	2-9	hepatocyte growth factor	Homo sapiens	55-58
10555961-8	1999	A heparin disaccharide analogue, sucrose octasulfate, binds with similar affinity to the N domain and to a naturally occurring HGF isoform, NK1, at nearly the same region as in heparin binding.	Heparin	2-9	hepatocyte growth factor	Homo sapiens	127-130
10971306-12	2000	CONCLUSIONS: Circulating HGF levels were selectively increased in response to pharmacological doses of two, widely used heparin preparations.	Heparin	120-127	hepatocyte growth factor	Homo sapiens	25-28
10748121-2	2000	np-1 also binds to the 165-amino acid heparin-binding form of VEGF (VEGF(165)) but not to the shorter VEGF(121) form, which lacks a heparin binding ability.	Heparin	38-45	neuropilin 1	Homo sapiens	0-4
16086578-5	2005	We report the structure of suramin, in complex with the heparin-binding site of vaccinia virus complement control protein (VCP), which interacts with heparin in a geometrically similar manner to many FGFs.	Heparin	150-157	valosin containing protein	Homo sapiens	123-126
10615547-10	1999	However, the test for antibodies against the PF4-heparin complex with the Elisa technique, was in favour of a heparin induced thrombocytopenia (TIH).	Heparin	49-56	platelet factor 4	Homo sapiens	45-48
10828022-2	2000	Fibroblast growth factor-2 (FGF-2)-induced angiogenesis in the chicken chorioallantoic membrane was inhibited by endostatin, but not by an endostatin mutant R158/270A, lacking heparin-binding ability.	Heparin	176-183	fibroblast growth factor 2	Gallus gallus	0-26
16088988-3	2005	The purpose of the present study is to test the hypothesis that the kinetics of bFGF release from fibrin gels could be controlled with heparin and concentrations of fibrinogen and thrombin.	Heparin	135-142	fibroblast growth factor 2	Mus musculus	80-84
10828022-2	2000	Fibroblast growth factor-2 (FGF-2)-induced angiogenesis in the chicken chorioallantoic membrane was inhibited by endostatin, but not by an endostatin mutant R158/270A, lacking heparin-binding ability.	Heparin	176-183	fibroblast growth factor 2	Gallus gallus	28-33
10545520-5	1999	Immobilized heparin, a mimic for extracellular matrix-associated proteoglycans, binds physiological concentrations of TFPI-1 in a conformation that supports TF-VIIa-dependent cell adhesion.	Heparin	12-19	tissue factor pathway inhibitor	Homo sapiens	118-124
16088988-7	2005	The addition of heparin to fibrin gels decreased the bFGF release rate.	Heparin	16-23	fibroblast growth factor 2	Mus musculus	53-57
10531393-4	1999	Exposure to D-Ala(2)-D-Leu(5) enkephalin (100 nM) for 90 s induced increases in [Ca2+](i) that were blocked by microinjection of the IP(3) receptor antagonist heparin (pipette concentration = 100 mg/ml) but not by sham injection.	Heparin	159-166	inositol 1,4,5-triphosphate receptor 3	Mus musculus	133-147
16229644-4	2005	In this study, heparin acrylic beads released fibroblast growth factor 2 (FGF2) to mimic constitutive signaling by mutated receptors, delivering FGF2 in addition to already existing normal tissue amounts.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	46-72
10531345-2	1999	We have recently reported that members of the heparin-binding group II subfamily of secretory PLA(2)s (sPLA(2)s) (types IIA and V), when transfected into 293 cells, released [(3)H]arachidonic acid (AA) preferentially in response to interleukin-1 (IL-1) and acted as "signaling" PLA(2)s that were functionally coupled with prostaglandin biosynthesis.	Heparin	46-53	phospholipase A2 group IID	Homo sapiens	103-111
10532694-5	1999	Heparin infusion increased both plasma lipoprotein and hepatic lipase activity and raised plasma FFAs two-fold (P &lt; 0.001).	Heparin	0-7	lipase C, hepatic type	Homo sapiens	55-69
10488098-0	1999	Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.	Heparin	14-21	serpin family D member 1	Homo sapiens	91-110
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	serpin family D member 1	Homo sapiens	38-57
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	serpin family D member 1	Homo sapiens	59-63
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	serpin family D member 1	Homo sapiens	124-128
10488098-6	1999	Whereas activation of HCII by heparin was chain-length dependent, stimulation by dermatan sulfate was not, suggesting that dermatan sulfate does not utilize a template mechanism to accelerate the inhibitory process.	Heparin	30-37	serpin family D member 1	Homo sapiens	22-26
10530936-1	1999	The synthesis of three heparin analogues (i.e. compounds VI-VIII) having perphosphorylated thrombin binding domains (TBDs) is reported.	Heparin	23-30	cytochrome c oxidase subunit 8A	Homo sapiens	60-64
16229644-4	2005	In this study, heparin acrylic beads released fibroblast growth factor 2 (FGF2) to mimic constitutive signaling by mutated receptors, delivering FGF2 in addition to already existing normal tissue amounts.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	74-78
16229644-4	2005	In this study, heparin acrylic beads released fibroblast growth factor 2 (FGF2) to mimic constitutive signaling by mutated receptors, delivering FGF2 in addition to already existing normal tissue amounts.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	145-149
15866045-6	2005	Heparin enhanced Sema3A"s binding to neuropilin-1-expressing cells and potentiated its growth cone collapsing activity.	Heparin	0-7	sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3A	Mus musculus	17-23
10498855-14	1999	Heparin is an IP3 receptor antagonist.	Heparin	0-7	inositol 1,4,5-triphosphate receptor 3	Mus musculus	14-26
15695515-4	2005	Moreover, these protein-protein interactions are dependent on the ionic strength of the medium and are inhibited by heparin, and the kinetics of binding of FGF-2, FGF-4 and HGF/SF to Npn-1 are characterized by fast association rate constants (270,000-1,600,000 m(-1) s(-1)).	Heparin	116-123	hepatocyte growth factor	Homo sapiens	173-179
10494777-4	1999	Beta-thromboglobulin increased from 116 (80-148) microg/l to 1039 (757-1298) microg/l with uncoated and to 352 (229-638) microg/l with heparin coated tubing (intergroup p = 0.005).	Heparin	135-142	pro-platelet basic protein	Homo sapiens	0-20
10383431-5	1999	The C4b binding site demonstrated herein was also found to be a specific heparin binding site.	Heparin	73-80	complement C4B (Chido blood group)	Homo sapiens	4-7
15695515-4	2005	Moreover, these protein-protein interactions are dependent on the ionic strength of the medium and are inhibited by heparin, and the kinetics of binding of FGF-2, FGF-4 and HGF/SF to Npn-1 are characterized by fast association rate constants (270,000-1,600,000 m(-1) s(-1)).	Heparin	116-123	neuropilin 1	Homo sapiens	183-188
15695515-5	2005	These results suggest that Npn-1 possesses a "heparin" mimetic site that is able to interact at least in part through ionic bonding with the heparin binding site on many of the proteins studied.	Heparin	46-53	neuropilin 1	Homo sapiens	27-32
15695515-5	2005	These results suggest that Npn-1 possesses a "heparin" mimetic site that is able to interact at least in part through ionic bonding with the heparin binding site on many of the proteins studied.	Heparin	141-148	neuropilin 1	Homo sapiens	27-32
15728475-6	2005	Because platelets are the sole source of PF4 in the circulation, these findings may be relevant to the pathogenesis of certain immune-mediated disorders associated with platelet activation, such as heparin-induced thrombocytopenia and autoimmune thrombocytopenic purpura.	Heparin	198-205	platelet factor 4	Homo sapiens	41-44
10381515-1	1999	Heparin-induced thrombocytopenia with thrombosis (HITT) is associated with antibodies specific for complexes consisting of heparin and platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	154-157
10456457-0	1999	Involvement of Lys 62(217) and Lys 63(218) of human anticoagulant protein C in heparin stimulation of inhibition by the protein C inhibitor.	Heparin	79-86	serpin family A member 5	Homo sapiens	120-139
15662666-4	2005	Moreover, the PTTH-stimulated increase of Ca2+ levels was eliminated in the presence of heparin (an IP3 receptor blocker), and by TMB-8 which also blocked any PTTH-dependent increase of ecdysteroid secretion.	Heparin	88-95	prothoracicotropic hormone	Bombyx mori	14-18
10358067-5	1999	However, unlike CTGF, CTGF-L lacks the C-terminal domain implicated in dimerization and heparin binding.	Heparin	88-95	cellular communication network factor 5	Homo sapiens	22-28
15840332-0	2005	[The effect of freezing and low molecular weight heparin treatment on the production of hepatocyte growth factor of human RPE cells].	Heparin	49-56	hepatocyte growth factor	Homo sapiens	88-112
10354124-0	1999	Hepatocyte growth factor in serum after injection of unfractionated and low molecular weight heparin in healthy individuals.	Heparin	93-100	hepatocyte growth factor	Homo sapiens	0-24
10346980-3	1999	The suppression of heparin-releasable LPL activity produced by combinations of LPS and interleukin 1 (IL-1), IL-11 or tumour necrosis factor alpha(TNF-alpha) was substantially less than that expected from the simple additive action of the corresponding two effectors.	Heparin	19-26	interleukin 11	Rattus norvegicus	109-114
15383398-0	2005	Ca(2+)/calmodulin-dependent protein kinase II inhibition by heparin in mesangial cells.	Heparin	60-67	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	0-42
10341219-0	1999	Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain.	Heparin	118-125	Tenascin major	Drosophila melanogaster	68-73
15383398-1	2005	Heparin exerts an antiproliferative effect in smooth muscle cells, and the Ca(2+)/calmodulin-dependent protein kinase (CaMK) signaling pathway is heparin sensitive.	Heparin	146-153	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	75-117
10348899-1	1999	We identified a unique phospholipase A (PLA) with relatively low heparin affinity, which was distinguishable from the heparin-binding secretory PLA2s, in rat, mouse, and bovine brains and testes.	Heparin	65-72	phospholipase A and acyltransferase 1	Rattus norvegicus	23-38
15383398-1	2005	Heparin exerts an antiproliferative effect in smooth muscle cells, and the Ca(2+)/calmodulin-dependent protein kinase (CaMK) signaling pathway is heparin sensitive.	Heparin	146-153	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	119-123
10348899-1	1999	We identified a unique phospholipase A (PLA) with relatively low heparin affinity, which was distinguishable from the heparin-binding secretory PLA2s, in rat, mouse, and bovine brains and testes.	Heparin	65-72	phospholipase A and acyltransferase 1	Rattus norvegicus	40-43
10348899-1	1999	We identified a unique phospholipase A (PLA) with relatively low heparin affinity, which was distinguishable from the heparin-binding secretory PLA2s, in rat, mouse, and bovine brains and testes.	Heparin	118-125	phospholipase A and acyltransferase 1	Rattus norvegicus	23-38
10348899-1	1999	We identified a unique phospholipase A (PLA) with relatively low heparin affinity, which was distinguishable from the heparin-binding secretory PLA2s, in rat, mouse, and bovine brains and testes.	Heparin	118-125	phospholipase A and acyltransferase 1	Rattus norvegicus	40-43
10341752-9	1999	An HIPA test and a PF4/heparin immunoassay, performed as heparin-induced type II thrombocytopenia was suspected, subsequently confirmed the diagnosis.	Heparin	57-64	platelet factor 4	Homo sapiens	19-22
10209287-3	1999	In this study we determined the concentrations (IC50) of various polyanions required to stimulate thrombin inhibition by native recombinant HCII in comparison with three recombinant HCII variants having decreased affinity for heparin (Lys-173--&gt;Gln), dermatan sulphate (Arg-189--&gt;His), or both heparin and dermatan sulphate (Lys-185--&gt;Asn).	Heparin	226-233	serpin family D member 1	Homo sapiens	182-186
10209287-8	1999	These results suggest that, like dermatan sulphate and heparin, other polyanions stimulate HCII primarily by an allosteric mechanism requiring the N-terminal acidic domain.	Heparin	55-62	serpin family D member 1	Homo sapiens	91-95
15383398-4	2005	Heparin (1 microg/ml), but not chondroitin or dermatan sulfate, significantly attenuated both serum- or ionomycin-induced CaMK-II activity, and attendant c-fos mRNA expression, but did not affect upstream Ca(2+)/calmodulin.	Heparin	0-7	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	122-129
10203088-12	1999	Blockade of CD14 abrogated both LPS-induced TNF-alpha release and the effect of heparin or enoxaparin to enhance LPS-induced TNF-alpha release.	Heparin	80-87	CD14 molecule	Homo sapiens	12-16
15383398-9	2005	These results suggest that heparin at physiological concentrations acts at or downstream of CaMK-II to suppress its activity independent of an effect on autophosphorylation.	Heparin	27-34	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	92-99
15304392-1	2005	Heparin-induced thrombocytopenia and thrombosis (HITT) is a severe complication of heparin therapy caused by antibodies to complexes between unfractionated heparin (UFH) and platelet factor 4 (PF4) that form over a narrow molar range of reactants and initiate antibody-induced platelet activation.	Heparin	0-7	platelet factor 4	Homo sapiens	193-196
10082659-0	1999	Hepatocyte growth factor is a major mediator in heparin-induced angiogenesis.	Heparin	48-55	hepatocyte growth factor	Homo sapiens	0-24
10082659-4	1999	Administration of 3,000 U or 10,000 U of heparin caused significant increases in plasma HGF (40- and 54-fold, respectively), in absence of obvious increases in bFGF and VEGF levels.	Heparin	41-48	hepatocyte growth factor	Homo sapiens	88-91
10082659-5	1999	Furthermore, compared with the serum collected before heparin administration, the serum collected after heparin administration had more prominent growth-promoting and vascular tube-inducing properties on endothelial cells, and these increased activities were completely inhibited by neutralization of HGF, whereas neutralization of bFGF and VEGF had no effect.	Heparin	104-111	hepatocyte growth factor	Homo sapiens	301-304
10082659-6	1999	These findings suggest that HGF plays a significant role in heparin-induced angiogenesis.	Heparin	60-67	hepatocyte growth factor	Homo sapiens	28-31
10063992-0	1999	Low levels of heparin-releasable tissue factor pathway inhibitor in young patients with thrombosis.	Heparin	14-21	tissue factor pathway inhibitor	Homo sapiens	33-64
10063992-3	1999	To investigate if deficiency of heparin-releasable TFPI is associated with thrombosis.	Heparin	32-39	tissue factor pathway inhibitor	Homo sapiens	51-55
10063992-4	1999	we measured TFPI activity in plasma before and 10 min after intravenous injection of 7500 IU unfractionated heparin in 64 young patients with venous thrombosis, 49 young patients with arterial thrombosis and 38 healthy individuals.	Heparin	108-115	tissue factor pathway inhibitor	Homo sapiens	12-16
10063992-8	1999	However, the causative role of low heparin-releasable TFPI remains uncertain, because co-segregation of the defect with thrombotic symptoms could not be demonstrated in the small number of families studied.	Heparin	35-42	tissue factor pathway inhibitor	Homo sapiens	54-58
9920817-7	1999	However, OGF fractions eluted at higher AcN concentrations (30-70%) showed heparin-binding activity and were inhibited in their bioactivity by the anti-MIP-1alpha antibody.	Heparin	75-82	C-C motif chemokine ligand 3	Rattus norvegicus	152-162
9867861-12	1999	These results indicate that the properdin modules of TSP1 specifically interact with fibrinogen/fibrin but not with heparin under physiologic conditions.	Heparin	116-123	thrombospondin 1	Rattus norvegicus	53-57
9882700-8	1999	All FGF2 catabolic fragments bound heparin, demonstrating the preservation of their HSPG-binding site during the in vivo intracellular catabolism of FGF2.	Heparin	35-42	fibroblast growth factor 2	Rattus norvegicus	4-8
9882700-8	1999	All FGF2 catabolic fragments bound heparin, demonstrating the preservation of their HSPG-binding site during the in vivo intracellular catabolism of FGF2.	Heparin	35-42	fibroblast growth factor 2	Rattus norvegicus	149-153
10338292-5	1999	Heparin blocked the association of beta-amyloid with cells, as did an antibody to one of the apolipoprotein E receptors (the low-density lipoprotein receptor-related protein).	Heparin	0-7	apolipoprotein E	Cricetulus griseus	93-109
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	hepatocyte growth factor	Homo sapiens	295-298
10209655-7	1998	The initial binding to proteoglycans may be facilitated by lipoprotein lipase and hepatic lipase which possess both lipid- and heparin-binding domains.	Heparin	127-134	lipase C, hepatic type	Homo sapiens	82-96
9790982-5	1998	Although phosphoinositide hydrolysis is shown to be coupled with group I mGluRs, we found that intracellular injections of various PLC inhibitors and an IP3 receptor antagonist heparin only partially inhibited the 1S, 3R-ACPD-induced current.	Heparin	177-184	inositol 1,4,5-triphosphate receptor 3	Mus musculus	153-165
9784593-6	1998	Furthermore, it was demonstrated that in cultures of mouse calvariae the production of MMP-13 was induced by the potent MMP-stimulator heparin and by parathyroid hormone (PTH), whereas the levels of MMP-3 remained unchanged.	Heparin	135-142	matrix metallopeptidase 13	Mus musculus	87-93
9799666-0	1998	Immediate increase in circulating hepatocyte growth factor/scatter factor by heparin.	Heparin	77-84	hepatocyte growth factor	Homo sapiens	34-58
9799666-3	1998	This study was designed to study the effect of heparin on the release of HGF.	Heparin	47-54	hepatocyte growth factor	Homo sapiens	73-76
9799666-5	1998	A dose-dependent increase in circulating HGF was measured with peak levels occurring 10 min after injection of 300 units/kg of heparin (15.4+/-2.0 ng/ml after v 0.	Heparin	127-134	hepatocyte growth factor	Homo sapiens	41-44
9799666-12	1998	This study suggests that heparin-induced effects such as the promotion of angiogenesis may be at least partly due to the release of HGF.	Heparin	25-32	hepatocyte growth factor	Homo sapiens	132-135
9798991-11	1998	Human neutrophil elastase release at 120 min was significantly inhibited in the presence of DUP 714 to 37% of the value with heparin alone.	Heparin	125-132	elastase, neutrophil expressed	Homo sapiens	6-25
9798992-0	1998	Fucoidan, as heparin, induces tissue factor pathway inhibitor release from cultured human endothelial cells.	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	30-61
9798992-2	1998	Tissue factor pathway inhibitor (TFPI), which regulates the tissue factor-dependent pathway of blood coagulation, is released from the endothelium by heparin, a mechanism contributing to its antithrombotic activity.	Heparin	150-157	tissue factor pathway inhibitor	Homo sapiens	0-31
9819002-0	1998	A supersulfated low-molecular-weight heparin (IK-SSH) increases plasma levels of free and total tissue factor pathway inhibitor after intravenous and subcutaneous administration in humans.	Heparin	37-44	tissue factor pathway inhibitor	Homo sapiens	96-127
9819002-1	1998	Unfractionated as well as low-molecular-weight heparins (LMWH) are known to cause an increase in blood levels of tissue factor pathway inhibitor (TFPI).	Heparin	47-55	tissue factor pathway inhibitor	Homo sapiens	113-144
9819002-1	1998	Unfractionated as well as low-molecular-weight heparins (LMWH) are known to cause an increase in blood levels of tissue factor pathway inhibitor (TFPI).	Heparin	47-55	tissue factor pathway inhibitor	Homo sapiens	146-150
9712870-0	1998	The putative heparin-specific N-acetylglucosaminyl N-Deacetylase/N-sulfotransferase also occurs in non-heparin-producing cells.	Heparin	13-20	sulfotransferase family 1D, member 1	Rattus norvegicus	65-83
9712870-3	1998	We have now found that cells derived from embryonic bovine trachea, a tissue that does not synthesize heparin, has a N-acetylglucosaminyl N-deacetylase/N-sulfotransferase, which has 95% amino acid sequence identity to the above enzyme postulated to be involved in the biosynthesis of heparin.	Heparin	284-291	sulfotransferase family 1D, member 1	Rattus norvegicus	152-170
9705269-4	1998	At concentrations of 10 microg protein/ml, both native phosphacan and the core protein obtained by chondroitinase treatment potentiated the mitogenic effect of FGF-2 (5 ng/ml) on NIH/3T3 cells by 75-90%, which is nearly the same potentiation as that produced by heparin at an equivalent concentration.	Heparin	262-269	fibroblast growth factor 2	Mus musculus	160-165
9736420-0	1998	Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy.	Heparin	45-52	tissue factor pathway inhibitor	Homo sapiens	122-153
9736420-0	1998	Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy.	Heparin	45-52	tissue factor pathway inhibitor	Homo sapiens	155-159
9736420-0	1998	Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy.	Heparin	72-79	tissue factor pathway inhibitor	Homo sapiens	122-153
9736420-0	1998	Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy.	Heparin	72-79	tissue factor pathway inhibitor	Homo sapiens	155-159
9736420-2	1998	Heparin exerts its function by potentiating antithrombin and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	75-106
9736420-2	1998	Heparin exerts its function by potentiating antithrombin and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	108-112
9736420-6	1998	Infusion of UFH, but not subcutaneous LMWH, was found to attenuate the antithrombotic defense by a selective decrease of both circulating antithrombin (-21+/-7%, p&lt;0.0001) and of free and endothelial-bound TFPI.	Heparin	12-15	tissue factor pathway inhibitor	Homo sapiens	209-213
9736420-8	1998	The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis.	Heparin	27-30	tissue factor pathway inhibitor	Homo sapiens	60-64
9688646-6	1998	The contraction induced by CCK was inhibited by the phospholipase C (PLC) inhibitor U-73122, anti-PLC-beta3 antibody, and the IP3 receptor antagonist heparin but was not inhibited by the the phospholipase D inhibitor propranolol or antibodies against PLC-beta1 or PLC-beta2.	Heparin	150-157	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	126-138
9692954-4	1998	Correctly folded PEDF bound to immobilized heparin, chondroitin sulfate-A, -B, -C, and dextran sulfate columns and eluted from each with an increase in NaCl concentration.	Heparin	43-50	serpin family F member 1	Homo sapiens	17-21
9641623-3	1998	We studied both their anticoagulant activity and the catalysis of thrombin (T) inhibition by heparin cofactor II (HCII) and antithrombin (AT) in the presence of these dextran derivatives relative to heparin and dextran sulfate (DXSu).	Heparin	93-100	serpin family D member 1	Homo sapiens	114-118
9616153-1	1998	A recent study indicated that negatively charged substances such as heparin and dextran sulfate accelerate thrombin activation of coagulation factor XI by a template mechanism.	Heparin	68-75	coagulation factor XI	Homo sapiens	130-151
10097819-1	1998	The discovery of the role of PF4 in the development and pathogenicity of heparin-dependent antibodies which trigger heparin-induced thrombocytopenia (HIT), a rare but severe adverse effect of heparin therapy, has allowed us to revisit the diagnosis of this complication and the pathological mechanisms involved.	Heparin	73-80	platelet factor 4	Homo sapiens	29-32
10097819-1	1998	The discovery of the role of PF4 in the development and pathogenicity of heparin-dependent antibodies which trigger heparin-induced thrombocytopenia (HIT), a rare but severe adverse effect of heparin therapy, has allowed us to revisit the diagnosis of this complication and the pathological mechanisms involved.	Heparin	116-123	platelet factor 4	Homo sapiens	29-32
9674734-2	1998	In the present study we investigated whether subcutaneous (s.c.) administration of a low molecular weight heparin (LMWH), enoxaparin, had a different effect on intravascular pools of TFPI compared with continuous i.v.	Heparin	106-113	tissue factor pathway inhibitor	Homo sapiens	183-187
9674734-6	1998	caused an 8-13-fold increase in plasma-free TFPI antigen (TFPI Ag), followed by a progressive decrease (81 +/- 4%, P&lt;0.001) during the 72 h infusion with UFH.	Heparin	157-160	tissue factor pathway inhibitor	Homo sapiens	44-48
9674734-6	1998	caused an 8-13-fold increase in plasma-free TFPI antigen (TFPI Ag), followed by a progressive decrease (81 +/- 4%, P&lt;0.001) during the 72 h infusion with UFH.	Heparin	157-160	tissue factor pathway inhibitor	Homo sapiens	58-62
9674734-7	1998	4 h after discontinuation of the infusion, basal free TFPI Ag and heparin-releasable TFPI were significantly decreased compared with the concentrations before the infusion (30 +/- 9%, and 27 +/- 7%, respectively).	Heparin	66-73	tissue factor pathway inhibitor	Homo sapiens	85-89
9674734-9	1998	The changes in plasma TFPI Ag by UFH and LMWH were statistically different between groups both in pre- (P&lt;0.001) and post-heparin (P&lt;0.0001) plasma.	Heparin	33-36	tissue factor pathway inhibitor	Homo sapiens	22-26
9674734-9	1998	The changes in plasma TFPI Ag by UFH and LMWH were statistically different between groups both in pre- (P&lt;0.001) and post-heparin (P&lt;0.0001) plasma.	Heparin	125-132	tissue factor pathway inhibitor	Homo sapiens	22-26
9674734-10	1998	The differential effect of UFH and LMWH on intravascular pools of TFPI may contribute to the understanding of the apparent superior efficacy of LMWHs in the treatment of both arterial and venous thrombosis.	Heparin	27-30	tissue factor pathway inhibitor	Homo sapiens	66-70
9674755-3	1998	Recent reports on altered distribution amongst individuals with heparin-induced thrombocytopenia (HIT) prompted us to examine the Fc gammaRIIA polymorphism in a cohort of patients with refractory idiopathic (immune) thrombocytopenic purpura (ITP), in whom severe disease had required them to undergo splenectomy.	Heparin	64-71	Fc gamma receptor IIa	Homo sapiens	130-142
9657912-7	1998	Basic fibroblast growth factor (bFGF), which rescues photoreceptors in several rodent models of retinal degeneration, produced a significant increase in survival time in the presence of the cofactor heparin.	Heparin	199-206	fibroblast growth factor 2	Rattus norvegicus	0-30
9657912-7	1998	Basic fibroblast growth factor (bFGF), which rescues photoreceptors in several rodent models of retinal degeneration, produced a significant increase in survival time in the presence of the cofactor heparin.	Heparin	199-206	fibroblast growth factor 2	Rattus norvegicus	32-36
9765663-3	1998	PATIENTS AND METHODS: One hundred thirteen patients with heparin-induced thrombocytopenia were treated with Refludan in two studies, HAT1 and HAT2.	Heparin	57-64	histone acetyltransferase 1	Homo sapiens	133-137
9591596-0	1998	Extraskeletal uptake of technetium-99m-MDP in sites of heparin administration.	Heparin	55-62	dipeptidase 1	Homo sapiens	39-42
9602078-0	1998	Identification of heparin-binding stretches of a naturally occurring deleted variant of hepatocyte growth factor (dHGF).	Heparin	18-25	hepatocyte growth factor	Homo sapiens	88-112
9602078-2	1998	While both HGF and dHGF bind to heparin, the residues involved in the binding to heparin have not been identified in either protein.	Heparin	32-39	hepatocyte growth factor	Homo sapiens	11-14
9537999-1	1998	Clusterin is a highly conserved mammalian glycoprotein which has been predicted to contain heparin-binding sites.	Heparin	91-98	clusterin	Homo sapiens	0-9
9537999-2	1998	We tested this prediction by studying the interactions between heparin and clusterin using ELISA and heparin affinity chromatography methodologies.	Heparin	63-70	clusterin	Homo sapiens	75-84
9537999-5	1998	There was a dose-dependent increase in the ELISA signal from bound biotinylated heparin with increasing concentrations of plate-bound clusterin.	Heparin	80-87	clusterin	Homo sapiens	134-143
9537999-6	1998	The apparent affinity constant for binding of biotinylated heparin to plate-bound clusterin at pH 6.0 was estimated as 0.06 +/- 0.02 microM.	Heparin	59-66	clusterin	Homo sapiens	82-91
9537999-7	1998	Unlabeled heparin blocked the binding of biotinylated heparin to clusterin over a concentration range similar to that of the binding of biotinylated heparin to plate-bound clusterin.	Heparin	10-17	clusterin	Homo sapiens	65-74
9537999-7	1998	Unlabeled heparin blocked the binding of biotinylated heparin to clusterin over a concentration range similar to that of the binding of biotinylated heparin to plate-bound clusterin.	Heparin	54-61	clusterin	Homo sapiens	65-74
9537999-7	1998	Unlabeled heparin blocked the binding of biotinylated heparin to clusterin over a concentration range similar to that of the binding of biotinylated heparin to plate-bound clusterin.	Heparin	54-61	clusterin	Homo sapiens	65-74
9537999-8	1998	The binding of biotinylated heparin to clusterin was independent of the presence or absence of Ca2+.	Heparin	28-35	clusterin	Homo sapiens	39-48
9537999-9	1998	The binding of biotinylated heparin to plate-bound clusterin increased with decreasing pH over the range 5.5-8.0 and was characterized by an apparent pKa of 6.9.	Heparin	28-35	clusterin	Homo sapiens	51-60
9537999-10	1998	Clusterin in human serum bound to heparin-Sepharose at pH 6.0 but not at pH 7.4.	Heparin	34-41	clusterin	Homo sapiens	0-9
9568695-5	1998	The binding of human amylin to perlecan was similarly observed using perlecan heparan sulfate glycosaminoglycans (GAGs), and was completely abolished by 10 micromol/l heparin.	Heparin	167-174	islet amyloid polypeptide	Homo sapiens	21-27
9568695-7	1998	Other sulfated GAGs and related macromolecules were also effective in the enhancement of amylin fibril formation in the order of heparin &gt; heparan sulfate &gt; chondroitin-4-sulfate = dermatan sulfate = dextran sulfate &gt; pentosan polysulfate, implicating the importance of the specific GAG/carbohydrate backbone.	Heparin	129-136	islet amyloid polypeptide	Homo sapiens	89-95
9568695-8	1998	The sulfate content of heparin/heparan sulfate was also important for the enhancement of amylin fibril formation in the order of heparin &gt; N-desulfated N-acetylated heparin &gt; completely desulfated N-sulfated heparin &gt; completely desulfated N-acetylated heparin.	Heparin	23-30	islet amyloid polypeptide	Homo sapiens	89-95
9568695-8	1998	The sulfate content of heparin/heparan sulfate was also important for the enhancement of amylin fibril formation in the order of heparin &gt; N-desulfated N-acetylated heparin &gt; completely desulfated N-sulfated heparin &gt; completely desulfated N-acetylated heparin.	Heparin	129-136	islet amyloid polypeptide	Homo sapiens	89-95
9669748-0	1998	Structural requirements of human tissue factor pathway inhibitor (TFPI) and heparin for TFPI-heparin interaction.	Heparin	76-83	tissue factor pathway inhibitor	Homo sapiens	88-92
9669748-1	1998	Heparin affinity chromatography of synthetic peptide fragments mimicking tissue factor pathway inhibitor (TFPI) indicated that the minimal heparin binding sequence consists of 12 amino acid residues located at the C-terminal tail.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	73-104
9669748-1	1998	Heparin affinity chromatography of synthetic peptide fragments mimicking tissue factor pathway inhibitor (TFPI) indicated that the minimal heparin binding sequence consists of 12 amino acid residues located at the C-terminal tail.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	106-110
9669748-1	1998	Heparin affinity chromatography of synthetic peptide fragments mimicking tissue factor pathway inhibitor (TFPI) indicated that the minimal heparin binding sequence consists of 12 amino acid residues located at the C-terminal tail.	Heparin	139-146	tissue factor pathway inhibitor	Homo sapiens	73-104
9669748-1	1998	Heparin affinity chromatography of synthetic peptide fragments mimicking tissue factor pathway inhibitor (TFPI) indicated that the minimal heparin binding sequence consists of 12 amino acid residues located at the C-terminal tail.	Heparin	139-146	tissue factor pathway inhibitor	Homo sapiens	106-110
9669748-3	1998	Affinity chromatography of TFPI using immobilized heparin derivatives regiospecifically desulfated at O-6 of the glucosamine residue, N-2 of the glucosamine residue, and/or O-2 of the iduronic acid residue indicated that all the sulfate groups in heparin appeared to be required for TFPI-heparin interaction.	Heparin	50-57	tissue factor pathway inhibitor	Homo sapiens	27-31
9669748-3	1998	Affinity chromatography of TFPI using immobilized heparin derivatives regiospecifically desulfated at O-6 of the glucosamine residue, N-2 of the glucosamine residue, and/or O-2 of the iduronic acid residue indicated that all the sulfate groups in heparin appeared to be required for TFPI-heparin interaction.	Heparin	50-57	tissue factor pathway inhibitor	Homo sapiens	283-287
9669748-3	1998	Affinity chromatography of TFPI using immobilized heparin derivatives regiospecifically desulfated at O-6 of the glucosamine residue, N-2 of the glucosamine residue, and/or O-2 of the iduronic acid residue indicated that all the sulfate groups in heparin appeared to be required for TFPI-heparin interaction.	Heparin	247-254	tissue factor pathway inhibitor	Homo sapiens	27-31
9669748-3	1998	Affinity chromatography of TFPI using immobilized heparin derivatives regiospecifically desulfated at O-6 of the glucosamine residue, N-2 of the glucosamine residue, and/or O-2 of the iduronic acid residue indicated that all the sulfate groups in heparin appeared to be required for TFPI-heparin interaction.	Heparin	247-254	tissue factor pathway inhibitor	Homo sapiens	27-31
9669748-5	1998	In vitro experiments on the inhibition of factor Xa by TFPI enhanced with native and chemically modified heparins afforded similar results.	Heparin	105-113	tissue factor pathway inhibitor	Homo sapiens	55-59
9622211-1	1998	Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins.	Heparin	19-27	tissue factor pathway inhibitor	Homo sapiens	98-129
9622211-1	1998	Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins.	Heparin	19-27	tissue factor pathway inhibitor	Homo sapiens	131-135
9500522-7	1998	Using this assay we demonstrate that IL-5 binds to heparin.	Heparin	51-58	interleukin 5	Homo sapiens	37-41
9500522-8	1998	The IL-5/heparin interaction is inhibited by ethylenediaminetetraacetate and enhanced by low concentrations of zinc ions.	Heparin	9-16	interleukin 5	Homo sapiens	4-8
9500522-9	1998	IL-5 interacts with iduronic acid containing glycosaminoglycans, and heparan sulfate preparations that have numerous N-sulfated domains per chain are especially efficient at inhibiting heparin binding.	Heparin	185-192	interleukin 5	Homo sapiens	0-4
9500522-10	1998	Both IL-5/heparin binding and the synergistic effect of IL-5 and heparan sulfate on cell proliferation were inhibited by an anti-IL-5 monoclonal antibody.	Heparin	10-17	interleukin 5	Homo sapiens	5-9
9548595-0	1998	Identification of the epitope of a monoclonal antibody that inhibits heparin binding of lipoprotein lipase: new evidence for a carboxyl-terminal heparin-binding domain.	Heparin	69-76	lipoprotein lipase	Bos taurus	88-106
9548595-0	1998	Identification of the epitope of a monoclonal antibody that inhibits heparin binding of lipoprotein lipase: new evidence for a carboxyl-terminal heparin-binding domain.	Heparin	145-152	lipoprotein lipase	Bos taurus	88-106
9548595-3	1998	In solid phase assays, xCAL 3-6a inhibited the binding of LPL to both heparan sulfate and heparin.	Heparin	90-97	lipoprotein lipase	Bos taurus	58-61
9548595-11	1998	Heparin-Sepharose chromatography of wild-type LPL and a mutant LPL in which the well-characterized heparin-binding sequence (Arg 281-Lys 282-Arg 284) has been mutated was carried out in the presence and absence of xCAL 3-6a.	Heparin	0-7	lipoprotein lipase	Bos taurus	46-49
9548595-11	1998	Heparin-Sepharose chromatography of wild-type LPL and a mutant LPL in which the well-characterized heparin-binding sequence (Arg 281-Lys 282-Arg 284) has been mutated was carried out in the presence and absence of xCAL 3-6a.	Heparin	0-7	lipoprotein lipase	Bos taurus	63-66
9548595-11	1998	Heparin-Sepharose chromatography of wild-type LPL and a mutant LPL in which the well-characterized heparin-binding sequence (Arg 281-Lys 282-Arg 284) has been mutated was carried out in the presence and absence of xCAL 3-6a.	Heparin	99-106	lipoprotein lipase	Bos taurus	63-66
9506849-0	1998	Heparin inhibits phorbol ester-induced ornithine decarboxylase gene expression in endothelial cells.	Heparin	0-7	ornithine decarboxylase 1	Homo sapiens	39-62
9506849-3	1998	Here we show that heparin markedly inhibited serum-stimulated DNA synthesis and ornithine decarboxylase (ODC) mRNA expression in human endothelial cells (HEC).	Heparin	18-25	ornithine decarboxylase 1	Homo sapiens	80-103
9506849-3	1998	Here we show that heparin markedly inhibited serum-stimulated DNA synthesis and ornithine decarboxylase (ODC) mRNA expression in human endothelial cells (HEC).	Heparin	18-25	ornithine decarboxylase 1	Homo sapiens	105-108
9506849-6	1998	In serum-free cultured HEC, heparin completely abolished the increase in DNA synthesis and ODC mRNA expression elicited by a number of PKC activators.	Heparin	28-35	ornithine decarboxylase 1	Homo sapiens	91-94
10850445-3	2000	TMPP demonstrated potent inhibition of binding of soluble FGF receptor 1 (FGFR1) to FGF2 immobilized on heparin at submicromolar concentrations.	Heparin	104-111	fibroblast growth factor receptor 1	Mus musculus	58-72
10850445-3	2000	TMPP demonstrated potent inhibition of binding of soluble FGF receptor 1 (FGFR1) to FGF2 immobilized on heparin at submicromolar concentrations.	Heparin	104-111	fibroblast growth factor receptor 1	Mus musculus	74-79
10850445-3	2000	TMPP demonstrated potent inhibition of binding of soluble FGF receptor 1 (FGFR1) to FGF2 immobilized on heparin at submicromolar concentrations.	Heparin	104-111	fibroblast growth factor 2	Mus musculus	84-88
10799506-2	2000	Using truncated recombinant HBHA forms and hybrid proteins containing HBHA repeats grafted onto the Escherichia coli maltose-binding protein (MBP), we found that these repeats are responsible for heparin binding.	Heparin	196-203	myelin basic protein	Homo sapiens	142-145
10747011-0	2000	Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin.	Heparin	135-142	laminin subunit alpha 2	Homo sapiens	62-76
10747011-3	2000	We report the 2.0 A crystal structure of the laminin alpha2 LG4-LG5 domain pair, which harbours binding sites for heparin and the cell surface receptor alpha-dystroglycan, and is 41% identical to the laminin alpha1 E3 fragment.	Heparin	114-121	laminin subunit alpha 2	Homo sapiens	45-59
10727405-0	2000	The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain.	Heparin	4-11	C-type lectin domain family 3 member B	Homo sapiens	28-39
10727405-1	2000	Tetranectin is a homotrimeric plasma and extracellular-matrix protein that binds plasminogen and complex sulphated polysaccharides including heparin.	Heparin	141-148	C-type lectin domain family 3 member B	Homo sapiens	0-11
10727405-6	2000	Here we show that the heparin-binding site in tetranectin resides not in the carbohydrate recognition domain but within the N-terminal region, comprising the 16 amino acid residues encoded by exon 1.	Heparin	22-29	C-type lectin domain family 3 member B	Homo sapiens	46-57
10864420-0	2000	Postheparin plasma diamine oxidase activity and the anticoagulant effect of heparin.	Heparin	4-11	amine oxidase copper containing 1	Homo sapiens	19-34
10864421-0	2000	Inhibition of diamine oxidase activity by heparins.	Heparin	42-50	amine oxidase copper containing 1	Homo sapiens	14-29
10704346-4	2000	The HS-GAG analog heparin decreased Ad5- and Ad2-mediated infection and binding starting from the concentration of 0.1 microgram/ml, up to a maximum of 50%.	Heparin	18-25	Alzheimer disease, familial, type 5	Homo sapiens	36-39
10704346-6	2000	The effect of heparin on Ad5 binding has not been observed in surface GAG-defective Raji cells and after treating A549 cells with heparin lyases I, II,and III.	Heparin	14-21	Alzheimer disease, familial, type 5	Homo sapiens	25-28
10704346-7	2000	The binding of Ad5 was completely abolished when both CAR was blocked with RmcB antibody and HS-GAGs were competitively inhibited by heparin.	Heparin	133-140	Alzheimer disease, familial, type 5	Homo sapiens	15-18
10688805-1	2000	Antibodies to PF4/heparin can be demonstrated in almost all patients with heparin-induced thrombocytopenia/thrombosis (HIT/HITT) and in some persons exposed to heparin who do not have clinical manifestations.	Heparin	74-81	platelet factor 4	Homo sapiens	14-17
10688805-3	2000	To circumvent this problem, we developed a murine monoclonal antibody (mAb) to human (h) PF4/heparin complexes.	Heparin	93-100	platelet factor 4	Homo sapiens	89-92
10688805-4	2000	A monoclonal IgG(2bkappa )antibody (designated KKO) was identified that bound specifically to hPF4/heparin complexes.	Heparin	99-106	platelet factor 4	Homo sapiens	94-98
10688805-9	2000	Variants of PF4 complexed to heparin were recognized equally well by KKO and HIT/HITT sera.	Heparin	29-36	platelet factor 4	Homo sapiens	12-15
10660581-13	2000	Dislodging MMPs by treatment with compounds such as heparin might be beneficial in attenuating excessive tissue breakdown such as occurs in cancer metastasis, arthritis, and angiogenesis.	Heparin	52-59	matrix metallopeptidase 2	Rattus norvegicus	11-15
10665930-13	2000	Treatment of rats with heparin blunted glomerular proliferation as well as ERK activation and restored p38 MAP kinase activity.	Heparin	23-30	mitogen activated protein kinase 14	Rattus norvegicus	103-106
10679527-3	2000	In particular, the collagen-like domain of ColQ contains two heparin-binding domains which interact with heparan sulfate proteoglycans in the basal lamina.	Heparin	61-68	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	43-47
10679527-6	2000	Moreover, this model permits the analysis of interactions between the heparin-binding domains of ColQ and heparin, and could also prove useful in the prediction of interaction domains with other putative basal lamina receptors.	Heparin	70-77	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	97-101
10606880-0	1999	Partial depletion of tissue factor pathway inhibitor during subcutaneous administration of unfractionated heparin, but not with two low molecular weight heparins.	Heparin	106-113	tissue factor pathway inhibitor	Homo sapiens	21-52
10606880-11	1999	On UFH administered once daily, basal free TFPI antigen decreased by 50%, 56% and 27% on day 2, 3 and 5 respectively, compared with day 1.	Heparin	3-6	tissue factor pathway inhibitor	Homo sapiens	43-47
10630202-8	1999	The activity of bFGF was enhanced by exogenous heparin added to the culture medium; although heparin alone failed to stimulate either neurite extension or neuronal cell sprouting.	Heparin	47-54	fibroblast growth factor 2	Gallus gallus	16-20
10497173-5	1999	Here, a series of homogeneously sized, (3)H-labeled heparin fragments were evaluated for their capacity to bind to free glutathione S-transferase (GST)-Tat protein and to immobilized GST-Tat.	Heparin	52-59	tyrosine aminotransferase	Homo sapiens	152-155
10497173-5	1999	Here, a series of homogeneously sized, (3)H-labeled heparin fragments were evaluated for their capacity to bind to free glutathione S-transferase (GST)-Tat protein and to immobilized GST-Tat.	Heparin	52-59	tyrosine aminotransferase	Homo sapiens	187-190
10497173-6	1999	Hexasaccharides represent the minimum sized heparin fragments able to interact with GST-Tat at physiological ionic strength.	Heparin	44-51	tyrosine aminotransferase	Homo sapiens	88-91
10497173-8	1999	6-Mer heparin binds GST-Tat with a dissociation constant (K(d)) equal to 0.7 +/- 0.4 microM and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	6-13	tyrosine aminotransferase	Homo sapiens	24-27
10497173-8	1999	6-Mer heparin binds GST-Tat with a dissociation constant (K(d)) equal to 0.7 +/- 0.4 microM and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	6-13	tyrosine aminotransferase	Homo sapiens	124-127
10497173-9	1999	Interaction of GST-Tat with 22-mer or full-size heparin is consistent instead with two-component binding.	Heparin	48-55	tyrosine aminotransferase	Homo sapiens	19-22
10497173-10	1999	At subsaturating concentrations, a single molecule of heparin interacts with 4-6 molecules of GST-Tat with high affinity (K(d) values in the nanomolar range of concentration); at saturating concentrations, heparin binds GST-Tat with lower affinity (K(d) values in the micromolar range of concentration) and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	54-61	tyrosine aminotransferase	Homo sapiens	98-101
10497173-10	1999	At subsaturating concentrations, a single molecule of heparin interacts with 4-6 molecules of GST-Tat with high affinity (K(d) values in the nanomolar range of concentration); at saturating concentrations, heparin binds GST-Tat with lower affinity (K(d) values in the micromolar range of concentration) and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	54-61	tyrosine aminotransferase	Homo sapiens	224-227
10497173-10	1999	At subsaturating concentrations, a single molecule of heparin interacts with 4-6 molecules of GST-Tat with high affinity (K(d) values in the nanomolar range of concentration); at saturating concentrations, heparin binds GST-Tat with lower affinity (K(d) values in the micromolar range of concentration) and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	54-61	tyrosine aminotransferase	Homo sapiens	224-227
10497173-10	1999	At subsaturating concentrations, a single molecule of heparin interacts with 4-6 molecules of GST-Tat with high affinity (K(d) values in the nanomolar range of concentration); at saturating concentrations, heparin binds GST-Tat with lower affinity (K(d) values in the micromolar range of concentration) and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	206-213	tyrosine aminotransferase	Homo sapiens	98-101
10497173-10	1999	At subsaturating concentrations, a single molecule of heparin interacts with 4-6 molecules of GST-Tat with high affinity (K(d) values in the nanomolar range of concentration); at saturating concentrations, heparin binds GST-Tat with lower affinity (K(d) values in the micromolar range of concentration) and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	206-213	tyrosine aminotransferase	Homo sapiens	224-227
10497173-10	1999	At subsaturating concentrations, a single molecule of heparin interacts with 4-6 molecules of GST-Tat with high affinity (K(d) values in the nanomolar range of concentration); at saturating concentrations, heparin binds GST-Tat with lower affinity (K(d) values in the micromolar range of concentration) and a molar oligosaccharide:GST-Tat ratio of about 1:1.	Heparin	206-213	tyrosine aminotransferase	Homo sapiens	224-227
10497173-12	1999	The data demonstrate that the modality of heparin-Tat interaction is strongly affected by the size of the saccharide chain.	Heparin	42-49	tyrosine aminotransferase	Homo sapiens	50-53
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	45-52	platelet factor 4	Homo sapiens	41-44
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	72-79	platelet factor 4	Homo sapiens	41-44
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	72-79	platelet factor 4	Homo sapiens	147-150
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	72-79	platelet factor 4	Homo sapiens	147-150
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	72-79	platelet factor 4	Homo sapiens	41-44
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	72-79	platelet factor 4	Homo sapiens	147-150
10464257-14	1999	Of particular interest to the biology of PF4-heparin complex formation, heparin-induced thrombocytopenia antibody binding occurs at about the same PF4-M2:H12 ratio as does this transition to a partially folded PF4-M2 state, strongly suggesting that heparin-induced thrombocytopenia antibody recognizes a less folded, lower aggregate state of the protein.	Heparin	72-79	platelet factor 4	Homo sapiens	147-150
10479670-0	1999	Cellular effects of heparin on the production and release of tissue factor pathway inhibitor in human endothelial cells in culture.	Heparin	20-27	tissue factor pathway inhibitor	Homo sapiens	61-92
10479670-3	1999	Here we describe the in vitro effects of heparin on the cellular localization, gene expression, and release of TFPI in human ECs in culture.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	111-115
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	20-27	tissue factor pathway inhibitor	Homo sapiens	144-148
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	20-27	tissue factor pathway inhibitor	Homo sapiens	197-201
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	20-27	tissue factor pathway inhibitor	Homo sapiens	197-201
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	29-32	tissue factor pathway inhibitor	Homo sapiens	144-148
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	29-32	tissue factor pathway inhibitor	Homo sapiens	197-201
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	29-32	tissue factor pathway inhibitor	Homo sapiens	197-201
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	144-148
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	197-201
10479670-4	1999	Both unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH; Fragmin) time-dependently induced a significant enhanced secretion of TFPI, paralleled by a redistribution and increase of TFPI on the cell surface and a decrease of intracellular TFPI.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	197-201
10479670-10	1999	After the first 4 to 8 hours, depletion of intracellular TFPI was observed, more significantly with UFH.	Heparin	100-103	tissue factor pathway inhibitor	Homo sapiens	57-61
10479670-13	1999	Heparin-stimulated release of TFPI decreased significantly in the presence of PMA to a level that was 2.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	30-34
10479670-16	1999	Altogether, our results suggest that the heparin-induced release of TFPI might involve a more specific mechanism(s) than the previously hypothesized simple displacement of TFPI from the cell surface glycocalyx.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	68-72
10479670-16	1999	Altogether, our results suggest that the heparin-induced release of TFPI might involve a more specific mechanism(s) than the previously hypothesized simple displacement of TFPI from the cell surface glycocalyx.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	172-176
10479670-17	1999	We assume that the increased secretion and redistribution of cellular TFPI induced by heparins in ECs in culture can play an important role in the modulation of the anticoagulant properties of the endothelium.	Heparin	86-94	tissue factor pathway inhibitor	Homo sapiens	70-74
10479671-10	1999	However, factor Xa activity, assayed after 24 hours by incubation of the injured arterial segments with the chromogenic substrate S-2222, was decreased more markedly on arteries from rTFPI-treated animals (0.14+/-0.13 OD) than those from heparin-treated animals (0.29+/-0.18 OD) compared with controls (0.	Heparin	238-245	tissue factor pathway inhibitor	Rattus norvegicus	183-188
10456887-3	1999	The mechanism involves specific bacterial recruitment of heparin, glycosaminoglycans, or related sulfated polysaccharides, which in turn serve as universal binding sites for a diverse array of mammalian heparin binding proteins, including adhesive glycoproteins (vitronectin and fibronectin), inflammatory (MCP-3, PF-4, and MIP-1alpha) and immunomodulatory (gamma interferon) intermediates, and fibroblast growth factor.	Heparin	57-64	platelet factor 4	Homo sapiens	314-318
10468530-12	1999	CONCLUSIONS: Heparin administration during LV hypertension increases heparin-binding angiogenic factors FGF-2 and VEGF in the LV and ameliorates decreases in LV perfusion capacity and capillary density.	Heparin	69-76	fibroblast growth factor 2	Ovis aries	104-109
10468530-12	1999	CONCLUSIONS: Heparin administration during LV hypertension increases heparin-binding angiogenic factors FGF-2 and VEGF in the LV and ameliorates decreases in LV perfusion capacity and capillary density.	Heparin	69-76	vascular endothelial growth factor A	Ovis aries	114-118
10466727-5	1999	Here we report that mice carrying a targeted disruption of the gene encoding NDST-2 are unable to synthesize sulphated heparin.	Heparin	119-126	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	77-83
10488968-5	1999	The DAO activity 30 min after the heparin injection significantly correlated with either the glycated albumin (GA) concentration or the plant sterol levels in all subjects.	Heparin	34-41	amine oxidase copper containing 1	Homo sapiens	4-7
10411593-0	1999	Association of heparin with basic fibroblast growth factor, epidermal growth factor, and constitutive nitric oxide synthase on healing of gastric ulcer in rats.	Heparin	15-22	fibroblast growth factor 2	Rattus norvegicus	28-58
10411593-0	1999	Association of heparin with basic fibroblast growth factor, epidermal growth factor, and constitutive nitric oxide synthase on healing of gastric ulcer in rats.	Heparin	15-22	epidermal growth factor like 1	Rattus norvegicus	60-83
10397725-11	1999	Cycloheximide, but not actinomycin-D, treatment inhibited the serum and bFGF/heparin-induced increase in TFPI activity in PASMC.	Heparin	77-84	tissue factor pathway inhibitor	Homo sapiens	105-109
10397733-6	1999	At the same time, the Tat basic sequence retrieves into a soluble form extracellular basic fibroblast growth factor (bFGF) bound to heparan sulfate proteoglycans by competing for heparin-binding sites.	Heparin	179-186	tyrosine aminotransferase	Homo sapiens	22-25
10413115-2	1999	However, it has been claimed that GSK-3beta can also phosphorylate the non-proline-directed KXGS motifs in the presence of heparin, including Ser262 in the repeat domain of tau, which could induce the detachment of tau from microtubules.	Heparin	123-130	glycogen synthase kinase 3 beta	Homo sapiens	34-43
10413115-5	1999	We also show that the non-proline-directed activity at KXGS motifs is not due to GSK-3beta itself, but to kinase contaminations in common GSK-3beta preparations from tissues which are activated upon addition of heparin.	Heparin	211-218	glycogen synthase kinase 3 beta	Homo sapiens	138-147
10354124-1	1999	Soluble heparin displaces the cytokine hepatocyte growth factor (HGF) from heparan sulphate proteoglycans on the cell surface and in the extracellular matrix into the circulation.	Heparin	8-15	hepatocyte growth factor	Homo sapiens	39-63
10354124-1	1999	Soluble heparin displaces the cytokine hepatocyte growth factor (HGF) from heparan sulphate proteoglycans on the cell surface and in the extracellular matrix into the circulation.	Heparin	8-15	hepatocyte growth factor	Homo sapiens	65-68
10354124-2	1999	We examined serum HGF elevation after heparin injections, and whether there is a difference between unfractionated heparin (UH) and low molecular weight heparin (LMWH) in their ability to increase serum HGF.	Heparin	115-122	hepatocyte growth factor	Homo sapiens	203-206
10354124-2	1999	We examined serum HGF elevation after heparin injections, and whether there is a difference between unfractionated heparin (UH) and low molecular weight heparin (LMWH) in their ability to increase serum HGF.	Heparin	115-122	hepatocyte growth factor	Homo sapiens	203-206
10354124-7	1999	When UH or LMWH were administered over a 5 d period, the increase in HGF, as well as the difference between treatments to induce HGF, remained stable throughout the treatment.	Heparin	5-7	hepatocyte growth factor	Homo sapiens	69-72
10354124-7	1999	When UH or LMWH were administered over a 5 d period, the increase in HGF, as well as the difference between treatments to induce HGF, remained stable throughout the treatment.	Heparin	5-7	hepatocyte growth factor	Homo sapiens	129-132
10354124-8	1999	In five patients treated with continuous intravenous heparin infusion HGF was increased throughout the treatment period of 5-7 d. In summary, the rise in bioactive HGF after heparin treatment was stable during continued treatment.	Heparin	53-60	hepatocyte growth factor	Homo sapiens	70-73
10354124-8	1999	In five patients treated with continuous intravenous heparin infusion HGF was increased throughout the treatment period of 5-7 d. In summary, the rise in bioactive HGF after heparin treatment was stable during continued treatment.	Heparin	53-60	hepatocyte growth factor	Homo sapiens	164-167
10354124-8	1999	In five patients treated with continuous intravenous heparin infusion HGF was increased throughout the treatment period of 5-7 d. In summary, the rise in bioactive HGF after heparin treatment was stable during continued treatment.	Heparin	174-181	hepatocyte growth factor	Homo sapiens	70-73
10354124-8	1999	In five patients treated with continuous intravenous heparin infusion HGF was increased throughout the treatment period of 5-7 d. In summary, the rise in bioactive HGF after heparin treatment was stable during continued treatment.	Heparin	174-181	hepatocyte growth factor	Homo sapiens	164-167
10503237-6	1999	This self-assembly occurs at low affinity, which can be greatly enhanced by the introduction of heparin, supporting a defined role for heparin in bFGF dimerization.	Heparin	96-103	fibroblast growth factor 2	Rattus norvegicus	146-150
10503237-6	1999	This self-assembly occurs at low affinity, which can be greatly enhanced by the introduction of heparin, supporting a defined role for heparin in bFGF dimerization.	Heparin	135-142	fibroblast growth factor 2	Rattus norvegicus	146-150
10201371-3	1999	Despite this improvement, heparin-induced thrombocytopaenia (HIT), related to an interaction with platelet factor 4 (PF4) and, to a lesser extent, haemorrhages, remain significant side effects of heparinotherapy.	Heparin	26-33	platelet factor 4	Homo sapiens	117-120
10235445-0	1999	Tissue factor reduction and tissue factor pathway inhibitor release after heparin administration.	Heparin	74-81	tissue factor pathway inhibitor	Homo sapiens	28-59
10050771-0	1999	Characterisation of the conformational and quaternary structure-dependent heparin-binding region of bovine seminal plasma protein PDC-109.	Heparin	74-81	seminal plasma protein PDC-109	Bos taurus	107-137
10050771-1	1999	PDC-109, the major heparin-binding protein of bull seminal plasma, binds to sperm choline lipids at ejaculation and modulates capacitation mediated by heparin.	Heparin	19-26	seminal plasma protein PDC-109	Bos taurus	0-7
10050771-2	1999	Affinity chromatography on heparin-Sepharose showed that polydisperse, but not monomeric, PDC-109 displayed heparin-binding capability.	Heparin	108-115	seminal plasma protein PDC-109	Bos taurus	90-97
10050771-3	1999	We sought to characterise the surface topology of the quaternary structure-dependent heparin-binding region of PDC-109 by comparing the arginine- and lysine-selective chemical modification patterns of the free and the heparin-bound protein.	Heparin	85-92	seminal plasma protein PDC-109	Bos taurus	111-118
10050771-3	1999	We sought to characterise the surface topology of the quaternary structure-dependent heparin-binding region of PDC-109 by comparing the arginine- and lysine-selective chemical modification patterns of the free and the heparin-bound protein.	Heparin	218-225	seminal plasma protein PDC-109	Bos taurus	111-118
10050771-9	1999	Our data suggest possible quaternary structure arrangements of PDC-109 molecules to form a heparin-binding oligomer.	Heparin	91-98	seminal plasma protein PDC-109	Bos taurus	63-70
9974412-7	1999	The TFPI in HMDM supernatants possessed heparin-binding affinity, suggesting potential interaction of TFPI with heparan sulfate proteoglycans.	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	4-8
10051750-4	1999	The HB-GAM-induced neurite outgrowth in thalamic neurons was inhibited by heparitinase, heparin, soluble N-syndecan and by an excess of soluble HB-GAM in the culture medium.	Heparin	88-95	pleiotrophin	Rattus norvegicus	4-10
10051750-7	1999	On the brain slices, the neurite outgrowth was significantly inhibited by heparitinase, heparin and soluble HB-GAM, thus displaying features of neurite outgrowth on matrix-bound HB-GAM.	Heparin	88-95	pleiotrophin	Rattus norvegicus	178-184
9916734-9	1999	The binding of recombinant p40 to heparin appears indistinguishable from that of the IL-12 heterodimer, implying that the heparin binding site is largely if not solely located in this subunit.	Heparin	34-41	interleukin 9	Homo sapiens	27-30
9916734-9	1999	The binding of recombinant p40 to heparin appears indistinguishable from that of the IL-12 heterodimer, implying that the heparin binding site is largely if not solely located in this subunit.	Heparin	122-129	interleukin 9	Homo sapiens	27-30
10092985-5	1999	Incremental integrated GLP-1 responses to oral carbohydrate post-heparin in lean (P &lt; 0.01) and obese (P &lt; 0.05) subjects were significantly lower than after acipimox.	Heparin	65-72	glucagon like peptide 1 receptor	Homo sapiens	23-28
9890310-7	1999	PPS and heparin also decreased MMP-9 (P &lt; 0.001) after treatment.	Heparin	8-15	matrix metallopeptidase 9	Mus musculus	31-36
9867821-9	1999	Furthermore, we have identified a 20-amino acid sequence in III5 (HBP/III5) which binds heparin and induces cell adhesion via CSPG exclusively.	Heparin	88-95	heme binding protein 1	Homo sapiens	66-74
10074643-5	1999	After 90 min simulated ECC, the heparin-coated systems showed significantly higher platelet count, lower platelet-factor 4 release, reduced contact activation (factor XIIa and kallikrein), and lower neutrophil elastase levels (p &lt; 0.05), compared to the noncoated oxygenator group.	Heparin	32-39	elastase, neutrophil expressed	Homo sapiens	199-218
9930556-6	1999	Heparin-induced immune thrombocytopenia (HIT) is associated with antibodies specific for complexes formed between heparin and platelet factor 4 (PF4), a basic protein of the chemokine family found normally in platelet alpha granules.	Heparin	0-7	platelet factor 4	Homo sapiens	145-148
9930557-2	1999	Following treatment with heparin, platelet factor 4 (PF4) is released into the circulation.	Heparin	25-32	platelet factor 4	Homo sapiens	53-56
9930557-3	1999	Heparin can bind to PF4 to form a reactive antigen on the platelet.	Heparin	0-7	platelet factor 4	Homo sapiens	20-23
9930557-4	1999	The formation of large heparin-PF4 (H-PF4) complexes that can react with HIT antibodies depends on the concentrations of heparin and PF4.	Heparin	23-30	platelet factor 4	Homo sapiens	31-34
9930557-4	1999	The formation of large heparin-PF4 (H-PF4) complexes that can react with HIT antibodies depends on the concentrations of heparin and PF4.	Heparin	23-30	platelet factor 4	Homo sapiens	38-41
9930557-4	1999	The formation of large heparin-PF4 (H-PF4) complexes that can react with HIT antibodies depends on the concentrations of heparin and PF4.	Heparin	23-30	platelet factor 4	Homo sapiens	38-41
10065895-7	1999	We showed that plasma-free TFPI levels after administration of heparin, which may indicate endothelial cell associated TFPI levels, increased in patients with angina pectoris compared with patients with chest pain syndrome.	Heparin	63-70	tissue factor pathway inhibitor	Homo sapiens	27-31
10065895-7	1999	We showed that plasma-free TFPI levels after administration of heparin, which may indicate endothelial cell associated TFPI levels, increased in patients with angina pectoris compared with patients with chest pain syndrome.	Heparin	63-70	tissue factor pathway inhibitor	Homo sapiens	119-123
9930483-8	1998	Activated protein C-protein C inhibitor levels showed a peak after heparinization in accordance with the accelerating effect of heparin on the complex formation but decreased thereafter.	Heparin	67-74	serpin family A member 5	Homo sapiens	20-39
9813026-10	1998	The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin.	Heparin	78-85	serpin family D member 1	Homo sapiens	57-61
9787161-9	1998	Thus our studies suggest that whereas the C-terminal lysine residues of PF4 are important for heparin binding, they do not comprise a critical antigenic site for most HIT antibodies.	Heparin	94-101	platelet factor 4	Homo sapiens	72-75
9787161-10	1998	Rather, we propose that maintaining a region near the third cysteine residue of PF4, distal from the proposed heparin-binding domain, is required to form the epitope recognized by many HIT antibodies.	Heparin	110-117	platelet factor 4	Homo sapiens	80-83
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	89-96	serpin family D member 1	Homo sapiens	0-19
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	89-96	serpin family D member 1	Homo sapiens	21-25
9790687-3	1998	Thermodynamic analysis using isothermal titration calorimetry confirmed heparin binding to BNP with a micromolar Kd.	Heparin	72-79	natriuretic peptide B	Homo sapiens	91-94
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	82-89	natriuretic peptide B	Homo sapiens	75-78
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	82-89	natriuretic peptide B	Homo sapiens	162-165
9778325-7	1998	For the entire group, 30000 IU SNAC and heparin elevated TFPI from 74.9+/-7.6 to 254.2+/-12.3 mg/mL (P&lt;0.001) 1 hour after dosing (P&lt;0.001).	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	57-61
9831891-0	1998	Inhibition of serum and transforming growth factor beta (TGF-beta1)-induced DNA synthesis in confluent airway smooth muscle by heparin.	Heparin	127-134	transforming growth factor beta 1	Bos taurus	57-66
9831891-17	1998	Heparin inhibited serum and TGF-beta1-induced DNA synthesis in confluent ASMC (55%), consistent with our previous observation of inhibition of division in sparsely populated ASMC (Kilfeather et al., 1995a).	Heparin	0-7	transforming growth factor beta 1	Bos taurus	28-37
9831891-20	1998	An anti-mitogenic effect of heparin was also observed against responses to combined exposure to TGF-beta1 and EGF.	Heparin	28-35	transforming growth factor beta 1	Bos taurus	96-105
9622039-7	1998	TFPI increased 2.3 times following dialysis and such an increase was directly correlated with post-dialysis plasma heparin concentration (r=0.571, p=0.0002) and inversely correlated with post-dialysis triglyceride variation (r=0.407, p=0.005).	Heparin	115-122	tissue factor pathway inhibitor	Homo sapiens	0-4
9622042-0	1998	Heparin-releasable endothelial cell-associated tissue factor pathway inhibitor (TFPI) is increased in the coronary circulation after coronary spasm in patients with coronary spastic angina.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	47-78
9622042-0	1998	Heparin-releasable endothelial cell-associated tissue factor pathway inhibitor (TFPI) is increased in the coronary circulation after coronary spasm in patients with coronary spastic angina.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	80-84
9622042-4	1998	Heparin-releasable TFPI level in the coronary spastic angina group significantly increased in the coronary sinus (1 22+/-46 to 147+/-63, p&lt;0.001) after the ischemic event but not in the aortic root (113+/-44 to 121+/-58).	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	19-23
9622042-6	1998	The coronary sinus-arterial difference in the amount of the heparin-releasable TFPI significantly increased after the ischemic event only in the coronary spastic angina group (10+/-18 to 26+/-18, p&lt;0.002).	Heparin	60-67	tissue factor pathway inhibitor	Homo sapiens	79-83
9622042-7	1998	Our result suggested that heparin-releasable TFPI is increased in the coronary circulation after coronary spasm.	Heparin	26-33	tissue factor pathway inhibitor	Homo sapiens	45-49
9473690-1	1998	Hepatocyte growth factor (HGF/SF), is a heparin-binding polypeptide which stimulates DNA synthesis in a variety of cell types and also promotes cell migration and morphogenesis.	Heparin	40-47	hepatocyte growth factor	Homo sapiens	26-32
9443108-7	1998	The gp120 and gp160 specifically recognize the C-terminal heparin-binding domain of Fn (Fn-CTHBD) with a calculated KD of 2.8 x 10(-7) M for gp160.	Heparin	58-65	glutamyl aminopeptidase	Homo sapiens	14-19
9443108-7	1998	The gp120 and gp160 specifically recognize the C-terminal heparin-binding domain of Fn (Fn-CTHBD) with a calculated KD of 2.8 x 10(-7) M for gp160.	Heparin	58-65	glutamyl aminopeptidase	Homo sapiens	141-146
9443108-8	1998	Binding of gp160 to Fn-CTHBD is a saturable and specific process that is blocked by antibodies to Fn-CTHBD and by heparin and is inhibited to a minor extent by heparan sulfate and dextran sulfate.	Heparin	114-121	glutamyl aminopeptidase	Homo sapiens	11-16
9931839-0	1998	[Improved postoperative prevention of thrombosis in trauma surgery by dose adjusted low molecular weight heparin based on TAT and D-dimer values].	Heparin	105-112	tyrosine aminotransferase	Homo sapiens	122-125
16793681-5	1998	The formation of complexes between PF4 and heparin or other glycosaminoglycans, leading in some circumstances to the generation of antigenic structures reactive with HIT antibodies, is analysed.	Heparin	43-50	platelet factor 4	Homo sapiens	35-38
9359845-4	1997	Natural hLF lacking the first two N-terminal amino acids (Gly1-Arg2) showed reactivities of one-half, two-thirds, one-third and one-third towards heparin, lipid A, hLZ and DNA respectively compared with N-terminally intact hLF.	Heparin	146-153	threonine aldolase 1, pseudogene	Homo sapiens	58-62
9360988-1	1997	The CD11c/CD18 integrin binds lipopolysaccharide, fibrinogen, and heparin, and mediates leukocyte adhesion, spreading, and migration.	Heparin	66-73	integrin subunit alpha X	Homo sapiens	4-9
9345040-7	1997	The binding of exogenously added 125I-TFPI increased linearly to HUVEC over the concentration range of 0 to 32 nmol/L without saturation, the binding was not affected by up to a thousand-fold molar excess of unlabeled TFPI, and heparin inhibited the binding dose dependently.	Heparin	228-235	tissue factor pathway inhibitor	Homo sapiens	38-42
9375738-1	1997	Heparin-induced thrombocytopenia (HIT) is frequently associated with antibodies (Abs) to heparin-PF4 complexes (H-PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	97-100
9375738-1	1997	Heparin-induced thrombocytopenia (HIT) is frequently associated with antibodies (Abs) to heparin-PF4 complexes (H-PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	114-117
9362347-3	1997	By immunoblotting, using a monoclonal antibody raised against the HGF alpha-subunit, the bile HGF, which was purified on a Heparin-Sepharose column, showed a band of the same size as the recombinant HGF alpha-subunit (69 kd).	Heparin	123-130	hepatocyte growth factor	Homo sapiens	66-69
9362347-3	1997	By immunoblotting, using a monoclonal antibody raised against the HGF alpha-subunit, the bile HGF, which was purified on a Heparin-Sepharose column, showed a band of the same size as the recombinant HGF alpha-subunit (69 kd).	Heparin	123-130	hepatocyte growth factor	Homo sapiens	94-97
9362347-3	1997	By immunoblotting, using a monoclonal antibody raised against the HGF alpha-subunit, the bile HGF, which was purified on a Heparin-Sepharose column, showed a band of the same size as the recombinant HGF alpha-subunit (69 kd).	Heparin	123-130	hepatocyte growth factor	Homo sapiens	94-97
9334164-6	1997	The interaction of PDGFBB with TSP1 was weakened by increasing salt concentration and essentially ablated at 0.65 ionic strength; it was inhibited by heparin with a half-maximal effect at 20 i.u./ml, implying that the binding was mediated largely by ionic interactions.	Heparin	150-157	thrombospondin 1	Rattus norvegicus	31-35
9346305-0	1997	Heparin binding of protein-C inhibitor--analysis of the effect of heparin on the interaction of protein-C inhibitor with tissue kallikrein.	Heparin	0-7	serpin family A member 5	Homo sapiens	19-38
9346305-0	1997	Heparin binding of protein-C inhibitor--analysis of the effect of heparin on the interaction of protein-C inhibitor with tissue kallikrein.	Heparin	0-7	serpin family A member 5	Homo sapiens	96-115
9346305-0	1997	Heparin binding of protein-C inhibitor--analysis of the effect of heparin on the interaction of protein-C inhibitor with tissue kallikrein.	Heparin	66-73	serpin family A member 5	Homo sapiens	96-115
9346305-2	1997	Heparin stimulates most PCI/protease reactions, but interferes with the inhibition of tissue kallikrein by PCI by a hitherto unknown mechanism.	Heparin	0-7	serpin family A member 5	Homo sapiens	24-27
9346305-2	1997	Heparin stimulates most PCI/protease reactions, but interferes with the inhibition of tissue kallikrein by PCI by a hitherto unknown mechanism.	Heparin	0-7	serpin family A member 5	Homo sapiens	107-110
9346305-3	1997	In this study we analyzed the inhibitory effect of heparin on the tissue-kallikrein-PCI interaction.	Heparin	51-58	serpin family A member 5	Homo sapiens	84-87
9346305-6	1997	However, heparin-bound PCI, which was able to form complexes with 125I-urokinase, did not form complexes with 125I-tissue-kallikrein.	Heparin	9-16	serpin family A member 5	Homo sapiens	23-26
9346305-7	1997	This suggests that the inhibitory effect of heparin is either based on the neutralization of positive charges in the PCI molecule, which might be required for the interaction of PCI with the acidic protease tissue kallikrein, or on a change in reactivity of PCI upon heparin binding, making heparin-bound PCI no longer a tissue-kallikrein inhibitor.	Heparin	44-51	serpin family A member 5	Homo sapiens	117-120
9346305-7	1997	This suggests that the inhibitory effect of heparin is either based on the neutralization of positive charges in the PCI molecule, which might be required for the interaction of PCI with the acidic protease tissue kallikrein, or on a change in reactivity of PCI upon heparin binding, making heparin-bound PCI no longer a tissue-kallikrein inhibitor.	Heparin	44-51	serpin family A member 5	Homo sapiens	178-181
9346305-7	1997	This suggests that the inhibitory effect of heparin is either based on the neutralization of positive charges in the PCI molecule, which might be required for the interaction of PCI with the acidic protease tissue kallikrein, or on a change in reactivity of PCI upon heparin binding, making heparin-bound PCI no longer a tissue-kallikrein inhibitor.	Heparin	44-51	serpin family A member 5	Homo sapiens	178-181
9346305-7	1997	This suggests that the inhibitory effect of heparin is either based on the neutralization of positive charges in the PCI molecule, which might be required for the interaction of PCI with the acidic protease tissue kallikrein, or on a change in reactivity of PCI upon heparin binding, making heparin-bound PCI no longer a tissue-kallikrein inhibitor.	Heparin	44-51	serpin family A member 5	Homo sapiens	178-181
9346305-7	1997	This suggests that the inhibitory effect of heparin is either based on the neutralization of positive charges in the PCI molecule, which might be required for the interaction of PCI with the acidic protease tissue kallikrein, or on a change in reactivity of PCI upon heparin binding, making heparin-bound PCI no longer a tissue-kallikrein inhibitor.	Heparin	267-274	serpin family A member 5	Homo sapiens	117-120
9346305-7	1997	This suggests that the inhibitory effect of heparin is either based on the neutralization of positive charges in the PCI molecule, which might be required for the interaction of PCI with the acidic protease tissue kallikrein, or on a change in reactivity of PCI upon heparin binding, making heparin-bound PCI no longer a tissue-kallikrein inhibitor.	Heparin	267-274	serpin family A member 5	Homo sapiens	117-120
9341987-1	1997	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder caused by heparin-dependent IgG (HIT-IgG) that recognizes a complex of heparin and platelet factor 4 (PF4), leading to platelet activation via the platelet Fc gammaIIa receptors (Fc gammaRIIa).	Heparin	0-7	platelet factor 4	Homo sapiens	169-172
9298697-3	1997	We have demonstrated that heparin binds to recombinant gp120, the envelope glycoprotein of HIV-1, at a site termed the V3 loop, or principle neutralizing domain, which consists of a disulphide-bridged loop of 32-35 amino acids particularly enriched with basic residues.	Heparin	26-33	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	55-60
9244238-8	1997	In contrast, luminal stenosis was only 11+/-12% and 6+/-3% in pigs given high and low doses, respectively, of rTFPI for 24 hours compared with 46+/-22% in pigs given heparin for 24 hours and 40+/-19% in those given both heparin and aspirin (P&lt;.0002).	Heparin	220-227	tissue factor pathway inhibitor	Rattus norvegicus	110-115
9212969-7	1997	These data demonstrated that in pediatric CPB, heparin-coated CPB circuits reduced the activation of complements and the production of PMN elastase and IL-6, suggesting the superior biocompatibility of the heparin-coated circuits.	Heparin	47-54	elastase, neutrophil expressed	Homo sapiens	135-147
9733717-1	1998	Platelets express a single class of Fcgamma receptor (FcgammaRIIA), which is involved in heparin-associated thrombocytopenia and possibly in inflammation.	Heparin	89-96	Fc gamma receptor IIa	Homo sapiens	54-65
9797082-2	1998	The patient had heparin-PF4 antibodies and the heparin-induced platelet activation (HIPA) test was positive, but platelet counts remained normal.	Heparin	16-23	platelet factor 4	Homo sapiens	24-27
9716155-0	1998	Heparin-induced thrombocytopenia: IgG binding to PF4-heparin complexes in the fluid phase and cross-reactivity with low molecular weight heparin and heparinoid.	Heparin	0-7	platelet factor 4	Homo sapiens	49-52
9716155-0	1998	Heparin-induced thrombocytopenia: IgG binding to PF4-heparin complexes in the fluid phase and cross-reactivity with low molecular weight heparin and heparinoid.	Heparin	53-60	platelet factor 4	Homo sapiens	49-52
9716155-3	1998	Our fluid phase assay produces consistently low background and can detect low levels of anti-PF4-heparin.	Heparin	97-104	platelet factor 4	Homo sapiens	93-96
9682007-0	1998	Heparin, but not other proteoglycans potentiates the mitogenic effects of FGF-2 on mesencephalic precursor cells.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	74-79
9682007-3	1998	Our results show the mitogenic effects of FGF-2 could be potentiated by heparin but not the other four proteoglycans.	Heparin	72-79	fibroblast growth factor 2	Rattus norvegicus	42-47
9682007-7	1998	However, there was a significant decrease in the number of astrocytes developing from cultures grown in FGF-2 + heparin when compared to FGF-2 alone.	Heparin	112-119	fibroblast growth factor 2	Rattus norvegicus	137-142
9682007-9	1998	However, there was a synergistic effect of combining EGF + FGF-2, which could be potentiated by heparin.	Heparin	96-103	fibroblast growth factor 2	Rattus norvegicus	59-64
9682007-10	1998	We conclude that heparin, but not other closely related proteoglycans, is vital for the growth of FGF-2-responsive mesencephalic neural precursors.	Heparin	17-24	fibroblast growth factor 2	Rattus norvegicus	98-103
15992020-5	1998	The inhibitory action of TFPI is accelerated by heparin.	Heparin	48-55	tissue factor pathway inhibitor	Homo sapiens	25-29
15992020-6	1998	Heparin, as well as low molecular weight heparin (LMWH) derivatives, release TFPI from the vascular endothelium, an effect which seems to contribute mainly to the antithrombotic effectiveness of these drugs.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	77-81
15992020-6	1998	Heparin, as well as low molecular weight heparin (LMWH) derivatives, release TFPI from the vascular endothelium, an effect which seems to contribute mainly to the antithrombotic effectiveness of these drugs.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	77-81
9202142-4	1997	Circular dichroism and binding experiments have shown that the designed leucine zipper peptide adopts a stable helical conformation and shows significant PF4-like heparin binding activity.	Heparin	163-170	platelet factor 4	Homo sapiens	154-157
9202142-5	1997	These results strongly suggest that the lysine residues play an important role in the binding of PF4 to heparin.	Heparin	104-111	platelet factor 4	Homo sapiens	97-100
15304392-1	2005	Heparin-induced thrombocytopenia and thrombosis (HITT) is a severe complication of heparin therapy caused by antibodies to complexes between unfractionated heparin (UFH) and platelet factor 4 (PF4) that form over a narrow molar range of reactants and initiate antibody-induced platelet activation.	Heparin	83-90	platelet factor 4	Homo sapiens	193-196
15304392-2	2005	We observed that UFH and tetrameric PF4 formed ultralarge (&gt; 670 kDa) complexes (ULCs) only over a narrow molar range with an optimal ratio of PF4 to heparin of approximately 1:1.	Heparin	17-20	platelet factor 4	Homo sapiens	146-149
9632653-6	1998	Accordingly, heparin binds immobilized GST-Tat and GST-TatR49/52/53/55/56/57A with a dissociation constant equal to 0.3 and 1.0 microM, respectively.	Heparin	13-20	tyrosine aminotransferase	Homo sapiens	43-46
9310184-8	1997	Heparin, mostly at 10 micrograms/mL (which caused an increase of 9.64 nmol reduced cytochrome c/mg protein per min) significantly changed both the nature and concentration of the radicals which were formed.	Heparin	0-7	LOC104968582	Bos taurus	83-95
9632653-7	1998	Also, the synthetic basic domain Tat-(41-60) competes with GST-Tat for heparin binding.	Heparin	71-78	tyrosine aminotransferase	Homo sapiens	33-36
15304392-2	2005	We observed that UFH and tetrameric PF4 formed ultralarge (&gt; 670 kDa) complexes (ULCs) only over a narrow molar range with an optimal ratio of PF4 to heparin of approximately 1:1.	Heparin	153-160	platelet factor 4	Homo sapiens	36-39
9632653-7	1998	Also, the synthetic basic domain Tat-(41-60) competes with GST-Tat for heparin binding.	Heparin	71-78	tyrosine aminotransferase	Homo sapiens	63-66
15304392-4	2005	ULCs formed inefficiently when PF4 was incubated with low-molecular-weight heparin, and none formed with the pentasaccharide fondaparinux sodium.	Heparin	75-82	platelet factor 4	Homo sapiens	31-34
9632653-10	1998	Although heparin was an antagonist more potent than suramin, modifications of the backbone structure in selected suramin derivatives originated Tat antagonists whose potency was close to that shown by heparin.	Heparin	201-208	tyrosine aminotransferase	Homo sapiens	144-147
16114264-8	2005	The clusterisation of AChE depends upon ColQ through three sites of interactions: two different heparin binding domains in the collagen domain interact with heparan sulfate proteoglycan particularly the perlecan and the C-terminal non collagenic domain interacts with MuSK, the tyrosine kinase receptor organiser of the neuromuscular junction.	Heparin	96-103	collagen like tail subunit of asymmetric acetylcholinesterase	Homo sapiens	40-44
9603953-6	1998	Both sPLA2s-IIA and -V, but not sPLA2-IIC, were heparin-binding PLA2s that exhibited significant affinity for cell-surface proteoglycans, and site-directed mutations in residues responsible for their membrane association or catalytic activity markedly reduced their ability to release AA from activated cells.	Heparin	48-55	phospholipase A2 group IID	Homo sapiens	5-11
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	150-157	tissue factor pathway inhibitor	Homo sapiens	0-31
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	150-157	tissue factor pathway inhibitor	Homo sapiens	33-37
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	237-244	tissue factor pathway inhibitor	Homo sapiens	0-31
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	237-244	tissue factor pathway inhibitor	Homo sapiens	33-37
9151897-4	1997	Recombinant MDC was expressed in Chinese hamster ovary cells and purified by heparin-Sepharose chromatography.	Heparin	77-84	C-C motif chemokine ligand 22	Homo sapiens	12-15
9092516-12	1997	Light scattering measurements on Ang-heparin mixtures suggest that 1 heparin chain (mass of 16.5 kDa) can accommodate approximately 9 Ang molecules.	Heparin	37-44	angiogenin	Homo sapiens	134-137
9092516-12	1997	Light scattering measurements on Ang-heparin mixtures suggest that 1 heparin chain (mass of 16.5 kDa) can accommodate approximately 9 Ang molecules.	Heparin	69-76	angiogenin	Homo sapiens	33-36
9092516-12	1997	Light scattering measurements on Ang-heparin mixtures suggest that 1 heparin chain (mass of 16.5 kDa) can accommodate approximately 9 Ang molecules.	Heparin	69-76	angiogenin	Homo sapiens	134-137
9092516-13	1997	The minimum size required for a heparin fragment to effectively inhibit HT-29 cell adhesion to Ang was determined to be 6 disaccharide units.	Heparin	32-39	angiogenin	Homo sapiens	95-98
9083079-7	1997	1) Heparin potentiated the multimer formation by MK.	Heparin	3-10	midkine	Bos taurus	49-51
9593692-4	1998	While heparin bound SLPI tightly, the highest affinity heparin chains unexpectedly contained a lower level of sulfation than more weakly interacting chains.	Heparin	6-13	antileukoproteinase	Ovis aries	20-24
9593692-7	1998	Isothermal titration calorimetry was used to determine the thermodynamics of SLPI interaction with a low molecular weight heparin, an undersulfated decasaccharide and a tetrasaccharide.	Heparin	122-129	antileukoproteinase	Ovis aries	77-81
15767980-7	2004	RESULTS: Heparin clearly had the highest degree of TAFI inhibition with an IC50 of 0.10 U, which correlates with its coagulation profile.	Heparin	9-16	carboxypeptidase B2	Homo sapiens	51-55
9593692-8	1998	The studies showed 12-14 saccharide units, corresponding to molecular weight of approximately 4,800, were required for a 1:1 (SLPI:heparin) binding stoichiometry.	Heparin	131-138	antileukoproteinase	Ovis aries	126-130
9593692-10	1998	The in vitro assessment of heparin and the decasaccharide and tetrasaccharide using stopped-flow kinetics suggested that heparin was the optimal choice to study SLPI-based in vivo protease inhibition.	Heparin	121-128	antileukoproteinase	Ovis aries	161-165
9593692-13	1998	Heparin also increased the therapeutic activity of SLPI against antigen-induced airway hyperresponsiveness.	Heparin	0-7	antileukoproteinase	Ovis aries	51-55
9096801-7	1997	In contrast, up-regulation of other surface molecules (CD14 and CD16) seems to be independent of heparin coating and complement activation and, thus, might be regulated by other mechanisms.	Heparin	97-104	CD14 molecule	Homo sapiens	55-59
15627717-5	2004	RESULTS: TAFI concentration, activity and markers of ongoing coagulation, i.e. prothrombin fragments 1 + 2 and thrombin-antithrombin complexes, were significantly higher in patients anticoagulated with unfractionated heparin when compared to both enoxaparin and dalteparin groups.	Heparin	217-224	carboxypeptidase B2	Homo sapiens	9-13
9105676-4	1997	Previously, we have demonstrated that N1E-115 cells possess two distinct subpopulations of AT2 receptors, defined as peak I and peak III receptors, that can be separated by heparin-sepharose chromatography.	Heparin	173-180	angiotensin II receptor type 2	Homo sapiens	91-94
9565561-5	1998	We found that the binding of a bivalent PECAM-1/IgG chimeric protein or multivalent PECAM-1-containing proteoliposomes to multiple different cell lines was 1) strictly dependent upon cell surface expression of PECAM-1 and 2) unaffected by the presence of excess heparin or heparan sulfate.	Heparin	262-269	platelet and endothelial cell adhesion molecule 1	Homo sapiens	40-47
9565561-5	1998	We found that the binding of a bivalent PECAM-1/IgG chimeric protein or multivalent PECAM-1-containing proteoliposomes to multiple different cell lines was 1) strictly dependent upon cell surface expression of PECAM-1 and 2) unaffected by the presence of excess heparin or heparan sulfate.	Heparin	262-269	platelet and endothelial cell adhesion molecule 1	Homo sapiens	84-91
9565561-8	1998	Together, these data suggest that the mechanism by which heparin is able to affect PECAM-1-dependent cell-cell adhesion is indirect and occurs via inhibition of events that occur downstream from PECAM-1 engagement.	Heparin	57-64	platelet and endothelial cell adhesion molecule 1	Homo sapiens	83-90
9565561-8	1998	Together, these data suggest that the mechanism by which heparin is able to affect PECAM-1-dependent cell-cell adhesion is indirect and occurs via inhibition of events that occur downstream from PECAM-1 engagement.	Heparin	57-64	platelet and endothelial cell adhesion molecule 1	Homo sapiens	195-202
15627717-7	2004	CONCLUSIONS: Our results suggest that low-molecular-weight heparins influence TAFI and other hemostatic parameters in hemodialyzed patients to a lesser degree than unfractionated heparin.	Heparin	59-67	carboxypeptidase B2	Homo sapiens	78-82
9227267-7	1997	The heparin-binding characteristics of HGF would result in increased binding to glycosaminoglycans and other heparin-like matrix components and, therefore, increased growth factor availability to the cognate recptor.	Heparin	4-11	hepatocyte growth factor	Homo sapiens	39-42
15627717-7	2004	CONCLUSIONS: Our results suggest that low-molecular-weight heparins influence TAFI and other hemostatic parameters in hemodialyzed patients to a lesser degree than unfractionated heparin.	Heparin	59-66	carboxypeptidase B2	Homo sapiens	78-82
15627717-8	2004	Increased TAFI is possibly due to thrombin appearance during hemodialysis with unfractionated heparin.	Heparin	94-101	carboxypeptidase B2	Homo sapiens	10-14
9347871-0	1997	Heparin-induced thrombocytopenia as an autoimmune disease--idiotypic evidence for the role of anti-heparin/PF4 autoantibodies.	Heparin	0-7	platelet factor 4	Homo sapiens	107-110
15570242-2	2004	Heparin treatment mobilizes TFPI into the circulation and contributes to the anticoagulant effects of heparins.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	28-32
9079643-0	1997	Heparin facilitates dissociation of complexes between thrombin and a reactive site mutant (L444R) of heparin cofactor II.	Heparin	0-7	serpin family D member 1	Homo sapiens	101-120
15570242-3	2004	Previous studies have demonstrated a selective depletion of intravascular TFPI by unfractionated heparin (UFH) but not by low-molecular-weight heparin (LMWH).	Heparin	97-104	tissue factor pathway inhibitor	Homo sapiens	74-78
9137511-3	1997	RESULTS: Serum HGF levels rapidly increased to six-fold higher levels immediately after heparin-injection even before embolization.	Heparin	88-95	hepatocyte growth factor	Homo sapiens	15-18
9137511-6	1997	The first increase may have been due to the injection of heparin which releases HGF from the cell-surface and extracellular matrix.	Heparin	57-64	hepatocyte growth factor	Homo sapiens	80-83
9131716-0	1997	Effects of heparin coating on the expression of CD11b, CD11c and CD62L by leucocytes in extracorporeal circulation in vitro.	Heparin	11-18	integrin subunit alpha X	Homo sapiens	55-60
9131716-6	1997	Heparin coating reduced the increase in CD11b and CD11c on granulocytes (p &lt; 0.02 at 2 h), but the delayed increase in CD11c on monocytes and the delayed downregulation of CD62L on granulocytes and monocytes did not reach statistical significance.	Heparin	0-7	integrin subunit alpha X	Homo sapiens	50-55
9089978-11	1997	This has led to the development of the PF4/ heparin EIA assay.	Heparin	44-51	platelet factor 4	Homo sapiens	39-42
15570242-3	2004	Previous studies have demonstrated a selective depletion of intravascular TFPI by unfractionated heparin (UFH) but not by low-molecular-weight heparin (LMWH).	Heparin	106-109	tissue factor pathway inhibitor	Homo sapiens	74-78
15570242-4	2004	In this study we sought to investigate the time- and dose-dependent relationships between release of TFPI and lipoprotein lipase (LPL) in respons to UFH and LMWH and to investigate whether the selective depletion of TFPI by UFH but not by LMWH is related to differential urinary excretion of TFPI.	Heparin	149-152	tissue factor pathway inhibitor	Homo sapiens	101-105
9047345-5	1997	Also the putative heparin binding sites and "hinge" regions are highly homologous in mouse and hPCI.	Heparin	18-25	serpin family A member 5	Homo sapiens	95-99
15292235-4	2004	Injecting hHLmt-expressing virus into C57BL/6J mice (1.8 x 10(10) virus particles/mouse) resulted in a 3-fold increase in pre-heparin HL activity, whereas infection with an identical dose of hHL virus did not change pre-heparin HL activity.	Heparin	126-133	hes family bHLH transcription factor 1	Homo sapiens	11-13
9089410-0	1997	Importance of 2-O-sulfate groups of uronate residues in heparin for activation of FGF-1 and FGF-2.	Heparin	56-63	fibroblast growth factor 2	Mus musculus	92-97
9089410-5	1997	These results suggest that a high content of 2-O-sulfate groups in uronate residues of heparin is required for activation of both FGF-1 and FGF-2.	Heparin	87-94	fibroblast growth factor 2	Mus musculus	140-145
15292235-4	2004	Injecting hHLmt-expressing virus into C57BL/6J mice (1.8 x 10(10) virus particles/mouse) resulted in a 3-fold increase in pre-heparin HL activity, whereas infection with an identical dose of hHL virus did not change pre-heparin HL activity.	Heparin	126-133	hes family bHLH transcription factor 1	Homo sapiens	10-13
8995662-4	1997	The recombinant soluble ectodomain of HSV-2 gB (gB2) but not the soluble ectodomain of HSV-2 gD bound readily to biosensor surfaces coated with heparin.	Heparin	144-151	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	48-51
15292235-5	2004	In hHLmt-expressing mice, the concentration of total cholesterol and phospholipids was inversely related to the hHL activity in pre-heparin plasma in a dose- and time-dependent manner, and the decrease was mainly attributable to high density lipoproteins (HDL) cholesterol and HDL phospholipids.	Heparin	132-139	hes family bHLH transcription factor 1	Homo sapiens	3-6
8995662-6	1997	gB2 binding to the heparin surface was competitively inhibited by low concentrations of heparin (50% effective dose [ED50] = 0.08 microg/ml).	Heparin	19-26	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	0-3
8995662-6	1997	gB2 binding to the heparin surface was competitively inhibited by low concentrations of heparin (50% effective dose [ED50] = 0.08 microg/ml).	Heparin	88-95	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	0-3
15203110-5	2004	Heparin, heparan sulfate and dermatan sulfate, at various HARP to glycosaminoglycan ratios, partially protect HARP from plasmin degradation.	Heparin	0-7	plasminogen	Homo sapiens	120-127
8995662-8	1997	Our biosensor analyses showed that both heparan sulfate and dermatan sulfate inhibited gB2 binding (ED50 = 1 to 5 microg/ml), indicating that gB2 interacts with both heparin-like and dermatan sulfate glycosaminoglycans.	Heparin	166-173	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	87-90
8995662-8	1997	Our biosensor analyses showed that both heparan sulfate and dermatan sulfate inhibited gB2 binding (ED50 = 1 to 5 microg/ml), indicating that gB2 interacts with both heparin-like and dermatan sulfate glycosaminoglycans.	Heparin	166-173	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	142-145
8995662-9	1997	Chondroitin sulfate A, in contrast, inhibited gB2 binding to heparin only at high levels (ED50 = 65 microg/ml).	Heparin	61-68	gamma-aminobutyric acid type B receptor subunit 2	Homo sapiens	46-49
15262417-8	2004	Subsequently, the ability of aminoBP-heparin conjugates to enhance the mineral affinity of basic fibroblast growth factor (bFGF) and bone morphogenetic protein-2 (BMP-2) was explored.	Heparin	37-44	bone morphogenetic protein 2	Homo sapiens	133-161
9238439-1	1997	Heparin-platelet factor 4 (H-PF4) complexes are the target for heparin-dependent antibodies present in most of heparin-induced thrombocytopenias (HIT).	Heparin	63-70	platelet factor 4	Homo sapiens	29-32
9238439-2	1997	The highest reactivity is obtained with 27 IU of heparin per mg of PF4.	Heparin	49-56	platelet factor 4	Homo sapiens	67-70
15262417-8	2004	Subsequently, the ability of aminoBP-heparin conjugates to enhance the mineral affinity of basic fibroblast growth factor (bFGF) and bone morphogenetic protein-2 (BMP-2) was explored.	Heparin	37-44	bone morphogenetic protein 2	Homo sapiens	163-168
15291808-3	2004	However, other studies have suggested that PF-4 acts via heparin-binding independent interactions.	Heparin	57-64	platelet factor 4	Homo sapiens	43-47
8993240-5	1997	Heparin coating, however, reduced maximum values of C3b/c (446 +/- 212 nmol/L versus 632 +/- 264 nmol/L with uncoated ECC; p = 0.0037) and maximum C4b/c values (92 +/- 48 nmol/L versus 172 +/- 148 nmol/L with uncoated ECC; p = 0.0069).	Heparin	0-7	complement C4B (Chido blood group)	Homo sapiens	147-150
15291808-4	2004	Here, we compared the effects of PF-4 on the signalling events involved in the proliferation induced by VEGF(165), which binds heparin, and by VEGF(121), which does not.	Heparin	127-134	platelet factor 4	Homo sapiens	33-37
27406868-8	1997	In contrast to the lack of any difference between groups with respect to TFPI, the level of heparin-releasable PF4 (HR-PF4) was significantly higher in ET and PV-H patients compared to PV-N patients or controls.	Heparin	92-99	platelet factor 4	Homo sapiens	111-114
15247982-2	2004	Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin.	Heparin	128-135	serpin family D member 1	Homo sapiens	0-19
27406868-8	1997	In contrast to the lack of any difference between groups with respect to TFPI, the level of heparin-releasable PF4 (HR-PF4) was significantly higher in ET and PV-H patients compared to PV-N patients or controls.	Heparin	92-99	platelet factor 4	Homo sapiens	119-122
9156410-0	1997	Tissue factor pathway inhibitor (TFPI) antigen plasma level in patients with interstitial lung disease before and after heparin administration.	Heparin	120-127	tissue factor pathway inhibitor	Homo sapiens	0-31
9156410-0	1997	Tissue factor pathway inhibitor (TFPI) antigen plasma level in patients with interstitial lung disease before and after heparin administration.	Heparin	120-127	tissue factor pathway inhibitor	Homo sapiens	33-37
9156410-6	1997	Five minutes after heparin administration the rise in TFPI was lower, although not statistically significant, in all sarcoidosis stages than in controls.	Heparin	19-26	tissue factor pathway inhibitor	Homo sapiens	54-58
9156410-8	1997	In sarcoidosis the elevated TFPI and the lower capacity by endothelial cells to release TFPI after heparin may represent a compensatory mechanism to prevent blood clotting and/or the endothelial cell dysfunction of the microvasculature in this condition.	Heparin	99-106	tissue factor pathway inhibitor	Homo sapiens	88-92
8980183-6	1996	A chemotactic factor was purified from the heparin-unbound fraction of Peak 2 by anion exchange and hydrophobic chromatography, and was named "fibroblast-derived motility factor (FDMF)".	Heparin	43-50	PEAK1 related, kinase-activating pseudokinase 1	Homo sapiens	71-77
15247982-2	2004	Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin.	Heparin	128-135	serpin family D member 1	Homo sapiens	21-25
9025066-1	1996	We have manipulated the chick limb bud by dorsoventrally inverting the ectoderm, by grafting the AER to the dorsal or ventral ectoderm and by insertion of an FGF-4 soaked heparin bead into the mesoderm.	Heparin	171-178	fibroblast growth factor 4	Gallus gallus	158-163
8972021-0	1996	Heparin stimulation of the inhibition of activated protein C and other enzymes by human protein C inhibitor--influence of the molecular weightof heparin and ionic strength.	Heparin	0-7	APC regulator of WNT signaling pathway	Homo sapiens	41-60
15247982-3	2004	The interaction of heparin with HCII has been the focus of many studies using affinity chromatography and fluorescence spectroscopy.	Heparin	19-26	serpin family D member 1	Homo sapiens	32-36
8972021-0	1996	Heparin stimulation of the inhibition of activated protein C and other enzymes by human protein C inhibitor--influence of the molecular weightof heparin and ionic strength.	Heparin	0-7	serpin family A member 5	Homo sapiens	88-107
8972021-0	1996	Heparin stimulation of the inhibition of activated protein C and other enzymes by human protein C inhibitor--influence of the molecular weightof heparin and ionic strength.	Heparin	145-152	APC regulator of WNT signaling pathway	Homo sapiens	41-60
15247982-4	2004	In this study, surface plasmon resonance (SPR) spectroscopy was used to quantitatively measure the interaction of heparin and HCII using a heparin biochip prepared by covalently immobilizing preformed albumin-heparin conjugate.	Heparin	139-146	serpin family D member 1	Homo sapiens	126-130
8972021-0	1996	Heparin stimulation of the inhibition of activated protein C and other enzymes by human protein C inhibitor--influence of the molecular weightof heparin and ionic strength.	Heparin	145-152	serpin family A member 5	Homo sapiens	88-107
8972021-1	1996	The ability of unfractionated (UF) heparin and low-molecular-weight heparin (LMWH) to potentiate the inhibition of fibrinolytic and coagulation factors by protein C inhibitor (PCI) was studied.	Heparin	35-42	serpin family A member 5	Homo sapiens	155-174
15247982-4	2004	In this study, surface plasmon resonance (SPR) spectroscopy was used to quantitatively measure the interaction of heparin and HCII using a heparin biochip prepared by covalently immobilizing preformed albumin-heparin conjugate.	Heparin	139-146	serpin family D member 1	Homo sapiens	126-130
8972021-1	1996	The ability of unfractionated (UF) heparin and low-molecular-weight heparin (LMWH) to potentiate the inhibition of fibrinolytic and coagulation factors by protein C inhibitor (PCI) was studied.	Heparin	68-75	serpin family A member 5	Homo sapiens	155-174
15247982-6	2004	The interactions of HCII with heparin, low-molecular-weight heparin, and heparin oligosaccharides (disaccharide, tetrasaccharide, hexasaccharide) were examined in solution competition experiments using SPR.	Heparin	30-37	serpin family D member 1	Homo sapiens	20-24
8885147-1	1996	The smallest circulating von Willebrand factor (vWF) molecule is a dimer composed of two identical subunits containing binding sites for heparin, collagen, platelet glycoproteins and coagulation factor VIII (FVIII).	Heparin	137-144	coagulation factor VIII	Homo sapiens	208-213
15347838-0	2004	Heparin increases prolactin and modifies the effects of fgf-2 upon prolactin accumulation in pituitary primary cultures.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	56-61
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Heparin	77-84	serpin family D member 1	Homo sapiens	21-25
15347838-4	2004	However, low doses of heparin reduced the effects of FGF-2, but higher doses of heparin increased the maximal FGF-2-induced prolactin secretion and ED50.	Heparin	22-29	fibroblast growth factor 2	Rattus norvegicus	53-58
15347838-4	2004	However, low doses of heparin reduced the effects of FGF-2, but higher doses of heparin increased the maximal FGF-2-induced prolactin secretion and ED50.	Heparin	80-87	fibroblast growth factor 2	Rattus norvegicus	110-115
15347838-6	2004	However, heparin restored cell responsiveness to FGF-2.	Heparin	9-16	fibroblast growth factor 2	Rattus norvegicus	49-54
15347838-7	2004	Our results suggest that heparin, when present in the medium, binds FGF-2, therefore reducing its ability to interact with FGF receptors in a dose-dependent manner up to a critical molar concentration, at which heparin itself starts to activate the FGF receptor, and strengthens the activation induced by its proper ligand, FGF-2.	Heparin	25-32	fibroblast growth factor 2	Rattus norvegicus	68-73
8841405-12	1996	p38/TPK-IIB, however, exhibits a specific activity which is sixfold higher than that of p72syk and appears to be 50-fold more sensitive to inhibition by heparin.	Heparin	153-160	mitogen activated protein kinase 14	Rattus norvegicus	0-3
15347838-7	2004	Our results suggest that heparin, when present in the medium, binds FGF-2, therefore reducing its ability to interact with FGF receptors in a dose-dependent manner up to a critical molar concentration, at which heparin itself starts to activate the FGF receptor, and strengthens the activation induced by its proper ligand, FGF-2.	Heparin	25-32	fibroblast growth factor 2	Rattus norvegicus	68-71
15347838-7	2004	Our results suggest that heparin, when present in the medium, binds FGF-2, therefore reducing its ability to interact with FGF receptors in a dose-dependent manner up to a critical molar concentration, at which heparin itself starts to activate the FGF receptor, and strengthens the activation induced by its proper ligand, FGF-2.	Heparin	25-32	fibroblast growth factor 2	Rattus norvegicus	324-329
15347838-7	2004	Our results suggest that heparin, when present in the medium, binds FGF-2, therefore reducing its ability to interact with FGF receptors in a dose-dependent manner up to a critical molar concentration, at which heparin itself starts to activate the FGF receptor, and strengthens the activation induced by its proper ligand, FGF-2.	Heparin	211-218	fibroblast growth factor 2	Rattus norvegicus	68-73
8780517-0	1996	Two hierarchies of FGF-2 signaling in heparin: mitogenic stimulation and high-affinity binding/receptor transphosphorylation.	Heparin	38-45	fibroblast growth factor 2	Mus musculus	19-24
15347838-7	2004	Our results suggest that heparin, when present in the medium, binds FGF-2, therefore reducing its ability to interact with FGF receptors in a dose-dependent manner up to a critical molar concentration, at which heparin itself starts to activate the FGF receptor, and strengthens the activation induced by its proper ligand, FGF-2.	Heparin	211-218	fibroblast growth factor 2	Rattus norvegicus	68-71
8780517-6	1996	As shown previously, fibroblasts treated with chlorate, which inhibits the sulfation of heparan sulfate and its subsequent binding to FGF-2, display a dramatically reduced response to picomolar concentrations of FGF-2, but binding to receptors and a mitogenic response is restored by heparin.	Heparin	284-291	fibroblast growth factor 2	Mus musculus	134-139
8718884-6	1996	The acid protease cathepsin D generated fragments of 31-33.5 kDa from the COOH-terminal heparin-binding domain of Fn which possessed high immunoreactivity with anti-CS-1.	Heparin	88-95	cathepsin D	Homo sapiens	18-29
8757639-7	1996	Daily systemic injections of RGD, CS-1, and/or peptides derived from the heparin-binding region of the A chain not only prevented leukocyte infiltration in the salivary glands of the TGF-beta1 -/- mice, but also reversed the acinar and ductal derangements.	Heparin	73-80	transforming growth factor, beta 1	Mus musculus	183-192
8840463-1	1996	Eight heparin derivatives (HD1 to HD8) were prepared by mixing various doses of protamine with a fixed amount of heparin.	Heparin	6-13	histone deacetylase 1	Rattus norvegicus	27-30
15347838-9	2004	In conclusion, heparin modulates PRL secretion and PRL responses to FGF-2 in vitro.	Heparin	15-22	fibroblast growth factor 2	Rattus norvegicus	68-73
8840463-1	1996	Eight heparin derivatives (HD1 to HD8) were prepared by mixing various doses of protamine with a fixed amount of heparin.	Heparin	6-13	histone deacetylase 8	Rattus norvegicus	34-37
15159114-3	2004	After 4-h capacitation in the presence of heparin, the addition of PDC-109 (0.5, 1.5 or 3.0mg/ml) significantly decreased the percentages of motile, progressive, and viable cells; these effects were also detected in the absence of heparin.	Heparin	42-49	seminal plasma protein PDC-109	Bos taurus	67-74
8865534-10	1996	The concentration of TFPI was significantly increased following the incubation with thrombin and heparin, including low molecular weight heparin, in a dose- and time-dependent manner.	Heparin	97-104	tissue factor pathway inhibitor	Homo sapiens	21-25
8663244-6	1996	Degradation of TSP2 was less sensitive to inhibition by heparin than degradation of TSP1.	Heparin	56-63	tumor suppressor region 2	Mus musculus	15-19
15159114-3	2004	After 4-h capacitation in the presence of heparin, the addition of PDC-109 (0.5, 1.5 or 3.0mg/ml) significantly decreased the percentages of motile, progressive, and viable cells; these effects were also detected in the absence of heparin.	Heparin	231-238	seminal plasma protein PDC-109	Bos taurus	67-74
15159114-4	2004	However, PDC-109 elicited a twofold increase (from 14 to 28%) in the proportion of acrosome-reacted spermatozoa, but only in the presence of heparin.	Heparin	141-148	seminal plasma protein PDC-109	Bos taurus	9-16
8641177-8	1996	Heparin markedly decreased initial IGFBP-3 cell adherence, but could not promote dissociation of IGFBP-3 from cells after the 48-h preincubation.	Heparin	0-7	insulin like growth factor binding protein 3	Bos taurus	35-42
15105424-9	2004	Heparin blockage of cell-surface proteoglycans also prevented carboxyl ester lipase stimulation of cholesteryl ester uptake by HepG2 cells.	Heparin	0-7	carboxyl ester lipase	Mus musculus	62-83
8641177-11	1996	They also suggest that IGFBP-3 binding to heparin-like molecules on the cell surface is not directly involved in this process.	Heparin	42-49	insulin like growth factor binding protein 3	Bos taurus	23-30
8984033-8	1996	There was an apparent fall in plasma GLP-1 values in all subjects after administration of heparin.	Heparin	90-97	glucagon like peptide 1 receptor	Homo sapiens	37-42
15205701-6	2004	CONCLUSION: The rise of plasma HGF after heparin treatment suggests that heparin has some other biological effects in addition to its anticoagulant property through HGF.	Heparin	41-48	hepatocyte growth factor	Homo sapiens	165-168
15205701-6	2004	CONCLUSION: The rise of plasma HGF after heparin treatment suggests that heparin has some other biological effects in addition to its anticoagulant property through HGF.	Heparin	73-80	hepatocyte growth factor	Homo sapiens	31-34
8723840-2	1996	Many neuregulin gene products bind heparin, and we hypothesize that affinity for heparin may implicate cell surface heparan sulfate proteoglycans (HeSPGs) as co-receptors for the soluble neuregulin gene product, recombinant human glial growth factor 2 (rhGGF2).	Heparin	81-88	neuregulin 1	Homo sapiens	230-251
15205701-6	2004	CONCLUSION: The rise of plasma HGF after heparin treatment suggests that heparin has some other biological effects in addition to its anticoagulant property through HGF.	Heparin	73-80	hepatocyte growth factor	Homo sapiens	165-168
14965340-8	2004	These data indicated that serum levels of endostatin changed in parallel with those of VEGF in response to myocardial ischaemia/reperfusion, and the marked increase in serum HGF levels after reperfusion seemed to be, at least in part, due to heparin administration.	Heparin	242-249	hepatocyte growth factor	Homo sapiens	174-177
8621980-2	1996	Recently, however, a body of data has indicated that platelet factor 4 (PF4) is required for heparin-induced thrombocytopenia (HIT) antibody to bind to heparin.	Heparin	93-100	platelet factor 4	Homo sapiens	72-75
8621980-2	1996	Recently, however, a body of data has indicated that platelet factor 4 (PF4) is required for heparin-induced thrombocytopenia (HIT) antibody to bind to heparin.	Heparin	152-159	platelet factor 4	Homo sapiens	72-75
8621980-6	1996	Our data suggest that the F(ab")2 domain of HIT antibody binds to heparin-PF4 complexes that accumulate on the platelet surface when equimolar concentrations of heparin and PF4 are present.	Heparin	66-73	platelet factor 4	Homo sapiens	74-77
8621980-6	1996	Our data suggest that the F(ab")2 domain of HIT antibody binds to heparin-PF4 complexes that accumulate on the platelet surface when equimolar concentrations of heparin and PF4 are present.	Heparin	66-73	platelet factor 4	Homo sapiens	173-176
9590145-1	1998	Heparin-induced thrombocytopenia (HIT) is mediated by antibody against complexes of platelet factor-4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	103-106
9590145-6	1998	We found that when the molar concentration of PF4 approximates or exceeds that of heparin, the ligands bind simultaneously to the cells and HIT-IgG binds also.	Heparin	82-89	platelet factor 4	Homo sapiens	46-49
9590145-7	1998	However, when heparin is in molar excess, both PF4 binding and HIT-IgG binding are diminished.	Heparin	14-21	platelet factor 4	Homo sapiens	47-50
9590145-8	1998	Our data are consistent with the hypothesis that heparin-PF4 complexes bind via their heparin component to heparin binding sites on the platelet membrane rather than by their PF4 component to PF4 sites.	Heparin	49-56	platelet factor 4	Homo sapiens	57-60
14695351-5	2004	By voltage-clamp recording, Ca(2+) influx through voltage-dependent Ca(2+) channels (VDCCs) was shown to be responsible for activating the initial SK current, whereas the IP(3)R blocker heparin abolished the delayed component.	Heparin	186-193	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	171-177
9590145-8	1998	Our data are consistent with the hypothesis that heparin-PF4 complexes bind via their heparin component to heparin binding sites on the platelet membrane rather than by their PF4 component to PF4 sites.	Heparin	86-93	platelet factor 4	Homo sapiens	57-60
9558385-10	1998	Furthermore, PF-4 complexed to FGF-2 and inhibited endogenous or heparin-induced FGF-2 dimerization.	Heparin	65-72	fibroblast growth factor 2	Mus musculus	81-86
9557662-6	1998	CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns.	Heparin	48-55	cyclin H	Homo sapiens	0-3
9557662-6	1998	CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns.	Heparin	48-55	cyclin H	Homo sapiens	131-134
9557662-6	1998	CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns.	Heparin	48-55	cyclin H	Homo sapiens	131-134
9557662-6	1998	CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns.	Heparin	226-233	cyclin H	Homo sapiens	0-3
9557662-6	1998	CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns.	Heparin	226-233	cyclin H	Homo sapiens	131-134
9557662-6	1998	CAK could be inhibited by the kinase inhibitors heparin and manganese ions but not by spermidine, DRB, H89, or H7, indicating that CAK is distinct from protein kinase A and protein kinase C. CAK could be partially purified by heparin-Sepharose CL-6B and phosphocellulose P11 columns.	Heparin	226-233	cyclin H	Homo sapiens	131-134
9537999-11	1998	Dot-blot experiments showed that one of the polypeptide chains of clusterin which had been reduced and alkylated under denaturing conditions bound to heparin-Sepharose.	Heparin	150-157	clusterin	Homo sapiens	66-75
9578489-0	1998	The conversion of recombinant human mast cell prochymase to enzymatically active chymase by dipeptidyl peptidase I is inhibited by heparin and histamine.	Heparin	131-138	cathepsin C	Homo sapiens	92-114
9578489-6	1998	The activation of prochymase by DPP I was strongly inhibited by heparin (IC50 = 0.5 microg ml[-1]) and histamine (IC50 = 2 mM), though these mast cell products had little effect on the action of DPP I towards a low molecular-mass substrate.	Heparin	64-71	cathepsin C	Homo sapiens	32-37
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	72-79	serpin family D member 1	Homo sapiens	0-19
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	72-79	serpin family D member 1	Homo sapiens	21-25
8627561-4	1996	Both an IP3 receptor monoclonal antibody (5 micrograms/ml) and an IP3 receptor antagonist, heparin (5 mg/ml), directly introduced into the cells via the patch pipette, reduced or abolished oscillations in Clca induced by ACh.	Heparin	91-98	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	66-78
8607674-3	1996	RESULTS: Heparin-coated extracorporeal circuits significantly reduced circulating complement activation product C3b/c and soluble C5b-9 concentrations at the end of cardiopulmonary bypass and after protamine sulfate administration compared with the uncoated circuits, but not iC3, C4b/c, or C3a concentrations.	Heparin	9-16	complement C4B (Chido blood group)	Homo sapiens	281-284
8732490-3	1996	Analysis of kinetic parameters after heparin-induced extracorporeal plasma apheresis revealed a reduced fractional catabolic rate for both low-density lipoprotein (LDL) and Lp(a).	Heparin	37-44	lipoprotein(a)	Homo sapiens	173-178
8631822-9	1996	Plasmin yields two fragments of VEGF as indicated by reverse phase high performance liquid chromatography and SDS-polyacrylamide gel electrophoresis: an amino-terminal homodimeric protein containing receptor binding determinants and a carboxyl-terminal polypeptide which bound heparin.	Heparin	277-284	plasminogen	Homo sapiens	0-7
8630391-2	1996	At near-plasma concentrations of TFPI, ATIII, and factor X, factor X activation that occurs in response to TF:VII is essentially abolished in the presence of heparin (0.5 micromol/L).	Heparin	158-165	tissue factor pathway inhibitor	Homo sapiens	33-37
8630391-6	1996	These results indicated that when the unactivated TF:VII complex is the initiating stimulus, heparin-dependent reduction in the rate and extent of factor X activation requires both ATIII and TFPI.	Heparin	93-100	tissue factor pathway inhibitor	Homo sapiens	191-195
8615699-3	1996	It binds heparin, a highly sulfated glycosaminoglycan also found in mast cell secretary granules, and the interaction increases its effectiveness as an inhibitor of neutrophil elastase.	Heparin	9-16	elastase, neutrophil expressed	Homo sapiens	165-184
9485475-3	1998	We recently observed that heparin induces dissociation of complexes containing thrombin and the reactive site mutant HCII(L444R) to yield active thrombin and cleaved inhibitor (Han, J.	Heparin	26-33	serpin family D member 1	Homo sapiens	117-121
9485475-7	1998	In the current study, we have investigated the mechanism by which heparin induces dissociation of the thrombin-HCII(L444R) complex.	Heparin	66-73	serpin family D member 1	Homo sapiens	111-115
9485475-9	1998	Binding of heparin to HCII(L444R) in the complex also does not appear to be required, since the heparin dose response is unaltered for complexes containing the double mutant HCII(L444R/K173Q), which has decreased affinity for heparin.	Heparin	11-18	serpin family D member 1	Homo sapiens	22-26
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	49-56	serpin family D member 1	Homo sapiens	152-156
8739535-4	1996	Heparin produced a marked release of TFPI and t-PA after i.v.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	37-41
15010305-2	2004	These two models represent the regular region of heparin lacking one type of O-sulfate group, either at C-6 of glucosamine or at C-2 of iduronate.	Heparin	49-56	complement C6	Homo sapiens	104-107
8739535-12	1996	Repeated administration of a hypersulfated heparin analogue produced marked increase in TFPI in both i.v.	Heparin	43-50	tissue factor pathway inhibitor	Homo sapiens	88-92
8576617-4	1996	Secondary PAPP-A containing fractions were applied to a Heparin-Sepharose column and eluted by a stepwise increase in NaCl 0.15, 0.30 and 0.60 M in 0.05 M Tris-HCl buffer, pH 7.8.	Heparin	56-63	pappalysin 1	Homo sapiens	10-16
8576617-6	1996	Thirdly the pooled fractions which contained PAPP-A after Heparin-Sepharose affinity chromatography were applied to DEAE-Sephacel Chromatography and eluted by a stepwise increase in NaCl 0.15, 0.30 and 0.45 M in 0.01 M acetate buffer, pH 5.5.	Heparin	58-65	pappalysin 1	Homo sapiens	45-51
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	90-97	serpin family D member 1	Homo sapiens	152-156
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	83-90	serpin family D member 1	Homo sapiens	24-28
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	165-172	serpin family D member 1	Homo sapiens	24-28
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	165-172	serpin family D member 1	Homo sapiens	24-28
9480888-3	1998	In order to investigate this, we isolated LPL from bovine milk via heparin Sepharose chromatography using a continuous salt gradient.	Heparin	67-74	lipoprotein lipase	Bos taurus	42-45
9500522-0	1998	Interleukin-5 binds to heparin/heparan sulfate.	Heparin	23-30	interleukin 5	Homo sapiens	0-13
9587967-3	1998	Heparin acrylic beads, each soaked in 100 micrograms/ml FGF-2, were applied to the Hamburger and Hamilton [(1951) J. Morphol.	Heparin	0-7	fibroblast growth factor 2	Gallus gallus	56-61
9645913-0	1998	Evaluation of a modified APTT-based method for determination of APC resistance in plasma from patients on heparin or oral anticoagulant therapy.	Heparin	106-113	APC regulator of WNT signaling pathway	Homo sapiens	64-67
8713780-3	1996	In the heparin tube, APC reacts completely and irreversibly with its major plasma inhibitors, protein C inhibitor (PCI) and alpha 1-antitrypsin (alpha 1AT), and the complexes formed are measured by ELISAs.	Heparin	7-14	serpin family A member 5	Homo sapiens	94-113
8713780-4	1996	The amount of circulating APC is calculated from the difference between the total amount of complexed APC (sample in citrate plus heparin) and the amount of APC complexed in vivo (sample in citrate plus inhibitor).	Heparin	130-137	APC regulator of WNT signaling pathway	Homo sapiens	26-29
8713780-5	1996	Over 95% of the APC added to blood collected with heparin was recovered in the assay.	Heparin	50-57	APC regulator of WNT signaling pathway	Homo sapiens	16-19
8713781-6	1996	K86E in PCI*B causes a charge alteration in helix D which is likely involved in heparin binding in antithrombin III but not likely involved in glycosaminoglycan binding in PCI.	Heparin	80-87	serpin family A member 5	Homo sapiens	8-13
8575238-2	1995	bFGF immunoreactivity was found mainly in the extracellular matrix, primarily in the endomysium, including the heparin-containing basal lamina and also in the capillary basal membrane of both normal and wounded muscles, however the signal intensity was much stronger in normal muscles.	Heparin	111-118	fibroblast growth factor 2	Rattus norvegicus	0-4
9478964-3	1998	We attempted to characterize the seven structural domains of OCIF by determining the capabilities of various OCIF mutants to inhibit osteoclastogenesis, to interact with heparin, and to form dimers.	Heparin	170-177	TNF receptor superfamily member 11b	Homo sapiens	61-65
14961988-10	2004	The combination of costimulatory blockade and heparin with Tx of a Gal-negative pig organ may prolong graft survival further.	Heparin	46-53	galanin and GMAP prepropeptide	Sus scrofa	67-70
9446652-1	1998	Antibodies associated with heparin-induced thrombocytopenia/ thrombosis (HITT) are now thought to be specific for complexes formed between heparin and platelet factor 4 (PF4), a basic protein found normally in platelet alpha granules.	Heparin	27-34	platelet factor 4	Homo sapiens	170-173
9446652-3	1998	We developed a novel method for antibody purification involving binding to and elution from PF4 complexed to heparin immobilized by end-linkage (EL) to a solid phase.	Heparin	109-116	platelet factor 4	Homo sapiens	92-95
9446652-6	1998	The antibodies did not bind to PF4 complexed with heparin immobilized by multiple chemical cross-linkages, suggesting that the heparin molecule must be in a flexible, relatively unconstrained state to react with PF4 in such a way as to create sites for HITT antibody binding.	Heparin	127-134	platelet factor 4	Homo sapiens	212-215
8522072-5	1995	Heparin increased alpha-FP levels in fetal liver cells, but not in cells obtained after birth.	Heparin	0-7	alpha-fetoprotein	Rattus norvegicus	18-26
7598278-2	1995	Platelet factor 4 (PF4) is a basic polypeptide stored in platelets that reverses heparin.	Heparin	81-88	platelet factor 4	Homo sapiens	19-22
7598278-9	1995	Recombinant PF4 at a 3.0:1 ratio reverses heparin-induced anticoagulation after cardiopulmonary bypass, and represents a potential alternative, especially for the protamine allergic patient.	Heparin	42-49	platelet factor 4	Homo sapiens	12-15
8588942-7	1995	A high affinity heparin binding site was identified within a region conserved in rodent and human APP, APLP1 and APLP2.	Heparin	16-23	amyloid beta precursor like protein 2	Homo sapiens	113-118
15123357-8	2004	RESULTS: CCN2 stimulated DNA synthesis and phosphorylation of FAK, Elk-1 and ERK1/2, the latter of which was blocked by heparin.	Heparin	120-127	ETS transcription factor ELK1	Rattus norvegicus	67-72
21232254-3	1995	The acceleration of TFPI"s inhibitory effect by heparin, the TFPI release caused by heparin injection, and TFPI"s heparin affinity may greatly contribute to the anticoagulant properties of the endothelium, and may be particularly important for the outcome of vascular injury.	Heparin	48-55	tissue factor pathway inhibitor	Homo sapiens	20-24
21232254-3	1995	The acceleration of TFPI"s inhibitory effect by heparin, the TFPI release caused by heparin injection, and TFPI"s heparin affinity may greatly contribute to the anticoagulant properties of the endothelium, and may be particularly important for the outcome of vascular injury.	Heparin	84-91	tissue factor pathway inhibitor	Homo sapiens	61-65
21232254-3	1995	The acceleration of TFPI"s inhibitory effect by heparin, the TFPI release caused by heparin injection, and TFPI"s heparin affinity may greatly contribute to the anticoagulant properties of the endothelium, and may be particularly important for the outcome of vascular injury.	Heparin	84-91	tissue factor pathway inhibitor	Homo sapiens	61-65
21232254-3	1995	The acceleration of TFPI"s inhibitory effect by heparin, the TFPI release caused by heparin injection, and TFPI"s heparin affinity may greatly contribute to the anticoagulant properties of the endothelium, and may be particularly important for the outcome of vascular injury.	Heparin	84-91	tissue factor pathway inhibitor	Homo sapiens	61-65
9518874-9	1998	In the presence of heparin, TGF-alpha showed synergistic interactions with insulin or IGF-I.	Heparin	19-26	insulin-like growth factor I	Ovis aries	86-91
9507993-6	1998	Heparin administration released lipoprotein lipase (LPL) and hepatic lipase (HL) activities after 20 min, and significantly reduced apoB-48 concentrations in d &lt; 1.006 g/mL fractions only.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	61-75
9473690-1	1998	Hepatocyte growth factor (HGF/SF), is a heparin-binding polypeptide which stimulates DNA synthesis in a variety of cell types and also promotes cell migration and morphogenesis.	Heparin	40-47	hepatocyte growth factor	Homo sapiens	0-24
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	interleukin 1 complex	Mus musculus	79-83
21232254-3	1995	The acceleration of TFPI"s inhibitory effect by heparin, the TFPI release caused by heparin injection, and TFPI"s heparin affinity may greatly contribute to the anticoagulant properties of the endothelium, and may be particularly important for the outcome of vascular injury.	Heparin	84-91	tissue factor pathway inhibitor	Homo sapiens	61-65
15123357-8	2004	RESULTS: CCN2 stimulated DNA synthesis and phosphorylation of FAK, Elk-1 and ERK1/2, the latter of which was blocked by heparin.	Heparin	120-127	mitogen activated protein kinase 3	Rattus norvegicus	77-83
14761186-5	2004	In vitro these heparin derivatives prevent the formation of FGFR/FGF2/heparan sulfate proteoglycan ternary complexes and inhibit FGF2-stimulated endothelial cell proliferation.	Heparin	15-22	fibroblast growth factor 2	Gallus gallus	65-69
7779780-7	1995	The Nter domain of apo(a) was purified as a soluble protein in a two-step procedure which involved sequential use of a heparin-Sepharose column and a lysine-Sepharose column.	Heparin	119-126	lipoprotein(a)	Homo sapiens	19-25
7779780-8	1995	The Cter domain of apo(a), which remained in disulfide linkage with apo B100 of Lp(a), was isolated as a lipoprotein particle by a combination of chromatographic steps on heparin-Sepharose and Q-Sepharose columns.	Heparin	171-178	lipoprotein(a)	Homo sapiens	19-25
7768918-0	1995	Influence of low molecular mass heparin on the kinetics of neutrophil elastase inhibition by mucus proteinase inhibitor.	Heparin	32-39	elastase, neutrophil expressed	Homo sapiens	59-78
7768918-1	1995	Commercial low molecular mass heparin accelerates the inhibition of neutrophil elastase by mucus proteinase inhibitor, the predominant antielastase of lung secretions (Faller, B., Mely, Y., Gerard, D., and Bieth, J.G.	Heparin	30-37	elastase, neutrophil expressed	Homo sapiens	68-87
7647223-4	1995	With the identification of tissue factor pathway inhibitor (TFPI) some of the unexpected effects of heparins can now be clarified.	Heparin	100-108	tissue factor pathway inhibitor	Homo sapiens	27-58
7647223-4	1995	With the identification of tissue factor pathway inhibitor (TFPI) some of the unexpected effects of heparins can now be clarified.	Heparin	100-108	tissue factor pathway inhibitor	Homo sapiens	60-64
7647223-5	1995	To investigate the role of heparin-releasable TFPI on LMWHs the anti-Xa and TFPI antigen levels after prophylactic and therapeutic administration of UFH and LMWHs have been studied in defined clinical trials.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	46-50
9463889-3	1998	PDC-109 displays phosphorylcholine- and heparin-binding activities which are thought to account for its sperm surface coating and glycosaminoglycan-induced sperm capacitating activities, respectively.	Heparin	40-47	seminal plasma protein PDC-109	Bos taurus	0-7
9647520-0	1998	Prevalence of heparin-induced PF4-heparin antibodies in hemodialysis patients.	Heparin	14-21	platelet factor 4	Homo sapiens	30-33
9395501-0	1997	Heparin-binding properties of the amyloidogenic peptides Abeta and amylin.	Heparin	0-7	islet amyloid polypeptide	Homo sapiens	67-73
9395501-11	1997	Studies with another human amyloidogenic protein, amylin, suggested that its heparin-binding properties were also dependent on aggregation state.	Heparin	77-84	islet amyloid polypeptide	Homo sapiens	50-56
9374687-1	1997	Using the major bone insulin-like growth factor-binding protein (IGFBP) IGFBP-5, we took a mechanistic approach in evaluating the role of the heparin-binding domain of IGFBP-5 in regulating plasmin (Pm) proteolysis of IGFBP-5.	Heparin	142-149	plasminogen	Homo sapiens	190-197
7774576-3	1995	Here we show that heparin is a growth factor-independent activating ligand for FGFR-4.	Heparin	18-25	fibroblast growth factor receptor 4	Homo sapiens	79-85
14761186-5	2004	In vitro these heparin derivatives prevent the formation of FGFR/FGF2/heparan sulfate proteoglycan ternary complexes and inhibit FGF2-stimulated endothelial cell proliferation.	Heparin	15-22	fibroblast growth factor 2	Gallus gallus	129-133
7774576-4	1995	Heparin stimulates FGFR-4 autophosphorylation on transfected myoblasts, fibroblasts and lymphoid cells, and is most potent on cells lacking surface heparan proteoglycan.	Heparin	0-7	fibroblast growth factor receptor 4	Homo sapiens	19-25
7774576-5	1995	Two functional analogs of heparin, fucoidan and dextran sulfate, are also activators of FGFR-4, while neither heparin nor its analogs can stimulate FGFR-1 in the absence of FGF.	Heparin	26-33	fibroblast growth factor receptor 4	Homo sapiens	88-94
9367173-6	1997	An altered ability to reduce cytochrome c was observed for heparins of different charge density; fragments with molecular mass lower than approximately 4000 were also unable to produce superoxide.	Heparin	59-67	LOC104968582	Bos taurus	29-41
7774576-7	1995	Heparin activation of FGFR-4 or of a chimeric receptor bearing FGFR-4 ectodomain and FGFR-1 cytodomain triggers downstream tyrosine phosphorylation of several signaling proteins, and induces proliferation of cells bearing the chimeric receptor.	Heparin	0-7	fibroblast growth factor receptor 4	Homo sapiens	22-28
14761186-8	2004	A significant relationship was found between the extent of glycol-splitting and the FGF2-antagonist/angiostatic activities of these heparin derivatives.	Heparin	132-139	fibroblast growth factor 2	Gallus gallus	84-88
7774576-7	1995	Heparin activation of FGFR-4 or of a chimeric receptor bearing FGFR-4 ectodomain and FGFR-1 cytodomain triggers downstream tyrosine phosphorylation of several signaling proteins, and induces proliferation of cells bearing the chimeric receptor.	Heparin	0-7	fibroblast growth factor receptor 4	Homo sapiens	63-69
7774576-8	1995	Consistent with these findings, a soluble FGFR-4 ectodomain has strong FGF-independent affinity for immobilized heparin resin, while soluble FGFR-1 requires FGF for stable heparin interaction.	Heparin	112-119	fibroblast growth factor receptor 4	Homo sapiens	42-48
9359432-8	1997	When HepG2 cells are washed with heparin or dextran sulphate, a substance that binds TFPI is removed from the cell surface and can be detected in a slot-blot assay.	Heparin	33-40	tissue factor pathway inhibitor	Homo sapiens	85-89
9342064-3	1997	The binding of extracellular Tat to heparan sulfate proteoglycans (HSPG) was determined by using trypsin, heparin or heparinase in pulse-chase experiments, by gel shift and competition assays with radiolabeled heparin, and by heparin-affinity chromatography.	Heparin	106-113	tyrosine aminotransferase	Homo sapiens	29-32
7774576-9	1995	Heparin activation of FGFR-4 is the first example of a mammalian polysaccharide serving as a signaling ligand.	Heparin	0-7	fibroblast growth factor receptor 4	Homo sapiens	22-28
14761186-9	2004	Molecular dynamics calculations support the assumption that glycol-split residues act as flexible joints that, while favoring 1:1 binding to FGF2, disrupt the linearity of heparin chains necessary for formation of active complexes with FGFRs.	Heparin	172-179	fibroblast growth factor 2	Gallus gallus	141-145
7706383-10	1995	Finally, hexadimethrine inhibited the specific binding and mitogenic activity of bFGF, suggesting that this cationic polymer can function as an antagonist of heparin-binding mitogens other than AR.	Heparin	158-165	fibroblast growth factor 2	Mus musculus	81-85
9342064-3	1997	The binding of extracellular Tat to heparan sulfate proteoglycans (HSPG) was determined by using trypsin, heparin or heparinase in pulse-chase experiments, by gel shift and competition assays with radiolabeled heparin, and by heparin-affinity chromatography.	Heparin	117-124	tyrosine aminotransferase	Homo sapiens	29-32
9342064-3	1997	The binding of extracellular Tat to heparan sulfate proteoglycans (HSPG) was determined by using trypsin, heparin or heparinase in pulse-chase experiments, by gel shift and competition assays with radiolabeled heparin, and by heparin-affinity chromatography.	Heparin	117-124	tyrosine aminotransferase	Homo sapiens	29-32
14607508-0	2004	Vascularization in vivo caused by the controlled release of fibroblast growth factor-2 from an injectable chitosan/non-anticoagulant heparin hydrogel.	Heparin	133-140	fibroblast growth factor 2	Mus musculus	60-86
9349723-9	1997	Recombinant rat kallistatin produced in E. coli is able to bind to tissue kallikrein, and the interaction is inhibited by heparin.	Heparin	122-129	serine (or cysteine) proteinase inhibitor, clade A, member 3C	Rattus norvegicus	16-27
7605876-2	1995	Heparin injection has previously been shown to increase the plasma levels of TFPI.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	77-81
7542256-1	1995	Vitronectin, a serum and extracellular matrix protein, is present in vivo in two different conformations: a native form, which does not bind heparin, and a heparin-binding conformer, which results from interactions of native vitronectin with either the thrombin-antithrombin III complex or the terminal complement complex, C5b-9.	Heparin	141-148	vitronectin	Bos taurus	0-11
7542256-1	1995	Vitronectin, a serum and extracellular matrix protein, is present in vivo in two different conformations: a native form, which does not bind heparin, and a heparin-binding conformer, which results from interactions of native vitronectin with either the thrombin-antithrombin III complex or the terminal complement complex, C5b-9.	Heparin	156-163	vitronectin	Bos taurus	0-11
7542256-1	1995	Vitronectin, a serum and extracellular matrix protein, is present in vivo in two different conformations: a native form, which does not bind heparin, and a heparin-binding conformer, which results from interactions of native vitronectin with either the thrombin-antithrombin III complex or the terminal complement complex, C5b-9.	Heparin	156-163	vitronectin	Bos taurus	225-236
7542256-3	1995	This effect is specific for the denatured, heparin-binding, form of vitronectin, since native vitronectin has no effect on the production of latent TGF-beta by those cells.	Heparin	43-50	vitronectin	Bos taurus	68-79
7542256-10	1995	This cellular response to the heparin-binding form of vitronectin seems to be mediated by alpha v beta 3 integrins.	Heparin	30-37	vitronectin	Bos taurus	54-65
9462483-1	1997	Connective tissue growth factor (CTGF) is a cysteine-rich mitogenic peptide that binds heparin and is secreted by fibroblasts after activation with transforming growth factor beta (TGF-beta).	Heparin	87-94	cellular communication network factor 2	Homo sapiens	0-31
9462483-1	1997	Connective tissue growth factor (CTGF) is a cysteine-rich mitogenic peptide that binds heparin and is secreted by fibroblasts after activation with transforming growth factor beta (TGF-beta).	Heparin	87-94	cellular communication network factor 2	Homo sapiens	33-37
9346305-8	1997	Neutralization of basic amino acids in the PCI molecule by glutamic acid, which prevented in a dose-dependent way the inhibitory effect of heparin, did not have any effect on the tissue-kallikrein-PCI interaction.	Heparin	139-146	serpin family A member 5	Homo sapiens	43-46
9346305-9	1997	Therefore, direct involvement of basic amino acid residues present in the heparin-binding site of PCI in the tissue-kallikrein-PCI interaction can be excluded.	Heparin	74-81	serpin family A member 5	Homo sapiens	98-101
9346305-9	1997	Therefore, direct involvement of basic amino acid residues present in the heparin-binding site of PCI in the tissue-kallikrein-PCI interaction can be excluded.	Heparin	74-81	serpin family A member 5	Homo sapiens	127-130
9346305-10	1997	Heparin binding might rather cause a change in reactivity of PCI (e.g. by inducing a conformational change or by steric interference), thereby preventing its interaction with tissue kallikrein.	Heparin	0-7	serpin family A member 5	Homo sapiens	61-64
7890669-4	1995	The p53 kinase activity co-purifies with UV-activated c-Jun kinase activity on heparin-Sepharose and on a c-Jun (but not a v-Jun-) affinity column.	Heparin	79-86	jun proto-oncogene	Mus musculus	54-59
14607508-2	2004	In the present work, we examined the capability of the chitosan/non-anticoagulant heparin (periodate-oxidized (IO(4)-) heparin) hydrogel to immobilize fibroblast growth factor (FGF)-2, as well as the controlled release of FGF-2 molecules from the hydrogel in vitro and in vivo.	Heparin	82-89	fibroblast growth factor 2	Mus musculus	151-183
15106730-26	2004	We developed a liposomal-based peptide vaccine, L(HBD) that targets the heparin binding domain of the FGF-2 molecule.	Heparin	72-79	fibroblast growth factor 2	Mus musculus	102-107
9308582-13	1997	Interruption of the vWF/platelet interaction is a promising antithrombotic strategy that may be met by novel heparin-based antithrombotic drugs.	Heparin	109-116	von Willebrand factor	Cavia porcellus	20-23
9306616-4	1997	4) Fucoidan enhanced the interaction of thrombin with both AT-III and heparin cofactor II (HC-II) and it was more effective than unfractionated heparin of LMwt-heparin in enhancing the interaction of HC-II with thrombin.	Heparin	70-77	serpin family D member 1	Homo sapiens	91-96
14961154-1	2004	Heparin-induced thrombocytopenia (HIT) is mediated by antibodies directed against the heparin/platelet factor 4 (PF4) complex.	Heparin	0-7	platelet factor 4	Homo sapiens	86-111
9254627-0	1997	Isolation and conformational analysis of fragment peptide corresponding to the heparin-binding site of hepatocyte growth factor.	Heparin	79-86	hepatocyte growth factor	Homo sapiens	103-127
9254627-4	1997	The binding of HGF to heparin or heparin-like molecules may induce oligomerization of HGF and facilitate c-Met-dependent mitogenesis [Zioncheck et al.	Heparin	22-29	hepatocyte growth factor	Homo sapiens	15-18
9254627-4	1997	The binding of HGF to heparin or heparin-like molecules may induce oligomerization of HGF and facilitate c-Met-dependent mitogenesis [Zioncheck et al.	Heparin	22-29	hepatocyte growth factor	Homo sapiens	86-89
9254627-4	1997	The binding of HGF to heparin or heparin-like molecules may induce oligomerization of HGF and facilitate c-Met-dependent mitogenesis [Zioncheck et al.	Heparin	33-40	hepatocyte growth factor	Homo sapiens	15-18
9254627-4	1997	The binding of HGF to heparin or heparin-like molecules may induce oligomerization of HGF and facilitate c-Met-dependent mitogenesis [Zioncheck et al.	Heparin	33-40	hepatocyte growth factor	Homo sapiens	86-89
7749849-6	1995	Glycation increased the negative charge of Lp(a) and LDL as monitored by electrophoresis and ion-exchange chromatography and also reduced the affinity of Lp(a) and LDL for heparin-Sepharose.	Heparin	172-179	lipoprotein(a)	Homo sapiens	154-159
7538368-5	1995	A low concentration of heparin increased DNA synthesis at the highest concentration of bFGF, but high doses of heparin inhibited the response to bFGF throughout the dose-response curve but without altering the ED50.	Heparin	23-30	fibroblast growth factor 2	Gallus gallus	87-91
7538368-5	1995	A low concentration of heparin increased DNA synthesis at the highest concentration of bFGF, but high doses of heparin inhibited the response to bFGF throughout the dose-response curve but without altering the ED50.	Heparin	111-118	fibroblast growth factor 2	Gallus gallus	145-149
7649820-3	1995	The antiparasitic drug, suramin (a heparin analogue) inhibits binding of various growth factors (e.g. PDGF, bFGF, TGF-beta, EGF, IGF-I, IGF-II) to their receptors in vitro.	Heparin	35-42	fibroblast growth factor 2	Rattus norvegicus	108-112
7744578-15	1995	Structural requirements for inhibition of heparanase activity and lung colonization of melanoma cells by species of heparin were different from those identified for a) release of ECM-bound basic fibroblast growth factor (bFGF), and b) stimulation of bFGF receptor binding and mitogenic activity.	Heparin	116-123	fibroblast growth factor 2	Mus musculus	250-254
9254627-7	1997	Thus, heparin binding is important for the biological activity of HGF.	Heparin	6-13	hepatocyte growth factor	Homo sapiens	66-69
9254627-8	1997	To identify the heparin-binding site of HGF, we isolated fragment peptides corresponding to the site by limited proteolysis and chemical degradation of recombinant human HGF (rhHGF).	Heparin	16-23	hepatocyte growth factor	Homo sapiens	40-43
14961154-1	2004	Heparin-induced thrombocytopenia (HIT) is mediated by antibodies directed against the heparin/platelet factor 4 (PF4) complex.	Heparin	0-7	platelet factor 4	Homo sapiens	113-116
9254627-8	1997	To identify the heparin-binding site of HGF, we isolated fragment peptides corresponding to the site by limited proteolysis and chemical degradation of recombinant human HGF (rhHGF).	Heparin	16-23	hepatocyte growth factor	Homo sapiens	170-173
9254627-10	1997	Because all of the heparin-binding peptides obtained in this study were isolated from the N-terminal hairpin-loop region (PyrGlu32-Asn127) of HGF, the region was identified as the heparin-binding site of HGF.	Heparin	19-26	hepatocyte growth factor	Homo sapiens	142-145
9254627-10	1997	Because all of the heparin-binding peptides obtained in this study were isolated from the N-terminal hairpin-loop region (PyrGlu32-Asn127) of HGF, the region was identified as the heparin-binding site of HGF.	Heparin	19-26	hepatocyte growth factor	Homo sapiens	204-207
9254627-10	1997	Because all of the heparin-binding peptides obtained in this study were isolated from the N-terminal hairpin-loop region (PyrGlu32-Asn127) of HGF, the region was identified as the heparin-binding site of HGF.	Heparin	180-187	hepatocyte growth factor	Homo sapiens	142-145
9254627-10	1997	Because all of the heparin-binding peptides obtained in this study were isolated from the N-terminal hairpin-loop region (PyrGlu32-Asn127) of HGF, the region was identified as the heparin-binding site of HGF.	Heparin	180-187	hepatocyte growth factor	Homo sapiens	204-207
9254627-11	1997	One of the isolated peptides, Phe42-Glu111, containing the N-terminal hairpin-loop structure, was considered a suitable model peptide for the heparin-binding site of HGF.	Heparin	142-149	hepatocyte growth factor	Homo sapiens	166-169
9254627-13	1997	In addition, oligomerization of HGF in the presence of heparin was observed by dynamic light scattering.	Heparin	55-62	hepatocyte growth factor	Homo sapiens	32-35
9254627-14	1997	Based on our evidence, it is considered that the conformational change in the heparin-binding site may induce the oligomerization of HGF.	Heparin	78-85	hepatocyte growth factor	Homo sapiens	133-136
7786411-2	1995	In this report, we find that the TPKI/GSK-3 beta/FA can be stimulated to phosphorylate brain tau up to 8.5 mol of phosphates per mol of protein by heparin, a polyanion compound.	Heparin	147-154	glycogen synthase kinase 3 alpha	Homo sapiens	38-48
7832299-2	1995	Recently, recombinant platelet factor 4 (rPF4) has been cloned, expressed in Escherichia coli, and infused to reverse heparin anticoagulation in the rat, without producing adverse hemodynamic or pulmonary morphologic effects.	Heparin	118-125	platelet factor 4	Rattus norvegicus	41-45
7832299-4	1995	METHODS: The authors evaluated the hemodynamic response and plasma release rates of thromboxane during intravenous challenges with heparin-rPF4 (n = 2), rPF-free carrier (n = 5), rPF4 (n = 5), rPF4 after indomethacin (n = 5), protamine (n = 5) and heparin-protamine (n = 5) in 17 awake, hemodynamically monitored lambs.	Heparin	131-138	platelet factor 4	Rattus norvegicus	139-143
7588997-4	1995	However after a 2 min interaction, heparin showed an increase in the HC-II-thrombin interaction at higher concentrations.	Heparin	35-42	serpin family D member 1	Homo sapiens	69-74
9258408-0	1997	G1 phase arrest of human smooth muscle cells by heparin, IL-4 and cAMP is linked to repression of cyclin D1 and cdk2.	Heparin	48-55	cyclin D1	Homo sapiens	98-107
9258408-0	1997	G1 phase arrest of human smooth muscle cells by heparin, IL-4 and cAMP is linked to repression of cyclin D1 and cdk2.	Heparin	48-55	cyclin dependent kinase 2	Homo sapiens	112-116
14729333-0	2004	Heparin binds to the laminin alpha4 chain LG4 domain at a site different from that found for other laminins.	Heparin	0-7	laminin subunit alpha 4	Homo sapiens	21-35
9258408-6	1997	Heparin, a strong inhibitor of HUASMC proliferation, strongly down-modulated the levels of cyclin D1 mRNA and protein, cdk2 mRNA and cdc2 protein.	Heparin	0-7	cyclin D1	Homo sapiens	91-100
9258408-6	1997	Heparin, a strong inhibitor of HUASMC proliferation, strongly down-modulated the levels of cyclin D1 mRNA and protein, cdk2 mRNA and cdc2 protein.	Heparin	0-7	cyclin dependent kinase 2	Homo sapiens	119-123
9245569-7	1997	Intravenous administration of heparin or neutralizing antibodies to bFGF or PDGF prior to injury reduced SMC proliferation and neointimal lesional formation but did not affect the early induction of MAPK activity.	Heparin	30-37	fibroblast growth factor 2	Rattus norvegicus	68-72
9245569-9	1997	IN CONCLUSION: (1) MAPK is activated in a time-dependent manner in response to injury; (2) the antiproliferative effect of heparin in vivo is not mediated through the inhibition of MAPK activity induced 30 min after injury; (3) the activation of MAPK after 30 min is not dependent on PDGF, bFGF, or thrombin following vessel injury in the rat.	Heparin	123-130	fibroblast growth factor 2	Rattus norvegicus	290-294
7660142-0	1995	Antithrombin III affinity dependence on the anticoagulant, antiprotease, and tissue factor pathway inhibitor actions of heparins.	Heparin	120-128	tissue factor pathway inhibitor	Homo sapiens	77-108
7660142-14	1995	The endogenous release of TFPI may contribute to the antithrombotic actions of heparin and related glycosaminoglycans.	Heparin	79-86	tissue factor pathway inhibitor	Homo sapiens	26-30
14729333-1	2004	We previously reported that the LG4 domain of the laminin alpha4 chain is responsible for high-affinity heparin binding.	Heparin	104-111	laminin subunit alpha 4	Homo sapiens	50-64
14730967-6	2004	The key heparin-binding loops of FGF19 have radically different conformations and charge patterns, compared to other FGFs, correlating with the unusually low affinity of FGF19 for heparin.	Heparin	8-15	fibroblast growth factor 19	Homo sapiens	33-38
7660146-5	1995	Compared on the basis of their ability to delay the initiation of and inhibit factor X and prothrombin activation, the anticoagulant effectiveness of 0.5 nM TFPI was greater than those of 10 nM hirudin and approximately 100 nM (0.1 unit/mL) heparin.	Heparin	241-248	tissue factor pathway inhibitor	Homo sapiens	157-161
7740492-1	1995	As heparin-PF4 (H-PF4) complexes are the target for antibodies associated to heparin-induced thrombocytopenia (HIT), an ELISA has been developed and optimised for testing antibodies binding to H-PF4.	Heparin	3-10	platelet factor 4	Homo sapiens	11-14
9181238-7	1997	The factors with endothelial cell retraction activity in the CM from PSN-1 cells were characterized as heat-stable, trypsin-sensitive glycoproteins ranging from 10,000 to 50,000 in molecular weight, and were found both in heparin-bound and unbound fractions.	Heparin	222-229	5'-nucleotidase, cytosolic IIIA	Homo sapiens	69-74
9187019-1	1997	Previous works suggest the interesting possibility of an effect of heparin on vascular smooth muscle cell (SMC) replication and migration via a selective inhibition of the expression of t-PA and u-PA both of which may play major roles during intimal hyperplasia following endothelial injury.	Heparin	67-74	plasminogen activator, tissue	Mus musculus	186-190
9187019-4	1997	On control cells, heparin inhibited in a dose-dependent manner the expression of both t-PA and u-PA protein and mRNA.	Heparin	18-25	plasminogen activator, tissue	Mus musculus	86-90
9187019-5	1997	Heparin however, similarly affected the mitogenic and chemotactic activity of FCS for SMC isolated from control, t-PA or u-PA-deficient mice therefore showing that heparin inhibits FCS-induced SMC proliferation via mechanism(s) other than single inhibition of t-PA or u-PA expression by smooth muscle cells.	Heparin	164-171	plasminogen activator, tissue	Mus musculus	260-264
9187023-0	1997	The effect of protamine sulphate on plasma tissue factor pathway inhibitor released by intravenous and subcutaneous unfractionated and low molecular weight heparin in man.	Heparin	156-163	tissue factor pathway inhibitor	Homo sapiens	43-74
9187023-3	1997	Tissue factor pathway inhibitor (TFPI) is an endogenous heparin releasable three domain Kunitz-type coagulation inhibitor which inhibits the crucial tissue factor-factor VIIa (TF-FVIIa) dependent coagulation pathway in the presence of FXa.	Heparin	56-63	tissue factor pathway inhibitor	Homo sapiens	0-31
9187023-3	1997	Tissue factor pathway inhibitor (TFPI) is an endogenous heparin releasable three domain Kunitz-type coagulation inhibitor which inhibits the crucial tissue factor-factor VIIa (TF-FVIIa) dependent coagulation pathway in the presence of FXa.	Heparin	56-63	tissue factor pathway inhibitor	Homo sapiens	33-37
9187023-5	1997	TFPI is located to different vascular pools, the largest being the vascular endothelium from where TFPI can be released dose-dependently to the blood by heparins (2).	Heparin	153-161	tissue factor pathway inhibitor	Homo sapiens	0-4
9187023-5	1997	TFPI is located to different vascular pools, the largest being the vascular endothelium from where TFPI can be released dose-dependently to the blood by heparins (2).	Heparin	153-161	tissue factor pathway inhibitor	Homo sapiens	99-103
9187023-6	1997	TFPI is speculated to contribute to the anticoagulant properties of heparins, but to which degree is not yet fully understood.	Heparin	68-76	tissue factor pathway inhibitor	Homo sapiens	0-4
7740492-1	1995	As heparin-PF4 (H-PF4) complexes are the target for antibodies associated to heparin-induced thrombocytopenia (HIT), an ELISA has been developed and optimised for testing antibodies binding to H-PF4.	Heparin	3-10	platelet factor 4	Homo sapiens	18-21
7534486-0	1994	Heparin modulation of the fibrinolytic activity of plasmin, miniplasmin and neutrophil leukocyte elastase in the presence of plasma protease inhibitors.	Heparin	0-7	plasminogen	Homo sapiens	51-58
7534486-0	1994	Heparin modulation of the fibrinolytic activity of plasmin, miniplasmin and neutrophil leukocyte elastase in the presence of plasma protease inhibitors.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	87-105
7534486-1	1994	The effect of heparin on the inactivation rates of fibrin-bound plasmin, miniplasmin and neutrophil leukocyte elastase (PMN-elastase) by their plasma inhibitors was studied.	Heparin	14-21	plasminogen	Homo sapiens	64-71
7534486-3	1994	Heparin slightly increases the rate of fibrin-bound enzyme inactivation by plasmin inhibitor.	Heparin	0-7	plasminogen	Homo sapiens	75-82
7534486-5	1994	In the case of PMN-elastase, heparin (300 nM) further increases enzyme protection against alpha 1-protease inhibitor; the rate constant decreases from 41 x 10(3) M-1 s-1 to 23 x 10(3) M-1 s-1.	Heparin	29-36	elastase, neutrophil expressed	Homo sapiens	15-27
7534486-6	1994	alpha 2-Macroglobulin inhibits fibrin-bound miniplasmin and PMN-elastase with a second-order rate constant of 1.8 x 10(4) M-1 s-1 and heparin (300 nM) increases the rate insignificantly for miniplasmin and by a factor of two for PMN-elastase.	Heparin	134-141	elastase, neutrophil expressed	Homo sapiens	60-72
7534486-9	1994	If heparin is present (300 nM) these values decrease to 240 s for plasmin and 42 s for miniplasmin, whereas that of PMN-elastase is unchanged.	Heparin	3-10	plasminogen	Homo sapiens	66-73
9158107-0	1997	Pathogenicity of human anti-platelet factor 4 (PF4)/heparin in vivo: generation of mouse anti-PF4/heparin and induction of thrombocytopenia by heparin.	Heparin	52-59	platelet factor 4	Homo sapiens	23-45
9158107-0	1997	Pathogenicity of human anti-platelet factor 4 (PF4)/heparin in vivo: generation of mouse anti-PF4/heparin and induction of thrombocytopenia by heparin.	Heparin	52-59	platelet factor 4	Homo sapiens	94-97
14730967-6	2004	The key heparin-binding loops of FGF19 have radically different conformations and charge patterns, compared to other FGFs, correlating with the unusually low affinity of FGF19 for heparin.	Heparin	8-15	fibroblast growth factor 19	Homo sapiens	170-175
7712048-2	1994	The knowledge of the relationship between the structure and function of the tissue factor pathway inhibitor molecule has been widely expanded, especially with regard to its interaction with heparin.	Heparin	190-197	tissue factor pathway inhibitor	Homo sapiens	76-107
14730967-6	2004	The key heparin-binding loops of FGF19 have radically different conformations and charge patterns, compared to other FGFs, correlating with the unusually low affinity of FGF19 for heparin.	Heparin	180-187	fibroblast growth factor 19	Homo sapiens	33-38
14730967-6	2004	The key heparin-binding loops of FGF19 have radically different conformations and charge patterns, compared to other FGFs, correlating with the unusually low affinity of FGF19 for heparin.	Heparin	180-187	fibroblast growth factor 19	Homo sapiens	170-175
9165218-3	1997	Compared to placebo rabbits, insulin-treated rabbits had higher levels of insulin antibodies in plasma, similar levels of intermediate density, low density and high density lipoprotein cholesterol and similar activities of hepatic and lipoprotein lipase in post-heparin plasma, but lower levels of plasma C-peptide, blood glucose, postprandial plasma triglycerides, plasma cholesterol and very low density lipoprotein cholesterol.	Heparin	262-269	insulin	Oryctolagus cuniculus	29-36
14699503-1	2004	BACKGROUND AND AIMS: The heparin-binding growth factors fibroblast growth factor (FGF) and hepatocyte growth factor (HGF) are potent mitogens for hepatocellular carcinomas (HCCs).	Heparin	25-32	hepatocyte growth factor	Homo sapiens	91-115
9111037-7	1997	Heparin and heparan sulfate (HS), but not dermatan sulfate, chondroitin sulfates A and C, hyaluronic acid, and K5 polysaccharide, competed with 3H-labeled heparin for binding to immobilized GST-Tat and inhibited HIV-LTR transactivation induced by extracellular GST-Tat.	Heparin	0-7	tyrosine aminotransferase	Homo sapiens	194-197
9092516-0	1997	Interaction of heparin with human angiogenin.	Heparin	15-22	angiogenin	Homo sapiens	34-44
9092516-4	1997	Soluble heparin inhibits adhesion, and Ang itself binds tightly to heparin-Sepharose.	Heparin	67-74	angiogenin	Homo sapiens	39-42
9092516-5	1997	In the present study, the interaction of Ang with heparin has been further characterized.	Heparin	50-57	angiogenin	Homo sapiens	41-44
7891388-5	1994	Heparin-binding fractions of FCS obtained by heparin-Sepharose chromatography synergized with TGF-beta 1 and beta 2 to produce a mitogenic response.	Heparin	0-7	transforming growth factor, beta 1	Mus musculus	94-104
7891388-5	1994	Heparin-binding fractions of FCS obtained by heparin-Sepharose chromatography synergized with TGF-beta 1 and beta 2 to produce a mitogenic response.	Heparin	45-52	transforming growth factor, beta 1	Mus musculus	94-104
7961820-1	1994	Protein C inhibitor (PCI) is a plasma serine proteinase inhibitor (serpin) that is a major physiological regulator of activated protein C. Inhibition of its target proteinase is accelerated by heparin in a reaction that involves the binding of both inhibitor and proteinase to heparin to form a ternary complex.	Heparin	193-200	endogenous retrovirus group K member 18	Homo sapiens	45-55
7961820-1	1994	Protein C inhibitor (PCI) is a plasma serine proteinase inhibitor (serpin) that is a major physiological regulator of activated protein C. Inhibition of its target proteinase is accelerated by heparin in a reaction that involves the binding of both inhibitor and proteinase to heparin to form a ternary complex.	Heparin	193-200	endogenous retrovirus group K member 18	Homo sapiens	164-174
7961820-1	1994	Protein C inhibitor (PCI) is a plasma serine proteinase inhibitor (serpin) that is a major physiological regulator of activated protein C. Inhibition of its target proteinase is accelerated by heparin in a reaction that involves the binding of both inhibitor and proteinase to heparin to form a ternary complex.	Heparin	193-200	endogenous retrovirus group K member 18	Homo sapiens	164-174
7961820-1	1994	Protein C inhibitor (PCI) is a plasma serine proteinase inhibitor (serpin) that is a major physiological regulator of activated protein C. Inhibition of its target proteinase is accelerated by heparin in a reaction that involves the binding of both inhibitor and proteinase to heparin to form a ternary complex.	Heparin	277-284	endogenous retrovirus group K member 18	Homo sapiens	164-174
7961820-1	1994	Protein C inhibitor (PCI) is a plasma serine proteinase inhibitor (serpin) that is a major physiological regulator of activated protein C. Inhibition of its target proteinase is accelerated by heparin in a reaction that involves the binding of both inhibitor and proteinase to heparin to form a ternary complex.	Heparin	277-284	endogenous retrovirus group K member 18	Homo sapiens	164-174
7961820-3	1994	The PCI fusion protein interfered in heparin-accelerated PCI-proteinase inhibition reactions, and it bound to heparin-Sepharose.	Heparin	37-44	endogenous retrovirus group K member 18	Homo sapiens	61-71
7961820-4	1994	Compared to the wild-type PCI fusion protein, deletion of the H helix from the fusion protein resulted in a reduction of both heparin-Sepharose binding and the ability to compete for heparin during PCI-proteinase inhibition reactions.	Heparin	126-133	endogenous retrovirus group K member 18	Homo sapiens	202-212
7961820-4	1994	Compared to the wild-type PCI fusion protein, deletion of the H helix from the fusion protein resulted in a reduction of both heparin-Sepharose binding and the ability to compete for heparin during PCI-proteinase inhibition reactions.	Heparin	183-190	endogenous retrovirus group K member 18	Homo sapiens	202-212
7961820-5	1994	Competition assays with H helix synthetic peptides revealed that the R269E altered peptide was the least effective at blocking heparin-catalyzed PCI-proteinase inhibition reactions.	Heparin	127-134	endogenous retrovirus group K member 18	Homo sapiens	149-159
9092516-6	1997	The basic cluster Arg-31/Arg-32/Arg-33 has been identified as an important component of the heparin binding site.	Heparin	92-99	activity regulated cytoskeleton associated protein	Homo sapiens	18-24
9092516-7	1997	Mutations of these residues, and of Arg-70 as well, decrease both the affinity of Ang for heparin-Sepharose and the capacity of Ang to support cell adhesion.	Heparin	90-97	angiogenin	Homo sapiens	82-85
9092516-9	1997	Heparin partially protects Ang from cleavage by trypsin at Lys-60, suggesting that heparin also binds to the region of Ang that contains this residue.	Heparin	0-7	angiogenin	Homo sapiens	27-30
9092516-9	1997	Heparin partially protects Ang from cleavage by trypsin at Lys-60, suggesting that heparin also binds to the region of Ang that contains this residue.	Heparin	0-7	angiogenin	Homo sapiens	119-122
9092516-9	1997	Heparin partially protects Ang from cleavage by trypsin at Lys-60, suggesting that heparin also binds to the region of Ang that contains this residue.	Heparin	83-90	angiogenin	Homo sapiens	27-30
9092516-9	1997	Heparin partially protects Ang from cleavage by trypsin at Lys-60, suggesting that heparin also binds to the region of Ang that contains this residue.	Heparin	83-90	angiogenin	Homo sapiens	119-122
9092516-10	1997	The map here determined indicates that the heparin recognition site on Ang lies outside the catalytic center; indeed, heparin has no significant effect on the ribonucleolytic activity of Ang.	Heparin	43-50	angiogenin	Homo sapiens	71-74
9227267-7	1997	The heparin-binding characteristics of HGF would result in increased binding to glycosaminoglycans and other heparin-like matrix components and, therefore, increased growth factor availability to the cognate recptor.	Heparin	109-116	hepatocyte growth factor	Homo sapiens	39-42
9120000-4	1997	Direct interaction between RG-13577 and FGF-2 was demonstrated by the ability of the former to compete with heparin on binding to FGF-2.	Heparin	108-115	fibroblast growth factor 2	Rattus norvegicus	40-45
9120000-4	1997	Direct interaction between RG-13577 and FGF-2 was demonstrated by the ability of the former to compete with heparin on binding to FGF-2.	Heparin	108-115	fibroblast growth factor 2	Rattus norvegicus	130-135
9120000-7	1997	Moreover, it abrogated heparin-mediated dimerization of FGF-2 and FGFR1, as well as FGF-2 mitogenic activity in HS-deficient F32 lymphoid cells.	Heparin	23-30	fibroblast growth factor 2	Rattus norvegicus	56-61
7955205-12	1994	CONCLUSIONS: Local therapy with the specific thrombin inhibitor r-hirudin significantly reduces short-term quantitative platelet deposition and macroscopic mural thrombus formation following balloon angioplasty compared with systemic treatment of conventional doses of heparin and hirudin and requires a significantly smaller amount of the recombinant drug.	Heparin	269-276	coagulation factor II, thrombin	Sus scrofa	45-53
7929392-6	1994	As previously reported for APP, zinc increased the recovery of APLP1 and APLP2 upon heparin-Sepharose chromatography.	Heparin	84-91	amyloid beta precursor like protein 2	Homo sapiens	73-78
14699503-1	2004	BACKGROUND AND AIMS: The heparin-binding growth factors fibroblast growth factor (FGF) and hepatocyte growth factor (HGF) are potent mitogens for hepatocellular carcinomas (HCCs).	Heparin	25-32	hepatocyte growth factor	Homo sapiens	117-120
15021974-5	2004	RESULTS: Administration of heparin (150 U/kg) significantly increased skin flap survival from 44% in vehicle-treated controls to 91%.	Heparin	27-34	arachidonate 5-lipoxygenase activating protein	Rattus norvegicus	75-79
7524476-7	1994	Heparin, 8-Br-cAMP or 8-Br-cGMP also suppressed c-myc, but this occurred later, after 24-48 h, and was also observed following arrest by metabolic block.	Heparin	0-7	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	48-53
9122872-1	1997	BACKGROUND: Recent studies have shown that patients with heparin-induced thrombocytopenia (HIT) form immunoglobulin G (IgG) and/or IgM antibodies directed against a complex of platelet factor 4 (PF4) and heparin.	Heparin	57-64	platelet factor 4	Homo sapiens	195-198
9134641-4	1997	The observed decrease in FVII:C coincided with a significant decrease in triglyceride levels presumably due to lipoprotein and hepatic lipase released by the heparin.	Heparin	158-165	lipase C, hepatic type	Homo sapiens	127-141
9134644-9	1997	When studying the platelet parameter PF4, whole blood was incubated without any stimuli for 60 min, and we found that heparin PPP contained 1180 ng/ml PF4, while hirudin PPP contained 469 ng/ml, citrate PPP 440 ng/ml, and EDTA PPP 217 ng/ml PF4, respectively.	Heparin	118-125	platelet factor 4	Homo sapiens	151-154
9134644-9	1997	When studying the platelet parameter PF4, whole blood was incubated without any stimuli for 60 min, and we found that heparin PPP contained 1180 ng/ml PF4, while hirudin PPP contained 469 ng/ml, citrate PPP 440 ng/ml, and EDTA PPP 217 ng/ml PF4, respectively.	Heparin	118-125	platelet factor 4	Homo sapiens	151-154
14633147-1	2003	BACKGROUND: Hepatocyte growth factor (HGF), activin A, and follistatin compose an organotrophic system that may be modulated by heparin.	Heparin	128-135	hepatocyte growth factor	Homo sapiens	12-36
9054449-0	1997	The hemopexin-like domain (C domain) of human gelatinase A (matrix metalloproteinase-2) requires Ca2+ for fibronectin and heparin binding.	Heparin	122-129	matrix metallopeptidase 2	Homo sapiens	46-86
9086406-4	1997	An in vitro study showed that coimmobilization of bFGF and heparin (bFGF/heparin) in a crosslinked gelatin gel significantly enhances proliferation of endothelial cells.	Heparin	59-66	fibroblast growth factor 2	Rattus norvegicus	68-72
8051085-8	1994	This inhibition of invasion by syndecan-1 is reversed by preincubating gels with heparin or by growing cells in chlorate, an inhibitor of glycosaminoglycan sulfation.	Heparin	81-88	syndecan 1	Homo sapiens	31-41
7974391-1	1994	Tissue Factor Pathway Inhibitor (TFPI) is a heparin binding protein and injection of heparin causes a release of TFPI to plasma.	Heparin	44-51	tissue factor pathway inhibitor	Homo sapiens	0-31
7974391-1	1994	Tissue Factor Pathway Inhibitor (TFPI) is a heparin binding protein and injection of heparin causes a release of TFPI to plasma.	Heparin	44-51	tissue factor pathway inhibitor	Homo sapiens	33-37
7974391-1	1994	Tissue Factor Pathway Inhibitor (TFPI) is a heparin binding protein and injection of heparin causes a release of TFPI to plasma.	Heparin	44-51	tissue factor pathway inhibitor	Homo sapiens	113-117
7974391-2	1994	In order to understand the binding between TFPI and heparin in more detail we have in this study looked into some of the heparin characteristics and their importance for the TFPI-heparin interaction.	Heparin	52-59	tissue factor pathway inhibitor	Homo sapiens	174-178
7974391-2	1994	In order to understand the binding between TFPI and heparin in more detail we have in this study looked into some of the heparin characteristics and their importance for the TFPI-heparin interaction.	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	43-47
7974391-2	1994	In order to understand the binding between TFPI and heparin in more detail we have in this study looked into some of the heparin characteristics and their importance for the TFPI-heparin interaction.	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	174-178
7974391-2	1994	In order to understand the binding between TFPI and heparin in more detail we have in this study looked into some of the heparin characteristics and their importance for the TFPI-heparin interaction.	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	43-47
7974391-2	1994	In order to understand the binding between TFPI and heparin in more detail we have in this study looked into some of the heparin characteristics and their importance for the TFPI-heparin interaction.	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	174-178
7974391-3	1994	We have developed an assay based on the use of heparin-Sepharose micro columns in order to compare small quantities of heparin fractions as well as different glycosaminoglycans on a weight basis for their TFPI binding.	Heparin	47-54	tissue factor pathway inhibitor	Homo sapiens	205-209
7974391-4	1994	In this assay a glycosaminoglycan in solution compete with heparin-Sepharose for TFPI binding.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	81-85
7974391-5	1994	Size fractionated heparin was analyzed for binding to TFPI, and a clear dependency on the molecular weight was observed.	Heparin	18-25	tissue factor pathway inhibitor	Homo sapiens	54-58
7974391-10	1994	A number of different glycosaminoglycans were tested and the following order of TFPI affinity was found: heparin &gt;&gt; dermatan sulphate &gt; heparan sulphate &gt; chondroitin sulphate C.	Heparin	105-112	tissue factor pathway inhibitor	Homo sapiens	80-84
9067497-1	1997	Recent reports indicate that antibodies associated with heparin-induced thrombocytopenia and thrombosis (HITP) are specific for complexes formed between heparin and the heparin-binding, platelet alpha granule protein, platelet factor 4 (PF4).	Heparin	56-63	platelet factor 4	Homo sapiens	237-240
9067497-1	1997	Recent reports indicate that antibodies associated with heparin-induced thrombocytopenia and thrombosis (HITP) are specific for complexes formed between heparin and the heparin-binding, platelet alpha granule protein, platelet factor 4 (PF4).	Heparin	153-160	platelet factor 4	Homo sapiens	237-240
9067497-3	1997	We therefore studied the class, subclass, and potency of antibodies specific for heparin:PF4 complexes formed by two groups of patients: one with severe thrombocytopenia, with or without thrombosis, and a positive serotonin release assay (SRA) (Group 1) and another with mild or absent thrombocytopenia, absence of thrombosis, and a negative SRA despite having formed antibodies reactive with heparin:PF4 complexes (Group 2).	Heparin	81-88	platelet factor 4	Homo sapiens	89-92
9060459-7	1997	Recombinant MCP-4 was expressed in mammalian cells and purified by heparin-Sepharose chromatography.	Heparin	67-74	mast cell protease 4	Mus musculus	12-17
9037201-2	1997	The 1000-fold enriched CPK activity depends on millimolar Mg2+ and is inhibited by low concentrations of heparin or by &gt; or = 100 microM Ca2+.	Heparin	105-112	phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 alpha	Homo sapiens	23-26
7955315-0	1994	Expression of HB-GAM (heparin-binding growth-associated molecules) in the pathways of developing axonal processes in vivo and neurite outgrowth in vitro induced by HB-GAM.	Heparin	22-29	pleiotrophin	Rattus norvegicus	14-20
7955315-0	1994	Expression of HB-GAM (heparin-binding growth-associated molecules) in the pathways of developing axonal processes in vivo and neurite outgrowth in vitro induced by HB-GAM.	Heparin	22-29	pleiotrophin	Rattus norvegicus	164-170
14633147-1	2003	BACKGROUND: Hepatocyte growth factor (HGF), activin A, and follistatin compose an organotrophic system that may be modulated by heparin.	Heparin	128-135	hepatocyte growth factor	Homo sapiens	38-41
7955315-11	1994	The interactions of HB-GAM with brain neurons are specifically inhibited by heparin and its fragments and by incubation of the neurons with heparitinase.	Heparin	76-83	pleiotrophin	Rattus norvegicus	20-26
7955315-12	1994	We suggest that in developing nervous tissues HB-GAM is deposited to an extracellular location in developing axon pathways and it interacts with heparin-like molecules of the neuron surface to promote formation of neural connections.	Heparin	145-152	pleiotrophin	Rattus norvegicus	46-52
14633147-12	2003	The switch from LMWH to UFH resulted in a significant increase in over-dialysis HGF, a fall in follistatin, and no change in activin A.	Heparin	24-27	hepatocyte growth factor	Homo sapiens	80-83
14675115-0	2003	Heparin-releasable TFPI is not depleted after repeated injections of tinzaparin at therapeutic dose for up to 30 days.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	19-23
7516183-10	1994	Using heparin affinity chromatography, at least three distinct photolabeled aFGF species were resolved.	Heparin	6-13	fibroblast growth factor 1	Bos taurus	76-80
21533365-5	1997	This growth factor(s) bound to heparin Sepharose (HS) beads and its effects on cell proliferation were partially blocked by a neutralizing bFGF antibody.	Heparin	31-38	fibroblast growth factor 2	Mus musculus	139-143
14637100-2	2003	This delivery system uses heparin to immobilize NGF and slow its diffusion from a fibrin matrix.	Heparin	26-33	nerve growth factor	Rattus norvegicus	48-51
9296889-0	1997	[Gastrinemia and heparin stimulated secretion of diamine oxidase on the course of diabetic autonomic neuropathy].	Heparin	17-24	amine oxidase copper containing 1	Homo sapiens	49-64
9200336-8	1997	In contrast, after heparin a significantly lower rise in TFPI antigen plasma levels was observed in obese patients (511.2 +/- 43.4 ng/mL) (p &lt; 0.003).	Heparin	19-26	tissue factor pathway inhibitor	Homo sapiens	57-61
9200336-9	1997	Moreover, a significant inverse correlation was found between the heparin-stimulated TFPI antigen plasma levels and both BMI and basal plasma insulin concentrations.	Heparin	66-73	tissue factor pathway inhibitor	Homo sapiens	85-89
8193358-15	1994	These studies indicate that heparin and other large, highly sulfated polysaccharides bind to PF4 to form a reactive antigen on the platelet surface.	Heparin	28-35	platelet factor 4	Homo sapiens	93-96
12933790-9	2003	The 175-kDa rHARE binds HA, dermatan sulfate, and chondroitin sulfates A, C, D, and E, but not chondroitin, heparin, heparan sulfate, or keratan sulfate.	Heparin	108-115	stabilin 2	Rattus norvegicus	12-17
7912672-3	1994	EPF has been purified from clinically outdated human platelets by heat extraction, ion-exchange and affinity chromatographies on SP-Sephadex and heparin-Sepharose respectively, high-performance hydrophobic interaction chromatography and three reverse-phase HPLC steps, with an average yield of 15 micrograms/100 platelet units (equivalent to approximately 50 1 blood).	Heparin	145-152	heat shock protein family E (Hsp10) member 1	Homo sapiens	0-3
8086743-2	1994	Heparin-induced extracorporeal LDL precipitation (HELP) eliminates selectively fibrinogen, LDL cholesterol, cholesterol, triglycerides and LP(a) from the blood plasma using extracorporeal circulation.	Heparin	0-7	lipoprotein(a)	Homo sapiens	139-144
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	89-93
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	196-200
7512726-3	1994	RAP also binds heparin and is identical to a mouse heparin binding protein (HBP-44) identified in a teratocarcinoma cell line (F9).	Heparin	15-22	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	0-3
7512726-3	1994	RAP also binds heparin and is identical to a mouse heparin binding protein (HBP-44) identified in a teratocarcinoma cell line (F9).	Heparin	15-22	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	76-82
7512726-5	1994	To facilitate the characterization of RAP"s function(s) we have mapped its gp330 and heparin binding sites by performing direct binding studies on fusion proteins representing overlapping domains of RAP.	Heparin	85-92	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	38-41
7512726-7	1994	Binding studies with radiolabeled heparin indicate that the heparin binding site is between amino acids 261 and 323, which is consistent with our previously proposed site (residues 287-306) based on the amphipathic nature of the C terminus of RAP.	Heparin	34-41	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	243-246
7512726-7	1994	Binding studies with radiolabeled heparin indicate that the heparin binding site is between amino acids 261 and 323, which is consistent with our previously proposed site (residues 287-306) based on the amphipathic nature of the C terminus of RAP.	Heparin	60-67	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	243-246
7512726-8	1994	These data demonstrate that the gp330 and heparin binding sites and the Heymann nephritis pathogenic epitope (amino acids 1-86) demonstrated earlier are represented by distinct domains of the RAP polypeptide.	Heparin	42-49	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	192-195
8939951-3	1996	Replacement of several conserved Lys residues in the C-terminal region of mouse and rat sPLA2s by Glu resulted in a marked reduction of their capacities to bind to heparin and mammalian cell surfaces without affecting their enzymatic activities toward dispersed phospholipid as a substrate.	Heparin	164-171	phospholipase A2 group IIA	Rattus norvegicus	88-93
8939951-7	1996	Taken together, these results suggest that sPLA2 expressed endogenously and anchored on cell surfaces via its C-terminal heparin-binding domain is involved in the PGHS-2-dependent delayed PG biosynthesis initiated by growth factors and cytokines during long term culture.	Heparin	121-128	phospholipase A2 group IIA	Rattus norvegicus	43-48
8901773-12	1996	CONCLUSIONS: At the dose used in this study, rPF4 was well tolerated and reversed the anticoagulant effect of heparin.	Heparin	110-117	platelet factor 4	Rattus norvegicus	45-49
8993944-7	1996	RESULTS: ATIII activity (mean +/- SD) of treated swine increased from a baseline of 103 +/- 10% to a peak of 266 +/- 48%, whereas trough levels were maintained at 259 +/- 55% for 72 h by drug infusions every 6 h. The delta MLD, the primary angiographic endpoint in the balloon injured vessel was -0.57 +/- 0.33 mm in heparin group versus -0.26 +/- 0.27 mm in the ATIII group (P &lt; or = 0.03).	Heparin	317-324	serpin family C member 1	Sus scrofa	9-14
8895319-0	1996	Binding of insulin-like growth factor (IGF) I or II to IGF-binding protein-2 enables it to bind to heparin and extracellular matrix.	Heparin	99-106	insulin like growth factor binding protein 2	Homo sapiens	55-76
8895319-6	1996	In this study we report that IGFBP-2 binds to heparin if IGF-I or IGF-II is also included in the incubation buffer.	Heparin	46-53	insulin like growth factor binding protein 2	Homo sapiens	29-36
8895319-8	1996	The binding of IGFBP-2 to heparin was detectable using an IGF-I to IGFBP-2 molar ratio of 2:1.	Heparin	26-33	insulin like growth factor binding protein 2	Homo sapiens	15-22
8895319-8	1996	The binding of IGFBP-2 to heparin was detectable using an IGF-I to IGFBP-2 molar ratio of 2:1.	Heparin	26-33	insulin like growth factor binding protein 2	Homo sapiens	67-74
7511169-3	1994	Accordingly, we have investigated whether the apparent precursor of protease-resistant PrP, protease-sensitive PrP, binds to Congo red and heparin, a highly sulfated glycosaminoglycan with an inhibitory potency like that of heparan sulfate.	Heparin	139-146	prion protein	Mus musculus	87-90
8994360-12	1996	In mice injected with bFGF without heparin, detachment was severe and gross disruption of neural retina was observed.	Heparin	35-42	fibroblast growth factor 2	Mus musculus	22-26
14529296-3	2003	Similar quenching was also observed with the addition of heparin or thenoyltrifluoroacetone (TTFA), inhibitors that bind ferredoxin:NADP(+) reductase (FNR) and prevent reduction of NADP(+).	Heparin	57-64	ferredoxin reductase	Homo sapiens	121-149
9063830-3	1996	(Heparin-induced extracorporal low-density lipoprotein precipitation) system selectively eliminates fibrinogen, LDL (low-density lipoprotein) cholesterol, triglycerides, and LP (a) (lipoprotein a) from the blood plasma by means of extracorporal circulation.	Heparin	1-8	lipoprotein(a)	Homo sapiens	174-180
8950772-8	1996	The post-dye levels of TFPI activity were significantly increased in the former group due to the heparin-induced release of TFPI.	Heparin	97-104	tissue factor pathway inhibitor	Homo sapiens	23-27
7511169-3	1994	Accordingly, we have investigated whether the apparent precursor of protease-resistant PrP, protease-sensitive PrP, binds to Congo red and heparin, a highly sulfated glycosaminoglycan with an inhibitory potency like that of heparan sulfate.	Heparin	139-146	prion protein	Mus musculus	111-114
7511169-4	1994	Protease-sensitive PrP released from the surface of mouse neuroblastoma cells bound to heparin-agarose and Congo red-glass beads.	Heparin	87-94	prion protein	Mus musculus	19-22
7511169-5	1994	Sucrose density gradient fractionation provided evidence that at least some of the PrP capable of binding heparin-agarose was monomeric.	Heparin	106-113	prion protein	Mus musculus	83-86
7511169-6	1994	Free Congo red blocked PrP binding to heparin and vice versa, suggesting that these ligands share a common binding site.	Heparin	38-45	prion protein	Mus musculus	23-26
7511169-7	1994	The relative efficacies of pentosan polysulfate, Congo red, heparin, and chondroitin sulfate in blocking PrP binding to heparin-agarose corresponded with their previously demonstrated potencies in inhibiting protease-resistant PrP accumulation.	Heparin	60-67	prion protein	Mus musculus	105-108
7511169-7	1994	The relative efficacies of pentosan polysulfate, Congo red, heparin, and chondroitin sulfate in blocking PrP binding to heparin-agarose corresponded with their previously demonstrated potencies in inhibiting protease-resistant PrP accumulation.	Heparin	120-127	prion protein	Mus musculus	105-108
8139577-6	1994	Despite its TFIIIC-independent, DNA sequence-dependent assembly, the TFIIIB-SNR6 complex shares important features with tDNA- and 5S rDNA-TFIIIB complexes, such as extent and location of footprint, stability, and resistance to heparin.	Heparin	227-234	SNR6	Saccharomyces cerevisiae S288C	76-80
8029808-0	1994	Role of tissue factor pathway inhibitor in post surgical deep venous thrombosis (DVT) prophylaxis in patients treated with low molecular weight heparin.	Heparin	144-151	tissue factor pathway inhibitor	Homo sapiens	8-39
8950772-8	1996	The post-dye levels of TFPI activity were significantly increased in the former group due to the heparin-induced release of TFPI.	Heparin	97-104	tissue factor pathway inhibitor	Homo sapiens	124-128
8950777-0	1996	Depletion of intravascular pools of tissue factor pathway inhibitor (TFPI) during repeated or continuous intravenous infusion of heparin in man.	Heparin	129-136	tissue factor pathway inhibitor	Homo sapiens	36-67
8950777-0	1996	Depletion of intravascular pools of tissue factor pathway inhibitor (TFPI) during repeated or continuous intravenous infusion of heparin in man.	Heparin	129-136	tissue factor pathway inhibitor	Homo sapiens	69-73
8950777-2	1996	TFPI is increased several-fold in postheparin plasma and thereby thought to contribute significantly to the antithrombotic action of heparin.	Heparin	38-45	tissue factor pathway inhibitor	Homo sapiens	0-4
8950777-3	1996	The present study was conducted to investigate how repeated (n = 8) and continuous (n = 6) administration of heparin affect plasma TFPI and the inhibition of tissue factor (TF)-induced coagulation ex vivo in humans.	Heparin	109-116	tissue factor pathway inhibitor	Homo sapiens	131-135
8950777-4	1996	Free TFPI antigen (TFPI Ag) increased from 19.2 +/- 4.0 ng/ml to 204.7 +/- 31.7 ng/ml after intravenous injection of 5000 IU of unfractionated heparin.	Heparin	143-150	tissue factor pathway inhibitor	Homo sapiens	5-9
8950777-4	1996	Free TFPI antigen (TFPI Ag) increased from 19.2 +/- 4.0 ng/ml to 204.7 +/- 31.7 ng/ml after intravenous injection of 5000 IU of unfractionated heparin.	Heparin	143-150	tissue factor pathway inhibitor	Homo sapiens	19-23
8950777-5	1996	Five repeated injections of 5000 IU of heparin at 4 h intervals caused a progressive decrease (-45 +/- 8%, p &lt; 0.0001 for time effect) in heparin-releasable TFPI and a progressive shortening of the clotting time as determined in a dilute prothrombin time assay (dPT) (-8.7 +/- 6.1 s, p &lt; 0.0001).	Heparin	39-46	tissue factor pathway inhibitor	Homo sapiens	160-164
8950777-5	1996	Five repeated injections of 5000 IU of heparin at 4 h intervals caused a progressive decrease (-45 +/- 8%, p &lt; 0.0001 for time effect) in heparin-releasable TFPI and a progressive shortening of the clotting time as determined in a dilute prothrombin time assay (dPT) (-8.7 +/- 6.1 s, p &lt; 0.0001).	Heparin	141-148	tissue factor pathway inhibitor	Homo sapiens	160-164
8950777-6	1996	The basal concentration of TFPI Ag in plasma collected immediately before each heparin injection was decreased by 29 +/- 15% (p &lt; 0.0001), whereas the dPT was decreased by 6.9 +/- 3.5 s (p &lt; 0.0001).	Heparin	79-86	tissue factor pathway inhibitor	Homo sapiens	27-31
8950777-8	1996	The contribution of TFPI to the inhibition of TF-induced coagulation during heparin infusion was estimated to decrease from 60 +/- 15% to 20 +/- 10% (p &lt; 0.0001).	Heparin	76-83	tissue factor pathway inhibitor	Homo sapiens	20-24
8950777-9	1996	The present data indicate partial depletion of intravascular pools of TFPI by repeated and continuous heparin administration and thereby attenuation of its contribution to the antithrombotic action of heparin.	Heparin	102-109	tissue factor pathway inhibitor	Homo sapiens	70-74
8950777-9	1996	The present data indicate partial depletion of intravascular pools of TFPI by repeated and continuous heparin administration and thereby attenuation of its contribution to the antithrombotic action of heparin.	Heparin	201-208	tissue factor pathway inhibitor	Homo sapiens	70-74
8052965-7	1994	When heparin was used, a high dose (&gt; 200 U/kg, which generated &gt; 3 anti-thrombin U/ml of plasma), was required to perform successful CPB and to maintain CPB pump patency.	Heparin	5-12	coagulation factor II, thrombin	Sus scrofa	79-87
14529296-3	2003	Similar quenching was also observed with the addition of heparin or thenoyltrifluoroacetone (TTFA), inhibitors that bind ferredoxin:NADP(+) reductase (FNR) and prevent reduction of NADP(+).	Heparin	57-64	ferredoxin reductase	Homo sapiens	151-154
8123642-8	1994	Heparin-induced secretion of the two HL mutants was also severely affected: no detectable activity could be measured in the media of S267F, although some inactive mass (12% of wild-type HL) was secreted; mutant T383M secreted 4% and 20% of wild-type activity and mass, respectively.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	37-39
8123642-8	1994	Heparin-induced secretion of the two HL mutants was also severely affected: no detectable activity could be measured in the media of S267F, although some inactive mass (12% of wild-type HL) was secreted; mutant T383M secreted 4% and 20% of wild-type activity and mass, respectively.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	186-188
12700335-5	2003	In transfected cells, the majority of hHLs bound to the cell surface, with only 4% of total extracellular hHL released into heparin-free media, whereas under the same conditions, 61% of total extracellular mHLs were released.	Heparin	124-131	hes family bHLH transcription factor 1	Homo sapiens	38-41
8123656-8	1994	After the monkeys received heparin infusions TFPI was increased about fivefold, but there was no significant difference in these increases between normal and hypercholesterolemic monkeys.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	45-49
8123656-9	1994	The increase in TFPI after heparin infusion is discussed in terms of the relationship between lipoprotein-associated TFPI in plasma and endothelial cell-associated TFPI.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	16-20
8123656-9	1994	The increase in TFPI after heparin infusion is discussed in terms of the relationship between lipoprotein-associated TFPI in plasma and endothelial cell-associated TFPI.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	117-121
8123656-9	1994	The increase in TFPI after heparin infusion is discussed in terms of the relationship between lipoprotein-associated TFPI in plasma and endothelial cell-associated TFPI.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	117-121
7959358-9	1994	Another important difference between in vitro and in vivo studies lies in the fact that sc injection of both heparins will release tissue factor pathway inhibitor (TFPI) in the blood.	Heparin	109-117	tissue factor pathway inhibitor	Homo sapiens	131-162
7959358-9	1994	Another important difference between in vitro and in vivo studies lies in the fact that sc injection of both heparins will release tissue factor pathway inhibitor (TFPI) in the blood.	Heparin	109-117	tissue factor pathway inhibitor	Homo sapiens	164-168
8029788-4	1994	During hemodialysis sessions using heparin, TFPI levels increased 1.2- to 3.5-fold compared with the level before hemodialysis and the degree of increase in TFPI was correlated with the heparin concentration (r = 0.648, p = 0.0001, n = 29).	Heparin	35-42	tissue factor pathway inhibitor	Homo sapiens	44-48
8029788-4	1994	During hemodialysis sessions using heparin, TFPI levels increased 1.2- to 3.5-fold compared with the level before hemodialysis and the degree of increase in TFPI was correlated with the heparin concentration (r = 0.648, p = 0.0001, n = 29).	Heparin	35-42	tissue factor pathway inhibitor	Homo sapiens	157-161
8029788-4	1994	During hemodialysis sessions using heparin, TFPI levels increased 1.2- to 3.5-fold compared with the level before hemodialysis and the degree of increase in TFPI was correlated with the heparin concentration (r = 0.648, p = 0.0001, n = 29).	Heparin	186-193	tissue factor pathway inhibitor	Homo sapiens	44-48
8029788-4	1994	During hemodialysis sessions using heparin, TFPI levels increased 1.2- to 3.5-fold compared with the level before hemodialysis and the degree of increase in TFPI was correlated with the heparin concentration (r = 0.648, p = 0.0001, n = 29).	Heparin	186-193	tissue factor pathway inhibitor	Homo sapiens	157-161
8029788-5	1994	During dialysis sessions using low molecular weight heparin, TFPI levels also increased, but the change was less marked than during dialysis with heparin.	Heparin	52-59	tissue factor pathway inhibitor	Homo sapiens	61-65
8029788-7	1994	In conclusion, TFPI levels were increased by renal failure and by long-term repeated injection of heparin, but the hemodialysis procedure itself did not alter the TFPI level.	Heparin	98-105	tissue factor pathway inhibitor	Homo sapiens	15-19
7509746-7	1994	The rate of complex formation was slow compared to that reported for PCI and activated protein C, but was enhanced up to sixfold in the presence of heparin.	Heparin	148-155	serpin family A member 5	Homo sapiens	69-72
8307953-4	1994	Varying the concentration of 125I-bFGF showed that heparin increased the amount of 125I-bFGF bound at low bFGF concentrations and increased the affinity of bFGF for its receptor by about 3-fold.	Heparin	51-58	fibroblast growth factor 2	Mus musculus	34-38
8798698-3	1996	In the present study, we demonstrated that heparin binding epidermal growth factor-like growth factor (HB-EGF) induced the expression of c-fms and the scavenger receptor in normal human medial smooth muscle cells to the level observed in the intima.	Heparin	43-50	colony stimulating factor 1 receptor	Homo sapiens	137-142
8823102-6	1996	RESULTS: The concentrations of terminal complement complex, lactoferrin, and beta-thromboglobulin were significantly lower in association with heparin-coated surfaces.	Heparin	143-150	pro-platelet basic protein	Homo sapiens	77-97
8798474-2	1996	The recombinant enzyme was purified from culture medium in milligram quantities and shown to have a molecular weight, specific activity, and heparin affinity equivalent to HL present in human post-heparin plasma.	Heparin	197-204	lipase C, hepatic type	Homo sapiens	172-174
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Heparin	77-84	serpin family D member 1	Homo sapiens	0-19
8841405-13	1996	Thus, the observation that Ca(2+)-dependent degradation of p72syk by particulate fraction of rat spleen is accompanied by increased catalytic activity and increased sensitivity to heparin would be consistent with the possibility that hyperactive p38/TPK-IIB might be proteolytically generated from p72syk in response to an increase of intracellular Ca2+.	Heparin	180-187	spleen associated tyrosine kinase	Rattus norvegicus	59-65
8702927-8	1996	Heparin potently inhibited binding of 6B4 proteoglycan to pleiotrophin (IC50 = 3.5 ng/ml).	Heparin	0-7	protein tyrosine phosphatase, receptor type Z1	Rattus norvegicus	38-54
8702927-8	1996	Heparin potently inhibited binding of 6B4 proteoglycan to pleiotrophin (IC50 = 3.5 ng/ml).	Heparin	0-7	pleiotrophin	Rattus norvegicus	58-70
8307953-4	1994	Varying the concentration of 125I-bFGF showed that heparin increased the amount of 125I-bFGF bound at low bFGF concentrations and increased the affinity of bFGF for its receptor by about 3-fold.	Heparin	51-58	fibroblast growth factor 2	Mus musculus	88-92
8307953-4	1994	Varying the concentration of 125I-bFGF showed that heparin increased the amount of 125I-bFGF bound at low bFGF concentrations and increased the affinity of bFGF for its receptor by about 3-fold.	Heparin	51-58	fibroblast growth factor 2	Mus musculus	88-92
8307953-4	1994	Varying the concentration of 125I-bFGF showed that heparin increased the amount of 125I-bFGF bound at low bFGF concentrations and increased the affinity of bFGF for its receptor by about 3-fold.	Heparin	51-58	fibroblast growth factor 2	Mus musculus	88-92
8307953-7	1994	When FGFR-1 or FGFR-2 were expressed in mutant CHO cells deficient in heparan sulfate synthesis, the cells also bound 125I-bFGF in the absence of heparin, and the addition of heparin increased the affinity of bFGF for its receptors 2-3-fold.	Heparin	175-182	fibroblast growth factor receptor 2	Cricetulus griseus	15-21
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	12-19	tissue factor pathway inhibitor	Homo sapiens	90-121
8043225-0	1994	Heparin specifically inhibits binding of V3 loop antibodies to HIV-1 gp120, an effect potentiated by CD4 binding.	Heparin	0-7	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	69-74
7507851-3	1994	Here we have tested the activity of KGF, acidic fibroblast growth factor (aFGF), and basic fibroblast growth factor (bFGF) on normal adult rat and human hepatocytes and their modulation by heparin.	Heparin	189-196	fibroblast growth factor 2	Rattus norvegicus	85-115
7507851-3	1994	Here we have tested the activity of KGF, acidic fibroblast growth factor (aFGF), and basic fibroblast growth factor (bFGF) on normal adult rat and human hepatocytes and their modulation by heparin.	Heparin	189-196	fibroblast growth factor 2	Rattus norvegicus	117-121
8186552-9	1994	This structure may represent the terminus of a biosynthetically formed native heparin chain or a newly formed non-reducing terminus exposed by a tissue endo-beta-glucuronidase which may be involved in the intracellular post-synthetic fragmentation of macromolecular heparin.	Heparin	78-85	glucuronidase beta	Homo sapiens	157-175
8812110-4	1996	The inhibitory effect of HB-GAM on cell proliferation was reversed by heparin, suggesting that HB-GAM may bind to a heparin-type carbohydrate epitope that is required for cell proliferation in the developing limb.	Heparin	70-77	pleiotrophin	Rattus norvegicus	25-31
8812110-4	1996	The inhibitory effect of HB-GAM on cell proliferation was reversed by heparin, suggesting that HB-GAM may bind to a heparin-type carbohydrate epitope that is required for cell proliferation in the developing limb.	Heparin	70-77	pleiotrophin	Rattus norvegicus	95-101
8765134-0	1996	Inhibition of human leukocyte elastase activity by heparins: influence of charge density.	Heparin	51-59	elastase, neutrophil expressed	Homo sapiens	20-38
8186552-9	1994	This structure may represent the terminus of a biosynthetically formed native heparin chain or a newly formed non-reducing terminus exposed by a tissue endo-beta-glucuronidase which may be involved in the intracellular post-synthetic fragmentation of macromolecular heparin.	Heparin	266-273	glucuronidase beta	Homo sapiens	157-175
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	12-19	tissue factor pathway inhibitor	Homo sapiens	123-127
8765134-1	1996	Heparins with different structures and physico-chemical properties were evaluated for their capacity to inhibit human leukocyte elastase activity in vitro by using a chromogenic substrate.	Heparin	0-8	elastase, neutrophil expressed	Homo sapiens	118-136
8765134-5	1996	Heparins strongly inhibit elastase activity, and there is a significant linear dependence between charge density (sulfate-to-carboxyl ratio) and enzymatic activity.	Heparin	0-8	elastase, neutrophil expressed	Homo sapiens	26-34
8696947-11	1996	The heparin-induced increase in cellular protein content includes a 60% to 100% increase in the expression of pericellular bFGF, FGF-R1, and cell membrane-integrated HSPG.	Heparin	4-11	fibroblast growth factor receptor 1	Bos taurus	129-135
8186654-8	1994	Both male and female patients had significantly higher HL activities than their respective controls at 5, 10, 20 and 30 minutes post-heparin.	Heparin	133-140	lipase C, hepatic type	Homo sapiens	55-57
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	12-19	tissue factor pathway inhibitor	Homo sapiens	219-223
7939382-5	1994	Ligand binding studies in aqueous solution indicate that pathophysiologic concentrations of different anions (e.g. heparin, lactate, bicarbonate, phosphate, acetate and sulfate) bind to Mg2+, effectively reducing its concentration in solution.	Heparin	115-122	mucin 7, secreted	Homo sapiens	186-189
8165616-12	1993	It is assumed that protamine displaces heparins from the binding sites of TFPI.	Heparin	39-47	tissue factor pathway inhibitor	Homo sapiens	74-78
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	183-190	tissue factor pathway inhibitor	Homo sapiens	90-121
8165623-6	1993	In vitro studies in blood and seminal plasma showed that heparin stimulated complexation of uPA and tPA with PCI, suggesting that negatively charged glycosaminoglycans in blood vessels and in the reproductive system may regulate PCI reactions with uPA and tPA.	Heparin	57-64	serpin family A member 5	Homo sapiens	109-112
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	183-190	tissue factor pathway inhibitor	Homo sapiens	123-127
8165623-6	1993	In vitro studies in blood and seminal plasma showed that heparin stimulated complexation of uPA and tPA with PCI, suggesting that negatively charged glycosaminoglycans in blood vessels and in the reproductive system may regulate PCI reactions with uPA and tPA.	Heparin	57-64	serpin family A member 5	Homo sapiens	229-232
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	183-190	tissue factor pathway inhibitor	Homo sapiens	219-223
8281931-4	1993	Appreciable amounts of type-II PLA2 were released into the medium from the TNF-stimulated cells when heparin was added extracellularly.	Heparin	101-108	tumor necrosis factor-like	Rattus norvegicus	75-78
12808176-8	2003	In patients switched to UFH, TF levels remained unchanged compared with pre-randomization values, TFPI increased at each interval of HD sessions (all P&lt;0.035) and PF 1+2 increased pre-dialysis (P=0.015).	Heparin	24-27	tissue factor pathway inhibitor	Homo sapiens	98-102
12808176-10	2003	In contrast, baseline TFPI and its 10-min rise correlated inversely with the UFH loading dose (both P&lt;0.040).	Heparin	77-80	tissue factor pathway inhibitor	Homo sapiens	22-26
8262149-0	1993	Heparin modulates the receptor-binding and mitogenic activity of hepatocyte growth factor on hepatocytes.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	65-89
8262149-1	1993	Hepatocyte growth factor (HGF) is a mitogen for hepatocytes, having high affinity for heparin.	Heparin	86-93	hepatocyte growth factor	Homo sapiens	0-24
12808176-12	2003	CONCLUSIONS: Depletion of heparin-releasable stores of TFPI is an untoward effect of repeated anticoagulation during maintenance HD therapy.	Heparin	26-33	tissue factor pathway inhibitor	Homo sapiens	55-59
8262149-1	1993	Hepatocyte growth factor (HGF) is a mitogen for hepatocytes, having high affinity for heparin.	Heparin	86-93	hepatocyte growth factor	Homo sapiens	26-29
12808176-13	2003	The traditional UFH regimen is more prothrombotic than single enoxaparin injections, with high loading doses of UFH being involved in TFPI exhaustion and subsequent hypercoagulability.	Heparin	112-115	tissue factor pathway inhibitor	Homo sapiens	134-138
8262149-3	1993	Binding studies using 125I-HGF showed that more than 85% of bound HGF was released from the cell surface by washing with heparin.	Heparin	121-128	hepatocyte growth factor	Homo sapiens	27-30
8262149-3	1993	Binding studies using 125I-HGF showed that more than 85% of bound HGF was released from the cell surface by washing with heparin.	Heparin	121-128	hepatocyte growth factor	Homo sapiens	66-69
22900309-7	2003	The 81 kDa VN bound to Heparin, whereas the 160 kDa preparation did not bind to Heparin in presence of urea.	Heparin	23-30	vitronectin	Capra hircus	11-13
8262149-6	1993	Furthermore, excess heparin added during the binding of 125I-HGF to hepatocytes, significantly diminished HGF bound to c-Met protein.	Heparin	20-27	hepatocyte growth factor	Homo sapiens	61-64
8262149-6	1993	Furthermore, excess heparin added during the binding of 125I-HGF to hepatocytes, significantly diminished HGF bound to c-Met protein.	Heparin	20-27	hepatocyte growth factor	Homo sapiens	106-109
8262149-7	1993	Moreover, when DNA synthesis of hepatocytes was repressed and retarded by excess HGF, exogenous heparin restored it.	Heparin	96-103	hepatocyte growth factor	Homo sapiens	81-84
12556442-1	2003	The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor"s binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contribute approximately 40 and approximately 60% of the binding free energy, respectively.	Heparin	42-49	endogenous retrovirus group K member 7	Homo sapiens	150-160
12753876-1	2003	PURPOSE: Heparin-induced thrombocytopenia is mediated by antibodies directed against the heparin-platelet factor 4 (heparin/PF4) complex.	Heparin	9-16	platelet factor 4	Homo sapiens	116-127
12753876-11	2003	CONCLUSION: Anti-heparin/PF4 antibody titers, which can be measured rapidly and reproducibly using a particle gel immunoassay, can be used as a confirmatory test to complement a clinical likelihood score among patients with suspected heparin-induced thrombocytopenia.	Heparin	17-24	platelet factor 4	Homo sapiens	25-28
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	0-7	C-C motif chemokine ligand 13	Homo sapiens	69-74
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	166-173	C-C motif chemokine ligand 13	Homo sapiens	69-74
12566461-2	2003	Within this functional domain, syndecan-1 promotes cell-cell adhesion and concentration of heparin binding growth factors.	Heparin	91-98	syndecan 1	Homo sapiens	31-41
12566461-4	2003	The addition of exogenous heparin or the treatment of polarized cells with heparitinase initiates a rapid and dramatic redistribution of uropod syndecan-1 over the entire cell surface, and a mutated syndecan-1 lacking heparan sulfate chains fails to concentrate within uropods.	Heparin	26-33	syndecan 1	Homo sapiens	144-154
12566461-4	2003	The addition of exogenous heparin or the treatment of polarized cells with heparitinase initiates a rapid and dramatic redistribution of uropod syndecan-1 over the entire cell surface, and a mutated syndecan-1 lacking heparan sulfate chains fails to concentrate within uropods.	Heparin	26-33	syndecan 1	Homo sapiens	199-209
12812389-0	2003	Hepatocyte growth factor: a possible mediator of heparin-induced osteoporosis?	Heparin	49-56	hepatocyte growth factor	Homo sapiens	0-24
12662295-2	2003	Recently, we developed a method of using heparin to induce differentiation of human monocytes into CD1a+ DCs without using FCS.	Heparin	41-48	CD1a molecule	Homo sapiens	99-103
12662295-3	2003	In order to determine the potential clinical applicability of heparin-induced CD1a+ DCs, we conducted this study to compare both types of CD1a+ DCs, immunophenotypically and functionally.	Heparin	62-69	CD1a molecule	Homo sapiens	78-82
12662295-4	2003	Our results showed that the expression of CD1a on heparin-DCs was lower than that on FCS-DCs.	Heparin	50-57	CD1a molecule	Homo sapiens	42-46
12606025-1	2003	Some synthetic dextran derivatives that mimic the action of heparin/heparan sulfate were previously shown to inhibit neutrophil elastase and plasmin.	Heparin	60-67	elastase, neutrophil expressed	Homo sapiens	117-136
12606025-1	2003	Some synthetic dextran derivatives that mimic the action of heparin/heparan sulfate were previously shown to inhibit neutrophil elastase and plasmin.	Heparin	60-67	plasminogen	Homo sapiens	141-148
12625842-4	2003	Using specific glycosaminoglycan degrading enzymes in spectrophotometric assays and PEDF-affinity chromatography, we detected heparin and heparan sulfate-like glycosaminoglycans in the Y-79 conditioned media, which had binding affinity for PEDF.	Heparin	126-133	serpin family F member 1	Homo sapiens	84-88
12625842-7	2003	CONCLUSIONS: These data indicate that retinoblastoma cells secrete heparin/heparan sulfate with binding affinity for PEDF, which may be important in efficient cell-surface receptor binding.	Heparin	67-74	serpin family F member 1	Homo sapiens	117-121
12575940-3	2003	The activity of PCI is affected by heparin binding in a manner unique among the heparin binding serpins, and, in addition, PCI binds hydrophobic hormones with apparent specificity for retinoids.	Heparin	35-42	serpin family A member 5	Homo sapiens	16-19
12568929-6	2003	We also determined the recognition structure of EDA(+)FN for Hep by an inhibition experiment on the heparin binding domain II (HepII) in EDA(+)FN with the synthetic peptides, Arg-Arg-Ala-Arg (RRAR), Asp-Gln-Ala-Arg (DNAR), Ile-Lys-Tyr-Glu-Lys (IKYEK), and Gly-Arg-Lys-Lys-Try (GRKKT).	Heparin	100-107	ectodysplasin A	Homo sapiens	48-51
12568929-6	2003	We also determined the recognition structure of EDA(+)FN for Hep by an inhibition experiment on the heparin binding domain II (HepII) in EDA(+)FN with the synthetic peptides, Arg-Arg-Ala-Arg (RRAR), Asp-Gln-Ala-Arg (DNAR), Ile-Lys-Tyr-Glu-Lys (IKYEK), and Gly-Arg-Lys-Lys-Try (GRKKT).	Heparin	100-107	ectodysplasin A	Homo sapiens	137-140
15041796-0	2003	An engineered heparin-binding form of VEGF-E (hbVEGF-E).	Heparin	14-21	platelet derived growth factor C	Homo sapiens	38-44
15041796-4	2003	Here, we have generated a novel heparin-binding form of VEGF-E by introducing the heparin-domain of the human VEGF-A(165) splice variant into the viral VEGF-E protein.	Heparin	32-39	platelet derived growth factor C	Homo sapiens	56-62
15041796-4	2003	Here, we have generated a novel heparin-binding form of VEGF-E by introducing the heparin-domain of the human VEGF-A(165) splice variant into the viral VEGF-E protein.	Heparin	32-39	platelet derived growth factor C	Homo sapiens	152-158
15041796-4	2003	Here, we have generated a novel heparin-binding form of VEGF-E by introducing the heparin-domain of the human VEGF-A(165) splice variant into the viral VEGF-E protein.	Heparin	82-89	platelet derived growth factor C	Homo sapiens	56-62
15041796-4	2003	Here, we have generated a novel heparin-binding form of VEGF-E by introducing the heparin-domain of the human VEGF-A(165) splice variant into the viral VEGF-E protein.	Heparin	82-89	platelet derived growth factor C	Homo sapiens	152-158
12871559-0	2003	Autoimmune disease antigen U1 snRNP neutralizes heparin.	Heparin	48-55	RNA, U1 small nuclear 1	Homo sapiens	27-35
12871566-0	2003	Rebuttal to: Effect of heparin on TAFI-dependent inhibition of fibrinolysis.	Heparin	23-30	carboxypeptidase B2	Homo sapiens	34-38
12393877-6	2002	PCPE2 is also shown to have markedly stronger affinity for heparin than PCPE1, which may account for higher affinities for cell layers.	Heparin	59-66	procollagen C-endopeptidase enhancer 2	Homo sapiens	0-5
12482841-6	2002	Pretreatment of the placental fragments with PIPLC increases the amount of heparin-releasable TFPI by approximately 3-fold.	Heparin	75-82	tissue factor pathway inhibitor	Homo sapiens	94-98
12482841-9	2002	Heparin-releasable TFPI likely represents only a small portion of the total TFPI on endothelium that remains attached to cell-surface glycosaminoglycans after cleavage of the GPI anchor by endogenous enzymes.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	19-23
12482841-9	2002	Heparin-releasable TFPI likely represents only a small portion of the total TFPI on endothelium that remains attached to cell-surface glycosaminoglycans after cleavage of the GPI anchor by endogenous enzymes.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	76-80
12848984-5	2002	Heparin and aspirin are the drugs of choice for APS-related miscarriage, although it is not clear whether combination of both drugs is necessary for all women.	Heparin	0-7	SH2B adaptor protein 2	Homo sapiens	48-51
12241544-3	2002	Heparin releases several endothelial proteins, including lipoprotein lipase, hepatic lipase, platelet factor-4 and superoxide dismutase.	Heparin	0-7	lipase C, hepatic type	Homo sapiens	77-91
8683944-8	1996	Both the human and yeast proteins show an unusual and almost identical arrangement of immunoglobulin type domains, WD40 repeats, a protein kinase C phosphorylation consensus site in the carboxyl region, and a positively charged amino-terminal region that in AAMP has heparin binding potential.	Heparin	267-274	angio associated migratory cell protein	Homo sapiens	258-262
12430897-5	2002	Ryudocan is a cell surface heparan sulfate proteoglycan, which bears heparin-like glycosaminoglycan (heparan sulfate) cahins, originally cloned from rat microvascular endothelial cells.	Heparin	69-76	syndecan 4	Mus musculus	0-8
8663258-5	1996	The binding was inhibited by CK2 effectors such as heparin, polyarginine, and histone H1, but was not affected by the CK2 substrate, casein.	Heparin	51-58	casein kinase 2, alpha prime polypeptide	Mus musculus	29-32
11994286-0	2002	Basic residues in azurocidin/HBP contribute to both heparin binding and antimicrobial activity.	Heparin	52-59	azurocidin 1	Bos taurus	18-28
8687422-3	1996	Compared to human HGF, it has much lower heparin-binding activity and lacks the beta-chain.	Heparin	41-48	hepatocyte growth factor	Homo sapiens	18-21
8687422-7	1996	The inhibitory activity was presumably attributed to this novel HGF because the inhibitory activity, as the existence of this novel HGF, was confined to the identical fractions after heparin-column chromatography.	Heparin	183-190	hepatocyte growth factor	Homo sapiens	64-67
11994286-2	2002	In addition, azurocidin is an inactive serine protease homolog with binding sites for diverse ligands including heparin and the bovine pancreatic trypsin inhibitor (BPTI).	Heparin	112-119	azurocidin 1	Bos taurus	13-23
8687422-7	1996	The inhibitory activity was presumably attributed to this novel HGF because the inhibitory activity, as the existence of this novel HGF, was confined to the identical fractions after heparin-column chromatography.	Heparin	183-190	hepatocyte growth factor	Homo sapiens	132-135
11994286-7	2002	Thus, we report that the 8 basic residues that were altered in the Loop 3/Loop 4 mutant contribute to the ability of the wild-type azurocidin molecule to bind heparin and to kill E. coli and C. albicans.	Heparin	159-166	azurocidin 1	Bos taurus	131-141
8638647-0	1996	Generation of antibodies to heparin-PF4 complexes without thrombocytopenia in patients treated with unfractionated or low-molecular-weight heparin.	Heparin	28-35	platelet factor 4	Homo sapiens	36-39
8638647-1	1996	The incidence of antibodies to heparin-PF4 complexes (H-PF4) has been evaluated in patients who were under heparin therapy for more than 7 days: 109 patients treated with unfractionated heparin (UH) and 100 patients with low-molecular-weight heparin (LMWH).	Heparin	31-38	platelet factor 4	Homo sapiens	39-42
8638647-1	1996	The incidence of antibodies to heparin-PF4 complexes (H-PF4) has been evaluated in patients who were under heparin therapy for more than 7 days: 109 patients treated with unfractionated heparin (UH) and 100 patients with low-molecular-weight heparin (LMWH).	Heparin	31-38	platelet factor 4	Homo sapiens	56-59
8638647-8	1996	Our study demonstrates that the induction of antibodies to H-PF4 is a frequent phenomenon in patients treated with UH or with LMWH.	Heparin	115-117	platelet factor 4	Homo sapiens	61-64
8638647-10	1996	We conclude that the measurement of antibodies to H-PF4 complexes allows the detection of heparin-treated patients at risk of developing type II HIT.	Heparin	90-97	platelet factor 4	Homo sapiens	52-55
8840000-0	1996	The effect of heparin on the regulation of factor VIIa-tissue factor activity by tissue factor pathway inhibitor.	Heparin	14-21	tissue factor pathway inhibitor	Homo sapiens	81-112
8840000-2	1996	Previous studies have shown that heparin binds to TFPI at two sites and enhances the inhibitory activity of TFPI towards factor Xa.	Heparin	33-40	tissue factor pathway inhibitor	Homo sapiens	50-54
8840000-2	1996	Previous studies have shown that heparin binds to TFPI at two sites and enhances the inhibitory activity of TFPI towards factor Xa.	Heparin	33-40	tissue factor pathway inhibitor	Homo sapiens	108-112
8840000-3	1996	We have studied the effect of heparin of the TFPI-mediated inhibition of factor VIIa-relipidated tissue factor amiodolytic activity and factor VIIa-tissue factor proteolytic activity towards factor IX and factor X on a human bladder carcinoma cell line, J82.	Heparin	30-37	tissue factor pathway inhibitor	Homo sapiens	45-49
8840000-4	1996	The inhibitory activity of full-length TFPI on factor VIIa-tissue factor amidolytic and proteolytic activities was greatly enhanced by heparin, whereas the inhibitory activity of a truncated form of TFPI lacking the third Kunitz-type domain and carboxy-terminal tail (TFPI1-161) was not affected by heparin.	Heparin	135-142	tissue factor pathway inhibitor	Homo sapiens	39-43
8840000-5	1996	Optimal inhibition of factor VIIa-tissue factor by TFPI was observed at 0.1 U/ml heparin.	Heparin	81-88	tissue factor pathway inhibitor	Homo sapiens	51-55
11964399-7	2002	Heparin also inhibited N-Shh endocytosis, implicating proteoglycans in the internalization process, as has been described for other megalin ligands.	Heparin	0-7	LDL receptor related protein 2	Homo sapiens	132-139
8840000-6	1996	Heparin enhanced the inhibitory activity of TFPI towards factor Xa even in the presence of factor VIIa-tissue factor complexes in solution phase.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	44-48
8840000-7	1996	In addition, heparin augmented the ability of TFPI to inhibit factor VIIa-tissue factor amidolytic activity in the presence of active-site mutated factor X (S376A factor X).	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	46-50
8840000-8	1996	Our collective results suggest that heparin may play a significant role in augmenting the physiological regulation of factor VIIa-tissue factor activity by TFPI.	Heparin	36-43	tissue factor pathway inhibitor	Homo sapiens	156-160
8840001-0	1996	Anticoagulant effects and tissue factor pathway inhibitor after intrapulmonary low-molecular-weight heparin.	Heparin	100-107	tissue factor pathway inhibitor	Homo sapiens	26-57
8840001-1	1996	The present study was designed to investigate the anticoagulant action of inhaled low-molecular-weight (LMW) heparin on the release of tissue factor pathway inhibitor (TFPI) and on antifactor Xa activity, Heptest, activated partial thromboplastin time (APTT) and thrombin clotting time (TCT) in healthy volunteers.	Heparin	109-116	tissue factor pathway inhibitor	Homo sapiens	135-166
8840001-1	1996	The present study was designed to investigate the anticoagulant action of inhaled low-molecular-weight (LMW) heparin on the release of tissue factor pathway inhibitor (TFPI) and on antifactor Xa activity, Heptest, activated partial thromboplastin time (APTT) and thrombin clotting time (TCT) in healthy volunteers.	Heparin	109-116	tissue factor pathway inhibitor	Homo sapiens	168-172
8666820-9	1996	They were, however, at least partially charge mediated, since heparin abolished the effects of MBP on IL-1-stimulated cells, and the surrogate cationic molecule poly-L-arginine mimicked the stimulatory effects of MBP on fibroblast IL-6-type cytokine elaboration.	Heparin	62-69	myelin basic protein	Homo sapiens	95-98
8827835-2	1996	FGF-1 or FGF-2 in the presence of heparin resulted in a significantly greater cell viability for exudate cells at 24 hours of culture relative to heparin alone or medium controls.	Heparin	34-41	fibroblast growth factor 2	Mus musculus	9-14
8108596-9	1993	The authors stress the needing of other studies better understand the action to mechanisms of heparin and to evaluate possible future clinical applications of this new interesting Lp(a)-clearing effect.	Heparin	94-101	lipoprotein(a)	Homo sapiens	180-185
8303690-0	1993	Tissue factor pathway inhibitor (TFPI) and its response to heparin in patients with spontaneous deep vein thrombosis.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	0-31
8303690-0	1993	Tissue factor pathway inhibitor (TFPI) and its response to heparin in patients with spontaneous deep vein thrombosis.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	33-37
7506473-4	1993	For further biochemical characterization, bFGF was isolated from entire porcine thyroid glands by ammonium sulfate precipitation, cation exchange chromatography and heparin affinity chromatography.	Heparin	165-172	fibroblast growth factor 2	Gallus gallus	42-46
8827835-2	1996	FGF-1 or FGF-2 in the presence of heparin resulted in a significantly greater cell viability for exudate cells at 24 hours of culture relative to heparin alone or medium controls.	Heparin	146-153	fibroblast growth factor 2	Mus musculus	9-14
8827835-3	1996	Cultures supplemented with FGF-1 or FGF-2 plus heparin showed a slight increase in tritiated[3H] thymidine uptake over heparin or medium alone.	Heparin	119-126	fibroblast growth factor 2	Mus musculus	36-41
12413592-3	2002	Heparin-enhanced PCI inhibition of R93A/R97A/R101A thrombin was only approximately 2-fold compared to 40-fold enhancement with wild-type recombinant thrombin.	Heparin	0-7	serpin family A member 5	Homo sapiens	17-20
8222097-7	1993	Survival curves with Cox logistic regression analysis showed that the improvement in survival without myocardial infarction with heparin (P = .035) was independent of other baseline characteristics.	Heparin	129-136	cytochrome c oxidase subunit 8A	Homo sapiens	21-24
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	59-66	serpin family D member 1	Homo sapiens	0-4
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	139-146	serpin family D member 1	Homo sapiens	0-4
8231204-8	1993	When human plasma was incubated for 5 minutes with rabbit pericardium at reduced heparin concentrations, we found significant generation of thrombin (p &lt; 0.05) and plasmin (p &lt; 0.05).	Heparin	81-88	plasminogen	Homo sapiens	167-174
8218851-4	1993	Using an isolated, exsanguinated and perfused rat liver preparation we confirmed that the TH hepatic clearance is calcium-independent and affected by heparin; PK clearance rates both in the presence (t1/2 10 +/- 2 min) or the absence (t1/2 10 +/- 1 min) of heparin were similar; the presence of beta-galactosides does not impair the TH clearance but adversely affects the PK clearance and a large excess of TH does not impair the PK clearance rate (t1/2 6 +/- 1 min).	Heparin	257-264	kallikrein B1	Rattus norvegicus	159-161
8325873-0	1993	Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin.	Heparin	157-164	dystroglycan 1	Bos taurus	101-113
8325873-8	1993	LBP120/dystroglycan, either as a native protein, or following SDS-PAGE and transfer to nitrocellulose, binds with high affinity (Kd = 90 nM) to a proteolytic fragment of laminin (E3) containing the major heparin binding domain.	Heparin	204-211	dystroglycan 1	Bos taurus	7-19
8319565-8	1993	The immunological behavior of CBG was not significantly changed after heparin-induced lipolysis, but the immunoreactivity of CBG from heparin-treated rats was more reduced by incubation with exogenous FFA than that from controls.	Heparin	134-141	serpin family A member 6	Rattus norvegicus	125-128
8319565-9	1993	FFA extracted from the plasma of heparin-treated rats and a standard FFA mixture both produced a dose-dependent drop in the immunodetection of pure CBG.	Heparin	33-40	serpin family A member 6	Rattus norvegicus	148-151
8737629-5	1996	Pig mucosal heparins also have a significantly higher content of 3-O-sulfated glucosamine units, which are markers for the active site of heparin for antithrombin-III.	Heparin	12-20	serpin family C member 1	Sus scrofa	150-166
8737629-5	1996	Pig mucosal heparins also have a significantly higher content of 3-O-sulfated glucosamine units, which are markers for the active site of heparin for antithrombin-III.	Heparin	12-19	serpin family C member 1	Sus scrofa	150-166
8762610-0	1996	Lipoprotein lipase activity of post-heparin plasma in Japanese black cattle affected with fat necrosis.	Heparin	36-43	lipoprotein lipase	Bos taurus	0-18
8725726-4	1996	The presence of heparin (1 U/ml, unfractionated) was able to significantly reduce the binding of TFPI to phospholipid.	Heparin	16-23	tissue factor pathway inhibitor	Homo sapiens	97-101
8620887-0	1996	Human bone morphogenetic protein 2 contains a heparin-binding site which modifies its biological activity.	Heparin	46-53	bone morphogenetic protein 2	Homo sapiens	6-34
8620887-6	1996	This conclusion was supported by a variant EHBMP-2, where the N-terminal residues 1-12 of BMP-2 had been substituted by a dummy sequence of equal length and which showed an EC50 value of around 1 nM which was affected neither by heparin nor by peptide 1-17.	Heparin	229-236	bone morphogenetic protein 2	Homo sapiens	45-50
8620887-7	1996	A physical interaction between BMP-2 and heparin could be seen in biosensor experiments, where BMP-2 bound to immobilized heparin with a dissociation constant, Kd, of approximately 20 nM, whereas the heparin-binding of variant EHBMP-2 was negligible.	Heparin	41-48	bone morphogenetic protein 2	Homo sapiens	31-36
8620887-7	1996	A physical interaction between BMP-2 and heparin could be seen in biosensor experiments, where BMP-2 bound to immobilized heparin with a dissociation constant, Kd, of approximately 20 nM, whereas the heparin-binding of variant EHBMP-2 was negligible.	Heparin	41-48	bone morphogenetic protein 2	Homo sapiens	95-100
8620887-7	1996	A physical interaction between BMP-2 and heparin could be seen in biosensor experiments, where BMP-2 bound to immobilized heparin with a dissociation constant, Kd, of approximately 20 nM, whereas the heparin-binding of variant EHBMP-2 was negligible.	Heparin	122-129	bone morphogenetic protein 2	Homo sapiens	31-36
8620887-7	1996	A physical interaction between BMP-2 and heparin could be seen in biosensor experiments, where BMP-2 bound to immobilized heparin with a dissociation constant, Kd, of approximately 20 nM, whereas the heparin-binding of variant EHBMP-2 was negligible.	Heparin	122-129	bone morphogenetic protein 2	Homo sapiens	95-100
8620887-7	1996	A physical interaction between BMP-2 and heparin could be seen in biosensor experiments, where BMP-2 bound to immobilized heparin with a dissociation constant, Kd, of approximately 20 nM, whereas the heparin-binding of variant EHBMP-2 was negligible.	Heparin	122-129	bone morphogenetic protein 2	Homo sapiens	31-36
8620887-7	1996	A physical interaction between BMP-2 and heparin could be seen in biosensor experiments, where BMP-2 bound to immobilized heparin with a dissociation constant, Kd, of approximately 20 nM, whereas the heparin-binding of variant EHBMP-2 was negligible.	Heparin	122-129	bone morphogenetic protein 2	Homo sapiens	95-100
7686555-6	1993	Trimeric recombinant TSP1 containing NH2-terminal sequences truncated after the procollagen-like module inhibited endothelial cell migration in vitro and corneal neovascularization in vivo whereas trimeric molecules truncated before this domain were inactive as was the NH2-terminal heparin-binding domain that is present in both recombinant molecules.	Heparin	283-290	thrombospondin 1	Rattus norvegicus	21-25
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	139-146	serpin family D member 1	Homo sapiens	0-4
7692436-6	1993	Addition of 50 micrograms/ml heparin enhanced the in vitro activity of the aFGFs, reducing the half-maximal dose to approximately 100 pg/ml for both forms, comparable to that observed previously for basic FGF with or without heparin in this assay system.	Heparin	29-36	fibroblast growth factor 1	Bos taurus	76-79
8620887-8	1996	These results identify the basic N-terminal domains of dimeric BMP-2 as heparin-binding sites that are not obligatory for receptor activation but modulate its biological activity.	Heparin	72-79	bone morphogenetic protein 2	Homo sapiens	63-68
12413592-7	2002	These results suggest that PCI is similar to ATIII and depends upon ternary complex formation with heparin and these specific thrombin exosite-2 residues to accelerate thrombin inhibition.	Heparin	99-106	serpin family A member 5	Homo sapiens	27-30
7692436-6	1993	Addition of 50 micrograms/ml heparin enhanced the in vitro activity of the aFGFs, reducing the half-maximal dose to approximately 100 pg/ml for both forms, comparable to that observed previously for basic FGF with or without heparin in this assay system.	Heparin	225-232	fibroblast growth factor 1	Bos taurus	76-79
8786175-5	1996	As HGF is a heparin-binding growth factor and similar changes in HGF were observed during CVVHD, one possible explanation is that heparin administered as anticoagulant for extracorporeal circulation is involved in the effects observed on HGF.	Heparin	12-19	hepatocyte growth factor	Homo sapiens	3-6
12028043-0	2002	Tissue factor and tissue factor pathway inhibitor levels in unstable angina patients during short-term low-molecular-weight heparin administration.	Heparin	124-131	tissue factor pathway inhibitor	Homo sapiens	18-49
8868511-15	1996	of heparin resulted in a reduced rise in plasma PF 4 in YSMI as compared to healthy controls.	Heparin	3-10	platelet factor 4	Homo sapiens	48-52
8634431-3	1996	When factor Xa is added to mixtures containing TFPI, prothrombin, calcium ions, and nonactivated platelets or factor V and phospholipids, TFPI significantly reduces subsequent thrombin generation, and the inhibitory effect is enhanced by heparin.	Heparin	238-245	tissue factor pathway inhibitor	Homo sapiens	47-51
8634431-3	1996	When factor Xa is added to mixtures containing TFPI, prothrombin, calcium ions, and nonactivated platelets or factor V and phospholipids, TFPI significantly reduces subsequent thrombin generation, and the inhibitory effect is enhanced by heparin.	Heparin	238-245	tissue factor pathway inhibitor	Homo sapiens	138-142
8740352-3	1996	The heparin coating significantly reduced the concentrations of C3bc, TCC, fibrinopeptide A, lactoferrin, myeloperoxidase and beta-thromboglobulin.	Heparin	4-11	pro-platelet basic protein	Homo sapiens	126-146
8907299-5	1996	Moreover, it is clearly established that both kinds of heparins (unfractionated heparin and LMWHs) induce the release of tissue factor pathway inhibitor (TFPI).	Heparin	55-63	tissue factor pathway inhibitor	Homo sapiens	121-152
8907299-5	1996	Moreover, it is clearly established that both kinds of heparins (unfractionated heparin and LMWHs) induce the release of tissue factor pathway inhibitor (TFPI).	Heparin	55-63	tissue factor pathway inhibitor	Homo sapiens	154-158
8907299-5	1996	Moreover, it is clearly established that both kinds of heparins (unfractionated heparin and LMWHs) induce the release of tissue factor pathway inhibitor (TFPI).	Heparin	55-62	tissue factor pathway inhibitor	Homo sapiens	121-152
8907299-5	1996	Moreover, it is clearly established that both kinds of heparins (unfractionated heparin and LMWHs) induce the release of tissue factor pathway inhibitor (TFPI).	Heparin	55-62	tissue factor pathway inhibitor	Homo sapiens	154-158
8514454-0	1993	Ectopic production of heparin-binding growth factors and receptors for basic fibroblast growth factor by rat mammary epithelial cell lines derived from malignant metastatic tumours.	Heparin	22-29	fibroblast growth factor 2	Rattus norvegicus	71-101
8358152-0	1993	Mode of interaction between platelet factor 4 and heparin.	Heparin	50-57	platelet factor 4	Homo sapiens	28-45
8358152-1	1993	Platelet factor 4 (PF4) is a platelet-derived protein capable of binding to, and thus neutralizing, the biological activities of heparin and heparan sulphate.	Heparin	129-136	platelet factor 4	Homo sapiens	0-17
8358152-1	1993	Platelet factor 4 (PF4) is a platelet-derived protein capable of binding to, and thus neutralizing, the biological activities of heparin and heparan sulphate.	Heparin	129-136	platelet factor 4	Homo sapiens	19-22
8358152-2	1993	The mode of binding of PF4 to heparin was investigated in a comparative study also involving antithrombin (AT; previously shown to selectively bind a specific oligosaccharide sequence) and fibronectin (FN; non-specific electrostatic interaction).	Heparin	30-37	platelet factor 4	Homo sapiens	23-26
8358152-8	1993	These results indicate that the binding of PF4 to heparin occurs by relatively non-specific electrostatic interactions.	Heparin	50-57	platelet factor 4	Homo sapiens	43-46
8579370-7	1996	alpha 2M* and RAP can inhibit the binding of LDL to macrophages completely (96 and 100% inhibition, respectively), after cell surface heparin has been removed by treatment with heparinase.	Heparin	134-141	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	14-17
12047378-1	2002	Group IID secretory phospholipase A(2) (sPLA(2)-IID), a heparin-binding sPLA(2) that is closely related to sPLA(2)-IIA, augments stimulus-induced cellular arachidonate release in a manner similar to sPLA(2)-IIA.	Heparin	56-63	phospholipase A2 group IID	Homo sapiens	40-51
8777277-6	1996	The first increase may be due to the injection of heparin which releases HGF from the cell-surface and extracellular matrix of the liver.	Heparin	50-57	hepatocyte growth factor	Homo sapiens	73-76
8567685-8	1996	Experiments with selectively desulfated heparins indicated that 2-O-sulfated iduronic acid units, in particular, are of importance to the interaction with HB-GAM, were implicated to a lesser extent.	Heparin	40-48	pleiotrophin	Rattus norvegicus	155-161
7686196-8	1993	All staining by anti-bFGF sera is abolished with heparin in the reactions.	Heparin	49-56	fibroblast growth factor 2	Rattus norvegicus	21-25
11986215-6	2002	PF4 variants with impaired heparin binding lacked the capacity to inhibit LDL.	Heparin	27-34	platelet factor 4	Homo sapiens	0-3
7690390-5	1993	In the presence of heparin, stimulation of DNA synthesis at 25 micrograms bFGF/l was 1.6-fold greater than at a concentration of 1 microgram bFGF/l.	Heparin	19-26	fibroblast growth factor 2	Gallus gallus	74-78
7690390-5	1993	In the presence of heparin, stimulation of DNA synthesis at 25 micrograms bFGF/l was 1.6-fold greater than at a concentration of 1 microgram bFGF/l.	Heparin	19-26	fibroblast growth factor 2	Gallus gallus	141-145
7690390-6	1993	Addition of heparin to incubations containing aFGF reduced the concentration required for maximum stimulation of DNA synthesis to 1 microgram/l.	Heparin	12-19	fibroblast growth factor 1	Gallus gallus	46-50
8548430-17	1996	However, it would be interesting to study the increased levels of endothelium-derived TFPI in plasma induced by the injection of heparin.	Heparin	129-136	tissue factor pathway inhibitor	Homo sapiens	86-90
11861638-0	2002	Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase.	Heparin	36-43	furin, paired basic amino acid cleaving enzyme	Homo sapiens	0-5
8341025-0	1993	Effects of heparin on the inhibitory activities of human urinary trypsin inhibitor (ulinastatin) on trypsin, chymotrypsin and leukocyte elastase.	Heparin	11-18	elastase, neutrophil expressed	Homo sapiens	126-144
8817142-11	1996	The platelet release of beta-thromboglobulin increased in both groups during CPB and significantly more in the control group at the end of bypass (P &lt; 0.01), indicating less platelet activation in the heparin-coated group.	Heparin	204-211	pro-platelet basic protein	Homo sapiens	24-44
11799124-2	2002	In optical biosensor binding assays, competition by oligosaccharides for binding of HGF/SF to immobilized heparin showed that disaccharides failed to compete, whereas tetrasaccharides inhibited HGF/SF binding (IC(50) 8 microg/ml).	Heparin	106-113	hepatocyte growth factor	Homo sapiens	84-90
8568456-4	1996	One of the proteins co-migrated on SDS-PAGE gels and co-eluted from heparin-affinity columns with 18 kDa recombinant human PTN, suggesting its identity as the intact native porcine PTN (pPTN) molecule.	Heparin	68-75	pleiotrophin	Sus scrofa	181-184
8713780-3	1996	In the heparin tube, APC reacts completely and irreversibly with its major plasma inhibitors, protein C inhibitor (PCI) and alpha 1-antitrypsin (alpha 1AT), and the complexes formed are measured by ELISAs.	Heparin	7-14	APC regulator of WNT signaling pathway	Homo sapiens	21-24
8747526-3	1996	VCL inhibited 50% of vWf binding to heparin, but it did not inhibit vWf binding to type I collagen.	Heparin	36-43	vinculin	Homo sapiens	0-3
8473484-5	1993	Inhibition of [3H]NMS binding by MBP was reversible by treatment with heparin, which binds and neutralizes MBP.	Heparin	70-77	myelin basic protein	Homo sapiens	33-36
8473484-5	1993	Inhibition of [3H]NMS binding by MBP was reversible by treatment with heparin, which binds and neutralizes MBP.	Heparin	70-77	myelin basic protein	Homo sapiens	107-110
11799124-7	2002	Heparin-derived oligosaccharides from dp 2 to dp 24 were added together with HGF/SF to chlorate-treated cells to determine the minimum size of oligosaccharides able to restore HGF/SF activity.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	176-182
8473549-0	1993	Antihypertensive action of heparin: role of the renin-angiotensin aldosterone system and prostaglandins.	Heparin	27-34	renin	Rattus norvegicus	48-53
8473549-8	1993	A significant (P &lt; .001) increase in plasma renin activity was found in heparin-treated SHRs and NWRs; however, a corresponding elevation of plasma aldosterone level was noted only in heparin-treated NWR.	Heparin	75-82	renin	Rattus norvegicus	47-52
8454611-15	1993	Heparin inhibited recombinant casein kinase I delta when phosvitin was the substrate, with half-maximal inhibition at 11.5 micrograms/ml.	Heparin	0-7	casein kinase 1, epsilon	Rattus norvegicus	30-45
8454611-17	1993	A truncated form of casein kinase I delta, lacking the COOH-terminal 111 amino acids, was no longer activated by heparin.	Heparin	113-120	casein kinase 1, epsilon	Rattus norvegicus	20-35
8454611-18	1993	Casein kinase I delta therefore represents a separate member of the casein kinase I family distinguished by its larger size and unique kinetic behavior with respect to heparin.	Heparin	168-175	casein kinase 1, epsilon	Rattus norvegicus	0-15
8454611-18	1993	Casein kinase I delta therefore represents a separate member of the casein kinase I family distinguished by its larger size and unique kinetic behavior with respect to heparin.	Heparin	168-175	casein kinase 1, epsilon	Rattus norvegicus	68-83
8772238-0	1995	On the role of platelet Fc gamma RIIa phenotype in heparin-induced thrombocytopenia.	Heparin	51-58	Fc gamma receptor IIa	Homo sapiens	24-37
8585041-0	1995	Full-length human tissue factor pathway inhibitor inhibits human activated protein C in the presence of heparin.	Heparin	104-111	tissue factor pathway inhibitor	Homo sapiens	18-49
11916630-0	2002	Binding of heparin to human thyroglobulin (Tg) involves multiple binding sites including a region corresponding to a binding site of rat Tg.	Heparin	11-18	thyroglobulin	Homo sapiens	28-41
8585041-0	1995	Full-length human tissue factor pathway inhibitor inhibits human activated protein C in the presence of heparin.	Heparin	104-111	APC regulator of WNT signaling pathway	Homo sapiens	65-84
8585041-3	1995	TFPI readily inhibited APC amidolytic activity only in the presence of heparin, whereas TFPI1-161 failed to inhibit APC amidolytic activity in the presence or absence of heparin.	Heparin	71-78	tissue factor pathway inhibitor	Homo sapiens	0-4
8585041-4	1995	Optimal inhibition of APC by TFPI was observed at 1 U/ml heparin.	Heparin	57-64	APC regulator of WNT signaling pathway	Homo sapiens	22-25
8585041-4	1995	Optimal inhibition of APC by TFPI was observed at 1 U/ml heparin.	Heparin	57-64	tissue factor pathway inhibitor	Homo sapiens	29-33
8585041-5	1995	The results of competition studies between factor Xa and APC for inhibition by TFPI in the presence of heparin suggested that the second Kunitz-type domain in TFPI was responsible for the inhibition of APC.	Heparin	103-110	APC regulator of WNT signaling pathway	Homo sapiens	57-60
8585041-5	1995	The results of competition studies between factor Xa and APC for inhibition by TFPI in the presence of heparin suggested that the second Kunitz-type domain in TFPI was responsible for the inhibition of APC.	Heparin	103-110	tissue factor pathway inhibitor	Homo sapiens	79-83
8585041-5	1995	The results of competition studies between factor Xa and APC for inhibition by TFPI in the presence of heparin suggested that the second Kunitz-type domain in TFPI was responsible for the inhibition of APC.	Heparin	103-110	tissue factor pathway inhibitor	Homo sapiens	159-163
8382315-4	1993	The expressed BMRF1 gene products were purified to near homogeneity from the nuclear extract of the recombinant baculovirus-infected insect cells by double-stranded DNA-cellulose column chromatography followed by heparin-agarose column chromatography.	Heparin	213-220	BMRF1	Human gammaherpesvirus 4	14-19
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Heparin	83-90	serpin family D member 1	Homo sapiens	59-63
8585041-5	1995	The results of competition studies between factor Xa and APC for inhibition by TFPI in the presence of heparin suggested that the second Kunitz-type domain in TFPI was responsible for the inhibition of APC.	Heparin	103-110	APC regulator of WNT signaling pathway	Homo sapiens	202-205
8449008-2	1993	In calvariae treated for 24h with heparin (25 micrograms/ml), a significant inhibition of methyl [3H]thymidine (Tdr) incorporation into DNA and [3H]proline labeling of collagenase-digestible protein (CDP) occurred compared to control.	Heparin	34-41	cut-like homeobox 1	Rattus norvegicus	168-198
11916630-1	2002	OBJECTIVE: Binding of thyroglobulin (Tg) to heparin allows efficient Tg interaction with its endocytic receptor, megalin.	Heparin	44-51	thyroglobulin	Homo sapiens	22-35
8449008-2	1993	In calvariae treated for 24h with heparin (25 micrograms/ml), a significant inhibition of methyl [3H]thymidine (Tdr) incorporation into DNA and [3H]proline labeling of collagenase-digestible protein (CDP) occurred compared to control.	Heparin	34-41	cut-like homeobox 1	Rattus norvegicus	200-203
8449008-5	1993	Basic FGF in combination with heparin overcame the inhibitory effects of heparin on Tdr incorporation.	Heparin	73-80	fibroblast growth factor 2	Rattus norvegicus	6-9
7583565-10	1995	In vivo, HGF induced a dose-dependent angiogenic response, which was enhanced by heparin.	Heparin	81-88	hepatocyte growth factor	Homo sapiens	9-12
11916630-1	2002	OBJECTIVE: Binding of thyroglobulin (Tg) to heparin allows efficient Tg interaction with its endocytic receptor, megalin.	Heparin	44-51	LDL receptor related protein 2	Homo sapiens	113-120
8449008-6	1993	The combination of bFGF plus heparin produced an even greater inhibition of CDP labeling than either effector alone.	Heparin	29-36	cut-like homeobox 1	Rattus norvegicus	76-79
11916630-9	2002	Heparin bound to synthetic peptides corresponding to the rat (rTgP) and to the human (hTgP) Tg sequence 2489-2503.	Heparin	0-7	transglutaminase 4	Homo sapiens	86-90
11916630-11	2002	An antibody against hTgP reduced binding of heparin to intact hTg by 30%, suggesting that in hTg this region is, in part, involved in heparin binding, but also that other regions account for most of the binding.	Heparin	44-51	transglutaminase 4	Homo sapiens	20-24
11916630-11	2002	An antibody against hTgP reduced binding of heparin to intact hTg by 30%, suggesting that in hTg this region is, in part, involved in heparin binding, but also that other regions account for most of the binding.	Heparin	134-141	transglutaminase 4	Homo sapiens	20-24
7592623-4	1995	FGF-2-dependent attachment of 32D-flg cells was prevented by inclusion of 10 micrograms/ml heparin in the incubation medium and was diminished when CHO mutants in glycosaminoglycan synthesis or wild-type CHO cells treated with heparinase were used, indicating that the attachment occurred through FGF-2 interactions with heparan sulfates on the CHO cells.	Heparin	91-98	fibroblast growth factor 2	Cricetulus griseus	0-5
11853545-5	2002	In addition, inhibition of phosphorylation by heparin and stimulation by spermidine indicate that the activity can be ascribed to CK2.	Heparin	46-53	casein kinase 2 beta S homeolog	Xenopus laevis	130-133
7592623-9	1995	In addition, induction of DNA synthesis in 32D-flg cells in response to FGF-2 was potentiated by the CHO-associated heparan sulfates to the same extent as by soluble heparin, indicating that this interaction has functional significance.	Heparin	166-173	fibroblast growth factor 2	Cricetulus griseus	72-77
7592624-7	1995	A comparison of two mammary epithelial cell lines showed a marked difference of potency and dependence upon heparin in their response to mouse Fgf3, suggesting a complex interaction between the ligand and its low and high affinity receptors.	Heparin	108-115	fibroblast growth factor 3	Mus musculus	143-147
7559536-5	1995	In this assay, full-length muPECAM-1 and all three isoforms containing exon 14 behaved like human PECAM-1 in that they mediated calcium- and heparin-dependent heterophilic aggregation.	Heparin	141-148	platelet and endothelial cell adhesion molecule 1	Homo sapiens	29-36
8653419-1	1995	The heparin-binding, growth-associated molecule (HB-GAM) is a developmentally regulated protein that belongs to a new family of heparin-binding molecules, not related to the fibroblast growth factors (FGFs), with putative functions during cell growth and differentiation.	Heparin	4-11	pleiotrophin	Rattus norvegicus	49-55
1334078-7	1992	However, heparin inhibited binding of SP-A in a concentration-dependent manner.	Heparin	9-16	surfactant protein A1	Homo sapiens	38-42
1334078-8	1992	In addition, heparin could also dissociate cell-bound SP-A, indicating that polyanionic oligosaccharides are involved in the binding of SP-A to virus-infected cells.	Heparin	13-20	surfactant protein A1	Homo sapiens	54-58
1334078-8	1992	In addition, heparin could also dissociate cell-bound SP-A, indicating that polyanionic oligosaccharides are involved in the binding of SP-A to virus-infected cells.	Heparin	13-20	surfactant protein A1	Homo sapiens	136-140
1450176-8	1992	Release of cell surface-associated LPL was assessed with the use of heparin.	Heparin	68-75	lipoprotein lipase	Bos taurus	35-38
1450176-9	1992	Less heparin was required to dissociate apical-surface LPL.	Heparin	5-12	lipoprotein lipase	Bos taurus	55-58
8653419-13	1995	HB-GAM, which possesses a classical signal sequence, might be release in the extracellular space and could mediate adhesion phenomena by binding to heparin-like molecules associated with the neuronal membrane.	Heparin	148-155	pleiotrophin	Rattus norvegicus	0-6
11861437-15	2002	PAPP-A was stable at 4 degrees C for at least 18 days in serum and for 8 days in heparin-derived whole blood or plasma.	Heparin	81-88	pappalysin 1	Homo sapiens	0-6
7547867-3	1995	A chimeric mutant of PF4 (called PF4-M2) which substitutes the first 11 N-terminal residues for the first eight residues from homologous interleukin-8 forms symmetric homo-tetramers with essentially the same heparin binding activity as native PF4.	Heparin	208-215	platelet factor 4	Homo sapiens	21-24
1484504-5	1992	Osteogenin was isolated from demineralized baboon bone matrix and purified by chromatography on heparin-Sepharose, hydroxyapatite, and Sephacryl S-200.	Heparin	96-103	bone morphogenetic protein 3	Homo sapiens	0-10
1428206-2	1992	Heparin-assisted dialysis resulted in a significant rise of VIII:C and AT III; with defibrotide, instead, there was evidence of thrombin activation (increased FPA and TAT).	Heparin	0-7	cytochrome c oxidase subunit 8A	Homo sapiens	60-64
7547867-3	1995	A chimeric mutant of PF4 (called PF4-M2) which substitutes the first 11 N-terminal residues for the first eight residues from homologous interleukin-8 forms symmetric homo-tetramers with essentially the same heparin binding activity as native PF4.	Heparin	208-215	platelet factor 4	Homo sapiens	33-39
11857593-9	2002	RESULTS: LPSb bound promptly to monocytes in EDTA- and heparin-treated blood.	Heparin	55-62	selenium binding protein 1	Homo sapiens	9-13
7547867-3	1995	A chimeric mutant of PF4 (called PF4-M2) which substitutes the first 11 N-terminal residues for the first eight residues from homologous interleukin-8 forms symmetric homo-tetramers with essentially the same heparin binding activity as native PF4.	Heparin	208-215	platelet factor 4	Homo sapiens	33-36
8585024-0	1995	Thrombotic risk during pregnancy and puerperium in women with APC-resistance--effective subcutaneous heparin prophylaxis in a pregnant patient.	Heparin	101-108	APC regulator of WNT signaling pathway	Homo sapiens	62-65
7797488-3	1995	The binding of 125I-VEGF165 to the VEGF receptors of endothelial cells, and the heparin-dependent binding of 125I-VEGF165 to a soluble extracellular domain of the VEGF receptor KDR/flk-1, were inhibited by the angiogenesis inhibitor platelet factor-4 (PF4).	Heparin	80-87	platelet factor 4	Homo sapiens	252-255
1525165-1	1992	Low molecular mass heparin (5.1 kDa) forms a tight complex with mucus proteinase inhibitor, the physiologic neutrophil elastase inhibitor of the upper respiratory tract.	Heparin	19-26	elastase, neutrophil expressed	Homo sapiens	108-127
1525165-8	1992	Heparin accelerates the inhibition of elastase in a concentration-dependent manner.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	38-46
1515082-0	1992	Heparin interferes with the inhibition of neutrophil elastase by its physiological inhibitors.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	42-61
1515082-1	1992	Heparin depresses the second-order rate constant kass for the inhibition of neutrophil elastase by alpha 1-proteinase inhibitor.	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	76-95
7797488-6	1995	Since PF4 mutants lacking a heparin binding ability retain their anti-angiogenic activity, alternative inhibitory mechanisms were also examined.	Heparin	28-35	platelet factor 4	Homo sapiens	6-9
7797488-8	1995	The binding of 125I-PF4 to the VEGF165-coated wells was inhibited by several types of heparin binding proteins, including unlabeled PF4 and unlabeled VEGF165.	Heparin	86-93	platelet factor 4	Homo sapiens	20-23
11857593-13	2002	CONCLUSION: Detection of membrane-bound LPSb on monocytes differed in EDTA or heparin-treated blood, and cell activation was better obtained in heparinized blood.	Heparin	78-85	selenium binding protein 1	Homo sapiens	40-44
7797488-8	1995	The binding of 125I-PF4 to the VEGF165-coated wells was inhibited by several types of heparin binding proteins, including unlabeled PF4 and unlabeled VEGF165.	Heparin	86-93	platelet factor 4	Homo sapiens	132-135
1376317-6	1992	Binding of Lys-plasminogen and active-site-blocked plasmin was at least 10-fold higher in affinity (KD = 85-100 nM) compared to Glu-plasminogen (KD approximately 1 microM) and could be inhibited by lysine analogs but not by glycosaminoglycans or PAI-1, indicating that heteropolar plasmin(ogen) binding of VN occurs to an adjacent segment upstream to the heparin and PAI-1-binding sites.	Heparin	355-362	plasminogen	Homo sapiens	15-22
1376317-6	1992	Binding of Lys-plasminogen and active-site-blocked plasmin was at least 10-fold higher in affinity (KD = 85-100 nM) compared to Glu-plasminogen (KD approximately 1 microM) and could be inhibited by lysine analogs but not by glycosaminoglycans or PAI-1, indicating that heteropolar plasmin(ogen) binding of VN occurs to an adjacent segment upstream to the heparin and PAI-1-binding sites.	Heparin	355-362	plasminogen	Homo sapiens	51-58
11723110-0	2002	The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells.	Heparin	67-74	S100 calcium binding protein A8	Homo sapiens	29-34
1381850-4	1992	HCII was purified from the supernatant of barium citrate adsorbed normal human plasma by polyethylene glycol precipitation followed by affinity chromatography on heparin-Sepharose CL-6B and ion-exchange chromatography on a QAE-Sephadex A-50.	Heparin	162-169	serpin family D member 1	Homo sapiens	0-4
1381850-8	1992	Using 0.03U/ml thrombin and 1nM HCII the stimulatory effect of GAGs was completely inhibited when Hep (less than or equal to 0.3 micrograms/ml) was preincubated with VN (60 micrograms/ml) and decreased to less than 50% when HS (50 micrograms/ml) was preincubated with VN (60 micrograms/ml).	Heparin	98-101	serpin family D member 1	Homo sapiens	32-36
7658169-1	1995	Phospholipid transfer protein (PLTP) from pig plasma was purified to homogeneity using ultracentrifugation and a combination of hydrophobic-, heparin-Sepharose-, and anti-pig-PLTP-affinity chromatography techniques.	Heparin	142-149	PLTP	Sus scrofa	0-29
7658169-1	1995	Phospholipid transfer protein (PLTP) from pig plasma was purified to homogeneity using ultracentrifugation and a combination of hydrophobic-, heparin-Sepharose-, and anti-pig-PLTP-affinity chromatography techniques.	Heparin	142-149	PLTP	Sus scrofa	31-35
7697848-2	1995	Platelet factor 4 (PF4) is a protein found in platelet alpha granules that binds to and thereby neutralizes heparin.	Heparin	108-115	platelet factor 4	Homo sapiens	19-22
7697848-3	1995	We evaluated the safety and effectiveness of intravenous recombinant PF4 to neutralize heparin anticoagulation after cardiac catheterization in a phase 1, open-label trial.	Heparin	87-94	platelet factor 4	Homo sapiens	69-72
7697848-14	1995	At lower doses, rPF4 neutralized the effects of heparin in most but not all patients.	Heparin	48-55	platelet factor 4	Rattus norvegicus	16-20
7697848-18	1995	Given in sufficient amounts, rPF4 can completely and rapidly reverse the anticoagulant effects of heparin.	Heparin	98-105	platelet factor 4	Rattus norvegicus	29-33
1374012-2	1992	In calvariae treated for 96 h, heparin (25 micrograms/ml) and bFGF (10(-9) M) inhibited collagenase-digestible protein (CDP) labeling by 52 and 60% of control, respectively, and the combination further inhibited CDP labeling.	Heparin	31-38	cut-like homeobox 1	Rattus norvegicus	88-118
1374012-2	1992	In calvariae treated for 96 h, heparin (25 micrograms/ml) and bFGF (10(-9) M) inhibited collagenase-digestible protein (CDP) labeling by 52 and 60% of control, respectively, and the combination further inhibited CDP labeling.	Heparin	31-38	cut-like homeobox 1	Rattus norvegicus	120-123
1374012-2	1992	In calvariae treated for 96 h, heparin (25 micrograms/ml) and bFGF (10(-9) M) inhibited collagenase-digestible protein (CDP) labeling by 52 and 60% of control, respectively, and the combination further inhibited CDP labeling.	Heparin	31-38	cut-like homeobox 1	Rattus norvegicus	212-215
1374012-3	1992	Inhibition of CDP labeling by heparin (25 micrograms/ml) or bFGF (10(-9), 10(-8) M) was similar in the presence or absence of aphidicolin (30 microM) an inhibitor of cell replication.	Heparin	30-37	cut-like homeobox 1	Rattus norvegicus	14-17
1374012-4	1992	Heparin selectively inhibited CDP labeling in the osteoblast rich central bone but bFGF alone or in combination with heparin inhibited CDP labeling both in the periosteum and central bone.	Heparin	0-7	cut-like homeobox 1	Rattus norvegicus	30-33
1374012-4	1992	Heparin selectively inhibited CDP labeling in the osteoblast rich central bone but bFGF alone or in combination with heparin inhibited CDP labeling both in the periosteum and central bone.	Heparin	117-124	cut-like homeobox 1	Rattus norvegicus	135-138
1374012-6	1992	A high concentration of insulin-like growth factor-1 (IGF-1, 3 x 10(-8) M) reversed the inhibitory effect of heparin on DNA synthesis and CDP labeling.	Heparin	109-116	cut-like homeobox 1	Rattus norvegicus	138-141
11854880-0	2002	Tissue factor pathway inhibitor antigen and activity in 96 patients receiving heparin for cardiopulmonary bypass.	Heparin	78-85	tissue factor pathway inhibitor	Homo sapiens	0-31
1569053-4	1992	Heparin, which inhibits the binding of InsP3 to its receptor, prevented the migration of Ca2+ waves induced by a poorly metabolized InsP3 (InsP3S3).	Heparin	0-7	carbonic anhydrase 2 L homeolog	Xenopus laevis	89-92
7534900-6	1995	The level of p185erbB-2 tyrosine phosphorylation-stimulating activity in the heparin-Sepharose fractions correlated directly with their content in NDF-like protein as immunodetected with an anti-rat NDF antibody.	Heparin	77-84	neuregulin 1	Homo sapiens	147-150
7858274-0	1995	Importance of PF4 in heparin-induced thrombocytopenia: confirmation with gray platelets.	Heparin	21-28	platelet factor 4	Homo sapiens	14-17
11854880-1	2002	OBJECTIVE: To identify patients with poor tissue factor pathway inhibitor (TFPI) response to heparin and observe any association with increased risk of excessive coagulation activation, morbidity, or mortality.	Heparin	93-100	tissue factor pathway inhibitor	Homo sapiens	42-73
7873546-1	1995	Heparin accelerates the inhibition of neutrophil elastase by mucus proteinase inhibitor (MPI), the physiological antielastase of airways as a result of its binding with the inhibitor [Faller, B., Mely, Y., Gerard, D., &amp; Bieth, J. G. (1992) Biochemistry 31, 8285-8290].	Heparin	0-7	elastase, neutrophil expressed	Homo sapiens	38-57
1562726-3	1992	Wild-type recombinant TFPI (rTFPI), expressed in mouse C127 cells, separates into two forms on heparin-agarose chromatography that elute at 0.3 mol/L and 0.6 mol/L NaCl.	Heparin	95-102	tissue factor pathway inhibitor	Rattus norvegicus	28-33
11854880-1	2002	OBJECTIVE: To identify patients with poor tissue factor pathway inhibitor (TFPI) response to heparin and observe any association with increased risk of excessive coagulation activation, morbidity, or mortality.	Heparin	93-100	tissue factor pathway inhibitor	Homo sapiens	75-79
11854880-12	2002	CONCLUSION: The TFPI response to heparin is heterogenous.	Heparin	33-40	tissue factor pathway inhibitor	Homo sapiens	16-20
1537108-6	1992	The anticoagulant activity of heparin was effectively reversed by all of the neutralizing agents (PS, PF4, and rPF4).	Heparin	30-37	platelet factor 4	Rattus norvegicus	102-105
7852353-6	1995	Recombinant thrombospondin-4 has been purified from the culture supernatant by heparin-Sepharose and anti-thrombospondin-4 antibody-Affi-gel affinity chromatography.	Heparin	79-86	thrombospondin 4	Homo sapiens	12-28
7852353-9	1995	These data indicate that thrombospondin-4 is a pentameric protein that binds to heparin and calcium.	Heparin	80-87	thrombospondin 4	Homo sapiens	25-41
1537108-6	1992	The anticoagulant activity of heparin was effectively reversed by all of the neutralizing agents (PS, PF4, and rPF4).	Heparin	30-37	platelet factor 4	Rattus norvegicus	111-115
11801647-0	2002	Heparin induces differentiation of CD1a+ dendritic cells from monocytes: phenotypic and functional characterization.	Heparin	0-7	CD1a molecule	Homo sapiens	35-39
1537108-9	1992	CONCLUSIONS: These results suggest that PF4 efficiently reverses heparin anticoagulation in the rat without the adverse effects of heparin-protamine complexes.	Heparin	65-72	platelet factor 4	Rattus norvegicus	40-43
11801647-4	2002	In this study, we demonstrate for the first time that heparin can reliably induce differentiation of CD1a+ DCs from monocytes with or without autologous serum or plasma.	Heparin	54-61	CD1a molecule	Homo sapiens	101-105
1319618-5	1992	Addition of leukocytes stimulated with endotoxin plus FMLP to cultured endothelial cells induced release of TM antigen to the medium accompanying cell injury as measured by 51Cr release, which was prevented by treatment with heparin.	Heparin	225-232	thrombomodulin	Oryctolagus cuniculus	108-110
7836453-3	1995	We show that a high affinity interaction between heparin and prochymase allows the 2-residue propeptide to be cleaved by dipeptidylpeptidase I.	Heparin	49-56	cathepsin C	Homo sapiens	121-142
7836453-7	1995	These observations indicate that heparin is an important cofactor in the prochymase activation process and explain how dipeptidylpeptidase I, a nonspecific processing enzyme, can effect a specific cleavage of the zymogen propeptide.	Heparin	33-40	cathepsin C	Homo sapiens	119-140
1319618-6	1992	It was suggested that the increase in plasma TM antigen level in parallel with the generation of DIC reflected endothelial injury of rabbits, and that the elevation of TM antigen and the endothelial cell injury were prevented by heparin treatment.	Heparin	229-236	thrombomodulin	Oryctolagus cuniculus	45-47
11801647-5	2002	The development of CD1a+ DCs is heparin concentration dependent (0-50 U/ml).	Heparin	32-39	CD1a molecule	Homo sapiens	19-23
1319618-6	1992	It was suggested that the increase in plasma TM antigen level in parallel with the generation of DIC reflected endothelial injury of rabbits, and that the elevation of TM antigen and the endothelial cell injury were prevented by heparin treatment.	Heparin	229-236	thrombomodulin	Oryctolagus cuniculus	168-170
1371276-2	1992	Previous experiments have shown that heparin inhibits induction of c-fos and c-myc protooncogene mRNA in rat VSMC stimulated by phorbol 12-myristate 13-acetate (PMA) but not when stimulated by epidermal growth factor (EGF) (Pukac, L. A., Castellot, J. J., Wright, T. C., Caleb, B. L., and Karnovsky, M. J.	Heparin	37-44	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	77-82
1371276-2	1992	Previous experiments have shown that heparin inhibits induction of c-fos and c-myc protooncogene mRNA in rat VSMC stimulated by phorbol 12-myristate 13-acetate (PMA) but not when stimulated by epidermal growth factor (EGF) (Pukac, L. A., Castellot, J. J., Wright, T. C., Caleb, B. L., and Karnovsky, M. J.	Heparin	37-44	epidermal growth factor like 1	Rattus norvegicus	193-216
1371276-2	1992	Previous experiments have shown that heparin inhibits induction of c-fos and c-myc protooncogene mRNA in rat VSMC stimulated by phorbol 12-myristate 13-acetate (PMA) but not when stimulated by epidermal growth factor (EGF) (Pukac, L. A., Castellot, J. J., Wright, T. C., Caleb, B. L., and Karnovsky, M. J.	Heparin	37-44	epidermal growth factor like 1	Rattus norvegicus	218-221
7479228-0	1995	[Plasma activity of diamine oxidase after heparin in patients with diabetic enteropathy].	Heparin	42-49	amine oxidase copper containing 1	Homo sapiens	20-35
7479228-12	1995	After injection of heparin a very high DAO activity was observed in all groups (&gt; 400 pmol/min/ml) except group IV (&lt; 270 pmol/min/ml) (p &lt; 0.001).	Heparin	19-26	amine oxidase copper containing 1	Homo sapiens	39-42
7840621-9	1995	Finally, addition of exogenous heparin restored bFGF binding to chlorate-treated chondrocytes in a concentration-dependent manner.	Heparin	31-38	fibroblast growth factor 2	Rattus norvegicus	48-52
8619928-7	1995	In conclusion FGF9 presents a unique case of ligand-receptor specificity and fulfills the criteria as a high affinity, heparin-dependent ligand for FGFR3.	Heparin	119-126	fibroblast growth factor receptor 3	Mus musculus	148-153
11801647-6	2002	Comparing with CD1a- DCs developed without heparin, CD1a+ DCs express higher CD40 and CD80 and lower CD86.	Heparin	43-50	CD1a molecule	Homo sapiens	52-56
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	79-86	complement component 4 binding protein, alpha	Rattus norvegicus	44-54
7477621-6	1995	Consequently, serum HGF is elevated in CRF, which may be attributed to the increased production of HGF in response to the chronic renal injury, the effect of heparin, or reduced removal of serum HGF in CRF patients.	Heparin	158-165	hepatocyte growth factor	Homo sapiens	20-23
1320301-5	1992	The effect of heparin and heparan sulfate was independent and synergic with respect to thrombomodulin.	Heparin	14-21	thrombomodulin	Oryctolagus cuniculus	87-101
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	79-86	complement component 4 binding protein	Mus musculus	45-49
7740492-1	1995	As heparin-PF4 (H-PF4) complexes are the target for antibodies associated to heparin-induced thrombocytopenia (HIT), an ELISA has been developed and optimised for testing antibodies binding to H-PF4.	Heparin	3-10	platelet factor 4	Homo sapiens	18-21
7740492-5	1995	Surprisingly, among 41 patients under heparin for &gt; 7 days, 5 showed antibodies to H-PF4, without HIT.	Heparin	38-45	platelet factor 4	Homo sapiens	88-91
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	141-148	complement component 4 binding protein, alpha	Rattus norvegicus	44-54
7740492-8	1995	The mechanism for HIT involves platelet PF4 receptors which bind the macromolecular H-PF4 complexes formed in the presence of a well defined heparin/PF4 ratio.	Heparin	141-148	platelet factor 4	Homo sapiens	40-43
7740492-8	1995	The mechanism for HIT involves platelet PF4 receptors which bind the macromolecular H-PF4 complexes formed in the presence of a well defined heparin/PF4 ratio.	Heparin	141-148	platelet factor 4	Homo sapiens	86-89
1372267-11	1992	Heparin augmented the effect of bFGF.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	32-36
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Heparin	105-112	serpin family D member 1	Homo sapiens	0-19
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	141-148	complement component 4 binding protein	Mus musculus	45-49
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Heparin	105-112	serpin family D member 1	Homo sapiens	21-25
7740492-8	1995	The mechanism for HIT involves platelet PF4 receptors which bind the macromolecular H-PF4 complexes formed in the presence of a well defined heparin/PF4 ratio.	Heparin	141-148	platelet factor 4	Homo sapiens	86-89
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	141-148	complement component 4 binding protein	Mus musculus	171-181
1319617-2	1992	Both HRG and PF4 effectively neutralized the ability of heparin to accelerate the activated protein C (APC) and the thrombin inhibitions by protein C inhibitor (PCI).	Heparin	56-63	platelet factor 4	Homo sapiens	13-16
1319617-2	1992	Both HRG and PF4 effectively neutralized the ability of heparin to accelerate the activated protein C (APC) and the thrombin inhibitions by protein C inhibitor (PCI).	Heparin	56-63	serpin family A member 5	Homo sapiens	140-159
11706034-6	2002	We have found that Noggin binds strongly to heparin in vitro, and to heparan sulfate proteoglycans on the surface of cultured cells.	Heparin	44-51	noggin	Homo sapiens	19-25
7528211-6	1994	268, 2984-2988) that heparin potentiates the mitogenic activity of acidic FGF (aFGF) but inhibits that of the keratinocyte growth factor (KGF) in cells that express the KGF receptor (KGFR).	Heparin	21-28	fibroblast growth factor receptor 2	Mus musculus	183-187
7528211-10	1994	Low concentrations of heparin inhibited the binding of KGF to the KGFR.	Heparin	22-29	fibroblast growth factor receptor 2	Mus musculus	66-70
11706034-7	2002	Noggin is detected only on the surface of cells that express heparan sulfate, can be specifically displaced from cells by heparin, and can be directly cross-linked to a cell surface proteoglycan in culture.	Heparin	122-129	noggin	Homo sapiens	0-6
7528211-12	1994	The effect of heparin was not unique to L6E9 cells expressing the KGFR; it was also observed in Balb/MK cells that naturally express KGFR.	Heparin	14-21	fibroblast growth factor receptor 2	Mus musculus	66-70
1346095-0	1992	Lipoprotein-associated coagulation inhibitor (LACI) is a cofactor for heparin: synergistic anticoagulant action between LACI and sulfated polysaccharides.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	0-44
7528211-12	1994	The effect of heparin was not unique to L6E9 cells expressing the KGFR; it was also observed in Balb/MK cells that naturally express KGFR.	Heparin	14-21	fibroblast growth factor receptor 2	Mus musculus	133-137
7534313-2	1994	Here we show that RHAMM also contains binding sites for heparin (HP) and that interaction of HP with these sites can regulate the locomotion of ras-transformed fibroblasts.	Heparin	56-63	hyaluronan mediated motility receptor	Homo sapiens	18-23
7534313-2	1994	Here we show that RHAMM also contains binding sites for heparin (HP) and that interaction of HP with these sites can regulate the locomotion of ras-transformed fibroblasts.	Heparin	65-67	hyaluronan mediated motility receptor	Homo sapiens	18-23
7534313-2	1994	Here we show that RHAMM also contains binding sites for heparin (HP) and that interaction of HP with these sites can regulate the locomotion of ras-transformed fibroblasts.	Heparin	93-95	hyaluronan mediated motility receptor	Homo sapiens	18-23
7534313-6	1994	In ligand blotting assays, GST-RHAMM fusion protein was shown to bind biotin-labelled HP and this binding was displaceable with unlabelled HP.	Heparin	86-88	hyaluronan mediated motility receptor	Homo sapiens	31-36
1346095-0	1992	Lipoprotein-associated coagulation inhibitor (LACI) is a cofactor for heparin: synergistic anticoagulant action between LACI and sulfated polysaccharides.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	46-50
1346095-0	1992	Lipoprotein-associated coagulation inhibitor (LACI) is a cofactor for heparin: synergistic anticoagulant action between LACI and sulfated polysaccharides.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	120-124
1346095-3	1992	Both LACI-depleted plasma and normal plasma have identical APTTs and similar prolongations of the APTT in response to heparin; both are fully anticoagulated (arbitrarily defined as clotting times of greater than 1 hour) at similar concentrations of heparin.	Heparin	118-125	tissue factor pathway inhibitor	Homo sapiens	5-9
1346095-6	1992	However, in the presence of heparin, the PTs of LACI-depleted plasma and normal plasma are different.	Heparin	28-35	tissue factor pathway inhibitor	Homo sapiens	48-52
1346095-7	1992	Prolongation of the PT occurred only moderately and linearly with increasing concentrations of heparin in LACI-depleted plasma.	Heparin	95-102	tissue factor pathway inhibitor	Homo sapiens	106-110
1346095-9	1992	These results suggest that LACI serves as a cofactor for heparin and thus greatly enhances the inhibition of TF-induced coagulation.	Heparin	57-64	tissue factor pathway inhibitor	Homo sapiens	27-31
1346095-10	1992	LACI-depleted plasma was supplemented with purified recombinant LACI and/or heparin and the effects on TF-induced clotting were studied.	Heparin	76-83	tissue factor pathway inhibitor	Homo sapiens	0-4
1346095-11	1992	A combination of LACI and heparin greatly enhanced anticoagulation compared with LACI or heparin alone.	Heparin	89-96	tissue factor pathway inhibitor	Homo sapiens	17-21
1346095-14	1992	Based on the above results, it is concluded that LACI is a cofactor for heparin in the inhibition of TF-induced clotting and that LACI and sulfated polysaccharides act synergistically in whole plasma.	Heparin	72-79	tissue factor pathway inhibitor	Homo sapiens	49-53
7534313-6	1994	In ligand blotting assays, GST-RHAMM fusion protein was shown to bind biotin-labelled HP and this binding was displaceable with unlabelled HP.	Heparin	139-141	hyaluronan mediated motility receptor	Homo sapiens	31-36
7534313-7	1994	In similar ligand binding analyses conducted with truncations of RHAMM fusion protein, the HP binding region was found to be localized in the same 35 amino acid segment of RHAMM that contains the two HA binding domains.	Heparin	91-93	hyaluronan mediated motility receptor	Homo sapiens	65-70
7534313-7	1994	In similar ligand binding analyses conducted with truncations of RHAMM fusion protein, the HP binding region was found to be localized in the same 35 amino acid segment of RHAMM that contains the two HA binding domains.	Heparin	91-93	hyaluronan mediated motility receptor	Homo sapiens	172-177
7534313-9	1994	Fusion proteins generated by linkage of these peptides to the non-HP binding amino terminus of RHAMM conferred HP binding capacity to the genetically engineered proteins.	Heparin	66-68	hyaluronan mediated motility receptor	Homo sapiens	95-100
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	junctophilin 3	Homo sapiens	108-112
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	junctophilin 3	Homo sapiens	193-197
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	lipase C, hepatic type	Homo sapiens	252-254
7534313-9	1994	Fusion proteins generated by linkage of these peptides to the non-HP binding amino terminus of RHAMM conferred HP binding capacity to the genetically engineered proteins.	Heparin	111-113	hyaluronan mediated motility receptor	Homo sapiens	95-100
11706034-9	2002	A Noggin mutant with a deletion in a putative heparin binding domain has reduced binding to heparin and does not bind to the cell surface but has preserved BMP binding and antagonist functions.	Heparin	46-53	noggin	Homo sapiens	2-8
7534313-10	1994	Conversely, deletion of the HA binding domains of RHAMM resulted in fusion proteins devoid of HP binding activity.	Heparin	94-96	hyaluronan mediated motility receptor	Homo sapiens	50-55
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	lipase C, hepatic type	Homo sapiens	280-282
7961933-10	1994	Neutrophil elastase binds the 5-kDa heparin fragment with an affinity identical to that of cathepsin G. alpha 1-Proteinase inhibitor reacts, however, much faster with heparin-elastase (ka = 1.8 x 10(6) M-1 S-1) than with heparin-cathepsin G (k2/Ki* = 700 M-1 S-1).	Heparin	36-43	elastase, neutrophil expressed	Homo sapiens	0-19
11772005-0	2002	Structural mechanism for heparin-binding of the third Kunitz domain of human tissue factor pathway inhibitor.	Heparin	25-32	tissue factor pathway inhibitor	Homo sapiens	77-108
7961820-1	1994	Protein C inhibitor (PCI) is a plasma serine proteinase inhibitor (serpin) that is a major physiological regulator of activated protein C. Inhibition of its target proteinase is accelerated by heparin in a reaction that involves the binding of both inhibitor and proteinase to heparin to form a ternary complex.	Heparin	277-284	endogenous retrovirus group K member 18	Homo sapiens	45-55
1334618-2	1992	Heparin inhibits the tissue kallikrein/PCI-interaction and complex formation of 125I-tissue kallikrein in serum.	Heparin	0-7	serpin family A member 5	Homo sapiens	39-42
11772005-1	2002	Tissue factor pathway inhibitor (TFPI) inhibits the activity of coagulation factor VIIa and Xa through its K1 and K2 domain, respectively, and the inhibitory activity is enhanced by heparin.	Heparin	182-189	tissue factor pathway inhibitor	Homo sapiens	0-31
1530877-4	1992	Heparin inhibits this effect, possibly by displacing Wnt-1 protein from its normal site of action.	Heparin	0-7	wingless-type MMTV integration site family, member 1	Mus musculus	53-58
1797562-4	1991	Thirty minutes before induction of ischemia, bFGF (0.3-300 nM) or bFGF (300 nM) with heparin was applied to the hippocampal CA1 subfield.	Heparin	85-92	fibroblast growth factor 2	Rattus norvegicus	66-70
7843648-5	1994	On the other hand we could demonstrate that the addition of heparins and protamine sulfate to platelets resulted in a significant release of intracellularly stored ADP and PF4.	Heparin	60-68	platelet factor 4	Homo sapiens	172-175
7881632-2	1994	In the present study, we demonstrated that inositolhexakisphosphate (InsP6) inhibits basic FGF (bFGF) binding to heparin.	Heparin	113-120	inositol hexaphosphate kinase 1	Mus musculus	69-74
7881632-2	1994	In the present study, we demonstrated that inositolhexakisphosphate (InsP6) inhibits basic FGF (bFGF) binding to heparin.	Heparin	113-120	fibroblast growth factor 2	Mus musculus	85-94
11772005-1	2002	Tissue factor pathway inhibitor (TFPI) inhibits the activity of coagulation factor VIIa and Xa through its K1 and K2 domain, respectively, and the inhibitory activity is enhanced by heparin.	Heparin	182-189	tissue factor pathway inhibitor	Homo sapiens	33-37
7881632-2	1994	In the present study, we demonstrated that inositolhexakisphosphate (InsP6) inhibits basic FGF (bFGF) binding to heparin.	Heparin	113-120	fibroblast growth factor 2	Mus musculus	96-100
11772005-10	2002	It is likely that heparin simply increases the local concentration of TFPI on the cell surface and stabilizes the initial complex that forms.	Heparin	18-25	tissue factor pathway inhibitor	Homo sapiens	70-74
11886166-6	2002	The protocol exploits the high binding affinity of MBP for amylose resin or vIL-10 for heparin and the ability of Triton-X114 to dissociate endotoxins from proteins.	Heparin	87-94	myelin basic protein	Homo sapiens	51-54
7962072-5	1994	The effects of PF-4 were antagonized by heparin.	Heparin	40-47	platelet factor 4	Homo sapiens	15-19
7929392-5	1994	Both APLP1 and APLP2 bound heparin-Sepharose and had NaCl elution profiles similar to that of APP.	Heparin	27-34	amyloid beta precursor like protein 2	Homo sapiens	15-20
7532447-7	1994	Vitronectin also decreased the inhibition rate of PCI-thrombin and PCI-APC in the presence of low concentrations of heparin.	Heparin	116-123	serpin family A member 5	Homo sapiens	50-53
7532447-8	1994	Leukocyte elastase proteolytically inactivated PCI in a reaction that was accelerated by heparin.	Heparin	89-96	elastase, neutrophil expressed	Homo sapiens	0-18
7532447-8	1994	Leukocyte elastase proteolytically inactivated PCI in a reaction that was accelerated by heparin.	Heparin	89-96	serpin family A member 5	Homo sapiens	47-50
1750550-7	1991	When heparin was present throughout the chase, labeled LPL began to appear in the medium after 30 min.	Heparin	5-12	lipoprotein lipase	Cavia porcellus	55-58
1750550-9	1991	After 90 min chase with heparin, approximately equal amounts of LPL (approximately 32%) had been released to the medium, remained in the heart, or had been degraded, respectively.	Heparin	24-31	lipoprotein lipase	Cavia porcellus	64-67
1750550-10	1991	In contrast, no detectable amount of labeled LPL appeared in the medium during 90 min chase without heparin, and a heparin flush at this time brought out only approximately 9% of the pulse-labeled LPL.	Heparin	115-122	lipoprotein lipase	Cavia porcellus	197-200
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	neuropilin 1	Homo sapiens	118-122
1724341-6	1991	These results indicate that both aFGF and bFGF can stimulate bone resorption by a prostaglandin-independent mechanism, particularly in the presence of heparin.	Heparin	151-158	fibroblast growth factor 2	Rattus norvegicus	42-46
7865689-0	1994	Measurement of tissue factor pathway inhibitor in normal and post-heparin plasma.	Heparin	66-73	tissue factor pathway inhibitor	Homo sapiens	15-46
11748573-1	2002	Pulmonary intravascular macrophages (PIMs) contain a unique electron-dense globular surface-coat which is sensitive to heparin treatment, halothane anesthesia, and the digestive effect of lipolytic lipase (LPL), suggesting that the coat is predominantly composed of lipoproteins.	Heparin	119-126	lipoprotein lipase	Capra hircus	206-209
7931292-2	1994	In this study, we found that the activity of kinase FA/GSK-3 alpha towards phosphorylation of brain tau could be stimulated approximately fourfold by heparin.	Heparin	150-157	glycogen synthase kinase 3 alpha	Homo sapiens	55-66
7931292-6	1994	As Ser235, Ser262, Ser324, Ser356, and Ser404 (particularly the site of Ser262) have been identified as five of the most potent sites in tau responsible for reducing microtubule binding possibly involved in neuronal degeneration, and Thr231, Ser235, Ser262, and Ser404 are four of the most well documented sites abnormally phosphorylated in Alzheimer-tau, the results provide initial evidence that protein kinase FA/GSK-3 alpha after heparin potentiation may represent one of the most potent systems possibly involved in the abnormal phosphorylation of PHF-tau in Alzheimer"s disease brains.	Heparin	434-441	glycogen synthase kinase 3 alpha	Homo sapiens	416-427
1788836-4	1991	The heparin binding site of ovine PF4 localized in the C-terminal region of the molecule was identified as LYKKIIKRLL.	Heparin	4-11	platelet factor 4	Homo sapiens	34-37
11754875-9	2002	Our results suggest that neutrophil migration in response to sPLA2s is independent of PLA activity, and involves an interaction of sPLA2s with cell surface heparin/heparan binding sites triggering the release of LTB4 and PAF.	Heparin	156-163	phospholipase A2 group IID	Homo sapiens	61-67
1915292-5	1991	Activities of D1 and D2 are inhibited by zinc, vanadate and EDTA and differentially susceptible to inhibition by heparin and poly(Glu4:Tyr1).	Heparin	113-120	leiomodin 1	Homo sapiens	14-23
7899138-5	1994	Human neutrophil elastase (HNE) activity is inhibited by heparin with Ki = 75 pM.	Heparin	57-64	elastase, neutrophil expressed	Homo sapiens	6-25
7899138-5	1994	Human neutrophil elastase (HNE) activity is inhibited by heparin with Ki = 75 pM.	Heparin	57-64	elastase, neutrophil expressed	Homo sapiens	27-30
7899138-6	1994	This strong interaction is electrostatic, involving HNE/arginine residues disposed in a "cluster shoe" arrangement on the surface of the molecule and mainly OSO3- groups of heparin.	Heparin	173-180	elastase, neutrophil expressed	Homo sapiens	52-55
7899138-7	1994	HNE-heparin interactions also interfere with HNE associations with its natural inhibitors: it decreases the rate of association of HNE with alpha 1 proteinase inhibitor (alpha 1 P(i)) by 3 orders of magnitude, while increasing kass between HNE and mucus bronchial inhibitor (MBI) by &gt; 10 fold.	Heparin	4-11	elastase, neutrophil expressed	Homo sapiens	0-3
7899138-7	1994	HNE-heparin interactions also interfere with HNE associations with its natural inhibitors: it decreases the rate of association of HNE with alpha 1 proteinase inhibitor (alpha 1 P(i)) by 3 orders of magnitude, while increasing kass between HNE and mucus bronchial inhibitor (MBI) by &gt; 10 fold.	Heparin	4-11	elastase, neutrophil expressed	Homo sapiens	45-48
7899138-7	1994	HNE-heparin interactions also interfere with HNE associations with its natural inhibitors: it decreases the rate of association of HNE with alpha 1 proteinase inhibitor (alpha 1 P(i)) by 3 orders of magnitude, while increasing kass between HNE and mucus bronchial inhibitor (MBI) by &gt; 10 fold.	Heparin	4-11	elastase, neutrophil expressed	Homo sapiens	45-48
7899138-7	1994	HNE-heparin interactions also interfere with HNE associations with its natural inhibitors: it decreases the rate of association of HNE with alpha 1 proteinase inhibitor (alpha 1 P(i)) by 3 orders of magnitude, while increasing kass between HNE and mucus bronchial inhibitor (MBI) by &gt; 10 fold.	Heparin	4-11	elastase, neutrophil expressed	Homo sapiens	45-48
7899138-8	1994	In vivo experiments demonstrated that heparin fragments lacking anticoagulant activity were able to nearly completely abolish emphysematous lesions induced in mice by a single intratracheal administration of 200 micrograms HNE.	Heparin	38-45	elastase, neutrophil expressed	Homo sapiens	223-226
7899138-11	1994	We synthesized N-oleoyl heparin derivative (3 oleoyl groups/one molecule of heparin); such a lipophilic glycosaminoglycan (LipoGAG), although acting as an elastin protecting agent, possessed lower HNE inhibitory capacity as compared with heparin.	Heparin	24-31	elastase, neutrophil expressed	Homo sapiens	197-200
7831680-4	1994	The inhibitory activity of TFPI was significantly enhanced when unfractionated heparin was present in the assay system at a concentration of 10 micrograms/ml which did not show any inhibitory effects on protease generation in the same system.	Heparin	79-86	tissue factor pathway inhibitor	Homo sapiens	27-31
7831680-6	1994	Whereas in the concentration range used (0.3-40 micrograms/ml) these glycosaminoglycans did not inhibit thrombin and factor Xa generation, after supplementation of the system with TFPI a concentration-dependent inhibition of the generation of the proteases up to 40-50% was seen for UFH, LMWH and HS.	Heparin	283-286	tissue factor pathway inhibitor	Homo sapiens	180-184
1835383-4	1991	The deleted form of recombinant F-TCF (rF-TCF) was slightly lower in heparin affinity than the intact form.	Heparin	69-76	hepatocyte growth factor	Homo sapiens	32-37
11754875-9	2002	Our results suggest that neutrophil migration in response to sPLA2s is independent of PLA activity, and involves an interaction of sPLA2s with cell surface heparin/heparan binding sites triggering the release of LTB4 and PAF.	Heparin	156-163	phospholipase A2 group IID	Homo sapiens	131-137
8077206-5	1994	Both dexamethasone and heparin reduced ET-1-activated PGHS-2 mRNA expression and protein formation.	Heparin	23-30	prostaglandin-endoperoxide synthase 2	Rattus norvegicus	54-60
11832997-6	2002	However, an additional elevation of plasma FFA by treatment with heparin for 2 - 4 h impaired the ipGTT responses in apo CIII tg mice compared to saline-treated mice.	Heparin	65-72	apolipoprotein C-III	Mus musculus	117-125
8074689-0	1994	Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1.	Heparin	53-60	fibroblast growth factor 2	Mus musculus	106-136
11832997-9	2002	In islets from heparin-treated apo CIII tg mice, the insulin secretion at 2.8 and 22.2 mmol glucose/l was lower than in heparin-treated control mice.	Heparin	15-22	apolipoprotein C-III	Mus musculus	31-39
8074689-2	1994	The molecular bases of this interaction were investigated by evaluating the capacity of conventional and selectively desulfated heparins i) to affect the binding of bFGF to FGFR and HSPGs of NIH 3T3 cells transfected with FGFR-1/flg cDNA, ii) to facilitate the interaction of bFGF with a recombinant soluble form of the extracellular domain of FGFR-1/flg (xcFGFR-1), and iii) to protect xcFGFR-1 from tryptic cleavage.	Heparin	128-136	fibroblast growth factor 2	Mus musculus	165-169
11832997-9	2002	In islets from heparin-treated apo CIII tg mice, the insulin secretion at 2.8 and 22.2 mmol glucose/l was lower than in heparin-treated control mice.	Heparin	120-127	apolipoprotein C-III	Mus musculus	31-39
11801740-13	2002	Data indicate that antithrombin directly inhibits chemokine-stimulated migration of monocytes and lymphocytes via the effects of its heparin-binding site on cell surface syndecan-4 by activation of protein kinase C and Rho signaling.	Heparin	133-140	syndecan 4	Homo sapiens	170-180
8068001-10	1994	Heparin inhibited Ca2+ release in response to the Ins(1,4,5)P3-generating receptor agonist N-formylmethionyl-leucyl-phenylalanine (f-MLP) (50 nM) and to thapsigargin (50 nM) at comparable concentrations.	Heparin	0-7	cysteine and glycine rich protein 3	Homo sapiens	133-136
11853152-1	2002	Lactoferrin with a molecular mass of 80 kDa was purified from equine seminal plasma by heparin-Agarose affinity chromatography and Sephacryl S-200 gel filtration.	Heparin	87-94	inhibitor of carbonic anhydrase	Equus caballus	0-11
8076651-1	1994	Carboxylester lipase obtained from pig pancreas is associated with fatty acid ethyl ester synthase as judged by their elution in the same fraction from a heparin-Sepharose column, coprecipitations by antibody against purified carboxylester lipase and identical profiles of inhibition by diisopropyl fluorophosphate.	Heparin	154-161	carboxyl ester lipase	Sus scrofa	0-20
11848461-3	2002	In the present study, it was found, by means of agarose gel electrophoresis, that the pre-incubation of full-length rTFPI with heparin or the carboxy (C)-terminal part (peptide 240-265) of TFPI prevented the association with ox-LDL in a dose-dependent manner.	Heparin	127-134	tissue factor pathway inhibitor	Homo sapiens	117-121
7841311-3	1994	The native and recombinant TFPI produced by mammalian cells in tissue culture and the TFPI released by heparin in vivo, however, are 34 kDa.	Heparin	103-110	tissue factor pathway inhibitor	Homo sapiens	27-31
7841311-3	1994	The native and recombinant TFPI produced by mammalian cells in tissue culture and the TFPI released by heparin in vivo, however, are 34 kDa.	Heparin	103-110	tissue factor pathway inhibitor	Homo sapiens	86-90
8040268-9	1994	Inhibition of bFGF activity by PF 4 could be overcome by exogenous heparin or chondroitin-4-sulfate, suggesting that inhibition of mitogenesis is caused by binding of PF 4 to cell-surface glycosaminoglycans.	Heparin	67-74	platelet factor 4	Homo sapiens	167-171
11728396-4	2001	Starting from a "supersulfated" low-molecular weight heparin, we obtained products with up to 40% of iduronate residues O-sulfated exclusively at C-2 and up to 40% of their glucosamine residues O-sulfated at both C-6 and C-3.	Heparin	53-60	complement C6	Homo sapiens	213-224
7911328-0	1994	Anti-HIV-1 activity of chemically modified heparins: correlation between binding to the V3 loop of gp120 and inhibition of cellular HIV-1 infection in vitro.	Heparin	43-51	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	99-104
7911328-1	1994	Chemically modified heparins were tested for their activities in (i) inhibiting HIV-1 replication in vitro and (ii) inhibiting the binding to recombinant HIV-1 gp120 of monoclonal antibodies specific for the V3 loop.	Heparin	20-28	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	160-165
11709459-2	2001	Although most TFPI is found in association with plasma lipoproteins and platelets, the functional pool is bound to vascular endothelium and is released into the circulation on stimulation with heparin or low molecular weight heparin (LMWH).	Heparin	193-200	tissue factor pathway inhibitor	Homo sapiens	14-18
7962199-11	1994	Syndecan-1 could also be released into the Triton X-100-soluble fraction by addition of heparin or heparan sulfate to the extraction medium.	Heparin	88-95	syndecan 1	Mus musculus	0-10
11709459-2	2001	Although most TFPI is found in association with plasma lipoproteins and platelets, the functional pool is bound to vascular endothelium and is released into the circulation on stimulation with heparin or low molecular weight heparin (LMWH).	Heparin	225-232	tissue factor pathway inhibitor	Homo sapiens	14-18
11687508-1	2001	We recently characterized a heparin-deficient mouse strain generated by targeting the gene for N-deacetylase/N-sulfotransferase-2 (NDST-2).	Heparin	28-35	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	95-129
8024698-4	1994	Regions of the BFGF molecule important in heparin binding, high-affinity receptor binding, and biologic function are highly conserved between placental mammals and this marsupial.	Heparin	42-49	fibroblast growth factor 2	Monodelphis domestica	15-19
8091389-2	1994	This study confirmed that rPF4 and PS neutralized heparin in rats.	Heparin	50-57	platelet factor 4	Rattus norvegicus	26-30
8091389-6	1994	Heparin prevented the rapid loss of 125I-rPF4 from the circulation within the first 2 min but modestly increased loss of radioiodinated derivatized PS.	Heparin	0-7	platelet factor 4	Rattus norvegicus	41-45
8091389-7	1994	Heparin extended the half-life of derivatized radioiodinated PS (measured between 2 and 60 min after injection) while modestly shortening that of 125I-rPF4.	Heparin	0-7	platelet factor 4	Rattus norvegicus	151-155
8091389-11	1994	These results indicate that rPF4 and PS affect the kinetics of heparin clearance similarly but that organ deposition of the two agents may differ and offer an explanation of different physiological effects seen previously.	Heparin	63-70	platelet factor 4	Rattus norvegicus	28-32
8091393-3	1994	The antigen is formed by a releasable platelet protein (in many cases PF4) complexed to heparin.	Heparin	88-95	platelet factor 4	Homo sapiens	70-73
8175664-2	1994	As expected, it binds with high affinity to heparin-Sepharose like FGF-2 and can displace the binding of radiolabeled FGF-2 to its high affinity receptor.	Heparin	44-51	fibroblast growth factor 2	Mus musculus	67-72
8175664-2	1994	As expected, it binds with high affinity to heparin-Sepharose like FGF-2 and can displace the binding of radiolabeled FGF-2 to its high affinity receptor.	Heparin	44-51	fibroblast growth factor 2	Mus musculus	118-123
11687508-1	2001	We recently characterized a heparin-deficient mouse strain generated by targeting the gene for N-deacetylase/N-sulfotransferase-2 (NDST-2).	Heparin	28-35	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2	Mus musculus	131-137
8017769-1	1994	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Heparin	43-50	serpin family D member 1	Homo sapiens	54-58
11606255-9	2001	In addition, the hepatic and renal activity of 5"-nucleotidase was inhibited by heparin and chondroitin sulfate, except for kidney membranes where chondroitin sulfate did not alter AMP hydrolysis.	Heparin	80-87	5' nucleotidase, ecto	Rattus norvegicus	47-62
8172612-7	1994	When RMCP-1 was reconstituted with either endogenous [35S]heparin proteoglycans or standard pig mucosal heparin, the enzyme regained its thrombin-inactivating properties.	Heparin	58-65	coagulation factor II, thrombin	Sus scrofa	137-145
11776326-1	2001	We investigated the localisation, gene expression, and activity of tissue factor pathway inhibitor (TFPI) in endothelial cells (EC) grown in static conditions or under shear stress, in the presence of unfractionated heparin (UFH) and two low-molecular-weight heparins (LMWHs).	Heparin	225-228	tissue factor pathway inhibitor	Homo sapiens	100-104
8161203-5	1994	The binding of [125I]bFGF to rat growth plate ECM was inhibited by the addition of heparin, heparan sulfate, and dermatan sulfate.	Heparin	83-90	fibroblast growth factor 2	Rattus norvegicus	21-25
11776326-4	2001	In EC grown under shear stress (0.27, 4.1 and 19 dyne/cm2) and incubated with each heparin for 24 h, the release of TFPI was significantly correlated with the level of flow for bemiparin and dalteparin, but not for UFH.	Heparin	83-90	tissue factor pathway inhibitor	Homo sapiens	116-120
11776326-4	2001	In EC grown under shear stress (0.27, 4.1 and 19 dyne/cm2) and incubated with each heparin for 24 h, the release of TFPI was significantly correlated with the level of flow for bemiparin and dalteparin, but not for UFH.	Heparin	215-218	tissue factor pathway inhibitor	Homo sapiens	116-120
11776326-6	2001	The expression of TFPI mRNA, determined by Northern blotting, was specifically modulated by heparins.	Heparin	92-100	tissue factor pathway inhibitor	Homo sapiens	18-22
7510698-8	1994	In addition, angiogenin binds tightly to heparin-Sepharose, requiring 0.78 M NaCl for elution.	Heparin	41-48	angiogenin	Homo sapiens	13-23
11588041-0	2001	Heparin-induced thrombocytopenia/thrombosis in a transgenic mouse model requires human platelet factor 4 and platelet activation through FcgammaRIIA.	Heparin	0-7	Fc gamma receptor IIa	Homo sapiens	137-148
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	131-138	serpin family D member 1	Homo sapiens	0-19
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	131-138	serpin family D member 1	Homo sapiens	21-25
11588041-6	2001	Nadir platelet counts for KKO/heparin-treated FcgammaRIIA/hPF4 mice were 80% below baseline values, significantly different (P &lt;.001) from similarly treated controls.	Heparin	30-37	Fc gamma receptor IIa	Homo sapiens	46-57
11588041-6	2001	Nadir platelet counts for KKO/heparin-treated FcgammaRIIA/hPF4 mice were 80% below baseline values, significantly different (P &lt;.001) from similarly treated controls.	Heparin	30-37	platelet factor 4	Homo sapiens	58-62
11588041-7	2001	FcgammaRIIA/hPF4 mice injected with KKO and 50 U/d heparin developed shock and showed fibrin-rich thrombi in multiple organs, including thrombosis in the pulmonary vasculature.	Heparin	51-58	Fc gamma receptor IIa	Homo sapiens	0-11
11588041-7	2001	FcgammaRIIA/hPF4 mice injected with KKO and 50 U/d heparin developed shock and showed fibrin-rich thrombi in multiple organs, including thrombosis in the pulmonary vasculature.	Heparin	51-58	platelet factor 4	Homo sapiens	12-16
1953650-11	1991	These data suggest that bovine thymus p56lck is responsible for the activity found in the early-eluting peak from heparin-agarose.	Heparin	114-121	lymphocyte protein tyrosine kinase	Mus musculus	38-44
11597123-1	2001	Midkine (MK) is a heparin binding multifunctional protein that promotes cell survival and cell migration.	Heparin	18-25	midkine	Mus musculus	0-7
1953650-16	1991	The phosphorylation of angiotensin I by bovine thymus p56lck was weakly activated by polyionic compounds such as heparin and polylysine, and was strongly activated by high concentrations of NaCl.	Heparin	113-120	lymphocyte protein tyrosine kinase	Mus musculus	54-60
11597123-1	2001	Midkine (MK) is a heparin binding multifunctional protein that promotes cell survival and cell migration.	Heparin	18-25	midkine	Mus musculus	9-11
1664252-1	1991	Injection of heparin releases tissue factor pathway inhibitor (TFPI) to the blood and, after heparin neutralization, it has been recently demonstrated that the released TFPI has an anticoagulant activity.	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	30-61
1664252-1	1991	Injection of heparin releases tissue factor pathway inhibitor (TFPI) to the blood and, after heparin neutralization, it has been recently demonstrated that the released TFPI has an anticoagulant activity.	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	63-67
11687304-3	2001	HAT/Proth-1 inactivated factor Xa approximately 3-4-fold better than HAT/Proth-2 in either the absence or presence of heparin cofactors.	Heparin	118-125	transmembrane serine protease 11D	Homo sapiens	0-3
1664252-1	1991	Injection of heparin releases tissue factor pathway inhibitor (TFPI) to the blood and, after heparin neutralization, it has been recently demonstrated that the released TFPI has an anticoagulant activity.	Heparin	13-20	tissue factor pathway inhibitor	Homo sapiens	169-173
11687304-6	2001	A similar 10(4)-10(5)-fold enhancement in the reactivity of factor Xa with prethrombin-2 and the HAT mutants was observed in the presence of the cofactors Va and heparin, respectively.	Heparin	162-169	transmembrane serine protease 11D	Homo sapiens	97-100
1833592-8	1991	Increased platelet activation was also found in patients with preoperative heparin therapy (beta-thromboglobulin at the end of cardiopulmonary bypass was 585 +/- 88 ng/ml in group M versus 1341 +/- 190 ng/ml in group Hsc, p less than 0.05).	Heparin	75-82	pro-platelet basic protein	Homo sapiens	92-112
1955380-6	1991	The tumor cell interaction with CH-271-substrate was inhibited by heparin, and monoclonal antibodies (IST-1 or IST-2) against the heparin-binding domain of fibronectin.	Heparin	130-137	IST1 factor associated with ESCRT-III	Homo sapiens	102-107
11668420-0	2001	Molecular weight-dependent influence of heparin on the form of tissue factor pathway inhibitor circulating in plasma.	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	63-94
1654330-10	1991	Heparin and unlabeled LPL decreased the cross-linking of radioiodinated LPL to the cell surface receptor.	Heparin	0-7	lipoprotein lipase	Bos taurus	72-75
11668420-1	2001	The increase of circulating tissue factor pathway inhibitor (TFPI) in plasma by heparins is thought to contribute to their overall antithrombotic activity.	Heparin	80-88	tissue factor pathway inhibitor	Homo sapiens	28-59
11668420-1	2001	The increase of circulating tissue factor pathway inhibitor (TFPI) in plasma by heparins is thought to contribute to their overall antithrombotic activity.	Heparin	80-88	tissue factor pathway inhibitor	Homo sapiens	61-65
1832058-5	1991	beta TG levels (339 +/- 105 ng/mL at T Oh) decreased to 203 +/- 48 (T 2h), 154 +/- 51 (T 3.5h), 187 +/- 40 (T 12h), and 142 +/- 32 (T 24h) ng/mL under heparin (P less than .01).	Heparin	151-158	pro-platelet basic protein	Homo sapiens	0-7
11668420-2	2001	In a clinical study in healthy volunteers, we recently found that the specific potency of a heparin to mobilize TFPI from the vessel wall increases with its molecular weight (MW).	Heparin	92-99	tissue factor pathway inhibitor	Homo sapiens	112-116
11668420-4	2001	A further question is whether the MW of heparin influences not only the release of TFPI but also its potential association with lipoproteins.	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	83-87
11668420-6	2001	Only the TFPI released by unfractionated heparin (UFH) circulated completely as free TFPI.	Heparin	41-48	tissue factor pathway inhibitor	Homo sapiens	9-13
11668420-6	2001	Only the TFPI released by unfractionated heparin (UFH) circulated completely as free TFPI.	Heparin	50-53	tissue factor pathway inhibitor	Homo sapiens	9-13
11668420-7	2001	With decreasing heparin MW, the percentage of released free TFPI on released total TFPI decreased to 57%.	Heparin	16-23	tissue factor pathway inhibitor	Homo sapiens	60-64
1894597-4	1991	This product has the biological characteristics of cADPR (it acts after depletion of the IP3 stores and after blockade of the IP3 receptor by heparin).	Heparin	142-149	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	126-138
11668420-7	2001	With decreasing heparin MW, the percentage of released free TFPI on released total TFPI decreased to 57%.	Heparin	16-23	tissue factor pathway inhibitor	Homo sapiens	83-87
11668420-8	2001	As a consequence, the longer the heparin chains are, the better they are at preventing the binding of the released, originally free, TFPI to plasma lipoproteins.	Heparin	33-40	tissue factor pathway inhibitor	Homo sapiens	133-137
1720904-0	1991	Limited proteolysis of vitronectin by plasmin destroys heparin binding activity.	Heparin	55-62	plasminogen	Homo sapiens	38-45
11668420-9	2001	Because only free TFPI is known to exhibit anticoagulant activity, the activity of released TFPI is better the higher the MW of the applied heparin is.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	18-22
11668420-9	2001	Because only free TFPI is known to exhibit anticoagulant activity, the activity of released TFPI is better the higher the MW of the applied heparin is.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	92-96
11668420-10	2001	In conclusion, in addition to the potency of heparin to mobilize TFPI, there is its influence on the circulating form, and thus the anticoagulant activity of the released TFPI depends on its MW.	Heparin	45-52	tissue factor pathway inhibitor	Homo sapiens	65-69
1659747-10	1991	With added RGDS peptide heparin still increased aggregation (p less than 0.001).	Heparin	24-31	ral guanine nucleotide dissociation stimulator	Homo sapiens	11-15
11668420-10	2001	In conclusion, in addition to the potency of heparin to mobilize TFPI, there is its influence on the circulating form, and thus the anticoagulant activity of the released TFPI depends on its MW.	Heparin	45-52	tissue factor pathway inhibitor	Homo sapiens	171-175
2070076-7	1991	A radioligand blot of the pre- and post-heparin plasma samples shows the increase to be in a 40-Kd form of LACI.	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	107-111
11560562-1	2001	AIMS: The objective of our study was to define the interaction between either unfractionated heparin (UFH) or a low molecular weight heparin, reviparin (REV), and the pharmacodynamic profile of the GPIIb/IIIa-antagonists abciximab (ABC) or tirofiban (T).	Heparin	93-100	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	204-236
2070076-9	1991	Following the injection of heparin into one patient with homozygous abetalipoproteinemia, the plasma LACI antigen level increased to a level comparable with that in normal individuals after heparin treatment.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	101-105
2070076-9	1991	Following the injection of heparin into one patient with homozygous abetalipoproteinemia, the plasma LACI antigen level increased to a level comparable with that in normal individuals after heparin treatment.	Heparin	190-197	tissue factor pathway inhibitor	Homo sapiens	101-105
11560562-1	2001	AIMS: The objective of our study was to define the interaction between either unfractionated heparin (UFH) or a low molecular weight heparin, reviparin (REV), and the pharmacodynamic profile of the GPIIb/IIIa-antagonists abciximab (ABC) or tirofiban (T).	Heparin	102-105	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	204-236
11560562-1	2001	AIMS: The objective of our study was to define the interaction between either unfractionated heparin (UFH) or a low molecular weight heparin, reviparin (REV), and the pharmacodynamic profile of the GPIIb/IIIa-antagonists abciximab (ABC) or tirofiban (T).	Heparin	133-140	ATP binding cassette subfamily B member 6 (Langereis blood group)	Homo sapiens	204-236
11504538-7	2001	Heparin, a gB-specific inhibitor of virus-induced cell fusion, inhibited both wild-type gB and gB(syn3)-mediated cell fusion.	Heparin	0-7	synapsin III	Homo sapiens	98-102
2050110-5	1991	Uptake and transactivation could be inhibited by incubation with heparin, dextran sulfate, an anti-Tat monoclonal antibody, or by incubation at 4 degrees C. In contrast, transactivation by Tat was markedly stimulated by the addition of basic peptides, such as Tat 38-58 or protamine.	Heparin	65-72	tyrosine aminotransferase	Homo sapiens	189-192
2050110-5	1991	Uptake and transactivation could be inhibited by incubation with heparin, dextran sulfate, an anti-Tat monoclonal antibody, or by incubation at 4 degrees C. In contrast, transactivation by Tat was markedly stimulated by the addition of basic peptides, such as Tat 38-58 or protamine.	Heparin	65-72	tyrosine aminotransferase	Homo sapiens	189-192
1922928-2	1991	The previously reported solubilization of asymmetric AChE by heparin, or the proven affinity of the tailed enzyme forms for this GAG, cannot therefore be taken as direct proof of the involvement of heparin-like heparan sulfate proteoglycans in the anchorage of the collagenous tail of the enzyme to the basal lamina in skeletal muscle.	Heparin	61-68	acetylcholinesterase (Cartwright blood group)	Gallus gallus	53-57
1922928-2	1991	The previously reported solubilization of asymmetric AChE by heparin, or the proven affinity of the tailed enzyme forms for this GAG, cannot therefore be taken as direct proof of the involvement of heparin-like heparan sulfate proteoglycans in the anchorage of the collagenous tail of the enzyme to the basal lamina in skeletal muscle.	Heparin	198-205	acetylcholinesterase (Cartwright blood group)	Gallus gallus	53-57
1710230-6	1991	The mitogens extracted from cell lysates and from the ECM are closely related to aFGF or bFGF by the criteria that they bind to heparin-sepharose and elute at 1.1 M (aFGF) or 1.5 M (bFGF) NaCl, have molecular weights of about 18,000, and react with anti-aFGF (1.1 M), or anti-bFGF (1.5 M) antibodies when analyzed by Western blots and by radioimmunoassay specific for aFGF and bFGF.	Heparin	128-135	fibroblast growth factor 1	Bos taurus	81-85
1708387-10	1991	In addition, these experiments indicate that Lp(a) may regulate fibrinolysis by competing with PAI-1 and plasminogen for fibrinogen- and heparin-bound t-PA.	Heparin	137-144	lipoprotein(a)	Homo sapiens	45-50
30429724-6	2001	Other inhibitors of plasmin, like a 2 -macroglobulin, antithrombin in the presence of heparin, and C1-esterase inhibitor should not interfere in the assay at the level usually found in pathological conditions or at the higher normal level.	Heparin	86-93	plasminogen	Homo sapiens	20-27
2012601-8	1991	Cathepsin D-digested pFn applied to a heparin-agarose column and eluted with an NaCl stepwise gradient (0.1 M, 0.25 M and 0.5 M) released two polypeptides (75 kDa and 65 kDa) in the 0.5 M-NaCl peak.	Heparin	38-45	cathepsin D	Homo sapiens	0-11
1900338-5	1991	Postheparin DAO activity was similar in both groups with a maximum increase between 15 and 60 min following heparin administration.	Heparin	4-11	D-amino acid oxidase	Canis lupus familiaris	12-15
11319227-6	2001	Our analysis suggests that EMBP specifically binds heparin.	Heparin	51-58	proteoglycan 2, pro eosinophil major basic protein	Homo sapiens	27-31
1999476-3	1991	The addition of EGF, TGF alpha, or aFGF reversed heparin-induced growth inhibition, while bFGF partially negated this effect.	Heparin	49-56	transforming growth factor alpha	Homo sapiens	21-30
11457474-1	2001	Several studies have shown that tissue factor pathway inhibitor (TFPI) is released after the intravenous and subcutaneous administration of heparin and heparin-related drugs.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	32-63
1992009-4	1991	Acidic FGF and bFGF from extracts of nervous tissue were found to differ considerably in their relative dependencies upon heparin to potentiate their mitogenic activities: the effect of aFGF was strongly dependent upon heparin, whereas the effect of bFGF was only slightly potentiated by heparin.	Heparin	122-129	fibroblast growth factor 2	Rattus norvegicus	15-19
1992009-4	1991	Acidic FGF and bFGF from extracts of nervous tissue were found to differ considerably in their relative dependencies upon heparin to potentiate their mitogenic activities: the effect of aFGF was strongly dependent upon heparin, whereas the effect of bFGF was only slightly potentiated by heparin.	Heparin	122-129	fibroblast growth factor 2	Rattus norvegicus	250-254
1992009-4	1991	Acidic FGF and bFGF from extracts of nervous tissue were found to differ considerably in their relative dependencies upon heparin to potentiate their mitogenic activities: the effect of aFGF was strongly dependent upon heparin, whereas the effect of bFGF was only slightly potentiated by heparin.	Heparin	219-226	fibroblast growth factor 2	Rattus norvegicus	15-19
1992009-4	1991	Acidic FGF and bFGF from extracts of nervous tissue were found to differ considerably in their relative dependencies upon heparin to potentiate their mitogenic activities: the effect of aFGF was strongly dependent upon heparin, whereas the effect of bFGF was only slightly potentiated by heparin.	Heparin	219-226	fibroblast growth factor 2	Rattus norvegicus	15-19
1992009-5	1991	Heparin was also found to stimulate differentially the mitogenic activity of extracts prepared from different areas of the nervous system, indicating that spinal cord, cortex, pituitary, and optic nerve contained different ratios of aFGF to bFGF, whereas sciatic nerve contained extremely high levels of only aFGF.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	241-245
11457474-1	2001	Several studies have shown that tissue factor pathway inhibitor (TFPI) is released after the intravenous and subcutaneous administration of heparin and heparin-related drugs.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	65-69
11457474-1	2001	Several studies have shown that tissue factor pathway inhibitor (TFPI) is released after the intravenous and subcutaneous administration of heparin and heparin-related drugs.	Heparin	152-159	tissue factor pathway inhibitor	Homo sapiens	32-63
11457474-1	2001	Several studies have shown that tissue factor pathway inhibitor (TFPI) is released after the intravenous and subcutaneous administration of heparin and heparin-related drugs.	Heparin	152-159	tissue factor pathway inhibitor	Homo sapiens	65-69
11441984-0	2001	Tissue factor pathway inhibitor release induced by defibrotide and heparins.	Heparin	67-75	tissue factor pathway inhibitor	Homo sapiens	0-31
1826095-7	1991	Heparin levels declined from 1-5-h dialysis and were associated with rises in plasma levels of FPA, thrombin-antithrombin complex (TAT) and beta thromboglobulin (BTG), but not of D-dimer.	Heparin	0-7	pro-platelet basic protein	Homo sapiens	140-160
1856049-9	1991	Since interaction with heparin has been observed also for selenoprotein P isolated from rat plasma, the protein in the heparin-binding fraction, demonstrated in this paper, may be a human analogue to selenoprotein P.	Heparin	23-30	selenoprotein P	Rattus norvegicus	58-73
1856049-9	1991	Since interaction with heparin has been observed also for selenoprotein P isolated from rat plasma, the protein in the heparin-binding fraction, demonstrated in this paper, may be a human analogue to selenoprotein P.	Heparin	119-126	selenoprotein P	Rattus norvegicus	58-73
11441984-4	2001	UFH caused a 4-fold increase in plasma TFPI at 5 minutes, with a decrease that was parallel to the heparin level measured by the anti-Xa assay.	Heparin	0-3	tissue factor pathway inhibitor	Homo sapiens	39-43
11441984-12	2001	Furthermore, the release of TFPI by heparin is mediated by non-antithrombin III binding fragments.	Heparin	36-43	tissue factor pathway inhibitor	Homo sapiens	28-32
11398076-5	2001	Heparin and pertussis toxin and different extracellular Ca(2+) concentrations were used to modulate mast cell reactivation by MBP.	Heparin	0-7	myelin basic protein	Homo sapiens	126-129
2020936-4	1991	AT III-heparin group pigs (n = 8) were pretreated with a bolus injection of 500 units AT III-heparin complex, followed by a continuous infusion of 1000 units of the complex for 6 hours given simultaneously with the infusion of 10 micrograms/kgh of S. abortus equi endotoxin.	Heparin	7-14	serpin family C member 1	Sus scrofa	0-6
2020936-9	1991	AT III activity in the AT III-heparin group was elevated throughout the whole observation period (greater than 100%), whereas it was significantly lower in the controls.	Heparin	30-37	serpin family C member 1	Sus scrofa	0-6
2020936-9	1991	AT III activity in the AT III-heparin group was elevated throughout the whole observation period (greater than 100%), whereas it was significantly lower in the controls.	Heparin	30-37	serpin family C member 1	Sus scrofa	23-29
11434705-0	2001	The effect of unfractionated vs. low molecular weight heparin on tissue factor pathway inhibitor levels in hospital inpatients.	Heparin	54-61	tissue factor pathway inhibitor	Homo sapiens	65-96
2090518-2	1990	The specificity of the affinity of bFGF for its receptors was assessed by competition experiments with unlabelled growth factor or with heparin, as well as by heparitinase treatment of the samples.	Heparin	136-143	fibroblast growth factor 2	Gallus gallus	35-39
2121582-0	1990	Polarized secretion of diamine oxidase by intestinal epithelial cells and its stimulation by heparin.	Heparin	93-100	amine oxidase copper containing 1	Homo sapiens	23-38
2121582-9	1990	Heparin may induce its marked stimulation of enzyme release by complexing with diamine oxidase bound to the cell surface or through interaction with specific binding sites also located in the basolateral membrane.	Heparin	0-7	amine oxidase copper containing 1	Homo sapiens	79-94
2211593-6	1990	Transfected cells expressed 1-2 micrograms/ml of recombinant EPI (rEPI) which was purified to homogeneity by heparin-Sepharose chromatography, ion-exchange chromatography, and reverse phase high performance liquid chromatography.	Heparin	109-116	tissue factor pathway inhibitor	Homo sapiens	61-64
1962905-20	1990	Fatty acid analysis (LPL and HTGL) was less affected by LMW heparin than by unfractionated heparin.	Heparin	60-67	lipase C, hepatic type	Homo sapiens	29-33
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	20-27	serpin family D member 1	Homo sapiens	117-122
11434705-2	2001	Recent work has suggested that tissue factor pathway inhibitor (TFPI) may contribute to the antithrombotic activity of heparin by inhibiting the extrinsic pathway of coagulation.	Heparin	119-126	tissue factor pathway inhibitor	Homo sapiens	31-62
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	103-110	serpin family D member 1	Homo sapiens	117-122
1962908-8	1990	Some low molecular weight heparin preparations have significant activity with HC II (approximately 10 to 20% that of standard heparin).	Heparin	26-33	serpin family D member 1	Homo sapiens	78-83
1962908-8	1990	Some low molecular weight heparin preparations have significant activity with HC II (approximately 10 to 20% that of standard heparin).	Heparin	126-133	serpin family D member 1	Homo sapiens	78-83
11434705-2	2001	Recent work has suggested that tissue factor pathway inhibitor (TFPI) may contribute to the antithrombotic activity of heparin by inhibiting the extrinsic pathway of coagulation.	Heparin	119-126	tissue factor pathway inhibitor	Homo sapiens	64-68
1962909-1	1990	The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system.	Heparin	34-41	serpin family D member 1	Homo sapiens	107-112
1962909-1	1990	The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system.	Heparin	61-69	serpin family D member 1	Homo sapiens	107-112
11434705-3	2001	We have investigated the effect of heparin on TFPI and have found that when unfractionated heparin is given by continuous intravenous infusion to hospitalized inpatients, TFPI levels increase 2.3-fold and remain high as long as heparin is continued, but return to baseline levels soon after the infusion is stopped.	Heparin	35-42	tissue factor pathway inhibitor	Homo sapiens	46-50
11434705-3	2001	We have investigated the effect of heparin on TFPI and have found that when unfractionated heparin is given by continuous intravenous infusion to hospitalized inpatients, TFPI levels increase 2.3-fold and remain high as long as heparin is continued, but return to baseline levels soon after the infusion is stopped.	Heparin	35-42	tissue factor pathway inhibitor	Homo sapiens	171-175
2400395-7	1990	3H-labelled HDL2 and HDL3 subfractions behaved differently under the precipitant action of heparin-Mn2+; fraction C (the richest in apolipoprotein E) produced the largest amount of radioactive and chemical precipitate.	Heparin	91-98	junctophilin 3	Homo sapiens	12-16
11434705-3	2001	We have investigated the effect of heparin on TFPI and have found that when unfractionated heparin is given by continuous intravenous infusion to hospitalized inpatients, TFPI levels increase 2.3-fold and remain high as long as heparin is continued, but return to baseline levels soon after the infusion is stopped.	Heparin	91-98	tissue factor pathway inhibitor	Homo sapiens	46-50
11434705-3	2001	We have investigated the effect of heparin on TFPI and have found that when unfractionated heparin is given by continuous intravenous infusion to hospitalized inpatients, TFPI levels increase 2.3-fold and remain high as long as heparin is continued, but return to baseline levels soon after the infusion is stopped.	Heparin	91-98	tissue factor pathway inhibitor	Homo sapiens	171-175
11434705-3	2001	We have investigated the effect of heparin on TFPI and have found that when unfractionated heparin is given by continuous intravenous infusion to hospitalized inpatients, TFPI levels increase 2.3-fold and remain high as long as heparin is continued, but return to baseline levels soon after the infusion is stopped.	Heparin	91-98	tissue factor pathway inhibitor	Homo sapiens	46-50
11434705-3	2001	We have investigated the effect of heparin on TFPI and have found that when unfractionated heparin is given by continuous intravenous infusion to hospitalized inpatients, TFPI levels increase 2.3-fold and remain high as long as heparin is continued, but return to baseline levels soon after the infusion is stopped.	Heparin	91-98	tissue factor pathway inhibitor	Homo sapiens	171-175
1974403-2	1990	Arteparon (GAGPS), heparin, heparan sulfate, chondroitin sulfate, and dextran sulfate, but not dextran, inhibited HLE-mediated hydrolysis of succinyl-ala2-val-pNA.	Heparin	19-26	elastase, neutrophil expressed	Homo sapiens	114-117
11434705-4	2001	In contrast, therapeutic doses of the low molecular weight heparin, dalteparin, resulted in significantly less TFPI induction.	Heparin	59-66	tissue factor pathway inhibitor	Homo sapiens	111-115
11278860-0	2001	Binding of heparin/heparan sulfate to fibroblast growth factor receptor 4.	Heparin	11-18	fibroblast growth factor receptor 4	Homo sapiens	38-73
2146125-3	1990	The apo(a) portion of Lp(a) binds to the carboxy-terminal heparin-binding domain of fibronectin.	Heparin	58-65	lipoprotein(a)	Homo sapiens	22-27
1700488-0	1990	Regulation of plasmin, miniplasmin, and streptokinase-plasmin complex by alpha 2-antiplasmin, alpha 2-macroglobulin, and antithrombin III in the presence of heparin.	Heparin	157-164	plasminogen	Homo sapiens	14-21
11278860-6	2001	We have performed structural characterization of heparin/heparan sulfate oligosaccharides with affinity toward FGFR4.	Heparin	49-56	fibroblast growth factor receptor 4	Homo sapiens	111-116
1700488-2	1990	Heparin enhanced the reaction of antithrombin III (AT) with plasmin (up to 40-fold with 20 units/ml).	Heparin	0-7	plasminogen	Homo sapiens	60-67
11278860-8	2001	The FGFR4-binding saccharide domains contained both 2-O-sulfated iduronic acid and 6-O-sulfated N-sulfoglucosamine residues, as shown by experiments with selectively desulfated heparin, compositional disaccharide analysis, and a novel exoenzyme-based sequence analysis of heparan sulfate oligosaccharides.	Heparin	177-184	fibroblast growth factor receptor 4	Homo sapiens	4-9
11278668-0	2001	Heparin-binding histidine and lysine residues of rat selenoprotein P.	Heparin	0-7	selenoprotein P	Rattus norvegicus	53-68
2197015-12	1990	OMMT has been purified from the livers of irradiated rats by solubilization in high-salt-containing buffer, ammonium sulfate precipitation and a series of column chromatographic steps, including phenyl-Sepharose, heparin-agarose, double-stranded DNA-cellulose and FPLC.	Heparin	213-220	O-6-methylguanine-DNA methyltransferase	Rattus norvegicus	0-4
2169656-0	1990	Protein C inhibitor and other components of the protein C pathway in patients with acute deep vein thrombosis during heparin treatment.	Heparin	117-124	serpin family A member 5	Homo sapiens	0-19
2402751-1	1990	Human platelet factor 4 (PF4), a high affinity heparin binding protein, is released from stimulated platelets and stored at vascular sites, predominantly in liver, from where it can be brought back into circulation by heparin.	Heparin	47-54	platelet factor 4	Homo sapiens	25-28
2402751-2	1990	We attempted to define structural requirements for PF4 binding to heparin and for the pattern of its clearance from the circulation.	Heparin	66-73	platelet factor 4	Homo sapiens	51-54
2402751-3	1990	Intact PF4 bound strongly to heparin agarose and was eluted at 1.4 M NaCl, while reduced PF4 and PF4 C-terminal peptides PF4 (47-70) and PF4 (58-70) bound weakly and were eluted at 0.2-0.5 M NaCl.	Heparin	29-36	platelet factor 4	Homo sapiens	7-10
2402751-5	1990	Heparin eliminated the fast component of PF4 clearance, but it did not affect clearance of reduced PF4 or C-terminal PF4 peptides.	Heparin	0-7	platelet factor 4	Homo sapiens	41-44
2402751-7	1990	In conclusion, specific binding sites and native conformation of the molecule are critical for high affinity PF4 binding to insolubilized heparin and for a pattern of PF4 clearance from the circulation in the presence of heparin.	Heparin	138-145	platelet factor 4	Homo sapiens	109-112
2402751-7	1990	In conclusion, specific binding sites and native conformation of the molecule are critical for high affinity PF4 binding to insolubilized heparin and for a pattern of PF4 clearance from the circulation in the presence of heparin.	Heparin	221-228	platelet factor 4	Homo sapiens	109-112
2402751-7	1990	In conclusion, specific binding sites and native conformation of the molecule are critical for high affinity PF4 binding to insolubilized heparin and for a pattern of PF4 clearance from the circulation in the presence of heparin.	Heparin	221-228	platelet factor 4	Homo sapiens	167-170
2116167-6	1990	t-PA and generated plasmin bound to the liposome surface heparin were protected from inhibition by plasminogen activator inhibitor type 1 and alpha 2-plasmin inhibitor, respectively.	Heparin	57-64	plasminogen	Homo sapiens	19-26
7907085-7	1994	Heparin, but not its inactive isoform, completely blocked the PACAP-stimulated increase in [Ca2+]i, while Ins(1,4,5)P3 stimulated oscillations in [Ca2+]i very similar to those observed in response to PACAP.	Heparin	0-7	adenylate cyclase activating polypeptide 1	Rattus norvegicus	62-67
7907085-7	1994	Heparin, but not its inactive isoform, completely blocked the PACAP-stimulated increase in [Ca2+]i, while Ins(1,4,5)P3 stimulated oscillations in [Ca2+]i very similar to those observed in response to PACAP.	Heparin	0-7	adenylate cyclase activating polypeptide 1	Rattus norvegicus	200-205
8307953-1	1994	The role of heparin or heparan sulfates in the interaction of basic fibroblast growth factor (bFGF) with its high affinity receptor were investigated using purified extracellular ligand-binding region of FGF receptor-1 (FGFR-1) and intact receptors expressed in a myeloid cell line (32D) that does not express detectable levels of heparan sulfate proteoglycans or in Chinese hamster ovary (CHO) cell mutants defective in heparan sulfate synthesis.	Heparin	12-19	fibroblast growth factor 2	Mus musculus	94-98
8043225-7	1994	Pre-incubation of gp120 with excess sCD4 increases the potency of heparin in blocking the binding of V3 loop monoclonals severalfold.	Heparin	66-73	stearoyl-CoA desaturase 5	Homo sapiens	36-40
8288571-0	1994	Hairpin loop and second kringle domain are essential sites for heparin binding and biological activity of hepatocyte growth factor.	Heparin	63-70	hepatocyte growth factor	Homo sapiens	106-130
11278668-11	2001	The present results indicate that histidine is a constituent of the heparin-binding site of selenoprotein P.	Heparin	68-75	selenoprotein P	Rattus norvegicus	92-107
8288571-1	1994	Hepatocyte growth factor (HGF) has a strong affinity for heparin.	Heparin	57-64	hepatocyte growth factor	Homo sapiens	0-24
8288571-1	1994	Hepatocyte growth factor (HGF) has a strong affinity for heparin.	Heparin	57-64	hepatocyte growth factor	Homo sapiens	26-29
1976012-4	1990	On the other hand, interaction of MTSP-1 with sulfated glycosaminoglycans, i.e., heparin and chondroitin sulfate, led to increased enzymatic activity and an altered fine specificity of MTSP-1 for peptide substrates.	Heparin	81-88	suppression of tumorigenicity 14 (colon carcinoma)	Mus musculus	34-40
11278668-12	2001	The presence of histidine, the pK(a) of which is 7.0, explains the release of selenoprotein P from heparin binding as pH rises above 7.0.	Heparin	99-106	selenoprotein P	Rattus norvegicus	78-93
1976012-4	1990	On the other hand, interaction of MTSP-1 with sulfated glycosaminoglycans, i.e., heparin and chondroitin sulfate, led to increased enzymatic activity and an altered fine specificity of MTSP-1 for peptide substrates.	Heparin	81-88	suppression of tumorigenicity 14 (colon carcinoma)	Mus musculus	185-191
8288571-2	1994	About one fourth of HGF secreted from MRC-5 human embryonic lung fibroblast cells was found to be associated with heparin and heparan sulfate proteoglycan on the cell surface and extracellular matrix.	Heparin	114-121	hepatocyte growth factor	Homo sapiens	20-23
8288571-3	1994	To identify heparin-binding sites within the HGF molecule, we constructed variously deleted mutant HGFs and examined their binding ability to an immobilized heparin column.	Heparin	12-19	hepatocyte growth factor	Homo sapiens	45-48
8288571-5	1994	These observations suggest that the N-terminal hairpin loop and the second kringle domain are essential for the heparin-binding of HGF.	Heparin	112-119	hepatocyte growth factor	Homo sapiens	131-134
11380428-2	2001	The major part of TFPI is releasable by heparin.	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	18-22
8288571-6	1994	The finding that HK1K2 competed the binding of 125I-HGF to immobilized heparin provided additional evidence that the N-terminal half of HGF alpha-chain is the principal heparin-binding site.	Heparin	71-78	hepatocyte growth factor	Homo sapiens	52-55
8288571-6	1994	The finding that HK1K2 competed the binding of 125I-HGF to immobilized heparin provided additional evidence that the N-terminal half of HGF alpha-chain is the principal heparin-binding site.	Heparin	71-78	hepatocyte growth factor	Homo sapiens	136-139
8288571-6	1994	The finding that HK1K2 competed the binding of 125I-HGF to immobilized heparin provided additional evidence that the N-terminal half of HGF alpha-chain is the principal heparin-binding site.	Heparin	169-176	hepatocyte growth factor	Homo sapiens	52-55
8288571-6	1994	The finding that HK1K2 competed the binding of 125I-HGF to immobilized heparin provided additional evidence that the N-terminal half of HGF alpha-chain is the principal heparin-binding site.	Heparin	169-176	hepatocyte growth factor	Homo sapiens	136-139
8288571-9	1994	Thus, it is likely that the basic clusters in these domains cooperatively contribute to the binding of HGF to the anionic heparin or heparan sulfate molecule.	Heparin	122-129	hepatocyte growth factor	Homo sapiens	103-106
7532390-4	1994	Heparin enhanced the mitogenic activity of aFGF, but it did no affect that of bFGF.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	43-47
7532390-5	1994	Heparin also partially inhibited or postponed the occurrence of cell differentiation induced by aFGF.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	96-100
8187229-2	1994	In in vitro experiments we could show that Lp(a) is quantitatively (&gt; 99%) precipitated from plasma by heparin in the pH range 4.6-5.2.	Heparin	106-113	lipoprotein(a)	Homo sapiens	43-48
8262929-11	1993	At optimal concentrations, the major mechanism of heparin action is also a reduction in the Ki of the initial encounter complex between factor Xa and rTFPI.	Heparin	50-57	tissue factor pathway inhibitor	Rattus norvegicus	150-155
8165616-0	1993	Protamine neutralization of the release of tissue factor pathway inhibitor activity by heparins.	Heparin	87-95	tissue factor pathway inhibitor	Homo sapiens	43-74
8165616-1	1993	The present study was designed to investigate the action of protamine on the release of tissue factor pathway inhibitor (TFPI) activity by unfractionated (UF) and low molecular weight (LMW) heparin in healthy individuals.	Heparin	190-197	tissue factor pathway inhibitor	Homo sapiens	88-119
8165616-1	1993	The present study was designed to investigate the action of protamine on the release of tissue factor pathway inhibitor (TFPI) activity by unfractionated (UF) and low molecular weight (LMW) heparin in healthy individuals.	Heparin	190-197	tissue factor pathway inhibitor	Homo sapiens	121-125
8269931-5	1993	The addition of heparin increased by approximately eightfold the initial rate of progelatinase A autolytic activation but did not affect the activation of a deletion mutant that lacked the C-terminal domain [des-(418-631)progelatinase A].	Heparin	16-23	matrix metallopeptidase 2	Homo sapiens	81-96
2317527-10	1990	To determine whether oleic acid release of 125I-LPL from heparin-agarose was due to binding of the fatty acid to heparin or LPL, oleic acid was incubated with either LPL or heparin-agarose prior to performing the affinity chromatography.	Heparin	57-64	lipoprotein lipase	Bos taurus	48-51
2317527-11	1990	Only the prior incubation with LPL affected the binding to heparin-agarose.	Heparin	59-66	lipoprotein lipase	Bos taurus	31-34
2317527-12	1990	This demonstrates that dissociation of LPL from heparin required interaction of fatty acid with LPL.	Heparin	48-55	lipoprotein lipase	Bos taurus	96-99
2099192-0	1990	Heparin inhibits c-fos and c-myc mRNA expression in vascular smooth muscle cells.	Heparin	0-7	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	27-32
2099192-2	1990	In this paper we show that heparin suppressed the induction of c-fos and c-myc mRNA in rat and calf VSMC.	Heparin	27-34	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	73-78
2155237-5	1990	The NGF-stimulated kinase activity is unaffected by direct addition to the assay of the heat-stable cAMP-dependent kinase peptide inhibitor, staurosporine, or K-252A, is slightly stimulated by heparin and is inhibited by sodium fluoride and calcium ions.	Heparin	193-200	nerve growth factor	Rattus norvegicus	4-7
2341544-1	1990	The heparin-binding growth factors aFGF and bFGF (acidic and basic fibroblast growth factor) from crude bovine brain extract were co-eluted with purified [125I]aFGF and/or [125I]bFGF as tracers from heparin-Sepharose and from several insoluble substituted polystyrenes used as stationary phases in low-pressure affinity chromatography.	Heparin	4-11	fibroblast growth factor 1	Bos taurus	35-39
2316625-3	1990	Epidermal growth factor (EGF) partially reversed heparin-induced growth inhibition in a dose-dependent fashion with a maximum effect seen at 1 ng/ml.	Heparin	49-56	epidermal growth factor like 1	Rattus norvegicus	0-23
2316625-3	1990	Epidermal growth factor (EGF) partially reversed heparin-induced growth inhibition in a dose-dependent fashion with a maximum effect seen at 1 ng/ml.	Heparin	49-56	epidermal growth factor like 1	Rattus norvegicus	25-28
2316625-5	1990	A decrease in EGF-stimulated incorporation of 3H-thymidine by GEC was seen with as little as 2 hours of heparin exposure and persisted for up to 48 hours.	Heparin	104-111	epidermal growth factor like 1	Rattus norvegicus	14-17
2316625-6	1990	Heparin consistently increased binding of 125I-EGF to GEC with a significant increase apparent after 2 hours of exposure and a further increase with a 24-hour exposure.	Heparin	0-7	epidermal growth factor like 1	Rattus norvegicus	47-50
2316625-7	1990	Increased EGF binding to heparin-treated cells was due to a significant increase in the association constant of EGF and its receptor with no effect on receptor number.	Heparin	25-32	epidermal growth factor like 1	Rattus norvegicus	10-13
2316625-7	1990	Increased EGF binding to heparin-treated cells was due to a significant increase in the association constant of EGF and its receptor with no effect on receptor number.	Heparin	25-32	epidermal growth factor like 1	Rattus norvegicus	112-115
8263781-8	1993	The IP3 receptor antagonist heparin, and depletion of intracellular Ca++ stores by thapsigargin or A23187, inhibited ACh-induced contraction of LES but not of esophageal muscle.	Heparin	28-35	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	4-16
8108596-5	1993	Statistically significant reductions of the basal values were found for Lp(a) and the other lipids in the blood taken before the beginning of dialysis, 30 min" after the heparin bolus.	Heparin	170-177	lipoprotein(a)	Homo sapiens	72-77
8108596-7	1993	The values of Lp(a) had not so high increase as consequence of more elevated affinity with heparin and of a possible enhanced metabolic rate via lipoprotein lipase.	Heparin	91-98	lipoprotein(a)	Homo sapiens	14-19
11380428-3	2001	We recently found eight patients with thrombosis and low levels of heparin-releasable TFPI in whom we investigated the TFPI gene for mutations.	Heparin	67-74	tissue factor pathway inhibitor	Homo sapiens	86-90
11380428-3	2001	We recently found eight patients with thrombosis and low levels of heparin-releasable TFPI in whom we investigated the TFPI gene for mutations.	Heparin	67-74	tissue factor pathway inhibitor	Homo sapiens	119-123
2159933-1	1990	The HeLa transcription factor LSF has been purified by heparin-agarose and DNA affinity chromatography, and its DNA binding and transcription properties have been characterized.	Heparin	55-62	transcription factor CP2	Homo sapiens	30-33
7693696-5	1993	However, the latter derivative competed with native heparin for binding to FGF-2 and thus blocked the ability of native heparin to promote the mitogenic activity of FGF-2.	Heparin	52-59	fibroblast growth factor 2	Mus musculus	75-80
11322758-0	2001	Mapping a heparin binding site on ErbB-3 epidermal growth factor receptor.	Heparin	10-17	erb-b2 receptor tyrosine kinase 3	Homo sapiens	34-40
7693696-5	1993	However, the latter derivative competed with native heparin for binding to FGF-2 and thus blocked the ability of native heparin to promote the mitogenic activity of FGF-2.	Heparin	52-59	fibroblast growth factor 2	Mus musculus	165-170
7693696-5	1993	However, the latter derivative competed with native heparin for binding to FGF-2 and thus blocked the ability of native heparin to promote the mitogenic activity of FGF-2.	Heparin	120-127	fibroblast growth factor 2	Mus musculus	165-170
7693696-6	1993	The 6-O-desulfated heparin also prevented the ability of FGF-2 to suppress myogenic differentiation in MM14 mouse myoblasts.	Heparin	19-26	fibroblast growth factor 2	Mus musculus	57-62
7693043-8	1993	Preliminary studies show that a proportion of the PECAM-1 molecules on the lymphomyeloid/multipotential progenitor cell line, KG1, and on the monocytic cell line, U937, binds to heparin-sepharose.	Heparin	178-185	platelet and endothelial cell adhesion molecule 1	Homo sapiens	50-57
7693043-9	1993	A soluble form of PECAM-1 also binds heparin-sepharose.	Heparin	37-44	platelet and endothelial cell adhesion molecule 1	Homo sapiens	18-25
2124560-0	1990	Effect of intestinal diamine oxidase (DAO) depletion by heparin on mucosal polyamine metabolism.	Heparin	56-63	amine oxidase, copper containing 1	Rattus norvegicus	21-36
2124560-0	1990	Effect of intestinal diamine oxidase (DAO) depletion by heparin on mucosal polyamine metabolism.	Heparin	56-63	amine oxidase, copper containing 1	Rattus norvegicus	38-41
2124560-3	1990	heparin to deplete intestinal mucosal DAO stores.	Heparin	0-7	amine oxidase, copper containing 1	Rattus norvegicus	38-41
2124560-4	1990	We found that heparin significantly reduced mean DAO activity (p less than 0.001).	Heparin	14-21	amine oxidase, copper containing 1	Rattus norvegicus	49-52
2124560-6	1990	Heparin-induced DAO depletion had no significant effect on spermine and spermidine levels at either site.	Heparin	0-7	amine oxidase, copper containing 1	Rattus norvegicus	16-19
33766781-4	2021	We used a heparin/PF4 immunoassay (PF4 ELISA) as a case study.	Heparin	10-17	platelet factor 4	Homo sapiens	35-38
8263410-3	1993	LPL and a number of other molecules, including growth factors and clotting factors, bind to heparin-affinity gels and are eluted using high concentrations of salt.	Heparin	92-99	lipoprotein lipase	Bos taurus	0-3
8408053-1	1993	Chondroitin 6-sulfotransferase, which transfers sulfate from 3"-phosphoadenylyl sulfate to position 6 of N-acetylgalactosamine in chondroitin, was purified 1,430-fold to apparent homogeneity with a 22% yield from the serum-free culture medium of chick embryo chondrocytes by affinity chromatography on heparin-Sepharose CL-6B, wheat germ agglutinin-agarose, and 3",5"-ADP-agarose.	Heparin	302-309	carbohydrate sulfotransferase 3	Gallus gallus	0-30
11322758-2	2001	Here we show that the ErbB-3 receptor, but not other members of this receptor family, binds to immobilized heparin and can be dissociated only at a high ionic strength comparable to that required for fibroblast growth factor receptors.	Heparin	107-114	erb-b2 receptor tyrosine kinase 3	Homo sapiens	22-28
33801235-3	2021	Our initial findings showed that heparin-mimicking moieties inhibited the fusion of mononucleated myoblasts into multinucleated myotubes, as indicated by the decreased gene and protein expression levels of myogenic factors, myotube fusion-related markers, and focal adhesion kinase (FAK).	Heparin	33-40	protein tyrosine kinase 2	Homo sapiens	260-281
33801235-3	2021	Our initial findings showed that heparin-mimicking moieties inhibited the fusion of mononucleated myoblasts into multinucleated myotubes, as indicated by the decreased gene and protein expression levels of myogenic factors, myotube fusion-related markers, and focal adhesion kinase (FAK).	Heparin	33-40	protein tyrosine kinase 2	Homo sapiens	283-286
7692842-9	1993	DNA or heparin (another polyanion) activated tyrosine hydroxylase and decreased fluorescence of the reporter group 30% at pH 6.0.	Heparin	7-14	tyrosine hydroxylase	Rattus norvegicus	45-65
11322758-4	2001	Primary sequence analysis of ErbB-3 identified a basic amino acid cluster (466)KHNRPRR(472) localized to the proximal, cysteine-rich extracellular ligand binding domain of the receptor, with charge density and distribution compatible with, but different to, known linear heparin binding motifs.	Heparin	271-278	erb-b2 receptor tyrosine kinase 3	Homo sapiens	29-35
33801235-4	2021	We further elucidated the underlying molecular mechanism via transcriptome analyses, observing that the insulin/PI3K/mTOR and Wnt signaling pathways were significantly downregulated by heparin-mimicking moieties through the inhibition of FAK/Cav3.	Heparin	185-192	protein tyrosine kinase 2	Homo sapiens	238-241
33801235-4	2021	We further elucidated the underlying molecular mechanism via transcriptome analyses, observing that the insulin/PI3K/mTOR and Wnt signaling pathways were significantly downregulated by heparin-mimicking moieties through the inhibition of FAK/Cav3.	Heparin	185-192	caveolin 3	Homo sapiens	242-246
11322758-6	2001	Finally, antibodies directed to the putative heparin binding peptide, efficiently bind the native receptor suggesting a novel target for blocking heparin mediated ErbB-3 interactions.	Heparin	45-52	erb-b2 receptor tyrosine kinase 3	Homo sapiens	163-169
8216224-11	1993	for protease nexin I, protein C inhibitor and antithrombin III showed a bell-shaped dependence on heparin concentration.	Heparin	98-105	serpin family A member 5	Homo sapiens	22-41
8216224-12	1993	At optimal concentrations, heparin accelerated the rate of inhibition by protease nexin I, protein C inhibitor and antithrombin III by 44-, 18- and 13-fold respectively.	Heparin	27-34	serpin family A member 5	Homo sapiens	91-110
11247813-3	2001	However, treatment of permeabilized Y-79 cells with heparin, a nonselective GRK inhibitor, reduced homologous desensitization of CRF1 receptors by approximately 35%.	Heparin	52-59	corticotropin releasing hormone receptor 1	Homo sapiens	129-133
8292716-6	1993	Heparin and Ca2+ together, but not individually, enhance the rate of factor Xa inhibition by full-length TFPI.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	105-109
34550550-6	2022	We further analyzed binding of BMP-4 GF to the proteoglycan Heparin and showed that an N-terminal basic sequence is essential for this interaction.	Heparin	60-67	bone morphogenetic protein 4	Cricetulus griseus	31-36
34550550-7	2022	Taken together, these results provide novel insights into the purification, localization, and Heparin binding of human BMP-4 that have implications for its bioprocessing and biological function.	Heparin	94-101	bone morphogenetic protein 4	Homo sapiens	119-124
11254842-9	2001	Heparin concentration correlated with levels of total TFPI (r2 = 0.613, p &lt; 0.0001) and free TFPI (r2 = 0.689, p &lt; 0.0001).	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	54-58
34961309-2	2022	Herein, gelatin was chemically modified with heparin that specifically interacted with and stabilized bone morphogenetic protein-2 (BMP-2).	Heparin	45-52	bone morphogenetic protein 2	Homo sapiens	102-130
34961309-2	2022	Herein, gelatin was chemically modified with heparin that specifically interacted with and stabilized bone morphogenetic protein-2 (BMP-2).	Heparin	45-52	bone morphogenetic protein 2	Homo sapiens	132-137
8270909-19	1993	Intracellular application of heparin or of the monoclonal antibody against the IP3 receptor, mAb18A10, inhibited the ACh and His responses in a concentration-dependent fashion.	Heparin	29-36	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	79-91
11254842-9	2001	Heparin concentration correlated with levels of total TFPI (r2 = 0.613, p &lt; 0.0001) and free TFPI (r2 = 0.689, p &lt; 0.0001).	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	96-100
7515734-2	1993	By Scatchard analysis of the aFGF binding to the BEL cell surface, we show that heparin at 10 micrograms/ml abolishes completely aFGF binding to LAR and reduces by half the number of aFGF HAR.	Heparin	80-87	fibroblast growth factor 1	Bos taurus	29-33
7515734-2	1993	By Scatchard analysis of the aFGF binding to the BEL cell surface, we show that heparin at 10 micrograms/ml abolishes completely aFGF binding to LAR and reduces by half the number of aFGF HAR.	Heparin	80-87	fibroblast growth factor 1	Bos taurus	129-133
11254842-11	2001	CONCLUSION: These data indicate that TFPI release by heparin probably has an important role in the suppression of the tissue factor-dependent coagulation pathway during CPB.	Heparin	53-60	tissue factor pathway inhibitor	Homo sapiens	37-41
7515734-2	1993	By Scatchard analysis of the aFGF binding to the BEL cell surface, we show that heparin at 10 micrograms/ml abolishes completely aFGF binding to LAR and reduces by half the number of aFGF HAR.	Heparin	80-87	fibroblast growth factor 1	Bos taurus	129-133
7515734-6	1993	The dimerization process of aFGF on LAR is abolished by addition of heparin.	Heparin	68-75	fibroblast growth factor 1	Bos taurus	28-32
11167786-0	2001	Anti-PF4-heparin immunoglobulin G is the major class of heparin-induced thrombocytopenia antibody: findings of an enzyme-linked immunofiltration assay using membrane-bound hPF4-heparin.	Heparin	9-16	platelet factor 4	Homo sapiens	5-8
7515734-8	1993	Heparin at 10 micrograms/ml suppresses specifically aFGF dimer internalization and reduces by half the total amount of internalized aFGF native form.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	52-56
7515734-8	1993	Heparin at 10 micrograms/ml suppresses specifically aFGF dimer internalization and reduces by half the total amount of internalized aFGF native form.	Heparin	0-7	fibroblast growth factor 1	Bos taurus	132-136
8358737-4	1993	An M(r) 29,000 bFGF-like form eluted from heparin-Sepharose by 0.6 M NaCl was found in extracts of both NDP and LTP cells.	Heparin	42-49	fibroblast growth factor 2	Mus musculus	15-19
8358737-4	1993	An M(r) 29,000 bFGF-like form eluted from heparin-Sepharose by 0.6 M NaCl was found in extracts of both NDP and LTP cells.	Heparin	42-49	Norrie disease (pseudoglioma) (human)	Mus musculus	104-107
8358737-8	1993	The M(r) 29,000 form present in the conditioned medium of NDP cells was retained on heparin-Sepharose.	Heparin	84-91	Norrie disease (pseudoglioma) (human)	Mus musculus	58-61
8395347-3	1993	We now demonstrate that low (physiological) agonist concentrations evoke local cytosolic Ca2+ spikes in the secretory pole of single mouse pancreatic acinar cells that are particularly sensitive to blockade by the IP3 receptor antagonist heparin.	Heparin	238-245	inositol 1,4,5-triphosphate receptor 3	Mus musculus	214-226
34929169-4	2022	Biochemical experiments corroborated the simulation results, showing that heparin inhibits the furin-mediated cleavage of spike by binding to the S1/S2 site.	Heparin	74-81	furin, paired basic amino acid cleaving enzyme	Homo sapiens	95-100
34929169-4	2022	Biochemical experiments corroborated the simulation results, showing that heparin inhibits the furin-mediated cleavage of spike by binding to the S1/S2 site.	Heparin	74-81	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	122-127
34929169-6	2022	In simulations of the closed spike homotrimer, heparin binds the RBD and the N-terminal domain of two adjacent spike subunits and hinders opening.	Heparin	47-54	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	29-34
34929169-6	2022	In simulations of the closed spike homotrimer, heparin binds the RBD and the N-terminal domain of two adjacent spike subunits and hinders opening.	Heparin	47-54	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	111-116
34929169-7	2022	In simulations of open spike conformations, heparin induces stabilization of the hinge region and a change in RBD motion.	Heparin	44-51	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	23-28
34929169-8	2022	Taken together, our results indicate that heparin can inhibit SARS-CoV-2 infection by three mechanisms: by allosterically hindering binding to the host cell receptor, by directly competing with binding to host heparan sulfate proteoglycan co-receptors, and by preventing spike cleavage by furin.	Heparin	42-49	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	271-276
34929169-8	2022	Taken together, our results indicate that heparin can inhibit SARS-CoV-2 infection by three mechanisms: by allosterically hindering binding to the host cell receptor, by directly competing with binding to host heparan sulfate proteoglycan co-receptors, and by preventing spike cleavage by furin.	Heparin	42-49	furin, paired basic amino acid cleaving enzyme	Homo sapiens	289-294
34946571-7	2021	Thus, by means of computational molecular modelling, docking and dynamics, we also provide a characterization at an atomic level of the binding modes of the Tat/heparin interaction, with heparin herein used as a structural analogue of the heparan sulfate chains of syndecan-1.	Heparin	161-168	tyrosine aminotransferase	Homo sapiens	157-160
34946571-7	2021	Thus, by means of computational molecular modelling, docking and dynamics, we also provide a characterization at an atomic level of the binding modes of the Tat/heparin interaction, with heparin herein used as a structural analogue of the heparan sulfate chains of syndecan-1.	Heparin	187-194	tyrosine aminotransferase	Homo sapiens	157-160
8349603-3	1993	HGF/NK1 was expressed in Escherichia coli and purified to homogeneity using heparin-affinity and fast protein liquid cation-exchange chromatography.	Heparin	76-83	hepatocyte growth factor	Homo sapiens	0-3
11167786-1	2001	An enzyme-linked immunofiltration assay (ELIFA) was developed for detecting anti-human platelet factor 4 (hPF4)-heparin antibody in sera of patients with heparin-induced thrombocytopenia (HIT).	Heparin	112-119	platelet factor 4	Homo sapiens	106-110
11167786-2	2001	The immunofiltration assay was developed to capture HIT antibody by hPF4-heparin complex adsorbed onto a positively charged nylon membrane, as an alternative to plastic bound hPF4.	Heparin	73-80	platelet factor 4	Homo sapiens	68-72
11167786-4	2001	With SRA-negative sera from thrombocytopenic patients treated with heparin, anti-hPF4-heparin IgG and IgA were detected in 16% (n = 126) and 14% (n = 74) of sera respectively; 6% (n = 71) of SRA-negative sera contained both IgG and IgA anti-hPF4-heparin antibodies.	Heparin	86-93	platelet factor 4	Homo sapiens	81-85
8344959-7	1993	Heparin and heparan sulfate, but not chondroitin sulfate, inhibited N-syndecan-bFGF binding.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	79-83
34214257-3	2021	Anti-PF4 antibodies are also seen in heparin-induced thrombocytopenia, though most cases of VITT do not have prior heparin exposure.	Heparin	37-44	platelet factor 4	Homo sapiens	5-8
11132652-5	2000	Additionally, we conducted in vitro experiments to investigate the effect of unfractionated heparin and TFPI, which is released from the endothelium by heparin, on FVII:C, FVIIa, and FVII:Ag.	Heparin	152-159	tissue factor pathway inhibitor	Homo sapiens	104-108
34233058-1	2021	In late February 2021, the first cases of vaccine-induced thrombosis and thrombocytopenia (VITT) were observed in patients after immunization with the ChAdOx1 nCoV-19 adenoviral vector vaccine (Oxford, AstraZeneca) against SARS-CoV-2.1 This prothrombotic response is presumed to be mediated by anti-platelet factor 4 (PF4) antibodies that activate platelets and induce activation and extracellular traps formation of neutrophils.2 These antibodies can also be seen in autoimmune heparin-induced thrombocytopenia, but all the described cases had no previous exposure to heparin.	Heparin	479-486	platelet factor 4	Homo sapiens	318-321
34233058-1	2021	In late February 2021, the first cases of vaccine-induced thrombosis and thrombocytopenia (VITT) were observed in patients after immunization with the ChAdOx1 nCoV-19 adenoviral vector vaccine (Oxford, AstraZeneca) against SARS-CoV-2.1 This prothrombotic response is presumed to be mediated by anti-platelet factor 4 (PF4) antibodies that activate platelets and induce activation and extracellular traps formation of neutrophils.2 These antibodies can also be seen in autoimmune heparin-induced thrombocytopenia, but all the described cases had no previous exposure to heparin.	Heparin	569-576	platelet factor 4	Homo sapiens	318-321
7688769-12	1993	We conclude that adult human lung fibroblasts produce at least two soluble heparin-binding growth factors, KGF and HGF/SF, which promote DNA synthesis and proliferation of rat alveolar type II cells in primary culture.	Heparin	75-82	hepatocyte growth factor	Homo sapiens	115-121
11132652-6	2000	Heparin infusion decreased triglycerides and increased FFA and TFPI.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	63-67
8397450-2	1993	One assay is specific for active PCI and measures its ability to form complexes with activated protein C (APC) in the presence of heparin (Espana et al, Thromb Res 64, 309, 1991) (Method A).	Heparin	130-137	APC regulator of WNT signaling pathway	Homo sapiens	106-109
8397450-3	1993	After incubation of samples with heparin and an excess of APC, the amount of APC:PCI formed is measured by an ELISA.	Heparin	33-40	APC regulator of WNT signaling pathway	Homo sapiens	77-80
8397450-3	1993	After incubation of samples with heparin and an excess of APC, the amount of APC:PCI formed is measured by an ELISA.	Heparin	33-40	serpin family A member 5	Homo sapiens	81-84
7683196-8	1993	Addition of the beta 2-agonists produced a mean inhibition of released heparin of 71% (50, 92), and 73% (55, 91), respectively.	Heparin	71-78	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	16-22
7683196-10	1993	The beta 2-agonists salbutamol and fenoterol strongly inhibited heparin release from mast cells.	Heparin	64-71	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	4-10
34940684-7	2021	RS inhibition of the interaction of heparin, a highly sulfated HS, with the SARS-CoV-2 spike protein (from wild type and different mutant variants) was studied using surface plasmon resonance (SPR).	Heparin	36-43	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	87-92
34336365-9	2021	Notably, seven cases presented with anti-PF4-heparin antibodies (range: 1.18-1.79 U/mL) after vaccination, and none of them exhibited any sign of thrombotic disorder.	Heparin	45-52	platelet factor 4	Homo sapiens	41-44
11156723-0	2000	Combining low-molecular-weight heparin and glycoprotein IIb/IIIa antagonists for the treatment of acute coronary syndromes: the NICE 3 story.	Heparin	31-38	chromosome 1 open reading frame 43	Homo sapiens	128-134
11101692-1	2000	Connective tissue growth factor (CTGF) is a recently described heparin-binding mitogen for fibroblasts and smooth muscle cells.	Heparin	63-70	cellular communication network factor 2	Homo sapiens	0-31
34189574-1	2021	Heparin-induced thrombocytopenia (HIT) is a prothrombotic disorder mediated by ultra-large immune complexes (ULICs) containing IgG antibodies to a multivalent antigen composed of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	198-201
8473315-7	1993	In addition, plasma concentrations of both forms of TFPI, in stoichiometric complex with factor Xa, inhibited cell surface factor VIIa-tissue factor proteolytic activity markedly faster than plasma levels of antithrombin III, even in the presence of 1 unit/ml heparin.	Heparin	260-267	tissue factor pathway inhibitor	Homo sapiens	52-56
8388739-9	1993	Because in this model the profibrinolytic effect of APC is directly related to its anticoagulant properties we predicted and confirmed that other anticoagulants--like heparin--also have profibrinolytic activity.	Heparin	167-174	APC regulator of WNT signaling pathway	Homo sapiens	52-55
11101692-1	2000	Connective tissue growth factor (CTGF) is a recently described heparin-binding mitogen for fibroblasts and smooth muscle cells.	Heparin	63-70	cellular communication network factor 2	Homo sapiens	33-37
34062319-6	2021	TTS is characterized by exposure to one of the aforementioned vaccines 4-30 days prior to presentation, followed by thrombosis, mild-to-severe thrombocytopenia, and a positive platelet factor-4 (PF4)-heparin enzyme-linked immunosorbent assay (ELISA).	Heparin	200-207	platelet factor 4	Homo sapiens	195-198
10944532-0	2000	Fibroblast growth factor-2 stimulation of p42/44MAPK phosphorylation and IkappaB degradation is regulated by heparan sulfate/heparin in rat mammary fibroblasts.	Heparin	125-132	fibroblast growth factor 2	Rattus norvegicus	0-26
8455038-0	1993	Transcription-independent activation of ornithine decarboxylase activity by heparin in cloned cerebral endothelial cells.	Heparin	76-83	ornithine decarboxylase 1	Homo sapiens	40-63
8455038-2	1993	Here we have shown that besides its growth factor-supportive role, heparin exerts a specific action on cerebral capillary endothelial cells (cECs), unrelated to serum or growth factors, by increasing activity of ornithine decarboxylase (ODC; EC 4.1.1.17) in these cells.	Heparin	67-74	ornithine decarboxylase 1	Homo sapiens	212-235
8455038-2	1993	Here we have shown that besides its growth factor-supportive role, heparin exerts a specific action on cerebral capillary endothelial cells (cECs), unrelated to serum or growth factors, by increasing activity of ornithine decarboxylase (ODC; EC 4.1.1.17) in these cells.	Heparin	67-74	ornithine decarboxylase 1	Homo sapiens	237-240
8455038-4	1993	Heparin action on ODC activity was shown to be dose dependent within the range of 1-100 micrograms/ml.	Heparin	0-7	ornithine decarboxylase 1	Homo sapiens	18-21
8455038-7	1993	As evidenced by northern analysis, the heparin-mediated enhancement of ODC activity was not accompanied by changes of ODC mRNA levels.	Heparin	39-46	ornithine decarboxylase 1	Homo sapiens	71-74
34461442-2	2021	A mechanism similar to heparin-induced thrombocytopenia was proposed with antibodies to platelet factor 4 (PF4).	Heparin	23-30	platelet factor 4	Homo sapiens	88-105
34461442-2	2021	A mechanism similar to heparin-induced thrombocytopenia was proposed with antibodies to platelet factor 4 (PF4).	Heparin	23-30	platelet factor 4	Homo sapiens	107-110
8388347-2	1993	TFPI is released to the blood after injection of heparin or low molecular weight heparin (LMWH).	Heparin	49-56	tissue factor pathway inhibitor	Homo sapiens	0-4
11041873-7	2000	However, when heparin was present, 6xHis-EK-mMCP-6 yielded active enzyme when enterokinase cleavage was performed at pH 5.5-6.0 but not at neutral pH.	Heparin	14-21	transmembrane protease, serine 15	Mus musculus	78-90
8388347-2	1993	TFPI is released to the blood after injection of heparin or low molecular weight heparin (LMWH).	Heparin	81-88	tissue factor pathway inhibitor	Homo sapiens	0-4
8388347-4	1993	Free TFPI has higher affinity for heparin than TFPI which is associated with lipoproteins.	Heparin	34-41	tissue factor pathway inhibitor	Homo sapiens	5-9
8388347-5	1993	Heparin increases the rate of inactivation of FXa and of tissue factor-F VIIa by TFPI.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	81-85
8388348-0	1993	Is tissue factor pathway inhibitor involved in the antithrombotic effect of heparins?	Heparin	76-84	tissue factor pathway inhibitor	Homo sapiens	3-34
8388348-2	1993	Tissue factor pathway inhibitor (TFPI) is released into the circulation after intravenous or subcutaneous injection of heparin or low-molecular-weight heparin (Logiparin) in humans.	Heparin	119-126	tissue factor pathway inhibitor	Homo sapiens	0-31
34769095-0	2021	Complexation of CXCL12, FGF-2 and VEGF with Heparin Modulates the Protein Release from Alginate Microbeads.	Heparin	44-51	C-X-C motif chemokine ligand 12	Homo sapiens	16-22
34769095-3	2021	In order to regulate such interactions between proteins and the Alg matrix, we propose to complex proteins of interest in this study - CXCL12, FGF-2, VEGF - with polyanionic heparin prior to their encapsulation into Alg microbeads of high content of alpha-L-guluronic acid units (high-G).	Heparin	174-181	C-X-C motif chemokine ligand 12	Homo sapiens	135-141
8388348-2	1993	Tissue factor pathway inhibitor (TFPI) is released into the circulation after intravenous or subcutaneous injection of heparin or low-molecular-weight heparin (Logiparin) in humans.	Heparin	119-126	tissue factor pathway inhibitor	Homo sapiens	33-37
11085010-8	2000	In addition, the concentrations of the soluble plasma protein markers F1 + 2, FPA, PMN-elastase, TCC and beta-TG were significantly lower (p &lt; 0.05) in the presence of heparin coating.	Heparin	171-178	elastase, neutrophil expressed	Homo sapiens	83-95
8388348-2	1993	Tissue factor pathway inhibitor (TFPI) is released into the circulation after intravenous or subcutaneous injection of heparin or low-molecular-weight heparin (Logiparin) in humans.	Heparin	151-158	tissue factor pathway inhibitor	Homo sapiens	0-31
8388348-2	1993	Tissue factor pathway inhibitor (TFPI) is released into the circulation after intravenous or subcutaneous injection of heparin or low-molecular-weight heparin (Logiparin) in humans.	Heparin	151-158	tissue factor pathway inhibitor	Homo sapiens	33-37
8388348-3	1993	The plasma concentration of TFPI is increased 2- to 4-fold by a prophylactic dose of Logiparin, and this excess TFPI remains in the circulation only in the presence of the heparin.	Heparin	172-179	tissue factor pathway inhibitor	Homo sapiens	28-32
8388348-4	1993	TFPI and heparin show strong synergism in clotting assays at concentrations obtained after heparin injection in humans.	Heparin	91-98	tissue factor pathway inhibitor	Homo sapiens	0-4
8388348-6	1993	It is concluded that the release of TFPI may contribute significantly to the antithrombotic effect of heparin.	Heparin	102-109	tissue factor pathway inhibitor	Homo sapiens	36-40
8468524-3	1993	LPL secretion in the presence of 10 U/ml heparin was used as a means of estimating LPL synthesis.	Heparin	41-48	lipoprotein lipase	Gallus gallus	83-86
8457651-1	1993	Bovine factor XIIa inhibitor was purified by an improved method employing affinity for heparin.	Heparin	87-94	serpin family G member 1	Bos taurus	7-28
34671356-1	2021	Syndecan-1 (SDC-1) is a transmembrane proteoglycan of heparin sulfate that can regulate various cell signal transduction pathways in the airway epithelial cells and fibroblasts.	Heparin	54-61	syndecan 1	Homo sapiens	0-10
34671356-1	2021	Syndecan-1 (SDC-1) is a transmembrane proteoglycan of heparin sulfate that can regulate various cell signal transduction pathways in the airway epithelial cells and fibroblasts.	Heparin	54-61	syndecan 1	Homo sapiens	12-17
34596979-3	2021	In this study, we compared the binding of four inflammatory cytokines (CCL8, IL-1beta, IL-2 and IL-6) to immobilized heparin by an SPR analysis.	Heparin	117-124	C-C motif chemokine ligand 8	Homo sapiens	71-75
34526009-0	2021	Platelet factor 4 polyanion immune complexes: heparin induced thrombocytopenia and vaccine-induced immune thrombotic thrombocytopenia.	Heparin	46-53	platelet factor 4	Homo sapiens	0-17
34526009-2	2021	MAIN BODY/TEXT: Immune-mediated thrombocytopenia occurs when specific antibodies bind to platelet factor 4 /heparin complexes.	Heparin	108-115	platelet factor 4	Homo sapiens	89-106
34526009-3	2021	Platelet factor 4 is a naturally occurring chemokine, and under certain conditions, may complex with negatively charged molecules and polyanions, including heparin.	Heparin	156-163	platelet factor 4	Homo sapiens	0-17
34526009-4	2021	The antibody-platelet factor 4/heparin complex may lead to platelet activation, accompanied by other cascading reactions, resulting in cerebral sinus thrombosis, deep vein thrombosis, lower limb arterial thrombosis, myocardial infarction, pulmonary embolism, skin necrosis, and thrombotic stroke.	Heparin	31-38	platelet factor 4	Homo sapiens	13-30
11085010-8	2000	In addition, the concentrations of the soluble plasma protein markers F1 + 2, FPA, PMN-elastase, TCC and beta-TG were significantly lower (p &lt; 0.05) in the presence of heparin coating.	Heparin	171-178	pro-platelet basic protein	Homo sapiens	105-112
34479472-0	2021	Correction to: 2-O, 3-O desulfated heparin (ODSH) increases bacterial clearance and attenuates lung injury in cystic fibrosis by restoring HMGB1-compromised macrophage function.	Heparin	35-42	high mobility group box 1	Homo sapiens	139-144
8444314-17	1993	Fractionation studies indicate that p120 has accessible free sulfhydryl group(s) and can bind ssDNA and heparin.	Heparin	104-111	catenin delta 1	Homo sapiens	36-40
10891449-0	2000	Heparin-induced thrombocytopenia: new evidence for the dynamic binding of purified anti-PF4-heparin antibodies to platelets and the resultant platelet activation.	Heparin	0-7	platelet factor 4	Homo sapiens	88-91
8434786-3	1993	GSH-Px was not retained by either of these columns but selenoprotein P was retained by heparin-Sepharose and albumin by reactive blue.	Heparin	87-94	selenoprotein P	Rattus norvegicus	55-70
8434786-4	1993	After the two columns were separated, selenoprotein P was eluted with heparin from heparin-Sepharose and albumin eluted from reactive blue with high salt.	Heparin	70-77	selenoprotein P	Rattus norvegicus	38-53
8434786-4	1993	After the two columns were separated, selenoprotein P was eluted with heparin from heparin-Sepharose and albumin eluted from reactive blue with high salt.	Heparin	83-90	selenoprotein P	Rattus norvegicus	38-53
8148157-1	1993	Basic fibroblast growth factor is a biologically active peptide with a strong affinity for heparin.	Heparin	91-98	fibroblast growth factor 2	Mus musculus	0-30
34153666-10	2021	Inhibition of ERK, CREB and interference with PTN expression notably weakened the heparin-mediated neuroprotective effects and restrained the expression of ERK/CREB and PTN/syndecan-3 pathway.	Heparin	82-89	pleiotrophin	Rattus norvegicus	46-49
34153666-11	2021	CONCLUSION: Heparin attenuates the secondary brain injury induced by CA-CPR through regulating the ERK/CREB-mediated PTN/syndecan-3 pathway.	Heparin	12-19	pleiotrophin	Rattus norvegicus	117-120
34386689-0	2021	Heparin-induced thrombocytopenia in end-stage renal disease: Reliability of the PF4-heparin ELISA.	Heparin	84-91	platelet factor 4	Homo sapiens	80-83
10928482-9	2000	Functional factor VIIa activity fell significantly in the systemic circulation, probably due to the heparin-induced increase (approximately 15-fold) in tissue factor pathway inhibitor (TFPI), but was elevated in pericardial blood compared with that taken from the central line catheter (p &lt;0.006).	Heparin	100-107	tissue factor pathway inhibitor	Homo sapiens	152-183
34386689-2	2021	Objective: To correlate 4T scores, IgG heparin-platelet factor 4 (PF4-heparin) ELISA results, and serotonin release assay (SRA) results in patients with ESRD.	Heparin	70-77	platelet factor 4	Homo sapiens	66-69
34386689-3	2021	Methods: We performed a retrospective review of patients with ESRD (creatinine clearance < 15 mL/min or on renal replacement therapy (RRT)) who underwent PF4-heparin ELISA testing from October 2015 to September 2019.	Heparin	158-165	platelet factor 4	Homo sapiens	154-157
34233346-2	2021	VITT resembles heparin-induced thrombocytopenia (HIT) as it is associated with platelet-activating antibodies against platelet factor 4 (PF4)4; however, patients with VITT develop thrombocytopenia and thrombosis without heparin exposure.	Heparin	15-22	platelet factor 4	Homo sapiens	137-142
34233346-4	2021	Using alanine scanning mutagenesis5, we determined the binding of VITT anti-PF4 antibodies (n=5) was restricted to 8 surface amino acids, all of which were located within the heparin binding site on PF4, and the binding was inhibited by heparin.	Heparin	175-182	platelet factor 4	Homo sapiens	76-79
1281430-0	1992	The interaction of a glycosaminoglycan, heparin, with HIV-1 major envelope glycoprotein.	Heparin	40-47	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	66-87
1454803-7	1992	Injecting heparin along with acidic fibroblast growth factor or basic fibroblast growth factor further enhanced the degree of photoreceptor survival and also suppressed the increased incidence of macrophages produced by either factor, especially basic fibroblast growth factor.	Heparin	10-17	fibroblast growth factor 2	Rattus norvegicus	246-276
34233346-4	2021	Using alanine scanning mutagenesis5, we determined the binding of VITT anti-PF4 antibodies (n=5) was restricted to 8 surface amino acids, all of which were located within the heparin binding site on PF4, and the binding was inhibited by heparin.	Heparin	175-182	platelet factor 4	Homo sapiens	199-202
1423638-7	1992	Heparin enhanced the growth-promoting effect of IL-1 on the IL-1-dependent helper T cell clone, D10.G4.1, and enhanced IL-1 receptor expression on these cells.	Heparin	0-7	interleukin 1 complex	Mus musculus	48-52
10928482-9	2000	Functional factor VIIa activity fell significantly in the systemic circulation, probably due to the heparin-induced increase (approximately 15-fold) in tissue factor pathway inhibitor (TFPI), but was elevated in pericardial blood compared with that taken from the central line catheter (p &lt;0.006).	Heparin	100-107	tissue factor pathway inhibitor	Homo sapiens	185-189
1423638-7	1992	Heparin enhanced the growth-promoting effect of IL-1 on the IL-1-dependent helper T cell clone, D10.G4.1, and enhanced IL-1 receptor expression on these cells.	Heparin	0-7	interleukin 1 complex	Mus musculus	60-64
1423638-7	1992	Heparin enhanced the growth-promoting effect of IL-1 on the IL-1-dependent helper T cell clone, D10.G4.1, and enhanced IL-1 receptor expression on these cells.	Heparin	0-7	interleukin 1 complex	Mus musculus	60-64
1423638-8	1992	These data indicate that heparin acts directly on the T cells and enhances their responsiveness to IL-1 by up-regulating IL-1 receptor expression.	Heparin	25-32	interleukin 1 complex	Mus musculus	99-103
1423638-8	1992	These data indicate that heparin acts directly on the T cells and enhances their responsiveness to IL-1 by up-regulating IL-1 receptor expression.	Heparin	25-32	interleukin 1 complex	Mus musculus	121-125
1517210-4	1992	Heparin/heparan sulfate interaction is required before, e.g. basic fibroblast growth factor (bFGF) can associate with its high affinity cell surface receptors and trigger signal transduction.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	61-91
34233346-4	2021	Using alanine scanning mutagenesis5, we determined the binding of VITT anti-PF4 antibodies (n=5) was restricted to 8 surface amino acids, all of which were located within the heparin binding site on PF4, and the binding was inhibited by heparin.	Heparin	237-244	platelet factor 4	Homo sapiens	76-79
34289657-8	2022	Moreover, SARS-CoV-2 spike proteins directly block complement factor H from binding to heparin, which may lead to complement dysregulation on the cell surface.	Heparin	87-94	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	21-26
34288442-1	2021	Heparin-induced thrombocytopenia (HIT) is a prothrombotic condition resulting from pathogenic antibodies to complexes of heparin and platelet factor 4 (PF4).	Heparin	0-7	platelet factor 4	Homo sapiens	152-155
34288442-1	2021	Heparin-induced thrombocytopenia (HIT) is a prothrombotic condition resulting from pathogenic antibodies to complexes of heparin and platelet factor 4 (PF4).	Heparin	121-128	platelet factor 4	Homo sapiens	152-155
34288442-3	2021	Laboratory testing for HIT typically includes an immunoassay to detect antibodies to PF4-heparin and a functional assay.	Heparin	89-96	platelet factor 4	Homo sapiens	85-88
1517210-4	1992	Heparin/heparan sulfate interaction is required before, e.g. basic fibroblast growth factor (bFGF) can associate with its high affinity cell surface receptors and trigger signal transduction.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	93-97
10847421-0	2000	Dose-dependent release of endogenous tissue factor pathway inhibitor by different low molecular weight heparins.	Heparin	103-111	tissue factor pathway inhibitor	Homo sapiens	37-68
1324733-2	1992	The HTGL activity released into the medium by heparin, increased after the addition of T3 in a both time- (27% increase after 24 and 75% increase after 48 h) and dose-dependent manner (maximum activity with over 0.2 micrograms/ml of T3 in the medium).	Heparin	46-53	lipase C, hepatic type	Homo sapiens	4-8
35471628-9	2022	Therefore, targeting of the HMGB1 pathway by anti-HMGB1 agents, such as heparin, resveratrol and metformin, may decrease COVID-19 severity.	Heparin	72-79	high mobility group box 1	Homo sapiens	28-33
10847421-1	2000	Tissue factor pathway inhibitor (TFPI) is released to circulating blood after intravenous and subcutaneous injections of heparins, and may thus contribute to the antithrombotic effect of heparins.	Heparin	121-129	tissue factor pathway inhibitor	Homo sapiens	0-31
35471628-9	2022	Therefore, targeting of the HMGB1 pathway by anti-HMGB1 agents, such as heparin, resveratrol and metformin, may decrease COVID-19 severity.	Heparin	72-79	high mobility group box 1	Homo sapiens	50-55
1510142-5	1992	Addition of heparin to the medium resulted in a peak of LPL activity during the first 2 min, followed by a shoulder of relatively high activity, which gradually declined to a constant rate from 30 min.	Heparin	12-19	lipoprotein lipase	Cavia porcellus	56-59
10847421-1	2000	Tissue factor pathway inhibitor (TFPI) is released to circulating blood after intravenous and subcutaneous injections of heparins, and may thus contribute to the antithrombotic effect of heparins.	Heparin	121-129	tissue factor pathway inhibitor	Homo sapiens	33-37
10847421-1	2000	Tissue factor pathway inhibitor (TFPI) is released to circulating blood after intravenous and subcutaneous injections of heparins, and may thus contribute to the antithrombotic effect of heparins.	Heparin	187-195	tissue factor pathway inhibitor	Homo sapiens	0-31
10847421-1	2000	Tissue factor pathway inhibitor (TFPI) is released to circulating blood after intravenous and subcutaneous injections of heparins, and may thus contribute to the antithrombotic effect of heparins.	Heparin	187-195	tissue factor pathway inhibitor	Homo sapiens	33-37
1420819-6	1992	Both unfractionated heparin, low-molecular-weight heparins and pentosan polysulphate induce release of TFPI after intravenous injection, whereas dermatan sulphate does not.	Heparin	20-27	tissue factor pathway inhibitor	Homo sapiens	103-107
1420819-6	1992	Both unfractionated heparin, low-molecular-weight heparins and pentosan polysulphate induce release of TFPI after intravenous injection, whereas dermatan sulphate does not.	Heparin	50-58	tissue factor pathway inhibitor	Homo sapiens	103-107
35313081-9	2022	All four heparin variants reverse histone-mediated impairment of APC generation in a dose-dependent manner.	Heparin	9-16	APC regulator of WNT signaling pathway	Homo sapiens	65-68
10847421-2	2000	A previous study suggested different abilities of various low molecular weight heparins (LMWH) to release endogenous TFPI, but the dose-response relationship was not determined.	Heparin	79-87	tissue factor pathway inhibitor	Homo sapiens	117-121
35313081-11	2022	In contrast, the ability of heparin to neutralize histone-mediated impairment of APC generation is independent of size and anticoagulant activity.	Heparin	28-35	APC regulator of WNT signaling pathway	Homo sapiens	81-84
1420819-7	1992	The interactions with TFPI account for a considerable amount of the anticoagulant effect of heparin.	Heparin	92-99	tissue factor pathway inhibitor	Homo sapiens	22-26
10952323-6	2000	The red cell clogging rate (RCR) and clogging particles (RCP) were significantly lower in the heparin group (p=0.0212 and p=0.0409 respectively.	Heparin	94-101	CGRP receptor component	Homo sapiens	57-60
1433988-4	1992	The deleted form of recombinant HGF (rHGF) had slightly lower heparin binding affinity than the intact form.	Heparin	62-69	hepatocyte growth factor	Homo sapiens	32-35
35533259-2	2022	A subset of heparin-treated patients produces detectable levels of antibodies against complexes of heparin bound to circulating platelet factor 4 (PF4).	Heparin	12-19	platelet factor 4	Homo sapiens	147-150
35533259-2	2022	A subset of heparin-treated patients produces detectable levels of antibodies against complexes of heparin bound to circulating platelet factor 4 (PF4).	Heparin	99-106	platelet factor 4	Homo sapiens	147-150
1378017-6	1992	The binding of GMP-140 to primed T cells is not influenced by preactivation with phorbol 12-myristate 13-acetate, is almost completely abolished by pretreatment of T cells with neuraminidase or trypsin, and is also strongly inhibited by EDTA, the soluble sulfated glycans dextran sulfate, fucoidan, and heparin, but not by chondroitin sulfates.	Heparin	303-310	neuraminidase 1	Homo sapiens	177-190
1380142-4	1992	Opossum brain heparin binding growth factor 1 (HBGF-1), a minor peak of activity, eluted from heparin-Sepharose at 1.1 NaCl and contained a 16.2 kDa protein that cross-reacted with antiserum against bovine aFGF.	Heparin	14-21	fibroblast growth factor 1	Bos taurus	47-53
35533259-3	2022	Using a genome-wide association study (GWAS) approach, we aimed to identify genetic variants associated with anti-PF4/heparin antibodies that account for the variable antibody response seen in HIT.	Heparin	118-125	platelet factor 4	Homo sapiens	114-117
35513125-6	2022	Heparin specifically mediated FGF23 binding to FGFR4, and increased FGF23 stimulatory effects on hypertrophic growth and contractility in isolated cardiac myocytes.	Heparin	0-7	fibroblast growth factor receptor 4	Homo sapiens	47-52
35132672-2	2022	Currently, information on the characteristics and persistence of anti-PF4 antibodies that cause VITT after Ad26.COV2.S vaccination is limited, and available diagnostic assays fail to differentiate Ad26.COV2.S and ChAdOx1 nCoV-19-associated VITT from similar clinical disorders, namely heparin-induced thrombocytopenia (HIT) and spontaneous HIT.	Heparin	285-292	platelet factor 4	Homo sapiens	70-73
1597470-12	1992	We identified in brain-derived HB-GAM fractions a 17-kDa protein (p17) that is detached from heparin by a slightly higher salt concentration as compared to HB-GAM.	Heparin	93-100	pleiotrophin	Rattus norvegicus	31-37
10823874-4	2000	In addition, this study shows that VCP-through its ability to bind to glycosaminoglycans (heparin-like molecules) on the surface of human endothelial cells-is able to block antibody binding to surface major histocompatibility complex class I molecules.	Heparin	90-97	valosin containing protein	Homo sapiens	35-38
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Heparin	102-109	serpin family D member 1	Homo sapiens	21-25
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Heparin	0-3	serpin family D member 1	Homo sapiens	21-25
1374012-8	1992	We conclude that the inhibitory effects of heparin and bFGF on CDP are independent of effects on cell replication.	Heparin	43-50	cut-like homeobox 1	Rattus norvegicus	63-66
1374012-10	1992	However, the inhibition of collagen synthesis by heparin and bFGF appears to involve divergent pathways since exogenous IGF-1 could overcome the effect of heparin but not bFGF on collagen synthesis.	Heparin	155-162	fibroblast growth factor 2	Rattus norvegicus	61-65
1562726-10	1992	This form of rTFPI elutes from heparin-agarose at 0.28 mol/L NaCl and inhibits factor Xa at a rate that is slower than rTFPI(0.3).	Heparin	31-38	tissue factor pathway inhibitor	Rattus norvegicus	13-18
35088086-0	2022	Glycosylation site Asn168 is important for slow in vivo clearance of recombinant human diamine oxidase heparin-binding motif mutants.	Heparin	103-110	amine oxidase copper containing 1	Homo sapiens	87-102
10823874-6	2000	Segments of this protein, generated by genetic engineering of the DNA encoding VCP into the Pichia pastoris expression system, were used to localize the regions with heparin binding activity.	Heparin	166-173	valosin containing protein	Homo sapiens	79-82
35196163-8	2022	Comparative quantitative tandem-mass-tag proteomics and functional assays on the heparin-binding secretomes of WT-MEF and Pdia3-/- MEF identified multiple ECM and growth factor proteins to be down-regulated in the CM of Pdia3-/- MEF.	Heparin	81-88	E74-like factor 4 (ets domain transcription factor)	Mus musculus	131-134
10864991-9	2000	CONCLUSION: Patients undergoing SPA column treatments, especially those with thrombocytopenia, may be at increased risk of bleeding as a result of the presence of a significant amount of heparin in their circulation during the entire period of SPA column treatment.	Heparin	187-194	surfactant protein A1	Homo sapiens	244-247
1313031-5	1992	Heparin interfered with the inhibition of tissue kallikrein by PCI and with the formation of tissue kallikrein-PCI complexes in a dose-dependent fashion and completely abolished PCI-tissue kallikrein interaction at 300 micrograms/ml.	Heparin	0-7	serpin family A member 5	Homo sapiens	63-66
10772861-8	2000	We modeled the LBP(205-229) domain, which is strongly predicted to have a helical secondary structure, and determined that this region likely possesses heparin-binding characteristics located to one side of the helix, while the opposite side appears to contain a hydrophobic patch where peptide 11 could bind.	Heparin	152-159	galectin 3	Homo sapiens	15-18
1313031-5	1992	Heparin interfered with the inhibition of tissue kallikrein by PCI and with the formation of tissue kallikrein-PCI complexes in a dose-dependent fashion and completely abolished PCI-tissue kallikrein interaction at 300 micrograms/ml.	Heparin	0-7	serpin family A member 5	Homo sapiens	111-114
1313031-5	1992	Heparin interfered with the inhibition of tissue kallikrein by PCI and with the formation of tissue kallikrein-PCI complexes in a dose-dependent fashion and completely abolished PCI-tissue kallikrein interaction at 300 micrograms/ml.	Heparin	0-7	serpin family A member 5	Homo sapiens	111-114
1313031-6	1992	This is in contrast to findings on the interaction of PCI with all other target proteases studied so far (i.e. stimulation of inhibition by heparin) but is similar to the reaction pattern of 125I-labeled tissue kallikrein with so called kallikrein binding protein described in serum and other systems.	Heparin	140-147	serpin family A member 5	Homo sapiens	54-57
1313031-8	1992	In normal serum, formed complexes co-migrated with complexes of purified PCI and 125I-kallikrein and were less intense in the presence of heparin.	Heparin	138-145	serpin family A member 5	Homo sapiens	73-76
1551875-3	1992	Here we show that synthetic peptides derived from similar V3 regions of several isolates of HIV-1 bind [3H]heparin, and we also demonstrate that [3H]heparin binds to recombinant gp120 IIIB.	Heparin	149-156	Envelope surface glycoprotein gp160, precursor	Human immunodeficiency virus 1	178-183
35419151-9	2022	A heparin-induced thrombocytopenia with thrombosis (HITT) like syndrome caused by the genesis of a platelet-activating autoantibody against platelet factor 4 (PF4) triggered by adenoviral vector-based COVID-19 vaccinations is understood to be the underlying pathophysiology.	Heparin	2-9	platelet factor 4	Homo sapiens	159-162
35419157-1	2022	Heparin-induced thrombocytopenia (HIT) is a prothrombotic state caused by autoantibodies against platelet factor 4 (PF4)-heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	116-119
10769077-7	2000	Finally, our analysis of NS3 processive unwinding under single cycle conditions by addition of heparin in both helicase and RNA-stimulated ATPase assays led to two conclusions: (i) NS3-associated helicase acts processively; (ii) most of the NS3 RNA-stimulated ATPase activity may not be directly coupled to translocation of the enzyme along the substrate RNA molecule.	Heparin	95-102	helicase for meiosis 1	Homo sapiens	196-204
35194375-0	2022	In silico investigations of heparin binding to SARS-CoV-2 variants with a focus at the RBD/ACE2 interface.	Heparin	28-35	angiotensin converting enzyme 2	Homo sapiens	91-95
35194375-2	2022	Several studies have indicated that heparin and its derivatives interact to SARS-CoV-2 S-RBD and inhibits the binding of ACE2 which blocks the viral invasion.	Heparin	36-43	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	87-88
35194375-2	2022	Several studies have indicated that heparin and its derivatives interact to SARS-CoV-2 S-RBD and inhibits the binding of ACE2 which blocks the viral invasion.	Heparin	36-43	angiotensin converting enzyme 2	Homo sapiens	121-125
35194375-3	2022	However, it is largely unclear how these SARS-CoV-2 variants affects ACE2 binding in the presence of heparin.	Heparin	101-108	angiotensin converting enzyme 2	Homo sapiens	69-73
35194375-6	2022	Further, we showed that most of the RBD mutations increased the binding affinity of ACE2 in the absence of heparin, with the maximum increase observed for N501Y (-13.7 kcal/mol).	Heparin	107-114	angiotensin converting enzyme 2	Homo sapiens	84-88
35194375-7	2022	Also, in the presence of heparin, ACE2 binds strongly to the mutant RBD as compared to WT RBD.	Heparin	25-32	angiotensin converting enzyme 2	Homo sapiens	34-38
35194375-8	2022	The strong RBD/ACE2 interaction was observed in case of triple variants (-11.3 kcal/mol) whereas, N501Y showed weakest binding of RBD/ACE2 in the presence of heparin (-9.2 kcal/mol).	Heparin	158-165	angiotensin converting enzyme 2	Homo sapiens	134-138
35194375-9	2022	The strong binding of ACE2 to RBD-heparin complex in these variants will leads to strong inhibition of their entry into host cells.	Heparin	34-41	angiotensin converting enzyme 2	Homo sapiens	22-26
35512905-1	2022	Vaccine-induced immune thrombotic thrombocytopenia (VITT) is a highly prothrombotic disorder that like heparin-induced thrombocytopenia (HIT) is caused by platelet-activating antibodies that recognize platelet factor 4 (PF4).	Heparin	103-110	platelet factor 4	Homo sapiens	220-223
1371124-9	1992	The relative ability of heparin to reduce SMC proliferation was not altered by the presence of bFGF.bFGF also induced profound angiogenesis within and surrounding the polymeric releasing device, and in the vasa vasorum immediately around the injured arteries.	Heparin	24-31	fibroblast growth factor 2	Rattus norvegicus	100-104
1377413-3	1992	In particular the antibody called 10B2, which also recognizes the human molecule, is able to block PF4"s ability to neutralize heparin in a modified Heparin-Factor Xa chromogenic assay.	Heparin	127-134	platelet factor 4	Homo sapiens	99-102
1283495-2	1992	Concentration of bFGF in cell extract was measured by sandwich radioimmunoassay (RIA) with heparin-Sepharose and 125I-labeled monoclonal antibody.	Heparin	91-98	fibroblast growth factor 2	Rattus norvegicus	17-21
1442260-1	1992	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Heparin	43-50	serpin family D member 1	Homo sapiens	54-58
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	89-93
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	196-200
1442261-0	1992	The interaction between LACI and heparin.	Heparin	33-40	tissue factor pathway inhibitor	Homo sapiens	24-28
35512907-8	2022	The transient nature of the immune response towards PF4 in VITT makes it likely that-as in heparin-induced thrombocytopenia -marginal zone B cells are key for antibody production.	Heparin	91-98	platelet factor 4	Homo sapiens	52-55
10764593-3	2000	Furthermore, NAP-1 and NAP-2 phosphorylation in crude HeLa cell extracts is abolished by heparin, a specific inhibitor of CKII.	Heparin	89-96	nucleosome assembly protein 1 like 4	Homo sapiens	23-28
35370682-2	2022	HGF is sequestered by heparin-like protein in its inactive form and is widespread in the extracellular matrix of most tissues.	Heparin	22-29	hepatocyte growth factor	Homo sapiens	0-3
35229724-7	2022	GPIHBP1 trafficking across ECs in the mutant mice was normalized by disrupting LPL-HSPG electrostatic interactions with either heparin or an AD peptide.	Heparin	127-134	GPI-anchored HDL-binding protein 1	Mus musculus	0-7
1554154-3	1992	Their results show that HRG, like PF 4, has an affinity, not only for heparin, but also for DS.	Heparin	70-77	platelet factor 4	Homo sapiens	34-38
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Heparin	176-183	serpin family D member 1	Homo sapiens	0-19
1530786-7	1992	In patients with fulminant hepatic failure serum human hepatocyte growth factor levels were increased immediately after plasma exchange using heparin as the anticoagulant in 71% of the determinations.	Heparin	142-149	hepatocyte growth factor	Homo sapiens	55-79
1530786-9	1992	In 17 of 39 patients with chronic renal failure who had no liver disease, serum human hepatocyte growth factor levels were abnormally increased before hemodialysis using heparin, and the levels were elevated immediately after hemodialysis in all the patients.	Heparin	170-177	hepatocyte growth factor	Homo sapiens	86-110
1721064-7	1991	Further, HBGF-1, in the presence of heparin, down-regulates the levels of the Cox transcript in a dose- and time-dependent manner.	Heparin	36-43	cytochrome c oxidase subunit 8A	Homo sapiens	78-81
35120527-2	2022	Pathogenesis has been mainly related to platelet activation via PF4-reactive antibodies that activate platelets and may cross-react with heparin.	Heparin	137-144	platelet factor 4	Homo sapiens	64-67
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Heparin	176-183	serpin family D member 1	Homo sapiens	21-25
35131751-1	2022	BACKGROUND: Antibodies against cationic platelet chemokine, platelet factor 4 (PF4/CXCL4), have been described in heparin-induced thrombocytopenia (HIT), but also in patients positive for antiphospholipid antibodies (aPL) even in the absence of heparin treatment and HIT-related clinical manifestations.	Heparin	114-121	platelet factor 4	Homo sapiens	79-82
35131751-1	2022	BACKGROUND: Antibodies against cationic platelet chemokine, platelet factor 4 (PF4/CXCL4), have been described in heparin-induced thrombocytopenia (HIT), but also in patients positive for antiphospholipid antibodies (aPL) even in the absence of heparin treatment and HIT-related clinical manifestations.	Heparin	114-121	platelet factor 4	Homo sapiens	83-88
10681494-5	2000	However, when the cells were cultured on the cell-binding fragment and the heparin-binding fragment was added to the medium, focal adhesion formation was impaired in the syndecan-4 null fibroblasts as compared with that in wild-type cells.	Heparin	75-82	syndecan 4	Mus musculus	170-180
35131751-1	2022	BACKGROUND: Antibodies against cationic platelet chemokine, platelet factor 4 (PF4/CXCL4), have been described in heparin-induced thrombocytopenia (HIT), but also in patients positive for antiphospholipid antibodies (aPL) even in the absence of heparin treatment and HIT-related clinical manifestations.	Heparin	245-252	platelet factor 4	Homo sapiens	79-82
35131751-1	2022	BACKGROUND: Antibodies against cationic platelet chemokine, platelet factor 4 (PF4/CXCL4), have been described in heparin-induced thrombocytopenia (HIT), but also in patients positive for antiphospholipid antibodies (aPL) even in the absence of heparin treatment and HIT-related clinical manifestations.	Heparin	245-252	platelet factor 4	Homo sapiens	83-88
35131751-8	2022	CONCLUSIONS: Heparin treatment-independent anti-PF4 antibodies can be found in aPL-positive patients and asymptomatic carriers, but their presence, titre as well as in vitro effect on platelet activation are not affected by COVID-19 vaccination.	Heparin	13-20	platelet factor 4	Homo sapiens	48-51
1799658-1	1991	This study was performed in order to separate plasma fractions of tissue factor pathway inhibitor (TFPI) on the basis of TFPI"s heparin binding properties.	Heparin	128-135	tissue factor pathway inhibitor	Homo sapiens	66-97
1799658-1	1991	This study was performed in order to separate plasma fractions of tissue factor pathway inhibitor (TFPI) on the basis of TFPI"s heparin binding properties.	Heparin	128-135	tissue factor pathway inhibitor	Homo sapiens	99-103
1799658-1	1991	This study was performed in order to separate plasma fractions of tissue factor pathway inhibitor (TFPI) on the basis of TFPI"s heparin binding properties.	Heparin	128-135	tissue factor pathway inhibitor	Homo sapiens	121-125
1799658-4	1991	Heparin affinity chromatography separated plasma TFPI into four fractions with increasing heparin affinity: the flow-through fraction, a low affinity fraction eluting at less than 0.3 M NaCl, an intermediate affinity fraction eluting at 0.3-0.55 M NaCl and a high affinity fraction eluting at 0.55-1.0 M NaCl.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	49-53
1799658-10	1991	The anticoagulant effect of TFPI, relative to the chromogenic substrate TFPI activity, was greater in plasma fractions with high heparin affinity than in the other plasma TFPI fractions, and it was five-fold greater than the anticoagulant effect of recombinant TFPI.	Heparin	129-136	tissue factor pathway inhibitor	Homo sapiens	28-32
1799658-11	1991	Thus, plasma TFPI is heterogenous in heparin affinity and in anticoagulant potency.	Heparin	37-44	tissue factor pathway inhibitor	Homo sapiens	13-17
1724341-1	1991	We tested acid and basic fibroblast growth factor (aFGF and bFGF), members of the heparin binding FGF family, for their ability to stimulate bone resorption as measured by the release of previously incorporated 45Ca from cultured fetal rat long bones in the presence and absence of heparin.	Heparin	82-89	fibroblast growth factor 2	Rattus norvegicus	19-49
1724341-1	1991	We tested acid and basic fibroblast growth factor (aFGF and bFGF), members of the heparin binding FGF family, for their ability to stimulate bone resorption as measured by the release of previously incorporated 45Ca from cultured fetal rat long bones in the presence and absence of heparin.	Heparin	82-89	fibroblast growth factor 2	Rattus norvegicus	60-64
1724341-1	1991	We tested acid and basic fibroblast growth factor (aFGF and bFGF), members of the heparin binding FGF family, for their ability to stimulate bone resorption as measured by the release of previously incorporated 45Ca from cultured fetal rat long bones in the presence and absence of heparin.	Heparin	282-289	fibroblast growth factor 2	Rattus norvegicus	19-49
1724341-1	1991	We tested acid and basic fibroblast growth factor (aFGF and bFGF), members of the heparin binding FGF family, for their ability to stimulate bone resorption as measured by the release of previously incorporated 45Ca from cultured fetal rat long bones in the presence and absence of heparin.	Heparin	282-289	fibroblast growth factor 2	Rattus norvegicus	60-64
35225866-3	2022	Notably, PF4 binds with high affinity to heparin, and in HIT, complexes of PF4/H may, in a small proportion of susceptible patients, trigger the development of anti-PF4 antibodies and subsequent platelet activation and aggregation, ultimately leading to the development of pathological thrombosis at sites of vessel occlusion.	Heparin	41-48	platelet factor 4	Homo sapiens	9-12
35225866-3	2022	Notably, PF4 binds with high affinity to heparin, and in HIT, complexes of PF4/H may, in a small proportion of susceptible patients, trigger the development of anti-PF4 antibodies and subsequent platelet activation and aggregation, ultimately leading to the development of pathological thrombosis at sites of vessel occlusion.	Heparin	41-48	platelet factor 4	Homo sapiens	75-78
35054772-6	2022	Pre-treatment with heparin completely blocked CXCL4 uptake.	Heparin	19-26	platelet factor 4	Homo sapiens	46-51
10684625-0	2000	Potentiation and inhibition of bFGF binding by heparin: a model for regulation of cellular response.	Heparin	47-54	fibroblast growth factor 2	Mus musculus	31-35
10684625-4	2000	The addition of soluble heparin or heparan sulfate has been demonstrated to rescue the bFGF receptor binding affinity on heparan sulfate deficient cells yet has also been shown to inhibit binding under some conditions.	Heparin	24-31	fibroblast growth factor 2	Mus musculus	87-91
1932024-5	1991	Previous experiments have shown that lipoprotein(a) [Lp(a)] inhibits Pg activation by t-PA, but only in the presence of a template which enhances t-PA activity such as fibrinogen fragments or intact heparin.	Heparin	199-206	lipoprotein(a)	Homo sapiens	37-51
10684625-6	2000	In the study presented here, we have investigated the possibility that heparin binding to the cell surface might play a role in modulating bFGF receptor binding and activity.	Heparin	71-78	fibroblast growth factor 2	Mus musculus	139-143
1932024-5	1991	Previous experiments have shown that lipoprotein(a) [Lp(a)] inhibits Pg activation by t-PA, but only in the presence of a template which enhances t-PA activity such as fibrinogen fragments or intact heparin.	Heparin	199-206	lipoprotein(a)	Homo sapiens	53-58
10684625-8	2000	Low concentrations of heparin (0.1-30 nM) enhanced bFGF receptor binding to an extent that was inversely proportional to the amount of endogenous heparan sulfate sites present.	Heparin	22-29	fibroblast growth factor 2	Mus musculus	51-55
10684625-9	2000	At high concentrations (10 microM), heparin inhibited bFGF receptor binding in cells under all conditions.	Heparin	36-43	fibroblast growth factor 2	Mus musculus	54-58
10684625-10	2000	The ability of heparin to stimulate and inhibit bFGF-receptor binding correlated with altered bFGF-stimulated tyrosine kinase activity and cell proliferation.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	48-52
1782285-1	1991	The substance concentration of ionized calcium (cCa2+) in blood, plasma or serum preanalytically may be affected by pH changes of the sample, calcium binding by heparin, and dilution by the anticoagulant solution.	Heparin	161-168	crystallin beta B2	Homo sapiens	48-52
10684625-10	2000	The ability of heparin to stimulate and inhibit bFGF-receptor binding correlated with altered bFGF-stimulated tyrosine kinase activity and cell proliferation.	Heparin	15-22	fibroblast growth factor 2	Mus musculus	94-98
1833087-11	1991	However, inhibition of thrombin with heparin, hirudin, or D-Phe-D-Pro-L-Arg-chloromethylketone was more effective in inhibiting the acceleration of platelet activation induced by plasminogen activation, despite the elaboration of plasmin activity.	Heparin	37-44	plasminogen	Homo sapiens	179-186
10684625-12	2000	A mathematical model of this process revealed that the dual functions of heparin in bFGF binding were accurately represented by heparin cell binding-mediated stimulation and soluble heparin-mediated inhibition of bFGF receptor binding.	Heparin	73-80	fibroblast growth factor 2	Mus musculus	84-88
1665594-8	1991	PF4-dependent neutralization of anti-factor Xa and anti-thrombin activities of fixed concentrations of the LMW heparins was studied by measuring rate constants as function of PF4 concentration.	Heparin	111-119	platelet factor 4	Homo sapiens	0-3
10684625-12	2000	A mathematical model of this process revealed that the dual functions of heparin in bFGF binding were accurately represented by heparin cell binding-mediated stimulation and soluble heparin-mediated inhibition of bFGF receptor binding.	Heparin	73-80	fibroblast growth factor 2	Mus musculus	213-217
10684625-12	2000	A mathematical model of this process revealed that the dual functions of heparin in bFGF binding were accurately represented by heparin cell binding-mediated stimulation and soluble heparin-mediated inhibition of bFGF receptor binding.	Heparin	128-135	fibroblast growth factor 2	Mus musculus	84-88
10684625-12	2000	A mathematical model of this process revealed that the dual functions of heparin in bFGF binding were accurately represented by heparin cell binding-mediated stimulation and soluble heparin-mediated inhibition of bFGF receptor binding.	Heparin	128-135	fibroblast growth factor 2	Mus musculus	84-88
1835913-3	1991	We also studied the effects of low-dose aspirin (81 mg/day) on the plasma level of heparin-releasable PF4 in the CAD patients.	Heparin	83-90	platelet factor 4	Homo sapiens	102-105
1835913-7	1991	The PF4/beta-TG ratio after heparin injection was also higher in the CAD group than in the control group (p less than 0.01).	Heparin	28-35	pro-platelet basic protein	Homo sapiens	8-15
1835913-8	1991	There was a correlation between the PF4/beta-TG ratio after heparin and the Gensini CAD score, which defines the severity of coronary atherosclerosis (r = 0.489, n = 23, p less than 0.01).	Heparin	60-67	platelet factor 4	Homo sapiens	36-39
1835913-8	1991	There was a correlation between the PF4/beta-TG ratio after heparin and the Gensini CAD score, which defines the severity of coronary atherosclerosis (r = 0.489, n = 23, p less than 0.01).	Heparin	60-67	pro-platelet basic protein	Homo sapiens	40-47
1715572-11	1991	FDC-P1 cells expressing FGFR-1 bound aFGF and bFGF with high affinity but only in the presence of heparin.	Heparin	98-105	fibroblast growth factor receptor 1	Mus musculus	24-30
10613999-5	2000	In patients receiving concomitant heparin, identification of heparin-induced thrombocytopenia using an enzyme-linked immunosorbent assay to detect anti-heparin-PF4 antibodies is preferred.	Heparin	61-68	platelet factor 4	Homo sapiens	160-163
1755003-5	1991	These results show that the anti-Xa activity of some HTGL preparations is neither due to the lipase itself nor to the content of AT III, but suggest, that it could be due to contamination with another protein, which binds to heparin sepharose columns but is removed during ion exchange chromatography.	Heparin	225-232	lipase C, hepatic type	Homo sapiens	53-57
1755003-6	1991	Most likely the effect is due to the extrinsic pathway inhibitor (EPI), also called lipoprotein-associated coagulation inhibitor (LACI), which has recently been shown to be released by heparin.	Heparin	185-192	tissue factor pathway inhibitor	Homo sapiens	37-64
10665801-11	2000	Since heparin reduced paw oedema induced by PLA2 from Naja mocambique mocambique venom it is likely that this sPLA2 is similar to the novel heparin-sensitive PLA2 found in mast cells.	Heparin	6-13	phospholipase A2 group IIA	Rattus norvegicus	110-115
1755003-6	1991	Most likely the effect is due to the extrinsic pathway inhibitor (EPI), also called lipoprotein-associated coagulation inhibitor (LACI), which has recently been shown to be released by heparin.	Heparin	185-192	tissue factor pathway inhibitor	Homo sapiens	84-128
1755003-6	1991	Most likely the effect is due to the extrinsic pathway inhibitor (EPI), also called lipoprotein-associated coagulation inhibitor (LACI), which has recently been shown to be released by heparin.	Heparin	185-192	tissue factor pathway inhibitor	Homo sapiens	130-134
10632704-6	2000	Heparin inhibited midkine binding to sulfatide but weakly inhibited its binding to CHO-3-SO4.	Heparin	0-7	midkine	Mus musculus	18-25
10629596-8	2000	Platelet factor 4 (PF4) displaced from endothelial heparan sulphate or directly from the platelets, binds to the heparin molecule to form an immunogenic complex.	Heparin	113-120	platelet factor 4	Homo sapiens	0-17
1649167-4	1991	The enzyme also phosphorylates casein and ribosomal protein S6 and shares many properties with casein kinase I: (a) similar molecular weight, (b) utilization of ATP but not GTP as phosphoryl donor, and (c) sensitivity to inhibition by heparin.	Heparin	235-242	ribosomal protein S6	Homo sapiens	42-62
1853931-0	1991	Heparin alters epidermal growth factor metabolism in cultured rat glomerular epithelial cells.	Heparin	0-7	epidermal growth factor like 1	Rattus norvegicus	15-38
1853931-2	1991	The authors have previously shown that heparin and heparan sulfate inhibit glomerular visceral epithelial cell (GEC) growth and that epidermal growth factor (EGF) can partially reverse the effect of heparin.	Heparin	199-206	epidermal growth factor like 1	Rattus norvegicus	133-156
1853931-2	1991	The authors have previously shown that heparin and heparan sulfate inhibit glomerular visceral epithelial cell (GEC) growth and that epidermal growth factor (EGF) can partially reverse the effect of heparin.	Heparin	199-206	epidermal growth factor like 1	Rattus norvegicus	158-161
10629596-8	2000	Platelet factor 4 (PF4) displaced from endothelial heparan sulphate or directly from the platelets, binds to the heparin molecule to form an immunogenic complex.	Heparin	113-120	platelet factor 4	Homo sapiens	19-22
1853931-3	1991	The authors studied EGF processing by GEC in an attempt to clarify the mechanism by which heparin inhibits GEC growth.	Heparin	90-97	epidermal growth factor like 1	Rattus norvegicus	20-23
1853931-4	1991	Control and heparin-treated GEC rapidly internalized 125I-EGF (within 15 minutes).	Heparin	12-19	epidermal growth factor like 1	Rattus norvegicus	58-61
11251341-4	2000	TFPI is released from the vascular endothelium after injection of either unfractionated heparin (UFH) or low-molecular-weight heparins (LMWHs), which may then provide high concentrations of TFPI at sites of tissue damage and ongoing thrombosis.	Heparin	88-95	tissue factor pathway inhibitor	Homo sapiens	0-4
1853931-5	1991	In heparin-treated cells, 125I-EGF reappeared on the cell surface during the course of a 1-hour incubation and the percent internalized dropped significantly to 59.0% +/- 8.6%, suggesting recycling of 125I-EGF-occupied receptors.	Heparin	3-10	epidermal growth factor like 1	Rattus norvegicus	31-34
1853931-5	1991	In heparin-treated cells, 125I-EGF reappeared on the cell surface during the course of a 1-hour incubation and the percent internalized dropped significantly to 59.0% +/- 8.6%, suggesting recycling of 125I-EGF-occupied receptors.	Heparin	3-10	epidermal growth factor like 1	Rattus norvegicus	206-209
1853931-6	1991	After incubation with 125I-EGF, heparin-treated cells also released significantly more cpm of 125I into EGF-free medium (2526 +/- 68 cpm-H; 903 +/- 32-C).	Heparin	32-39	epidermal growth factor like 1	Rattus norvegicus	27-30
1853931-6	1991	After incubation with 125I-EGF, heparin-treated cells also released significantly more cpm of 125I into EGF-free medium (2526 +/- 68 cpm-H; 903 +/- 32-C).	Heparin	32-39	epidermal growth factor like 1	Rattus norvegicus	104-107
1853931-7	1991	Analysis of the released 125I by gel filtration chromatography showed more totally degraded 125I-EGF in media from heparin-treated cells (30.8% +/- 1.6% in heparin-treated versus 17.8% +/- 3.2 in control; P less than 0.05).	Heparin	115-122	epidermal growth factor like 1	Rattus norvegicus	97-100
1853931-7	1991	Analysis of the released 125I by gel filtration chromatography showed more totally degraded 125I-EGF in media from heparin-treated cells (30.8% +/- 1.6% in heparin-treated versus 17.8% +/- 3.2 in control; P less than 0.05).	Heparin	156-163	epidermal growth factor like 1	Rattus norvegicus	97-100
11251341-4	2000	TFPI is released from the vascular endothelium after injection of either unfractionated heparin (UFH) or low-molecular-weight heparins (LMWHs), which may then provide high concentrations of TFPI at sites of tissue damage and ongoing thrombosis.	Heparin	97-100	tissue factor pathway inhibitor	Homo sapiens	0-4
11251341-4	2000	TFPI is released from the vascular endothelium after injection of either unfractionated heparin (UFH) or low-molecular-weight heparins (LMWHs), which may then provide high concentrations of TFPI at sites of tissue damage and ongoing thrombosis.	Heparin	97-100	tissue factor pathway inhibitor	Homo sapiens	190-194
1853931-9	1991	These studies suggest that heparin decreases GEC response to EGF by accelerating its uptake and degradation.	Heparin	27-34	epidermal growth factor like 1	Rattus norvegicus	61-64
1892484-9	1991	LPL activities in the post-heparin plasma were decreased significantly from 2.53 +/- 0.71 mumol free fatty acids (FFA)/ml/h to 1.71 +/- 0.71 mumol FFA/ml/h by probucol while HTGL activities remained unchanged.	Heparin	27-34	lipase C, hepatic type	Homo sapiens	174-178
1645764-2	1991	Antibody inhibition and chromatography on heparin-Sepharose showed that most of the activity was due to lipoprotein lipase (LPL), and that there was only a small amount of hepatic lipase activity.	Heparin	42-49	lipoprotein lipase	Cavia porcellus	104-122
1708387-7	1991	Previous studies demonstrated that Lp(a) competes with plasminogen for the active site of fibrinogen- and heparin-bound t-PA.	Heparin	106-113	lipoprotein(a)	Homo sapiens	35-40
11251341-4	2000	TFPI is released from the vascular endothelium after injection of either unfractionated heparin (UFH) or low-molecular-weight heparins (LMWHs), which may then provide high concentrations of TFPI at sites of tissue damage and ongoing thrombosis.	Heparin	126-134	tissue factor pathway inhibitor	Homo sapiens	0-4
11251341-4	2000	TFPI is released from the vascular endothelium after injection of either unfractionated heparin (UFH) or low-molecular-weight heparins (LMWHs), which may then provide high concentrations of TFPI at sites of tissue damage and ongoing thrombosis.	Heparin	126-134	tissue factor pathway inhibitor	Homo sapiens	190-194
11251341-5	2000	In dilute prothrombin-time-based assays, released TFPI contributes approximately one-third to the anticoagulant effect of heparin, the remaining being accounted for by antithrombin.	Heparin	122-129	tissue factor pathway inhibitor	Homo sapiens	50-54
1849357-3	1991	Here we demonstrate the purification of HGF from human placenta with heparin-agarose chromatography and TSK-heparin high-pressure liquid chromatography and describe the distribution of placental HGF by immunohistochemistry using a polyclonal antibody to HGF.	Heparin	69-76	hepatocyte growth factor	Homo sapiens	40-43
11251341-7	2000	UFH and LMWH exert differential effects on intravascular TFPI.	Heparin	0-3	tissue factor pathway inhibitor	Homo sapiens	57-61
11251341-8	2000	UFH, but not LMWH, given in therapeutic doses, is associated with a progressive depletion of TFPI, which is associated with a strong rebound activation of coagulation after cessation of treatment.	Heparin	0-3	tissue factor pathway inhibitor	Homo sapiens	93-97
10958381-11	2000	Only heparin inhibited both MMP-1 and MMP-2/MMP-9 activity.	Heparin	5-12	matrix metallopeptidase 2	Homo sapiens	38-43
1879335-10	1991	Heparin-sepharose affinity chromatography suggests that the biological activities of CAF probably correspond to the presence of acidic and basic fibroblast growth factor (aFGF and bFGF).	Heparin	0-7	fibroblast growth factor 1	Gallus gallus	171-175
1879335-10	1991	Heparin-sepharose affinity chromatography suggests that the biological activities of CAF probably correspond to the presence of acidic and basic fibroblast growth factor (aFGF and bFGF).	Heparin	0-7	fibroblast growth factor 2	Gallus gallus	180-184
10901180-6	2000	Heparin binding EGF was increased early, by day one in injured kidneys and gene expression for the EGF receptor was increased as well.	Heparin	0-7	epidermal growth factor like 1	Rattus norvegicus	16-19
1847668-3	1991	It is demonstrated that free heparin and heparan sulfate can reconstitute a low affinity receptor that is, in turn, required for the high affinity binding of bFGF.	Heparin	29-36	fibroblast growth factor 2	Mus musculus	158-162
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Heparin	101-108	serpin family D member 1	Homo sapiens	0-19
10901180-6	2000	Heparin binding EGF was increased early, by day one in injured kidneys and gene expression for the EGF receptor was increased as well.	Heparin	0-7	epidermal growth factor like 1	Rattus norvegicus	99-102
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Heparin	101-108	serpin family D member 1	Homo sapiens	21-25
10664333-4	2000	We found that changes in the total plasma TFPI antigen level were significantly dependent on the level of free TFPI antigen (r = 0.96, P &lt; 0.0001) which increased significantly after heparin injection (P &lt; 0.0001), and increased further during the bypass period (P &lt; 0.005).	Heparin	186-193	tissue factor pathway inhibitor	Homo sapiens	42-46
1999192-6	1991	This protein (partly purified from the conditioned medium) was shown by crossed immunoelectrophoresis to bind to heparin, CaCl2 and plasminogen kringle 4, as previously described for tetranectin in plasma.	Heparin	113-120	C-type lectin domain family 3 member B	Homo sapiens	183-194
10664333-4	2000	We found that changes in the total plasma TFPI antigen level were significantly dependent on the level of free TFPI antigen (r = 0.96, P &lt; 0.0001) which increased significantly after heparin injection (P &lt; 0.0001), and increased further during the bypass period (P &lt; 0.005).	Heparin	186-193	tissue factor pathway inhibitor	Homo sapiens	111-115
10664333-6	2000	When heparin was neutralized by protamine, the free TFPI antigen level decreased immediately, but remained higher than the preoperative level (P &lt; 0.005).	Heparin	5-12	tissue factor pathway inhibitor	Homo sapiens	52-56
10581158-5	1999	Among the polysaccharides, heparin, chondroitin sulphates A, B, and C, fucoidan, and dextran sulphate, CD69 dimer gives a weak binding signal with fucoidan.	Heparin	27-34	CD69 molecule	Homo sapiens	103-107
1776715-2	1991	The substance concentration of ionized calcium (cCa2+) in blood, plasma or serum preanalytically may be affected by pH changes of the sample, calcium binding by heparin, and dilution by the anticoagulant solution.	Heparin	161-168	crystallin beta B2	Homo sapiens	48-52
1776715-7	1991	Conversion of the measured values to cCa2+ (7.4) is only valid if the pH is in the range 7.2-7.6 Ca2+ binding by heparin can be minimized by using either of the following: a final concentration of sodium or lithium heparinate of 15 IU/ml blood or less, by use of calcium titrated heparin with a final concentration less than 50 IU/ml blood.	Heparin	113-120	crystallin beta B2	Homo sapiens	37-41
1721035-0	1991	Pregnancy-associated plasma protein A interaction with heparin: a critical appraisal.	Heparin	55-62	pappalysin 1	Homo sapiens	0-37
10583216-1	1999	Patients with immune heparin-induced thrombocytopenia (HIT) possess antibodies that bind to a complex of platelet factor 4 (PF4) and heparin.	Heparin	21-28	platelet factor 4	Homo sapiens	124-127
1721035-1	1991	Positive affinity chromatography on heparin-Sepharose has proved a most crucial step in the purification of pregnancy-associated plasma protein A (PAPP-A).	Heparin	36-43	pappalysin 1	Homo sapiens	108-145
1721035-1	1991	Positive affinity chromatography on heparin-Sepharose has proved a most crucial step in the purification of pregnancy-associated plasma protein A (PAPP-A).	Heparin	36-43	pappalysin 1	Homo sapiens	147-153
2049182-1	1991	A heparin-binding protein with neurotrophic activity for perinatal rat neurons, termed HBNF, was purified to homogeneity from bovine brain utilizing pH 4.5 extraction, ammonium sulfate precipitation, cation exchange and heparin-Sepharose affinity chromatographies, and reverse phase HPLC.	Heparin	2-9	pleiotrophin	Rattus norvegicus	87-91
1794748-5	1991	A major pool of EPI is bound to the endothelial surface, and this fraction may be released by heparin.	Heparin	94-101	tissue factor pathway inhibitor	Homo sapiens	16-19
1794751-0	1991	Heparin requires both antithrombin and extrinsic pathway inhibitor for its anticoagulant effect in human blood.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	39-66
2015950-2	1991	A triglyceride (TG) lipase is present in whole homogenate and tissue extracts of beef myocardium with characteristics of lipoprotein lipase (LPL); i.e., activity is stimulated by serum, inhibited by NaCl and protamine sulfate, the protein binds to heparin-Sepharose, and the enzyme has an alkaline pH optimum.	Heparin	248-255	lipoprotein lipase	Bos taurus	121-139
2015950-2	1991	A triglyceride (TG) lipase is present in whole homogenate and tissue extracts of beef myocardium with characteristics of lipoprotein lipase (LPL); i.e., activity is stimulated by serum, inhibited by NaCl and protamine sulfate, the protein binds to heparin-Sepharose, and the enzyme has an alkaline pH optimum.	Heparin	248-255	lipoprotein lipase	Bos taurus	141-144
10583216-7	1999	Binding of PF4 to heparin (optimal) or polystyrene/agarose (suboptimal) promotes recognition of this epitope.	Heparin	18-25	platelet factor 4	Homo sapiens	11-14
1645379-0	1991	Acute dialysis: PMN-elastase as a new parameter for controlling individual anticoagulation with low molecular weight heparin (Fragmin).	Heparin	117-124	elastase, neutrophil expressed	Homo sapiens	16-28
10510057-2	1999	Recently, it has been described that leukocytes adhere on immobilized heparin mediated by the integrin Mac-1 (CD11b/CD18, alphaMbeta2, or CR3).	Heparin	70-77	teratocarcinoma-derived growth factor 1 pseudogene 3	Homo sapiens	122-141
2222404-3	1990	The lipase bound to heparin-agarose and co-eluted with 125I-labelled bovine lipoprotein lipase in a salt gradient.	Heparin	20-27	lipoprotein lipase	Bos taurus	76-94
10496984-0	1999	Matrix localization of tissue factor pathway inhibitor-2/matrix-associated serine protease inhibitor (TFPI-2/MSPI) involves arginine-mediated ionic interactions with heparin and dermatan sulfate: heparin accelerates the activity of TFPI-2/MSPI toward plasmin.	Heparin	196-203	plasminogen	Homo sapiens	251-258
10726033-2	1999	The major one is generated in the presence of platelet factor 4 (PF4) and heparin at a well-defined concentration that allows formation of heparin-PF4 complexes and induces an alteration of the PF4 molecule.	Heparin	74-81	platelet factor 4	Homo sapiens	147-150
10726033-2	1999	The major one is generated in the presence of platelet factor 4 (PF4) and heparin at a well-defined concentration that allows formation of heparin-PF4 complexes and induces an alteration of the PF4 molecule.	Heparin	74-81	platelet factor 4	Homo sapiens	147-150
10500046-2	1999	Soluble human complement receptor type 1 (sCR1) is a potent inhibitor of complement, as are heparin-bonded (HB) cardiopulmonary bypass (CPB) circuits.	Heparin	92-99	complement C3b/C4b receptor 1 (Knops blood group)	Homo sapiens	14-40
2118625-4	1990	The last result also suggests the use of heparin as a specific inhibitor of purified mammalian DNA polymerases alpha and delta, similar to the use of aphidicolin.	Heparin	41-48	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	95-116
2142941-6	1990	After 1 h at 37 degrees C, 28% of the LPL initially bound to the cell surface was no longer releasable by heparin or trypsin treatments, suggesting that LPL was internalized by the cells.	Heparin	106-113	lipoprotein lipase	Bos taurus	38-41
2142941-7	1990	Addition of heparin to the medium or pretreatment of the cells with heparinase markedly reduced the amount of LPL internalized, establishing a requirement for cell surface heparan sulfate proteoglycans in the process.	Heparin	12-19	lipoprotein lipase	Bos taurus	110-113
10478144-6	1999	Because syndecan-1 interacts with heparin-binding growth factors such as FGF-2, accumulation of syndecan-1 within the tumor stroma may contribute to the extensive angiogenesis and stromal proliferation characteristic of infiltrating breast carcinoma.	Heparin	34-41	syndecan 1	Homo sapiens	96-106
2142941-10	1990	The catalytic activity, molecular size, and heparin-binding characteristics of the released LPL was similar to native LPL.	Heparin	44-51	lipoprotein lipase	Bos taurus	92-95
2142941-11	1990	Addition of either heparin, heparinase, or excess unlabeled LPL to prevent the rebinding of released 125I-LPL to the cell surface increased the amount of 125I-LPL present in the medium, suggesting that there is a process of recycling of 125I-LPL bound to the cell surface.	Heparin	19-26	lipoprotein lipase	Bos taurus	106-109
2142941-11	1990	Addition of either heparin, heparinase, or excess unlabeled LPL to prevent the rebinding of released 125I-LPL to the cell surface increased the amount of 125I-LPL present in the medium, suggesting that there is a process of recycling of 125I-LPL bound to the cell surface.	Heparin	19-26	lipoprotein lipase	Bos taurus	106-109
2142941-11	1990	Addition of either heparin, heparinase, or excess unlabeled LPL to prevent the rebinding of released 125I-LPL to the cell surface increased the amount of 125I-LPL present in the medium, suggesting that there is a process of recycling of 125I-LPL bound to the cell surface.	Heparin	19-26	lipoprotein lipase	Bos taurus	106-109
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Heparin	82-89	serpin family D member 1	Homo sapiens	0-19
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Heparin	82-89	serpin family D member 1	Homo sapiens	21-25
2229028-2	1990	The new glycoprotein was termed heparin binding protein-44 (HBP-44), since it was absorbed to a heparin-agarose column and was eluted from it by a buffer containing 1.5 M NaCl.	Heparin	32-39	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	60-66
2229028-9	1990	We propose that HBP-44 is extruded from plasma membranes and interacts with heparin and related molecules and that it is involved in the interactions of plasma membranes with basement membranes.	Heparin	76-83	low density lipoprotein receptor-related protein associated protein 1	Mus musculus	16-22
10494757-5	1999	Intravenous injection of 7500 IU unfractionated heparin induced a significant further increase of TFPI in two patients with high pre-heparin levels.	Heparin	48-55	tissue factor pathway inhibitor	Homo sapiens	98-102
2196322-2	1990	A role for HCII as an inhibitor of thrombin in the presence of dermatan sulfate and heparin has been proposed.	Heparin	84-91	serpin family D member 1	Homo sapiens	11-15
10494757-5	1999	Intravenous injection of 7500 IU unfractionated heparin induced a significant further increase of TFPI in two patients with high pre-heparin levels.	Heparin	133-140	tissue factor pathway inhibitor	Homo sapiens	98-102
10468530-10	1999	Compared with untreated sheep with aortic stenosis, in heparin-treated sheep LV FGF-2 protein increased 2-fold, whereas FGF-2 mRNA remained unchanged.	Heparin	55-62	fibroblast growth factor 2	Ovis aries	80-85
10468530-12	1999	CONCLUSIONS: Heparin administration during LV hypertension increases heparin-binding angiogenic factors FGF-2 and VEGF in the LV and ameliorates decreases in LV perfusion capacity and capillary density.	Heparin	13-20	fibroblast growth factor 2	Ovis aries	104-109
2224097-0	1990	[Heparin-sepharose affinity chromatography and reduction conditions as a method of a selective process for separate isoforms of apolipoprotein A].	Heparin	1-8	lipoprotein(a)	Homo sapiens	128-144
10468530-12	1999	CONCLUSIONS: Heparin administration during LV hypertension increases heparin-binding angiogenic factors FGF-2 and VEGF in the LV and ameliorates decreases in LV perfusion capacity and capillary density.	Heparin	13-20	vascular endothelial growth factor A	Ovis aries	114-118
10419890-2	1999	We show that a peptide between amino acids 47 and 70 that contains the heparin-binding lysine-rich site inhibits FGF-2 or VEGF function.	Heparin	71-78	fibroblast growth factor 2	Cricetulus griseus	113-118
2163607-5	1990	Heparin, a sulphated polysaccharide which binds to Ins(1,4,5)P3 receptors in several tissues, inhibited both the binding of radiolabelled Ins(1,4,5)P3 and its Ca2(+)-releasing activity in adrenal microsomes.	Heparin	0-7	carbonic anhydrase 2	Bos taurus	159-162
2163607-7	1990	Such differential inhibition of the Ins(1,4,5)P3- and Ins(1,3,4,5)P4-induced Ca2+ responses by heparin indicates that Ins(1,3,4,5)P4 stimulates the release of Ca2+ from a discrete intracellular store, and exerts this action via a specific receptor site that is distinct from the Ins(1,4,5)P3 receptor.	Heparin	95-102	carbonic anhydrase 2	Bos taurus	77-80
2163607-7	1990	Such differential inhibition of the Ins(1,4,5)P3- and Ins(1,3,4,5)P4-induced Ca2+ responses by heparin indicates that Ins(1,3,4,5)P4 stimulates the release of Ca2+ from a discrete intracellular store, and exerts this action via a specific receptor site that is distinct from the Ins(1,4,5)P3 receptor.	Heparin	95-102	carbonic anhydrase 2	Bos taurus	159-162
2163608-6	1990	In cells dialysed intracellularly with heparin, a potent antagonist of Ins(1,4,5)P3 action, the rapid response to extracellular stimulation with TRH was abolished, as were the effects of intracellular application of Ins(1,4,5)P3.	Heparin	39-46	thyrotropin releasing hormone	Rattus norvegicus	145-148
2163608-7	1990	Heparin, which abolished Ins(1,4,5)P3 action completely, blocked responses to TRH in some cells only partially, revealing that Ca2+ mobilization response to TRH is in part slower in onset than the response to Ins(1,4,5)P3.	Heparin	0-7	thyrotropin releasing hormone	Rattus norvegicus	78-81
2163608-7	1990	Heparin, which abolished Ins(1,4,5)P3 action completely, blocked responses to TRH in some cells only partially, revealing that Ca2+ mobilization response to TRH is in part slower in onset than the response to Ins(1,4,5)P3.	Heparin	0-7	thyrotropin releasing hormone	Rattus norvegicus	157-160
2324746-5	1990	Chicken globular AChE forms (G-forms, both low-salt-soluble and detergent-soluble) also bound to immobilized heparin in the absence of salt.	Heparin	109-116	acetylcholinesterase (Cartwright blood group)	Gallus gallus	17-21
2324746-8	1990	We conclude that the molecular forms of AChE in these vertebrate species interact with heparin, at salt concentrations that are characteristic for asymmetric and globular forms.	Heparin	87-94	acetylcholinesterase (Cartwright blood group)	Gallus gallus	40-44
10419890-5	1999	Peptide 17-58, which is located in the central part of the molecule, although it does not inhibit FGF-2 or VEGF binding or biologic activity in endothelial cells, inhibited heparin-dependent binding of (125)I-FGF-2 or (125)I-VEGF to CHOmFGFR1 or CHOmVEGFR2 cells, respectively.	Heparin	173-180	fibroblast growth factor 2	Cricetulus griseus	209-214
2194316-2	1990	Based on experiments using ECGF (4-20 micrograms/ml) with heparin (90 micrograms/ml), we obtained the following results: 1) In confluent HUVEC cultures, ECGF had essentially no influence on the levels of inducible TF.	Heparin	58-65	thymidine phosphorylase	Homo sapiens	153-157
2317527-8	1990	Release of LPL from heparin-agarose followed a similar pattern, suggesting that the fatty acids specifically affected LPL-heparin interaction.	Heparin	20-27	lipoprotein lipase	Bos taurus	11-14
10511296-1	1999	Hepatic lipase (HL) is one of two major lipases released from the vascular bed by intravenous injection of heparin.	Heparin	107-114	lipase C, hepatic type	Homo sapiens	0-14
2317527-8	1990	Release of LPL from heparin-agarose followed a similar pattern, suggesting that the fatty acids specifically affected LPL-heparin interaction.	Heparin	122-129	lipoprotein lipase	Bos taurus	11-14
2317527-8	1990	Release of LPL from heparin-agarose followed a similar pattern, suggesting that the fatty acids specifically affected LPL-heparin interaction.	Heparin	122-129	lipoprotein lipase	Bos taurus	118-121
10397725-8	1999	On Western blot analysis, a protein consistent with full-length TFPI (42 kD) was identified in the conditioned media of PASMC, and the levels of the protein were much higher in the conditioned media of serum and bFGF/heparin-treated cells.	Heparin	217-224	tissue factor pathway inhibitor	Homo sapiens	64-68
2300584-8	1990	Model studies with bovine LPL showed that fatty acids displace the enzyme from heparin-agarose.	Heparin	79-86	lipoprotein lipase	Bos taurus	26-29
10381515-6	1999	After 14 days in culture with antigen (heparin:PF4 complexes), but not after culture with PF4, heparin, or medium alone, patient cells, but not cells from normal subjects, preferentially expressed T-cell receptor (TCR)-containing beta chains of the BV 5.1 family.	Heparin	39-46	platelet factor 4	Homo sapiens	47-50
10332802-6	1999	In contrast, intracellular infusion of either GDP beta S or the IP3 receptor antagonist heparin prevented oxo-M mediated enhancement of NMDA depolarizations.	Heparin	88-95	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	64-76
2139798-3	1990	The immobilization condition rendering maximum co-immobilized heparin and plasmin activity was identified to require heparin immobilization followed by plasmin immobilization.	Heparin	62-69	plasminogen	Homo sapiens	152-159
2139798-3	1990	The immobilization condition rendering maximum co-immobilized heparin and plasmin activity was identified to require heparin immobilization followed by plasmin immobilization.	Heparin	117-124	plasminogen	Homo sapiens	74-81
2139798-4	1990	Soluble heparin exerts a positive synergistic effect on soluble plasmin.	Heparin	8-15	plasminogen	Homo sapiens	64-71
2139798-5	1990	Immobilized heparin enhances plasmin loading on the CET as compared to the heparin-free graft.	Heparin	12-19	plasminogen	Homo sapiens	29-36
10340997-4	1999	A time-course analysis of PCI-uPA complex formation showed that &gt;80% of the complex had been formed within 15 min in normal seminal plasma in the presence of heparin, compared with the total complex formed after 150 min incubation, whereas no response to heparin stimulation was observed in the assays with the two patient samples.	Heparin	161-168	serpin family A member 5	Homo sapiens	26-29
2139798-6	1990	Heparin, in both the soluble or immobilized state, significantly decreases the Michaelis-Menten (M-M) parameter Km for immobilized plasmin over heparin-free immobilized plasmin.	Heparin	0-7	plasminogen	Homo sapiens	131-138
10340997-5	1999	Similarly, &gt;90% of PCI-tPA complex was formed after 30 min of heparin stimulation in normal seminal plasma but no response was observed in the two patient samples.	Heparin	65-72	serpin family A member 5	Homo sapiens	22-25
2139798-6	1990	Heparin, in both the soluble or immobilized state, significantly decreases the Michaelis-Menten (M-M) parameter Km for immobilized plasmin over heparin-free immobilized plasmin.	Heparin	0-7	plasminogen	Homo sapiens	169-176
2139798-6	1990	Heparin, in both the soluble or immobilized state, significantly decreases the Michaelis-Menten (M-M) parameter Km for immobilized plasmin over heparin-free immobilized plasmin.	Heparin	144-151	plasminogen	Homo sapiens	131-138
10330384-0	1999	Antibodies to platelet factor 4-heparin after cardiopulmonary bypass in patients anticoagulated with unfractionated heparin or a low-molecular-weight heparin : clinical implications for heparin-induced thrombocytopenia.	Heparin	32-39	platelet factor 4	Homo sapiens	14-31
2139798-7	1990	Furthermore, the M-M parameter Vmax for the immobilized plasmin in the presence of heparin decreases over heparin-free immobilized plasmin.	Heparin	83-90	plasminogen	Homo sapiens	56-63
2139798-7	1990	Furthermore, the M-M parameter Vmax for the immobilized plasmin in the presence of heparin decreases over heparin-free immobilized plasmin.	Heparin	106-113	plasminogen	Homo sapiens	56-63
2139798-7	1990	Furthermore, the M-M parameter Vmax for the immobilized plasmin in the presence of heparin decreases over heparin-free immobilized plasmin.	Heparin	106-113	plasminogen	Homo sapiens	131-138
2139798-8	1990	These results suggest a decrease in the kinetic constant k3 for heparin-modified immobilized plasmin over the heparin-free form.	Heparin	64-71	plasminogen	Homo sapiens	93-100
2139798-8	1990	These results suggest a decrease in the kinetic constant k3 for heparin-modified immobilized plasmin over the heparin-free form.	Heparin	110-117	plasminogen	Homo sapiens	93-100
2085440-1	1990	bFGF was extracted from either mouse, rat and human cell lines or mouse, rat bovine and human brain tissue and partially purified by cation exchange chromatography and heparin-affinity chromatography.	Heparin	168-175	fibroblast growth factor 2	Mus musculus	0-4
2193204-4	1990	The growth-stimulating factor in the mouse serum, like hHGF, had affinity for heparin and was heat-labile.	Heparin	78-85	hepatocyte growth factor	Homo sapiens	55-59
10330384-0	1999	Antibodies to platelet factor 4-heparin after cardiopulmonary bypass in patients anticoagulated with unfractionated heparin or a low-molecular-weight heparin : clinical implications for heparin-induced thrombocytopenia.	Heparin	116-123	platelet factor 4	Homo sapiens	14-31
10330384-0	1999	Antibodies to platelet factor 4-heparin after cardiopulmonary bypass in patients anticoagulated with unfractionated heparin or a low-molecular-weight heparin : clinical implications for heparin-induced thrombocytopenia.	Heparin	116-123	platelet factor 4	Homo sapiens	14-31
10330384-0	1999	Antibodies to platelet factor 4-heparin after cardiopulmonary bypass in patients anticoagulated with unfractionated heparin or a low-molecular-weight heparin : clinical implications for heparin-induced thrombocytopenia.	Heparin	116-123	platelet factor 4	Homo sapiens	14-31
10330384-1	1999	BACKGROUND: Cardiopulmonary bypass (CPB) induces platelet activation with release of platelet factor 4 (PF4), and patients are exposed to high doses of heparin (H).	Heparin	152-159	platelet factor 4	Homo sapiens	85-102
10330384-1	1999	BACKGROUND: Cardiopulmonary bypass (CPB) induces platelet activation with release of platelet factor 4 (PF4), and patients are exposed to high doses of heparin (H).	Heparin	152-159	platelet factor 4	Homo sapiens	104-107
24102149-0	2013	Alternative diagnosis to heparin-induced thrombocytopenia in two critically ill patients despite a positive PF4/heparin-antibody test.	Heparin	25-32	platelet factor 4	Homo sapiens	108-111
10336236-3	1999	Blood samples were drawn before and 5 minutes after an intravenous injection of unfractionated heparin 5000 IE, which is known to cause TFPI release in healthy individuals.	Heparin	95-102	tissue factor pathway inhibitor	Homo sapiens	136-140
10336236-6	1999	The TFPI levels showed a considerable rise in both patients and controls after heparin injection.	Heparin	79-86	tissue factor pathway inhibitor	Homo sapiens	4-8
10336236-11	1999	In conclusion, we have found that patients with APA have higher TFPI amidolytic activity/antigen level both before and after heparin stimulation of TFPI release.	Heparin	125-132	tissue factor pathway inhibitor	Homo sapiens	148-152
34971707-2	2022	Exostosin glycosyltransferase 1 (EXT1), an enzyme involved in the biosynthesis of heparin sulfate, has also been reported to be a host factor essential for a wide variety of pathogens.	Heparin	82-89	exostosin glycosyltransferase 1	Homo sapiens	0-31
10427858-5	1999	Endowed with the full anticoagulant activity of heparin but devoid of undesired non-specific interactions, particularly with platelet factor 4 (PF4), they might represent "the ideal heparin-like antithrombotic".	Heparin	182-189	platelet factor 4	Homo sapiens	144-147
34971707-2	2022	Exostosin glycosyltransferase 1 (EXT1), an enzyme involved in the biosynthesis of heparin sulfate, has also been reported to be a host factor essential for a wide variety of pathogens.	Heparin	82-89	exostosin glycosyltransferase 1	Sus scrofa	33-37
33754901-3	2021	Here, heparin-coupled polyvinyl alcohol (PVA-H) microspheres have been developed as an adsorbent for selectively remove tumour-induced immunosuppressive cytokines, such as vascular endothelial growth factor (VEGF) and transforming growth factor-beta (TGF-beta), but not tumour necrosis factor-alpha (TNF-alpha) which has an immune-stimulating effect and can inhibit tumour growth.	Heparin	6-13	transforming growth factor alpha	Homo sapiens	251-259
10408373-7	1999	Protein modeling together with site directed mutagenesis indicate that R39, R64 and R66 from the C4BP alpha-chain form a key binding site for heparin, suggesting that this region could be of major importance for interaction with C4b.	Heparin	142-149	complement C4B (Chido blood group)	Homo sapiens	229-232
34275201-7	2021	A laboratory testing model that utilized an in-house platelet factor 4 (PF4)-heparin enzyme-linked immunosorbent assay (ELISA) completed three days weekly, and reflex serotonin release assay (SRA) with a five-day turnaround resulted in the shortest mean time to HIT testing finalization, lowest percentage of patients discharged prior to HIT testing finalization, and lowest total alternative anticoagulant days.	Heparin	77-84	platelet factor 4	Homo sapiens	72-75
34275201-9	2021	Testing models utilizing a PF4-heparin antibody ELISA with a reflex SRA for positive results may improve testing metrics and lead to lower utilization of alternative anticoagulants.	Heparin	31-38	platelet factor 4	Homo sapiens	27-30
10212269-8	1999	FGF-10 requires 1.4 times higher NaCl for elution from immobilized heparin than does FGF-7 and binds to four times the number of sites on the pericellular matrix of epithelial cells.	Heparin	67-74	fibroblast growth factor 10	Rattus norvegicus	0-6
10207021-6	1999	The interaction of biotin-laminin-1 with alphaDG was inhibited by soluble alphaDG contained in the conditioned medium from DG cDNA-transfected BAE cells and by a series of glycosaminoglycans (heparin, dextran sulfate, and fucoidan).	Heparin	192-199	dystroglycan 1	Bos taurus	46-48
34795305-3	2021	We have previously engineered growth factors to bind to exposed extracellular matrix (ECM) in the wound environment using the heparin-binding domain of placental growth factor-2 (PlGF-2123-144), which binds promiscuously to ECM proteins.	Heparin	126-133	placental growth factor	Mus musculus	179-183
10209287-2	1999	Previous investigations indicated that the binding sites on HCII for heparin and dermatan sulphate overlap but are not identical.	Heparin	69-76	serpin family D member 1	Homo sapiens	60-64
34699015-5	2022	Here we demonstrated that Furin is a novel heparin/heparan sulfate binding protein by the use of biochemical and genetic assays.	Heparin	43-50	furin, paired basic amino acid cleaving enzyme	Homo sapiens	26-31
34699015-8	2022	Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate.	Heparin	27-34	furin, paired basic amino acid cleaving enzyme	Homo sapiens	70-75
34699015-8	2022	Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate.	Heparin	27-34	furin, paired basic amino acid cleaving enzyme	Homo sapiens	111-116
10195936-0	1999	Effect of cardiopulmonary bypass and heparin on plasma levels of Lp(a) and Apo(a) fragments.	Heparin	37-44	lipoprotein(a)	Homo sapiens	65-70
34699015-8	2022	Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate.	Heparin	27-34	furin, paired basic amino acid cleaving enzyme	Homo sapiens	120-125
34699015-8	2022	Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate.	Heparin	91-98	furin, paired basic amino acid cleaving enzyme	Homo sapiens	70-75
34699015-8	2022	Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate.	Heparin	91-98	furin, paired basic amino acid cleaving enzyme	Homo sapiens	111-116
34699015-8	2022	Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate.	Heparin	91-98	furin, paired basic amino acid cleaving enzyme	Homo sapiens	120-125
34768908-5	2021	Here in this paper, we report a novel heparin and arginine-based plasmin nanoformulation that exhibits increased plasmin stability and efficacy.	Heparin	38-45	plasminogen	Homo sapiens	65-72
34768908-5	2021	Here in this paper, we report a novel heparin and arginine-based plasmin nanoformulation that exhibits increased plasmin stability and efficacy.	Heparin	38-45	plasminogen	Homo sapiens	113-120
10075664-1	1999	Heparin affin regulatory peptide (HARP) is a polypeptide belonging to a family of heparin binding growth/differentiation factors.	Heparin	82-89	pleiotrophin	Mus musculus	0-32
34406867-6	2021	This last mutation affects S protein processing, transforms the unprocessed furin cleavage site into the heparin-binding peptide and makes viruses less capable of syncytia formation.	Heparin	105-112	furin, paired basic amino acid cleaving enzyme	Homo sapiens	76-81
10075664-1	1999	Heparin affin regulatory peptide (HARP) is a polypeptide belonging to a family of heparin binding growth/differentiation factors.	Heparin	82-89	pleiotrophin	Mus musculus	34-38
10075664-2	1999	The high affinity of HARP for heparin suggests that this secreted polypeptide should also bind to heparan sulfate proteoglycans derived from cell surface and extracellular matrix defined as extracellular compartments.	Heparin	30-37	pleiotrophin	Mus musculus	21-25
34537241-6	2021	The dissociation constant (KD) values obtained by surface plasmon resonance (SPR) of the wild type SARS-CoV-2 spike (S)-protein receptor binding domain (RBD) and N501Y mutant RBD in interactions with the heparin-immobilized sensor chip were 94 and 1.8 x 103 nM, respectively.	Heparin	204-211	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	110-115
10075664-4	1999	Heparitinase treatment of BEL cells inhibited HARP-induced cell proliferation, and the biological activity of HARP in this system was restored by the addition of heparin.	Heparin	162-169	pleiotrophin	Mus musculus	110-114
34404617-4	2021	Heparin inhibits the CXCR4/SDF1 axis, as does plerixafor.	Heparin	0-7	C-X-C motif chemokine ligand 12	Homo sapiens	27-31
10075664-6	1999	Binding analyses with a biosensor showed that HARP bound heparin with fast association and dissociation kinetics (kass = 1.6 x 10(6) M-1 s-1; kdiss = 0.02 s-1), yielding a Kd value of 13 nM; the interaction between HARP and dermatan sulfate was characterized by slower association kinetics (kass = 0.68 x 10(6) M-1 s-1) and a lower affinity (Kd = 51 nM).	Heparin	57-64	pleiotrophin	Mus musculus	46-50
10075664-6	1999	Binding analyses with a biosensor showed that HARP bound heparin with fast association and dissociation kinetics (kass = 1.6 x 10(6) M-1 s-1; kdiss = 0.02 s-1), yielding a Kd value of 13 nM; the interaction between HARP and dermatan sulfate was characterized by slower association kinetics (kass = 0.68 x 10(6) M-1 s-1) and a lower affinity (Kd = 51 nM).	Heparin	57-64	pleiotrophin	Mus musculus	215-219
34660719-4	2021	At physiological antithrombin levels, heparin treatment resulted in complete and sustained inhibition of thrombin-induced PAR4-mediated platelet activation, but transient PAR1 signaling was sufficient to elicit significant alpha-granule release and platelet aggregation.	Heparin	38-45	Prader Willi/Angelman region RNA 4	Homo sapiens	122-126
10075664-7	1999	Exogenous heparin, heparan sulfate, and dermatan sulfate potentiated the growth-stimulatory activity of HARP, suggesting that corresponding proteoglycans could be involved in the regulation of the mitogenic activity of HARP.	Heparin	10-17	pleiotrophin	Mus musculus	104-108
34660719-7	2021	Our results show that heparin and bivalirudin have different and complementary inhibitory effects on the activation of PAR1 and PAR4 by thrombin.	Heparin	22-29	Prader Willi/Angelman region RNA 4	Homo sapiens	128-132
10075664-7	1999	Exogenous heparin, heparan sulfate, and dermatan sulfate potentiated the growth-stimulatory activity of HARP, suggesting that corresponding proteoglycans could be involved in the regulation of the mitogenic activity of HARP.	Heparin	10-17	pleiotrophin	Mus musculus	219-223
34153666-0	2021	The ERK/CREB/PTN/syndecan-3 pathway involves in heparin-mediated neuro-protection and neuro-regeneration against cerebral ischemia-reperfusion injury following cardiac arrest.	Heparin	48-55	pleiotrophin	Rattus norvegicus	13-16
34153666-1	2021	BACKGROUND: Heparin, a commonly used anticoagulant, has been found to improve cerebral ischemia-reperfusion injury (CIR-CA) following cardiopulmonary resuscitation (CPR).	Heparin	12-19	corepressor interacting with RBPJ, 1	Rattus norvegicus	116-119
10103013-10	1999	Potential modulators of angiogenesis such as protamine, heparin and the placental ribonuclease inhibitor competed for angiogenin binding to the cells.	Heparin	56-63	angiogenin	Homo sapiens	118-128
34153666-2	2021	Here, we aimed to explore the role of pleiotrophin (PTN)/syndecan-3 pathway in heparin therapy for CIR-CA.	Heparin	79-86	pleiotrophin	Rattus norvegicus	38-50
34153666-2	2021	Here, we aimed to explore the role of pleiotrophin (PTN)/syndecan-3 pathway in heparin therapy for CIR-CA.	Heparin	79-86	pleiotrophin	Rattus norvegicus	52-55
34153666-9	2021	In terms of the mechanism, heparin upregulated the expression of ERK, CREB, NF200, BDNF, NGF, PTN and syndecan-3 in the rat brains.	Heparin	27-34	nerve growth factor	Rattus norvegicus	89-92
34153666-9	2021	In terms of the mechanism, heparin upregulated the expression of ERK, CREB, NF200, BDNF, NGF, PTN and syndecan-3 in the rat brains.	Heparin	27-34	pleiotrophin	Rattus norvegicus	94-97
10024677-4	1999	Addition of exogenous TGF-alpha, EGF, AR, or HB-EGF with heparin accelerated cell proliferation.	Heparin	57-64	transforming growth factor alpha	Homo sapiens	22-31
34107198-6	2021	Variable patterns of serum-induced platelet activation were observed in response to heparin and platelet factor 4 (PF4), indicating the heterogeneity of the manifestations of VITT in serum.	Heparin	84-91	platelet factor 4	Homo sapiens	115-118
9974412-7	1999	The TFPI in HMDM supernatants possessed heparin-binding affinity, suggesting potential interaction of TFPI with heparan sulfate proteoglycans.	Heparin	40-47	tissue factor pathway inhibitor	Homo sapiens	102-106
10030389-2	1999	Here we demonstrate that endotoxin (LPS) induces a 56% decrease in hepatic lipase activity in liver and a 45% decrease in hepatic lipase activity in post heparin plasma in Syrian hamsters.	Heparin	154-161	lipase C, hepatic type	Homo sapiens	122-136
34484238-7	2021	The pre-existence of natural antibodies binding PF4/heparin complexes may amplify platelet activation and thrombotic events.	Heparin	52-59	platelet factor 4	Homo sapiens	48-51
34368658-6	2021	Notably, endogenous production by hMSCs within Heparin scaffolds most significantly inhibits osteoclastogenesis via secreted osteoprotegerin (OPG), while the secretome generated by CS6 scaffolds reduced pro-inflammatory immune response and increased endothelial tube formation.	Heparin	47-54	TNF receptor superfamily member 11b	Homo sapiens	125-140
34368658-6	2021	Notably, endogenous production by hMSCs within Heparin scaffolds most significantly inhibits osteoclastogenesis via secreted osteoprotegerin (OPG), while the secretome generated by CS6 scaffolds reduced pro-inflammatory immune response and increased endothelial tube formation.	Heparin	47-54	TNF receptor superfamily member 11b	Homo sapiens	142-145
10398089-9	1999	These results suggest that syndecan-1 participates in cell adhesion mainly at the foveolar epithelium and plays a role in the healing of gastric ulcers by interacting with heparin-binding growth factors.	Heparin	172-179	syndecan 1	Homo sapiens	27-37
34144250-1	2021	Heparin-induced thrombocytopenia (HIT) is characterized clinically by thrombocytopenia, hypercoagulability, and increased thrombosis risk, and serologically by platelet-activating anti-platelet factor 4 (PF4)/heparin antibodies.	Heparin	0-7	platelet factor 4	Homo sapiens	204-207
34144250-10	2021	The emerging concept is that classic HIT reflects platelet-activating anti-PF4/heparin antibodies whereas spontaneous HIT syndrome and other atypical "autoimmune HIT" presentations (delayed-onset HIT, persisting HIT, heparin "flush" HIT) reflect heparin-independent platelet-activating anti-PF4 antibodies-although the precise relationships between PF4 epitope targets and the clinical syndromes remain to be determined.	Heparin	246-253	platelet factor 4	Homo sapiens	291-294
34271850-0	2021	2-O, 3-O desulfated heparin (ODSH) increases bacterial clearance and attenuates lung injury in cystic fibrosis by restoring HMGB1-compromised macrophage function.	Heparin	20-27	high mobility group box 1	Mus musculus	124-129
34271850-3	2021	A heparin derivative, 2-O, 3-O desulfated heparin (ODSH), has been shown to inhibit HMGB1 release from a macrophage cell line and is efficacious in increasing bacterial clearance in a mouse model of pneumonia.	Heparin	2-9	high mobility group box 1	Mus musculus	84-89
34271850-3	2021	A heparin derivative, 2-O, 3-O desulfated heparin (ODSH), has been shown to inhibit HMGB1 release from a macrophage cell line and is efficacious in increasing bacterial clearance in a mouse model of pneumonia.	Heparin	42-49	high mobility group box 1	Mus musculus	84-89
34210960-6	2021	The binding of heparin as well as a second HGF to the 2:1 c-MET:HGF complex further stabilize this active conformation.	Heparin	15-22	hepatocyte growth factor	Homo sapiens	64-67
11938732-3	1999	The results were that TFPI and ACT were significantly increased after heparin injection and during CPB.	Heparin	70-77	tissue factor pathway inhibitor	Homo sapiens	22-26
34235261-4	2021	Surface plasmon resonance showed the SARS-CoV-2 spike protein binds with a much higher affinity to heparin (K D = 55 nM) compared to the RBD (K D = 1 muM) alone.	Heparin	99-106	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	48-53
34447906-7	2021	Some amelioration of the damaged cells and tissues in RA may be achieved by the use of highly anionic heparins, which can neutralize cationic histone activity, provided that these polyanions are co-administrated with anti-inflammatory drugs such as steroids, colchicine, or methotrexate, low molecular weight antioxidants, proteinase inhibitors, and phospholipase A2 inhibitors.	Heparin	102-110	endogenous retrovirus group K member 18	Homo sapiens	323-333
34277977-0	2021	Heparin impairs skeletal muscle glucose uptake by inhibiting insulin binding to insulin receptor.	Heparin	0-7	insulin receptor	Mus musculus	80-96
11938732-4	1999	The changes of TFPI and ACT were similar and pathophysiological; it was evident that heparin stimulated TFPI release and ACT prolonged during cardiac operation with CPB.	Heparin	85-92	tissue factor pathway inhibitor	Homo sapiens	15-19
11938732-4	1999	The changes of TFPI and ACT were similar and pathophysiological; it was evident that heparin stimulated TFPI release and ACT prolonged during cardiac operation with CPB.	Heparin	85-92	tissue factor pathway inhibitor	Homo sapiens	104-108
9867821-11	1999	These results establish that adhesion to the Hep III domain involves the cooperation of activated alpha4 beta1 and CSPG and show that HBP/III5 is a novel heparin and CSPG-binding site contributing to cell adhesion to this domain.	Heparin	154-161	heme binding protein 1	Homo sapiens	134-142
35225150-2	2022	Anti-PF4/polyanion antibodies are related to heparin-induced thrombocytopenia (HIT) and thrombus formation, but data on these antibodies in unselected COVID-19 populations are scarce.	Heparin	45-52	platelet factor 4	Homo sapiens	5-8
10397905-2	1999	Like heparin and heparan sulfates, RGTA potentiate in vitro the biological activities of heparin-binding growth factors (HBGFs), such as fibroblast growth factor (FGF), by stabilizing them against denaturations and by enhancing their binding with cellular receptors.	Heparin	89-96	fibroblast growth factor 2	Mus musculus	163-166
9927147-4	1999	Bile hepatocyte growth factor was purified on a heparin-Sepharose column and subjected to Western blotting.	Heparin	48-55	hepatocyte growth factor	Homo sapiens	5-29
35524641-3	2022	Herein, an injectable protein hydrogel with anti-thrombosis and anti-inflammation competency is developed to impede this cycle, cross-linked by silver ion mediated metal-ligand coordination and electronic interaction with sulfhydryl functionalized bovine serum albumin and heparin, respectively.	Heparin	273-280	albumin	Mus musculus	255-268
10349131-6	1999	In our laboratory, we measured HCII plasmatic levels in the normal Buenos Aires city population and in patients under different clinical conditions, such as sepsis, diabetis, burns, oral anticoagulation and in patients treated with heparin, hyperhomcysteinemia in whom septic and diabetic patients showed decreased values.	Heparin	232-239	serpin family D member 1	Homo sapiens	31-35
35486845-3	2022	This complication is characterized by low platelet counts, and in the case of VITT also by platelet-activating platelet factor 4 (PF4) antibodies reminiscent of heparin-induced thrombocytopenia leading to a prothrombotic state with clot formation at unusual anatomic sites.	Heparin	161-168	platelet factor 4	Homo sapiens	130-133
10094397-9	1999	Calreticulin and grp94/endoplasmin could be partially resolved from CK2 by chromatography on heparin-agarose and almost completely on ConA-Sepharose.	Heparin	93-100	calreticulin	Rattus norvegicus	0-12
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	82-89	natriuretic peptide B	Homo sapiens	162-165
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	170-177	natriuretic peptide B	Homo sapiens	75-78
35444491-0	2022	Upregulated serum granulysin levels in women with antiphospholipid antibody-associated recurrent miscarriage are downregulated by heparin treatment.	Heparin	130-137	granulysin	Homo sapiens	18-28
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	170-177	natriuretic peptide B	Homo sapiens	162-165
35444491-2	2022	The authors aimed to evaluate whether granulysin is associated with the antiphospholipid antibody syndrome and whether heparin changes the granulysin levels.	Heparin	119-126	granulysin	Homo sapiens	139-149
35444491-4	2022	The authors examined granulysin levels under RPL and evaluated the changes in serum granulysin levels before and 1 week after the commencement of heparin treatment.	Heparin	146-153	granulysin	Homo sapiens	84-94
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	170-177	natriuretic peptide B	Homo sapiens	162-165
35444491-5	2022	Results: Serum granulysin levels before heparin treatment were significantly higher in women who tested positive for one or more types of antiphospholipid antibodies (2.75 +- 1.03 vs. 2.44 +- 0.69, p = 0.0341 by Welch"s t test), particularly anti-phosphatidylethanolamine antibodies (IgG: 2.98 +- 1.09 vs. 2.51 +- 0.86, p = 0.0013; IgM: 2.85 +- 1.09 vs. 2.47 +- 0.77, p = 0.0024 by Welch"s t test).	Heparin	40-47	granulysin	Homo sapiens	15-25
35444491-6	2022	After heparin treatment for 1 week, serum granulysin levels were significantly reduced (p = 0.0017 by the paired t test).	Heparin	6-13	granulysin	Homo sapiens	42-52
35444491-8	2022	Conclusion: The results suggest that heparin may reduce the incidence of miscarriage by suppressing serum granulysin levels.	Heparin	37-44	granulysin	Homo sapiens	106-116
35220018-6	2022	Heparin-bile acid based conjugates, as ECM-mimicking component, were synthesized to selectively target the TEC marker doppel and doppel/VEGFR2 axis.	Heparin	0-7	prion like protein doppel	Homo sapiens	118-124
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	170-177	natriuretic peptide B	Homo sapiens	75-78
35220018-6	2022	Heparin-bile acid based conjugates, as ECM-mimicking component, were synthesized to selectively target the TEC marker doppel and doppel/VEGFR2 axis.	Heparin	0-7	prion like protein doppel	Homo sapiens	129-135
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	170-177	natriuretic peptide B	Homo sapiens	162-165
9790687-6	1998	These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin.	Heparin	170-177	natriuretic peptide B	Homo sapiens	162-165
9790687-8	1998	Heparin contains few nonpolar functional groups, and a positive change in heat capacity (DeltaCp = 1 kcal/mol) demonstrates the loss of polar residues on BNP-heparin binding.	Heparin	158-165	natriuretic peptide B	Homo sapiens	154-157
9776412-2	1998	In this study, we measured serum levels of pleiotrophin, a secreted heparin-binding growth and angiogenesis factor, in mice bearing human tumor xenografts to determine whether these levels reflected overall tumor burden, and we examined the relationship between tumor expression of pleiotrophin and serum levels of this factor in patients with cancer.	Heparin	68-75	pleiotrophin	Mus musculus	43-55
35125202-1	2022	Platelet factor 4 (PF4), a protein stored in the alpha-granules of platelets and released upon activation, forms cationic tetramers that bind with various polymeric anions, including heparin.	Heparin	183-190	platelet factor 4	Homo sapiens	0-17
35125202-1	2022	Platelet factor 4 (PF4), a protein stored in the alpha-granules of platelets and released upon activation, forms cationic tetramers that bind with various polymeric anions, including heparin.	Heparin	183-190	platelet factor 4	Homo sapiens	19-22
35125202-2	2022	Some individuals develop antibodies against PF4 in complex with heparin (PF4/H), which potentially lead to the onset of heparin induced thrombocytopenia (HIT).	Heparin	64-71	platelet factor 4	Homo sapiens	44-47
35125202-2	2022	Some individuals develop antibodies against PF4 in complex with heparin (PF4/H), which potentially lead to the onset of heparin induced thrombocytopenia (HIT).	Heparin	64-71	platelet factor 4	Homo sapiens	73-76
35125202-2	2022	Some individuals develop antibodies against PF4 in complex with heparin (PF4/H), which potentially lead to the onset of heparin induced thrombocytopenia (HIT).	Heparin	120-127	platelet factor 4	Homo sapiens	44-47
35125202-2	2022	Some individuals develop antibodies against PF4 in complex with heparin (PF4/H), which potentially lead to the onset of heparin induced thrombocytopenia (HIT).	Heparin	120-127	platelet factor 4	Homo sapiens	73-76
9798992-2	1998	Tissue factor pathway inhibitor (TFPI), which regulates the tissue factor-dependent pathway of blood coagulation, is released from the endothelium by heparin, a mechanism contributing to its antithrombotic activity.	Heparin	150-157	tissue factor pathway inhibitor	Homo sapiens	33-37
35113987-2	2022	In this observational study, we followed VITT patients for changes in their reactivity of platelet-activating anti-platelet factor 4 (PF4) IgG antibodies by an anti-PF4/heparin IgG enzyme immunoassay (EIA) and a functional test for PF4-dependent, platelet-activating antibodies, and new thrombotic complications.	Heparin	169-176	platelet factor 4	Homo sapiens	134-137
35113987-2	2022	In this observational study, we followed VITT patients for changes in their reactivity of platelet-activating anti-platelet factor 4 (PF4) IgG antibodies by an anti-PF4/heparin IgG enzyme immunoassay (EIA) and a functional test for PF4-dependent, platelet-activating antibodies, and new thrombotic complications.	Heparin	169-176	platelet factor 4	Homo sapiens	232-235
9798992-3	1998	In this study, we demonstrated that fucoidan, as heparin, induces TFPI release from cultured human umbilical vein endothelial cells (HUVEC).	Heparin	49-56	tissue factor pathway inhibitor	Homo sapiens	66-70
9727035-8	1998	Most interestingly, the alpha-dystroglycan binding activity of residual laminins expressed in merosin-deficient dy/dy skeletal muscle was inhibited dramatically (69 +/- 19%) by heparin.	Heparin	177-184	laminin, alpha 2	Mus musculus	94-101
35449682-6	2022	A positive PF4 heparin enzyme-linked immunosorbent assay confirmed the VITT diagnosis, and the patient was started on intravenous immunoglobulin.	Heparin	15-22	platelet factor 4	Homo sapiens	11-14
10420071-0	1998	Efficacy of unfractionated heparin, low molecular weight heparin and both combined for releasing total and free tissue factor pathway inhibitor.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	112-143
10420071-0	1998	Efficacy of unfractionated heparin, low molecular weight heparin and both combined for releasing total and free tissue factor pathway inhibitor.	Heparin	57-64	tissue factor pathway inhibitor	Homo sapiens	112-143
35377938-1	2022	Heparin-induced thrombocytopenia (HIT) is an unpredictable, potentially catastrophic adverse effect resulting from an immune response to platelet factor 4 (PF4)/heparin complexes.	Heparin	0-7	platelet factor 4	Homo sapiens	156-159
35377938-1	2022	Heparin-induced thrombocytopenia (HIT) is an unpredictable, potentially catastrophic adverse effect resulting from an immune response to platelet factor 4 (PF4)/heparin complexes.	Heparin	161-168	platelet factor 4	Homo sapiens	156-159
10420071-2	1998	Apart from this main action release of tissue factor pathway inhibitor (TFPI) from endothelial cells could also be important for the antithrombotic activity of heparins.	Heparin	160-168	tissue factor pathway inhibitor	Homo sapiens	39-70
35377938-4	2022	We observed a strong association for positive functional assay with increasing PF4/heparin IgG level (odds ratio (OR) 16.53(95% confidence interval 13.83-19.74), p=1.51x10-209) and female sex (OR 1.15(1.01-1.32), p=0.034).	Heparin	83-90	platelet factor 4	Homo sapiens	79-82
10420071-2	1998	Apart from this main action release of tissue factor pathway inhibitor (TFPI) from endothelial cells could also be important for the antithrombotic activity of heparins.	Heparin	160-168	tissue factor pathway inhibitor	Homo sapiens	72-76
9846168-1	1998	Heparin affin regulatory peptide (HARP), also named pleiotropin, is a secreted polypeptide that belongs to a new family of heparin-binding growth/differentiation factors.	Heparin	123-130	pleiotrophin	Rattus norvegicus	0-32
34986404-4	2022	Treatment with intravenous immunoglobulins, however, could mask the ability of anti-PF4-heparin antibodies to bind and activate platelets in the presence of heparin, leading to false negative results at the immunoassay functional test.	Heparin	88-95	platelet factor 4	Homo sapiens	84-87
34986404-4	2022	Treatment with intravenous immunoglobulins, however, could mask the ability of anti-PF4-heparin antibodies to bind and activate platelets in the presence of heparin, leading to false negative results at the immunoassay functional test.	Heparin	157-164	platelet factor 4	Homo sapiens	84-87
35215371-9	2022	Both PPS and MPS showed stronger inhibition than heparin on the S-protein RBD or spike pseudotyped lentiviral particles binding to immobilized heparin.	Heparin	49-56	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	81-86
35215371-9	2022	Both PPS and MPS showed stronger inhibition than heparin on the S-protein RBD or spike pseudotyped lentiviral particles binding to immobilized heparin.	Heparin	143-150	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	81-86
9846168-1	1998	Heparin affin regulatory peptide (HARP), also named pleiotropin, is a secreted polypeptide that belongs to a new family of heparin-binding growth/differentiation factors.	Heparin	123-130	pleiotrophin	Rattus norvegicus	34-38
9712834-6	1998	By using heparin-Sepharose affinity to discriminate between the monomer and homodimer forms of FGF-1 and resolution by conventional and limited denaturant gel shift immunoblot analysis, it was possible to identify FGF-1 and Syn-1 as potential components of a denaturant- and reducing agent-sensitive extracellular complex.	Heparin	9-16	fibroblast growth factor 1	Bos taurus	95-100
35060381-0	2022	Structural Insights into the Cofactor Role of Heparin/Heparan Sulfate in Binding between the SARS-CoV-2 Spike Protein and Host Angiotensin-Converting Enzyme II.	Heparin	46-53	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	104-109
9712834-6	1998	By using heparin-Sepharose affinity to discriminate between the monomer and homodimer forms of FGF-1 and resolution by conventional and limited denaturant gel shift immunoblot analysis, it was possible to identify FGF-1 and Syn-1 as potential components of a denaturant- and reducing agent-sensitive extracellular complex.	Heparin	9-16	fibroblast growth factor 1	Bos taurus	214-219
35060381-1	2022	The viral entry process of the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) requires heparin and heparan sulfates from the cell surface, functioning as a cofactor for human angiotensin-converting enzyme 2 (ACE2) for recognizing the receptor-binding domain (RBD) of the spike (S) protein on the surface of the virion.	Heparin	107-114	angiotensin converting enzyme 2	Homo sapiens	195-226
35060381-1	2022	The viral entry process of the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) requires heparin and heparan sulfates from the cell surface, functioning as a cofactor for human angiotensin-converting enzyme 2 (ACE2) for recognizing the receptor-binding domain (RBD) of the spike (S) protein on the surface of the virion.	Heparin	107-114	angiotensin converting enzyme 2	Homo sapiens	228-232
9748709-0	1998	Pharmacokinetics of danaparoid sodium, dalteparin sodium and heparin determined by inhibitory effect on the activated coagulation factor X activity after single intravenous administration in rabbits.	Heparin	61-68	coagulation factor X	Oryctolagus cuniculus	118-138
35060381-1	2022	The viral entry process of the novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) requires heparin and heparan sulfates from the cell surface, functioning as a cofactor for human angiotensin-converting enzyme 2 (ACE2) for recognizing the receptor-binding domain (RBD) of the spike (S) protein on the surface of the virion.	Heparin	107-114	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	291-296
34991339-2	2022	Methods: The authors functionalized collagen nanofibers by conjugating heparin to the following growth factors for sustained release: PDGF-BB, TGF-beta1 and CTGF.	Heparin	71-78	cellular communication network factor 2	Homo sapiens	157-161
9692954-8	1998	PEDF chemically modified on lysine residues by biotinylation lost its capacity for interacting with heparin, implicating the involvement of PEDF lysine residues in heparin binding.	Heparin	100-107	serpin family F member 1	Homo sapiens	0-4
9692954-8	1998	PEDF chemically modified on lysine residues by biotinylation lost its capacity for interacting with heparin, implicating the involvement of PEDF lysine residues in heparin binding.	Heparin	164-171	serpin family F member 1	Homo sapiens	0-4
9692954-8	1998	PEDF chemically modified on lysine residues by biotinylation lost its capacity for interacting with heparin, implicating the involvement of PEDF lysine residues in heparin binding.	Heparin	164-171	serpin family F member 1	Homo sapiens	140-144
9692954-10	1998	A limited proteolysis product containing residues 21-approximately 260 bound to heparin with similar affinity as the intact PEDF.	Heparin	80-87	serpin family F member 1	Homo sapiens	124-128
9630674-2	1998	A 5-fold increase in heparin releasable HL activity was accompanied by moderate (approx.	Heparin	21-28	hes family bHLH transcription factor 1	Homo sapiens	40-42
9565256-2	1998	Nonanticoagulant activities of low molecular weight heparin (LMWH) include solubilization of the TNF-alpha receptor protein, inhibition of neutrophil adhesion, and regulation of thromboxane B2 (TXB2) biosynthesis.	Heparin	52-59	tumor necrosis factor	Sus scrofa	97-106
2597694-0	1989	Phosphate promotes glycation of antithrombin III which interferes with heparin binding.	Heparin	71-78	serpin family C member 1	Homo sapiens	32-48
2597694-1	1989	Nonenzymatic glycation of antithrombin III has been reported to cause the reduction of heparin-catalyzed thrombin-inhibiting activity in diabetes.	Heparin	87-94	serpin family C member 1	Homo sapiens	26-42
2597694-2	1989	The effect of in vitro nonenzymatic glycation of pure antithrombin III on heparin binding and heparin-potentiated activity under a variety of buffers and pH values was studied to further clarify the physiological significance of this reaction.	Heparin	74-81	serpin family C member 1	Homo sapiens	54-70
2597694-2	1989	The effect of in vitro nonenzymatic glycation of pure antithrombin III on heparin binding and heparin-potentiated activity under a variety of buffers and pH values was studied to further clarify the physiological significance of this reaction.	Heparin	94-101	serpin family C member 1	Homo sapiens	54-70
2597694-4	1989	Conversely, the heparin-catalyzed antithrombin activity decreased from 93.1% of controls for 0.01 M phosphate to 73.5% for 0.2 M phosphate as the extent of glycation increased.	Heparin	16-23	serpin family C member 1	Homo sapiens	34-46
2597694-5	1989	The increase in intrinsic fluorescence induced by binding of heparin to antithrombin III was also moderated by glycation of antithrombin III in a dose-dependent manner with a negative correlation coefficient of -0.94.	Heparin	61-68	serpin family C member 1	Homo sapiens	72-88
2597694-5	1989	The increase in intrinsic fluorescence induced by binding of heparin to antithrombin III was also moderated by glycation of antithrombin III in a dose-dependent manner with a negative correlation coefficient of -0.94.	Heparin	61-68	serpin family C member 1	Homo sapiens	124-140
2532218-6	1989	We also demonstrate that N-CAM-mediated intercellular adhesiveness is inhibited by 0.2 mg/ml heparin; but, at higher concentrations, reduced adhesion of parental cells was also seen.	Heparin	93-100	neural cell adhesion molecule 1	Homo sapiens	25-30
2480118-2	1989	Purified platelet GMP-140 bound to Heparin-Sepharose CL-6B and was eluted by approximately 0.5 M sodium chloride.	Heparin	35-42	selectin P	Homo sapiens	18-25
2480118-3	1989	Radioiodinated GMP-140 bound specifically and saturably to heparin immobilized on Matrex-Pel 102 beads.	Heparin	59-66	selectin P	Homo sapiens	15-22
2480118-4	1989	Binding of radioiodinated GMP-140 to heparin-Matrex-Pel 102 beads was divalent cation-independent and was strongly inhibited by excess fluid phase GMP-140 and heparin and by other sulfated glycans such as fucoidin and dextran-sulfate.	Heparin	37-44	selectin P	Homo sapiens	26-33
2480118-4	1989	Binding of radioiodinated GMP-140 to heparin-Matrex-Pel 102 beads was divalent cation-independent and was strongly inhibited by excess fluid phase GMP-140 and heparin and by other sulfated glycans such as fucoidin and dextran-sulfate.	Heparin	37-44	selectin P	Homo sapiens	147-154
2480118-4	1989	Binding of radioiodinated GMP-140 to heparin-Matrex-Pel 102 beads was divalent cation-independent and was strongly inhibited by excess fluid phase GMP-140 and heparin and by other sulfated glycans such as fucoidin and dextran-sulfate.	Heparin	159-166	selectin P	Homo sapiens	26-33
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	32-48
2509458-5	1989	Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin.	Heparin	79-86	serpin family C member 1	Homo sapiens	32-48
2509458-6	1989	In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding.	Heparin	5-12	serpin family C member 1	Homo sapiens	23-39
2509458-6	1989	In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding.	Heparin	178-185	serpin family C member 1	Homo sapiens	23-39
2627551-1	1989	Affinity chromatography on heparin-Sepharose was used to isolate two forms of antithrombin III(AT) from human, bovine, rabbit and rat blood plasma.	Heparin	27-34	serpin family C member 1	Homo sapiens	78-94
2632043-1	1989	It is known that antithrombin III (ATIII) activity is inhibited by tissue thromboplastin (TP) in the presence of heparin.	Heparin	113-120	serpin family C member 1	Homo sapiens	17-33
2632043-1	1989	It is known that antithrombin III (ATIII) activity is inhibited by tissue thromboplastin (TP) in the presence of heparin.	Heparin	113-120	serpin family C member 1	Homo sapiens	35-40
2806726-0	1989	The mechanism of precartilage mesenchymal condensation: a major role for interaction of the cell surface with the amino-terminal heparin-binding domain of fibronectin.	Heparin	129-136	fibronectin 1	Gallus gallus	155-166
2625740-3	1989	Moreover and ratio of AT-III-heparin complex formation was significantly reduced during two years, too (50.7 +/- 3.0% to 53.0 +/- 1.5%).	Heparin	29-36	serpin family C member 1	Homo sapiens	22-28
2625740-5	1989	Therefore, it was interestingly suggested the possibility that prolonged hemodialysis treatment induced a functional loss of AT-III, especially in a capacity to form a AT-III-heparin complex due to partial loss of the affinity for heparin.	Heparin	175-182	serpin family C member 1	Homo sapiens	125-131
2625740-5	1989	Therefore, it was interestingly suggested the possibility that prolonged hemodialysis treatment induced a functional loss of AT-III, especially in a capacity to form a AT-III-heparin complex due to partial loss of the affinity for heparin.	Heparin	231-238	serpin family C member 1	Homo sapiens	125-131
2478195-9	1989	The results suggest that heparin and high molecular weight dextran sulfate may be a useful dissociating agent of polymerized SAP in amyloid deposits.	Heparin	25-32	amyloid P component, serum	Homo sapiens	125-128
2478364-0	1989	The heparin and pentosan polysulfate binding sites of human antithrombin overlap but are not identical.	Heparin	4-11	serpin family C member 1	Homo sapiens	60-72
2478364-6	1989	Compared to the unfractionated heparin on an equal mass basis, the low-molecular-mass heparin (molecular mass 4-6 kDa) binds more strongly to antithrombin, induces a greater conformational change (about twofold), but is less potent in accelerating the inhibitory activity.	Heparin	31-38	serpin family C member 1	Homo sapiens	142-154
2478364-6	1989	Compared to the unfractionated heparin on an equal mass basis, the low-molecular-mass heparin (molecular mass 4-6 kDa) binds more strongly to antithrombin, induces a greater conformational change (about twofold), but is less potent in accelerating the inhibitory activity.	Heparin	86-93	serpin family C member 1	Homo sapiens	142-154
2478364-9	1989	These data clearly demonstrate that the heparin and pentosan polysulfate binding sites of antithrombin overlap (at Lys-125) but are not identical.	Heparin	40-47	serpin family C member 1	Homo sapiens	90-102
2511018-3	1989	The patient"s LpL purified from the PHP by heparin-Sepharose and phenyl-Sepharose chromatographies hydrolysed tributryrin, but not triolein emulsified with Triton X-100 and phosphatidylcholine (PC), or in chylomicrons, whereas normal LpL hydrolysed these substrates.	Heparin	43-50	lipoprotein lipase	Homo sapiens	14-17
2511019-7	1989	Thus although both class II and class III patients had an LPL protein with abnormal catalytic activity, class III patients also appeared to have a defect in heparin binding of LPL.	Heparin	157-164	lipoprotein lipase	Homo sapiens	176-179
2511019-9	1989	In contrast to class II patients, the LPL immunoreactive mass of class III patients did not show affinity for the heparin and eluted in the column void volume, suggesting the class III defect is also associated with a defect in heparin binding.	Heparin	228-235	lipoprotein lipase	Homo sapiens	38-41
2796749-3	1989	Familial lipoprotein-lipase-activity deficiency was diagnosed by the absence of lipoprotein-lipase activity in the plasma withdrawn ten and 20 minutes after intravenous injection of ten units of heparin per kilogram of body weight.	Heparin	195-202	lipoprotein lipase	Homo sapiens	9-27
2478015-3	1989	Patients receiving ATIII/heparin had significantly higher postoperative ATIII concentrations than dextran-treated patients and also had a low incidence of venous thromboembolic disease (7 percent).	Heparin	25-32	serpin family C member 1	Homo sapiens	72-77
2801725-0	1989	Antithrombin inactivation by neutrophil elastase requires heparin.	Heparin	58-65	serpin family C member 1	Homo sapiens	0-12
2801725-2	1989	Alternatively, we have recently observed an unexpected and paradoxical in vitro functioning of heparin that could result in the inactivation of antithrombin in pathologic conditions.	Heparin	95-102	serpin family C member 1	Homo sapiens	144-156
2801725-3	1989	Specifically, antithrombin was rendered nonfunctional as an inhibitor of clotting enzymes as a result of a limited, heparin-dependent cleavage by neutrophil elastase.	Heparin	116-123	serpin family C member 1	Homo sapiens	14-26
2801725-7	1989	This affinity of both antithrombin and elastase for heparin suggests a novel mechanism of potential specificity.	Heparin	52-59	serpin family C member 1	Homo sapiens	22-47
2801726-4	1989	After heating, a second heparin-affinity chromatography step is employed to isolate the active ATIII and to remove heat-denatured protein.	Heparin	24-31	serpin family C member 1	Homo sapiens	95-100
2801726-6	1989	The final product has a specific activity of not less than 6.4 IU ATIII per mg protein, of which over 90 percent binds to heparin on crossed immunoelectrophoresis.	Heparin	122-129	serpin family C member 1	Homo sapiens	66-71
2814937-2	1989	The abnormal antithrombin was isolated from plasma by chromatography on heparin-Sepharose at pH 6.0, and ion exchange on DEAE-Sephadex at pH 8.6 and 6.0.	Heparin	72-79	serpin family C member 1	Homo sapiens	13-25
2508778-9	1989	Heparin suppressed cumulus expansion in both EGF- and FSH-treated CEO, but did not prevent GVB stimulated by either hormone.	Heparin	0-7	epidermal growth factor	Mus musculus	45-48
2551064-8	1989	The second order rate constants for inhibition of bovine APC and Gla-domainless bovine APC by human PCI were 0.61 x 10(4) and 0.26 x 10(4) M-1s-1 in the absence of heparin and 0.54 x 10(6) and 0.71 x 10(6) M-1s-1 in the presence of heparin, respectively.	Heparin	164-171	GLA	Bos taurus	65-68
2551064-8	1989	The second order rate constants for inhibition of bovine APC and Gla-domainless bovine APC by human PCI were 0.61 x 10(4) and 0.26 x 10(4) M-1s-1 in the absence of heparin and 0.54 x 10(6) and 0.71 x 10(6) M-1s-1 in the presence of heparin, respectively.	Heparin	232-239	GLA	Bos taurus	65-68
2544589-0	1989	Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages.	Heparin	0-7	serpin family C member 1	Homo sapiens	32-48
2544589-2	1989	Human antithrombin III (AT-III) was partially reduced under mild conditions in the absence or presence of low molecular weight heparin.	Heparin	127-134	serpin family C member 1	Homo sapiens	6-22
12106141-7	1989	When the cells were treated with heparin prior to antibody incubation, the GDN immunoreactivity completely disappeared, whereas the distribution and abundance of laminin and fibronectin was not affected.	Heparin	33-40	serpin family E member 2	Rattus norvegicus	75-78
2738155-3	1989	Heparin-releasable (HR) LPL activity was approximately 2.5-fold higher in the 15 obese subjects, when compared with six lean subjects.	Heparin	0-7	lipoprotein lipase	Homo sapiens	24-27
2571074-1	1989	The heparin-induced secretion of LPL into the incubation medium of cardiac myocytes occurred in two phases: a rapid release (5-10 min), followed by a slower rate of release (10-60 min).	Heparin	4-11	lipoprotein lipase	Homo sapiens	33-36
2571074-4	1989	The rapid heparin-induced release of LPL probably occurs from sites that are at or near the cell surface, and so microtubules must participate in the intracellular transport of LPL from sites of synthesis and glycosylation to the surface binding sites.	Heparin	10-17	lipoprotein lipase	Homo sapiens	37-40
2571074-4	1989	The rapid heparin-induced release of LPL probably occurs from sites that are at or near the cell surface, and so microtubules must participate in the intracellular transport of LPL from sites of synthesis and glycosylation to the surface binding sites.	Heparin	10-17	lipoprotein lipase	Homo sapiens	177-180
2571074-5	1989	Heparin-releasable LPL could be resolved into two fractions by chromatography on con A-Sepharose; this pattern of elution was not affected by the prior treatment of cardiac myocytes with taxol.	Heparin	0-7	lipoprotein lipase	Homo sapiens	19-22
2732232-4	1989	A potentially complex reaction mechanism is suggested by the binding of both neutrophil elastase and antithrombin to heparin.	Heparin	117-124	serpin family C member 1	Homo sapiens	101-113
2732232-8	1989	Maximum acceleratory effects of heparin on the inactivation of antithrombin occur at heparin concentrations significantly lower than those required to saturate antithrombin.	Heparin	32-39	serpin family C member 1	Homo sapiens	63-75
2732232-8	1989	Maximum acceleratory effects of heparin on the inactivation of antithrombin occur at heparin concentrations significantly lower than those required to saturate antithrombin.	Heparin	32-39	serpin family C member 1	Homo sapiens	160-172
2732232-8	1989	Maximum acceleratory effects of heparin on the inactivation of antithrombin occur at heparin concentrations significantly lower than those required to saturate antithrombin.	Heparin	85-92	serpin family C member 1	Homo sapiens	63-75
2732232-9	1989	The divergence in acceleratory effect and antithrombin binding contrasts with the anticoagulant functioning of heparin in promoting the formation of covalent antithrombin-enzyme complexes and is likely to derive from the fact that neutrophil elastase is not consumed in the inactivation reaction.	Heparin	111-118	serpin family C member 1	Homo sapiens	158-170
2732232-10	1989	A size dependence was observed for the heparin effect since an anticoagulantly active octasaccharide fragment of heparin, with avid antithrombin binding activity, was without effect on the inactivation of antithrombin by neutrophil elastase.	Heparin	113-120	serpin family C member 1	Homo sapiens	132-144
2799763-4	1989	Fractionation of VSMC-conditioned medium by heparin-affigel chromatography separated three immunologically and functionally distinct PA inhibitors (PAI), namely PAI-1, PAI-2 and protease-nexin I.	Heparin	44-51	serpin family E member 1	Homo sapiens	133-146
2799763-6	1989	PA inhibitor 2 (PAI-2) had little affinity for heparin, whereas PA inhibitor 1 (PAI-1) bound to heparin and was eluted from the column at NaCl concentrations of 0.1 to 0.35 M. Protease-nexin I, eluted at NaCl concentrations of 0.5 M and higher.	Heparin	96-103	serpin family E member 1	Homo sapiens	64-78
2799763-6	1989	PA inhibitor 2 (PAI-2) had little affinity for heparin, whereas PA inhibitor 1 (PAI-1) bound to heparin and was eluted from the column at NaCl concentrations of 0.1 to 0.35 M. Protease-nexin I, eluted at NaCl concentrations of 0.5 M and higher.	Heparin	96-103	serpin family E member 1	Homo sapiens	80-85
2799763-10	1989	Thus, human VSMC produce all three presently known PAI and these can be separated in single heparin affinity purification step.	Heparin	92-99	serpin family E member 1	Homo sapiens	51-54
2739146-2	1989	The lipoprotein lipase (LpL) and hepatic triglyceride lipase (HTGL) activities of the post-heparin plasma were low, but detectable.	Heparin	91-98	lipoprotein lipase	Homo sapiens	4-22
2739146-2	1989	The lipoprotein lipase (LpL) and hepatic triglyceride lipase (HTGL) activities of the post-heparin plasma were low, but detectable.	Heparin	91-98	lipoprotein lipase	Homo sapiens	24-27
2541434-0	1989	Heparin suppresses the induction of c-fos and c-myc mRNA in murine fibroblasts by selective inhibition of a protein kinase C-dependent pathway.	Heparin	0-7	FBJ osteosarcoma oncogene	Mus musculus	36-41
2541434-3	1989	We show that heparin suppressed the induction of c-fos and c-myc mRNA by serum in murine (BALB/c) 3T3 fibroblasts.	Heparin	13-20	FBJ osteosarcoma oncogene	Mus musculus	49-54
2541434-7	1989	These results suggest that heparin inhibits a protein kinase C-dependent pathway for cell proliferation and suppresses the induction of c-fos and c-myc mRNA at a site distal to activation of the kinase.	Heparin	27-34	FBJ osteosarcoma oncogene	Mus musculus	136-141
2713384-3	1989	It was observed that lipoprotein lipase accounted for most of the triglyceride hydrolase activity in the heparin-treated plasma, and that the heparin-releasable activities caused an increase in HDL density but no measurable change in particle size when LCAT was inhibited.	Heparin	105-112	lipase G, endothelial type	Rattus norvegicus	33-39
2713384-10	1989	It is concluded that changes in HDL particle size are mainly attributable to LCAT, but that lipase activities, which are either free in rat plasma or releasable by heparin, play a role in restructuring the phospholipid moiety and altering the protein composition of the HDL, especially with respect to apoE, a potential ligand to cellular receptors.	Heparin	164-171	lipase G, endothelial type	Rattus norvegicus	92-98
2650580-3	1989	The authors investigated the effect of two heparin regimens (regimen I: 2,000 U/hr and regimen II: 500 U/hr) upon plasma antithrombin level (IU/mL) and activated thromboplastin time (sec).	Heparin	43-50	serpin family C member 1	Homo sapiens	121-133
2541026-10	1989	The level of C1q (a subcomponent of the first component of the complement system) was decreased in the UFH group (P less than 0.04), whereas in the LMWH group C1q levels increased.	Heparin	103-106	complement C1q A chain	Homo sapiens	13-16
2726317-6	1989	However, de novo generation of thrombin activity was very susceptible to inhibition by heparin, even in neonatal plasmas with physiologically low AT III levels.	Heparin	87-94	serpin family C member 1	Homo sapiens	146-152
2752479-6	1989	Inhibition of thrombin activity by the ATIII-APC-heparin mixture was weak as compared with that by the ATIII-heparin mixture after a 1-min incubation, but after a 2-min incubation the inhibitory activities were equal.	Heparin	49-56	serpin family C member 1	Homo sapiens	39-44
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	serpin family C member 1	Homo sapiens	40-45
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	serpin family C member 1	Homo sapiens	134-139
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	50-57	serpin family C member 1	Homo sapiens	134-139
2752479-7	1989	Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis.	Heparin	144-151	serpin family C member 1	Homo sapiens	40-45
2732214-1	1989	Extracellular phospholipase A2 was purified about 1.7 X 10(5) fold to near homogeneity from human synovial fluid of rheumatoid arthritis by sequential use of column chromatographies on heparin-Sepharose, butyl-Toyopearl, and reversed-phase HPLC.	Heparin	185-192	phospholipase A2 group IB	Rattus norvegicus	14-30
2749590-0	1989	Homozygous variant of antithrombin III that lacks affinity for heparin, AT III Kumamoto.	Heparin	63-70	serpin family C member 1	Homo sapiens	22-38
9485475-14	1998	These results suggest that binding of heparin to thrombin induces an allosteric effect causing destabilization of the thrombin-HCII(L444R) complex and that the allosteric effect may be mediated by the 60-loop.	Heparin	38-45	serpin family D member 1	Homo sapiens	127-131
2749590-4	1989	Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin.	Heparin	106-113	serpin family C member 1	Homo sapiens	154-160
2749590-4	1989	Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin.	Heparin	106-113	serpin family C member 1	Homo sapiens	154-160
2749590-7	1989	The patient"s parents and three of her brothers demonstrated qualitative abnormality of AT III; heparin cofactor activity was 30-50% of normal levels in the presence of both thrombin and F.Xa.	Heparin	96-103	serpin family C member 1	Homo sapiens	88-94
9531034-0	1998	Importance of the FcgammaRIIa-Arg/His-131 polymorphism in heparin-induced thrombocytopenia diagnosis.	Heparin	58-65	Fc gamma receptor IIa	Homo sapiens	18-29
2749590-8	1989	These findings indicate that the propositus" AT III lacks affinity for heparin and the mode of its inheritance seems to be autosomal dominant and, hence, the propositus would be a homozygote.	Heparin	71-78	serpin family C member 1	Homo sapiens	45-51
2713360-2	1989	The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration.	Heparin	41-48	serpin family C member 1	Homo sapiens	59-71
2713360-2	1989	The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration.	Heparin	280-287	serpin family C member 1	Homo sapiens	59-71
2713360-3	1989	In the absence of metal ions, H-kininogen minimally affected kappa obsd, measured at a constant concentration of heparin with high affinity for antithrombin (30 nM), at I = 0.15, pH 7.4 and 25 degrees C. However, at a saturating concentration of Zn2+ (10 microM), kappa obsd was reduced to 50% at approximately 20 nM H-kininogen and to that of the uncatalyzed reaction at greater than or equal to approximately 0.2 microM H-kininogen.	Heparin	113-120	serpin family C member 1	Homo sapiens	144-156
9495304-13	1998	CONCLUSIONS: Direct inhibition of thrombin activity with r-hirudin completely inhibits growth of thrombus, causes dissolution of a preexisting mural thrombus, and is more effective at lower levels of anticoagulation than the highest dose of heparin at shear rates typical of a moderate coronary stenosis.	Heparin	241-248	coagulation factor II, thrombin	Sus scrofa	34-42
2713873-6	1989	The resonance of the H-2 atom of the histidine, considered to be the N-terminal residue and to be located in the heparin binding-site, is strongly perturbed by heparin binding both to native and modified antithrombin.	Heparin	113-120	serpin family C member 1	Homo sapiens	204-216
2713873-6	1989	The resonance of the H-2 atom of the histidine, considered to be the N-terminal residue and to be located in the heparin binding-site, is strongly perturbed by heparin binding both to native and modified antithrombin.	Heparin	160-167	serpin family C member 1	Homo sapiens	204-216
9651145-8	1998	These results suggest that in the presence of heparin, antithrombin III interferes with the catabolism of TFPI mediated via Xa.	Heparin	46-53	tissue factor pathway inhibitor	Homo sapiens	106-110
2713873-8	1989	Resonances from two of the remaining four histidine units are sensitive to longer-range conformational changes, and show differences between binding of the two heparin species both in native and modified ATIII.	Heparin	160-167	serpin family C member 1	Homo sapiens	204-209
2713873-10	1989	This is particularly significant as regards the mechanism of action of heparin, because the synthetic pentasaccharide activates ATIII towards Factor Xa, but not towards thrombin.	Heparin	71-78	serpin family C member 1	Homo sapiens	128-133
9562412-8	1998	MxA values were relatively similar in heparin-treated samples and EDTA-treated samples, with differences not exceeding 1 ng/ml.	Heparin	38-45	MX dynamin like GTPase 1	Homo sapiens	0-3
2463827-4	1989	Predictions were then made as to the heparin-binding domains in endothelial cell growth factor, purpurin, and antithrombin-III.	Heparin	37-44	serpin family C member 1	Homo sapiens	110-126
2713428-0	1989	Activity toward thrombin-antithrombin of heparin immobilized on two hydrogels.	Heparin	41-48	serpin family C member 1	Homo sapiens	25-37
2713428-2	1989	We found that as tresyl chloride activation of PVA increased, the specific activity of the bound heparin toward thrombin and antithrombin decreased by nearly a factor of 10 and that commercial heparin bound to PEO had nearly ten-fold greater activity than when bound to PVA at comparable concentrations.	Heparin	97-104	serpin family C member 1	Homo sapiens	125-137
2713428-3	1989	These findings suggest that the long "leash" provided by PEO hydrogels may give the heparin more access to the thrombin-antithrombin pair than the tight bond to PVA, and that crowding of heparin units on a surface limits access of the thrombin-antithrombin pair.	Heparin	84-91	serpin family C member 1	Homo sapiens	120-132
2713428-3	1989	These findings suggest that the long "leash" provided by PEO hydrogels may give the heparin more access to the thrombin-antithrombin pair than the tight bond to PVA, and that crowding of heparin units on a surface limits access of the thrombin-antithrombin pair.	Heparin	187-194	serpin family C member 1	Homo sapiens	120-132
2576935-0	1989	Heparin-induced increase in plasma and serum gamma-glutamyl transpeptidase activity.	Heparin	0-7	gamma-glutamyltransferase 1	Rattus norvegicus	45-74
9493272-0	1998	The solution structure of the N-terminal domain of hepatocyte growth factor reveals a potential heparin-binding site.	Heparin	96-103	hepatocyte growth factor	Homo sapiens	51-75
2576935-3	1989	The present study was designed to determine the effect of heparin on serum and plasma GGT activity.	Heparin	58-65	gamma-glutamyltransferase 1	Rattus norvegicus	86-89
2576935-5	1989	GGT activity was 45.1 +/- 9.5 U/l (mean +/- SD) for serum compared with 161.2 +/- 46.1 U/l for serum plus heparin and 93.3 +/- 30.9 U/l for plasma prepared with heparin.	Heparin	161-168	gamma-glutamyltransferase 1	Rattus norvegicus	0-3
9493272-6	1998	This first structure of HGF reveals a novel folding topology with a distinct pattern of charge distribution and indicates a possible heparin-binding site.	Heparin	133-140	hepatocyte growth factor	Homo sapiens	24-27
9422744-5	1998	Residues 568-631 of the progelatinase A C-terminal domain are important in formation of the heparin binding site, since replacement of this region with the corresponding stromelysin-1 sequence abolished binding to heparin and the potentiation of activation.	Heparin	92-99	matrix metallopeptidase 2	Homo sapiens	24-39
2910581-1	1989	We compared concentrations of antithrombin III (AT-III) in plasma, as determined by an immunological method and by a functional thrombin inhibition method, in the presence of heparin in 160 blood samples from Type I diabetics.	Heparin	175-182	serpin family C member 1	Homo sapiens	30-46
2910581-1	1989	We compared concentrations of antithrombin III (AT-III) in plasma, as determined by an immunological method and by a functional thrombin inhibition method, in the presence of heparin in 160 blood samples from Type I diabetics.	Heparin	175-182	serpin family C member 1	Homo sapiens	48-54
9422744-5	1998	Residues 568-631 of the progelatinase A C-terminal domain are important in formation of the heparin binding site, since replacement of this region with the corresponding stromelysin-1 sequence abolished binding to heparin and the potentiation of activation.	Heparin	214-221	matrix metallopeptidase 2	Homo sapiens	24-39
2910581-6	1989	We suggest that the high concentrations of heparin cofactor II, 117 (SD 17)%, might have caused an overestimation of AT III in this group of patients with diabetes Type I, and should not be overlooked in other clinical situations.	Heparin	43-50	serpin family C member 1	Homo sapiens	117-123
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	interleukin 1 complex	Mus musculus	88-92
9447247-1	1997	Recombinant von Willebrand factor (r-vWF) was produced in serum-free medium on a large scale in recombinant Chinese hamster ovary cells and was purified from fermentation supernatant by a combination of anion exchange chromatography and heparin affinity chromatography.	Heparin	237-244	von Willebrand factor	Cricetulus griseus	12-40
2562205-3	1989	The anticoagulant activity of heparin arises primarily from its ability to bind to antithrombin III (AT III), altering the conformation and enhancing the activity of this major protease inhibitor.	Heparin	30-37	serpin family C member 1	Homo sapiens	83-99
2562205-3	1989	The anticoagulant activity of heparin arises primarily from its ability to bind to antithrombin III (AT III), altering the conformation and enhancing the activity of this major protease inhibitor.	Heparin	30-37	serpin family C member 1	Homo sapiens	101-107
2562205-4	1989	Passage of heparin through an immobilised AT III column yields two fractions: a high affinity fraction with 300-350 iu mg-1 anticoagulant activity, comprising one-third of the total, and a low affinity fraction with an activity of less than 10 iu mg-1, comprising the remaining two-thirds.	Heparin	11-18	serpin family C member 1	Homo sapiens	42-48
9353333-5	1997	Purified recombinant meizothrombin and meizothrombin(desF1) were inhibited by HCII in the presence of dermatan sulfate with maximal second-order rate constants of 8 x 10(6) M-1.min-1 and 1.8 x 10(7) M-1.min-1, respectively, but were inhibited less than one-tenth as fast by AT in the presence of heparin.	Heparin	296-303	serpin family D member 1	Homo sapiens	78-82
2530427-6	1989	Antithrombin III inhibition of activated Hageman factor is augmented by heparin which is also an activator of Hageman factor.	Heparin	72-79	serpin family C member 1	Homo sapiens	0-16
2741397-1	1989	Histones H2A, H2B, H3 and H5 were shown to be concerned with inhibitors of heparin and its complexes responsible for nonenzymatic fibrinolytic effect on unstabilized fibrin.	Heparin	75-82	H2B clustered histone 21	Homo sapiens	14-28
9342064-8	1997	The HSPG-bound Tat can be retrieved into a soluble form by heparin, heparinase or trypsin.	Heparin	59-66	tyrosine aminotransferase	Homo sapiens	15-18
16130275-1	1997	Naturally occurring forms of hepatocyte growth factor/scatter factor (HGF/SF) have been purified by heparin-Sepharose chromatography, followed by cation exchange chromatography from a pool of human seminal plasma.	Heparin	100-107	hepatocyte growth factor	Homo sapiens	29-53
3265623-0	1988	The heparin-catalysed inhibition of human factor XIa by antithrombin III is dependent on the heparin type.	Heparin	4-11	serpin family C member 1	Homo sapiens	56-72
3265623-0	1988	The heparin-catalysed inhibition of human factor XIa by antithrombin III is dependent on the heparin type.	Heparin	93-100	serpin family C member 1	Homo sapiens	56-72
16130275-2	1997	Using an enzyme-linked immunosorbant assay, MDCK scatter assay, and Western blot analysis, it was found that, after heparin-Sepharose chromatography, human HGF/SF present in seminal plasma eluted in two different fractions, between 0.72 and 0.85 M NaCl (fraction I) and between 0.95 and 1.10 M NaCl (fraction II).	Heparin	116-123	hepatocyte growth factor	Homo sapiens	156-162
9324156-2	1997	METHODS: The effect of taurolidine and heparin on growth of colon adenocarcinoma DHD/K12/TRb was measured in vitro and in vivo.	Heparin	39-46	keratin 12	Rattus norvegicus	85-88
3196724-5	1988	Immediately following its uptake by the liver, a large fraction of the lipoprotein lipase could be released by heparin, but the magnitude of this fraction decreased with time.	Heparin	111-118	lipase G, endothelial type	Rattus norvegicus	83-89
9363730-3	1997	Pharmacological dose of low molecular weight heparin (20 IU/ml) significantly (P &lt; 0.02) reduced the antiphospholipid antibody (aPL) binding in the ELISA and was able to restore GnRH-induced HCG secretion (P &lt; 0.05) in presence of aPL-containing sera.	Heparin	45-52	gonadotropin releasing hormone 1	Homo sapiens	181-185
3192507-1	1988	An endothelial cell glycoprotein that inhibits the initiation of the coagulation process promoted by tissue factor has been isolated by heparin-sepharose, hydroxyapatite and gel filtration chromatography.	Heparin	136-143	coagulation factor III, tissue factor	Homo sapiens	101-114
3186758-7	1988	The model accounted for enzymatic degradation as well as the binding of heparin and its breakdown products to antithrombin.	Heparin	72-79	serpin family C member 1	Homo sapiens	110-122
9308582-5	1997	METHODS: Standard heparin was oxidized with periodate, refined to have high vWF affinity and inhibitory potency, and tested in a guinea pig model of platelet-dependent arterial thrombosis.	Heparin	18-25	von Willebrand factor	Cavia porcellus	76-79
9308582-12	1997	CONCLUSIONS: The modified heparin with high vWF affinity was a more effective arterial antithrombotic agent, with fewer conventional anticoagulant effects than standard heparin.	Heparin	26-33	von Willebrand factor	Cavia porcellus	44-47
9483172-4	1997	Heparin-cofactor-II-dependent antithrombin activity of DHG or UFH was neutralized by PF4 at a high concentration to the same extent; however, prolongation of the APTT by DHG was more resistant to neutralization by PF4 at a physiological plasma level than that by UFH.	Heparin	62-65	platelet factor 4	Rattus norvegicus	85-88
9483172-4	1997	Heparin-cofactor-II-dependent antithrombin activity of DHG or UFH was neutralized by PF4 at a high concentration to the same extent; however, prolongation of the APTT by DHG was more resistant to neutralization by PF4 at a physiological plasma level than that by UFH.	Heparin	62-65	platelet factor 4	Rattus norvegicus	214-217
9483172-4	1997	Heparin-cofactor-II-dependent antithrombin activity of DHG or UFH was neutralized by PF4 at a high concentration to the same extent; however, prolongation of the APTT by DHG was more resistant to neutralization by PF4 at a physiological plasma level than that by UFH.	Heparin	263-266	platelet factor 4	Rattus norvegicus	85-88
9207927-14	1997	Immunoprecipitation analysis found that heparin inhibited serum, PMA, and PDGF but not EGF induced raf-1 phosphorylation.	Heparin	40-47	Raf-1 proto-oncogene, serine/threonine kinase	Rattus norvegicus	99-104
9208230-4	1997	Addition of heparin, or treatment with chlorate, an inhibitor of proteoglycan sulfation, resulted in enhanced or reduced growth factor response, respectively, and eliminated the differences between FGF-1 and FGF-2.	Heparin	12-19	fibroblast growth factor 2	Mus musculus	208-213
9169495-2	1997	The ability of heparin to prolong the activated partial thromboplastin time and the factor Xa- one-stage clotting time of normal plasma was markedly enhanced by addition of purified APC to the assays.	Heparin	15-22	APC regulator of WNT signaling pathway	Homo sapiens	182-185
9169495-3	1997	Experiments using purified clotting factors showed that heparin enhanced by fourfold the phospholipid-dependent inactivation of factor V by APC.	Heparin	56-63	APC regulator of WNT signaling pathway	Homo sapiens	140-143
9169495-6	1997	Coagulation assays using immunodepleted plasmas showed that the enhancement of heparin action by APC was independent of antithrombin III, heparin cofactor II, and protein S. Experiments using purified proteins showed that heparin did not inhibit factor V activation by thrombin.	Heparin	79-86	APC regulator of WNT signaling pathway	Homo sapiens	97-100
9210545-4	1997	The animals in bFGF-treated group were injected with 4 microg bFGF/rat in 0.15 mL normal saline solution containing heparin 0.1% (w/v) through the jugular vein at the onset of reperfusion.	Heparin	116-123	fibroblast growth factor 2	Rattus norvegicus	15-19
3262615-11	1988	Unfractionated heparin (1 micrograms/ml) stimulated the antithrombin III-dependent inhibition of factor IXa during factor X activation 400-fold.	Heparin	15-22	serpin family C member 1	Homo sapiens	56-72
18634104-1	1997	A peptide termed P189, derived from the sequence of a newly discovered protein, AAMP (angio-associated migratory cell protein), contains a motif that is predicted to a bind heparin.	Heparin	173-180	angio associated migratory cell protein	Homo sapiens	80-84
3169017-2	1988	A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups.	Heparin	70-77	serpin family C member 1	Homo sapiens	108-124
2611327-6	1989	Although heparin significantly accelerated thrombin inhibition by antithrombin lll, the remaining thrombin levels were still significantly above the minimum threshold required for irreversible platelet aggregation.	Heparin	9-16	serpin family C member 1	Homo sapiens	66-78
18634104-1	1997	A peptide termed P189, derived from the sequence of a newly discovered protein, AAMP (angio-associated migratory cell protein), contains a motif that is predicted to a bind heparin.	Heparin	173-180	angio associated migratory cell protein	Homo sapiens	86-125
9111037-8	1997	Selective 2-O-, 6-O-, total-O-desulfation, or N-desulfation/N-acetylation dramatically reduced the capacity of heparin to bind GST-Tat.	Heparin	111-118	tyrosine aminotransferase	Homo sapiens	131-134
2809592-6	1989	Binding of N-CAM 110 to collagens could be prevented in a concentration-dependent manner by the glycosaminoglycans heparin and chondroitin sulfate.	Heparin	115-122	neural cell adhesion molecule 1	Homo sapiens	11-16
3056863-5	1988	In experiments with CR and high heparin doses (4 U/ml) b2M release occurred during the first 15 minutes of in-vitro dialysis, but this increase was inhibited by removing the leukocytes from the blood, indicating that b2M is released from leukocytes.	Heparin	32-39	beta-2-microglobulin	Homo sapiens	55-58
3056863-5	1988	In experiments with CR and high heparin doses (4 U/ml) b2M release occurred during the first 15 minutes of in-vitro dialysis, but this increase was inhibited by removing the leukocytes from the blood, indicating that b2M is released from leukocytes.	Heparin	32-39	beta-2-microglobulin	Homo sapiens	217-220
2809592-7	1989	N-CAM 110 also interacted with immobilized heparin, and this interaction could be prevented by heparin and chondroitin sulfate.	Heparin	43-50	neural cell adhesion molecule 1	Homo sapiens	0-5
9111037-9	1997	Totally-O-desulfated and 2-O-desulfated heparins also showed a reduced capacity to inhibit the transactivating activity of GST-Tat.	Heparin	40-48	tyrosine aminotransferase	Homo sapiens	127-130
2809592-7	1989	N-CAM 110 also interacted with immobilized heparin, and this interaction could be prevented by heparin and chondroitin sulfate.	Heparin	95-102	neural cell adhesion molecule 1	Homo sapiens	0-5
3417867-1	1988	In obese women (n = 16) at their weight, fasting adipose tissue lipoprotein lipase (LPL) activity, obtained by elution with serum and heparin at 4 degrees and 37 degrees C, was inversely correlated to plasma estradiol levels (r = -0.724; P = 0.002) and (r = -0.641; P = 0.010), respectively.	Heparin	134-141	lipoprotein lipase	Homo sapiens	64-82
3417867-1	1988	In obese women (n = 16) at their weight, fasting adipose tissue lipoprotein lipase (LPL) activity, obtained by elution with serum and heparin at 4 degrees and 37 degrees C, was inversely correlated to plasma estradiol levels (r = -0.724; P = 0.002) and (r = -0.641; P = 0.010), respectively.	Heparin	134-141	lipoprotein lipase	Homo sapiens	84-87
9111037-10	1997	Very low molecular weight heparins showed a significant decrease in their capacity to bind GST-Tat and to inhibit its LTR transactivating activity when compared with conventional 13.6-kDa heparin.	Heparin	26-34	tyrosine aminotransferase	Homo sapiens	95-98
3417867-2	1988	Furthermore, fasting postheparin plasma LPL activity during a heparin infusion, showed an even stronger inverse correlation to plasma estradiol when measured at 60 min (r = -0.815; P less than 0.001).	Heparin	25-32	lipoprotein lipase	Homo sapiens	40-43
3417867-4	1988	Postprandial LPL activity in postheparin plasma, measured 10 min after a heparin injection, showed a strong positive correlation with plasma free testosterone (r = 0.780; P = 0.001).	Heparin	33-40	lipoprotein lipase	Homo sapiens	13-16
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	13-19
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
3187949-3	1988	Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern.	Heparin	115-122	serpin family C member 1	Homo sapiens	124-130
2555220-7	1989	The catalytic subunit of protein phosphatase 2A (PP2Ac) with EF-2 as a substrate exhibits the same sensitivity towards okadaic acid and insensitivity towards heparin as the EF-2 phosphatase of epidermal cytosol.	Heparin	158-165	protein phosphatase 2 (formerly 2A), catalytic subunit, beta isoform	Mus musculus	49-54
2555220-7	1989	The catalytic subunit of protein phosphatase 2A (PP2Ac) with EF-2 as a substrate exhibits the same sensitivity towards okadaic acid and insensitivity towards heparin as the EF-2 phosphatase of epidermal cytosol.	Heparin	158-165	eukaryotic translation elongation factor 2	Mus musculus	61-65
2478195-0	1989	Calcium-dependent polymerization of human serum amyloid P component is inhibited by heparin and dextran sulfate.	Heparin	84-91	amyloid P component, serum	Homo sapiens	42-67
2478195-8	1989	The polymerized SAP was reversibly dissociated by heparin and high molecular weight dextran sulfate.	Heparin	50-57	amyloid P component, serum	Homo sapiens	16-19
2766306-3	1989	Systemically administered heparin and intravesical therapy with recombinant tissue plasminogen activator duplicated the activity of intravesical heparin.	Heparin	145-152	plasminogen activator, tissue type	Rattus norvegicus	76-104
3187951-1	1988	A decreased plasma antithrombin activity in presence or in absence of heparin was discovered in a 47-year-old patient presenting with recurrent venous thromboembolism.	Heparin	70-77	serpin family C member 1	Homo sapiens	19-31
3187951-4	1988	The propositus" AT III was coeluted with normal AT III from an heparin-sepharose column.	Heparin	63-70	serpin family C member 1	Homo sapiens	16-22
9111037-12	1997	The results demonstrate that Tat interacts in a size-dependent manner with heparin/HS and that high affinity Tat-heparin interaction requires at least some 2-O-, 6-O-, and N-positions to be sulfated.	Heparin	75-82	tyrosine aminotransferase	Homo sapiens	29-32
3187951-7	1988	The specific activities measured as heparin cofactor antithrombin or factor Xa inhibition in absence of heparin were decreased to half the normal value.	Heparin	36-43	serpin family C member 1	Homo sapiens	53-65
9111037-12	1997	The results demonstrate that Tat interacts in a size-dependent manner with heparin/HS and that high affinity Tat-heparin interaction requires at least some 2-O-, 6-O-, and N-positions to be sulfated.	Heparin	113-120	tyrosine aminotransferase	Homo sapiens	29-32
3142530-0	1988	Heparin inhibits specific glycosyltransferase activities in interleukin 2 activated murine T cells.	Heparin	0-7	interleukin 2	Mus musculus	60-73
3142530-1	1988	In order to better understand the role of cell surface glycolipids in T lymphocyte activation, heparin was used to simultaneously modulate the expression of glycolipids and the lytic capacity of lymphocytes activated by interleukin-2.	Heparin	95-102	interleukin 2	Mus musculus	220-233
3142530-6	1988	Comparison of the glycosyltransferase activities of untreated and heparin-treated cells shows that the activities of a 2-3-sialyltransferase and a beta 1-3 galactosyltransferase are inhibited dramatically, while a third enzyme, N-acetyl-galactosaminyltransferase is unaffected.	Heparin	66-73	beta-1,4-N-acetyl-galactosaminyl transferase 2	Mus musculus	228-262
2794060-2	1989	The genes of seven structural mutants of antithrombin III (ATIII), presenting either defective serine protease reactivity or abnormal heparin binding, were analyzed.	Heparin	134-141	serpin family C member 1	Homo sapiens	41-57
2794060-2	1989	The genes of seven structural mutants of antithrombin III (ATIII), presenting either defective serine protease reactivity or abnormal heparin binding, were analyzed.	Heparin	134-141	serpin family C member 1	Homo sapiens	59-64
2504719-5	1989	However, these preparations of heparin still efficiently accelerate the inhibition of thrombin by antithrombin III.	Heparin	31-38	serpin family C member 1	Homo sapiens	98-114
2552799-8	1989	Since this ATIII is probably associated with heparin-like substances and exists in a high-affinity state, the inhibitor rapidly binds proteinases such as alpha-thrombin.	Heparin	45-52	serpin family C member 1	Homo sapiens	11-16
9111037-12	1997	The results demonstrate that Tat interacts in a size-dependent manner with heparin/HS and that high affinity Tat-heparin interaction requires at least some 2-O-, 6-O-, and N-positions to be sulfated.	Heparin	113-120	tyrosine aminotransferase	Homo sapiens	109-112
3136192-0	1988	The addition of endothelial cell growth factor and heparin to human umbilical vein endothelial cell cultures decreases plasminogen activator inhibitor-1 expression.	Heparin	51-58	serpin family E member 1	Homo sapiens	119-152
3136192-7	1988	A decrease in PAI-1 is also seen with higher concentrations of ECGF alone, but is greatly enhanced by the addition of heparin.	Heparin	118-125	serpin family E member 1	Homo sapiens	14-19
9111037-13	1997	The Tat binding activity of the glycosaminoglycans tested correlates with their capacity to affect the transactivating activity of extracellular Tat, indicating the possibility to design specific heparin/HS-like structures with Tat-antagonist activity.	Heparin	196-203	tyrosine aminotransferase	Homo sapiens	4-7
3215905-0	1988	Permeability of a heparin-polyvinyl alcohol hydrogel to thrombin and antithrombin III.	Heparin	18-25	serpin family C member 1	Homo sapiens	69-85
2529852-2	1989	The maximum observed second-order rate constant was, for the antithrombin III-thrombin reaction, 1.2 x 10(9) M-1.min-1 compared with 2.4 x 10(9) M-1.min-1 in the presence of high-affinity heparin.	Heparin	188-195	serpin family C member 1	Homo sapiens	61-77
9111037-13	1997	The Tat binding activity of the glycosaminoglycans tested correlates with their capacity to affect the transactivating activity of extracellular Tat, indicating the possibility to design specific heparin/HS-like structures with Tat-antagonist activity.	Heparin	196-203	tyrosine aminotransferase	Homo sapiens	145-148
2529852-4	1989	Differences were also observed in the maximal acceleration of the antithrombin III-Factor Xa interaction: 1.2 x 10(9) M-1.min-1 at 0.2 microM-heparin sulphate compared with 2.2 x 10(9) M-1.min-1 at 0.04 microM-heparin.	Heparin	142-149	serpin family C member 1	Homo sapiens	66-82
2529852-11	1989	The rate constant for transformation of the antithrombin III-Factor Xa complex into irreversible product differed between heparan sulphate (96 min-1) and heparin (429 min-1).	Heparin	154-161	serpin family C member 1	Homo sapiens	44-60
9111037-13	1997	The Tat binding activity of the glycosaminoglycans tested correlates with their capacity to affect the transactivating activity of extracellular Tat, indicating the possibility to design specific heparin/HS-like structures with Tat-antagonist activity.	Heparin	196-203	tyrosine aminotransferase	Homo sapiens	145-148
9092516-12	1997	Light scattering measurements on Ang-heparin mixtures suggest that 1 heparin chain (mass of 16.5 kDa) can accommodate approximately 9 Ang molecules.	Heparin	37-44	angiogenin	Homo sapiens	33-36
2855291-0	1988	[Effect of antithrombin III on the binding of heparin and its low molecular weight fraction CY 216 with endothelium in vitro].	Heparin	46-53	serpin family C member 1	Homo sapiens	11-27
9101641-5	1997	In these rats, the TFPI reappeared in the circulation following an intravenous injection of heparin sodium with reduced immunohistochemical staining of the TFPI on hepatic sinusoidal walls.	Heparin	92-106	tissue factor pathway inhibitor	Rattus norvegicus	19-23
2665815-4	1989	Addition of heparin to the medium resulted in a 2-fold increase in lipase secretion rate, whereas cell-surface-associated and intracellular lipase decreased by 76 and 20%, respectively.	Heparin	12-19	lipase G, endothelial type	Rattus norvegicus	67-73
2598315-0	1989	Dependence of the rate of thrombin/antithrombin III reaction upon the turnover rate of a catalytic amount of heparin.	Heparin	109-116	serpin family C member 1	Homo sapiens	35-51
2598315-1	1989	Commercially available heparin preparations slightly enhanced the rate of thrombin/antithrombin (AT) III reaction at pH 6.05 in the absence of NaCl.	Heparin	23-30	serpin family C member 1	Homo sapiens	74-104
3421540-7	1988	Ethylenediamine tetraacetate and heparin adversely affected the assay, resulting in lower assayed gastrin concentration values.	Heparin	33-40	gastrin	Equus caballus	98-105
9101641-5	1997	In these rats, the TFPI reappeared in the circulation following an intravenous injection of heparin sodium with reduced immunohistochemical staining of the TFPI on hepatic sinusoidal walls.	Heparin	92-106	tissue factor pathway inhibitor	Rattus norvegicus	156-160
2598315-2	1989	However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin).	Heparin	81-88	serpin family C member 1	Homo sapiens	112-118
2598315-2	1989	However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin).	Heparin	81-88	serpin family C member 1	Homo sapiens	201-207
9057637-6	1997	The production of HGF was enhanced by addition of heparin and phorbol ester.	Heparin	50-57	hepatocyte growth factor	Homo sapiens	18-21
2598315-2	1989	However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin).	Heparin	81-88	serpin family C member 1	Homo sapiens	201-207
2598315-2	1989	However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin).	Heparin	123-130	serpin family C member 1	Homo sapiens	112-118
2598315-2	1989	However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin).	Heparin	123-130	serpin family C member 1	Homo sapiens	112-118
2505842-5	1989	It is concluded that (1) PAI can function as both inhibitor and substrate of its target proteases, (2) if APC promotes fibrinolysis via inactivation of PAI, then APC must be present in concentrations several orders of magnitude greater than t-PA, or the interaction of APC and PAI must be accelerated by presently unknown mechanisms, and (3) in the absence of heparin, platelet PAI is the most rapid inhibitor of APC yet described.	Heparin	360-367	serpin family E member 1	Homo sapiens	25-28
2508260-9	1989	Plasma PAI 1 showed a slightly higher decrease after dDAVP plus standard heparin than after dDAVP plus saline but this difference was not statistically significant.	Heparin	73-80	serpin family E member 1	Homo sapiens	7-12
2799755-1	1989	We investigated the effect on thrombin generation in plasma of the pentasaccharide that represent the AT III/binding site in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	102-108
3055413-3	1988	An abnormal cathodal peak of antithrombin antigen was found in the presence, but not the absence, of heparin in the first dimension gel.	Heparin	101-108	serpin family C member 1	Homo sapiens	29-41
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Heparin	104-111	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	0-24
3391615-1	1988	Glucosamine-6-sulphatase (G6S), a lysosomal enzyme found in all cells, is involved in the catabolism of heparin, heparan sulphate, and keratan sulphate.	Heparin	104-111	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	26-29
9075122-0	1997	Effect of glucose and heparin on mesangial alpha 1(IV)COLL and MMP-2/TIMP-2 mRNA expression.	Heparin	22-29	matrix metallopeptidase 2	Homo sapiens	63-68
2458470-2	1988	The embryo-derived histamine-releasing factor (EHRF) has been isolated from the culture medium by means of heparin-Sepharose affinity chromatography.	Heparin	107-114	tumor protein, translationally-controlled 1	Homo sapiens	19-45
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	12-19	serpin family C member 1	Homo sapiens	142-148
9075122-7	1997	Interestingly, a shift in the balance of alpha 1(IV)COLL, MMP-2 and TIMP-2 was observed in high glucose, which was partially reversed by heparin supplementation.	Heparin	137-144	matrix metallopeptidase 2	Homo sapiens	58-63
2722856-10	1989	243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin.	Heparin	21-29	serpin family C member 1	Homo sapiens	220-226
2722856-10	1989	243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin.	Heparin	21-28	serpin family C member 1	Homo sapiens	220-226
9031720-9	1997	These data indicate that heparin-HC II complex reactivity is greater than that of the heparin-AT complex towards thrombin, whereas heparin affinity is stronger for AT.	Heparin	25-32	serpin family D member 1	Homo sapiens	33-38
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	130-138	serpin family C member 1	Homo sapiens	180-186
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	130-138	serpin family C member 1	Homo sapiens	308-314
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	206-214	serpin family C member 1	Homo sapiens	180-186
3339006-0	1988	Behavior of antithrombin III isoforms on immobilized heparins.	Heparin	53-61	serpin family C member 1	Homo sapiens	12-28
3339006-2	1988	Antithrombin III exists in plasma as major and minor isoforms differing in affinity for heparin.	Heparin	88-95	serpin family C member 1	Homo sapiens	0-16
8995378-0	1997	Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II.	Heparin	0-7	serpin family D member 1	Homo sapiens	103-122
3339006-7	1988	Because the modified lower-affinity isoform eluted with the similarly sized bovine serum albumin in these experiments, the difference in isoform affinity for heparin appears to be the result of a unique, secondary heparin-binding site in the higher-affinity isoform that can bind a heparin site with low affinity for antithrombin III.	Heparin	158-165	serpin family C member 1	Homo sapiens	317-333
3339006-7	1988	Because the modified lower-affinity isoform eluted with the similarly sized bovine serum albumin in these experiments, the difference in isoform affinity for heparin appears to be the result of a unique, secondary heparin-binding site in the higher-affinity isoform that can bind a heparin site with low affinity for antithrombin III.	Heparin	214-221	serpin family C member 1	Homo sapiens	317-333
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	206-214	serpin family C member 1	Homo sapiens	308-314
3339006-7	1988	Because the modified lower-affinity isoform eluted with the similarly sized bovine serum albumin in these experiments, the difference in isoform affinity for heparin appears to be the result of a unique, secondary heparin-binding site in the higher-affinity isoform that can bind a heparin site with low affinity for antithrombin III.	Heparin	214-221	serpin family C member 1	Homo sapiens	317-333
9105632-2	1997	Anti-platelet factor 4 (PF4)-heparin complex antibodies were detected in the sera of these five patients, although they had never previously been exposed to heparin.	Heparin	29-36	platelet factor 4	Homo sapiens	24-27
3339006-11	1988	A general model of heparin-antithrombin III interaction is proposed in which a high-affinity heparin site initially interacts with a primary site on antithrombin III.	Heparin	19-26	serpin family C member 1	Homo sapiens	27-43
3339006-11	1988	A general model of heparin-antithrombin III interaction is proposed in which a high-affinity heparin site initially interacts with a primary site on antithrombin III.	Heparin	19-26	serpin family C member 1	Homo sapiens	149-165
3339006-12	1988	The subsequent conformational change leads to a cooperative, entropy-driven association between secondary sites on the protein and low-affinity sites on heparin, stabilizing antithrombin III in its activated form.	Heparin	153-160	serpin family C member 1	Homo sapiens	174-190
3349123-1	1988	Heparin-like materials, characterized by a defined superficial density of functional groups which activate antithrombin III (AT III), when in contact with blood specifically inhibit thrombin as soon as it appears.	Heparin	0-7	serpin family C member 1	Homo sapiens	107-123
3349123-1	1988	Heparin-like materials, characterized by a defined superficial density of functional groups which activate antithrombin III (AT III), when in contact with blood specifically inhibit thrombin as soon as it appears.	Heparin	0-7	serpin family C member 1	Homo sapiens	125-131
2459037-1	1988	The effect of hirudin and heparin on thrombin-induced consumption of antithrombin III, fibrinogen and platelets was studied in a rat model.	Heparin	26-33	serpin family C member 1	Homo sapiens	69-85
2615648-4	1989	These occurred in individuals with a history of thromboembolic disease due to functional abnormalities of circulating antithrombin: ten had decreased heparin binding and activation, two had decreased inhibitory activity.	Heparin	150-157	serpin family C member 1	Homo sapiens	118-130
2719674-1	1989	The bone inductive protein, osteogenin, was isolated recently by heparin affinity chromatography.	Heparin	65-72	bone morphogenetic protein 3	Bos taurus	28-38
2749602-7	1989	The binding of Fab fragments of MA-15C5 and MA-8D3 was independent of the age (1 to 72 hrs) of the clot and of heparin anticoagulation and was only slightly decreased (by 20%) in the presence of circulating human fibrinogen (90 mg/kg body weight) and of human cross-linked fibrin degradation products at a plasma concentration of 10 micrograms/ml.	Heparin	111-118	FA complementation group B	Homo sapiens	15-18
9105632-4	1997	PF4 might be released from activated platelets and bind to endogenous heparin-like molecules, and antibodies with cross-reactivity to the PF4-heparin complex may have been generated by the endogenous complex before the first heparin treatment.	Heparin	70-77	platelet factor 4	Homo sapiens	0-3
2785004-2	1989	In this study we evaluated complement activation (C3a and C4a) by the heparin-protamine complex in 46 consecutive patients (40 received protamine sulfate to reverse heparin, and six did not) during and after coronary angiography.	Heparin	70-77	complement C4A (Rodgers blood group)	Homo sapiens	58-61
2465218-3	1988	The authors observed 5 patients with severe AT III decrease type I, 3 with functional abnormality and 2 with a pathological heparin binding.	Heparin	124-131	serpin family C member 1	Homo sapiens	44-50
9105632-5	1997	We conclude that it is worthwhile to check the platelet count and screen for anti-PF4-heparin complex antibody in advance to prevent thrombotic complications due to heparin treatment in patients with AMI.	Heparin	86-93	platelet factor 4	Homo sapiens	82-85
9162283-5	1997	And this direct effect of inhibition of the coagulation factors could be immediately arrested by intravenous injection of a neutralizing dose of the heparin antagonist VIM-DEMA.	Heparin	149-156	vimentin	Oryctolagus cuniculus	168-171
2709525-5	1989	In the second patient heparin did induce release of N-AC (39.7% of releasable N-AC) and aspirin, despite abolishing TxA2 synthesis, did not prevent aggregation or granule release.	Heparin	22-29	synuclein alpha	Homo sapiens	52-56
2709525-5	1989	In the second patient heparin did induce release of N-AC (39.7% of releasable N-AC) and aspirin, despite abolishing TxA2 synthesis, did not prevent aggregation or granule release.	Heparin	22-29	synuclein alpha	Homo sapiens	78-82
9386989-11	1997	Heparin had no effect on 125I-VEGF165 binding to the three Ig-domain receptor, suggesting that there are heparin binding determinants located in KDR Ig-domains 4 to 7.	Heparin	105-112	kinase insert domain receptor	Bos taurus	145-148
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	55-62	serpin family C member 1	Homo sapiens	127-143
3280421-10	1988	Antithrombin III can be isolated by linkage to its cofactor, heparin, on heparin-Sepharose.	Heparin	61-68	serpin family C member 1	Homo sapiens	0-16
3280421-10	1988	Antithrombin III can be isolated by linkage to its cofactor, heparin, on heparin-Sepharose.	Heparin	73-80	serpin family C member 1	Homo sapiens	0-16
27406868-0	1997	The Release of Tissue Factor Pathway Inhibitor and Platelet Factor 4 After Heparin Injection in Patients with Thrombocytosis.	Heparin	75-82	tissue factor pathway inhibitor	Homo sapiens	15-46
2492530-0	1989	Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236.	Heparin	11-18	serpin family C member 1	Homo sapiens	28-44
27406868-0	1997	The Release of Tissue Factor Pathway Inhibitor and Platelet Factor 4 After Heparin Injection in Patients with Thrombocytosis.	Heparin	75-82	platelet factor 4	Homo sapiens	51-68
2492530-2	1989	A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin.	Heparin	203-210	serpin family C member 1	Homo sapiens	150-166
3121595-2	1987	Heparin binds to human antithrombin III and accelerates its inhibitory activity in the blood coagulation system.	Heparin	0-7	serpin family C member 1	Homo sapiens	23-39
3121595-13	1987	When antithrombin III was pretreated with heparin, followed by trinitrobenzene sulfonic acid modification, the extent of modification at Lys114 and Lys125 decreased from 75% and 94% to 20% and 40%, respectively, whereas the modification at Lys287 remained nearly quantitative (greater than 95%).	Heparin	42-49	serpin family C member 1	Homo sapiens	5-21
2492530-3	1989	Antithrombin, modified with S-DABITC in the presence and absence of low molecular weight heparin (Mr 5000) was reduced, carboxymethylated, and digested with trypsin.	Heparin	89-96	serpin family C member 1	Homo sapiens	0-12
27406868-1	1997	Platelet factor 4 (PF4) and tissue factor pathway inhibitor (TFPI) are two proteins with high affinity for heparin.	Heparin	107-114	platelet factor 4	Homo sapiens	0-17
2492530-6	1989	When antithrombin was preincubated with heparin (2-fold by weight), followed by S-DABITC modification, the recovery of peptide T4 remained unchanged, but the recoveries of T1, T2, and T3 were reduced by 93, 86, and 98%, respectively.	Heparin	40-47	serpin family C member 1	Homo sapiens	5-17
2492530-9	1989	Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236.	Heparin	17-24	serpin family C member 1	Homo sapiens	34-46
27406868-1	1997	Platelet factor 4 (PF4) and tissue factor pathway inhibitor (TFPI) are two proteins with high affinity for heparin.	Heparin	107-114	platelet factor 4	Homo sapiens	19-22
2749590-4	1989	Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin.	Heparin	67-74	serpin family C member 1	Homo sapiens	154-160
2713360-1	1989	The binding of heparin to high molecular weight kininogen (H-kininogen) was analyzed by the effect of kininogen in decreasing the heparin-induced enhancement of the rate of inactivation of thrombin by antithrombin.	Heparin	15-22	serpin family C member 1	Homo sapiens	201-213
2713360-1	1989	The binding of heparin to high molecular weight kininogen (H-kininogen) was analyzed by the effect of kininogen in decreasing the heparin-induced enhancement of the rate of inactivation of thrombin by antithrombin.	Heparin	130-137	serpin family C member 1	Homo sapiens	201-213
2491851-10	1989	Calcium and calmodulin added to neurofilament preparations in the presence of heparin modestly stimulated the phosphorylation of L-1 and L-3, but not L-2, and the stimulation was reversed by trifluoperazine.	Heparin	78-85	L1 cell adhesion molecule	Mus musculus	129-140
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	17-24	serpin family C member 1	Homo sapiens	76-88
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	17-24	serpin family C member 1	Homo sapiens	193-205
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	115-122	serpin family C member 1	Homo sapiens	193-205
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	30-37	serpin family C member 1	Homo sapiens	110-122
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	serpin family C member 1	Homo sapiens	110-122
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	serpin family C member 1	Homo sapiens	110-122
2445746-7	1987	Furthermore, S protein/vitronectin neutralized the anti-Factor Xa activity of a synthetic pentasaccharide comprising the antithrombin-binding sequence of heparin.	Heparin	154-161	serpin family C member 1	Homo sapiens	121-133
2445746-10	1987	These findings suggest that S protein/vitronectin may interact through its glycosaminoglycan binding domain(s) with various functional domains of the heparin (heparan sulfate) molecule, including the antithrombin-binding pentasaccharide sequence.	Heparin	150-157	serpin family C member 1	Homo sapiens	200-212
27406868-1	1997	Platelet factor 4 (PF4) and tissue factor pathway inhibitor (TFPI) are two proteins with high affinity for heparin.	Heparin	107-114	tissue factor pathway inhibitor	Homo sapiens	28-59
27406868-3	1997	Prior work has demonstrated that the platelet count is one of the factors affecting the levels of heparin-releasable PF4.	Heparin	98-105	platelet factor 4	Homo sapiens	117-120
2523675-1	1989	Heparin and heparan sulfate can be cleaved selectively at their N-sulfated glucosamine residues by direct treatment with nitrous acid at pH 1.5.	Heparin	0-7	alanine--glyoxylate and serine--pyruvate aminotransferase	Homo sapiens	137-141
27406868-4	1997	We therefore characterized the response to a dose of intravenous heparin previously demonstrated to completely displace PF4 from the non-platelet pool in subjects with normal or increased platelet counts.	Heparin	65-72	platelet factor 4	Homo sapiens	120-123
2543347-0	1989	In vivo and in vitro release of lipoprotein lipase and hepatic lipase by low molecular weight heparins.	Heparin	94-102	lipoprotein lipase	Homo sapiens	32-50
2829825-1	1987	Heparin (5 units/ml) produced a rapid (5-10 min) release of lipoprotein lipase (LPL) into the incubation medium of cardiac myocytes.	Heparin	0-7	lipoprotein lipase	Homo sapiens	60-78
2829825-1	1987	Heparin (5 units/ml) produced a rapid (5-10 min) release of lipoprotein lipase (LPL) into the incubation medium of cardiac myocytes.	Heparin	0-7	lipoprotein lipase	Homo sapiens	80-83
9040053-7	1997	Gelatinase A (MMP-2) activity increased in heparin treated cells, and the TIMP-1 level increased in cholesterol-treated cells.	Heparin	43-50	matrix metallopeptidase 2	Homo sapiens	14-19
2730347-2	1989	Commercial heparin has now been shown to be a mixture of over 100 different closely related sulfated polysaccharides of which only 10% activate antithrombin-III.	Heparin	11-18	serpin family C member 1	Homo sapiens	144-160
2730347-9	1989	(e) Commercial heparin releases enzymes from the endothelium, lipoprotein lipase and histaminase (D.A.O.).	Heparin	15-22	lipoprotein lipase	Homo sapiens	62-80
9040053-8	1997	Based on Northern blot analysis, we observed that both MMP-1 and MMP-2 were induced at the gene transcription level by heparin and that TIMP-1 was induced by cholesterol.	Heparin	119-126	matrix metallopeptidase 2	Homo sapiens	65-70
9247321-1	1997	In rat olfactory bulb membranes, the stimulation of adenylyl cyclase by the cholinergic agonist carbachol (CCh) was markedly inhibited by heparin at concentrations (0.3-10 microM) that had smaller or no effects on the enzyme stimulations elicited by vasoactive intestinal peptide, pituitary adenylate cyclase activating polypeptide (PACAP), 1-isoproterenol and corticotropin releasing hormone.	Heparin	138-145	adenylate cyclase activating polypeptide 1	Rattus norvegicus	333-338
2481530-7	1989	In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin doses required might entail an unexceptable bleeding risk, e.g. in simultaneous thrombocytopenia.	Heparin	122-129	serpin family C member 1	Homo sapiens	46-62
2481530-7	1989	In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin doses required might entail an unexceptable bleeding risk, e.g. in simultaneous thrombocytopenia.	Heparin	191-198	serpin family C member 1	Homo sapiens	21-33
2481530-7	1989	In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin doses required might entail an unexceptable bleeding risk, e.g. in simultaneous thrombocytopenia.	Heparin	191-198	serpin family C member 1	Homo sapiens	46-62
3667601-5	1987	The fraction of biologically active ATIII has been purified from total ATIII by affinity fractionation on heparin-Sepharose.	Heparin	106-113	serpin family C member 1	Homo sapiens	36-41
3667601-6	1987	This fractionation indicates that the differences in the active and inactive forms of expressed ATIII result from differences in their ability to bind heparin.	Heparin	151-158	serpin family C member 1	Homo sapiens	96-101
3667601-7	1987	Purified ATIII has a specific activity very similar to that of plasma-derived ATIII and exhibits typical heparin-accelerated ATIII activity.	Heparin	105-112	serpin family C member 1	Homo sapiens	9-14
3478684-0	1987	Isolation of osteogenin, an extracellular matrix-associated, bone-inductive protein, by heparin affinity chromatography.	Heparin	88-95	bone morphogenetic protein 3	Bos taurus	13-23
3621562-1	1987	We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III).	Heparin	62-69	serpin family C member 1	Homo sapiens	158-174
3621562-1	1987	We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III).	Heparin	62-69	serpin family C member 1	Homo sapiens	176-182
2910358-8	1989	Cell surface bound heparin was functionally active and markedly accelerated the inactivation of thrombin by antithrombin III.	Heparin	19-26	serpin family C member 1	Homo sapiens	108-124
2910359-2	1989	The effects of this heparin-neutralizing protein on the interaction between antithrombin III and cultured porcine aortic endothelial cells were examined.	Heparin	20-27	serpin family C member 1	Homo sapiens	76-92
2805645-4	1989	A method utilizing heparin-agarose affinity chromatography was more efficient for purifying lactoferrin than a method including gel filtration, ion exchange chromatography and a second gel filtration.	Heparin	19-26	lactotransferrin	Bos taurus	92-103
3621562-1	1987	We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III).	Heparin	99-106	serpin family C member 1	Homo sapiens	158-174
9469632-1	1997	An immune response to heparin, which is clinically manifested by the development of thrombocytopenia with or without thrombosis, is stimulated by a complex of heparin with platelet factor 4 (PF4).	Heparin	22-29	platelet factor 4	Homo sapiens	191-194
3621562-1	1987	We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III).	Heparin	99-106	serpin family C member 1	Homo sapiens	176-182
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	15-22	APC regulator of WNT signaling pathway	Homo sapiens	70-73
3305015-0	1987	Probing the heparin-binding domain of human antithrombin III with V8 protease.	Heparin	12-19	serpin family C member 1	Homo sapiens	44-60
2920976-9	1989	The low antithrombin III concentration (0.44 +/- 0.13 mg/dl) in protein-poor dialysate seems to be sufficient to inhibit the thrombin activity after acceleration by heparin.	Heparin	165-172	serpin family C member 1	Homo sapiens	8-24
2488845-1	1989	Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes.	Heparin	0-7	serpin family C member 1	Homo sapiens	128-144
2488845-1	1989	Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes.	Heparin	75-82	serpin family C member 1	Homo sapiens	128-144
3305015-9	1987	259, 939-941], the heparin-binding site of antithrombin III has been suggested to be in the region of Pro-41, Arg-47 and Trp-49.	Heparin	19-26	serpin family C member 1	Homo sapiens	43-59
8948048-0	1996	The effect of heparin and its neutralisation on functional assays for factor VIIa, factor VII and TFPI.	Heparin	14-21	tissue factor pathway inhibitor	Homo sapiens	70-102
3305015-10	1987	In this study the heparin-binding site was probed by preferential cleavage of V8 protease on heparin-treated and non-treated native antithrombin III.	Heparin	18-25	serpin family C member 1	Homo sapiens	132-148
3305015-10	1987	In this study the heparin-binding site was probed by preferential cleavage of V8 protease on heparin-treated and non-treated native antithrombin III.	Heparin	93-100	serpin family C member 1	Homo sapiens	132-148
3305015-11	1987	The study has been based on the presumption that the heparin-binding site of antithrombin III is situated at exposed surface domain and may be preferentially attacked during limited proteolytic digestion.	Heparin	53-60	serpin family C member 1	Homo sapiens	77-93
3624220-0	1987	Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides.	Heparin	49-56	serpin family C member 1	Homo sapiens	14-26
2488845-2	1989	The extent of inactivation, for a constant flow time, was approximately constant over ten cycles of exposure to thrombin and antithrombin III, suggesting that the immobilized heparin was reusable, as expected from the catalytic nature of non-immobilized heparin.	Heparin	175-182	serpin family C member 1	Homo sapiens	125-141
2922702-1	1989	Heparins from different species and tissues show similar levels of ATIII and HCII mediated anti-IIa activities.	Heparin	0-8	serpin family C member 1	Homo sapiens	67-72
2922702-3	1989	Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity.	Heparin	106-113	serpin family C member 1	Homo sapiens	116-121
2922702-3	1989	Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity.	Heparin	106-113	serpin family C member 1	Homo sapiens	184-189
3238650-1	1988	Antithrombin Milano is an unusual antithrombin variant, exhibiting an abnormal, fast moving component on crossed immunoelectrophoresis (in the absence of heparin).	Heparin	154-161	serpin family C member 1	Homo sapiens	0-12
8948048-7	1996	In the amidolytic substrate assays for TFPI and FVII, heparin with or without neutralisation resulted in only small changes in the optical density at 405nm and hence plasma levels of these factors were not significantly changed.	Heparin	54-61	tissue factor pathway inhibitor	Homo sapiens	39-43
8948051-1	1996	Tissue factor pathway inhibitor (TFPI) is mainly bound to the vessel wall and is released to circulating blood after injections of heparin.	Heparin	131-138	tissue factor pathway inhibitor	Rattus norvegicus	33-37
3179438-4	1988	Two dimensional immunoelectrophoresis of antithrombin-III-Hamilton in the presence of heparin is normal.	Heparin	86-93	serpin family C member 1	Homo sapiens	41-57
3499176-1	1987	The inactivation of human factor XIa by human antithrombin III was studied under pseudo-first-order reaction conditions (excess antithrombin III) both in the absence and in the presence of heparin.	Heparin	189-196	serpin family C member 1	Homo sapiens	46-62
3499176-9	1987	From the kinetic data, a binding constant (Kd) of 0.14 microM was inferred for the binding of antithrombin III to heparin.	Heparin	114-121	serpin family C member 1	Homo sapiens	94-110
8948051-2	1996	It has been suggested that the highly positively charged carboxy terminal end of heparin releasable TFPI is bound to negatively charged binding molecule(s), presumably glycosaminoglycans (GAGs), on the luminal surface of endothelial cells.	Heparin	81-88	tissue factor pathway inhibitor	Rattus norvegicus	100-104
3584126-14	1987	The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin.	Heparin	57-64	serpin family C member 1	Homo sapiens	182-194
3584126-14	1987	The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin.	Heparin	123-130	serpin family C member 1	Homo sapiens	182-194
3584127-2	1987	Is the heparin-induced conformational change in antithrombin required for rapid inactivation of thrombin?	Heparin	7-14	serpin family C member 1	Homo sapiens	48-60
3584127-3	1987	The role of antithrombin conformation in heparin-catalyzed inhibition of thrombin was investigated using antithrombins modified with the tryptophan reagent dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNB).	Heparin	41-48	serpin family C member 1	Homo sapiens	12-24
3584127-4	1987	Affinity fractionation of HNB-labeled antithrombin (0.6-0.7 mol of HNB/mol of protein) on heparin-Sepharose using a linear salt gradient allowed separation of three singly labeled protein species and a fourth HNB-antithrombin species which co-eluted with unlabeled protein.	Heparin	90-97	serpin family C member 1	Homo sapiens	38-50
3584127-9	1987	The kinetic analysis indicated that each of these HNB-antithrombin derivatives, which undergo the heparin-induced changes to varying extents, can react with thrombin at the same maximal rate.	Heparin	98-105	serpin family C member 1	Homo sapiens	54-66
3584127-10	1987	Thus, this series of chemically modified antithrombin species demonstrated that the conformational change which is induced in antithrombin by heparin does not render the protein intrinsically more reactive toward thrombin.	Heparin	142-149	serpin family C member 1	Homo sapiens	41-53
3584127-10	1987	Thus, this series of chemically modified antithrombin species demonstrated that the conformational change which is induced in antithrombin by heparin does not render the protein intrinsically more reactive toward thrombin.	Heparin	142-149	serpin family C member 1	Homo sapiens	126-138
2851191-7	1988	This concentration of the three LMW heparins increased, by approximately 70-fold, the rate of factor Xa inhibition by purified antithrombin III compared to the 50-fold increase seen with the two unfractionated heparins.	Heparin	36-44	serpin family C member 1	Homo sapiens	127-143
3180999-1	1988	A 56-nucleotide mutagenic oligomer containing six mismatches with the wild-type template was used to construct multiple transversion mutations in the putative heparin binding region of the rat neural cell adhesion molecule (NCAM) cDNA sequence.	Heparin	159-166	neural cell adhesion molecule 1	Rattus norvegicus	193-222
3180999-1	1988	A 56-nucleotide mutagenic oligomer containing six mismatches with the wild-type template was used to construct multiple transversion mutations in the putative heparin binding region of the rat neural cell adhesion molecule (NCAM) cDNA sequence.	Heparin	159-166	neural cell adhesion molecule 1	Rattus norvegicus	224-228
2978866-2	1988	The strong affinity for heparin of the secreted protein made it possible to purify the hst-1 protein to homogeneity in a two-step procedure.	Heparin	24-31	hybrid sterility 1	Mus musculus	87-92
8948051-11	1996	The potency of different GAGs to displace bound rTFPI was in the following order: Unfractionated heparin (UF) &gt; low-molecular weight (LMW) heparin &gt; hexadecasaccharides/octasaccharides/dodecasaccharides &gt; heparan sulfate &gt; dermatan sulfate.	Heparin	97-104	tissue factor pathway inhibitor	Rattus norvegicus	48-53
8824228-8	1996	PGHS-2-dependent delayed-phase PGD2 generation elicited by IgE-dependent activation of BALB/cJ BMMC primed with KL + IL-10 was also accompanied by the induction of type IIA PLA2 transcripts and was suppressed by heparin, with concomitant release of PLA2 into the supernatant.	Heparin	212-219	prostaglandin-endoperoxide synthase 2	Mus musculus	0-6
3553188-0	1987	Heparin decreases the degradation rate of lipoprotein lipase in adipocytes.	Heparin	0-7	lipoprotein lipase	Homo sapiens	42-60
8878536-2	1996	Addition of heparin to cultures of human fibroblasts, leukemic cells, and umbilical vein endothelial cells stimulated HGF production to 3-6-fold higher levels than seen in the absence of heparin.	Heparin	12-19	hepatocyte growth factor	Homo sapiens	118-121
3553188-10	1987	The above data demonstrate that the increase in lipoprotein lipase protein secretion, observed upon addition of heparin to cultured adipocytes, is due to a decreased degradation rate with no change in synthetic rate.	Heparin	112-119	lipoprotein lipase	Homo sapiens	48-66
3553850-4	1987	Adipose tissue lipoprotein lipase activity released by heparin was also determined.	Heparin	55-62	lipoprotein lipase	Homo sapiens	15-33
3224126-4	1988	In order to ascertain the heparin-like mechanism of this activity, we have studied the interactions of thrombin, antithrombin III and thrombin-antithrombin III complex with the inner face of these treated tubings under controlled-flow conditions.	Heparin	26-33	serpin family C member 1	Homo sapiens	143-159
8798721-10	1996	However, HGF/NK2, another HGF/SF splice variant, as well as heparin, potently inhibit HGF/SF-induced collagenase-1 synthesis.	Heparin	60-67	hepatocyte growth factor	Homo sapiens	86-92
3416077-5	1988	These results suggested that the Fab portion of IgG binds to heparin forming an immune complex and the immune complexes initiate the platelet release reaction by binding to the platelet Fc receptors.	Heparin	61-68	FA complementation group B	Homo sapiens	33-36
3416077-10	1988	These studies indicate that heparin-induced thrombocytopenia is an IgG-heparin immune complex disorder involving both the Fab and Fc portion of the IgG molecule.	Heparin	28-35	FA complementation group B	Homo sapiens	122-125
8857955-5	1996	With the exception of a subpopulation of patient samples (5/29, 17%), we found that reduced PF4 and the peptides were uniformly non-reactive with the HIT-Abs in the presence of heparin.	Heparin	177-184	platelet factor 4	Homo sapiens	92-95
3496682-3	1987	In the presence of heparin, factor VIIa activity was inhibited 50% by purified antithrombin III and plasma in 90 min and 75 min, respectively.	Heparin	19-26	serpin family C member 1	Homo sapiens	79-95
3496682-6	1987	These data indicate that antithrombin III appears to be the sole plasma protease inhibitor of human factor VIIa, and the expression of its inhibitory activity against factor VIIa is absolutely dependent upon the presence of exogenous heparin.	Heparin	234-241	serpin family C member 1	Homo sapiens	25-41
3198064-7	1988	In all patients the adipose tissue lipoprotein lipase activity in post-heparin plasma was blunted or near absent.	Heparin	71-78	lipoprotein lipase	Homo sapiens	35-53
8857955-6	1996	Reduced PF4 and PF4 carboxy-terminal peptides with a minimum size of 19 amino acids were recognized by a minority (5/29) of HIT-Abs samples but only when heparin was present.	Heparin	154-161	platelet factor 4	Homo sapiens	8-11
8857955-6	1996	Reduced PF4 and PF4 carboxy-terminal peptides with a minimum size of 19 amino acids were recognized by a minority (5/29) of HIT-Abs samples but only when heparin was present.	Heparin	154-161	platelet factor 4	Homo sapiens	16-19
3191114-10	1988	Patient antithrombin III, isolated by affinity chromatography on heparin-Sepharose, was reacted with purified thrombin.	Heparin	65-72	serpin family C member 1	Homo sapiens	8-24
3580302-0	1987	Antithrombin III Northwick Park: demonstration of an inactive high MW complex with increased affinity for heparin.	Heparin	106-113	serpin family C member 1	Homo sapiens	0-16
3576117-0	1987	Plasma kinetics of lipoprotein lipase and hepatic lipase activities induced by heparin and a low molecular weight heparin fragment.	Heparin	79-86	lipoprotein lipase	Homo sapiens	19-37
3576117-0	1987	Plasma kinetics of lipoprotein lipase and hepatic lipase activities induced by heparin and a low molecular weight heparin fragment.	Heparin	114-121	lipoprotein lipase	Homo sapiens	19-37
3576117-3	1987	The peak values, as well as the accumulated release of LPL activity, were dose dependent and were twice as high after heparin as after LMWH.	Heparin	118-125	lipoprotein lipase	Homo sapiens	55-58
3576117-3	1987	The peak values, as well as the accumulated release of LPL activity, were dose dependent and were twice as high after heparin as after LMWH.	Heparin	135-139	lipoprotein lipase	Homo sapiens	55-58
3576117-4	1987	The plasma half-life of LPL activity followed first order kinetics and was similar for both heparin preparations when given in comparable doses.	Heparin	92-99	lipoprotein lipase	Homo sapiens	24-27
3215905-1	1988	The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels.	Heparin	56-63	serpin family C member 1	Homo sapiens	34-50
3215905-1	1988	The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels.	Heparin	189-196	serpin family C member 1	Homo sapiens	34-50
2840071-3	1988	Rechromatography of peak GII on heparin-agarose, in the presence of 0.5% sodium cholate, resulted in separation of PLC and GTP-binding activities, and loss of GTP-dependent PLC activity.	Heparin	32-39	heparan sulfate proteoglycan 2	Homo sapiens	115-118
3582495-1	1987	PAF-acether (platelet-activating factor) and adrenaline synergized to induce aggregation of human platelets in whole blood and in platelet-rich plasma (PRP) irrespective of the use of citrate, of heparin or acid-citrate dextrose (ACD) as anticoagulants, whereas the partial adrenoceptor agonist clonidine imitated adrenaline in a limited number of cases and only when blood was collected in ACD.	Heparin	196-203	PCNA clamp associated factor	Homo sapiens	0-3
8857955-9	1996	These studies demonstrate that the majority of HIT-Abs recognize a noncontiguous conformational epitope on the PF4 molecule that is produced when four to eight PF4 molecules are bound together by heparin.	Heparin	196-203	platelet factor 4	Homo sapiens	111-114
8857955-9	1996	These studies demonstrate that the majority of HIT-Abs recognize a noncontiguous conformational epitope on the PF4 molecule that is produced when four to eight PF4 molecules are bound together by heparin.	Heparin	196-203	platelet factor 4	Homo sapiens	160-163
2455567-1	1988	Vitronectin, also known as serum-spreading factor or S-protein, mediates cell adhesion and inhibits formation of the membrane-lytic complex of complement and the rapid inactivation of thrombin by antithrombin III in the presence of heparin.	Heparin	232-239	serpin family C member 1	Homo sapiens	196-212
8979119-5	1996	Current research on TFPI is mainly focused on the cell biology of TFPI, on the contribution of TFPI to the anticoagulant action of heparins, and on the role of lipoprotein-associated TFPI.	Heparin	131-139	tissue factor pathway inhibitor	Homo sapiens	20-24
3413737-4	1988	Two populations of ATIII were detected by affinity chromatography on heparin-sepharose from affected members" plasma.	Heparin	69-76	serpin family C member 1	Homo sapiens	19-24
3556575-1	1987	We have previously communicated that heparin released asymmetric acetylcholinesterase (AChE) from cholinergic synapses.	Heparin	37-44	acetylcholinesterase	Rattus norvegicus	65-85
3556575-1	1987	We have previously communicated that heparin released asymmetric acetylcholinesterase (AChE) from cholinergic synapses.	Heparin	37-44	acetylcholinesterase	Rattus norvegicus	87-91
3556575-2	1987	Here we report studies showing that heparin, besides releasing asymmetric AChE from the skeletal muscle extracellular matrix (ECM), specifically solubilizes a dermatan sulfate proteoglycan (DSPG) which accounts for more than 95% of the 35S-released material.	Heparin	36-43	acetylcholinesterase	Rattus norvegicus	74-78
3556575-3	1987	The co-solubilization of AChE and the proteoglycan opens up the possibility that both macromolecules could be involved in the formation of the soluble AChE complex observed after incubation of muscle homogenate with heparin.	Heparin	216-223	acetylcholinesterase	Rattus norvegicus	25-29
3556575-3	1987	The co-solubilization of AChE and the proteoglycan opens up the possibility that both macromolecules could be involved in the formation of the soluble AChE complex observed after incubation of muscle homogenate with heparin.	Heparin	216-223	acetylcholinesterase	Rattus norvegicus	151-155
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	50-57	serpin family C member 1	Homo sapiens	98-114
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	serpin family C member 1	Homo sapiens	98-114
8979119-7	1996	The binding molecule(s) have not yet been characterized, but TFPI is rapidly released by heparin and other negatively charged ions.	Heparin	89-96	tissue factor pathway inhibitor	Homo sapiens	61-65
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	serpin family C member 1	Homo sapiens	98-114
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	serpin family C member 1	Homo sapiens	98-114
8979119-11	1996	Moreover, in the presence of heparin, antithrombin and TFPI cooperate to inhibit activation of coagulation.	Heparin	29-36	tissue factor pathway inhibitor	Homo sapiens	55-59
3410869-6	1988	We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface.	Heparin	160-167	serpin family C member 1	Homo sapiens	98-114
3803739-4	1987	Heparin infusion was able to significantly preserve ATIII activity from glycemia-induced alterations.	Heparin	0-7	serpin family C member 1	Homo sapiens	52-57
2948956-7	1987	The calcium-dependent binding of [3H]heparan sulfate and [3H]dermatan sulfate to SAP was strongly inhibited by heparan sulfate, heparin, and dermatan sulfate.	Heparin	128-135	amyloid P component, serum	Homo sapiens	81-84
3374326-2	1988	Infusion of heparin into fed rats caused a rapid accumulation in plasma of two distinct lipase activities in approximately equal amounts: heparin releasable lipoprotein lipase (HR-LPL) and heparin releasable triglyceride lipase (HR-TGL).	Heparin	12-19	lipase G, endothelial type	Rattus norvegicus	88-94
3374326-2	1988	Infusion of heparin into fed rats caused a rapid accumulation in plasma of two distinct lipase activities in approximately equal amounts: heparin releasable lipoprotein lipase (HR-LPL) and heparin releasable triglyceride lipase (HR-TGL).	Heparin	12-19	lipase G, endothelial type	Rattus norvegicus	169-175
3374326-2	1988	Infusion of heparin into fed rats caused a rapid accumulation in plasma of two distinct lipase activities in approximately equal amounts: heparin releasable lipoprotein lipase (HR-LPL) and heparin releasable triglyceride lipase (HR-TGL).	Heparin	12-19	lipase G, endothelial type	Rattus norvegicus	169-175
3593208-11	1987	Thus treatment of granules with heparinase resulted in loss of their ability to bind LDL, and substances known to bind to heparin, such as Toluidine Blue, avidin, lipoprotein lipase, fibronectin and protamine, all effectively competed with LDL for binding to the granules.	Heparin	32-39	fibronectin 1	Rattus norvegicus	183-194
3377765-5	1988	The relative specific activities of the unbound heparin molecules were 0.06 with antithrombin and 0.76 with heparin cofactor II in comparison to unfractionated heparin (specific activity = 1.00).	Heparin	48-55	serpin family C member 1	Homo sapiens	81-93
8833886-1	1996	Recent studies have demonstrated a strong association between type II (immunologically mediated) heparin-induced thrombocytopenia/thrombosis (HITP) and antibodies reactive with complexes consisting of heparin and platelet factor 4 (PF4), a heparin-binding protein normally found in platelet-alpha granules.	Heparin	97-104	platelet factor 4	Homo sapiens	232-235
3414028-0	1988	[Blood antithrombin III levels after prolonged administration of heparin].	Heparin	65-72	serpin family C member 1	Homo sapiens	7-23
3790607-1	1987	This paper demonstrates that structural modification of the heparin-releasable salt-resistant lipase of rat liver (liver lipase) alters its relative capacity to hydrolyze phospholipid and triacylglycerol emulsions.	Heparin	60-67	lipase G, endothelial type	Rattus norvegicus	94-100
3790607-1	1987	This paper demonstrates that structural modification of the heparin-releasable salt-resistant lipase of rat liver (liver lipase) alters its relative capacity to hydrolyze phospholipid and triacylglycerol emulsions.	Heparin	60-67	lipase G, endothelial type	Rattus norvegicus	121-127
3790599-1	1987	Significant differences between saturation kinetic properties of heparin-stimulated reactions between thrombin and antithrombin III from human and bovine species were observed.	Heparin	65-72	serpin family C member 1	Homo sapiens	115-131
3790599-2	1987	In both systems, the apparent Km for antithrombin III was higher than the KD for antithrombin III-heparin interaction, monitored by intrinsic protein fluorescence change.	Heparin	98-105	serpin family C member 1	Homo sapiens	81-97
8833886-4	1996	Eleven of the 51 patients (22%) had antibodies reactive with heparin:PF4 when they were admitted for cardiac surgery; these antibodies were mainly of the immunoglobulin M (IgM) class and were apparently stimulated by exposure to UFH at cardiac catheterization.	Heparin	229-232	platelet factor 4	Homo sapiens	69-72
3360140-0	1988	Antithrombin Glasgow, 393 Arg to His: a P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity.	Heparin	80-87	serpin family C member 1	Homo sapiens	0-12
8833886-15	1996	We conclude that UFH is more immunogenic than has been thought and that patients exposed to this anticoagulant during open heart surgery are at high risk to form low titer (&lt;/= 1:200) antibodies reactive with heparin:PF4.	Heparin	17-20	platelet factor 4	Homo sapiens	220-223
3360140-3	1988	Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl.	Heparin	52-59	serpin family C member 1	Homo sapiens	0-12
3360140-9	1988	The findings suggest that heparin, on binding, interacts indirectly with the reactive centre region of antithrombin.	Heparin	26-33	serpin family C member 1	Homo sapiens	103-115
8902986-0	1996	A heparin cofactor II mutation (HCII Rimini) combined with factor V Leiden or type I protein C deficiency in two unrelated thrombophilic subjects.	Heparin	2-9	serpin family D member 1	Homo sapiens	32-36
3301469-2	1987	The latter is also known as antithrombin BM, because of its moderate binding affinity to heparin.	Heparin	89-96	serpin family C member 1	Homo sapiens	28-40
2455066-7	1988	A 31,000-dalton fibronectin fragment representing the heparin-binding domain elicited neurite elongation comparable to that promoted by the intact fibronectin molecule.	Heparin	54-61	fibronectin 1	Gallus gallus	16-27
8865534-10	1996	The concentration of TFPI was significantly increased following the incubation with thrombin and heparin, including low molecular weight heparin, in a dose- and time-dependent manner.	Heparin	137-144	tissue factor pathway inhibitor	Homo sapiens	21-25
2455066-7	1988	A 31,000-dalton fibronectin fragment representing the heparin-binding domain elicited neurite elongation comparable to that promoted by the intact fibronectin molecule.	Heparin	54-61	fibronectin 1	Gallus gallus	147-158
3114102-3	1987	Crossed immunoelectrophoresis of AT III on heparin-agarose was also carried out in plasma and serum.	Heparin	43-50	serpin family C member 1	Homo sapiens	33-39
3114102-7	1987	In all groups all serum AT III parameters were higher than in controls; crossed immunoelectrophoresis of AT III on heparin-agarose indicated that this finding was due to a lower formation of complexed AT III in serum.	Heparin	115-122	serpin family C member 1	Homo sapiens	105-111
8695787-0	1996	Presence of autoantibodies to interleukin-8 or neutrophil-activating peptide-2 in patients with heparin-associated thrombocytopenia.	Heparin	96-103	pro-platelet basic protein	Homo sapiens	47-78
3114102-7	1987	In all groups all serum AT III parameters were higher than in controls; crossed immunoelectrophoresis of AT III on heparin-agarose indicated that this finding was due to a lower formation of complexed AT III in serum.	Heparin	115-122	serpin family C member 1	Homo sapiens	105-111
3114102-8	1987	AT III heparin cofactor serum values were the same whatever the INR over a large range (9.3-1.5); the highest anti-Xa heparin cofactor serum levels were noted in the groups treated more intensely (groups 1 and 2).	Heparin	7-14	serpin family C member 1	Homo sapiens	0-6
3349091-5	1988	The identity of the lipase activity was demonstrated by specific inhibition with antisera to lipoprotein lipase, and to hepatic lipase, respectively, and by separation of the two lipase activities by chromatography on heparin-Sepharose.	Heparin	218-225	lipase G, endothelial type	Rattus norvegicus	20-26
8695787-5	1996	Five of these nine patients with anti-IL-8 or anti-NAP-2 developed thrombosis during heparin treatment, which is not statistically different from the patients with H-PF4 antibodies.	Heparin	85-92	pro-platelet basic protein	Homo sapiens	51-56
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	147-151
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	170-174
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	170-174
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	170-174
2969081-5	1988	In the presence of antithrombin III, thrombin action on adenylate cyclase was blocked by unfractionated and high molecular weight heparin at 0.1 microgram/ml.	Heparin	130-137	serpin family C member 1	Homo sapiens	19-35
2956468-5	1987	The glycosaminoglycan containing ectodomain of this PG binds with high affinity Type I, III and V collagen fibrils and the C-terminal heparin binding domain of fibronectin.	Heparin	134-141	fibronectin 1	Mus musculus	160-171
2837726-7	1987	In doses where the lipoprotein lipase activities released by the 2 heparins were similar, the hepatic lipase released with low molecular weight heparin was significantly higher than with standard heparin.	Heparin	67-75	lipoprotein lipase	Homo sapiens	19-37
2837726-7	1987	In doses where the lipoprotein lipase activities released by the 2 heparins were similar, the hepatic lipase released with low molecular weight heparin was significantly higher than with standard heparin.	Heparin	67-74	lipoprotein lipase	Homo sapiens	19-37
3559389-3	1986	LPL activation was achieved by the infusion of normal plasma containing apoC-II and HL was released by the injection of heparin.	Heparin	120-127	lipoprotein lipase	Homo sapiens	0-3
2969081-8	1988	The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III.	Heparin	23-31	serpin family C member 1	Homo sapiens	284-300
2969081-8	1988	The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III.	Heparin	237-245	serpin family C member 1	Homo sapiens	284-300
8874868-8	1996	In the pulmonary vein plasma levels of activated factor VII decreased following heparin administration (P &lt; 0.001) in the majority of patients which was coincidental to an increase (P &lt; 0.001) in tissue factor pathway inhibitor (TFPI).	Heparin	80-87	tissue factor pathway inhibitor	Homo sapiens	202-233
3602697-0	1986	[Antithrombin III levels in patients with acute thromboembolism during treatment with heparin].	Heparin	86-93	serpin family C member 1	Homo sapiens	1-17
8874868-8	1996	In the pulmonary vein plasma levels of activated factor VII decreased following heparin administration (P &lt; 0.001) in the majority of patients which was coincidental to an increase (P &lt; 0.001) in tissue factor pathway inhibitor (TFPI).	Heparin	80-87	tissue factor pathway inhibitor	Homo sapiens	235-239
3782075-0	1986	Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.	Heparin	36-43	serpin family C member 1	Homo sapiens	55-67
8691148-4	1996	Interaction of CD31Rg with CD31- T helper cell (Th) clones was divalent cation independent but could be blocked by heparin, thus indicating that the CD31 counterreceptor on T cells can be distinguished from the ligands identified on other cell types.	Heparin	115-122	platelet and endothelial cell adhesion molecule 1	Homo sapiens	15-19
3782075-0	1986	Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.	Heparin	36-43	serpin family C member 1	Homo sapiens	129-141
3782075-2	1986	Moreover, all high-affinity oligosaccharides and heparins enhanced, to a similar extent, the amount of free proteolytically modified antithrombin cleaved at the reactive bond by Factor Xa.	Heparin	49-57	serpin family C member 1	Homo sapiens	133-145
3782075-3	1986	In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme.	Heparin	37-44	serpin family C member 1	Homo sapiens	164-176
3782075-3	1986	In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme.	Heparin	37-44	serpin family C member 1	Homo sapiens	219-231
3782075-5	1986	In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin.	Heparin	109-117	serpin family C member 1	Homo sapiens	48-60
3782075-5	1986	In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin.	Heparin	109-116	serpin family C member 1	Homo sapiens	48-60
3782075-7	1986	These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units.	Heparin	95-102	serpin family C member 1	Homo sapiens	52-64
3782075-7	1986	These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units.	Heparin	95-102	serpin family C member 1	Homo sapiens	148-160
3363529-5	1988	Affinity adsorption of affected members" plasma to heparin-sepharose beads revealed one population of ATIII in the supernatant corresponding to the abnormal ATIII, devoid of heparin cofactor activity and showing a peak between pH range: 4.6-4.8 in CIEF.	Heparin	51-58	serpin family C member 1	Homo sapiens	102-107
3363529-5	1988	Affinity adsorption of affected members" plasma to heparin-sepharose beads revealed one population of ATIII in the supernatant corresponding to the abnormal ATIII, devoid of heparin cofactor activity and showing a peak between pH range: 4.6-4.8 in CIEF.	Heparin	174-181	serpin family C member 1	Homo sapiens	102-107
3363529-8	1988	This abnormal ATIII was characterized by a lack of affinity for heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	14-19
3338469-7	1988	At 37 degrees C, heparin-releasable binding of LDL and binding of Fab fragments were double that at 4 degrees C, whereas binding of antibody remained unchanged.	Heparin	17-24	FA complementation group B	Homo sapiens	66-69
3361696-5	1988	When low dose heparin was administered to patients with AF, plasma FPA levels were decreased to the near normal range, accompanied by an increase in heparin-AT III complex activity and heparin concentration 0.5-1.0 h after injection.	Heparin	14-21	serpin family C member 1	Homo sapiens	157-163
3361696-5	1988	When low dose heparin was administered to patients with AF, plasma FPA levels were decreased to the near normal range, accompanied by an increase in heparin-AT III complex activity and heparin concentration 0.5-1.0 h after injection.	Heparin	149-156	serpin family C member 1	Homo sapiens	157-163
3361696-5	1988	When low dose heparin was administered to patients with AF, plasma FPA levels were decreased to the near normal range, accompanied by an increase in heparin-AT III complex activity and heparin concentration 0.5-1.0 h after injection.	Heparin	149-156	serpin family C member 1	Homo sapiens	157-163
2430976-5	1986	Four of these were inhibitors, two of which also recognized a heparin-binding N-CAM fragment.	Heparin	62-69	neural cell adhesion molecule 1	Homo sapiens	78-83
2430978-15	1986	We have also shown that the B1A3 mAb recognizes not only chicken N-CAM but also rat and mouse N-CAM, indicating that the heparin-binding domain of N-CAM is evolutionarily conserved among different N-CAM forms.	Heparin	121-128	neural cell adhesion molecule 1	Gallus gallus	65-70
3771529-3	1986	PN-I preferentially binds thrombin, urokinase, trypsin, and plasmin, and its binding to thrombin is accelerated by heparin.	Heparin	115-122	serpin family E member 2	Homo sapiens	0-4
3790498-6	1986	The first-order rate constants of these reactions at 200 nM antithrombin III and normalized to heparin at 1 microgram/mL were 0.33 and 9.5 min-1 in the presence and absence of factor Va and phospholipid, respectively.	Heparin	95-102	serpin family C member 1	Homo sapiens	60-76
8691148-4	1996	Interaction of CD31Rg with CD31- T helper cell (Th) clones was divalent cation independent but could be blocked by heparin, thus indicating that the CD31 counterreceptor on T cells can be distinguished from the ligands identified on other cell types.	Heparin	115-122	platelet and endothelial cell adhesion molecule 1	Homo sapiens	27-31
3691497-2	1987	Three forms of heparin fractionated on the basis of their affinity for antithrombin III and unfractionated heparin were found to act as noncompetitive inhibitors of the formation of the thrombin-hirudin complex.	Heparin	15-22	serpin family C member 1	Homo sapiens	71-87
8691148-4	1996	Interaction of CD31Rg with CD31- T helper cell (Th) clones was divalent cation independent but could be blocked by heparin, thus indicating that the CD31 counterreceptor on T cells can be distinguished from the ligands identified on other cell types.	Heparin	115-122	platelet and endothelial cell adhesion molecule 1	Homo sapiens	27-31
2962279-6	1987	When BTG was again elevated, the dose of heparin was increased stepwise to 2 x 15,000 IU/d; in this way functional AT III levels remained in the range of 28-50%.	Heparin	41-48	serpin family C member 1	Homo sapiens	115-121
8663023-4	1996	Using heparin-Sepharose, we isolated two of the protein forms from immunoaffinity-purified selenoprotein P.	Heparin	6-13	selenoprotein P	Rattus norvegicus	91-106
2432885-7	1986	Fractions of standard heparin with high affinity for antithrombin III also had greater affinity for endothelium.	Heparin	22-29	serpin family C member 1	Homo sapiens	53-69
2432885-8	1986	However, these two properties of heparin (affinity for antithrombin III and affinity for endothelial cells) could be dissociated.	Heparin	33-40	serpin family C member 1	Homo sapiens	55-71
8640408-7	1996	We applied this new method to measure the amount of endothelial cell-associated TFPI, which can be released by heparin injection, as "free-form TFPI."	Heparin	111-118	tissue factor pathway inhibitor	Homo sapiens	80-84
3768351-0	1986	Chemically modified heparins as inhibitors of heparan sulfate specific endo-beta-glucuronidase (heparanase) of metastatic melanoma cells.	Heparin	20-28	glucuronidase, beta	Mus musculus	76-94
3689206-4	1987	This binding was displaced by heparin and was completely abolished by selective removal of heparan sulfate from cells with heparitinase, indicating that antithrombin III binds to heparan sulfate on the surface of endothelial cells.	Heparin	30-37	serpin family C member 1	Homo sapiens	153-169
3427019-0	1987	Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III.	Heparin	66-73	serpin family C member 1	Homo sapiens	107-123
8640408-7	1996	We applied this new method to measure the amount of endothelial cell-associated TFPI, which can be released by heparin injection, as "free-form TFPI."	Heparin	111-118	tissue factor pathway inhibitor	Homo sapiens	144-148
8662798-6	1996	Analysis of baculovirus-expressed HGF/NK1 revealed that this isoform possesses the heparin binding properties of HGF/SF and modest mitogenic and scattering activity relative to HGF/SF.	Heparin	83-90	hepatocyte growth factor	Homo sapiens	34-37
3309544-3	1987	Comparative studies were performed on tissue (brain, adipose, and heart) heparin releasable lipoprotein lipase in the fasted and diabetic (streptozotocin 100 mg/kg BW IP) rat.	Heparin	73-80	lipase G, endothelial type	Rattus norvegicus	104-110
3488664-5	1986	During thrombolytic infusion, concomitant heparin infusion was usually used to reduce the frequency of thrombus formation on the infusion catheter or recurrent thrombosis of the graft, once the tip of the infusion catheter was advanced distally.	Heparin	42-49	TOR signaling pathway regulator	Homo sapiens	194-197
3800942-1	1986	The effect of heparin fractions of various Mr, with high affinity for antithrombin III, on the kinetics of the reaction between factor Xa and antithrombin III have been studied using purified human proteins.	Heparin	14-21	serpin family C member 1	Homo sapiens	70-86
3800942-1	1986	The effect of heparin fractions of various Mr, with high affinity for antithrombin III, on the kinetics of the reaction between factor Xa and antithrombin III have been studied using purified human proteins.	Heparin	14-21	serpin family C member 1	Homo sapiens	142-158
8662798-6	1996	Analysis of baculovirus-expressed HGF/NK1 revealed that this isoform possesses the heparin binding properties of HGF/SF and modest mitogenic and scattering activity relative to HGF/SF.	Heparin	83-90	hepatocyte growth factor	Homo sapiens	113-119
3424283-5	1987	The AT III fraction with normal affinity to heparin displayed H-CIE and CIEF patterns identical to the control AT III.	Heparin	44-51	serpin family C member 1	Homo sapiens	4-10
8665956-7	1996	The bindings of Sg II to both iPr2P-PSA and PCI were influenced by pH, ionic strength, heparin, dextran sulfate, and divalent cations, particularly by Zn2+.	Heparin	87-94	serpin family A member 5	Homo sapiens	44-47
3653103-5	1987	Here we show that, besides dsRNA other polyanions, especially heparin, can also activate the p68 kinase for the autophosphorylation reaction.	Heparin	62-69	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	93-103
3800942-7	1986	These data suggest that the increased rates of inhibition observed with heparins of higher Mr may be due to an involvement of heparin binding to factor Xa as well as to antithrombin III.	Heparin	72-80	serpin family C member 1	Homo sapiens	169-185
3800942-7	1986	These data suggest that the increased rates of inhibition observed with heparins of higher Mr may be due to an involvement of heparin binding to factor Xa as well as to antithrombin III.	Heparin	72-79	serpin family C member 1	Homo sapiens	169-185
3653103-6	1987	Heparin activation of the p68 kinase is reversible since it can be prevented by addition of antithrombin III, heparin-binding protein.	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	26-36
3653103-6	1987	Heparin activation of the p68 kinase is reversible since it can be prevented by addition of antithrombin III, heparin-binding protein.	Heparin	0-7	serpin family C member 1	Homo sapiens	92-108
3653103-8	1987	The p68 kinase binds to heparin-Sepharose.	Heparin	24-31	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	4-14
3653103-9	1987	Further evidence that the p68 kinase can be activated by heparin was provided by photoaffinity labeling with 8-azido-[alpha-32P]ATP.	Heparin	57-64	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	26-36
3653103-10	1987	This ATP analog can bind to the p68 kinase only in the presence of heparin or dsRNA.	Heparin	67-74	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	32-42
3611110-7	1987	Heparin catalyzed the AT III inhibition of thrombin but not meizothrombin(des F1) formed during the prothrombin activation.	Heparin	0-7	serpin family C member 1	Homo sapiens	22-28
3611110-8	1987	Thrombin, generated by (Xa-Va-phospholipid-Ca2+) was inhibited by AT III/heparin more slowly than purified thrombin, and the saturation kinetics of the inhibition with respect to AT III differed from those found with purified thrombin.	Heparin	73-80	serpin family C member 1	Homo sapiens	66-72
3730427-0	1986	A comparison of the strength of binding of antithrombin III, protamine and poly(L-lysine) to heparin samples of different anticoagulant activities.	Heparin	93-100	serpin family C member 1	Homo sapiens	43-59
3730427-1	1986	The limiting concentrations, i.e., those concentrations of sodium chloride required to completely disrupt the complexes of heparin with antithrombin III, protamine and poly(L-lysine), were determined using fluorescence techniques, in order to compare the binding strengths of these complexes.	Heparin	123-130	serpin family C member 1	Homo sapiens	136-152
3730427-4	1986	In contrast, the limiting salt concentration values for complexes formed between antithrombin III and heparin did not change with either the degree of sulphation or the biological potency of the heparin samples.	Heparin	102-109	serpin family C member 1	Homo sapiens	81-97
3730427-5	1986	A low-potency heparin simply contained a smaller number of molecules which possessed the intact antithrombin III binding site (thus being fully "anticoagulant active") than a high-potency sample.	Heparin	14-21	serpin family C member 1	Homo sapiens	96-112
3730427-6	1986	Low-affinity heparin did not contain these binding sites and thus showed a low affinity for antithrombin III.	Heparin	13-20	serpin family C member 1	Homo sapiens	92-108
3730427-7	1986	High-potency heparin, being highly sulphated, possessed a higher affinity for protamine and poly(L-lysine) than for antithrombin III.	Heparin	13-20	serpin family C member 1	Homo sapiens	116-132
3730427-8	1986	However, after partial N-desulphation of heparin, the subsequent heparin-protamine complex was more weakly bound than a significant proportion of the corresponding heparin-antithrombin III complexes.	Heparin	41-48	serpin family C member 1	Homo sapiens	172-188
3750270-4	1986	SAP suppressed the anticoagulant activity of heparin in the TEG assay, unlike results obtained in heparinized cell free plasma, by facilitating a more rapid onset of coagulation, increasing the rate of fibrin formation/polymerization, and correcting clot patency.	Heparin	45-52	amyloid P component, serum	Homo sapiens	0-3
3618551-1	1987	Antithrombin-III assays are performed to assess response to heparin therapy and efficacy of antithrombin concentrate therapy and in diagnosing hereditary thrombophilia, deep venous thrombosis, pulmonary embolus, and disseminated intravascular coagulation.	Heparin	60-67	serpin family C member 1	Homo sapiens	0-16
8963717-5	1996	Adhesion to glass-coated vWF was partially inhibited by heparin and completely inhibited by prostaglandin I(2) and anti-glycoprotein (GP) Ib and anti-GPIIb-IIIa antibodies.	Heparin	56-63	von Willebrand factor	Cricetulus griseus	25-28
3663508-0	1987	An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy.	Heparin	47-54	serpin family C member 1	Homo sapiens	12-28
3663508-0	1987	An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy.	Heparin	47-54	serpin family C member 1	Homo sapiens	30-36
3663508-0	1987	An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy.	Heparin	47-54	serpin family C member 1	Homo sapiens	65-71
3663509-0	1987	Antithrombin III Glasgow: a variant with increased heparin affinity and reduced ability to inactivate thrombin, associated with familial thrombosis.	Heparin	51-58	serpin family C member 1	Homo sapiens	0-16
3747493-11	1986	In comparing FN levels, no significant differences were found between the groups except on the second day--the CLPS + heparin group had a significantly lower FN level on Day 2 than CLP +/- heparin.	Heparin	118-125	fibronectin 1	Rattus norvegicus	158-160
3087016-3	1986	Esterification also abolished the binding of heparin to antithrombin as measured by changes in the intrinsic fluorescence.	Heparin	45-52	serpin family C member 1	Homo sapiens	56-68
3663509-7	1987	AT III from the patient was reapplied to heparin-Sepharose and eluted with a NaCl gradient.	Heparin	41-48	serpin family C member 1	Homo sapiens	0-6
8796266-3	1996	Heparin stimulates most PCI/protease reactions, but interferes with the tissue kallikrein/PCI-interaction.	Heparin	0-7	serpin family A member 5	Homo sapiens	24-27
3663509-9	1987	It is concluded that this variant, designated AT III Glasgow, has increased affinity for heparin but reduced ability to inactivate thrombin.	Heparin	89-96	serpin family C member 1	Homo sapiens	46-52
3663595-10	1987	From the tentative assignment of one of these resonances to histidine-1, it is proposed that the heparin binding site of antithrombin III is located in the N-terminal region and that this region forms a separate domain from the rest of the protein.	Heparin	97-104	serpin family C member 1	Homo sapiens	121-137
3697371-1	1986	Fluorescence polarization has been used to study the interaction of thrombin and heparin, and the catalysis by heparin of the combination of thrombin and antithrombin.	Heparin	111-118	serpin family C member 1	Homo sapiens	154-166
3697371-8	1986	The complex formed between thrombin and heparin, to which antithrombin was attached, has a dissociation constant of 1-2 microM, again irrespective of the heparin molecular weight.	Heparin	40-47	serpin family C member 1	Homo sapiens	58-70
3697371-8	1986	The complex formed between thrombin and heparin, to which antithrombin was attached, has a dissociation constant of 1-2 microM, again irrespective of the heparin molecular weight.	Heparin	154-161	serpin family C member 1	Homo sapiens	58-70
3699029-0	1986	S protein modulates the heparin-catalyzed inhibition of thrombin by antithrombin III.	Heparin	24-31	serpin family C member 1	Homo sapiens	68-84
3699029-2	1986	The interference of S protein with the heparin-catalyzed inhibition of thrombin by antithrombin III was studied in a purified system and in plasma.	Heparin	39-46	serpin family C member 1	Homo sapiens	83-99
3699029-6	1986	While the association constant of thrombin--antithrombin III in the presence of 0.05 U/ml heparin amounted to 2.5 X 10(8) M-1, an approximately 200-fold decrease of this value was observed in the presence of S protein.	Heparin	90-97	serpin family C member 1	Homo sapiens	44-60
8796266-3	1996	Heparin stimulates most PCI/protease reactions, but interferes with the tissue kallikrein/PCI-interaction.	Heparin	0-7	serpin family A member 5	Homo sapiens	90-93
3699029-7	1986	The fast formation of the covalent complex between thrombin and antithrombin III in the presence of heparin was impaired as a result of the presence of S protein, as was shown by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate.	Heparin	100-107	serpin family C member 1	Homo sapiens	64-80
3010999-6	1986	Phosphorylation of phosvitin or synthase was inhibited by heparin (1/2 maximally by 0.5 microgram/ml without salt and 37 micrograms/ml with 150 mM NaCl).	Heparin	58-65	casein kinase 2 beta	Bos taurus	19-28
2956270-4	1987	PD 31 cells recognize a different domain of the fibronectin molecule, which is contained within the carboxy terminal segment possessing a high-affinity binding site for heparin.	Heparin	169-176	fibronectin 1	Mus musculus	48-59
3310396-4	1987	AT III became functionally active in presence of heparin, which operates as a catalyst and accelerates significantly the formation of inactive complexes between AT III and proteinases, which usually developed slowly in absence of the activator.	Heparin	49-56	serpin family C member 1	Homo sapiens	0-6
3310396-4	1987	AT III became functionally active in presence of heparin, which operates as a catalyst and accelerates significantly the formation of inactive complexes between AT III and proteinases, which usually developed slowly in absence of the activator.	Heparin	49-56	serpin family C member 1	Homo sapiens	161-167
8796266-4	1996	Thereby heparin not only regulates PCI-activity but also its specificity in systems containing two or more of its target proteases.	Heparin	8-15	serpin family A member 5	Homo sapiens	35-38
3584126-2	1987	Does cleavage by thrombin induce structural changes in the heparin-binding region of antithrombin?	Heparin	59-66	serpin family C member 1	Homo sapiens	85-97
3715788-4	1986	Crossed immunoelectrophoresis of AT III in the presence of heparin revealed in the plasma an abnormal slow-moving peak.	Heparin	59-66	serpin family C member 1	Homo sapiens	33-39
3715788-5	1986	When tested by affinity chromatography on heparin Sepharose, this abnormal AT III did not bind to heparin.	Heparin	42-49	serpin family C member 1	Homo sapiens	75-81
3584126-3	1987	Heparin has been shown to exhibit lower affinity for the antithrombin-thrombin complex than for antithrombin alone (Carlstrom, A.-S., Lieden, K., and Bjork, I.	Heparin	0-7	serpin family C member 1	Homo sapiens	57-69
3715788-8	1986	We therefore considered our patient as homozygous for an AT III molecular abnormality affecting the binding site for heparin.	Heparin	117-124	serpin family C member 1	Homo sapiens	57-63
8605586-10	1996	However, the fact that the dissociation constants of dextran sulfate and heparin are orders of magnitude larger compared with the NCAs indicates that the spatial structure of the proteins and/or hydrophobic interactions between the NCAs and the envelope protein may also be involved.	Heparin	73-80	endogenous retrovirus group K member 6, envelope	Homo sapiens	245-261
3949798-8	1986	218, 725-732), therefore requires interaction with saccharide sequences in addition to the antithrombin-binding pentasaccharide of heparin in order to efficiently express its antiheparin activity.	Heparin	131-138	serpin family C member 1	Homo sapiens	91-103
3949807-1	1986	The molecular interactions between components of the heparin-catalyzed antithrombin III/thrombin reaction were investigated by light scattering.	Heparin	53-60	serpin family C member 1	Homo sapiens	71-87
3949807-2	1986	When heparin was added to antithrombin III, the molecular weight increased to a maximum and then decreased to that of a 1:1 (antithrombin III X heparin) complex.	Heparin	5-12	serpin family C member 1	Homo sapiens	26-42
3949807-2	1986	When heparin was added to antithrombin III, the molecular weight increased to a maximum and then decreased to that of a 1:1 (antithrombin III X heparin) complex.	Heparin	5-12	serpin family C member 1	Homo sapiens	26-38
3949807-3	1986	The initial molecular weights at low heparin to antithrombin III ratios were consistent with the formation of a 2:1 (antithrombin III X heparin) complex in which only one antithrombin III molecule had undergone the conformational change measured by protein fluorescence enhancement.	Heparin	37-44	serpin family C member 1	Homo sapiens	117-133
3949807-8	1986	In the presence of stoichiometric amounts of heparin, the bovine proteins formed an initial complex of Mr = 230,000 (corresponding to a dimer of heparin-antithrombin III-thrombin) which underwent further aggregation.	Heparin	45-52	serpin family C member 1	Homo sapiens	153-165
3949807-9	1986	The human proteins, however, formed a 1:1 (antithrombin III X thrombin) initial complex in the presence of heparin, followed by aggregation.	Heparin	107-114	serpin family C member 1	Homo sapiens	43-55
3584126-7	1987	The hydroxy-nitrobenzyl (HNB) group attached to a unique tryptophan has been used in the present study as an extrinsic probe for localization of conformational changes to the heparin-binding region within antithrombin III using immunochemical and spectral techniques.	Heparin	175-182	serpin family C member 1	Homo sapiens	205-221
3584126-8	1987	Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol.	Heparin	103-110	serpin family C member 1	Homo sapiens	47-59
3584126-8	1987	Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol.	Heparin	171-178	serpin family C member 1	Homo sapiens	47-59
2955807-0	1987	Comparative effect of heparin and heparan sulphate on two abnormal antithrombin III type 3 variants.	Heparin	22-29	serpin family C member 1	Homo sapiens	67-83
2955807-4	1987	In an attempt to explain the thrombotic tendency observed in this abnormality we compared the effect of heparin and heparan sulphate on these abnormal AT III, since, unlike heparin, heparan sulphate is a naturally occurring anticoagulant in the human.	Heparin	104-111	serpin family C member 1	Homo sapiens	151-157
3949807-10	1986	These interactions of thrombin and antithrombin with heparin suggest complex interactions that could relate to heparin function.	Heparin	53-60	serpin family C member 1	Homo sapiens	35-47
3949807-10	1986	These interactions of thrombin and antithrombin with heparin suggest complex interactions that could relate to heparin function.	Heparin	111-118	serpin family C member 1	Homo sapiens	35-47
8735146-0	1996	Is heparin the ideal anticoagulant in patients with a high plasma leukocyte elastase level?	Heparin	3-10	elastase, neutrophil expressed	Homo sapiens	66-84
3955055-8	1986	When heparin was used in these assays, the rate of inhibition of thrombin by antithrombin was much more rapid and 62% of thrombin activity remained after 1 min.	Heparin	5-12	serpin family C member 1	Homo sapiens	77-89
3949769-0	1986	Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity-purified heparin.	Heparin	136-143	serpin family C member 1	Homo sapiens	14-30
3949769-1	1986	Heparin was fractionated by affinity chromatography on immobilized antithrombin III followed by gel filtration on Sephadex G-100.	Heparin	0-7	serpin family C member 1	Homo sapiens	67-83
3949769-3	1986	The binding stoichiometries of antithrombin III and thrombin interactions with the heparin of these fractions were measured, using changes in intrinsic and extrinsic fluorescence.	Heparin	83-90	serpin family C member 1	Homo sapiens	31-47
3949769-5	1986	As the molecular weight of heparin varied from about 10,000 to 30,000, the average number of antithrombin and thrombin sites/heparin molecule varied from 1.0 to 2.1 and 2.4 to 6.8.	Heparin	27-34	serpin family C member 1	Homo sapiens	93-105
3949769-8	1986	This can be explained by assuming that heparin functions as a template for both proteins, that all bound thrombin and antithrombin III molecules are accessible to each other, and that the rate at which a bound molecule reacts is proportional to the number of molecules of its interacting counterpart bound.	Heparin	39-46	serpin family C member 1	Homo sapiens	118-134
3949769-12	1986	259, 5670-5677), who demonstrated that the rate at which single molecules of antithrombin III, covalently attached to heparin, react increases as the thrombin binding capacity (chain length) of heparin increases.	Heparin	118-125	serpin family C member 1	Homo sapiens	77-93
3949769-12	1986	259, 5670-5677), who demonstrated that the rate at which single molecules of antithrombin III, covalently attached to heparin, react increases as the thrombin binding capacity (chain length) of heparin increases.	Heparin	194-201	serpin family C member 1	Homo sapiens	77-93
3629543-3	1987	In comparison with heparin, the administration of LMWH resulted in a significantly higher antiFXa activity (p less than 0.001) but a lower release of LPL and HL (p less than 0.001), which did not increase plasma FFA.	Heparin	50-54	lipoprotein lipase	Homo sapiens	150-153
3034924-6	1987	At 4 degrees C binding of PN-I:protease complexes was competed by heparin.	Heparin	66-73	serpin family E member 2	Homo sapiens	26-30
3603409-2	1987	The unusual circumstances of apparition, the age and the increased heparin requirements suggested an antithrombin III (AT III) deficiency.	Heparin	67-74	serpin family C member 1	Homo sapiens	101-117
3603409-6	1987	Affinity chromatography on heparin-Sepharose revealed two populations of AT III, one of which was devoid of heparin cofactor activity.	Heparin	27-34	serpin family C member 1	Homo sapiens	73-79
3603409-7	1987	The toponym AT III Geneva is proposed for this new familial abnormal AT III with defective heparin cofactor activity.	Heparin	91-98	serpin family C member 1	Homo sapiens	12-18
3603409-7	1987	The toponym AT III Geneva is proposed for this new familial abnormal AT III with defective heparin cofactor activity.	Heparin	91-98	serpin family C member 1	Homo sapiens	69-75
3510669-1	1986	Rat hearts were perfused with heparin for 2 min at 4 degrees C. The lipoprotein lipase activity in the perfusate was inhibited by antiserum to rat adipose tissue lipoprotein lipase.	Heparin	30-37	lipase G, endothelial type	Rattus norvegicus	80-86
8613703-11	1996	Competition experiments showed that serglycin was as efficient as heparin sulfate in blocking the binding of [3H] chondrotin sulfate to PF4, whereas heparin was one order of magnitude more efficient.	Heparin	66-73	platelet factor 4	Homo sapiens	136-139
3300414-3	1987	The first step alone, heparin-agarose chromatography, is sufficient to purify the enzyme from yeast bearing a cloned copy of the ADE3 gene that overexpresses the protein.	Heparin	22-29	trifunctional formate-tetrahydrofolate ligase/methenyltetrahydrofolate cyclohydrolase/methylenetetrahydrofolate dehydrogenase ADE3	Saccharomyces cerevisiae S288C	129-133
8613703-12	1996	Affinity measurements using fluoresceinamine-labeled glycosaminoglycans showed that the affinity of heparin for PF4 is on the order of 30 nM, whereas chondroitin sulfate has an affinity of 260 nM.	Heparin	100-107	platelet factor 4	Homo sapiens	112-115
3943548-3	1986	Adhesion to poly-L-lysine, fibronectin- and laminin-coated dishes was significantly inhibited by added dextran sulfate and to a lesser extent heparin--but not by chondroitin sulfate.	Heparin	142-149	fibronectin 1	Rattus norvegicus	27-38
8656041-3	1996	We found that binding of iodine 125-labeled PF4 to HEL cells was inhibited by heparin, heparan sulfate, and dermatan sulfate and to a smaller extent by chondroitin sulfate.	Heparin	78-85	platelet factor 4	Homo sapiens	44-47
3943548-8	1986	On fibronectin and poly-L-lysine-coated dishes this neurite growth is inhibited by added heparin and dextran sulfate, while on laminin it is not.	Heparin	89-96	fibronectin 1	Rattus norvegicus	3-14
2418031-5	1986	We have identified a monoclonal antibody, designated B1A3, that inhibits heparin binding to N-CAM and cell-to-substratum adhesion.	Heparin	73-80	neural cell adhesion molecule 1	Gallus gallus	92-97
2418031-6	1986	A 25,000-mol-wt heparin (heparan sulfate)-binding domain of N-CAM has been identified by limited proteolysis, and this fragment promotes cell attachment when bound to glass surfaces.	Heparin	16-23	neural cell adhesion molecule 1	Gallus gallus	60-65
3606566-1	1987	S protein, a plasma glycoprotein with Mr 78,000, has been shown to interfere with the heparin-catalysed inhibition of thrombin by antithrombin III.	Heparin	86-93	serpin family C member 1	Homo sapiens	130-146
3590108-7	1987	Furthermore, insoluble sulfonated polystyrenes grafted with different amino acid were shown to possess an heparin-like behaviour and catalyse the generation of thrombin-AT III complex.	Heparin	106-113	serpin family C member 1	Homo sapiens	169-175
2437972-2	1987	Sephadex derivatives bearing carboxymethyl, sulphonated benzylamine and amino acid groups exhibit heparin-like behaviour as demonstrated by the kinetic study of the thrombin inactivation in the presence of antithrombin III.	Heparin	98-105	serpin family C member 1	Homo sapiens	206-222
2418031-8	1986	These data are the first evidence that N-CAM is a multifunctional protein that contains both cell-and heparin (heparan sulfate)-binding domains.	Heparin	102-109	neural cell adhesion molecule 1	Gallus gallus	39-44
8656041-4	1996	Ninety percent of 125I-labeled PF4 bound to HEL cells was released by cells after exposure to heparin and heparan sulfate.	Heparin	94-101	platelet factor 4	Homo sapiens	31-34
8901022-6	1996	An IP3 receptor antagonist, heparin, reduced both the substance P-induced O2- production and the transient increase in [Ca2+]i without any significant effects on the sustained increase in [Ca2+]i.	Heparin	28-35	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	3-15
3814109-1	1986	Heparin and synthetic inhibitors of thrombin are able to decrease the rate of division of porcine vascular smooth muscle cells in primary culture and to increase their myosin content.	Heparin	0-7	myosin heavy chain 14	Homo sapiens	168-174
3597343-1	1987	It was found that phospholipase A2 and lysophospholipase, both of which were released from thrombin-stimulated rat platelets, had high affinity to insolubilized heparin.	Heparin	161-168	phospholipase A2 group IB	Rattus norvegicus	18-56
3597343-2	1987	Phospholipase A2 released from rat platelets was purified by the sequential use of column chromatography on heparin-Sepharose and TSK gel G2000SW (high-performance liquid chromatography, HPLC).	Heparin	108-115	phospholipase A2 group IB	Rattus norvegicus	0-16
8868511-18	1996	These results suggest that mobilisable pool of platelet factor 4 in young survivors of myocardial infarction derives from the "nonplatelet pool" and that reduction of heparin- or Fraxiparine-releasable pool of PF4 may reflect an impaired endothelium function, probably due to atherosclerosis.	Heparin	167-174	platelet factor 4	Homo sapiens	210-213
8868518-7	1996	One hundred eighty minutes after initiation of dialysis, by which time all patients were receiving heparin there was a further increase in TFPI (to more than 200% of baseline), due to the presence of the glycosaminoglycan.	Heparin	99-106	tissue factor pathway inhibitor	Homo sapiens	139-143
3812352-1	1987	Neutralization by protamine of the heparin activation of antithrombin III in plasma, in vitro, represents an equilibrium reaction in which by mass action heparin remains complexed only in the presence of an excess of protamine.	Heparin	35-42	serpin family C member 1	Homo sapiens	57-73
3812352-1	1987	Neutralization by protamine of the heparin activation of antithrombin III in plasma, in vitro, represents an equilibrium reaction in which by mass action heparin remains complexed only in the presence of an excess of protamine.	Heparin	154-161	serpin family C member 1	Homo sapiens	57-73
3812352-2	1987	Loss of this excess through enzymatic breakdown of the free protamine leads to instability of the complexes with liberation of the heparin, reestablishing antithrombin activity.	Heparin	131-138	serpin family C member 1	Homo sapiens	155-167
3812352-3	1987	This "heparin rebound" can also be produced by an increase in heparin levels or increased amounts of antithrombin III.	Heparin	6-13	serpin family C member 1	Homo sapiens	101-117
3812352-5	1987	A larger excess of protamine does not itself act as an anticoagulant but produces large heparin-protamine complexes that can still activate antithrombin III.	Heparin	88-95	serpin family C member 1	Homo sapiens	140-156
3620582-3	1987	The anticoagulant action of heparin is mainly antithrombin III (AT III) dependent and the binding site of AT III on the heparin molecule has been recently identified.	Heparin	28-35	serpin family C member 1	Homo sapiens	46-62
3620582-3	1987	The anticoagulant action of heparin is mainly antithrombin III (AT III) dependent and the binding site of AT III on the heparin molecule has been recently identified.	Heparin	28-35	serpin family C member 1	Homo sapiens	64-70
3620582-3	1987	The anticoagulant action of heparin is mainly antithrombin III (AT III) dependent and the binding site of AT III on the heparin molecule has been recently identified.	Heparin	28-35	serpin family C member 1	Homo sapiens	106-112
20493103-1	1986	This study describes the specificity, time-course and characteristics of the solubilization of class I-A forms of AChE by heparin, from the endplate regions of rat diaphragm muscle.	Heparin	122-129	acetylcholinesterase	Rattus norvegicus	114-118
20493103-2	1986	Heparin fractions which differed in size charge, anticoagulant activity and capacity to bind type I collagen, were probed in their ability to extract AChE.	Heparin	0-7	acetylcholinesterase	Rattus norvegicus	150-154
20493103-6	1986	The existence of a heparin-binding domain in class I- and class II-A forms of AChE, opens the possibility, that heparan sulfate proteoglycans could be involved in the anchorage of both types of esterase to synaptic regions.	Heparin	19-26	acetylcholinesterase	Rattus norvegicus	78-82
3517772-2	1986	It is by potentiating antithrombin III (AT III) a natural inhibitor of coagulation, that heparin exerts its anticoagulant effect.	Heparin	89-96	serpin family C member 1	Homo sapiens	22-38
3517772-2	1986	It is by potentiating antithrombin III (AT III) a natural inhibitor of coagulation, that heparin exerts its anticoagulant effect.	Heparin	89-96	serpin family C member 1	Homo sapiens	40-46
3517772-3	1986	Actually, it has been demonstrated that only 30% of the molecule in commercial heparin preparations are capable of binding to AT III: moreover, several procedures were used to prepare low molecular weight heparin fractions or fragments.	Heparin	79-86	serpin family C member 1	Homo sapiens	126-132
8868518-8	1996	This was due the previously reported displacement by heparin of the major intravascular pool of TFPI, from endothelial cell surfaces.	Heparin	53-60	tissue factor pathway inhibitor	Homo sapiens	96-100
8616093-0	1996	Pathogenicity of IgA and/or IgM antibodies to heparin-PF4 complexes in patients with heparin-induced thrombocytopenia.	Heparin	46-53	platelet factor 4	Homo sapiens	54-57
4096360-11	1985	The determined stability of AT III in autologous plasma--without AT III prophylaxis of thrombosis by Heparin is ineffective--and all other clotting factors leads to an expectancy of a not activated clotting mechanism and at the same time to low thrombosis risks.	Heparin	101-108	serpin family C member 1	Homo sapiens	28-34
2416361-7	1985	AT III is a weak inhibitor of polymerization, but its effect is magnified in the presence of PAPP-A or heparin.	Heparin	103-110	serpin family C member 1	Homo sapiens	0-6
3794520-1	1987	To test the hypothesis that binding to an endogenous heparin-like substance controls breakdown of antithrombin III (ATIII) in vivo, the metabolic behavior of a commercial ATIII concentrate was investigated in three normal volunteers and five subjects with hereditary ATIII deficiency.	Heparin	53-60	serpin family C member 1	Homo sapiens	98-114
3794520-1	1987	To test the hypothesis that binding to an endogenous heparin-like substance controls breakdown of antithrombin III (ATIII) in vivo, the metabolic behavior of a commercial ATIII concentrate was investigated in three normal volunteers and five subjects with hereditary ATIII deficiency.	Heparin	53-60	serpin family C member 1	Homo sapiens	116-121
3794520-7	1987	Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction.	Heparin	113-120	serpin family C member 1	Homo sapiens	24-29
3794520-7	1987	Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction.	Heparin	202-209	serpin family C member 1	Homo sapiens	24-29
3794520-7	1987	Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction.	Heparin	202-209	serpin family C member 1	Homo sapiens	86-91
3794520-7	1987	Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction.	Heparin	202-209	serpin family C member 1	Homo sapiens	86-91
8616093-1	1996	Antibodies to heparin-PF4 (H-PF4) complexes have been tested and isotyped in 38 patients who developed severe heparin-induced thrombocytopenia (type II HIT).	Heparin	14-21	platelet factor 4	Homo sapiens	22-25
4071470-4	1985	The reactivity of ATIII with heparin or, thrombin was investigated using this technique.	Heparin	29-36	serpin family C member 1	Homo sapiens	18-23
8616093-1	1996	Antibodies to heparin-PF4 (H-PF4) complexes have been tested and isotyped in 38 patients who developed severe heparin-induced thrombocytopenia (type II HIT).	Heparin	14-21	platelet factor 4	Homo sapiens	29-32
8641009-13	1996	CONCLUSIONS: Thrombin inhibition with heparin or r-hirudin significantly accelerated thrombolysis of occlusive platelet-rich thrombosis, but only the best antithrombotic therapy (r-hirudin) eliminated or nearly eliminated residual thrombus.	Heparin	38-45	coagulation factor II, thrombin	Sus scrofa	13-21
3901791-7	1985	Heparin achieves its prophylactic benefit by activating antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	56-72
3901791-9	1985	It has been shown that 1 micrograms of antithrombin III inhibits the formation of 1 unit of thrombin; however, in the presence of heparin, 1 micrograms of activated antithrombin III inhibits 750 units of thrombin.	Heparin	130-137	serpin family C member 1	Homo sapiens	165-181
3433205-4	1987	In 72-96 h of treatment intravenous heparin administration resulted in a decrease in a level of blood antithrombin III causing a decrease in the efficacy of heparin therapy.	Heparin	36-43	serpin family C member 1	Homo sapiens	102-118
3433205-4	1987	In 72-96 h of treatment intravenous heparin administration resulted in a decrease in a level of blood antithrombin III causing a decrease in the efficacy of heparin therapy.	Heparin	157-164	serpin family C member 1	Homo sapiens	102-118
2436331-2	1986	Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively.	Heparin	0-7	serpin family C member 1	Homo sapiens	81-87
2436331-11	1986	This suggest that clinical conditions associated with heparin treatment may be important for the effect of heparin on AT III metabolism previously reported in patients.	Heparin	54-61	serpin family C member 1	Homo sapiens	118-124
2436331-11	1986	This suggest that clinical conditions associated with heparin treatment may be important for the effect of heparin on AT III metabolism previously reported in patients.	Heparin	107-114	serpin family C member 1	Homo sapiens	118-124
3563966-1	1986	Four members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and half-normal antithrombin activity with or without heparin.	Heparin	223-230	serpin family C member 1	Homo sapiens	109-125
3563966-1	1986	Four members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and half-normal antithrombin activity with or without heparin.	Heparin	223-230	serpin family C member 1	Homo sapiens	109-121
3563966-4	1986	A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography.	Heparin	42-49	serpin family C member 1	Homo sapiens	21-37
3563966-4	1986	A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography.	Heparin	68-75	serpin family C member 1	Homo sapiens	21-37
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Heparin	32-39	serpin family C member 1	Homo sapiens	141-147
2432917-6	1986	Pentosan polysulphate, high molecular weight dextran sulphate, heparin with low affinity for AT III and a sulphated heparin derivative had weaker anticoagulant activities in normal plasma than standard heparin.	Heparin	63-70	serpin family C member 1	Homo sapiens	93-99
3840916-2	1985	HC II was functionally determined by thrombin inhibition in the presence of heparin in AT III-free plasma prepared by immunoadsorption on anti-AT III-Sepharose 4B column.	Heparin	76-83	serpin family C member 1	Homo sapiens	87-93
4082851-1	1985	Hypercoagulation caused by decreased antithrombin III level leads to thrombosis inspite of postoperative prophylactic heparin therapy.	Heparin	118-125	serpin family C member 1	Homo sapiens	37-53
4082851-5	1985	One should always suspect an ATIII deficiency when in spite of full heparin dosage a prolonged plasma thrombin time is not attained.	Heparin	68-75	serpin family C member 1	Homo sapiens	29-34
4014455-7	1985	The regression of LPL activity in plasma after a 60-min heparin infusion on adipose tissue LPL yielded higher correlation coefficients for activities recorded after elution at 4 and 37 degrees C (r = 0.725 and 0.754, respectively) than for detergent extraction (r = 0.607).	Heparin	56-63	lipoprotein lipase	Homo sapiens	18-21
4014455-7	1985	The regression of LPL activity in plasma after a 60-min heparin infusion on adipose tissue LPL yielded higher correlation coefficients for activities recorded after elution at 4 and 37 degrees C (r = 0.725 and 0.754, respectively) than for detergent extraction (r = 0.607).	Heparin	56-63	lipoprotein lipase	Homo sapiens	91-94
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Heparin	146-153	serpin family D member 1	Homo sapiens	0-19
4003344-2	1985	In an antithrombin-III (AT-III) deficient patient suffering from recurrent episodes of venous and arterial thrombosis requiring major surgery an attempt was made to institute antithrombotic protection by long-term stanozolol treatment supplemented during periods of thrombogenic exposure with subcutaneous heparin and, when needed, infusion of AT-III as plasma or concentrate.	Heparin	306-313	serpin family C member 1	Homo sapiens	24-30
3771538-7	1986	These studies suggest the occurrence of contiguous binding sites on heparin for Xa, antithrombin III, and heparin cofactor II.	Heparin	68-75	serpin family C member 1	Homo sapiens	84-100
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Heparin	146-153	serpin family D member 1	Homo sapiens	21-25
8739284-3	1996	Serum levels of Lp were significantly correlated with serum levels of lipoprotein lipase (LPL), hepatic triglyceride lipase (H-TGL) and nonesterified fatty acid (NEFA) 20 min after the administration of heparin during maintenance hemodialysis.	Heparin	203-210	lipase C, hepatic type	Homo sapiens	96-123
3773728-1	1986	We sought to determine the optimal dose of heparin for evaluating the activities of lipoprotein lipase (LPLA) and hepatic triglyceride hydrolase (HTGLA) in postheparin plasma.	Heparin	43-50	lipoprotein lipase	Homo sapiens	84-102
3773728-1	1986	We sought to determine the optimal dose of heparin for evaluating the activities of lipoprotein lipase (LPLA) and hepatic triglyceride hydrolase (HTGLA) in postheparin plasma.	Heparin	43-50	lipoprotein lipase	Homo sapiens	104-108
3773728-4	1986	The greatest LPLA was obtained after a heparin dose of 75 IU/kg, but LPLA after the three highest doses were not significantly different.	Heparin	39-46	lipoprotein lipase	Homo sapiens	13-17
3773728-8	1986	We also examined the effect of repeated daily injections of 75 IU/kg heparin on LPLA, HTGLA, and serum lipids.	Heparin	69-76	lipoprotein lipase	Homo sapiens	80-84
3995171-4	1985	More factor IXa was inhibited by antithrombin III in the presence of heparin than in its absence, but factor IXa levels sufficient for factor X activation appeared to be present in the heparinized plasma.	Heparin	69-76	serpin family C member 1	Homo sapiens	33-49
8554336-2	1996	Separate experiments were carried out in which plasma from rats administered 75Se and immunoaffinity-purified 75Se-labeled selenoprotein P were applied to a heparin-Sepharose column at pH 7.	Heparin	157-164	selenoprotein P	Rattus norvegicus	123-138
4024538-2	1985	Rabbit albumin enhanced the effect of heparin on the LPL activity, while heterologous protein, to the contrary, diminished it.	Heparin	38-45	lipoprotein lipase	Oryctolagus cuniculus	53-56
3095665-0	1986	Interactions of N-CAM with heparin-like molecules.	Heparin	27-34	neural cell adhesion molecule 1	Homo sapiens	16-21
9112630-5	1996	The interaction of TFPI with heparin has been demonstrated.	Heparin	29-36	tissue factor pathway inhibitor	Homo sapiens	19-23
3780071-8	1986	We suggest that the fibrinopeptide A is produced intraperitoneally and the antithrombin III-concentration in dialysate is sufficient to inhibit the fibrin formation after acceleration by heparin.	Heparin	187-194	serpin family C member 1	Homo sapiens	75-91
4037242-4	1985	These findings suggest that the administration of AT-III concentrates may significantly enhance the therapeutic efficacy of heparin, and that the use of AT-III concentrates with heparin is a safe and effective regimen for the treatment of childhood DIC.	Heparin	178-185	serpin family C member 1	Homo sapiens	153-159
3988937-0	1985	Antithrombotic properties in rabbits of heparin and heparin fragments covalently coupled to human antithrombin III.	Heparin	40-47	serpin family C member 1	Homo sapiens	98-114
3988937-0	1985	Antithrombotic properties in rabbits of heparin and heparin fragments covalently coupled to human antithrombin III.	Heparin	52-59	serpin family C member 1	Homo sapiens	98-114
3988937-1	1985	Clinical grade heparin is a very heterogeneous mucopolysaccharide, containing molecules with Mr ranging from 6,000 to 30,000 that have either a high affinity or a low affinity for antithrombin III (AT).	Heparin	15-22	serpin family C member 1	Homo sapiens	180-196
4035368-1	1985	We have synthesized the pentasaccharide representing the binding site of heparin to AT III.	Heparin	73-80	serpin family C member 1	Homo sapiens	84-90
3970943-6	1985	In these circumstances the lipoprotein lipase-apolipoprotein C-II interaction is much tighter (Kd = (7-10) X 10(-9) M) and is insensitive to salt and heparin.	Heparin	150-157	lipoprotein lipase	Homo sapiens	27-45
2428602-6	1986	In contrast, chorioallantoic membranes treated with combinations of angiostatic steroid and heparin exhibited capillary BM fragmentation and eventually complete loss of fibronectin and laminin from regions of capillary involution.	Heparin	92-99	fibronectin 1	Gallus gallus	169-180
3764810-0	1986	The effect of operation and subcutaneous heparin on plasma levels of antithrombin-III.	Heparin	41-48	serpin family C member 1	Homo sapiens	69-85
3764810-8	1986	These findings support the hypothesis that AT-III is consumed during coagulation and its utilization is increased in the presence of heparin.	Heparin	133-140	serpin family C member 1	Homo sapiens	43-49
3988155-2	1985	The antithrombotic effect of heparin is closely related to the presence of Antithrombin III (AT III) as cofactor.	Heparin	29-36	serpin family C member 1	Homo sapiens	75-91
9112630-6	1996	The heparin binding site of TFPI (HBS-1) locates in its C-terminal basic portion.	Heparin	4-11	tissue factor pathway inhibitor	Homo sapiens	28-32
3988155-2	1985	The antithrombotic effect of heparin is closely related to the presence of Antithrombin III (AT III) as cofactor.	Heparin	29-36	serpin family C member 1	Homo sapiens	93-99
3988155-9	1985	This decrease of AT III can be avoided by application of the AT III factor in an active form during the procedure (AT III in solution with heparin).	Heparin	139-146	serpin family C member 1	Homo sapiens	17-23
9112630-7	1996	We found another heparin-binding site in K3 domain of TFPI, using each of the three Kunitz domains prepared by the limited cleavage of TFPI and also synthetic peptides mimicking the amino acid sequence of a Kunitz domain.	Heparin	17-24	tissue factor pathway inhibitor	Homo sapiens	54-58
3988155-9	1985	This decrease of AT III can be avoided by application of the AT III factor in an active form during the procedure (AT III in solution with heparin).	Heparin	139-146	serpin family C member 1	Homo sapiens	61-67
3988155-9	1985	This decrease of AT III can be avoided by application of the AT III factor in an active form during the procedure (AT III in solution with heparin).	Heparin	139-146	serpin family C member 1	Homo sapiens	61-67
3743657-2	1986	Only 15% of the biologic activity of the complex carbohydrates derived from human skin fibroblasts was expressed when the heparin-binding domain an antithrombin was chemically modified at the Trp 49 residue.	Heparin	122-129	serpin family C member 1	Homo sapiens	148-160
9112630-7	1996	We found another heparin-binding site in K3 domain of TFPI, using each of the three Kunitz domains prepared by the limited cleavage of TFPI and also synthetic peptides mimicking the amino acid sequence of a Kunitz domain.	Heparin	17-24	tissue factor pathway inhibitor	Homo sapiens	135-139
3973025-6	1985	When lipolysis of VLDL was enhanced in these subjects upon release of lipoprotein lipase by intravenous heparin, a shift of the apo E from VLDL into fractions II and III was observed.	Heparin	104-111	lipoprotein lipase	Homo sapiens	70-88
9112630-8	1996	These heparin binding sites of TFPI will play an important role for the association with endothelial cells, interacting with heparin sulphate on the surface.	Heparin	6-13	tissue factor pathway inhibitor	Homo sapiens	31-35
3973025-11	1985	When both lipoprotein lipase and hepatic triglyceride lipase were released by intravenous heparin injection into normal subjects (n = 3), fraction I declined and the apo E content of fraction III increased by an equivalent amount.	Heparin	90-97	lipoprotein lipase	Homo sapiens	10-28
9112638-1	1996	Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation.	Heparin	114-121	serpin family D member 1	Homo sapiens	0-19
3541907-4	1986	In the presence of heparin, cell-surface immunodetectable lipoprotein lipase increased by up to 20%, whereas in the presence of cycloheximide they decreased by up to 60%.	Heparin	19-26	lipoprotein lipase	Homo sapiens	58-76
9112638-1	1996	Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation.	Heparin	114-121	serpin family D member 1	Homo sapiens	21-26
3973461-5	1985	Heparin-like catalytic activity of these materials (assayed by measuring the generation of thrombin-antithrombin complex in plasma) correlated well with the amount of heparin bound, but not as well with AT binding capacity.	Heparin	0-7	serpin family C member 1	Homo sapiens	100-112
3973671-5	1985	Fibronectin fragments with differing biological activities were produced by proteolytic digestion with trypsin and cathepsin D and sequential affinity chromatography on gelatin-agarose and heparin-Sepharose.	Heparin	189-196	fibronectin 1	Gallus gallus	0-11
7494002-3	1995	Heparan sulfate (HS)-conjugated gel also bound HGF, and the binding was competitively inhibited by heparin and bovine liver HS, but not by Engelbreth-Holm-Swarm sarcoma HS, pig aorta HS, or other glycosaminoglycans, suggesting the specific structural domain in HS for the binding of HGF.	Heparin	99-106	hepatocyte growth factor	Sus scrofa	283-286
2579452-1	1985	Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway.	Heparin	28-35	serpin family C member 1	Homo sapiens	63-79
3720853-0	1986	Substratum contacts and cytoskeletal reorganization of BALB/c 3T3 cells on a cell-binding fragment and heparin-binding fragments of plasma fibronectin.	Heparin	103-110	fibronectin 1	Mus musculus	139-150
2579452-1	1985	Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway.	Heparin	28-35	serpin family C member 1	Homo sapiens	81-87
8536714-7	1995	In vitro studies showed that the tKK:PCI complex formation in semen was accomplished in about 1 h and that heparin stimulated both the rate and the extent of complexation of tKK with PCI.	Heparin	107-114	serpin family A member 5	Homo sapiens	183-186
3966799-1	1985	The therapeutic anticoagulant action of heparin is mediated by the ability of a multifunctional octadecasaccharide region of the molecule to bind to and differentially alter the conformational integrity of antithrombin, and the sugar sequence of the primary binding domain is known.	Heparin	40-47	serpin family C member 1	Homo sapiens	206-218
4026390-5	1985	Whereas catalytic amounts of heparin accelerate greatly the inhibitory effect of ATIII, no accelerating effect of heparin on PP5 could be observed under the same conditions.	Heparin	29-36	serpin family C member 1	Homo sapiens	81-86
3754869-9	1986	The protective effect of S-protein on inactivation of thrombin by ATIII was demonstrated in functional assays with purified proteins and in plasma only in the presence of low concentrations of heparin.	Heparin	193-200	serpin family C member 1	Homo sapiens	66-71
3754869-10	1986	Thus, S-protein may mediate its effect by scavenging heparin required for ATIII activation.	Heparin	53-60	serpin family C member 1	Homo sapiens	74-79
3771670-3	1986	Preventive treatment applied involves low-dose heparin (1.5 mg/kg/d) to maintain an antithrombin III concentration of at least 65%.	Heparin	47-54	serpin family C member 1	Homo sapiens	84-100
3697371-9	1986	In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin.	Heparin	7-14	serpin family C member 1	Homo sapiens	34-46
3697371-9	1986	In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin.	Heparin	84-91	serpin family C member 1	Homo sapiens	34-46
3697371-10	1986	A possible explanation is that thrombin, after initial binding to the heparin, moves rapidly to the site where it combines with antithrombin.	Heparin	70-77	serpin family C member 1	Homo sapiens	128-140
3486013-0	1986	Interaction of factor XIa and antithrombin in the presence and absence of heparin.	Heparin	74-81	serpin family C member 1	Homo sapiens	30-42
2581861-3	1985	Now some conditions (AT III Trento, for example) are known to show an abnormal pattern only in the absence of heparin.	Heparin	110-117	serpin family C member 1	Homo sapiens	21-27
2581861-6	1985	Therefore, the test should be carried out as a screening procedure both in plasma and serum and in the presence or absence of heparin in every case of suspected AT III abnormality.	Heparin	126-133	serpin family C member 1	Homo sapiens	161-167
4008141-0	1985	Inhibition of human and guinea pig complement by heparin fractions differing in affinity for antithrombin III or in average molecular weight.	Heparin	49-56	antithrombin-III	Cavia porcellus	93-109
4008141-3	1985	In this study heparin fractions prepared by affinity chromatography on immobilized AT III and by gel filtration chromatography were compared for their ability to inhibit complement mediated haemolysis and both classical and alternative pathway C3 activation as measured by crossed immunoelectrophoresis.	Heparin	14-21	serpin family C member 1	Homo sapiens	83-89
8750779-1	1995	The human hepatoblastoma cell line Hep G2 releases the enzyme hepatic lipase during incubation with heparin.	Heparin	100-107	lipase C, hepatic type	Homo sapiens	62-76
3880772-5	1985	LPL was measured as activity secreted into the culture medium (CM), released from cells by heparin (HR), and extracted from cell digests.	Heparin	91-98	lipoprotein lipase	Homo sapiens	0-3
3880772-6	1985	A broad range of heparin concentrations produced a prompt release of LPL from a rapidly replenishable pool of cellular activity.	Heparin	17-24	lipoprotein lipase	Homo sapiens	69-72
3698718-5	1986	Low-dose heparin acts through its effect of factor Xa and activation of antithrombin III; DHE selectively increases venous smooth muscle tone to accelerate venous blood flow velocity and minimize venous pooling.	Heparin	9-16	serpin family C member 1	Homo sapiens	72-88
3715809-0	1986	Effects of different ions on the interactions of heparin with bovine antithrombin III and thrombin.	Heparin	49-56	serpin family C member 1	Homo sapiens	69-85
3715809-1	1986	Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution.	Heparin	139-146	serpin family C member 1	Homo sapiens	106-122
3715809-1	1986	Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution.	Heparin	139-146	serpin family C member 1	Homo sapiens	124-130
3715809-5	1986	These findings indicate that the affinity of heparin to AT III was influenced only by strongly electronegative ions, whereas its affinity to thrombin was affected by both strongly electropositive and strongly electronegative ions.	Heparin	45-52	serpin family C member 1	Homo sapiens	56-62
3838602-0	1985	Histidine-rich glycoprotein inhibits the antithrombin activity of heparin cofactor II in the presence of heparin or dermatan sulfate.	Heparin	66-73	serpin family C member 1	Homo sapiens	41-53
8750779-2	1995	In this study, hepatic lipase activity was released by low concentrations of heparin, and the release was linear with time for up to about 10 hours.	Heparin	77-84	lipase C, hepatic type	Homo sapiens	15-29
8720143-0	1995	Importance of 6-O-sulfate groups of glucosamine residues in heparin for activation of FGF-1 and FGF-2.	Heparin	60-67	fibroblast growth factor 2	Mus musculus	96-101
4082034-4	1985	The use of small doses of heparin was shown to result in a rise of antithrombin III activity in the plasma irrespective of an obvious clinical effect of treatment.	Heparin	26-33	serpin family C member 1	Homo sapiens	67-83
6598053-4	1984	Hepatic lipase and lipoprotein lipase activities were measured selectively in post-heparin plasma from all 18 patients using a substrate-specific method.	Heparin	83-90	lipoprotein lipase	Homo sapiens	19-37
6598053-6	1984	Lipoprotein lipase activities correlated inversely with serum triglyceride concentrations, but positively with in vivo post-heparin fractional clearance rates of Intralipid and with serum high-density lipoprotein concentrations.	Heparin	124-131	lipoprotein lipase	Homo sapiens	0-18
3955063-12	1986	Heparin injection increased plasma lipoprotein lipase activity in cld/cld mice, but the increment was less than 10% of that in unaffected mice.	Heparin	0-7	lipase maturation factor 1	Mus musculus	66-69
3955063-12	1986	Heparin injection increased plasma lipoprotein lipase activity in cld/cld mice, but the increment was less than 10% of that in unaffected mice.	Heparin	0-7	lipase maturation factor 1	Mus musculus	70-73
8720143-4	1995	However, complete 6-O-desulfation of trisulfated disaccharide units in heparin resulted in loss of the ability to activate FGF-2, although the desulfated product bound strongly to FGF-2.	Heparin	71-78	fibroblast growth factor 2	Mus musculus	123-128
8720143-4	1995	However, complete 6-O-desulfation of trisulfated disaccharide units in heparin resulted in loss of the ability to activate FGF-2, although the desulfated product bound strongly to FGF-2.	Heparin	71-78	fibroblast growth factor 2	Mus musculus	180-185
6498225-7	1984	The proaggregating effect of heparin subfractions correlates with the lipoprotein lipase activity and, slightly, with the molecular weight, but it does not correlate with the anticoagulant activity.	Heparin	29-36	lipoprotein lipase	Homo sapiens	70-88
3515966-5	1986	Adipose tissue heparin-releasable lipoprotein lipase activity (LPL) was also determined.	Heparin	15-22	lipoprotein lipase	Homo sapiens	63-66
8588202-4	1995	The release of TFPI, after heparin administration, was proportionally reduced in the two siblings as compared with controls.	Heparin	27-34	tissue factor pathway inhibitor	Homo sapiens	15-19
3754413-1	1986	Heparin cofactor II and antithrombin III are plasma proteins functionally similar in their ability to inhibit thrombin at accelerated rates in the presence of heparin.	Heparin	159-166	serpin family C member 1	Homo sapiens	24-40
6525337-1	1984	We have isolated from nitrous acid cleavage products of heparin two major octasaccharide fragments which bind with high affinity to human antithrombin.	Heparin	56-63	serpin family C member 1	Homo sapiens	138-150
7491926-8	1995	These results demonstrate that the Trpl cation channel is activated by Ins(1,4,5)P3 in a heparin-sensitive fashion.	Heparin	89-96	transient receptor potential-like	Drosophila melanogaster	35-39
6523441-6	1984	Low- and high affinity heparin fractions were obtained by affinity chromatography using immobilized AT III.	Heparin	23-30	serpin family C member 1	Homo sapiens	100-106
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Heparin	115-122	serpin family C member 1	Homo sapiens	126-128
6477958-9	1984	The extrahepatic uptake was strongly impeded by injection of heparin prior to injection of the lipase, and the uptake could to a large extent be reversed by injection of heparin after the lipase.	Heparin	61-68	lipase G, endothelial type	Rattus norvegicus	95-101
6477958-9	1984	The extrahepatic uptake was strongly impeded by injection of heparin prior to injection of the lipase, and the uptake could to a large extent be reversed by injection of heparin after the lipase.	Heparin	170-177	lipase G, endothelial type	Rattus norvegicus	188-194
6477958-10	1984	Even after 1 h lipase that had been taken up by extrahepatic tissues reappeared immediately in the blood on injection of heparin.	Heparin	121-128	lipase G, endothelial type	Rattus norvegicus	15-21
6500155-1	1984	Prophylactic treatment of two asymptomatic antithrombin III (AT III) -deficient women with oral anticoagulants and heparin during pregnancy and after delivery appeared to be feasible.	Heparin	115-122	serpin family C member 1	Homo sapiens	43-59
6500155-1	1984	Prophylactic treatment of two asymptomatic antithrombin III (AT III) -deficient women with oral anticoagulants and heparin during pregnancy and after delivery appeared to be feasible.	Heparin	115-122	serpin family C member 1	Homo sapiens	61-67
6500155-3	1984	A high dose of heparin intravenously in one of them caused a strong reduction in the AT III level which was corrected by infusion of AT III concentrate during delivery.	Heparin	15-22	serpin family C member 1	Homo sapiens	85-91
6500155-3	1984	A high dose of heparin intravenously in one of them caused a strong reduction in the AT III level which was corrected by infusion of AT III concentrate during delivery.	Heparin	15-22	serpin family C member 1	Homo sapiens	133-139
3513873-7	1986	Proteases, such as plasmin, streptokinase and urokinase did not influence the assay and the inhibitory effect of heparin on the PC-activation could easily be overcome by the addition of protamine sulphate.	Heparin	113-120	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	128-130
3512602-4	1986	Purification of the patient"s plasma AT-III by heparin-sepharose affinity chromatography showed a normal protein recovery and elution profile, but the purified AT-III fraction showed only 50% of the normal progressive thrombin neutralization and anti-Xa activity.	Heparin	47-54	serpin family C member 1	Homo sapiens	37-43
3512602-9	1986	These studies indicate that the patients" variant AT-III molecule was characterized by normal heparin interaction but defective binding and inhibition of thrombin and Xa.	Heparin	94-101	serpin family C member 1	Homo sapiens	50-56
3961733-5	1986	When heparin was bound to antithrombin III-Sepharose, the aggregating activity eluted totally in the high-affinity fraction.	Heparin	5-12	serpin family C member 1	Homo sapiens	26-42
3961735-2	1986	Functional antithrombin III levels fell to 0.32 U/ml during heparin treatment, but it was possible to achieve a heparin effect, measured by the activated partial thromboplastin time, thrombin clotting time and heparin assay with subcutaneous heparin in doses of 30,000 U to 35,000 U/24 hours.	Heparin	60-67	serpin family C member 1	Homo sapiens	11-27
3947081-4	1986	This antiserum inhibited LPL enzymatic activity in human milk and in human post-heparin plasma.	Heparin	80-87	lipoprotein lipase	Homo sapiens	25-28
6520110-2	1984	In the eluate from a Sephacryl S-200 column, heparin caused a peak and then a trough in the fluorescence of 48 nM antithrombin III or 63 nM thrombin.	Heparin	45-52	serpin family C member 1	Homo sapiens	114-130
6520110-5	1984	The ability to form a complex of heparin preparations with different anticoagulant activities for thrombin and antithrombin III could be determined satisfactorily.	Heparin	33-40	serpin family C member 1	Homo sapiens	111-127
8544408-11	1995	However, vimentin was significantly reduced only after 48 hours of treatment with a high dose of heparin (500 U/ml), from baseline OD 1.82 +/- 0.052 to 1.41 +/- 0.004 (P &lt; 0.002).	Heparin	97-104	vimentin	Rattus norvegicus	9-17
6520110-7	1984	Of 4 preparations with one low-affinity and three high-affinity subfractions of heparin for antithrombin III, the species with the lowest affinity for antithrombin III had the highest affinity for thrombin.	Heparin	80-87	serpin family C member 1	Homo sapiens	92-108
6520110-7	1984	Of 4 preparations with one low-affinity and three high-affinity subfractions of heparin for antithrombin III, the species with the lowest affinity for antithrombin III had the highest affinity for thrombin.	Heparin	80-87	serpin family C member 1	Homo sapiens	151-167
6486808-2	1984	This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease inhibitor for mucopolysaccharide.	Heparin	51-58	serpin family C member 1	Homo sapiens	103-115
3510115-2	1986	Heparin is a complex polysaccharide, consisting of repeating dissacharide subunits, which exerts its anticoagulant effect by potentiating the inhibition of activated clotting proteins by the naturally occurring inhibitor antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	221-237
2436996-5	1986	An absence of the heparin effect should always lead to the use of an antithrombin III assay.	Heparin	18-25	serpin family C member 1	Homo sapiens	69-85
6486808-3	1984	Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor.	Heparin	72-79	serpin family C member 1	Homo sapiens	17-29
7574939-4	1995	RESULTS: Heparin administration resulted in a significant prolongation of the bleeding time (from 6.3 +/- 2.1 to 12.6 +/- 4.9 minutes; p &lt; 0.00001), a significant reduction in the level of shed blood thromboxane B2 (from 1,152 +/- 669 to 538 +/- 187 pg/0.1 mL; p = 0.00002), and an increase in the plasma levels of plasmin (from 11.8 +/- 9.7 to 125.4 +/- 34.8 U/L; p &lt; 0.0001) and D-dimer (from 571.3 +/- 297.1 to 698.5 +/- 358.6 micrograms/mL; p = 0.05).	Heparin	9-16	plasminogen	Homo sapiens	318-325
6487709-0	1984	Interaction of antithrombin III with preadsorbed albumin-heparin conjugates.	Heparin	57-64	serpin family C member 1	Homo sapiens	15-31
6487709-1	1984	The adsorption of antithrombin III (AT III) onto polystyrene surfaces preadsorbed with albumin or albumin-heparin conjugates was studied using a two step enzyme immuno assay.	Heparin	106-113	serpin family C member 1	Homo sapiens	18-34
3583099-6	1986	Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII.	Heparin	199-206	serpin family C member 1	Homo sapiens	71-76
3583099-6	1986	Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII.	Heparin	199-206	serpin family C member 1	Homo sapiens	267-272
6487709-1	1984	The adsorption of antithrombin III (AT III) onto polystyrene surfaces preadsorbed with albumin or albumin-heparin conjugates was studied using a two step enzyme immuno assay.	Heparin	106-113	serpin family C member 1	Homo sapiens	36-42
6487709-2	1984	When AT III-buffer solutions were used, the highest adsorption values were measured on high affinity albumin-heparin conjugate pretreated surfaces.	Heparin	109-116	serpin family C member 1	Homo sapiens	5-11
6487709-3	1984	Less AT III adsorption was found on nonfractionated albumin-heparin conjugate preadsorbed surfaces.	Heparin	60-67	serpin family C member 1	Homo sapiens	5-11
6487709-5	1984	When AT III was adsorbed from plasma or plasma dilutions with buffer, only AT III on surfaces preadsorbed with high affinity or nonfractionated albumin-heparin conjugate was found.	Heparin	152-159	serpin family C member 1	Homo sapiens	5-11
6484894-1	1984	Effect of purification of AT III-binding sequence of heparin.	Heparin	53-60	serpin family C member 1	Homo sapiens	26-32
3710297-2	1986	Heparin inhibits blood coagulation by 3 independent mechanisms by augmenting the effect of antithrombin III (the major effect), by augmenting the inhibitory effect of thrombin or heparin cofactor II, and by disrupting the activation of blood coagulation on the platelet surface; it has an additional effect on hemostasis through its interaction with blood platelets.	Heparin	0-7	serpin family C member 1	Homo sapiens	91-107
3734344-1	1986	Thrombo-embolic complications in pregnant women who have congenital antithrombin III deficiency are usually prevented by giving injections of sub-cutaneous heparin from the beginning to the end of pregnancy and with the administration of concentrated doses of antithrombin III (A.T. III) at delivery and in the following days.	Heparin	156-163	serpin family C member 1	Homo sapiens	68-84
7670097-0	1995	Heparin inhibits the expression of interleukin-11 and granulocyte-macrophage colony-stimulating factor in primate bone marrow stromal fibroblasts through mRNA destabilization.	Heparin	0-7	LOC102118349	Macaca fascicularis	35-49
6379981-7	1984	This is also the case with heparins of low and high affinity for antithrombin.	Heparin	27-35	serpin family C member 1	Homo sapiens	65-77
4089534-0	1985	Changes in plasma antithrombin (heparin cofactor activity) during intravenous heparin therapy: observations in 198 patients with deep venous thrombosis.	Heparin	32-39	serpin family C member 1	Homo sapiens	18-30
7556445-8	1995	Whereas addition of suramin to COS cell cultures significantly increases the levels of all six Wnts in the medium, the addition of heparin only influences the levels of Wnt-1, Wnt-6, and Wnt-7b.	Heparin	131-138	wingless-type MMTV integration site family, member 1	Mus musculus	169-174
4089534-1	1985	Plasma antithrombin (AT) measured as heparin cofactor activity decreased 0.16 +/- 0.13 U/ml (mean +/- SD) in 198 patients who received heparin infusion during 1 wk for deep venous thrombosis (DVT).	Heparin	37-44	serpin family C member 1	Homo sapiens	7-19
6375731-0	1984	Effects of hormones, amino acids and specific inhibitors on rat heart heparin-releasable lipoprotein lipase and tissue neutral lipase activities during long-term perfusion.	Heparin	70-77	lipase G, endothelial type	Rattus norvegicus	101-107
8697247-5	1995	Heparin could enhance activity of bFGF to stimulate formation of granulation tissue, regeneration of capillary, proliferation of fibroblast and DNA synthesis.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	34-38
6740566-0	1984	Antithrombin III in patients with acute deep vein thrombosis during heparin treatment (subcutaneous and intravenous) and during and after treatment with oral coumarins.	Heparin	68-75	serpin family C member 1	Homo sapiens	0-16
4089794-7	1985	The changes in heparin kinetics in FHF are likely to be complex with the balance between the proteins that act as cofactors, (e.g. AT III) and the proteins that have heparin neutralising activity, controlling the response of added heparin.	Heparin	15-22	serpin family C member 1	Homo sapiens	131-137
4082106-5	1985	The area under the activity time curve (AUC) of LPL and factor Xa was double with LMW heparin (p less than 0.05).	Heparin	86-93	lipoprotein lipase	Homo sapiens	48-51
6740566-4	1984	The AT-III concentration was estimated daily during heparin treatment and repeatedly during the first year.	Heparin	52-59	serpin family C member 1	Homo sapiens	4-10
7500917-2	1995	Interaction of the virus with its receptor is mediated by the envelope glycoprotein C (PrV-gC), a protein with heparin-binding properties.	Heparin	111-118	envelope glycoprotein C	Suid alphaherpesvirus 1	62-85
6740566-5	1984	The mean AT-III concentration decreased progressively 25% during 5 days of heparin treatment regardless of whether heparin was given intravenously or subcutaneously.	Heparin	75-82	serpin family C member 1	Homo sapiens	9-15
6715365-0	1984	Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	87-103
6715365-0	1984	Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III.	Heparin	43-50	serpin family C member 1	Homo sapiens	87-103
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	21-28	serpin family C member 1	Homo sapiens	64-80
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	21-28	serpin family C member 1	Homo sapiens	129-145
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	172-179	serpin family C member 1	Homo sapiens	64-80
6715365-1	1984	The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200).	Heparin	172-179	serpin family C member 1	Homo sapiens	64-80
3875906-10	1985	Our study provides the first clinical evidence that the protamine-heparin complex activates complement via the classic (C4a) pathway.	Heparin	66-73	complement C4A (Rodgers blood group)	Homo sapiens	120-123
3875633-10	1985	This data suggests that alpha 1-PI does not function as a major inhibitor of factor Xa in vivo, and that a tonically active heparin-dependent mechanism exists in humans for accelerating the neutralization of this enzyme by antithrombin.	Heparin	124-131	serpin family C member 1	Homo sapiens	223-235
6715365-6	1984	Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic.	Heparin	75-82	serpin family C member 1	Homo sapiens	58-74
8533128-0	1995	Effect of protamine on heparin releasable TFPI antigen levels in normal volunteers.	Heparin	23-30	tissue factor pathway inhibitor	Homo sapiens	42-46
6715365-6	1984	Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic.	Heparin	190-197	serpin family C member 1	Homo sapiens	58-74
6715365-6	1984	Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic.	Heparin	190-197	serpin family C member 1	Homo sapiens	58-74
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	87-94	serpin family C member 1	Homo sapiens	132-148
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	87-94	serpin family C member 1	Homo sapiens	355-371
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	serpin family C member 1	Homo sapiens	132-148
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	serpin family C member 1	Homo sapiens	132-148
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	serpin family C member 1	Homo sapiens	132-148
6715365-7	1984	We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III.	Heparin	152-159	serpin family C member 1	Homo sapiens	132-148
6713636-0	1984	Sensitive non-radioisotopic method for measuring lipoprotein lipase and hepatic triglyceride lipase in post-heparin plasma.	Heparin	108-115	lipoprotein lipase	Homo sapiens	49-67
6713636-1	1984	In this method for measuring lipoprotein lipase (LPL) and hepatic triglyceride lipase (H-TGL) in post-heparin plasma, we determine the released free fatty acids enzymically.	Heparin	102-109	lipoprotein lipase	Homo sapiens	29-47
6713636-1	1984	In this method for measuring lipoprotein lipase (LPL) and hepatic triglyceride lipase (H-TGL) in post-heparin plasma, we determine the released free fatty acids enzymically.	Heparin	102-109	lipoprotein lipase	Homo sapiens	49-52
6713636-5	1984	A 5-microL sample of post-heparin plasma suffices to measure the activity of LPL and H-TGL; thus the method is as sensitive as the radioisotopic method.	Heparin	26-33	lipoprotein lipase	Homo sapiens	77-80
6471667-4	1984	Hepatic lipase and lipoprotein lipase activities were selectively measured in post-heparin plasma in 59 patients.	Heparin	83-90	lipoprotein lipase	Homo sapiens	19-37
3873967-0	1985	Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III.	Heparin	10-17	serpin family C member 1	Homo sapiens	76-92
3873967-7	1985	Using purified factor XIIa and ATIII, we found that heparin (0.7 to 34.0 U/mL) increased the rate of inhibition of Factor XIIa.	Heparin	52-59	serpin family C member 1	Homo sapiens	31-36
3873967-11	1985	Furthermore, using purified factor XIIf and antithrombin III, heparin (3.6 to 57.2 U/mL) increased the inactivation rate constant of factor XIIf by 1.6 to 14.0 times.	Heparin	62-69	serpin family C member 1	Homo sapiens	44-60
3998153-7	1985	Heparin, which is known to prevent the binding of lipoprotein lipase to the cell surface membrane, abrogated the transfer of tocopherol to fibroblasts without altering the rate of triglyceride hydrolysis.	Heparin	0-7	lipoprotein lipase	Homo sapiens	50-68
3988727-0	1985	The role of surface charge on the accelerating action of heparin on the antithrombin III-inhibited activity of alpha-thrombin.	Heparin	57-64	serpin family C member 1	Homo sapiens	72-88
3988727-8	1985	Heparin acts on the antithrombin III-thrombin reaction through cooperative electrostatic binding to thrombin and nonelectrostatic interaction with antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	20-36
3988727-8	1985	Heparin acts on the antithrombin III-thrombin reaction through cooperative electrostatic binding to thrombin and nonelectrostatic interaction with antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	147-163
3988735-0	1985	Apolipoprotein effects on the lipolysis of perfused triglyceride by heparin-immobilized milk lipase.	Heparin	68-75	carboxyl ester lipase	Homo sapiens	88-99
3988735-1	1985	Bovine milk lipase was noncovalently bound to a heparin-Sepharose support and a [3H]glycerol/[14C]triolein emulsion was circulated through it.	Heparin	48-55	carboxyl ester lipase	Homo sapiens	7-18
6704414-9	1984	Labelled apolipoprotein uptake by the heart was reduced by 90% when lipoprotein lipase was first released by heparin or when VLDL was treated with 1,2-cyclohexanedione to modify arginine residues of apolipoproteins.	Heparin	109-116	lipoprotein lipase	Homo sapiens	68-86
7600119-2	1995	A major pool of TFPI is associated with the vascular endothelium and can be mobilized into the circulation by heparin.	Heparin	110-117	tissue factor pathway inhibitor	Homo sapiens	16-20
6698980-20	1984	Based on these models, it is proposed that the unstable helical segment composed of residues 281-292 is the heparin-binding site in antithrombin III.	Heparin	108-115	serpin family C member 1	Homo sapiens	132-148
3994667-0	1985	Binding of active and inactive forms of lipoprotein lipase to heparin.	Heparin	62-69	lipoprotein lipase	Homo sapiens	40-58
3994667-7	1985	Binding of active lipoprotein lipase to heparin-Sepharose could be demonstrated at pH down to 6.5.	Heparin	40-47	lipoprotein lipase	Homo sapiens	18-36
7600119-4	1995	In this study, heparin administration caused a 2.2-fold and a 7.5-fold increase in TFPI activity and TFPI antigen, respectively, in 25 patients with phenotypes IIa and IIb hyperbetalipoproteinemia.	Heparin	15-22	tissue factor pathway inhibitor	Homo sapiens	83-87
3994667-11	1985	Catalytically inactive lipoprotein lipase retained the ability to bind to heparin-Sepharose.	Heparin	74-81	lipoprotein lipase	Homo sapiens	23-41
6714944-3	1984	Activities of mitochondrial enzymes within the Kupffer cells increased during the early phase of phagocytosis; they later declined, reaching the endogenous level of the Kupffer cell mitochondria after 3 to 4 h. The uptake was enhanced in the presence of heparin or rat serum, while iodoacetate, cytochalasin B or anti-fibronectin antisera were inhibitory.	Heparin	254-261	fibronectin 1	Rattus norvegicus	318-329
6583694-0	1984	Evaluation of critical groups required for the binding of heparin to antithrombin.	Heparin	58-65	serpin family C member 1	Homo sapiens	69-81
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	136-143	serpin family C member 1	Homo sapiens	56-72
2987072-0	1985	Hepatic triglyceride lipase and lipoprotein lipase activities in post-heparin plasma of patients with various cancers.	Heparin	70-77	lipoprotein lipase	Homo sapiens	32-50
3920639-5	1985	Lipoprotein lipase activity of post-heparin plasma increased from 14 to 35 mumol free fatty acids/ml/h during parenteral nutrition whereas hepatic lipase activity remained unchanged at 40 mumol free fatty acids/ml/h.	Heparin	36-43	lipoprotein lipase	Homo sapiens	0-18
7600119-4	1995	In this study, heparin administration caused a 2.2-fold and a 7.5-fold increase in TFPI activity and TFPI antigen, respectively, in 25 patients with phenotypes IIa and IIb hyperbetalipoproteinemia.	Heparin	15-22	tissue factor pathway inhibitor	Homo sapiens	101-105
3967090-1	1985	A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin.	Heparin	272-279	serpin family C member 1	Homo sapiens	24-40
6201043-0	1984	Heparin and plasma proteinase inhibitors: influence of heparin on the inhibition of thrombin by alpha 2 macroglobulin.	Heparin	55-62	alpha-2-macroglobulin	Homo sapiens	96-117
7600119-5	1995	Because the antigen determination of TFPI almost exclusively measures carrier-free TFPI, more than 90% of the heparin-induced increase in TFPI activity was caused by mobilization of carrier-free TFPI from the vascular endothelium.	Heparin	110-117	tissue factor pathway inhibitor	Homo sapiens	37-41
3967090-1	1985	A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin.	Heparin	272-279	serpin family C member 1	Homo sapiens	42-48
3967090-1	1985	A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin.	Heparin	272-279	serpin family C member 1	Homo sapiens	24-36
7600119-5	1995	Because the antigen determination of TFPI almost exclusively measures carrier-free TFPI, more than 90% of the heparin-induced increase in TFPI activity was caused by mobilization of carrier-free TFPI from the vascular endothelium.	Heparin	110-117	tissue factor pathway inhibitor	Homo sapiens	83-87
3967090-3	1985	AT III was purified from normal and propositus plasma by sulfate dextran precipitation followed by heparin affinity chromatography.	Heparin	99-106	serpin family C member 1	Homo sapiens	0-6
3970857-0	1985	Purification of antithrombin "Vicenza": a molecule with normal heparin affinity and impaired reactivity to thrombin.	Heparin	63-70	serpin family C member 1	Homo sapiens	16-28
6731952-0	1984	[Automatization of heparin determination using chronometric evaluation of anti-Xa activity of the AT III-heparin complex].	Heparin	19-26	serpin family C member 1	Homo sapiens	98-104
7600119-5	1995	Because the antigen determination of TFPI almost exclusively measures carrier-free TFPI, more than 90% of the heparin-induced increase in TFPI activity was caused by mobilization of carrier-free TFPI from the vascular endothelium.	Heparin	110-117	tissue factor pathway inhibitor	Homo sapiens	83-87
6731952-0	1984	[Automatization of heparin determination using chronometric evaluation of anti-Xa activity of the AT III-heparin complex].	Heparin	105-112	serpin family C member 1	Homo sapiens	98-104
3970857-1	1985	Antithrombin III (AT) "Vicenza", a previously described dysfunctional AT associated with familial thrombosis, has been isolated by heparin affinity chromatography.	Heparin	131-138	serpin family C member 1	Homo sapiens	0-16
7600119-5	1995	Because the antigen determination of TFPI almost exclusively measures carrier-free TFPI, more than 90% of the heparin-induced increase in TFPI activity was caused by mobilization of carrier-free TFPI from the vascular endothelium.	Heparin	110-117	tissue factor pathway inhibitor	Homo sapiens	83-87
7569739-4	1995	The heparin injection induced a significant elevation of plasmin (PL) (p &lt; 0.05) which stayed elevated during extracorporeal circulation.	Heparin	4-11	plasminogen	Homo sapiens	57-64
3965464-6	1985	Kinetic studies of thrombin inactivation by both antithrombins, in the presence of nonsaturating amounts of heparin, indicated that AT-III beta inhibited thrombin more rapidly.	Heparin	108-115	serpin family C member 1	Homo sapiens	132-138
3965464-7	1985	AT-III beta is also distinguishable from AT-III alpha on the basis of heparin-binding affinity estimated from titration of protein fluorescence with heparin.	Heparin	70-77	serpin family C member 1	Homo sapiens	0-6
3965464-7	1985	AT-III beta is also distinguishable from AT-III alpha on the basis of heparin-binding affinity estimated from titration of protein fluorescence with heparin.	Heparin	149-156	serpin family C member 1	Homo sapiens	0-6
3965464-8	1985	Thus, antithrombin III exists as two molecular entities in human plasma which differ both structurally, in carbohydrate content, and functionally, in their heparin-binding behavior.	Heparin	156-163	serpin family C member 1	Homo sapiens	6-22
2944348-5	1985	However, at high concentration of heparin, plasmin inactivation by antithrombin III is accelerated even in the presence of fibrinogen or fibrin.	Heparin	34-41	serpin family C member 1	Homo sapiens	67-83
6083957-1	1984	In a trial involving 61 patients suffering from shock and DIC, the relations between the concentration of heparin, the effect of heparin on coagulation and the activity of AT III were studied.	Heparin	106-113	serpin family C member 1	Homo sapiens	172-178
6083957-2	1984	The effect of heparin decreased to one-half when the activity of AT III was 75 per cent of the average normal level.	Heparin	14-21	serpin family C member 1	Homo sapiens	65-71
6442908-6	1984	Abnormality of AT-III was also found in heparin-binding studies.	Heparin	40-47	serpin family C member 1	Homo sapiens	15-21
3919676-11	1985	Not only may platelet aggregation persist with low molecular weight heparin which rekindles the debate as to its pathogenic mechanism, but also low molecular weight heparin may have a slight antithrombin effect which limits its use in patients at high risk of thromboembolism, imposing treatment with fast acting vitamin K antagonists.	Heparin	165-172	serpin family C member 1	Homo sapiens	191-203
7569739-4	1995	The heparin injection induced a significant elevation of plasmin (PL) (p &lt; 0.05) which stayed elevated during extracorporeal circulation.	Heparin	4-11	plasminogen	Homo sapiens	66-68
6724355-3	1984	This type of AT-III deficiency (type 1) was later divided into type 1a and 1b on the basis of the heparin affinity of the AT-III molecule.	Heparin	98-105	serpin family C member 1	Homo sapiens	13-19
7601155-4	1995	After ligation, the covalently closed substrate was used to follow an 1800-fold purification of the mouse X-solvase (EMX1) from crude nuclear extracts by chromatography on DEAE-cellulose, MonoQ and heparin-Sepharose.	Heparin	198-205	empty spiracles homeobox 1	Mus musculus	117-121
6724356-5	1984	There are several types of AT-III defect; they are characterized by a decrease in amount and function, a functional decrease, or a pathological heparin-binding.	Heparin	144-151	serpin family C member 1	Homo sapiens	27-33
6718507-0	1984	[Clinical problems posed by the consumption of antithrombin III induced by heparin].	Heparin	75-82	serpin family C member 1	Homo sapiens	47-63
6718507-1	1984	Two cases of resistance to the heparin treatment, induced by large consumption of antithrombin III, are reported.	Heparin	31-38	serpin family C member 1	Homo sapiens	82-98
6718507-2	1984	Normally small, this consumption does not automatically call for the systematic dosage of Antithrombin III for each treatment using heparin.	Heparin	132-139	serpin family C member 1	Homo sapiens	90-106
6718507-3	1984	On the other hand, any clinical or biological resistance to higher doses of heparin, any personal or family history of thrombosis necessitate the administration of Antithrombin III.	Heparin	76-83	serpin family C member 1	Homo sapiens	164-180
6582486-0	1984	Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability.	Heparin	115-122	serpin family C member 1	Homo sapiens	0-16
6582486-0	1984	Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability.	Heparin	115-122	serpin family C member 1	Homo sapiens	87-103
6397248-8	1984	Adipose tissue heparin-releasable lipoprotein lipase activity was also determined and expressed in micromoles of free fatty acids per hour per gram of tissue and per 10(6) cells.	Heparin	15-22	lipoprotein lipase	Homo sapiens	34-52
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipoprotein lipase	Homo sapiens	155-173
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipoprotein lipase	Homo sapiens	175-178
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipase G, endothelial type	Rattus norvegicus	167-173
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipoprotein lipase	Homo sapiens	155-173
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipoprotein lipase	Homo sapiens	175-178
6522147-1	1984	The frequent inclusion of heparin in fluids used for total parenteral nutrition in infants, prompted an investigation of the ability of heparin to release lipoprotein lipase (LPL) and hepatic lipase (HL) from the endothelial surface into the circulation, and of the effect of heparin on tissue stores of lipase in the postnatal period.	Heparin	136-143	lipase G, endothelial type	Rattus norvegicus	167-173
6544786-6	1984	Albumin-heparin conjugates with high affinity for antithrombin III gave more prolonged clotting times as low affinity conjugates when used as coatings for glass.	Heparin	8-15	serpin family C member 1	Homo sapiens	50-66
6516292-1	1984	A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS).	Heparin	170-177	serpin family C member 1	Homo sapiens	73-89
6516292-1	1984	A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS).	Heparin	170-177	serpin family C member 1	Homo sapiens	91-97
7647220-6	1995	Heparin strongly accelerates AT and releases TFPI to the blood.	Heparin	0-7	tissue factor pathway inhibitor	Homo sapiens	45-49
6198746-11	1983	We conclude that plasma contains a component(s) which displaces (thrombin-antithrombin-III) complex from immobilised heparin: presumably this leaves the heparin sites free for further use in enzyme inactivation.	Heparin	117-124	serpin family C member 1	Homo sapiens	74-90
6198746-11	1983	We conclude that plasma contains a component(s) which displaces (thrombin-antithrombin-III) complex from immobilised heparin: presumably this leaves the heparin sites free for further use in enzyme inactivation.	Heparin	153-160	serpin family C member 1	Homo sapiens	74-90
6207810-10	1984	The catalysis was shown to be due to a weak electrostatic interaction, since it was completely reversed by concentrations of NaCl greater than 0.3 M. It is concluded that the mechanism is independent of the heparin high-affinity binding site on antithrombin III and is probably due to binding of the high-charge-density polysaccharide to the proteinase.	Heparin	207-214	serpin family C member 1	Homo sapiens	245-261
6207810-11	1984	It is calculated that the acceleration in rate achieved, although lower than that of heparin, approaches that required to be of physiological significance and may be of importance in the anticoagulation role of antithrombin III at sites of high charge density which may occur in vivo.	Heparin	85-92	serpin family C member 1	Homo sapiens	211-227
7647222-0	1995	Tissue factor pathway inhibitor: proposed heparin recognition region.	Heparin	42-49	tissue factor pathway inhibitor	Homo sapiens	0-31
6209818-0	1984	Abolition by dextran sulfate of the heparin-accelerated antithrombin III/thrombin reaction.	Heparin	36-43	serpin family C member 1	Homo sapiens	56-72
6209818-4	1984	These findings indicate that binding of dextran sulfate to a site other than the active site of thrombin to prevent the approach of AT III in the presence of heparin.	Heparin	158-165	serpin family C member 1	Homo sapiens	132-138
6661357-0	1983	Release of LPL activity after intravenous injection of a low molecular weight heparin.	Heparin	78-85	lipoprotein lipase	Homo sapiens	11-14
7647222-1	1995	After intravenous and subcutaneous injection, heparins and low-molecular-weight heparins release tissue factor pathway inhibitor (TFPI) into the blood stream.	Heparin	46-54	tissue factor pathway inhibitor	Homo sapiens	97-128
7647222-1	1995	After intravenous and subcutaneous injection, heparins and low-molecular-weight heparins release tissue factor pathway inhibitor (TFPI) into the blood stream.	Heparin	46-54	tissue factor pathway inhibitor	Homo sapiens	130-134
7647222-7	1995	This proposed heparin recognition region in TFPI is similar to the recognition region in antithrombin III and other proteins.	Heparin	14-21	tissue factor pathway inhibitor	Homo sapiens	44-48
7647222-9	1995	A comparison of a helical wheel diagram of antithrombin III and tissue factor pathway inhibitor support also the proposal of this form of a heparin recognition region in TFPI.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	64-95
6355100-3	1983	This was associated with significant reductions in heparin-releasable (functional) lipoprotein lipase and tissue lipoprotein lipase of perfused hearts.	Heparin	51-58	lipase G, endothelial type	Rattus norvegicus	95-101
6197951-8	1983	Heparin stimulated RNA polymerase II activity decreased 10% in the P1 and 44% in the P2 fraction.	Heparin	0-7	zinc finger protein 185	Mus musculus	67-76
6640057-3	1983	In order to ascertain the heparin-like mechanism of this activity we have studied the interactions of thrombin and antithrombin III with two polymers of this series: sulphonated polystyrene and sulphonate-glutamic acid sulphonamide polystyrene.	Heparin	26-33	serpin family C member 1	Homo sapiens	115-131
6147249-0	1984	The interaction of skeletal myosin subfragment 1 with the polyanion, heparin.	Heparin	69-76	myosin heavy chain 14	Homo sapiens	28-34
6147249-1	1984	The association between chymotryptic skeletal muscle myosin subfragment 1 (S1) and the polyanion, heparin, was investigated as an experimental approach in probing the functional importance of the cationic sites on S1 and their involvement in ionic interactions within the myosin head during energy transduction.	Heparin	98-105	myosin heavy chain 14	Homo sapiens	272-278
6496919-5	1984	Heparin sensitivity, measured as an increase in the ratio of activated coagulation time (ACT) X IU heparin-1 X kg-1 as a response to initial heparin dose, was found to be significantly higher (1.22 +/- 0.30 sec X IU heparin-1 X kg-1) in patients receiving AT III as measured in the control group (0.95 +/- 0.23 s X IU heparin-1 X kg-1).	Heparin	0-7	serpin family C member 1	Homo sapiens	256-262
7647222-9	1995	A comparison of a helical wheel diagram of antithrombin III and tissue factor pathway inhibitor support also the proposal of this form of a heparin recognition region in TFPI.	Heparin	140-147	tissue factor pathway inhibitor	Homo sapiens	170-174
6638506-7	1983	Despite the finding that BAL interacts with heparin-Sepharose, soluble heparin had no effect on BAL activity.	Heparin	44-51	carboxyl ester lipase	Homo sapiens	25-28
7647223-0	1995	The role of tissue factor pathway inhibitor in the mediation of the antithrombotic actions of heparin and low-molecular-weight heparin.	Heparin	94-101	tissue factor pathway inhibitor	Homo sapiens	12-43
6638506-8	1983	The possible physiological role of BAL-heparin interaction has also been discussed.	Heparin	39-46	carboxyl ester lipase	Homo sapiens	35-38
7647223-0	1995	The role of tissue factor pathway inhibitor in the mediation of the antithrombotic actions of heparin and low-molecular-weight heparin.	Heparin	127-134	tissue factor pathway inhibitor	Homo sapiens	12-43
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Heparin	21-28	serpin family C member 1	Homo sapiens	39-55
6435583-4	1984	The recurrence of local signs of DVT after 12 day"s heparin therapy with AT III levels (B) of 40%, led to a change in management with infusion of purified AT III concentrate at a dose of 40 U per kg (2 500 U per hour).	Heparin	52-59	serpin family C member 1	Homo sapiens	73-79
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Heparin	121-128	serpin family C member 1	Homo sapiens	39-55
7727433-0	1995	Effect of heparin on the inhibition of factor Xa by tissue factor pathway inhibitor: a segment, Gly212-Phe243, of the third Kunitz domain is a heparin-binding site.	Heparin	10-17	tissue factor pathway inhibitor	Homo sapiens	52-83
6625618-1	1983	The present study has shown that calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction.	Heparin	54-61	serpin family C member 1	Homo sapiens	72-88
6625618-2	1983	The initial rate of thrombin (4.0 nM) inhibition by antithrombin III (200 nM) in the presence of heparin (2.5 ng/ml) decreased from 3.6 nM/min (in the absence of calcium) to 0.12 nM/min in the presence of 10 mM calcium.	Heparin	97-104	serpin family C member 1	Homo sapiens	52-68
6625618-4	1983	The heparin-catalyzed antithrombin III/thrombin reaction is described by the general rate equation for a random-order, bireactant, enzyme-catalyzed reaction (M. J. Griffith (1982) J. Biol.	Heparin	4-11	serpin family C member 1	Homo sapiens	22-38
6625618-8	1983	The apparent kinetic parameters for the heparin-catalyzed antithrombin III/thrombin reaction were determined in the presence and absence of calcium.	Heparin	40-47	serpin family C member 1	Homo sapiens	58-74
6888269-0	1983	Lipoprotein lipase and hepatic lipase activity after heparin administration in abetalipoproteinemia and hypobetalipoproteinemia.	Heparin	53-60	lipoprotein lipase	Homo sapiens	0-18
6888269-5	1983	Lipoprotein lipase activity in the three patients with abetalipoproteinemia was 46%, 29%, and 34% of that of the controls in the samples obtained 15 minutes after heparin injection, whereas the values obtained after 30 minutes were 53%, 64%, and 47% of that of the controls.	Heparin	163-170	lipoprotein lipase	Homo sapiens	0-18
6888269-6	1983	We conclude that an inherent absence of triglyceride-rich lipoproteins, as occurs in abetalipoproteinemia, is associated with reduced enzyme activity of both hepatic lipase and lipoprotein lipase in plasma after heparin administration.	Heparin	212-219	lipoprotein lipase	Homo sapiens	177-195
6474360-0	1984	Effect of continuous low-dose intravenous heparin administered during operation on postoperative measurements of antithrombin III and antifactor Xa.	Heparin	42-49	serpin family C member 1	Homo sapiens	113-129
6474360-2	1984	The anticoagulant effect of heparin was determined by immunologic measurements of antithrombin III (AT III) and by assay of AT III and antifactor Xa activity on postoperative days 1 and 3.	Heparin	28-35	serpin family C member 1	Homo sapiens	82-98
6474360-2	1984	The anticoagulant effect of heparin was determined by immunologic measurements of antithrombin III (AT III) and by assay of AT III and antifactor Xa activity on postoperative days 1 and 3.	Heparin	28-35	serpin family C member 1	Homo sapiens	100-106
6474360-2	1984	The anticoagulant effect of heparin was determined by immunologic measurements of antithrombin III (AT III) and by assay of AT III and antifactor Xa activity on postoperative days 1 and 3.	Heparin	28-35	serpin family C member 1	Homo sapiens	124-130
6474360-3	1984	Despite lowered plasma AT III levels on postoperative day 3, the patients who had received low-dose heparin had significantly increased plasma antifactor Xa activity when compared with control patients (P less than 0.05).	Heparin	100-107	serpin family C member 1	Homo sapiens	23-29
7727433-0	1995	Effect of heparin on the inhibition of factor Xa by tissue factor pathway inhibitor: a segment, Gly212-Phe243, of the third Kunitz domain is a heparin-binding site.	Heparin	143-150	tissue factor pathway inhibitor	Homo sapiens	52-83
7771542-6	1995	Isolated adult myocytes were found to be capable of heparin-resistant internalization of 125I-labeled bFGF, to lose their viability after interaction with bFGF-saporin (a mitotoxin known to kill cells after entry via the bFGF receptor), and to respond to bFGF by activation of mitogen-activated protein kinase.	Heparin	52-59	fibroblast growth factor 2	Rattus norvegicus	102-106
6746897-6	1984	The above mucopolysaccharides function in a manner similar to commercial heparin, since modification of antithrombin at a site critical for heparin-dependent acceleration of the protease inhibitor resulted in a level of interaction product identical to the uncatalyzed amount.	Heparin	140-147	serpin family C member 1	Homo sapiens	104-116
6747440-3	1984	Antithrombin III from two members of this family was purified by dextran sulfate precipitation, affinity chromatography on heparin-Sepharose, and ion-exchange chromatography on DEAE-Sephadex A-50.	Heparin	123-130	serpin family C member 1	Homo sapiens	0-16
6747440-6	1984	The nonreactive as well as the reactive population of antithrombin III bound heparin with the same affinity as normal antithrombin III.	Heparin	77-84	serpin family C member 1	Homo sapiens	54-70
6747440-7	1984	This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence.	Heparin	163-170	serpin family C member 1	Homo sapiens	141-157
6747440-7	1984	This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence.	Heparin	163-170	serpin family C member 1	Homo sapiens	141-157
6747440-8	1984	Kinetic studies in the absence and in the presence of heparin indicated that the fraction of antithrombin III that could inactivate thrombin was functionally normal.	Heparin	54-61	serpin family C member 1	Homo sapiens	93-109
6467606-3	1984	The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis.	Heparin	33-40	serpin family C member 1	Homo sapiens	23-29
6467606-3	1984	The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis.	Heparin	33-40	serpin family C member 1	Homo sapiens	124-130
6467606-3	1984	The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis.	Heparin	33-40	serpin family C member 1	Homo sapiens	124-130
6467606-3	1984	The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis.	Heparin	204-211	serpin family C member 1	Homo sapiens	23-29
6740570-0	1984	Reactivity of heparin with the human plasma heparin-binding proteins thrombin, antithrombin III, and apolipoproteins E and B-100.	Heparin	14-21	serpin family C member 1	Homo sapiens	79-95
6740570-1	1984	The heparin-binding properties of human plasma apolipoproteins B-100 and E (apoB-100 and E) of low density lipoproteins (LDL), thrombin, and antithrombin-III (AT-III) were investigated.	Heparin	4-11	serpin family C member 1	Homo sapiens	141-157
6577437-4	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and antithrombin III/factor Xa reactions differed in terms of apparent maximum velocity (Vmax) and apparent heparin-protease dissociation constant values.	Heparin	31-38	serpin family C member 1	Homo sapiens	49-65
6577437-4	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and antithrombin III/factor Xa reactions differed in terms of apparent maximum velocity (Vmax) and apparent heparin-protease dissociation constant values.	Heparin	31-38	serpin family C member 1	Homo sapiens	79-95
6415849-0	1983	Interaction of heparin with histidine-rich glycoprotein and with antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	65-81
6415849-1	1983	The interaction between heparin, histidine-rich glycoprotein and antithrombin III was studied in purified systems.	Heparin	24-31	serpin family C member 1	Homo sapiens	65-81
6415849-2	1983	Histidine-rich glycoprotein binds heparin and thereby interferes with its interaction with antithrombin III, resulting in neutralization of the anticoagulant activity.	Heparin	34-41	serpin family C member 1	Homo sapiens	91-107
6415849-3	1983	This interaction occurs with clinical grade heparin as well as with high affinity (for antithrombin III) heparin and with a high affinity heparin fragment with Mr 4,300.	Heparin	105-112	serpin family C member 1	Homo sapiens	87-103
6615439-7	1983	The similar properties of antithrombin-thrombin complexes formed with or without heparin support the concept of a catalytic role for the polysaccharide in the antithrombin-thrombin reaction.	Heparin	81-88	serpin family C member 1	Homo sapiens	159-171
6679339-0	1983	Comparison of heparin-releasable lipase and tissue neutral lipase activity of rat heart.	Heparin	14-21	lipase G, endothelial type	Rattus norvegicus	33-39
6871478-3	1983	The main laboratory features were: normal routine clotting tests, slightly decreased AT III activities in all assays carried out in the presence of heparin.	Heparin	148-155	serpin family C member 1	Homo sapiens	85-91
6871107-2	1983	The abnormal molecule, called AT III "Vicenza", was characterized by two-dimensional crossed immunoelectrophoresis either in the absence or presence of heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	30-36
6740570-1	1984	The heparin-binding properties of human plasma apolipoproteins B-100 and E (apoB-100 and E) of low density lipoproteins (LDL), thrombin, and antithrombin-III (AT-III) were investigated.	Heparin	4-11	serpin family C member 1	Homo sapiens	159-165
6740570-5	1984	The unretained fraction of heparin (HRH1) had a low affinity for AT-III.	Heparin	27-34	histamine receptor H1	Homo sapiens	36-40
6740570-5	1984	The unretained fraction of heparin (HRH1) had a low affinity for AT-III.	Heparin	27-34	serpin family C member 1	Homo sapiens	65-71
7726132-10	1995	In patients with cardiovascular disease, a 7-day treatment with subcutaneous standard heparin increased TFPI activity.	Heparin	86-93	tissue factor pathway inhibitor	Homo sapiens	104-108
6722352-9	1984	Heparin inhibited the tissue factor-dependent activation of factor IX almost completely, apparently through the effect of antithrombin on the feedback reactions of factors Xa and IXa on factor VII.	Heparin	0-7	serpin family C member 1	Homo sapiens	122-134
6883717-4	1983	Based on the fact that protamine sulfate did not show any direct action on the antithrombin III molecule, the presence of AT III with progressive activity was considered to play an important role in the rebound phenomenon of heparin after heparin neutralization with protamine sulfate.	Heparin	225-232	serpin family C member 1	Homo sapiens	122-128
6883717-4	1983	Based on the fact that protamine sulfate did not show any direct action on the antithrombin III molecule, the presence of AT III with progressive activity was considered to play an important role in the rebound phenomenon of heparin after heparin neutralization with protamine sulfate.	Heparin	239-246	serpin family C member 1	Homo sapiens	122-128
7706485-7	1995	Full-length 125I-TFPI binding to hepatoma cells could be inhibited &gt; 90% by heparin and other highly charged molecules.	Heparin	79-86	tissue factor pathway inhibitor	Homo sapiens	17-21
6622513-5	1983	When rat lungs were perfused in situ with heparin, 49% of the total lipoprotein lipase activity was released into the perfusate.	Heparin	42-49	lipase G, endothelial type	Rattus norvegicus	80-86
6464516-3	1984	- The sensitivity of the functional AT III test for the recognition of increased heparin tolerances is quite satisfactory, and the test for the answer of this questioning also suitable and more sensitive than the immunological proof method.	Heparin	81-88	serpin family C member 1	Homo sapiens	36-42
6740557-1	1984	A preparation of heparin was separated by affinity chromatography into two fractions: one of high ( HAH ) and the other of low (LAH) affinity to antithrombin III.	Heparin	17-24	desmoglein 4	Homo sapiens	128-131
6740557-1	1984	A preparation of heparin was separated by affinity chromatography into two fractions: one of high ( HAH ) and the other of low (LAH) affinity to antithrombin III.	Heparin	17-24	serpin family C member 1	Homo sapiens	145-161
6321520-6	1984	However, the inhibitory effect of fibronectin was greatly enhanced by adding the protein together with heparin, heparan sulfate, collagen, or a fibronectin-binding collagen peptide (CB-7), which is consistent with an "activation" of fibronectin on binding to these matrix components.	Heparin	103-110	fibronectin 1	Rattus norvegicus	34-45
6856582-3	1983	This method, which involves affinity chromatography with heparin-Sepharose, ion exchange chromatography using DEAE-Sepharose, and Sephadex G-100 gel chromatography, results in purified, functionally active AT III with a 39% yield.	Heparin	57-64	antithrombin-III	Cavia porcellus	206-212
6218503-6	1983	This fragment contains the gelatin binding site and the strong heparin binding site present in fibronectin.	Heparin	63-70	fibronectin 1	Bos taurus	95-106
7722640-6	1995	The ATP-evoked Ca2+ response was blocked by the IP3 receptor antagonist heparin, applied intracellularly, but not by N-desulfated heparin, which is not an antagonist at these receptors.	Heparin	72-79	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	48-60
6344178-2	1983	Although heparin activates ATIII, thereby accelerating its consumption, it cannot increase the overall inhibitory capacity towards coagulation.	Heparin	9-16	serpin family C member 1	Homo sapiens	27-32
6344178-3	1983	The anticoagulant effect of heparin is in relation with the presence of sufficient amounts of ATIII.	Heparin	28-35	serpin family C member 1	Homo sapiens	94-99
6231919-3	1984	This effect of antithrombin III was potentiated by heparin, and to a modest extent by heparan sulphate, cellulose sulphate, dextran sulphate and xylan sulphate.	Heparin	51-58	serpin family C member 1	Homo sapiens	15-31
6420409-5	1984	Modification in the presence of added heparin decreased the extent of labeling by 1-2 mol of pyridoxyl phosphate per mol of antithrombin and protected against the loss of heparin cofactor activity.	Heparin	38-45	serpin family C member 1	Homo sapiens	124-136
6420409-6	1984	To further examine the role of lysine residues in the interaction of antithrombin III with heparin, the protein was singly labeled with pyridoxyl phosphate and affinity fractionated on heparin-agarose.	Heparin	91-98	serpin family C member 1	Homo sapiens	69-85
7890615-6	1995	Using rotation-mediated aggregation assays, we find that aggregation of syndecan-1-transfected cells is dependent on divalent cations and is inhibited by the following: (i) addition of heparin and heparin-like glycosaminoglycans, (ii) removal of heparan sulfate from the cell surface, or (iii) addition of exogenous purified syndecan-1.	Heparin	185-192	syndecan 1	Homo sapiens	72-82
6420409-10	1984	Fluorescence emission spectra of the phosphopyridoxyl-antithrombin derivative that does not bind to heparin-agarose indicated fluorescence energy transfer from tryptophan to the bound phosphopyridoxyl moiety.	Heparin	100-107	serpin family C member 1	Homo sapiens	54-66
6420409-13	1984	255, 824-826) in the heparin-binding domain of antithrombin III.	Heparin	21-28	serpin family C member 1	Homo sapiens	47-63
7140568-1	1982	Haemodialysis had become impossible or possible only using high doses of heparin in 20 patients with dialysis-dependent renal insufficiency due to lowering of antithrombin III (AT III).	Heparin	73-80	serpin family C member 1	Homo sapiens	159-175
7140568-1	1982	Haemodialysis had become impossible or possible only using high doses of heparin in 20 patients with dialysis-dependent renal insufficiency due to lowering of antithrombin III (AT III).	Heparin	73-80	serpin family C member 1	Homo sapiens	177-183
7140568-6	1982	Dialysis was performed with continuous substitution of the AT III-heparin-complex in 6 patients prone to haemorrhage.	Heparin	66-73	serpin family C member 1	Homo sapiens	59-65
6208738-14	1984	This is the first AT III abnormality to show an abnormal crossed-immunoelectrophoresis in the absence of heparin.	Heparin	105-112	serpin family C member 1	Homo sapiens	18-24
7890615-6	1995	Using rotation-mediated aggregation assays, we find that aggregation of syndecan-1-transfected cells is dependent on divalent cations and is inhibited by the following: (i) addition of heparin and heparin-like glycosaminoglycans, (ii) removal of heparan sulfate from the cell surface, or (iii) addition of exogenous purified syndecan-1.	Heparin	185-192	syndecan 1	Homo sapiens	325-335
7890615-6	1995	Using rotation-mediated aggregation assays, we find that aggregation of syndecan-1-transfected cells is dependent on divalent cations and is inhibited by the following: (i) addition of heparin and heparin-like glycosaminoglycans, (ii) removal of heparan sulfate from the cell surface, or (iii) addition of exogenous purified syndecan-1.	Heparin	197-204	syndecan 1	Homo sapiens	72-82
6294139-5	1982	On the basis of its ability to form a complex with radiolabeled APC, the APC-binding protein was purified to homogeneity from normal human plasma by ammonium sulfate fractionation, heparin-agarose chromatography, and QAE-Sephadex A-50 chromatography.	Heparin	181-188	microtubule associated protein RP/EB family member 3	Homo sapiens	73-92
7890615-6	1995	Using rotation-mediated aggregation assays, we find that aggregation of syndecan-1-transfected cells is dependent on divalent cations and is inhibited by the following: (i) addition of heparin and heparin-like glycosaminoglycans, (ii) removal of heparan sulfate from the cell surface, or (iii) addition of exogenous purified syndecan-1.	Heparin	197-204	syndecan 1	Homo sapiens	325-335
6375273-5	1984	S-ASAT and S-gamma-GT increased significantly during heparin treatment, but did not differ significantly from the values of the TED group.	Heparin	53-60	ATP binding cassette subfamily B member 7	Homo sapiens	2-6
7662509-9	1995	In both beta 2AR- and beta 1AR-expressing cells, heparin inhibited the reduction in Vmax and the PKA inhibitor blocked the increase in EC50.	Heparin	49-56	adrenoceptor beta 1	Homo sapiens	22-30
6735277-8	1984	The extra antithrombin III that is added in the assays had to be freed of heparin neutralising activity to obtain reliable estimates of the heparin concentration in the low range (0-200 U/l).	Heparin	140-147	serpin family C member 1	Homo sapiens	10-26
6198531-8	1984	The therapeutic effects of heparin were assessed by prolonged APTT (45-250 sec) and elevated Anti-FXa activity (0.2-1.2 u/ml of plasma heparin concentration) as an indicator for the evaluation of anticoagulation activity and by normalized FPA, Fbg, FDP, Plg and AT III as an indicator for evaluation of antithrombolic activity.	Heparin	27-34	serpin family C member 1	Homo sapiens	262-268
7139957-0	1982	Some examples of the clinical importance of the basic and heparin-induced phospholipase A in human plasma.	Heparin	58-65	phospholipase A and acyltransferase 1	Homo sapiens	74-89
7852412-0	1995	CXC chemokines connective tissue activating peptide-III and neutrophil activating peptide-2 are heparin/heparan sulfate-degrading enzymes.	Heparin	96-103	pro-platelet basic protein	Homo sapiens	15-55
6756395-0	1982	The storage and synthetic pools of heparin-releasable lipoprotein lipase and hepatic triacylglycerol lipase in the growing puppy.	Heparin	35-42	lipoprotein lipase	Homo sapiens	54-72
6812640-1	1982	Whole-irradiated rabbit pre-heparin plasma had an important inhibitory effect on hepatic triacylglycerol lipase and lipoprotein lipase activities, whereas control rabbit pre-heparin plasma slightly inhibited hepatic triacylglycerol lipase activity at a high concentration and enhanced lipoprotein lipase activity.	Heparin	28-35	lipoprotein lipase	Oryctolagus cuniculus	116-134
6811862-1	1982	A murine BALB/c IgG2a (lambda 3) myeloma immunoglobulin SAPC-15 with binding activity for negatively charged polysaccharides has been purified by affinity chromatography, and its interaction with heparin and various other polyanionic antigens has been studied.	Heparin	196-203	immunoglobulin heavy variable V1-9	Mus musculus	16-21
7082587-6	1982	In the presence of heparin, two peaks of AT III were observed in the patients" plasmas: the mobility of one peak was similar to that of the control, whereas the other showed a decreased mobility, suggesting a lack of binding to heparin.	Heparin	19-26	serpin family C member 1	Homo sapiens	41-47
6896131-3	1982	These findings include the following: (1) On the vascular endothelium, a cofactor for antithrombin III (with an activity comparable to stationary phase heparin) catalyzes thrombin inhibition in vivo.	Heparin	152-159	serpin family C member 1	Homo sapiens	86-102
6382162-2	1984	There is now considerable evidence that the antithrombotic and the hemorrhagic effects of heparin can be dissociated by using low molecular weight heparins, and heparinoids, and by using heparin with low affinity to AT III.	Heparin	90-97	serpin family C member 1	Homo sapiens	216-222
6473093-1	1984	In order to investigate the specificity of heparin-antithrombin binding and to precisely define the nature of the structural requirements in heparin, we have synthesized several oligosaccharides and have assessed their affinity for antithrombin.	Heparin	43-50	serpin family C member 1	Homo sapiens	51-63
6643505-0	1983	A simple rate law that describes the kinetics of the heparin-catalyzed reaction between antithrombin III and thrombin.	Heparin	53-60	serpin family C member 1	Homo sapiens	88-104
6643505-1	1983	The kinetics of the reaction between human thrombin and antithrombin III were studied in the presence of heparin fractionated according to its molecular size and affinity for antithrombin III.	Heparin	105-112	serpin family C member 1	Homo sapiens	56-72
6643505-1	1983	The kinetics of the reaction between human thrombin and antithrombin III were studied in the presence of heparin fractionated according to its molecular size and affinity for antithrombin III.	Heparin	105-112	serpin family C member 1	Homo sapiens	175-191
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	20-27	serpin family C member 1	Homo sapiens	269-285
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	20-27	serpin family C member 1	Homo sapiens	388-404
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	269-285
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	388-404
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	269-285
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	388-404
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	269-285
6643505-7	1983	The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	388-404
6607710-0	1983	Antithrombin in vertebrate species: conservation of the heparin-dependent anticoagulant mechanism.	Heparin	56-63	serpin family C member 1	Homo sapiens	0-12
7852412-0	1995	CXC chemokines connective tissue activating peptide-III and neutrophil activating peptide-2 are heparin/heparan sulfate-degrading enzymes.	Heparin	96-103	pro-platelet basic protein	Homo sapiens	60-91
6607710-1	1983	Heparin is thought to regulate the rate of mammalian blood clotting by enhancing the activity of antithrombin, an inhibitor of coagulation enzymes.	Heparin	0-7	serpin family C member 1	Homo sapiens	97-109
6607710-4	1983	The purified vertebrate inhibitors all show the following physical and functional homologies to human antithrombin: (i) heparin-enhanced inhibition of both bovine thrombin and human Factor Xa, (ii) molecular masses of approximately 60,000, and (iii) heparin-induced increases in ultraviolet fluorescence.	Heparin	120-127	serpin family C member 1	Homo sapiens	102-114
7066204-6	1982	This discrepancy was associated with the presence in the patient"s plasma of an AT III fraction showing a slower mobility than the main AT III peak on two-dimensional immunoelectrophoresis in the presence of heparin.	Heparin	208-215	serpin family C member 1	Homo sapiens	80-86
6175043-0	1982	Antithrombin BM from human plasma: an antithrombin binding moderately to heparin.	Heparin	73-80	serpin family C member 1	Homo sapiens	0-12
6175043-0	1982	Antithrombin BM from human plasma: an antithrombin binding moderately to heparin.	Heparin	73-80	serpin family C member 1	Homo sapiens	38-50
6175043-3	1982	Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column.	Heparin	93-100	serpin family C member 1	Homo sapiens	117-129
6175043-3	1982	Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column.	Heparin	157-164	serpin family C member 1	Homo sapiens	117-129
6175043-3	1982	Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column.	Heparin	157-164	serpin family C member 1	Homo sapiens	117-129
6175043-5	1982	From AT III, AT BM further differs in its absolute dependency on the presence of heparin(oids) for antithrombin activity, in its more pronounced inhibitory specificity largely restricted to thrombin, and in the absence of substantial immunological crossreaction with antibody to AT III.	Heparin	81-88	serpin family C member 1	Homo sapiens	99-111
6607710-4	1983	The purified vertebrate inhibitors all show the following physical and functional homologies to human antithrombin: (i) heparin-enhanced inhibition of both bovine thrombin and human Factor Xa, (ii) molecular masses of approximately 60,000, and (iii) heparin-induced increases in ultraviolet fluorescence.	Heparin	250-257	serpin family C member 1	Homo sapiens	102-114
6607710-5	1983	Also, the heparin-binding interaction of vertebrate antithrombins is highly selective with each demonstrating the same rigid specificity for heparin species fractionated on the basis of their affinity for human antithrombin.	Heparin	10-17	serpin family C member 1	Homo sapiens	52-64
6607710-5	1983	Also, the heparin-binding interaction of vertebrate antithrombins is highly selective with each demonstrating the same rigid specificity for heparin species fractionated on the basis of their affinity for human antithrombin.	Heparin	141-148	serpin family C member 1	Homo sapiens	52-64
6640109-0	1983	Antithrombin "Chicago": a functionally abnormal molecule with increased heparin affinity causing familial thrombophilia.	Heparin	72-79	serpin family C member 1	Homo sapiens	0-12
6640109-7	1983	The abnormal antithrombin ("Chicago") was found to elute from heparin-Sepharose at a higher ionic strength than normal inhibitor.	Heparin	62-69	serpin family C member 1	Homo sapiens	13-25
6640109-8	1983	The functionally defective antithrombin molecules exhibit a reduced ability to neutralize thrombin in the presence or absence of heparin (approximately 10%-20% of normal).	Heparin	129-136	serpin family C member 1	Homo sapiens	27-39
7053378-0	1982	Heparin with two binding sites for antithrombin or platelet factor 4.	Heparin	0-7	serpin family C member 1	Homo sapiens	35-47
7053378-6	1982	The stoichiometries of interaction of antithrombin and platelet factor 4 with HMW highly active heparin as determined by fluorescence spectroscopy indicated that 2 molecules of either protein are able to bind to 1 molecule of the mucopolysaccharide.	Heparin	96-103	serpin family C member 1	Homo sapiens	38-50
7053378-7	1982	These studies also reveal that the binding of antithrombin to HMW highly active heparin is characterized by KDISSHAT = 5.0 X 10(-8) M and KDISSHAT2 = 1.0 x 10(-7) M, respectively.	Heparin	80-87	serpin family C member 1	Homo sapiens	46-58
6643466-12	1983	On the basis of these data, the binding of heparin to antithrombin III is interpreted in terms of a two-step mechanism.	Heparin	43-50	serpin family C member 1	Homo sapiens	54-70
7740509-0	1995	TFPI antigen levels in normal human volunteers after intravenous and subcutaneous administration of unfractionated heparin and a low molecular weight heparin.	Heparin	115-122	tissue factor pathway inhibitor	Homo sapiens	0-4
7159223-1	1982	Lipoprotein lipase activity was measured in heparin extracts of aortic intima and adventitia from normal and cholesterol-fed turkeys.	Heparin	44-51	lipoprotein lipase	Meleagris gallopavo	0-18
7740509-0	1995	TFPI antigen levels in normal human volunteers after intravenous and subcutaneous administration of unfractionated heparin and a low molecular weight heparin.	Heparin	150-157	tissue factor pathway inhibitor	Homo sapiens	0-4
7116792-5	1982	The haemorrhagic risk of continuing modest doses of heparin with high dose ATIII therapy appears small.	Heparin	52-59	serpin family C member 1	Homo sapiens	75-80
6670740-3	1983	Several hearts could be sequentially perfused with the same heparin solution to enrich it in lipase activity.	Heparin	60-67	lipase G, endothelial type	Rattus norvegicus	93-99
7740509-1	1995	Tissue factor pathway inhibitor (TFPI) is an important mediator of the in vivo anticoagulant/antithrombotic properties of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	137-144	tissue factor pathway inhibitor	Homo sapiens	0-31
7740509-1	1995	Tissue factor pathway inhibitor (TFPI) is an important mediator of the in vivo anticoagulant/antithrombotic properties of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	137-144	tissue factor pathway inhibitor	Homo sapiens	33-37
6651612-6	1983	Baseline apolipoprotein B, 124 mg/dl and apolipoprotein C-III (heparin precipitate) 5.6 mg/dl were decreased 40 mg/dl (31%) and 2.4 mg/dl (41%) respectively.	Heparin	63-70	apolipoprotein C3	Homo sapiens	41-61
7740509-1	1995	Tissue factor pathway inhibitor (TFPI) is an important mediator of the in vivo anticoagulant/antithrombotic properties of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	146-149	tissue factor pathway inhibitor	Homo sapiens	0-31
7740509-1	1995	Tissue factor pathway inhibitor (TFPI) is an important mediator of the in vivo anticoagulant/antithrombotic properties of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	146-149	tissue factor pathway inhibitor	Homo sapiens	33-37
6176454-8	1982	There was also a weak but statistically significant positive correlation between plasma concentrations of alpha 2 macroglobulin and baseline APTT values (0.02 greater than 0 greater than 0.01) and slope values of the ln APTT vs heparin curves (0.02 greater than p greater than 0.01).	Heparin	228-235	alpha-2-macroglobulin	Homo sapiens	106-127
7740509-1	1995	Tissue factor pathway inhibitor (TFPI) is an important mediator of the in vivo anticoagulant/antithrombotic properties of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	176-183	tissue factor pathway inhibitor	Homo sapiens	0-31
6579053-1	1983	Four criteria were used to examine serum-free conditioned cell culture medium for protease nexin (PN):(1) formation of SDS-stable approximately 77 K Da complexes between a medium component and [125I]thrombin; (2) acceleration by heparin of the rate of formation of these complexes; (3) cellular binding of these complexes; and (4) inhibition by heparin of the cellular binding of complexes.	Heparin	229-236	serpin family E member 2	Homo sapiens	82-104
7740509-1	1995	Tissue factor pathway inhibitor (TFPI) is an important mediator of the in vivo anticoagulant/antithrombotic properties of unfractionated heparin (UFH) and low molecular weight heparin (LMWH).	Heparin	176-183	tissue factor pathway inhibitor	Homo sapiens	33-37
6631483-10	1983	Treatment of HEMA/ fibronectin gels with heparin or incorporation of heparin along with fibronectin in the gel profoundly diminished the efficacy of fibronectin in supporting nerve fiber growth.	Heparin	41-48	fibronectin 1	Gallus gallus	19-30
7117919-0	1982	Pregnancy in women with congenital antithrombin III deficiency: experience of treatment with heparin and antithrombin.	Heparin	93-100	serpin family C member 1	Homo sapiens	35-47
7064387-0	1982	[Lipoprotein lipase and liver triglyceride lipase in blood plasma of rabbits and rats subjected to heparin administration].	Heparin	99-106	lipoprotein lipase	Oryctolagus cuniculus	1-19
7308558-0	1981	The antithrombin-binding sequence of heparin.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
7740509-2	1995	The vascular pool of TFPI is released into the circulation after intravenous and subcutaneous administration of both UFH and LMWH.	Heparin	117-120	tissue factor pathway inhibitor	Homo sapiens	21-25
7740509-4	1995	Our results demonstrate that the TFPI antigen levels increase upon the intravenous and subcutaneous administration of UFH and Ardeparin.	Heparin	118-121	tissue factor pathway inhibitor	Homo sapiens	33-37
6194790-5	1983	In the presence of saturating concentrations of ATIII and heparin, an apparent first-order rate constant of 6.8 X 10(-1) s-1 was calculated for the inhibition of urokinase.	Heparin	58-65	serpin family C member 1	Homo sapiens	48-53
7740509-7	1995	The plasma concentration of TFPI was increased 0.5-2 fold when UFH or Ardeparin was administered subcutaneously and was 3 fold higher when administered intravenously.	Heparin	63-66	tissue factor pathway inhibitor	Homo sapiens	28-32
7287751-0	1981	Binding of high affinity heparin to antithrombin III.	Heparin	25-32	serpin family C member 1	Homo sapiens	36-52
7813818-10	1995	It can be concluded that TFPI activity, especially after stimulation with heparin, is affected by chronic hyperglycemia in diabetic subjects without vascular complications.	Heparin	74-81	tissue factor pathway inhibitor	Homo sapiens	25-29
7287752-0	1981	Binding of high affinity heparin to antithrombin III.	Heparin	25-32	serpin family C member 1	Homo sapiens	36-52
7287752-2	1981	The kinetics of high affinity heparin binding to human antithrombin III has been studied by stopped flow fluorimetry, using the 40% antithrombin fluorescence enhancement resulting from this interaction.	Heparin	30-37	serpin family C member 1	Homo sapiens	55-71
7287752-2	1981	The kinetics of high affinity heparin binding to human antithrombin III has been studied by stopped flow fluorimetry, using the 40% antithrombin fluorescence enhancement resulting from this interaction.	Heparin	30-37	serpin family C member 1	Homo sapiens	55-67
7287752-3	1981	At mu 0.15, pH 7.4, and 25 degrees C, the observed pseudo-first order rate constant varies hyperbolically with heparin concentration with a limiting rate constant of 440 +/- 90 s-1, demonstrating that heparin binding is a two-step process involving a conformational change in antithrombin III.	Heparin	111-118	serpin family C member 1	Homo sapiens	276-292
7287752-3	1981	At mu 0.15, pH 7.4, and 25 degrees C, the observed pseudo-first order rate constant varies hyperbolically with heparin concentration with a limiting rate constant of 440 +/- 90 s-1, demonstrating that heparin binding is a two-step process involving a conformational change in antithrombin III.	Heparin	201-208	serpin family C member 1	Homo sapiens	276-292
7287752-4	1981	An identical dependence is produced when antithrombin is varied, consistent with a symmetrical mechanism in which heparin binding induces a conformational change in antithrombin rather than perturbing an equilibrium between two conformational states of the protein.	Heparin	114-121	serpin family C member 1	Homo sapiens	41-53
7287752-4	1981	An identical dependence is produced when antithrombin is varied, consistent with a symmetrical mechanism in which heparin binding induces a conformational change in antithrombin rather than perturbing an equilibrium between two conformational states of the protein.	Heparin	114-121	serpin family C member 1	Homo sapiens	165-177
7287752-5	1981	The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide.	Heparin	55-62	serpin family C member 1	Homo sapiens	42-54
7287752-5	1981	The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide.	Heparin	55-62	serpin family C member 1	Homo sapiens	196-208
6882687-4	1983	These results confirm previous findings of heterogeneity in At III concentrates and show that some concentrates contain substantial amounts of altered At III molecules in which the heparin-binding site has been denatured but the thrombin-neutralizing site left largely intact.	Heparin	181-188	serpin family C member 1	Homo sapiens	151-157
6328252-9	1983	It is difficult to determine the optimal dose of heparin because of decreased antithrombin III and metabolism in the liver due to loss of hepatic parenchyma.	Heparin	49-56	serpin family C member 1	Homo sapiens	78-94
6577437-6	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and heparin cofactor II/thrombin reactions differed in terms of apparent Vmax and apparent heparin-inhibitor dissociation constant values.	Heparin	31-38	serpin family C member 1	Homo sapiens	49-65
7287752-5	1981	The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide.	Heparin	147-154	serpin family C member 1	Homo sapiens	42-54
7287752-5	1981	The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide.	Heparin	147-154	serpin family C member 1	Homo sapiens	42-54
7897316-8	1994	HDL density profiles of the study groups prior to the administration of heparin demonstrated two distinct peaks at density 1.09 g/ml (HDL2) and 1.13 g/ml (HDL3).	Heparin	72-79	junctophilin 3	Homo sapiens	134-138
7287752-9	1981	A major function of the conformational change is, thus, to increase the affinity of heparin for antithrombin III greater than 300-fold.	Heparin	84-91	serpin family C member 1	Homo sapiens	96-112
7287752-10	1981	The implications of these findings for the mechanism of the heparin-catalyzed inhibition of coagulation proteases by antithrombin III are discussed.	Heparin	60-67	serpin family C member 1	Homo sapiens	117-133
6885772-0	1983	The antithrombin-binding sequence in heparin.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
6885772-7	1983	It is concluded that the 6-sulfate group on the N-acetylglucosamine residue is of critical importance to the interaction between heparin and antithrombin.	Heparin	129-136	serpin family C member 1	Homo sapiens	141-153
7897316-9	1994	However, after the administration of heparin to the HTG group, only a single peak in the HDL profile was evident that was located at the density region corresponding to HDL2 (1.09 g/ml).	Heparin	37-44	junctophilin 3	Homo sapiens	169-173
7896734-7	1994	On the other hand, basic FGF (bFGF) scarcely bound to nucleolin in the absence of heparin, while both MK and bFGF bound weakly to nucleolin in the presence of heparin.	Heparin	159-166	midkine	Mus musculus	102-104
6410910-10	1983	AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump.	Heparin	72-79	serpin family C member 1	Homo sapiens	0-6
6410910-10	1983	AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump.	Heparin	106-113	serpin family C member 1	Homo sapiens	0-6
6410910-11	1983	The AT III heparin affinity fraction showed primarily a fast component.	Heparin	11-18	serpin family C member 1	Homo sapiens	4-10
6879278-1	1983	A patient with antithrombin III (ATT) deficiency after arterial embolism manifested an increasing requirement for heparin to adjust a partial thromboplastin time.	Heparin	114-121	serpin family C member 1	Homo sapiens	15-31
6879278-1	1983	A patient with antithrombin III (ATT) deficiency after arterial embolism manifested an increasing requirement for heparin to adjust a partial thromboplastin time.	Heparin	114-121	serpin family C member 1	Homo sapiens	33-36
6949499-4	1981	The activity of AT III, a progressive inhibitor of thrombin and cofactor of heparin, is always below 50% after L-asparaginase.	Heparin	76-83	serpin family C member 1	Homo sapiens	16-22
6976931-2	1981	In the first step the method exploits the affinity of C1q for heparin and in the second the interaction between C1q and IgG.	Heparin	62-69	complement C1q A chain	Homo sapiens	54-57
7029926-4	1981	In contrast to liver cirrhosis and proteinuria, in septicaemia (33 patients) the ratio between AT III antigen (radial immunodiffusion) and functional AT III (heparin cofactor assay using a chromogenic substrate) demonstrated an excess of AT III antigen probably due to inactive AT III-enzyme complexes.	Heparin	158-165	serpin family C member 1	Homo sapiens	150-156
7029926-4	1981	In contrast to liver cirrhosis and proteinuria, in septicaemia (33 patients) the ratio between AT III antigen (radial immunodiffusion) and functional AT III (heparin cofactor assay using a chromogenic substrate) demonstrated an excess of AT III antigen probably due to inactive AT III-enzyme complexes.	Heparin	158-165	serpin family C member 1	Homo sapiens	150-156
7029926-4	1981	In contrast to liver cirrhosis and proteinuria, in septicaemia (33 patients) the ratio between AT III antigen (radial immunodiffusion) and functional AT III (heparin cofactor assay using a chromogenic substrate) demonstrated an excess of AT III antigen probably due to inactive AT III-enzyme complexes.	Heparin	158-165	serpin family C member 1	Homo sapiens	150-156
6135060-0	1983	Effective prophylaxis with oral anticoagulants and low-dose heparin during pregnancy in an antithrombin III deficient woman.	Heparin	60-67	serpin family C member 1	Homo sapiens	91-107
7896734-7	1994	On the other hand, basic FGF (bFGF) scarcely bound to nucleolin in the absence of heparin, while both MK and bFGF bound weakly to nucleolin in the presence of heparin.	Heparin	159-166	fibroblast growth factor 2	Mus musculus	109-113
7859927-3	1994	N-Terminal and tryptic peptide fragment analysis of these polypeptides revealed that they are identical to midkine (MK) and pleiotrophin (PTN), respectively, which form a new family of heparin-binding growth/differentiation factors.	Heparin	185-192	midkine	Bos taurus	107-114
6636046-6	1983	These results suggest that in antithrombin III Toyama an amino acid residue at the heparin-binding site has been replaced by less basic or more acidic one which has no ability to interact with heparin, resulting in a loss of heparin cofactor activity of this protein.	Heparin	83-90	serpin family C member 1	Homo sapiens	30-46
6636046-6	1983	These results suggest that in antithrombin III Toyama an amino acid residue at the heparin-binding site has been replaced by less basic or more acidic one which has no ability to interact with heparin, resulting in a loss of heparin cofactor activity of this protein.	Heparin	193-200	serpin family C member 1	Homo sapiens	30-46
6851887-0	1983	[Perioperative plasma-antithrombin activity during low-dose heparin prophylaxis].	Heparin	60-67	serpin family C member 1	Homo sapiens	22-34
7330836-0	1981	Studies on the neutralizing mechanism of antithrombin activity of heparin by protamine.	Heparin	66-73	serpin family C member 1	Homo sapiens	41-53
7859927-3	1994	N-Terminal and tryptic peptide fragment analysis of these polypeptides revealed that they are identical to midkine (MK) and pleiotrophin (PTN), respectively, which form a new family of heparin-binding growth/differentiation factors.	Heparin	185-192	midkine	Bos taurus	116-118
7900087-0	1994	Evolution of antibodies anti-PF4/heparin in a patient with a history of heparin-induced thrombocytopenia reexposed to heparin.	Heparin	72-79	platelet factor 4	Homo sapiens	29-32
6412390-5	1983	The increase in lipoprotein lipase activity in SSHA patients 2 hours after injection was significantly greater than in heparin patients.	Heparin	119-126	lipoprotein lipase	Homo sapiens	16-34
6412390-7	1983	The results indicate a difference in the effect on lipoprotein lipase release between heparin and SSHA at the used dosage schedules.	Heparin	86-93	lipoprotein lipase	Homo sapiens	51-69
7925941-5	1994	The binding of laminin and merosin is Ca2+ dependent and is inhibited by NaCl and heparin.	Heparin	82-89	laminin, alpha 2	Mus musculus	27-34
6223404-4	1983	Heparin, complexed with LDL, retains its enhancing effect on the rate of thrombin and plasmin inactivation by antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	110-126
7316178-0	1981	A method for rapid quantitation and preparation of antithrombin III--high-affinity heparin fractions.	Heparin	83-90	serpin family C member 1	Homo sapiens	51-67
7272219-3	1981	Their half-time of AT III elimination was 8.4--13.6 h. The patient in whom AT III concentrate was injected at the start of heparin therapy showed a very rapid decrease of AT III activity with a three-fold increase in the elimination rate constant.	Heparin	123-130	serpin family C member 1	Homo sapiens	75-81
6832369-0	1983	Heparin solubilizes asymmetric acetylcholinesterase from rat neuromuscular junction.	Heparin	0-7	acetylcholinesterase	Rattus norvegicus	31-51
8078949-2	1994	HL was detected in the plasma of all rabbits only after the administration of heparin; HL activity in transgenic rabbits was found at levels up to 80-fold greater than that in nontransgenic littermates.	Heparin	78-85	hepatic triacylglycerol lipase	Oryctolagus cuniculus	0-2
6832369-2	1983	Here, we report studies showing that heparin, a sulfated glycosaminoglycan, specifically solubilized AChE from endplate regions of rat diaphragm muscle.	Heparin	37-44	acetylcholinesterase	Rattus norvegicus	101-105
6832369-3	1983	Of the several molecular forms of AChE present in that region, heparin only released the asymmetric A12 and A8 forms of the enzyme.	Heparin	63-70	acetylcholinesterase	Rattus norvegicus	34-38
6832369-4	1983	Our results strongly support the involvement of heparin-like macromolecules in the in vivo immobilization of the collagen-tailed forms of AChE to the basal lamina of the neuromuscular junction.	Heparin	48-55	acetylcholinesterase	Rattus norvegicus	138-142
6831687-3	1983	In the AT III assay the sample is incubated with excess thrombin and heparin to form the functionally inactive AT III-thrombin complex.	Heparin	69-76	serpin family C member 1	Homo sapiens	7-13
7026867-1	1981	The paper contains new data on the pharmacodynamics of heparin and its interaction with the Xa factor, antithrombin III and thrombin.	Heparin	55-62	serpin family C member 1	Homo sapiens	103-119
6831687-3	1983	In the AT III assay the sample is incubated with excess thrombin and heparin to form the functionally inactive AT III-thrombin complex.	Heparin	69-76	serpin family C member 1	Homo sapiens	111-117
6833231-6	1983	The mechanism of the interaction between histidine-rich glycoprotein and heparin appeared to be different from that between antithrombin III and heparin, since the former is abolished by EDTA and occurs both with heparin molecules having a high affinity or a low affinity for antithrombin III.	Heparin	73-80	serpin family C member 1	Homo sapiens	276-292
8070564-6	1994	This value remained constant in swim-up sperm and decreased to (7.7 +/- 0.4) x 10(6)/spermatozoon after incubation for 24 h in capacitation medium at 39 degrees C. These data substantiate the hypothesis that PDC-109 may be one of the seminal plasma components that enhance the fertilizing capacity of bull spermatozoa upon interaction with heparin-like glycosaminoglycans present in the female genital tract.	Heparin	340-347	seminal plasma protein PDC-109	Bos taurus	208-215
6602754-5	1983	This reaction was complete after 15 s and is comparable with the fast heparin induced formation of modified antithrombin III.	Heparin	70-77	serpin family C member 1	Homo sapiens	108-124
8067851-3	1994	In both groups, significant complement activation was observed after the onset of cardiopulmonary bypass, but the maximum levels of C3b, iC3b, and C3c and the terminal C5b-9 complement complex were significantly lower in the heparin-coated group.	Heparin	225-232	endogenous retrovirus group K member 3	Homo sapiens	132-135
6187377-5	1983	About 80% of the lipoprotein lipase activity from all three lines was present in the medium and 50-70% of cellular activity could be released into the medium by a 3-min exposure to heparin.	Heparin	181-188	lipoprotein lipase	Homo sapiens	17-35
7822240-5	1994	Apolipoprotein (apo) E-free HDL2 from the patients, separated by heparin-Sepharose column chromatography, was rich in CE, poor in triglycerides (TG), and enlarged in size on 4-30% nondenaturing polyacrylamide gradient gel electrophoresis.	Heparin	65-72	junctophilin 3	Homo sapiens	28-32
8031770-5	1994	A positively charged ring of lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding.	Heparin	153-160	platelet factor 4	Homo sapiens	75-78
6830263-0	1983	Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation.	Heparin	74-81	serpin family C member 1	Homo sapiens	44-60
6830263-1	1983	Heparin accelerates the rate of inhibition of thrombin by antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	58-74
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	60-67	plasminogen	Homo sapiens	294-301
8011637-10	1994	Heparin was also found to potentiate the ability of wild-type glia-derived nexin to inhibit the thrombin-induced retraction of neurites from neuroblastoma NB2a cells.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade E, member 2	Mus musculus	62-80
6860684-7	1983	Attachment of lipoprotein lipase to the cell surface was mandatory for the transfer of cholesteryl ether and could be prevented by heparin.	Heparin	131-138	lipoprotein lipase	Homo sapiens	14-32
8086755-9	1994	In addition, ECGF reversed the inhibitory effect of heparin.	Heparin	52-59	fibroblast growth factor 1	Bos taurus	13-17
6822493-5	1983	Differences between thrombin and Factor Xa at low (nanomolar) concentrations of heparin were evident in this rate constant and the relative affinities for the heparin-antithrombin complex (Km for Factor Xa = 100 nM; Km for thrombin less than or equal to 2 nM).	Heparin	80-87	serpin family C member 1	Homo sapiens	167-179
8195119-4	1994	Bound DAO is displaced by heparin with 24-fold greater potency than dextran sulfate, implicating structural specificity of heparin-like glycosaminoglycan moieties as a critical factor in initial receptor/enzyme interaction at fast and slow sites.	Heparin	26-33	amine oxidase copper containing 1	Homo sapiens	6-9
6421075-1	1983	Heparin, sodium butyrate, and the absence of platelet derived factors in the nutrient medium are able to inhibit the decrease of the content of myosin in cultivated arterial smooth muscle cells.	Heparin	0-7	myosin heavy chain 14	Homo sapiens	144-150
8195119-4	1994	Bound DAO is displaced by heparin with 24-fold greater potency than dextran sulfate, implicating structural specificity of heparin-like glycosaminoglycan moieties as a critical factor in initial receptor/enzyme interaction at fast and slow sites.	Heparin	123-130	amine oxidase copper containing 1	Homo sapiens	6-9
8195119-8	1994	In cells plated at high density, half of the bound DAO becomes nondisplaceable by heparin within 15 min at 37 degrees C, a time consistent with receptor internalization, whereas cells plated at low density retain all bound DAO in a heparin-sensitive state.	Heparin	232-239	amine oxidase copper containing 1	Homo sapiens	223-226
6660606-4	1983	Heparin is prescribed as soon as AT III activity reaches 70%.	Heparin	0-7	serpin family C member 1	Homo sapiens	33-39
8180167-9	1994	At the optimal heparin concentration, the value of kass for the acrosin-protein C inhibitor reaction was 230-fold higher ((5.6 +/- 0.1) x 10(7) M-1 s-1) than in the absence of heparin.	Heparin	15-22	serpin family A member 5	Homo sapiens	72-91
6184096-5	1983	Antithrombin-heparin cofactor, which eluted from heparin-agarose with buffer containing 2.0 M NaCl, was functionally and antigenically identified as antithrombin III.	Heparin	13-20	serpin family C member 1	Homo sapiens	149-165
8180167-9	1994	At the optimal heparin concentration, the value of kass for the acrosin-protein C inhibitor reaction was 230-fold higher ((5.6 +/- 0.1) x 10(7) M-1 s-1) than in the absence of heparin.	Heparin	176-183	serpin family A member 5	Homo sapiens	72-91
8180167-10	1994	The results suggest that protein C inhibitor may be important in the physiological control of acrosin activity, particularly where the presence of heparin-like glycosaminoglycans would stimulate the acrosin-protein C inhibitor reaction.	Heparin	147-154	serpin family A member 5	Homo sapiens	25-44
8180167-10	1994	The results suggest that protein C inhibitor may be important in the physiological control of acrosin activity, particularly where the presence of heparin-like glycosaminoglycans would stimulate the acrosin-protein C inhibitor reaction.	Heparin	147-154	serpin family A member 5	Homo sapiens	207-226
6654191-6	1983	A significant decrease in the AT-III level (p less than 0.01) and a significant increase (p less than 0.01) in the fibrinogen level were observed after heparin-dipyridamole treatment of patients suspected of IUGR.	Heparin	152-159	serpin family C member 1	Homo sapiens	30-36
7754532-3	1994	It was originally thought that caffeine acts solely as an agonist for the ryanodine receptor and heparin acts solely as an inhibitor for the IP3 receptor.	Heparin	97-104	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	141-153
6840561-3	1983	The lipoprotein lipase activity was shown after intravenous injection of heparin.	Heparin	73-80	lipoprotein lipase	Homo sapiens	4-22
6961402-0	1982	Circular dichroism spectroscopy of heparin-antithrombin interactions.	Heparin	35-42	serpin family C member 1	Homo sapiens	43-55
6961402-10	1982	The second of these patterns is apparent when octadecasaccharide, low molecular weight heparin (6,500), and high molecular weight heparin (22,000) interact with antithrombin.	Heparin	87-94	serpin family C member 1	Homo sapiens	161-173
6961402-10	1982	The second of these patterns is apparent when octadecasaccharide, low molecular weight heparin (6,500), and high molecular weight heparin (22,000) interact with antithrombin.	Heparin	130-137	serpin family C member 1	Homo sapiens	161-173
7164033-0	1982	Heparin with low affinity to antithrombin III inhibits the activation of prothrombin in normal plasma.	Heparin	0-7	serpin family C member 1	Homo sapiens	29-45
7164033-2	1982	Unfractionated heparin enhances the rates at which antithrombin III inactivates activated clotting factors, and inhibits the activation of both Factor X and prothrombin by disrupting the calcium and phospholipid dependent assembly of the Factor X and prothrombin activator complexes.	Heparin	15-22	serpin family C member 1	Homo sapiens	51-67
6183640-0	1982	[A study of antithrombin systems during heparin therapy].	Heparin	40-47	serpin family C member 1	Homo sapiens	12-24
7754532-5	1994	In the same concentration range, caffeine activates the ryanodine receptor and inhibits the IP3 receptor, and heparin inhibits the IP3 receptor and activates the ryanodine receptor.	Heparin	110-117	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	131-143
6183640-2	1982	A decrease in AT III levels was observed during treatment and found to correlate significantly with heparin plasma levels, but there were no significant changes in alpha 2M and alpha 1 AT levels.	Heparin	100-107	serpin family C member 1	Homo sapiens	14-20
8191560-15	1994	CONCLUSION: The majority of HAT antibodies react with a PF4/heparin complex, but there is strong evidence that other antigens are involved in some patients.	Heparin	60-67	platelet factor 4	Homo sapiens	56-59
7115961-0	1982	Effect of heparin on the inactivation rate of human factor XIa by antithrombin-III.	Heparin	10-17	serpin family C member 1	Homo sapiens	66-82
7115961-2	1982	Although antithrombin-III, an inhibitor of factor XIa, normally accounts for only one-sixth of the plasma inhibitory activity against factor XIa, its effectiveness has been reported to be enhanced by heparin.	Heparin	200-207	serpin family C member 1	Homo sapiens	9-25
7115961-3	1982	We have reinvestigated the ability of heparin to potentiate factor XIa inhibition by both purified antithrombin-III and plasma using synthetic tripeptide amide substrates as well as a coagulant assay.	Heparin	38-45	serpin family C member 1	Homo sapiens	99-115
7115961-7	1982	Only at heparin concentrations of 5 and 10 U/ml, was a 2- and 4-fold increase in the inactivation rate of factor XIa by purified antithrombin III observed.	Heparin	8-15	serpin family C member 1	Homo sapiens	129-145
8144574-5	1994	HGF binding to SM4 was strongly inhibited by dextran sulfate, heparin, and fucoidan, whereas neither keratan sulfate nor hyaluronic acid had any inhibitory activity.	Heparin	62-69	hepatocyte growth factor	Homo sapiens	0-3
7104393-7	1982	The estrogen receptor interacted both with heparin and with DNA covalently coupled to agarose, and was eluted from either column by NaCl.	Heparin	43-50	estrogen receptor 1	Rattus norvegicus	4-21
7104393-8	1982	Chromatography of crude cytosol on heparin-agarose or DNA-agarose lead to an at least 10-fold or 25-fold purification of the estrogen receptor, respectively.	Heparin	35-42	estrogen receptor 1	Rattus norvegicus	125-142
8118960-0	1994	Deregulated expression of the c-myc oncogene abolishes inhibition of proliferation of rat vascular smooth muscle cells by serum reduction, interferon-gamma, heparin, and cyclic nucleotide analogues and induces apoptosis.	Heparin	157-164	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	30-35
7082587-7	1982	The two populations of AT III were separated by affinity chromatography on heparin-agarose.	Heparin	75-82	serpin family C member 1	Homo sapiens	23-29
7082587-10	1982	This familial AT III variant characterized a reduced affinity for heparin is tentatively named "Antithrombin III Paris".	Heparin	66-73	serpin family C member 1	Homo sapiens	14-20
7082587-10	1982	This familial AT III variant characterized a reduced affinity for heparin is tentatively named "Antithrombin III Paris".	Heparin	66-73	serpin family C member 1	Homo sapiens	96-112
7068594-0	1982	The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin.	Heparin	33-40	serpin family C member 1	Homo sapiens	51-63
7068594-1	1982	The heparin-catalyzed inactivation of thrombin by antithrombin was examined using saturation kinetics and fractional reaction lifetimes.	Heparin	4-11	serpin family C member 1	Homo sapiens	50-62
7514059-2	1994	We provide evidence that, similar to vitronectin, one of these proteins, PVN1 (plant vitronectin-like 1), isolated from 428 mM NaCl-adapted tobacco cells binds to glass surfaces an heparin.	Heparin	181-188	elongation factor 1-alpha	Nicotiana tabacum	73-77
7068594-2	1982	Based solely on kinetic analysis, the reaction binding sequence was determined to be heparin binding to antithrombin followed by binding of thrombin.	Heparin	85-92	serpin family C member 1	Homo sapiens	104-116
7095150-0	1982	The N-terminal sequence of human plasma histidine-rich glycoprotein homologous to antithrombin with high affinity for heparin.	Heparin	118-125	serpin family C member 1	Homo sapiens	82-94
8191407-7	1994	High heparin concentrations released PF4 in a dose dependent manner from microtiter plates if PF4/heparin, but not if PF4 alone, was covalently linked.	Heparin	5-12	platelet factor 4	Homo sapiens	37-40
7112512-1	1982	The role of antithrombin III (AT III) in heparin-induced potentiation of platelet aggregation was investigated using purified AT III and AT III depleted plasma.	Heparin	41-48	serpin family C member 1	Homo sapiens	12-28
7112512-1	1982	The role of antithrombin III (AT III) in heparin-induced potentiation of platelet aggregation was investigated using purified AT III and AT III depleted plasma.	Heparin	41-48	serpin family C member 1	Homo sapiens	30-36
7112512-4	1982	When purified AT III was added to AT III depleted plasma at a concentration of 20 microgram/ml, potentiation of platelet aggregation by heparin was clearly demonstrated.	Heparin	136-143	serpin family C member 1	Homo sapiens	14-20
7112512-4	1982	When purified AT III was added to AT III depleted plasma at a concentration of 20 microgram/ml, potentiation of platelet aggregation by heparin was clearly demonstrated.	Heparin	136-143	serpin family C member 1	Homo sapiens	34-40
7112512-5	1982	These results suggest that the effect of heparin on platelet aggregation is also mediated by AT III.	Heparin	41-48	serpin family C member 1	Homo sapiens	93-99
8191407-7	1994	High heparin concentrations released PF4 in a dose dependent manner from microtiter plates if PF4/heparin, but not if PF4 alone, was covalently linked.	Heparin	5-12	platelet factor 4	Homo sapiens	94-97
7112514-2	1982	The experiments (thrombin and Factor Xa inactivation, heparin affinity chromatography, modified two dimensional immunoelectrophoresis and gel filtration) showed a distinct difference between the two antithrombin III anomalies.	Heparin	54-61	serpin family C member 1	Homo sapiens	199-215
6792876-0	1981	Effect of intrapulmonary heparin on plasma diamine oxidase (histaminase) activity in mice.	Heparin	25-32	amine oxidase, copper-containing 1	Mus musculus	43-58
7101237-5	1982	Neutralization of heparin by PF4 and PS probably proceeds by similar mechanisms, but the details of structure outside the antithrombin III-binding oligosaccharide of heparin may enter in differently.	Heparin	166-173	serpin family C member 1	Homo sapiens	122-138
6792876-0	1981	Effect of intrapulmonary heparin on plasma diamine oxidase (histaminase) activity in mice.	Heparin	25-32	amine oxidase, copper-containing 1	Mus musculus	60-71
6792876-3	1981	In this study we have examined the effect of intrapulmonary administration of heparin on plasma DAO activity in mice.	Heparin	78-85	amine oxidase, copper-containing 1	Mus musculus	96-99
7317012-0	1981	Heparin-releasable lipase activity of rat adrenals, ovaries and testes.	Heparin	0-7	lipase G, endothelial type	Rattus norvegicus	19-25
7317012-7	1981	The lipase activity of adrenals and of ovaries was largely releasable from these organs by heparin and could be inhibited by an antibody against heparin-releasable liver lipase.	Heparin	91-98	lipase G, endothelial type	Rattus norvegicus	4-10
6461438-6	1982	Antithrombin III activity could be determined with 2 microliter of human plasma using human thrombin and heparin as cofactor.	Heparin	105-112	serpin family C member 1	Homo sapiens	0-16
7037067-0	1982	Differential role of fractionated heparin in antithrombin-III proteolysis.	Heparin	34-41	serpin family C member 1	Homo sapiens	45-61
7317012-7	1981	The lipase activity of adrenals and of ovaries was largely releasable from these organs by heparin and could be inhibited by an antibody against heparin-releasable liver lipase.	Heparin	91-98	lipase G, endothelial type	Rattus norvegicus	170-176
8191407-7	1994	High heparin concentrations released PF4 in a dose dependent manner from microtiter plates if PF4/heparin, but not if PF4 alone, was covalently linked.	Heparin	5-12	platelet factor 4	Homo sapiens	94-97
7236529-0	1981	Thrombin-induced proteolysis of human antithrombin III: an outstanding contribution of heparin.	Heparin	87-94	serpin family C member 1	Homo sapiens	38-54
7037067-1	1982	Commercial heparin was fractionated by affinity chromatography on immobilized antithrombin-III (AT-III) into nonbinding (NB), lower affinity (LA), and high affinity (HA) heparin, with specific anticoagulant activity of 9, 205, and 284 U/mg, respectively, Each fraction, in microgram quantities, was examined in the reaction of alpha-thrombin with a molar excess of 125I-labeled AT-III.	Heparin	11-18	serpin family C member 1	Homo sapiens	78-94
7037067-1	1982	Commercial heparin was fractionated by affinity chromatography on immobilized antithrombin-III (AT-III) into nonbinding (NB), lower affinity (LA), and high affinity (HA) heparin, with specific anticoagulant activity of 9, 205, and 284 U/mg, respectively, Each fraction, in microgram quantities, was examined in the reaction of alpha-thrombin with a molar excess of 125I-labeled AT-III.	Heparin	11-18	serpin family C member 1	Homo sapiens	96-102
7037067-3	1982	In the presence of HA heparin, 36% of AT-III participating in the reaction was degraded into a 50,000-dalton inactive fragment.	Heparin	22-29	serpin family C member 1	Homo sapiens	38-44
7236529-1	1981	Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin.	Heparin	96-103	serpin family C member 1	Homo sapiens	40-56
8191407-7	1994	High heparin concentrations released PF4 in a dose dependent manner from microtiter plates if PF4/heparin, but not if PF4 alone, was covalently linked.	Heparin	98-105	platelet factor 4	Homo sapiens	37-40
7236529-1	1981	Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin.	Heparin	96-103	serpin family C member 1	Homo sapiens	58-64
7236529-1	1981	Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin.	Heparin	96-103	serpin family C member 1	Homo sapiens	152-158
8191407-8	1994	Concomitant to the release of PF4, binding of HAT antibodies to PF4/heparin decreased, as indicated by the median optical density (OD) values of OD 0.88 in the presence of buffer compared to OD 0.181 in the presence of 100 IU/ml heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	30-33
7236529-1	1981	Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin.	Heparin	202-209	serpin family C member 1	Homo sapiens	40-56
7236529-1	1981	Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin.	Heparin	202-209	serpin family C member 1	Homo sapiens	58-64
7083257-0	1982	Further characterization of the antithrombin-binding sequence in heparin.	Heparin	65-72	serpin family C member 1	Homo sapiens	32-44
8191407-8	1994	Concomitant to the release of PF4, binding of HAT antibodies to PF4/heparin decreased, as indicated by the median optical density (OD) values of OD 0.88 in the presence of buffer compared to OD 0.181 in the presence of 100 IU/ml heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	64-67
7236529-4	1981	The optimum amount of heparin required to facilitate AT III proteolysis was of 5 microgram/ml (0.8 u/ml).	Heparin	22-29	serpin family C member 1	Homo sapiens	53-59
7236529-5	1981	Excessive reduction of the residual inhibitory activity and changes in two-dimensional immunoelectrophoresis suggested that AT III in plasma is also subjected to nonproductive proteolysis and formation of a modified AT III derivative following addition of thrombin and heparin.	Heparin	269-276	serpin family C member 1	Homo sapiens	124-130
7071806-1	1982	Antithrombin III (AT-III) was isolated by heparin affinity chromatography from adult venous and newborn term and preterm umbilical cord blood.	Heparin	42-49	serpin family C member 1	Homo sapiens	0-16
8191407-8	1994	Concomitant to the release of PF4, binding of HAT antibodies to PF4/heparin decreased, as indicated by the median optical density (OD) values of OD 0.88 in the presence of buffer compared to OD 0.181 in the presence of 100 IU/ml heparin.	Heparin	229-236	platelet factor 4	Homo sapiens	30-33
7071806-1	1982	Antithrombin III (AT-III) was isolated by heparin affinity chromatography from adult venous and newborn term and preterm umbilical cord blood.	Heparin	42-49	serpin family C member 1	Homo sapiens	18-24
7236529-5	1981	Excessive reduction of the residual inhibitory activity and changes in two-dimensional immunoelectrophoresis suggested that AT III in plasma is also subjected to nonproductive proteolysis and formation of a modified AT III derivative following addition of thrombin and heparin.	Heparin	269-276	serpin family C member 1	Homo sapiens	216-222
7236529-6	1981	These data indicate that the effect of heparin on AT III is more complex than generally recognized.	Heparin	39-46	serpin family C member 1	Homo sapiens	50-56
7236529-7	1981	On the one hand, heparin interacting with AT III and thrombin contributes to a rapid binding and neutralization of the enzyme; on the other, heparin facilitates proteolytic degradation of unbound inhibitor even in the presence of small quantities of thrombin accounting for excessive reduction of the overall inhibitory potential of AT III.	Heparin	17-24	serpin family C member 1	Homo sapiens	42-48
8191407-8	1994	Concomitant to the release of PF4, binding of HAT antibodies to PF4/heparin decreased, as indicated by the median optical density (OD) values of OD 0.88 in the presence of buffer compared to OD 0.181 in the presence of 100 IU/ml heparin.	Heparin	229-236	platelet factor 4	Homo sapiens	64-67
7236529-7	1981	On the one hand, heparin interacting with AT III and thrombin contributes to a rapid binding and neutralization of the enzyme; on the other, heparin facilitates proteolytic degradation of unbound inhibitor even in the presence of small quantities of thrombin accounting for excessive reduction of the overall inhibitory potential of AT III.	Heparin	17-24	serpin family C member 1	Homo sapiens	333-339
7245036-8	1981	Antithrombin deficiency should be suspected when there is an unusual propensity to develop thrombus, when heparin cannot prolong coagulation time, and when measurements show reduced levels of antithrombin.	Heparin	106-113	serpin family C member 1	Homo sapiens	0-12
6895615-0	1982	Diagnostic enzymology of alpha-L-iduronidase with special reference to a sulphated disaccharide derived from heparin.	Heparin	109-116	alpha-L-iduronidase	Homo sapiens	25-44
7055531-1	1982	Antithrombin III (At III) levels in plasma samples were determined by incubation of diluted plasma with thrombin, either with or without heparin.	Heparin	137-144	serpin family C member 1	Homo sapiens	0-16
7055531-6	1982	Heat defibrination and ancrod defibrination methods are compared using the amidolytic heparin cofactor assay and it is shown that heat defibrination can cause the loss of nearly 50% of the functional At III in a reconstituted freeze-dried plasma which was used as a standard.	Heparin	86-93	serpin family C member 1	Homo sapiens	200-206
7292454-0	1981	Antithrombin III in patients treated with subcutaneous or intravenous heparin.	Heparin	70-77	serpin family C member 1	Homo sapiens	0-16
8307172-5	1994	Furin was specifically inhibited by alpha 1-antitrypsin Pittsburgh (358 Met--&gt;Arg), (K1/2 = 3 microM) but not by 50 microM normal antitrypsin M or by antithrombin, however, antithrombin/heparin was a good inhibitor (K1/2 = 9 microM).	Heparin	189-196	furin, paired basic amino acid cleaving enzyme	Homo sapiens	0-5
7237831-2	1981	In the same subjects the heparin-releasable lipoprotein lipase activity was assayed from biopsies of adipose tissue and skeletal muscle.	Heparin	25-32	lipoprotein lipase	Homo sapiens	44-62
7238175-1	1981	The low-dose heparin prophylaxis depends upon a low-level activation of antithrombin III to prevent thrombin generation.	Heparin	13-20	serpin family C member 1	Homo sapiens	72-88
6187643-3	1982	Owing to the fact that a certain degree of antithrombin III level can be regarded as a prerequisite for a sufficient heparin effect the missing cofactor, antithrombin III, has to be absolutely substituted, if heparinization is necessary in the newborn period.	Heparin	117-124	serpin family C member 1	Homo sapiens	43-59
6187643-3	1982	Owing to the fact that a certain degree of antithrombin III level can be regarded as a prerequisite for a sufficient heparin effect the missing cofactor, antithrombin III, has to be absolutely substituted, if heparinization is necessary in the newborn period.	Heparin	117-124	serpin family C member 1	Homo sapiens	154-170
8294485-0	1994	Molecular cloning and expression of a glycosaminoglycan N-acetylglucosaminyl N-deacetylase/N-sulfotransferase from a heparin-producing cell line.	Heparin	117-124	sulfotransferase family 1D, member 1	Rattus norvegicus	91-109
7164279-0	1982	Invalidation of concerns with long-term use of heparin: thrombin/antithrombin III interactions.	Heparin	47-54	serpin family C member 1	Homo sapiens	65-81
6462134-4	1981	Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx.	Heparin	0-7	serpin family C member 1	Homo sapiens	90-106
6462134-4	1981	Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx.	Heparin	134-141	serpin family C member 1	Homo sapiens	90-106
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	0-7	serpin family C member 1	Homo sapiens	55-71
6462134-7	1981	Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin.	Heparin	191-198	serpin family C member 1	Homo sapiens	55-71
7213784-1	1981	It was found that lipolytic activity in bovine post-heparin plasma differed from that of other mammalian species by the fact that intravenous heparin induced the release of lipoprotein lipase but not hepatic triacylglycerol lipase.	Heparin	142-149	lipoprotein lipase	Homo sapiens	173-191
8276857-0	1994	Inhibition by heparin of thrombin-catalyzed activation of the factor VIII-von Willebrand factor complex.	Heparin	14-21	coagulation factor VIII	Homo sapiens	62-73
7305940-1	1981	The interaction between bovine antithrombin, a plasma proteinase inhibitor, and heparin species of different molecular weights was studied.	Heparin	80-87	serpin family C member 1	Homo sapiens	31-43
6462134-8	1981	Increasing the concentration of antithrombin III, at a constant amount of heparin, results in increase of the inactivation rate.	Heparin	74-81	serpin family C member 1	Homo sapiens	32-48
6462134-9	1981	By contrast, the effect of increasing the amount of plasmin in the presence of constant amount of heparin and antithrombin III is such that higher plasmin-to-heparin ratios are associated with lower rates of inactivation.	Heparin	158-165	serpin family C member 1	Homo sapiens	110-126
6462134-11	1981	Arrhenius plots of the plasmin-antithrombin III reaction are linear both in the absence and presence of heparin, at concentrations of 1 or 2mug/ml, over a range of 26K.	Heparin	104-111	serpin family C member 1	Homo sapiens	31-47
8276857-2	1994	In a defined, plasma-free assay of fVIII activation and at physiological ionic strength and pH, heparin inhibited the rate of activation of either human or porcine fVIII by thrombin in either the presence or absence of von Willebrand factor (vWf).	Heparin	96-103	coagulation factor VIII	Homo sapiens	164-169
7305940-8	1981	difference absorption studies showed that the non-adsorbed heparin fraction bound to antithrombin in solution with a binding constant at physiological ionic strength only slightly lower than that of low-affinity heparin.	Heparin	59-66	serpin family C member 1	Homo sapiens	85-97
8276857-4	1994	At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml).	Heparin	165-172	coagulation factor VIII	Homo sapiens	28-33
6160891-2	1981	In the presence of heparin (incorporated into the agarose gel matrix), the AT-III of normal human plasma was separated into four components: two major, faster-moving components, and two minor, slower-moving components.	Heparin	19-26	serpin family C member 1	Homo sapiens	75-81
8276857-4	1994	At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml).	Heparin	165-172	coagulation factor VIII	Homo sapiens	98-103
7338523-1	1981	Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III.	Heparin	19-26	serpin family C member 1	Homo sapiens	122-138
8276857-4	1994	At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml).	Heparin	209-216	coagulation factor VIII	Homo sapiens	28-33
6977940-7	1981	Elevation of the antithrombin III inhibitory activity in presence of heparin was apparently responsible for an increase in the antitryptic activity under conditions of severe forms of SH when content of alpha 1-antitrypsin decreased.	Heparin	69-76	serpin family C member 1	Homo sapiens	17-33
6895327-2	1981	Lipoprotein lipase is bound to heparin-like molecules at the surface of capillary endothelial cells.	Heparin	31-38	lipoprotein lipase	Homo sapiens	0-18
6895327-4	1981	In this report, the interactions of apolipoprotein C-II, heparin and sonicated vesicles of dipalmitoylphosphatidylcholine with purified bovine milk lipoprotein lipase were studied by gel filtration on Bio-Gel A5m.	Heparin	57-64	lipoprotein lipase	Homo sapiens	148-166
6783500-5	1981	This indicates that heparin binding sites of antithrombin III are occupied or affected by the elastase-induced peptide bond cleavage(s).	Heparin	20-27	serpin family C member 1	Homo sapiens	45-61
6168228-0	1981	The interaction of protein-bound heparin and antithrombin III.	Heparin	33-40	serpin family C member 1	Homo sapiens	45-61
6168228-1	1981	When commercially prepared porcine mucosal heparin is added to human plasma, some of the heparin fractions form a complex with antithrombin III activating it to an immediate inhibitor of thrombin as well as of other serine proteases.	Heparin	43-50	serpin family C member 1	Homo sapiens	127-143
6168228-1	1981	When commercially prepared porcine mucosal heparin is added to human plasma, some of the heparin fractions form a complex with antithrombin III activating it to an immediate inhibitor of thrombin as well as of other serine proteases.	Heparin	89-96	serpin family C member 1	Homo sapiens	127-143
6168228-2	1981	Certain fractions of heparin may complex with other proteins such as alpha 2-macroglobulin, another progressive inhibitor of thrombin.	Heparin	21-28	alpha-2-macroglobulin	Homo sapiens	69-90
6168228-4	1981	Protamine sulfate inactivates those heparin fractions that bind to antithrombin III but not those bound to alpha 2-macroglobulin.	Heparin	36-43	serpin family C member 1	Homo sapiens	67-83
6895327-10	1981	The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl.	Heparin	19-26	lipoprotein lipase	Homo sapiens	32-50
6895327-10	1981	The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl.	Heparin	19-26	lipoprotein lipase	Homo sapiens	154-172
6895327-10	1981	The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl.	Heparin	84-91	lipoprotein lipase	Homo sapiens	32-50
6895327-10	1981	The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl.	Heparin	84-91	lipoprotein lipase	Homo sapiens	154-172
8276857-4	1994	At plasma concentrations of fVIII (approximately 1 nM) and vWf (approximately 35 nM), the rate of fVIII activation was inhibited by 50% at approximately 0.1 unit/ml heparin, which is below the normal range of heparin concentrations in plasma during therapeutic anticoagulation (0.2-0.7 unit/ml).	Heparin	209-216	coagulation factor VIII	Homo sapiens	98-103
6895327-10	1981	The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl.	Heparin	84-91	lipoprotein lipase	Homo sapiens	32-50
6895327-10	1981	The interaction of heparin with lipoprotein lipase was studied using a specific [3H]heparin, which was isolated by affinity chromatography on immobilized lipoprotein lipase; the [3H]heparin eluted with 0.6 M NaCl.	Heparin	84-91	lipoprotein lipase	Homo sapiens	154-172
6791550-0	1981	Heparin binding and protease inhibitor activity of chemically modified antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	71-87
8276857-5	1994	We propose that, in addition to catalyzing the inhibition of thrombin and other intrinsic pathway coagulation proteases by antithrombin, heparin functions as an anticoagulant by direct inhibition of the activation of the fVIII-vWf complex by thrombin.	Heparin	137-144	coagulation factor VIII	Homo sapiens	221-226
6895327-11	1981	Specific [3H]heparin coeluted with lipoprotein lipase when the enzyme was associated with phospholipid; the [3H]heparin was released from the enzyme by 0.75 M NaCl.	Heparin	13-20	lipoprotein lipase	Homo sapiens	35-53
8002784-0	1994	Evidence for a multistep mechanism for cell-cell fusion by herpes simplex virus with mutations in the syn 3 locus using heparin derivatives during fusion from within.	Heparin	120-127	synapsin III	Homo sapiens	102-107
7302889-2	1981	The endothelial cell At-III (EC-At-III) consists of a small fraction similar to plasma At-III and a larger fraction with decreased heparin-binding as tested by crossed immunoelectrophoresis.	Heparin	131-138	serpin family C member 1	Homo sapiens	21-27
7302889-3	1981	However, both the anti-Xa and thrombin-neutralizing activities of the EC-At-III were rapid and active even in the absence of added heparin.	Heparin	131-138	serpin family C member 1	Homo sapiens	73-79
6800936-2	1981	The binding of the alkaline phosphatase conjugated fibronectin to C1q was dose dependent and inhibited by fibronectin and by the sulfated polymers heparin and chondroitin sulfate.	Heparin	147-154	complement C1q A chain	Homo sapiens	66-69
6783633-0	1981	Preparation of biologically active fluorescent heparin composed of fluorescein-labeled species and its behavior to antithrombin III.	Heparin	47-54	serpin family C member 1	Homo sapiens	115-131
6783633-4	1981	The fluorescent heparin was separated into the low-affinity (56.6%) and high-affinity (43.4%) fractions for antithrombin III, and the anticoagulant activities of the two types of fluorescent heparin were compared with those of the starting heparin and the partially N-desulfated heparin, suggesting that FTC-substitution in heparin molecules had no effect on the known biological interaction with mobilized or immobilized antithrombin III.	Heparin	16-23	serpin family C member 1	Homo sapiens	108-124
8002784-1	1994	Addition of heparin-Na+ as well as related substances of high and intermediate MW (Arteparon and polyanion SP54) 3 h after infection inhibit fusion from within (FFWI) induced by HSV strains with mutations in the syn 3 locus only.	Heparin	12-19	synapsin III	Homo sapiens	212-217
7819340-6	1994	A strong heparin-binding site within a region conserved in rodent and human APP, APLP1 and APLP2, was identified.	Heparin	9-16	amyloid beta precursor like protein 2	Homo sapiens	91-96
7255875-0	1981	Decreased retention of fatty acid conjugated DDT metabolites in rats given injections of heparin, bile salts or lecithin.	Heparin	89-96	D-dopachrome tautomerase	Rattus norvegicus	45-48
7255875-1	1981	Intravenous injections of solutions of heparin, bile salts or lecithin into rats previously intraperitoneally injected with 14C-DDT significantly removed fatty acid conjugated 14C-DDT metabolites retained in their livers and spleens.	Heparin	39-46	D-dopachrome tautomerase	Rattus norvegicus	128-131
7255875-1	1981	Intravenous injections of solutions of heparin, bile salts or lecithin into rats previously intraperitoneally injected with 14C-DDT significantly removed fatty acid conjugated 14C-DDT metabolites retained in their livers and spleens.	Heparin	39-46	D-dopachrome tautomerase	Rattus norvegicus	180-183
7281335-0	1981	[Thrombosis patients with familial antithrombin-III deficiency treated with heparin and antithrombin].	Heparin	76-83	serpin family C member 1	Homo sapiens	35-47
6270073-6	1981	In addition, certain 2-O-sulfates on IdUA flanked with GlcNS(6X) (X=H or S) in the heparin molecule are suggested to be important for the activity.	Heparin	83-90	alpha-L-iduronidase	Homo sapiens	37-41
7267980-3	1981	In the present research, AT III has been determined both as substance concentration, by radial immunodiffusion, and on the base of its activity on a chromogenic substrate (Chromozym) in patients with DIC before and after heparin therapy.	Heparin	221-228	serpin family C member 1	Homo sapiens	25-31
7317004-1	1981	Antithrombin III binds to, and thereby augments the fluorescence of, dansyl-(5-dimethylaminonaphthalene-1-sulphonyl)-heparin; platelet factor 4 binding to the fluorescent heparin has little of this effect.	Heparin	117-124	serpin family C member 1	Homo sapiens	0-16
7317004-2	1981	Competition studies in which antithrombin III competes with platelet factor 4 for heparin binding demonstrate that heparin can simultaneously bind both proteins.	Heparin	82-89	serpin family C member 1	Homo sapiens	29-45
7459342-6	1980	The anticoagulant activity of heparin, determined in an antithrombin III activation assay, was markedly reduced after treatment with the heparitinase.	Heparin	30-37	serpin family C member 1	Homo sapiens	56-72
7735321-5	1994	Affinity chromatography of the concentrated ecto-PK through a heparin-matrix resolved two phosvitin/casein kinase activities upon elution with a NaCl gradient, termed as peak I and peak II.	Heparin	62-69	casein kinase 2 beta	Homo sapiens	90-99
7469415-0	1980	Binding of heparin to antithrombin III: The use of dansyl and rhodamine labels.	Heparin	11-18	serpin family C member 1	Homo sapiens	22-38
7462246-0	1981	The antithrombin-binding sequence of heparin.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
7213813-1	1981	Binding constants for the binding of high-affinity heparin to antithrombin at different ionic strengths were determined by fluorescence titrations and were also estimated from dissociation curves of the heparin-antithrombin complex.	Heparin	51-58	serpin family C member 1	Homo sapiens	62-74
7213813-1	1981	Binding constants for the binding of high-affinity heparin to antithrombin at different ionic strengths were determined by fluorescence titrations and were also estimated from dissociation curves of the heparin-antithrombin complex.	Heparin	51-58	serpin family C member 1	Homo sapiens	211-223
7430111-1	1980	A protease-resistant functional polypeptide domain of fibronectin that contains a heparin-binding site has been purified from chick cellular fibronectin following pronase digestion, heparin-Sepharose affinity chromatography, and molecular sieve chromatography on Sephacryl S-200.	Heparin	82-89	fibronectin 1	Gallus gallus	54-65
8187229-0	1994	Heparin extracorporeal LDL precipitation (HELP): an effective apheresis procedure for lowering Lp(a) levels.	Heparin	0-7	lipoprotein(a)	Homo sapiens	95-100
7430111-1	1980	A protease-resistant functional polypeptide domain of fibronectin that contains a heparin-binding site has been purified from chick cellular fibronectin following pronase digestion, heparin-Sepharose affinity chromatography, and molecular sieve chromatography on Sephacryl S-200.	Heparin	82-89	fibronectin 1	Gallus gallus	141-152
7430111-1	1980	A protease-resistant functional polypeptide domain of fibronectin that contains a heparin-binding site has been purified from chick cellular fibronectin following pronase digestion, heparin-Sepharose affinity chromatography, and molecular sieve chromatography on Sephacryl S-200.	Heparin	182-189	fibronectin 1	Gallus gallus	54-65
6914196-0	1981	The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin.	Heparin	64-71	serpin family C member 1	Homo sapiens	168-180
8200121-8	1994	After intravenous administration of heparin, DAO is released from its capillary binding sites in the lamina propria into the peripheral circulation.	Heparin	36-43	amine oxidase copper containing 1	Homo sapiens	45-48
6943957-9	1981	The antithrombotic action of heparin depends on a normal quantity of plasma AT-III.	Heparin	29-36	serpin family C member 1	Homo sapiens	76-82
6935668-0	1980	Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin.	Heparin	90-97	serpin family C member 1	Homo sapiens	57-69
7657522-8	1994	Structural requirement for the inhibition of melanoma cell heparanase and lung colonization by species of heparin were different from those identified for (1) release of ECM-bound basic fibroblast growth factor (b-FGF) and (2) stimulation of b-FGF receptor binding and mitogenic activity.	Heparin	106-113	fibroblast growth factor 2	Mus musculus	180-210
6935668-1	1980	An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid.	Heparin	105-112	serpin family C member 1	Homo sapiens	41-53
6935668-7	1980	These results suggest that 3-sulfated glucosamine is a unique component of high-affinity heparin, located at a specific position in the antithrombin-binding sequence of the molecule.	Heparin	89-96	serpin family C member 1	Homo sapiens	136-148
7236660-3	1980	Antithrombin III, the major contaminant after affinity chromatography with heparin-Sepharose 4B, could be removed by gel filtration on Bio-Gel A-5m.	Heparin	75-82	serpin family C member 1	Homo sapiens	0-16
6448845-3	1980	Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion.	Heparin	44-51	serpin family C member 1	Homo sapiens	115-127
7408210-1	1980	The methods proposed by Nilsson-Ehle and Ekman [8] for the specific estimation of lipoprotein lipase and hepatic lipase activities in post-heparin plasma were investigated.	Heparin	139-146	lipoprotein lipase	Homo sapiens	82-100
6448846-0	1980	The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin.	Heparin	100-107	serpin family C member 1	Homo sapiens	34-46
7657522-8	1994	Structural requirement for the inhibition of melanoma cell heparanase and lung colonization by species of heparin were different from those identified for (1) release of ECM-bound basic fibroblast growth factor (b-FGF) and (2) stimulation of b-FGF receptor binding and mitogenic activity.	Heparin	106-113	fibroblast growth factor 2	Mus musculus	212-217
6448846-1	1980	The kinetics of inhibition of four hemostatic system enzymes by antithrombin were examined as a function of heparin concentration.	Heparin	108-115	serpin family C member 1	Homo sapiens	64-76
7657522-8	1994	Structural requirement for the inhibition of melanoma cell heparanase and lung colonization by species of heparin were different from those identified for (1) release of ECM-bound basic fibroblast growth factor (b-FGF) and (2) stimulation of b-FGF receptor binding and mitogenic activity.	Heparin	106-113	fibroblast growth factor 2	Mus musculus	242-247
6448846-17	1980	Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor.	Heparin	43-50	serpin family C member 1	Homo sapiens	54-66
6448846-18	1980	Furthermore, a careful comparison of the various constants suggests that the direct interaction between heparin and antithrombin may be largely responsible for the kinetic effect of this mucopolysaccharide.	Heparin	104-111	serpin family C member 1	Homo sapiens	116-128
7457802-1	1980	Dependence of the effect of heparin on the activity of antithrombin III (author"s transl)].	Heparin	28-35	serpin family C member 1	Homo sapiens	55-71
7457802-4	1980	A distinct relation was found between the effect of heparin on the aPTT and on the thrombin clotting time and the activity of antithrombin III.	Heparin	52-59	serpin family C member 1	Homo sapiens	126-142
7457802-6	1980	Since this effect is of primary importance for the efficacy of prophylaxis of DIC, regular assays of antithrombin III are proposed in shock patients receiving heparin.	Heparin	159-166	serpin family C member 1	Homo sapiens	101-117
7457881-0	1980	Immobilization of heparin with trichloro-s-triazine: purification of mouse antithrombin.	Heparin	18-25	serpin family C member 1	Homo sapiens	75-87
7417484-0	1980	Effects of the reduction and S-carbamidomethylation on the conformation, activity and heparin-binding capacity of human antithrombin III.	Heparin	86-93	serpin family C member 1	Homo sapiens	120-136
7417484-8	1980	The reduction and S-carbamidomethylation of antithrombin III induces some local changes in the tertiary structure affecting the inhibitor activity, heparin binding and near-ultraviolet circular dichroic spectrum, but do not seem to induce any substantial general conformation change.	Heparin	148-155	serpin family C member 1	Homo sapiens	44-60
7406509-0	1980	Tryptophan residue at the heparin binding site in antithrombin III.	Heparin	26-33	serpin family C member 1	Homo sapiens	50-66
8282825-4	1994	Complexes formed at an apparent heparin/PF4 molecular ratio of approximately 1:2 (fresh heparin) and approximately 1:12 (outdated heparin) were most effective in binding antibody.	Heparin	32-39	platelet factor 4	Homo sapiens	40-43
6771264-3	1980	Fibronectin isolated from chick embryo fibroblasts binds both hyaluronic acid and heparin; heparan sulfate is bound less efficiently, and chondroitin sulfate and glycopeptides are bound minimally.	Heparin	82-89	fibronectin 1	Gallus gallus	0-11
6771264-4	1980	The binding of hyaluronic acid and heparin to fibronectin is saturable and reversible and occurs at separate binding sites.	Heparin	35-42	fibronectin 1	Gallus gallus	46-57
6771264-7	1980	The affinity for heparin was utilized for the isolation of heparin-binding domains of fibronectin on heparin-agarose affinity columns.	Heparin	17-24	fibronectin 1	Gallus gallus	86-97
6771264-7	1980	The affinity for heparin was utilized for the isolation of heparin-binding domains of fibronectin on heparin-agarose affinity columns.	Heparin	59-66	fibronectin 1	Gallus gallus	86-97
6771264-7	1980	The affinity for heparin was utilized for the isolation of heparin-binding domains of fibronectin on heparin-agarose affinity columns.	Heparin	59-66	fibronectin 1	Gallus gallus	86-97
7437065-0	1980	The interaction of heparin with thrombin and antithrombin.	Heparin	19-26	serpin family C member 1	Homo sapiens	45-57
7209874-0	1980	Preparation and partial characterization of human plasma depleted of antithrombin-III by heparin-sepharose affinity chromatography.	Heparin	89-96	serpin family C member 1	Homo sapiens	69-85
7408210-0	1980	The validation and use of specific methods for the estimation of lipoprotein lipase and hepatic lipase activities in post-heparin plasma of children with hyperlipidaemia.	Heparin	122-129	lipoprotein lipase	Homo sapiens	65-83
8282825-4	1994	Complexes formed at an apparent heparin/PF4 molecular ratio of approximately 1:2 (fresh heparin) and approximately 1:12 (outdated heparin) were most effective in binding antibody.	Heparin	88-95	platelet factor 4	Homo sapiens	40-43
8282825-4	1994	Complexes formed at an apparent heparin/PF4 molecular ratio of approximately 1:2 (fresh heparin) and approximately 1:12 (outdated heparin) were most effective in binding antibody.	Heparin	88-95	platelet factor 4	Homo sapiens	40-43
7007650-1	1980	The activity of LIF, produced in vitro by sensitized lymphocytes exposed to the appropriate antigens, is readily abolished in the simultaneous presence of heparin and thrombin.	Heparin	155-162	LIF interleukin 6 family cytokine	Homo sapiens	16-19
7007650-3	1980	Adding AT III together with heparin and thrombin restores the LIF activity.	Heparin	28-35	LIF interleukin 6 family cytokine	Homo sapiens	62-65
8282825-5	1994	Immune complexes consisting of PF4, heparin, and antibody reacted with resting platelets; this interaction was inhibited by a monoclonal antibody specific for the Fc gamma RII receptor and by excess heparin.	Heparin	199-206	platelet factor 4	Homo sapiens	31-34
7007650-4	1980	We suggest that the migrating leucocytes on their cell membranes have receptors, composed of AT III-like molecules, which are blocked or destroyed, by forming complexes with heparin and thrombin.	Heparin	174-181	serpin family C member 1	Homo sapiens	93-99
7349668-5	1980	Thrombin and Factor Xa were instantaneously inhibited by AT III in the presence of soluble heparin.	Heparin	91-98	serpin family C member 1	Homo sapiens	57-63
8282825-6	1994	Human umbilical vein endothelial cells, known to express heparin-like glycosaminoglycan molecules on their surface, were recognized by antibody in the presence of PF4 alone; this reaction was inhibited by excess heparin, but not by anti-Fc gamma RII.	Heparin	57-64	platelet factor 4	Homo sapiens	163-166
8282825-6	1994	Human umbilical vein endothelial cells, known to express heparin-like glycosaminoglycan molecules on their surface, were recognized by antibody in the presence of PF4 alone; this reaction was inhibited by excess heparin, but not by anti-Fc gamma RII.	Heparin	212-219	platelet factor 4	Homo sapiens	163-166
7444870-1	1980	Correlation between the anticoagulant activity of the fractions and their content of heparin with high affinity for antithrombin.	Heparin	85-92	serpin family C member 1	Homo sapiens	116-128
6158112-0	1980	Heparin prevents thrombin inhibition by alpha 2 macroglobulin.	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	40-61
8282825-8	1994	These findings indicate that antibodies associated with HITP react with PF4 complexed with heparin in solution or with glycosaminoglycan molecules on the surface of endothelial cells and provide the basis for a new hypothesis to explain the development of thrombocytopenia with thrombosis or disseminated intravascular coagulation in patients sensitive to heparin.	Heparin	91-98	platelet factor 4	Homo sapiens	72-75
8282825-8	1994	These findings indicate that antibodies associated with HITP react with PF4 complexed with heparin in solution or with glycosaminoglycan molecules on the surface of endothelial cells and provide the basis for a new hypothesis to explain the development of thrombocytopenia with thrombosis or disseminated intravascular coagulation in patients sensitive to heparin.	Heparin	356-363	platelet factor 4	Homo sapiens	72-75
8186150-8	1994	Immunofluorescence shows that the distribution of fibronectin-containing fibrils is normal in heparin-treated embryos, whereas there are no such fibrils in suramin-treated embryos at control stage 12.	Heparin	94-101	fibronectin 1 S homeolog	Xenopus laevis	50-61
7374436-3	1980	In subjects with primary hypertriglyceridemia the fasting lipoprotein lipase activity eluted from pieces of adipose tissue by heparin and the enzyme activity present in extracts of acetone--ether tissue powders were similar to the level of enzyme activity found in normal subjects.	Heparin	126-133	lipoprotein lipase	Homo sapiens	58-76
7368150-1	1980	The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides.	Heparin	123-130	serpin family C member 1	Homo sapiens	94-110
7407200-6	1980	Approximately stoichiometric amounts of heparin completely inhibited the reaction of papain with antithrombin.	Heparin	40-47	serpin family C member 1	Homo sapiens	97-109
7409165-0	1980	The molecular size of the antithrombin-binding sequence in heparin.	Heparin	59-66	serpin family C member 1	Homo sapiens	26-38
7444377-4	1980	The patient was treated with human AT III concentrate as a result of the development of progressive disseminated intravascular coagulation (DIC), the further deterioration of renal function, the risk for thromboembolic complications and the possible adverse effects of heparin therapy.	Heparin	269-276	serpin family C member 1	Homo sapiens	35-41
7455972-2	1980	We obtained different antithrombin III patterns in the plasma of the affected members of the two families with the modified two dimensional immunoelectrophoresis method (heparin in agarose).	Heparin	170-177	serpin family C member 1	Homo sapiens	22-38
7455972-5	1980	The relatively low affinity of this antithrombin III to heparin could be directly proved by the heparin-agarose affinity chromatography, too.	Heparin	56-63	serpin family C member 1	Homo sapiens	36-52
7455972-5	1980	The relatively low affinity of this antithrombin III to heparin could be directly proved by the heparin-agarose affinity chromatography, too.	Heparin	96-103	serpin family C member 1	Homo sapiens	36-52
7368150-1	1980	The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides.	Heparin	123-130	serpin family C member 1	Homo sapiens	112-118
7368150-4	1980	Samples of purified At III from four different manufacturers all displayed heterogeneity with respect to heparin binding.	Heparin	105-112	serpin family C member 1	Homo sapiens	20-26
7368150-6	1980	An antiserum made against purifed At III contained antibodies with different cross-reactivities against heparin bound and non-heparin bound At III.	Heparin	104-111	serpin family C member 1	Homo sapiens	34-40
7356660-0	1980	The heparin binding site of antithrombin III.	Heparin	4-11	serpin family C member 1	Homo sapiens	28-44
7356660-8	1980	These results indicate that the integrity of a specific tryptophan residue is critical to the binding of heparin to antithrombin III.	Heparin	105-112	serpin family C member 1	Homo sapiens	116-132
6993082-1	1980	Heparin binds reversibly to its target sites of action, antithrombin and the other serine proteases involved in coagulation, especially activated factor X.	Heparin	0-7	serpin family C member 1	Homo sapiens	56-68
8140602-6	1994	The binding activity of immature rat CBG for B dropped 50% (P &lt; 0.001) 60 minutes post-heparin injection, decreased B binding and increased plasma FFA were correlated (r = -0.8).	Heparin	90-97	serpin family A member 6	Rattus norvegicus	37-40
7368101-4	1980	Heparin activates lipoprotein lipase, and therefore some triglyceride in the perfusate was lipolyzed with a resultant increase in serum free fatty acids (FFAs) to 253 mumole/dl.	Heparin	0-7	lipoprotein lipase	Homo sapiens	18-36
7436418-0	1980	Studies on the interaction of heparin with thrombin, antithrombin, and other plasma proteins.	Heparin	30-37	serpin family C member 1	Homo sapiens	53-65
7002115-2	1980	Lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle before and after the exercise.	Heparin	54-61	lipoprotein lipase	Homo sapiens	0-18
7002115-2	1980	Lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle before and after the exercise.	Heparin	54-61	lipoprotein lipase	Homo sapiens	20-23
8054816-5	1994	The simultaneous administration of heparin and prostagladin E1 (PGE1), which is known to suppress the production of TNF and IL-1, reduced the magnitude of liver injury and the mortality of these rats.	Heparin	35-42	tumor necrosis factor-like	Rattus norvegicus	116-119
6243142-5	1980	Fractionation of heparin yielded preparations that varied in molecular weight and, within a given molecular weight fraction, in affinity for antithrombin III.	Heparin	17-24	serpin family C member 1	Homo sapiens	141-157
7353045-0	1980	Exposure to solvent of tyrosyl and tryptophanyl residues of bovine antithrombin in the absence and presence of high-affinity and low-affinity heparin.	Heparin	142-149	serpin family C member 1	Homo sapiens	67-79
7353045-6	1980	The binding of low-affinity of high-affinity heparin to antithrombin had neglibible effects on the solvent perturbation spectra and on the spectrophotometric titration curves.	Heparin	45-52	serpin family C member 1	Homo sapiens	56-68
7353045-8	1980	The binding of heparin to antithrombin therefore apparently leads to, at most, minimal changes of the exposure of the aromatic amino acids of the protein to the surrounding solvent.	Heparin	15-22	serpin family C member 1	Homo sapiens	26-38
7368150-6	1980	An antiserum made against purifed At III contained antibodies with different cross-reactivities against heparin bound and non-heparin bound At III.	Heparin	126-133	serpin family C member 1	Homo sapiens	34-40
7368151-3	1980	The method allows the specific determination of heparin concentrations from 0.02 USP to 0.8 USP/ml of plasma in the presence of normal At III levels.	Heparin	48-55	serpin family C member 1	Homo sapiens	135-141
6243142-10	1980	These results suggest that formation of an antithrombin-heparin complex protected platelets from aggregation by heparin.	Heparin	56-63	serpin family C member 1	Homo sapiens	43-55
6243142-10	1980	These results suggest that formation of an antithrombin-heparin complex protected platelets from aggregation by heparin.	Heparin	112-119	serpin family C member 1	Homo sapiens	43-55
7518263-1	1993	Recombinant human acidic fibroblast growth factor (haFGF) was purified from E. coli lysate by heparin-sepharose affinity chromatography.	Heparin	94-101	fibroblast growth factor 1	Bos taurus	18-49
6243142-11	1980	Selection of heparin fractions of low molecular weight and high antithrombin affinity may improve anticoagulant therapy and development of thromboresistant heparin-coated artificial materials.	Heparin	13-20	serpin family C member 1	Homo sapiens	64-76
527591-0	1979	Evidence by chemical modification for the involvement of one or more tryptophanyl residues of bovine antithrombin in the binding of high-affinity heparin.	Heparin	146-153	serpin family C member 1	Homo sapiens	101-113
527591-5	1979	Addition of an excess of high-affinity heparin to a similarly modified antithrombin sample resulted in much smaller circular dichroism, ultraviolet absorption and fluorescence changes than those observed with the intact protein.	Heparin	39-46	serpin family C member 1	Homo sapiens	71-83
7368180-0	1980	A differential effect of low-affinity heparin on the inhibition of thrombin and factor Xa by antithrombin.	Heparin	38-45	serpin family C member 1	Homo sapiens	93-105
6158827-6	1980	Together with the increased concentration of antithrombin III this might explain the potentiating effect of DHE or prophylactic treatment with low-dose heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	45-61
527591-7	1979	These studies thus reinforce the conclusion from previous spectroscopic analyses that one or more tryptophanyl residues of antithrombin are involved in the binding of high-affinity heparin, presumably by being located at or close to the heparin binding site.	Heparin	181-188	serpin family C member 1	Homo sapiens	123-135
8269931-0	1993	Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain.	Heparin	110-117	matrix metallopeptidase 2	Homo sapiens	6-21
527591-7	1979	These studies thus reinforce the conclusion from previous spectroscopic analyses that one or more tryptophanyl residues of antithrombin are involved in the binding of high-affinity heparin, presumably by being located at or close to the heparin binding site.	Heparin	237-244	serpin family C member 1	Homo sapiens	123-135
120212-0	1979	Chromatography of heparin on sepharose-lysine: molecular size fractionation and its relevance to thrombin and antithrombin III binding.	Heparin	18-25	serpin family C member 1	Homo sapiens	110-126
7417594-3	1980	Heparin stimulates the inactivation of Factor Xa and thrombin by AT III.	Heparin	0-7	serpin family C member 1	Homo sapiens	65-71
118968-2	1979	Human, porcine, rabbit, and rat antithrombin III have been purified by affinity chromatography using heparin-agarose.	Heparin	101-108	serpin family C member 1	Homo sapiens	32-48
8138538-0	1993	Heparin as an inducer of hepatocyte growth factor.	Heparin	0-7	hepatocyte growth factor	Homo sapiens	25-49
500822-4	1979	Antithrombin affinity chromatography of purified heparin with an anticoagulant activity of 137 U/mg, revealed that the one-third that was bound and eluted had a 273 U/mg sp act, whereas the unbound activity was 31 U/mg.	Heparin	49-56	serpin family C member 1	Homo sapiens	0-12
500822-5	1979	Thus, the previously observed heterogeneity of commercial porcine heparin for binding to human antithrombin was also observed with human heparin.	Heparin	66-73	serpin family C member 1	Homo sapiens	95-107
111639-7	1979	Pretreatment with heparin prevents the consumption of fibrinogen and antithrombin III but does not prevent the increase in fibrin split products which was observed.	Heparin	18-25	serpin family C member 1	Homo sapiens	69-85
89015-0	1979	[Heparin inhibition of the antithrombin activity of alpha-2-macroglobulin].	Heparin	1-8	serpin family C member 1	Homo sapiens	27-39
89015-0	1979	[Heparin inhibition of the antithrombin activity of alpha-2-macroglobulin].	Heparin	1-8	alpha-2-macroglobulin	Homo sapiens	52-73
89015-3	1979	In the presence of heparin the rate of inhibition of thrombin clotting activity by alpha-2-macroglobulin is strongly decreased.	Heparin	19-26	alpha-2-macroglobulin	Homo sapiens	83-104
89015-4	1979	Heparin binds to thrombin, impairing the formation of thrombin-alpha-2-macroglobulin complex.	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	63-84
89015-5	1979	These data show that heparin paradoxically protects thrombin from inhibition by alpha-2-macroglobulin whereas it increases the enzyme inhibition by antithrombin III.	Heparin	21-28	alpha-2-macroglobulin	Homo sapiens	80-101
89015-5	1979	These data show that heparin paradoxically protects thrombin from inhibition by alpha-2-macroglobulin whereas it increases the enzyme inhibition by antithrombin III.	Heparin	21-28	serpin family C member 1	Homo sapiens	148-164
384999-0	1979	Localization of the heparin-releasable lipase in situ in the rat liver.	Heparin	20-27	lipase G, endothelial type	Rattus norvegicus	39-45
8138538-2	1993	We have now obtained evidence that heparin is a potent inducer of HGF production.	Heparin	35-42	hepatocyte growth factor	Homo sapiens	66-69
486155-1	1979	The inactivation of thrombin and factor Xa by antithrombin was determined in the presence of heparin fractions of different molecular weights and with high affinity for antithrombin.	Heparin	93-100	serpin family C member 1	Homo sapiens	46-58
436823-0	1979	Studies on the mechanism of the rate-enhancing effect of heparin on the thrombin-antithrombin III reaction.	Heparin	57-64	serpin family C member 1	Homo sapiens	81-97
436823-1	1979	The rate of the reaction between thrombin and antithrombin III is greatly increased in the presence of heparin.	Heparin	103-110	serpin family C member 1	Homo sapiens	46-62
486155-1	1979	The inactivation of thrombin and factor Xa by antithrombin was determined in the presence of heparin fractions of different molecular weights and with high affinity for antithrombin.	Heparin	93-100	serpin family C member 1	Homo sapiens	169-181
8138538-3	1993	The addition of heparin to a culture of MRC-5 human embryonic lung fibroblasts increased the HGF concentration in the conditioned medium, in a dose-dependent manner.	Heparin	16-23	hepatocyte growth factor	Homo sapiens	93-96
436823-4	1979	The strength of the binding of the two heparin fractions to antithrombin III and thrombin, respectively, was determined by a crossed immunoelectrophoresis technique.	Heparin	39-46	serpin family C member 1	Homo sapiens	60-76
436823-7	1979	The ability of the two heparin fractions to catalyse the inhibition of thrombin by antithrombin III was determined and was found to be much greater for the high activity heparin fraction.	Heparin	23-30	serpin family C member 1	Homo sapiens	83-99
8138538-5	1993	The rate of HGF synthesis in MRC-5 cells, as measured by pulse-labeling with [35S]methionine, and subsequent immunoprecipitation of HGF from both conditioned medium and a cell lysate, was 3-4-fold stimulated by 1 microgram/ml heparin, whereas heparin apparently had no significant effect on the HGF mRNA level.	Heparin	226-233	hepatocyte growth factor	Homo sapiens	12-15
436823-7	1979	The ability of the two heparin fractions to catalyse the inhibition of thrombin by antithrombin III was determined and was found to be much greater for the high activity heparin fraction.	Heparin	170-177	serpin family C member 1	Homo sapiens	83-99
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	103-110	serpin family C member 1	Homo sapiens	50-66
113002-0	1979	Properties of salt-resistant lipase and lipoprotein lipase purified from human post-heparin plasma.	Heparin	84-91	lipoprotein lipase	Homo sapiens	40-58
8138538-5	1993	The rate of HGF synthesis in MRC-5 cells, as measured by pulse-labeling with [35S]methionine, and subsequent immunoprecipitation of HGF from both conditioned medium and a cell lysate, was 3-4-fold stimulated by 1 microgram/ml heparin, whereas heparin apparently had no significant effect on the HGF mRNA level.	Heparin	243-250	hepatocyte growth factor	Homo sapiens	12-15
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	103-110	serpin family C member 1	Homo sapiens	133-149
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	103-110	serpin family C member 1	Homo sapiens	133-149
8138538-6	1993	The stimulatory effect of heparin on HGF production was evident in various types of cells, such as MRC-9, IMR-90, and WI-38 human embryonic lung fibroblasts, human skin fibroblasts, HL-60 human promyelocytic leukemic cells and human umbilical vein endothelial cells.	Heparin	26-33	hepatocyte growth factor	Homo sapiens	37-40
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	serpin family C member 1	Homo sapiens	50-66
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	serpin family C member 1	Homo sapiens	133-149
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	serpin family C member 1	Homo sapiens	133-149
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	serpin family C member 1	Homo sapiens	50-66
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	serpin family C member 1	Homo sapiens	133-149
436823-8	1979	A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III.	Heparin	162-169	serpin family C member 1	Homo sapiens	133-149
553509-7	1979	In the treatment of DIC priority is given to intravenous application of AT-III complex human, concentrated and purified, activated in vitro with heparin.	Heparin	145-152	serpin family C member 1	Homo sapiens	72-78
116567-2	1979	The importance of antithrombin III as a cofactor of heparin is stressed.	Heparin	52-59	serpin family C member 1	Homo sapiens	18-34
37280-4	1979	Lipoprotein lipase activity was characterized with this substrate by previously established criteria including an alkaline pH optimum, increased activity in the presence of heparin and heat-inactivated plasma, and reduced activity in the presence of NaCl and protamine sulfate.	Heparin	173-180	lipoprotein lipase	Oryctolagus cuniculus	0-18
37280-7	1979	Intact microvessels, when incubated in the presence of heparin, release lipoprotein lipase into the incubation solution.	Heparin	55-62	lipoprotein lipase	Oryctolagus cuniculus	72-90
8263410-9	1993	267: 16517-16522) have shown that a heparin-sensitive, non-proteoglycan 116-kDa LPL-binding protein is present on cultured bovine aortic endothelial cells (BAEC).	Heparin	36-43	lipoprotein lipase	Bos taurus	80-83
444323-1	1979	Activity of lipoprotein lipase was studied in rabbit blood plasma after administration of heparin at a dose 50 un/kg into animals.	Heparin	90-97	lipoprotein lipase	Oryctolagus cuniculus	12-30
8263410-13	1993	Specific LPL binding was eliminated by incubating the BAEC at 4 degrees C with heparin containing buffer prior to the addition of LPL.	Heparin	79-86	lipoprotein lipase	Bos taurus	9-12
8276720-4	1993	HGF/SF is well known to have a strong affinity for heparin in vitro, and from the results of our immunohistochemical assay, we considered that HGF/SF was bound to heparin or heparan sulfate of the extracellular matrix and basement membrane.	Heparin	51-58	hepatocyte growth factor	Homo sapiens	0-6
107070-0	1978	The influence of heparin on the immunochemical evaluation of antithrombin III by electroimmunoassay.	Heparin	17-24	serpin family C member 1	Homo sapiens	61-77
8276720-4	1993	HGF/SF is well known to have a strong affinity for heparin in vitro, and from the results of our immunohistochemical assay, we considered that HGF/SF was bound to heparin or heparan sulfate of the extracellular matrix and basement membrane.	Heparin	51-58	hepatocyte growth factor	Homo sapiens	143-149
741437-0	1978	Appearance of heparin antithrombin-active chains in vivo after injection of commercial heparin and in anaphylaxis.	Heparin	14-21	serpin family C member 1	Homo sapiens	22-34
160191-7	1979	Antithrombin III was promoted by heparin in its inhibitory effect.	Heparin	33-40	serpin family C member 1	Homo sapiens	0-16
8276720-4	1993	HGF/SF is well known to have a strong affinity for heparin in vitro, and from the results of our immunohistochemical assay, we considered that HGF/SF was bound to heparin or heparan sulfate of the extracellular matrix and basement membrane.	Heparin	163-170	hepatocyte growth factor	Homo sapiens	0-6
8276720-4	1993	HGF/SF is well known to have a strong affinity for heparin in vitro, and from the results of our immunohistochemical assay, we considered that HGF/SF was bound to heparin or heparan sulfate of the extracellular matrix and basement membrane.	Heparin	163-170	hepatocyte growth factor	Homo sapiens	143-149
8259546-6	1993	DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation.	Heparin	51-58	serpin family D member 1	Homo sapiens	72-76
456150-3	1979	In this situation special emphasis should be placed on the levels of antithrombin III regarding application of heparin.	Heparin	111-118	serpin family C member 1	Homo sapiens	69-85
8259547-3	1993	TFPI was most potent in the PT assay and the effect of TFPI was most pronounced in the presence of other anticoagulants (heparin and hirudin).	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	0-4
687588-0	1978	Binding of low-affinity and high-affinity heparin to antithrombin.	Heparin	42-49	serpin family C member 1	Homo sapiens	53-65
8259547-3	1993	TFPI was most potent in the PT assay and the effect of TFPI was most pronounced in the presence of other anticoagulants (heparin and hirudin).	Heparin	121-128	tissue factor pathway inhibitor	Homo sapiens	55-59
8259547-7	1993	In an ATIII deficient plasma heparin did not augment the effect of TFPI, showing that the increased effect of TFPI in the presence of heparin is dependent on the anticoagulant activity of ATIII/heparin.	Heparin	134-141	tissue factor pathway inhibitor	Homo sapiens	110-114
8259548-2	1993	In humans, injection of heparin results in a 2-6 fold increase in plasma TFPI and recent studies suggest that TFPI may be important for the anticoagulant activity of heparin.	Heparin	24-31	tissue factor pathway inhibitor	Homo sapiens	73-77
511016-6	1979	Serum samples showed two antithrombin III peaks due to a decreased heparin binding of the slower peak (2.1-3.9 times), which was probably antithrombin III-activated procoagulant complexes.	Heparin	67-74	serpin family C member 1	Homo sapiens	25-41
511016-6	1979	Serum samples showed two antithrombin III peaks due to a decreased heparin binding of the slower peak (2.1-3.9 times), which was probably antithrombin III-activated procoagulant complexes.	Heparin	67-74	serpin family C member 1	Homo sapiens	138-154
652506-0	1978	[Changes in antithrombin III during treatment with heparin].	Heparin	51-58	serpin family C member 1	Homo sapiens	12-28
8259548-2	1993	In humans, injection of heparin results in a 2-6 fold increase in plasma TFPI and recent studies suggest that TFPI may be important for the anticoagulant activity of heparin.	Heparin	24-31	tissue factor pathway inhibitor	Homo sapiens	110-114
511016-7	1979	Heparin analogue (A 73025) also bound antithrombin III in vitro but the mobility of the peak was slower than with mucosal heparin and only a single peak was obtained in serum samples.	Heparin	0-7	serpin family C member 1	Homo sapiens	38-54
511016-10	1979	Heparin therapy gave rise to a double peak in the plasma antithrombin III profile and with continuous infusion, quantitative decreases were noted in all subjects studied, two of whom rethrombosed at the end of 7 days therapy.	Heparin	0-7	serpin family C member 1	Homo sapiens	57-73
8259548-2	1993	In humans, injection of heparin results in a 2-6 fold increase in plasma TFPI and recent studies suggest that TFPI may be important for the anticoagulant activity of heparin.	Heparin	166-173	tissue factor pathway inhibitor	Homo sapiens	73-77
217091-3	1978	25 patients receiving heparin therapy had low antithrombin III concentration.	Heparin	22-29	serpin family C member 1	Homo sapiens	46-62
217091-6	1978	Antithrombin III decreased activity induced by heparin treatment is pointed out.	Heparin	47-54	serpin family C member 1	Homo sapiens	0-16
350729-3	1978	The inactivation is accelerated by heparin, permitting assay systems which rapidly measure the At-III content of diluted plasma.	Heparin	35-42	serpin family C member 1	Homo sapiens	95-101
658785-4	1978	Heparin accelerates the saturation of antithrombin with factor Xa.	Heparin	0-7	serpin family C member 1	Homo sapiens	38-50
8259548-2	1993	In humans, injection of heparin results in a 2-6 fold increase in plasma TFPI and recent studies suggest that TFPI may be important for the anticoagulant activity of heparin.	Heparin	166-173	tissue factor pathway inhibitor	Homo sapiens	110-114
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	serpin family D member 1	Homo sapiens	154-173
618990-8	1978	The results suggest that a surface with covalently bonded heparin is reactive toward platelets but can be passivated by formation of a heparin/AT III complex.	Heparin	58-65	serpin family C member 1	Homo sapiens	143-149
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	serpin family D member 1	Homo sapiens	175-179
618990-8	1978	The results suggest that a surface with covalently bonded heparin is reactive toward platelets but can be passivated by formation of a heparin/AT III complex.	Heparin	135-142	serpin family C member 1	Homo sapiens	143-149
710412-0	1978	The binding of low-affinity and high-affinity heparin to antithrombin.	Heparin	46-53	serpin family C member 1	Homo sapiens	57-69
710412-2	1978	The interaction between antithrombin and two forms of heparin, differing in their affinity for the matrix-linked protein, has been studied by fluorescence.	Heparin	54-61	serpin family C member 1	Homo sapiens	24-36
8321249-2	1993	The three allotypes all bound to heparin, DNA, Con A, and methylamine-treated mouse C3 (C3(MA)mo) with similar affinities for each protein immobilized, showed identical mobilities on SDS-PAGE, and were reacted well with rabbit polyclonal antibody against H.1 and H.2.	Heparin	33-40	complement component 3	Mus musculus	84-86
710412-3	1978	The binding of the high-affinity heparin fraction to antithrombin leads to activation of the inhibitor, allowing it to react more rapidly with a number of serine proteases of the coagulation cascade.	Heparin	33-40	serpin family C member 1	Homo sapiens	53-65
710412-7	1978	The fluorescence enhancement caused by high-affinity heparin is consistent with a conformational change of antithrombin related to its activation.	Heparin	53-60	serpin family C member 1	Homo sapiens	107-119
710412-9	1978	These showed high-affinity heparin to bind to antithrombin with a stoichiometry of about one and with a binding constant at physiological ionic strength of about 8 X 10(7) M-1.	Heparin	27-34	serpin family C member 1	Homo sapiens	46-58
710423-0	1978	The binding of low-affinity and high-affinity heparin to antithrombin.	Heparin	46-53	serpin family C member 1	Homo sapiens	57-69
353657-0	1977	[Electrophoretic mobility of antithrombin III in an agarose gel with heparin.	Heparin	69-76	serpin family C member 1	Homo sapiens	29-45
353657-4	1977	The inactige antithrombin III with higher molecular size, separated by gel filtration, was found to be homogenous even if there was heparin in the gel.	Heparin	132-139	serpin family C member 1	Homo sapiens	13-29
8503856-3	1993	After 10 min pulse-labelling, LPL protein was eluted as two peaks from heparin-agarose: peak 1 at about 0.65 M NaCl, peak 2 at about 0.95 M NaCl.	Heparin	71-78	lipoprotein lipase	Cavia porcellus	30-33
74248-3	1977	Heparin facilitated complex-formation between alpha-thrombin and antithrombin-III, whereas inactivation of beta-thrombin by antithrombin was only slightly influenced, even at a heparin concentration two orders of magnitude higher.	Heparin	0-7	serpin family C member 1	Homo sapiens	65-81
74248-3	1977	Heparin facilitated complex-formation between alpha-thrombin and antithrombin-III, whereas inactivation of beta-thrombin by antithrombin was only slightly influenced, even at a heparin concentration two orders of magnitude higher.	Heparin	0-7	serpin family C member 1	Homo sapiens	65-77
210351-4	1978	Differences in the kinetics of lipoprotein lipase-related triglyceride removal during a maximal heparin infusion were also demonstrated between these two disorders.	Heparin	96-103	lipoprotein lipase	Homo sapiens	31-49
705690-0	1978	Inhibition of urokinase by complex formation with human antithrombin III in absence and presence of heparin.	Heparin	100-107	serpin family C member 1	Homo sapiens	56-72
8477692-11	1993	The affinity for heparin was as high with c-LPL as with intact LPL.	Heparin	17-24	lipoprotein lipase	Bos taurus	44-47
705690-1	1978	Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis.	Heparin	90-97	serpin family C member 1	Homo sapiens	6-22
24016-4	1977	The binding of heparin to antithrombin III influences the number of solvent-exposed tryptophan residues.	Heparin	15-22	serpin family C member 1	Homo sapiens	26-42
603757-2	1977	A study has been made of a low molecular weight semi-synthetic heparin analogue, A73025, that may be clinically useful as an antithrombotic agent because of its reported high specificity for antithrombin III.	Heparin	63-70	serpin family C member 1	Homo sapiens	191-207
8477692-11	1993	The affinity for heparin was as high with c-LPL as with intact LPL.	Heparin	17-24	lipoprotein lipase	Bos taurus	63-66
8511754-3	1993	Of these proteins platelet factor-4 (PF4) has the greatest affinity for heparin and is present in relatively high concentrations.	Heparin	72-79	platelet factor 4	Homo sapiens	37-40
912599-1	1977	The stereochemical course of in vivo hydrolysis of triacylglycerols by lipoprotein lipase was investigated by determining the structure of diacylglycerol intermediates in postheparin plasma of rats which had been fed [3H]glycerol-labeled Intralipid 2 h before an injection of heparin or had been given an injection of a mixture of [3H]glycerol-Intralipid and heparin.	Heparin	175-182	lipase G, endothelial type	Rattus norvegicus	83-89
71399-0	1977	Heparin-induced decrease in circulating antithrombin-III.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-56
97200-5	1978	Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan.	Heparin	64-71	serpin family C member 1	Homo sapiens	57-63
656463-0	1978	The increase in human antithrombin III tryptophan fluorescence produced by heparin.	Heparin	75-82	serpin family C member 1	Homo sapiens	22-38
656463-1	1978	The increase in fluorescence of human antithrombin III has been used to study the binding of a semi-synthetic heparin analogue.	Heparin	110-117	serpin family C member 1	Homo sapiens	38-54
149555-6	1978	Thus only between 3 and 11% of the in vivo formed plasmin is neutralized by antithrombin-heparin complex.	Heparin	89-96	serpin family C member 1	Homo sapiens	76-88
149555-7	1978	Repeated activation of the fibrinolytic system resulted in a shortening of the plasma radioactivity half-life of labelled antithrombin from 2.45 to 2.03 d in the absence of heparin (three patients), and from 3.13 to 2.35 d following heparin administration (two patients).	Heparin	173-180	serpin family C member 1	Homo sapiens	122-134
149555-7	1978	Repeated activation of the fibrinolytic system resulted in a shortening of the plasma radioactivity half-life of labelled antithrombin from 2.45 to 2.03 d in the absence of heparin (three patients), and from 3.13 to 2.35 d following heparin administration (two patients).	Heparin	233-240	serpin family C member 1	Homo sapiens	122-134
347919-5	1978	Heparin tremendously accelerates the inhibitory function of antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	60-76
347919-7	1978	Heparin retards the thrombin-fibrinogen reaction, but otherwise the effectiveness of heparin as an anticoagulant depends on antithrombin III in laboratory experiments, as well as in therapeutics.	Heparin	85-92	serpin family C member 1	Homo sapiens	124-140
71399-2	1977	In all patients, including 1 with congenital AT-III deficiency, heparin therapy was associated with a considerable progressive reduction in AT-III-binding capacity and antigenic protein.	Heparin	64-71	serpin family C member 1	Homo sapiens	45-51
71399-4	1977	Plasma-AT-III returned to normal two to three days after heparin was stopped.	Heparin	57-64	serpin family C member 1	Homo sapiens	7-13
71399-6	1977	When present in blood for long periods heparin significantly reduced AT-III, the proteinase inhibitor that is responsible for the anticoagulant effect of this drug.	Heparin	39-46	serpin family C member 1	Homo sapiens	69-75
71399-7	1977	The finding is very relevant to the interpretation of clinical data in patients treated with heparin and suggests that AT-III depletion may underly the thromboembolic complications sometimes encountered during heparin therapy.	Heparin	93-100	serpin family C member 1	Homo sapiens	119-125
71399-7	1977	The finding is very relevant to the interpretation of clinical data in patients treated with heparin and suggests that AT-III depletion may underly the thromboembolic complications sometimes encountered during heparin therapy.	Heparin	210-217	serpin family C member 1	Homo sapiens	119-125
8511754-5	1993	Nevertheless, by gel-filtering platelets in the presence of 5 micrograms/ml heparin, we prepared platelets that were virtually free of PF4.	Heparin	76-83	platelet factor 4	Homo sapiens	135-138
410640-9	1977	In conclusion, the marked structural similarity of human and bovine antithrombin indicates that the two proteins may also exhibit extensive functional similarities in the binding of heparin and the inhibition of various coagulation factors.	Heparin	182-189	serpin family C member 1	Homo sapiens	68-80
8511754-7	1993	In contrast, neither the high- nor the low-affinity heparin binding capacity of these cells was altered, indicating that PF4, even though it binds to both heparin and platelets, appears not to link heparin to platelets.	Heparin	155-162	platelet factor 4	Homo sapiens	121-124
639306-3	1978	The dose of heparin (100 I.U./kg body weight) used intravenously to get maximal release of both HL and LPL was the same in patients and in healthy individuals.	Heparin	12-19	lipoprotein lipase	Homo sapiens	103-106
8511754-7	1993	In contrast, neither the high- nor the low-affinity heparin binding capacity of these cells was altered, indicating that PF4, even though it binds to both heparin and platelets, appears not to link heparin to platelets.	Heparin	155-162	platelet factor 4	Homo sapiens	121-124
631129-1	1978	Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable.	Heparin	124-131	serpin family C member 1	Homo sapiens	174-190
631129-1	1978	Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable.	Heparin	124-131	serpin family C member 1	Homo sapiens	204-220
884118-6	1977	The release of these four histones (H2A, H2B, H3, and H4) is coordinate and occurs in a highly cooperative manner, as indicated by (1) dependence of the initial kinetics of histone removal upon heparin concentration, (2) analysis of DNA and histones in the fractions obtained from differential sedimentation of heparin-treated nuclei, and (3) analysis of the products from heparin-treated nuclei by equilibrium centrifugation in metrizamide density gradients.	Heparin	311-318	H2B clustered histone 21	Homo sapiens	41-56
8387369-4	1993	Characterization of DNA helicases after further purification on heparin column revealed that the DNA helicase in the DNA polymerase alpha fraction required ATP (or dCTP) in addition to ATP (or dATP).	Heparin	64-71	DNA polymerase alpha 1, catalytic subunit	Homo sapiens	117-137
884847-2	1977	Heparin scarcely affects the ASAT determination, but the ALAT activity in plasma is about 70% of the activity in serum, when the enzyme determination is carried out in Tris buffer.	Heparin	0-7	ATP binding cassette subfamily B member 7	Homo sapiens	29-33
631129-2	1978	It is suggested that heparin accelerates the thrombin antithrombin-III reaction by interacting with thrombin.	Heparin	21-28	serpin family C member 1	Homo sapiens	54-70
75564-6	1978	These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography.	Heparin	134-141	serpin family C member 1	Homo sapiens	43-59
75564-6	1978	These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography.	Heparin	134-141	lipoprotein lipase	Homo sapiens	114-117
75564-6	1978	These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography.	Heparin	152-159	serpin family C member 1	Homo sapiens	43-59
75564-6	1978	These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography.	Heparin	152-159	lipoprotein lipase	Homo sapiens	114-117
560216-0	1977	Effect of heparin modification on its activity in enhancing the inhibition of thrombin by antithrombin III.	Heparin	10-17	serpin family C member 1	Homo sapiens	90-106
8452552-2	1993	EC-SOD C, the high-heparin-affinity type, exposed to immobilized trypsin and plasmin was found to rapidly lose its affinity for heparin, without any loss of enzymic activity or major change in molecular mass as judged by size-exclusion chromatography.	Heparin	128-135	plasminogen	Homo sapiens	77-84
74632-0	1978	Heparin-induced decrease in circulating antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-56
8096177-6	1993	Direct binding analysis showed that NDF binds with high affinity (Kd approximately 10(-9) M) to mammary cells, but its weak association with ovarian cells is probably mediated by heparin-like molecules.	Heparin	179-186	neuregulin 1	Homo sapiens	36-39
735880-9	1978	The effect of heparin in these patients is impaired since the heparin co-factor, which is identical with AT III, is lowered.	Heparin	14-21	serpin family C member 1	Homo sapiens	105-111
139938-4	1977	About 50% of heart cell lipase activity applied to heparin-Sepharose bound to the gel and was eluted with a NaCl gradient.	Heparin	51-58	lipase G, endothelial type	Rattus norvegicus	24-30
849484-3	1977	Thus, the unique specificity for heparin in the anticoagulation system (which involves two or more lysine residues on the antithrombin molecule) is not paralleled by the findings with the basic homopolymers.	Heparin	33-40	serpin family C member 1	Homo sapiens	122-134
857429-1	1977	Antithrombin III (AT III) was determined in 290 patients with deep venous thrombosis and/or pulmonary embolism by immunological methods (radial immunodiffusion, Laurell technique) and by biological activity (heparin cofactor activity and anti-Xa activity).	Heparin	208-215	serpin family C member 1	Homo sapiens	0-16
201820-7	1978	Hepatic triglyceride lipase and lipoprotein lipase activities in post-heparin plasma were found to be low despite normal triglyceride concentrations.	Heparin	70-77	lipoprotein lipase	Homo sapiens	32-50
7678252-7	1993	Furthermore, TAT in patient plasmas (disseminated intravascular coagulation and sepsis) was found to bind to heparin-Sepharose, indicating that this endogenously formed TAT was also associated with VN.	Heparin	109-116	tyrosine aminotransferase	Homo sapiens	13-16
303667-5	1977	Evidence is presented which supports previous findings that C1-INH, alpha1-AT, and antithrombin (in the presence of heparin) contribute to factor XIIa and XI a inactivation in ellagic acid-activated plasma and that plasma albumin may compete with factor XII for ellagic acid binding.	Heparin	116-123	serpin family C member 1	Homo sapiens	83-95
353657-6	1977	When heparin is incorporated in the agarose plate, the electrophoretic mobility of this polymerized antithrombin III is not modified.	Heparin	5-12	serpin family C member 1	Homo sapiens	100-116
146278-0	1977	Role of heparin in the inactivation of thrombin, factor Xa, and plasmin by antithrombin III.	Heparin	8-15	serpin family C member 1	Homo sapiens	75-91
601748-0	1977	Heparin-like effect of polymethacrylic acid on the reaction between thrombin and antithrombin-III.	Heparin	0-7	serpin family C member 1	Homo sapiens	81-97
601749-0	1977	Decreased binding of heparin to antithrombin following the interaction between antithrombin and thrombin.	Heparin	21-28	serpin family C member 1	Homo sapiens	32-44
836327-0	1977	Evidence for a heparin-induced conformational change on antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	56-72
65891-4	1977	Immunoreactive AT III showed a positive correlation to both AT III and heparin cofactor activities.	Heparin	71-78	serpin family C member 1	Homo sapiens	15-21
601749-0	1977	Decreased binding of heparin to antithrombin following the interaction between antithrombin and thrombin.	Heparin	21-28	serpin family C member 1	Homo sapiens	79-91
7678252-7	1993	Furthermore, TAT in patient plasmas (disseminated intravascular coagulation and sepsis) was found to bind to heparin-Sepharose, indicating that this endogenously formed TAT was also associated with VN.	Heparin	109-116	tyrosine aminotransferase	Homo sapiens	169-172
579514-0	1977	Studies of heparin affinity to antithrombin III and other proteins in vitro and in vivo.	Heparin	11-18	serpin family C member 1	Homo sapiens	31-47
200085-0	1977	Lipoprotein lipase and hepatic lipase activity in post-heparin plasma of patients with hypertriglyceridemia.	Heparin	55-62	lipoprotein lipase	Homo sapiens	0-18
7686384-2	1993	We analysed the relationship between the binding of aFGF on the HAR and on the LAR in bovine lens epithelial (BEL) cells in the presence of heparin or suramin.	Heparin	140-147	fibroblast growth factor 1	Bos taurus	52-56
579516-7	1977	A possible explanation may be that the normal liver removes heparin bound to antithrombin III, and that this function is impaired in liver cirrhosis.	Heparin	60-67	serpin family C member 1	Homo sapiens	77-93
579490-5	1977	Heparin itself was neutralized in thrombin-AT III reaction losing its anticoagulant property in proportion to the amount of thrombin bound by inhibitor.	Heparin	0-7	serpin family C member 1	Homo sapiens	43-49
579490-6	1977	This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex.	Heparin	36-43	serpin family C member 1	Homo sapiens	110-116
579490-6	1977	This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex.	Heparin	36-43	serpin family C member 1	Homo sapiens	201-207
1006626-0	1976	Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin iii and by gel filtration.	Heparin	28-35	serpin family C member 1	Homo sapiens	92-108
7686384-6	1993	It has been observed that heparin at 10 micrograms/ml (1) in cross-linking experiments, reduces by half the total number of HAR complexes by preventing the formation of the 150 kDa complex but does not affect the 135 kDa complex, (2) in binding experiments, suppress the spontaneous formation of the 125I aFGF dimer bound to LAR, and then its internalization and degradation in the cells.	Heparin	26-33	fibroblast growth factor 1	Bos taurus	305-309
8362268-6	1993	In the HC II-mediated inhibition of thrombin, heparin and lactobionic acid both had strong inhibitory actions.	Heparin	46-53	serpin family D member 1	Homo sapiens	7-12
1283096-4	1992	A single heparin-Sepharose chromatography of the ultrafiltrates yielded essentially homogenous, biologically active, recombinant rat aFGF or bFGF.	Heparin	9-16	fibroblast growth factor 2	Rattus norvegicus	141-145
974107-0	1976	The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III.	Heparin	49-56	serpin family C member 1	Homo sapiens	92-108
974107-2	1976	Two molecules of 1-anilino-8-naphthalenesulfonate were found to bind per antithrombin molecule with an average dissociation constant of 4.4-10(-5) M. The binding of heparin to antithrombin was studied by ultraviolet difference spectroscopy.	Heparin	165-172	serpin family C member 1	Homo sapiens	73-85
974107-2	1976	Two molecules of 1-anilino-8-naphthalenesulfonate were found to bind per antithrombin molecule with an average dissociation constant of 4.4-10(-5) M. The binding of heparin to antithrombin was studied by ultraviolet difference spectroscopy.	Heparin	165-172	serpin family C member 1	Homo sapiens	176-188
974107-3	1976	The stoichiometry of the heparin binding indicated 1.8 binding sites with an average dissociation constant of 4.3 - 10(-6) M. Further the fluorometric competition experiments with 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate indicated two different classes of anion binding sites on the antithrombin molecule.	Heparin	25-32	serpin family C member 1	Homo sapiens	310-322
872292-8	1977	However, in experiments in which Xa inhibitory activity of antithrombin III is altered by heparin, a simple formula, Total activity (%) = 65% + 0.35 x human plasma (%), permits translation of rabbit data on the Xa-antithrombin III-heparin reaction to man.	Heparin	90-97	serpin family C member 1	Homo sapiens	59-75
330064-5	1977	The basis for this phenomenon is most probably the binding of the heparin-antithrombin cofactor (AT III) to a complex with heparin and thrombin.	Heparin	66-73	serpin family C member 1	Homo sapiens	97-103
1280230-3	1992	CSK and TPK-IIB once resolved from each other by heparin-Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp60c-src, namely Tyr-416 and Tyr-527.	Heparin	49-56	C-terminal Src kinase	Homo sapiens	0-3
865246-2	1977	Lipoprotein lipase and hepatic triglyceride lipase were differentiated by assay under high and low salt conditions and also by separation on heparin-agarose affinity chromatography columns.	Heparin	141-148	lipoprotein lipase	Homo sapiens	0-18
142314-0	1977	The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin.	Heparin	90-97	serpin family C member 1	Homo sapiens	44-60
407761-0	1977	[The studies on the influence of heparin on the reaction of antithrombin with thrombin, and the optimal dosis of heparin in the reaction (author"s transl)].	Heparin	33-40	serpin family C member 1	Homo sapiens	60-72
854877-0	1977	Evaluation of an amidolytic heparin assay method: increased sensitivity by adding purified antithrombin III.	Heparin	28-35	serpin family C member 1	Homo sapiens	91-107
60879-1	1976	An assay technic for measuring heparin cofactor activity in which antithrombin activity can be assessed without plasma attenuation even in the presence of therapeutic levels of heparin is presented.	Heparin	31-38	serpin family C member 1	Homo sapiens	66-78
982345-0	1976	Inhibition of the activated Cls subunit of the first component of complement by antithrombin III in the presence of heparin.	Heparin	116-123	serpin family C member 1	Homo sapiens	80-96
8061-1	1976	Human heart lipoprotein lipase was purified by affinity chromatography on heparin-Sepharose 4B.	Heparin	74-81	lipoprotein lipase	Homo sapiens	12-30
1425685-6	1992	Rhodopsin kinase is inhibited by heparin, but not by the protein inhibitor of cAMP-dependent protein kinase.	Heparin	33-40	G protein-coupled receptor kinase 1	Drosophila melanogaster	0-16
1247538-4	1976	Lipoprotein lipase active in perfused adipose tissue had significantly different kinetic properties, including a low substrate affinity (Km" 0.70 mM triglyceride), diffusion dependence of Km" at low flow rates, and slow release of enzyme by heparin.	Heparin	241-248	lipoprotein lipase	Homo sapiens	0-18
402555-4	1977	Since disorders of hemostasis due to therapy occur sporadically, early postoperative raising of the dose of heparin should only be done under regular laboratory controll, to which activated PTT and antithrombin time is well suited.	Heparin	108-115	serpin family C member 1	Homo sapiens	198-210
64653-0	1977	A heparin analogue with specific action on antithrombin III.	Heparin	2-9	serpin family C member 1	Homo sapiens	43-59
64653-3	1977	When given by parenteral injection, the heparin analogue had almost the same potentiating effect on antithrombin III as mucous heparin, but without a comparable effect on the K.C.C.T.	Heparin	40-47	serpin family C member 1	Homo sapiens	100-116
1430226-1	1992	Interaction of heparin with basic fibroblast growth factor.	Heparin	15-22	fibroblast growth factor 2	Rattus norvegicus	28-58
209676-6	1977	The simultaneous elevation of LPL and PHE activity in type IV and V patients with a high serum lipoprotein concentration shows that the response of patients with extreme HLP to heparin is more pronounced.	Heparin	177-184	lipoprotein lipase	Homo sapiens	30-33
754468-5	1977	Thrombin inactivation by antithrombin did not proceed at 0 degrees C in 60 min, but the interaction between thrombin and antithrombin was facilitated in the presence of heparin.	Heparin	169-176	serpin family C member 1	Homo sapiens	25-37
754468-5	1977	Thrombin inactivation by antithrombin did not proceed at 0 degrees C in 60 min, but the interaction between thrombin and antithrombin was facilitated in the presence of heparin.	Heparin	169-176	serpin family C member 1	Homo sapiens	121-133
1430226-3	1992	Since the initiation of SMC proliferation is mediated by basic fibroblast growth factor (bFGF), we have investigated the possibility that heparin inhibits SMC proliferation by displacing bFGF from the arterial wall.	Heparin	138-145	fibroblast growth factor 2	Rattus norvegicus	187-191
1430226-4	1992	Using a rat carotid artery model of balloon catheter injury, we demonstrate that a bolus injection of heparin depletes the arterial wall of both systemically administered bFGF and of endogenous bFGF.	Heparin	102-109	fibroblast growth factor 2	Rattus norvegicus	171-175
1430226-4	1992	Using a rat carotid artery model of balloon catheter injury, we demonstrate that a bolus injection of heparin depletes the arterial wall of both systemically administered bFGF and of endogenous bFGF.	Heparin	102-109	fibroblast growth factor 2	Rattus norvegicus	194-198
1430226-7	1992	SMC proliferation induced in a denuded artery by injection of bFGF is inhibited almost completely by a bolus injection of heparin; however, pretreatment with a bolus of heparin does not prevent SMC from responding to a subsequent bolus of bFGF.	Heparin	122-129	fibroblast growth factor 2	Rattus norvegicus	62-66
63389-0	1977	Structural requirements for the interaction of heparin with antithrombin III.	Heparin	47-54	serpin family C member 1	Homo sapiens	60-76
1430226-8	1992	These experiments suggest that heparin can inhibit SMC proliferation in part by removal of released bFGF from sites of injury.	Heparin	31-38	fibroblast growth factor 2	Rattus norvegicus	100-104
1411526-2	1992	To investigate this difference in Ca2+ signaling, airway epithelial cells were loaded with heparin, an inositol 1,4,5-triphosphate (IP3) receptor antagonist, by pulsed, high-frequency electroporation.	Heparin	91-98	inositol 1,4,5-trisphosphate receptor type 3	Homo sapiens	132-145
75141-0	1977	[The role of heparin in thrombin inhibition by antithrombin].	Heparin	13-20	serpin family C member 1	Homo sapiens	47-59
402327-2	1977	Antithrombin III (AT-III), being an alpha2-globulin, will have an electrophoretic mobility in the presence of heparin like prealbumin in agarose gels.	Heparin	110-117	serpin family C member 1	Homo sapiens	0-16
402327-2	1977	Antithrombin III (AT-III), being an alpha2-globulin, will have an electrophoretic mobility in the presence of heparin like prealbumin in agarose gels.	Heparin	110-117	serpin family C member 1	Homo sapiens	18-24
1329921-3	1992	At low concentrations of PF4, the activity of LMW heparins in the thrombin generation test was neutralized less than that of UFH, but at higher PF4 concentrations all their activities could be neutralized except in anti-Xa assays.	Heparin	125-128	platelet factor 4	Homo sapiens	25-28
402327-3	1977	This phenomenon was utilized to quantitate AT-III from serum and plasma by electroimmunodiffusion (EID) for 90 min agarose gels containing 75 USP units of heparin/ml gel.	Heparin	155-162	serpin family C member 1	Homo sapiens	43-49
1468448-6	1992	Additionally, when EC were treated with either 1 mM beta-D xyloside, an inhibitor of proteoglycan assembly, or 100 micrograms/ml heparin, there was a 40% reduction in matrix-associated bFGF (quantified by image analysis of antibody stained cultures).	Heparin	129-136	fibroblast growth factor 2	Mus musculus	185-189
557071-1	1977	The binding of heparin to antithrombin III and the antithrombin III--thrombin complex.	Heparin	15-22	serpin family C member 1	Homo sapiens	26-42
557071-1	1977	The binding of heparin to antithrombin III and the antithrombin III--thrombin complex.	Heparin	15-22	serpin family C member 1	Homo sapiens	51-67
557071-2	1977	A two-dimensional immunoelectrophoretic method has been used to obtain information on the binding of heparin to purified antithrombin III and the antithrombin III--thrombin complex.	Heparin	101-108	serpin family C member 1	Homo sapiens	121-137
557071-2	1977	A two-dimensional immunoelectrophoretic method has been used to obtain information on the binding of heparin to purified antithrombin III and the antithrombin III--thrombin complex.	Heparin	101-108	serpin family C member 1	Homo sapiens	146-162
557071-3	1977	The difference in mobility of the components in a gel containing heparin enables distinction between free and complexed forms of antithrombin III.	Heparin	65-72	serpin family C member 1	Homo sapiens	129-145
557071-4	1977	The results obtained with purified preparations show that heparin is bound more strongly to antithrombin III than to the antithrombin III--thrombin complex.	Heparin	58-65	serpin family C member 1	Homo sapiens	92-108
557071-4	1977	The results obtained with purified preparations show that heparin is bound more strongly to antithrombin III than to the antithrombin III--thrombin complex.	Heparin	58-65	serpin family C member 1	Homo sapiens	121-137
557071-5	1977	In plasma heparin is bound to several components, only a fraction being bound to antithrombin III.	Heparin	10-17	serpin family C member 1	Homo sapiens	81-97
976270-2	1976	It was demonstrated that one molecule of heparin was able to promote the binding of a large number of antithrombin molecules to thrombin.	Heparin	41-48	serpin family C member 1	Homo sapiens	102-114
976270-3	1976	Thus heparin may affect the rate of the inactivation of thrombin by antithrombin in a catalytic manner.	Heparin	5-12	serpin family C member 1	Homo sapiens	68-80
1402341-4	1992	The inhibitory effect of PF4 could be abrogated by the addition of heparin (5 to 10 micrograms/ml).	Heparin	67-74	platelet factor 4	Homo sapiens	25-28
1278445-0	1976	Anticoagulant activity of heparin: separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin.	Heparin	26-33	serpin family C member 1	Homo sapiens	138-150
1402341-6	1992	Binding of 125I-PF4 to HEL cells reached equilibrium within 20 to 30 minutes with dissociation constant of 1.3 x 10(-10)M and Bmax of 6.3 pmol/10(5) cells and was inhibited by an excess of unlabeled PF4, beta TG, and heparin but was not affected by PMA, IL-3, IL-6, GM-CSF, and interferon-alpha.	Heparin	217-224	platelet factor 4	Homo sapiens	16-19
819194-10	1976	Therefore, the decrease of DAO release after heparin stimulation in patients with chronic renal failure may be explained, in part, by inhibition of the enzyme as well as by a decreased coenzyme level.	Heparin	45-52	D-amino acid oxidase	Homo sapiens	27-30
1402341-8	1992	These data demonstrate that PF4 inhibits the growth of HEL cells by specific binding to HEL cells and suggest that the action of PF4 may be associated with the heparin-binding sites of the molecule.	Heparin	160-167	platelet factor 4	Homo sapiens	28-31
1402341-8	1992	These data demonstrate that PF4 inhibits the growth of HEL cells by specific binding to HEL cells and suggest that the action of PF4 may be associated with the heparin-binding sites of the molecule.	Heparin	160-167	platelet factor 4	Homo sapiens	129-132
1351851-9	1992	One milligram per milliliter of heparin, a concentration that inhibited bFGF-induced neurite outgrowth, also inhibited bFGF-induced increases in S6 phosphorylation and ODC activity.	Heparin	32-39	fibroblast growth factor 2	Rattus norvegicus	72-76
1259970-8	1976	In the presence of heparin, the bound lipase is released in the medium in amounts representing one-third to one half the total activity contained in the cells.	Heparin	19-26	lipase G, endothelial type	Rattus norvegicus	38-44
1259970-14	1976	During incubations in the presence of heparin, it was observed that the release of monoester lipase was quantitatively related to a simultaneous decrease in membrane-bound as well as in total monoester lipase activity measureable in the cells after homogenization.	Heparin	38-45	lipase G, endothelial type	Rattus norvegicus	93-99
1259970-14	1976	During incubations in the presence of heparin, it was observed that the release of monoester lipase was quantitatively related to a simultaneous decrease in membrane-bound as well as in total monoester lipase activity measureable in the cells after homogenization.	Heparin	38-45	lipase G, endothelial type	Rattus norvegicus	202-208
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	27-34	serpin family C member 1	Homo sapiens	223-235
1191673-1	1975	It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy.	Heparin	102-109	serpin family C member 1	Homo sapiens	223-235
1351851-9	1992	One milligram per milliliter of heparin, a concentration that inhibited bFGF-induced neurite outgrowth, also inhibited bFGF-induced increases in S6 phosphorylation and ODC activity.	Heparin	32-39	fibroblast growth factor 2	Rattus norvegicus	119-123
1315738-1	1992	Protein C inhibitor is a plasma protein whose ability to inhibit activated protein C, thrombin, and other enzymes is stimulated by heparin.	Heparin	131-138	serpin family A member 5	Homo sapiens	0-19
812191-5	1975	units of heparin per kilogram of body weight per hour released more lipoprotein lipase than the fat emulsion alone.	Heparin	9-16	lipoprotein lipase	Homo sapiens	68-86
1315738-2	1992	These studies were undertaken to further understand how heparin binds to protein C inhibitor and how it accelerates proteinase inhibition.	Heparin	56-63	serpin family A member 5	Homo sapiens	73-92
1315738-2	1992	These studies were undertaken to further understand how heparin binds to protein C inhibitor and how it accelerates proteinase inhibition.	Heparin	56-63	endogenous retrovirus group K member 18	Homo sapiens	116-126
53066-1	1975	Human and bovine antithrombin II/III have been isolated by a simple procedure essentially using only affinity chromatography on heparin-agarose and polyethylene glycol precipitation.	Heparin	128-135	serpin family C member 1	Homo sapiens	17-36
1315738-3	1992	The region of protein C inhibitor from residues 264-283 was identified as the heparin-binding site.	Heparin	78-85	serpin family A member 5	Homo sapiens	14-33
1315738-5	1992	The glycosaminoglycan specificity of protein C inhibitor was relatively broad, including heparin and heparan sulfate, but not dermatan sulfate.	Heparin	89-96	serpin family A member 5	Homo sapiens	37-56
1315738-9	1992	The optimum heparin concentration for maximal rate stimulation varied from 10 to 100 micrograms/ml and was related to the apparent affinity of the proteinase for heparin.	Heparin	12-19	endogenous retrovirus group K member 18	Homo sapiens	147-157
1315738-9	1992	The optimum heparin concentration for maximal rate stimulation varied from 10 to 100 micrograms/ml and was related to the apparent affinity of the proteinase for heparin.	Heparin	162-169	endogenous retrovirus group K member 18	Homo sapiens	147-157
1315738-12	1992	The importance of protein C inhibitor as a regulator of the protein C system may depend on the relatively large increase in heparin-enhanced inhibition rate for activated protein C compared to other proteinases.	Heparin	124-131	serpin family A member 5	Homo sapiens	18-37
1123348-8	1975	It was therefore concluded that C-5 inversion of D-glucuronic acid to L-iduronic acid occurred on the polymer level as shown previously for the biosynthesis of heparin (Hook, M., Lindahl, U., Backstrom, G., Malmstrom, A., AND Fransson, L-A., J. Biol.	Heparin	160-167	complement C5	Homo sapiens	32-35
1315743-5	1992	These peptides completely reversed nearly total inhibition of CK2 phosphotransferase activity toward itself, casein, and phosvitin by either heparin or poly(Glu,Tyr; 4:1), whereas CK2-NT was ineffective.	Heparin	141-148	casein kinase 2 beta	Homo sapiens	121-130
1387549-1	1992	N-desulphated heparin, partially N-acylated on average with three oleoyl chains per molecule, inhibits the amidolytic activity of plasmin (IC50 16 nM) and urokinase (IC50 10mM) when assayed on N-p-tosyl-Gly-Pro-Lys-4-nitroanilide and benzoyl-Ala-Gly-Arg-4-nitroanilide substrates respectively.	Heparin	14-21	plasminogen	Homo sapiens	130-137
24194402-2	1975	aureus by human blood leukocyte lysates, by extracts of rabbit small intestines and pancreas, and by the "cocktail" of enzymes (containing trypsin, lysolecithin, and lysozyme) is strongly inhibited by anionic polyelectrolytes (e.g., heparin, chondroitin sulfate, liquoid (polyanethole sulfonic acid), and DNA).	Heparin	233-240	lysozyme C-like	Oryctolagus cuniculus	166-174
1115795-0	1975	Action of heparin on thrombin-antithrombin reaction.	Heparin	10-17	serpin family C member 1	Homo sapiens	30-42
4846413-11	1974	MBP precipitated DNA, neutralized heparin, and activated papain.	Heparin	34-41	myelin basic protein	Cavia porcellus	0-3
1536850-0	1992	Importance of size and sulfation of heparin in release of basic fibroblast growth factor from the vascular endothelium and extracellular matrix.	Heparin	36-43	fibroblast growth factor 2	Rattus norvegicus	58-88
5548506-0	1971	Lipoprotein-lipase responses to heparin.	Heparin	32-39	lipoprotein lipase	Homo sapiens	0-18
1536850-1	1992	We have characterized the importance of size, sulfation, and anticoagulant activity of heparin in release of basic fibroblast growth factor (bFGF) from the subendothelial extracellular matrix (ECM) and the luminal surface of the vascular endothelium.	Heparin	87-94	fibroblast growth factor 2	Rattus norvegicus	109-139
5536999-2	1970	Influence of 3,5-dimethylisoxazole on heparin induced increase of lipoproteinlipase and non esterified fatty acids].	Heparin	38-45	lipoprotein lipase	Homo sapiens	66-83
1536850-1	1992	We have characterized the importance of size, sulfation, and anticoagulant activity of heparin in release of basic fibroblast growth factor (bFGF) from the subendothelial extracellular matrix (ECM) and the luminal surface of the vascular endothelium.	Heparin	87-94	fibroblast growth factor 2	Rattus norvegicus	141-145
1536850-2	1992	For this purpose, 125I-bFGF was first incubated with ECM and confluent endothelial cell cultures, or administered as a bolus into the blood of rats, the immobilized 125I-bFGF was then subjected to release by various chemically modified species of heparin and size-homogeneous oligosaccharides derived from depolymerized heparin.	Heparin	247-254	fibroblast growth factor 2	Rattus norvegicus	23-27
1536850-2	1992	For this purpose, 125I-bFGF was first incubated with ECM and confluent endothelial cell cultures, or administered as a bolus into the blood of rats, the immobilized 125I-bFGF was then subjected to release by various chemically modified species of heparin and size-homogeneous oligosaccharides derived from depolymerized heparin.	Heparin	320-327	fibroblast growth factor 2	Rattus norvegicus	23-27
4971215-0	1968	[The behavior of histaminase, diamine oxidase and benzylamine oxidase in the blood plasma of guinea pigs and man following intravenous injection of heparin].	Heparin	148-155	amiloride-sensitive amine oxidase [copper-containing]	Cavia porcellus	30-45
1536850-4	1992	Likewise, substitution of N-sulfate groups of heparin and low molecular weight heparin (fragmin) by acetyl or hexanoyl residues resulted in an almost complete inhibition of bFGF release by these polysaccharides.	Heparin	46-53	fibroblast growth factor 2	Rattus norvegicus	173-177
1536850-4	1992	Likewise, substitution of N-sulfate groups of heparin and low molecular weight heparin (fragmin) by acetyl or hexanoyl residues resulted in an almost complete inhibition of bFGF release by these polysaccharides.	Heparin	79-86	fibroblast growth factor 2	Rattus norvegicus	173-177
1311947-1	1992	Low-molecular-weight heparin subfractions more specifically inhibit factor Xa than thrombin, and they may have advantages over unfractionated heparin in arterial thrombosis.	Heparin	21-28	coagulation factor II, thrombin	Sus scrofa	83-91
5643308-0	1968	Protamine, polybrene and the antithrombin action of heparin.	Heparin	52-59	serpin family C member 1	Homo sapiens	29-41
4966101-0	1968	The effect of heparin on diamine oxidase and lipoprotein lipase in human lymph and blood plasma.	Heparin	14-21	lipoprotein lipase	Homo sapiens	45-63
1311947-9	1992	It was less effective than 100 units/kg unfractionated heparin, except at high dosages, producing similar prolongation of the aPTT and the thrombin time.	Heparin	55-62	coagulation factor II, thrombin	Sus scrofa	139-147
5637480-0	1968	Highly purified antithrombin 3 with heparin cofactor activity prepared by disc electrophoresis.	Heparin	36-43	serpin family C member 1	Homo sapiens	16-28
1730066-7	1992	The bone inductive protein, osteogenin, was isolated by heparin affinity chromatography.	Heparin	56-63	bone morphogenetic protein 3	Homo sapiens	28-38
5994635-0	1966	[Determination of activity of lipoprotein lipase in plasma following heparin administration by means of the bromsulphalein method].	Heparin	69-76	lipoprotein lipase	Homo sapiens	30-48
1323979-2	1992	Heparin or heparinase pretreatment of the cells inhibits the specific binding of [125I]-bFGF by over 70%, and abolishes binding to the low-affinity sites.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	88-92
1289680-5	1992	Because of the propensity of human prostate cancer to metastasize to the bone, this study defined a 1.0 M NaCl-eluted fraction, MS1, from the conditioned medium of a bone stromal cell line (MS) by heparin-affinity column chromatography.	Heparin	197-204	MS	Homo sapiens	128-131
14264516-0	1965	POST-HEPARIN LIPOLYTIC ACTIVITY FOLLOWING INTRAVENOUS HEPARIN-S35.	Heparin	5-12	solute carrier family 35 member G1	Homo sapiens	0-4
1309590-0	1992	Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	45-75
13888345-0	1962	[Relation between variations of plasmatic clearing and antithrombin power after heparin and fatty meal].	Heparin	80-87	serpin family C member 1	Homo sapiens	55-67
1309590-1	1992	Heparin is required for the binding of basic fibroblast growth factor (bFGF) to high-affinity receptors on cells deficient in cell surface heparan sulfate proteoglycan.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	39-69
13648508-0	1959	[Antithrombin effect of heparin under the influence of activating and inhibitory factors].	Heparin	24-31	serpin family C member 1	Homo sapiens	1-13
1309590-1	1992	Heparin is required for the binding of basic fibroblast growth factor (bFGF) to high-affinity receptors on cells deficient in cell surface heparan sulfate proteoglycan.	Heparin	0-7	fibroblast growth factor 2	Mus musculus	71-75
1944270-4	1991	Increasing concentrations of heparin not only compete for Int-2 binding in a dose-dependent manner but also inhibit the growth of these cells and revert the transformed phenotype.	Heparin	29-36	fibroblast growth factor 3	Mus musculus	58-63
13417492-0	1957	[Mechanism of action of heparin as antithrombin and dynamics of fibrin formation].	Heparin	24-31	serpin family C member 1	Homo sapiens	35-47
13243272-0	1955	[Thrombin time and antithrombin power of human plasma in the presence of heparin and some synthetic heparinoids].	Heparin	73-80	serpin family C member 1	Homo sapiens	19-31
1262050-5	1976	Purified C1q aggregated heparin-protamine complexes formed or forming in the presence or absence of serum.	Heparin	24-31	complement C1q A chain	Homo sapiens	9-12
1725227-1	1991	Protein C inhibitor (PCI) is a heparin-dependent serpin present in a native form in plasma at concentrations of 5 micrograms/mL.	Heparin	31-38	serpin family A member 5	Homo sapiens	0-19
789043-5	1976	Heparin is a potent inhibitor of several steps on the intrinsic coagulation pathway through its effect on a plasma cofactor, antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	125-141
13198841-0	1954	The antithrombin activity of heparin.	Heparin	29-36	serpin family C member 1	Homo sapiens	4-16
1725227-1	1991	Protein C inhibitor (PCI) is a heparin-dependent serpin present in a native form in plasma at concentrations of 5 micrograms/mL.	Heparin	31-38	serpin family A member 5	Homo sapiens	21-24
33929278-8	2021	Heparin potentiates antithrombin and hirudin binds to active thrombin, inactivating the thrombin irreversibly.	Heparin	0-7	serpin family C member 1	Homo sapiens	20-32
34056268-3	2021	In the present study, we analyzed the effect of amyloid-beta-derived peptidomimetics for inhibiting heparin-induced tau aggregation in vitro.	Heparin	100-107	microtubule associated protein tau	Homo sapiens	116-119
942661-2	1976	An acute intravenous injection of heparin produced the following changes in enzyme activities: in serum, phospholipase and lipase were increased, cholesterol esterase unchanged; in tissues phospholipase was increased, lipase was increased in heart and liver but decreased in aorta, cholesterol esterase was increased in heart but decreased in liver and aorta.	Heparin	34-41	carboxyl ester lipase	Homo sapiens	282-302
1209544-0	1975	Adverse effect of heparin in thrombin-antithrombin III interaction.	Heparin	18-25	serpin family C member 1	Homo sapiens	38-54
1209544-8	1975	These results may have some bearings on the approach to heparin therapy in the event when thrombin continuously generates or when a marked deficiency of antithrombin III exists.	Heparin	56-63	serpin family C member 1	Homo sapiens	153-169
1201212-2	1975	Mixing various quantities of heparin with agarose in the first phase of electrophoresis, AT-III from normal human plasma and serum revealed a heterogeneity which depended on the heparin concentration in the agarose gel.	Heparin	29-36	serpin family C member 1	Homo sapiens	89-95
1725227-4	1991	PCI antigen was assayed by ELISA and PCI activity was measured by its capability to form complexes with APC in the presence of heparin.	Heparin	127-134	serpin family A member 5	Homo sapiens	0-3
1201212-2	1975	Mixing various quantities of heparin with agarose in the first phase of electrophoresis, AT-III from normal human plasma and serum revealed a heterogeneity which depended on the heparin concentration in the agarose gel.	Heparin	178-185	serpin family C member 1	Homo sapiens	89-95
1201212-3	1975	At heparin concentrations higher than 16 u/ml, AT-III displayed three components with different electrophoretic mobilities.	Heparin	3-10	serpin family C member 1	Homo sapiens	47-53
1725227-4	1991	PCI antigen was assayed by ELISA and PCI activity was measured by its capability to form complexes with APC in the presence of heparin.	Heparin	127-134	serpin family A member 5	Homo sapiens	37-40
1201212-10	1975	It is concluded that high molecular weight complexes between AT-III and activated coagulation factors may be present in normally circulating blood and that their detection and possibly quantitation can be achieved using the heparin/agarose crossed immunoelectrophoresis system.	Heparin	224-231	serpin family C member 1	Homo sapiens	61-67
33601159-1	2021	The highly anionic synthetic pentasaccharide fondaparinux (FDPX) - representing the antithrombin binding sequence of heparin - is in clinical use as a potent anticoagulant.	Heparin	117-124	serpin family C member 1	Homo sapiens	84-96
1725227-4	1991	PCI antigen was assayed by ELISA and PCI activity was measured by its capability to form complexes with APC in the presence of heparin.	Heparin	127-134	APC regulator of WNT signaling pathway	Homo sapiens	104-107
1716989-1	1991	The potentiation of mouse liver derived heparin binding growth factors 1 and 2 (HBGF-1, HBGF-2) activity has been investigated.	Heparin	40-47	fibroblast growth factor 2	Mus musculus	88-94
1835913-1	1991	Recently, platelet factor 4 (PF4) release by heparin (heparin-releasable PF4) has been examined as a useful marker of the interaction between the substances liberated from circulating platelets and the vascular endothelium.	Heparin	45-52	platelet factor 4	Homo sapiens	29-32
33917853-0	2021	Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods.	Heparin	52-59	serpin family C member 1	Homo sapiens	36-48
33917853-1	2021	Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin.	Heparin	88-95	serpin family C member 1	Homo sapiens	0-12
1154312-3	1975	However, when heparin was mixed with agarose in the first phase of electrophoresis, the propositus" plasma displayed a different AT-III pattern from normal plasma.	Heparin	14-21	serpin family C member 1	Homo sapiens	129-135
1835913-1	1991	Recently, platelet factor 4 (PF4) release by heparin (heparin-releasable PF4) has been examined as a useful marker of the interaction between the substances liberated from circulating platelets and the vascular endothelium.	Heparin	45-52	platelet factor 4	Homo sapiens	73-76
1835913-1	1991	Recently, platelet factor 4 (PF4) release by heparin (heparin-releasable PF4) has been examined as a useful marker of the interaction between the substances liberated from circulating platelets and the vascular endothelium.	Heparin	54-61	platelet factor 4	Homo sapiens	29-32
1835913-1	1991	Recently, platelet factor 4 (PF4) release by heparin (heparin-releasable PF4) has been examined as a useful marker of the interaction between the substances liberated from circulating platelets and the vascular endothelium.	Heparin	54-61	platelet factor 4	Homo sapiens	73-76
1129269-1	1975	There was a positive correlation in normal man between heparin releasable lipoprotein lipase and lipoprotein lipase of ammonium hydroxide homongenate of acetoneether powder in adipose tissue.	Heparin	55-62	lipoprotein lipase	Homo sapiens	74-92
1835913-2	1991	We compared the plasma levels of PF4 and beta-thromboglobulin (beta-TG) after intravenous heparin injection in patients with coronary artery disease (CAD) and normal control subjects.	Heparin	90-97	platelet factor 4	Homo sapiens	33-36
1129269-1	1975	There was a positive correlation in normal man between heparin releasable lipoprotein lipase and lipoprotein lipase of ammonium hydroxide homongenate of acetoneether powder in adipose tissue.	Heparin	55-62	lipoprotein lipase	Homo sapiens	97-115
1129269-2	1975	Heparin releasable as lipoprotein lipase activity was about twice as high as the enzymatic activity in acetone powder, even though 40-70% of the original activity remained in the tissue after incubation with heparin.	Heparin	0-7	lipoprotein lipase	Homo sapiens	22-40
33826208-2	2021	In comparison, only the R3 repeat forms the core of the heparin-induced fibrils of the three repeat tau isoforms.&nbsp; For developing therapeutics, it is desirable to have an <italic>in vitro</italic> tau aggregation system producing fibrils corresponding to the disease morphology.	Heparin	56-63	microtubule associated protein tau	Homo sapiens	100-103
33826208-2	2021	In comparison, only the R3 repeat forms the core of the heparin-induced fibrils of the three repeat tau isoforms.&nbsp; For developing therapeutics, it is desirable to have an <italic>in vitro</italic> tau aggregation system producing fibrils corresponding to the disease morphology.	Heparin	56-63	microtubule associated protein tau	Homo sapiens	202-205
1129269-2	1975	Heparin releasable as lipoprotein lipase activity was about twice as high as the enzymatic activity in acetone powder, even though 40-70% of the original activity remained in the tissue after incubation with heparin.	Heparin	208-215	lipoprotein lipase	Homo sapiens	22-40
33826208-3	2021	Here we report the self-aggregation of truncated tau segment R3R4 peptide without requiring heparin for aggregation induction.	Heparin	92-99	microtubule associated protein tau	Homo sapiens	49-52
1835913-2	1991	We compared the plasma levels of PF4 and beta-thromboglobulin (beta-TG) after intravenous heparin injection in patients with coronary artery disease (CAD) and normal control subjects.	Heparin	90-97	pro-platelet basic protein	Homo sapiens	41-61
33860518-4	2021	Thus, by activating antithrombin, heparin mainly inhibits factor Xa and thrombin, whereas VKAs lower the levels of the vitamin K-dependent clotting factors.	Heparin	34-41	serpin family C member 1	Homo sapiens	20-32
5761-5	1975	The soluble phospholipase A is inhibited by albumin, soluble protein (cytoplasmic), heparin, and protamine sulfate.	Heparin	84-91	phospholipase A and acyltransferase 1	Homo sapiens	12-27
1835913-2	1991	We compared the plasma levels of PF4 and beta-thromboglobulin (beta-TG) after intravenous heparin injection in patients with coronary artery disease (CAD) and normal control subjects.	Heparin	90-97	pro-platelet basic protein	Homo sapiens	63-70
4809149-0	1974	Evaluation of the BART test (a modification of the whole-blood activated recalcification time test) as a means of monitoring heparin therapy.	Heparin	125-132	ADP ribosylation factor like GTPase 2 binding protein	Homo sapiens	18-22
1835913-6	1991	There was a significant difference in plasma PF4 levels at 5 min after heparin injection between the CAD group (100.1 +/- 38.1) and the control group (61.0 +/- 24.0) (p less than 0.01).	Heparin	71-78	platelet factor 4	Homo sapiens	45-48
33065736-6	2021	ODN antisense for RHAMM, however, attenuated LMWH-induced hyperalgesia in female rats treated with ODN antisense to GPR30, as well as in ovariectomized females.	Heparin	45-49	CD44 molecule (Indian blood group)	Rattus norvegicus	18-23
1835913-7	1991	The PF4/beta-TG ratio after heparin injection was also higher in the CAD group than in the control group (p less than 0.01).	Heparin	28-35	platelet factor 4	Homo sapiens	4-7
33065736-6	2021	ODN antisense for RHAMM, however, attenuated LMWH-induced hyperalgesia in female rats treated with ODN antisense to GPR30, as well as in ovariectomized females.	Heparin	45-49	G protein-coupled estrogen receptor 1	Rattus norvegicus	116-121
2070076-6	1991	Plasma LACI levels were elevated in women undergoing the early stages of labor (29%), in patients receiving intravenous tissue-type plasminogen activator (45%), and in patients receiving intravenous heparin (375%).	Heparin	199-206	tissue factor pathway inhibitor	Homo sapiens	7-11
4608937-0	1974	Lipoprotein lipase and its interaction with heparin.	Heparin	44-51	lipoprotein lipase	Homo sapiens	0-18
33690235-8	2020	Global transcriptional analysis revealed that the expression of Amphiregulin (Areg), a gene encoding a heparin-binding epidermal growth factor receptor ligand, was decreased drastically in Sox17+/- uterine epithelia.	Heparin	103-110	SRY (sex determining region Y)-box 17	Mus musculus	189-194
1711938-3	1991	METHODS AND RESULTS: Western-blot analysis of heparin-bound material from neonatal heart extracts identified a single band with a molecular weight of approximately 18 kD for both bFGF and aFGF.	Heparin	46-53	fibroblast growth factor 2	Rattus norvegicus	179-183
33746978-5	2021	In this study, we clarified the actions of DcR3 and its non-decoy action motif heparin sulfate proteoglycan (HSPG) binding domain (HBD) in the MSU crystal-induced NLRP3 inflammasome activation in the macrophages and in mice.	Heparin	79-86	NLR family, pyrin domain containing 3	Mus musculus	163-168
4201585-0	1973	On the elimination of transfused heparin-induced diamine oxidase (DAO) activity in rabbits.	Heparin	33-40	D-amino-acid oxidase	Oryctolagus cuniculus	49-64
4201585-0	1973	On the elimination of transfused heparin-induced diamine oxidase (DAO) activity in rabbits.	Heparin	33-40	D-amino-acid oxidase	Oryctolagus cuniculus	66-69
4661518-0	1972	[Behavior of placental lactogen level in serum and estradiol excretion in pregnant women under the treatment for EPH (edema, proteinuria, hypertension) gestosis with heparin and complamin].	Heparin	166-173	EPH receptor A1	Homo sapiens	113-116
1832572-5	1991	The heparin-induced PF4 release, which is reported to reflect release of PF4 attached on endothelial cells, was significantly reduced in 12 asymptomatic asthmatic patients compared with 11 normal subjects, and it was much more reduced in 7 symptomatic asthmatic patients, suggesting the possibility of the reduced PF4 binding on endothelial cell surface.	Heparin	4-11	platelet factor 4	Homo sapiens	20-23
1832572-5	1991	The heparin-induced PF4 release, which is reported to reflect release of PF4 attached on endothelial cells, was significantly reduced in 12 asymptomatic asthmatic patients compared with 11 normal subjects, and it was much more reduced in 7 symptomatic asthmatic patients, suggesting the possibility of the reduced PF4 binding on endothelial cell surface.	Heparin	4-11	platelet factor 4	Homo sapiens	73-76
5059200-3	1972	Addition of heparin to the eluted fractions markedly stimulated activity of LPL(a), but suppressed that of LPL(b).	Heparin	12-19	lipoprotein lipase	Homo sapiens	76-79
33187852-0	2021	Successful Antithrombin Administration in Andexanet Alfa-Associated Heparin Resistance.	Heparin	68-75	serpin family C member 1	Homo sapiens	11-23
1832572-5	1991	The heparin-induced PF4 release, which is reported to reflect release of PF4 attached on endothelial cells, was significantly reduced in 12 asymptomatic asthmatic patients compared with 11 normal subjects, and it was much more reduced in 7 symptomatic asthmatic patients, suggesting the possibility of the reduced PF4 binding on endothelial cell surface.	Heparin	4-11	platelet factor 4	Homo sapiens	73-76
5059200-3	1972	Addition of heparin to the eluted fractions markedly stimulated activity of LPL(a), but suppressed that of LPL(b).	Heparin	12-19	lipoprotein lipase	Homo sapiens	107-110
1646716-2	1991	The relationship between thrombomodulin-associated O-linked glycosammoglycans (GAGs) and the exogenous GAGs heparin or dermatan sulfate was studied in the inhibition of thrombin by antithrombin III (AT III) or heparin cofactor II (HC II).	Heparin	108-115	thrombomodulin	Oryctolagus cuniculus	25-39
6035543-0	1967	Heparin cofactor and plasma antithrombin in relation to the mechanism of inactivation of thrombin by heparin.	Heparin	101-108	serpin family C member 1	Homo sapiens	28-40
32536326-12	2021	Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003).	Heparin	99-106	serpin family C member 1	Homo sapiens	0-12
32536326-12	2021	Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003).	Heparin	99-106	serpin family C member 1	Homo sapiens	0-12
32536326-14	2021	Utilization of a goal-directed algorithm for the administration of antithrombin for the treatment of heparin resistance is effective in patients undergoing cardiac surgery.	Heparin	101-108	serpin family C member 1	Homo sapiens	67-79
1718466-4	1991	The mean plasma HCII level was significantly higher in patients with acute deep vein thrombosis (DVT) under heparin therapy than in patients with a history of thrombosis, who were studied more than 3 months after the acute event, and were either on, or had been on, oral anticoagulant therapy.	Heparin	108-115	serpin family D member 1	Homo sapiens	16-20
32650697-3	2021	Antithrombin is administered to potentiate heparin"s effects.	Heparin	43-50	serpin family C member 1	Homo sapiens	0-12
14258688-2	1964	ACTION OF BLOOD PLATELETS AND THEIR PHOSPHOLIPID SUBSTITUTES ON THE ANTITHROMBIN ACTIVITY OF HEPARIN].	Heparin	93-100	serpin family C member 1	Homo sapiens	68-80
14162310-0	1964	SERUM REQUIREMENT FOR RELEASE OF HEPARIN-INDUCED LIPASE FROM PERFUSED RAT HEART.	Heparin	33-40	lipase G, endothelial type	Rattus norvegicus	49-55
13895954-0	1961	Demonstration of lipoprotein lipase activity (free fatty acid release) by in vitro sonic oscillation (sonation) of post-heparin plasma from subjects with "heparin-unresponsive" hyperglyceridemia (hyperlipemia).	Heparin	120-127	lipoprotein lipase	Homo sapiens	17-35
13895954-0	1961	Demonstration of lipoprotein lipase activity (free fatty acid release) by in vitro sonic oscillation (sonation) of post-heparin plasma from subjects with "heparin-unresponsive" hyperglyceridemia (hyperlipemia).	Heparin	155-162	lipoprotein lipase	Homo sapiens	17-35
33508081-11	2021	This low anticoagulant heparin version, a novel TLR4 agonist, could contribute to human cervical ripening during the initiation of labour.	Heparin	23-30	toll like receptor 4	Homo sapiens	48-52
33476796-3	2021	Our analyses show that both recombinant Sod3a and Sod3b express SOD activity, however, only Sod3b is able to bind heparin.	Heparin	114-121	superoxide dismutase 3, extracellular a	Danio rerio	40-45
33476796-3	2021	Our analyses show that both recombinant Sod3a and Sod3b express SOD activity, however, only Sod3b is able to bind heparin.	Heparin	114-121	superoxide dismutase 3, extracellular b	Danio rerio	50-55
33476796-3	2021	Our analyses show that both recombinant Sod3a and Sod3b express SOD activity, however, only Sod3b is able to bind heparin.	Heparin	114-121	superoxide dismutase 3, extracellular b	Danio rerio	92-97
1706960-0	1991	Inhibition of tumor growth in mice by an analogue of platelet factor 4 that lacks affinity for heparin and retains potent angiostatic activity.	Heparin	95-102	platelet factor 4	Homo sapiens	53-70
33869655-5	2021	We also fused the heparin-binding (HB) domain from HB epidermal growth factor-like growth factor (HB-EGF) to LAMA2(G1-5) to test whether this would increase muscle ECM expression.	Heparin	18-25	heparin-binding EGF-like growth factor	Mus musculus	98-104
13341284-0	1956	[Plasmatic cofactor of heparin and its relations with antithrombin].	Heparin	23-30	serpin family C member 1	Homo sapiens	54-66
1829439-6	1991	The increase in plasma PF4 was related to the effect of heparin.	Heparin	56-63	platelet factor 4	Homo sapiens	23-26
14945138-0	1952	[The antithrombin effect of heparin.	Heparin	28-35	serpin family C member 1	Homo sapiens	5-17
33567713-0	2021	Suppression of Hypoxia-Inducible Factor 1alpha by Low-Molecular-Weight Heparin Mitigates Ventilation-Induced Diaphragm Dysfunction in a Murine Endotoxemia Model.	Heparin	71-78	hypoxia inducible factor 1, alpha subunit	Mus musculus	15-46
1821782-3	1991	Like hPF4, our recombinant hPF4 (rhPF4) is tetrameric under physiological conditions, binds heparin, and inhibits angiogenesis.	Heparin	92-99	platelet factor 4	Homo sapiens	27-31
14875159-0	1951	Identification of a heparin as a main component of the third factor involved in the virulence-enhancing action of hog gastric mucin.	Heparin	20-27	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	118-131
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	129-136	serpin family D member 1	Homo sapiens	0-19
32920809-13	2021	On crossed immunoelectrophoresis, an increase of antithrombin fractions with reduced heparin affinity was observed under high ionic strength conditions but not under physiological conditions.	Heparin	85-92	serpin family C member 1	Homo sapiens	49-61
32920809-17	2021	CONCLUSION:  Antithrombin p.Thr147Ala, responsible for antithrombin type II heparin binding site deficiency, is the first founder mutation reported in people of African ancestry.	Heparin	76-83	serpin family C member 1	Homo sapiens	13-25
32920809-17	2021	CONCLUSION:  Antithrombin p.Thr147Ala, responsible for antithrombin type II heparin binding site deficiency, is the first founder mutation reported in people of African ancestry.	Heparin	76-83	serpin family C member 1	Homo sapiens	55-67
33982044-4	2021	Here, a multifunctional, structurally simple strategy involving heparin-loaded sutures (PPH) that are clinically applicable is reported, in the form of electrospun core-shell nanofibers, with the ability to perform sustained release of anticoagulants heparin (verified in our previous publication) for the improvement of the healing of Achilles tendon.	Heparin	64-71	enolase 1	Homo sapiens	88-91
33982044-4	2021	Here, a multifunctional, structurally simple strategy involving heparin-loaded sutures (PPH) that are clinically applicable is reported, in the form of electrospun core-shell nanofibers, with the ability to perform sustained release of anticoagulants heparin (verified in our previous publication) for the improvement of the healing of Achilles tendon.	Heparin	251-258	enolase 1	Homo sapiens	88-91
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	129-136	serpin family D member 1	Homo sapiens	21-25
1673023-3	1991	Administration of 1 ml of Intralipid (500 microliters at -30 min and 500 microliters at -25 min) plus heparin (50 IU at -15 min) induced a marked decrease in GH responses to both 1 and 5 micrograms/kg of GHRH (p less than 0.01 at 5, 10 and 15 min for GHRH alone vs. GHRH plus Intralipid).	Heparin	102-109	growth hormone releasing hormone	Rattus norvegicus	204-208
33983722-0	2021	Inclusion of the C-Terminal Domain in the beta-Sheet Core of Heparin-Fibrillized Three-Repeat Tau Protein Revealed by Solid-State Nuclear Magnetic Resonance Spectroscopy.	Heparin	61-68	microtubule associated protein tau	Homo sapiens	94-97
33983722-3	2021	Here, we use solid-state NMR spectroscopy to identify the beta-sheet core of full-length 0N3R tau fibrillized using heparin.	Heparin	116-123	microtubule associated protein tau	Homo sapiens	94-97
33789211-5	2021	In this paper, we have shown that the SARS-CoV-2 S1 RBD binds to a number of aggregation-prone, heparin binding proteins including Abeta, alpha-synuclein, tau, prion, and TDP-43 RRM.	Heparin	96-103	synuclein alpha	Homo sapiens	138-153
33789211-5	2021	In this paper, we have shown that the SARS-CoV-2 S1 RBD binds to a number of aggregation-prone, heparin binding proteins including Abeta, alpha-synuclein, tau, prion, and TDP-43 RRM.	Heparin	96-103	microtubule associated protein tau	Homo sapiens	155-158
33984343-9	2021	Heparin impaired the positive effect of hPL on cell growth.	Heparin	0-7	galectin 1	Homo sapiens	40-43
33901051-0	2021	A Tale of Two Centers: Is Low-Molecular-Weight Heparin Really Superior for Prevention of Post-Traumatic Venous Thromboembolism?	Heparin	47-54	solute carrier family 35 member G1	Homo sapiens	89-93
33901051-3	2021	We compared LMWH and UFH for prevention of post-traumatic deep venous thrombosis (DVT) and pulmonary embolism (PE).	Heparin	21-24	solute carrier family 35 member G1	Homo sapiens	43-47
33829789-4	2021	MOS inhibited heparin-induced aggregation of the Tau-K18 oligomer and suppressed the levels of phosphorylated Tau protein.	Heparin	14-21	microtubule associated protein tau	Homo sapiens	49-52
33829789-4	2021	MOS inhibited heparin-induced aggregation of the Tau-K18 oligomer and suppressed the levels of phosphorylated Tau protein.	Heparin	14-21	microtubule associated protein tau	Homo sapiens	110-113
34040631-5	2021	A temporary rise in post-heparin LPL concentration (1.5-2.5 times of controls) was noted during the early days of AP whilst LPL activity was consistently low (50~70% of controls).	Heparin	25-32	lipoprotein lipase	Homo sapiens	33-36
33610598-7	2021	The results indicated that heparin-iron has significantly reduced anticoagulant activity in vitro and in vivo, strongly decreases hepcidin mRNA and IL-6 induced high level of secreted hepcidin in HepG2 cell.	Heparin	27-34	hepcidin antimicrobial peptide	Homo sapiens	130-138
33610598-7	2021	The results indicated that heparin-iron has significantly reduced anticoagulant activity in vitro and in vivo, strongly decreases hepcidin mRNA and IL-6 induced high level of secreted hepcidin in HepG2 cell.	Heparin	27-34	hepcidin antimicrobial peptide	Homo sapiens	184-192
32882780-3	2021	Methods: We evaluated the practical use of heparin-conjugated PLGA nanoparticles (molecular weight ~15,000) in conjugation with VEGF-A/C, embryoid body (EB) formation, and LEC differentiation using immunofluorescence staining followed by quantification and quantitative real-time polymerase chain reaction (qPCR) analysis.	Heparin	43-50	laryngotracheo esophageal cleft	Mus musculus	172-175
33129446-3	2021	Both heparin (HP) and heparan sulfate (HS) bind to the N-lobe domain of hLF.	Heparin	5-12	HLF transcription factor, PAR bZIP family member	Homo sapiens	72-75
33129446-3	2021	Both heparin (HP) and heparan sulfate (HS) bind to the N-lobe domain of hLF.	Heparin	14-16	HLF transcription factor, PAR bZIP family member	Homo sapiens	72-75
32829961-4	2021	Reductions in circulating levels of Antithrombin III (AT), the primary mediator of heparin"s action, is present in cases of coronavirus related critical illness.	Heparin	83-90	serpin family C member 1	Homo sapiens	36-52
33401230-3	2021	In this study, a heparin oligosaccharide library, including dp2, dp4 and dp6, were prepared from the chemical modification of the fully sulfated dp2, dp4 and dp6.	Heparin	17-24	transcription factor Dp-2	Homo sapiens	60-63
33401230-3	2021	In this study, a heparin oligosaccharide library, including dp2, dp4 and dp6, were prepared from the chemical modification of the fully sulfated dp2, dp4 and dp6.	Heparin	17-24	transcription factor Dp-2	Homo sapiens	145-148
32452079-2	2021	Since cancer patients treated with the anticoagulant heparin showed reduced metastasis rates and improved survival, it is supposed that heparin suppresses the cloak"s formation by inhibiting the interaction between platelet"s adhesion molecule P-selectin with its ligands on cancer cells.	Heparin	53-60	selectin P	Homo sapiens	244-254
32452079-2	2021	Since cancer patients treated with the anticoagulant heparin showed reduced metastasis rates and improved survival, it is supposed that heparin suppresses the cloak"s formation by inhibiting the interaction between platelet"s adhesion molecule P-selectin with its ligands on cancer cells.	Heparin	136-143	selectin P	Homo sapiens	244-254
32452079-7	2021	The effect of heparin on P-selectin was tested using anti-P-selectin antibodies alone and in combination with heparin.	Heparin	14-21	selectin P	Homo sapiens	25-35
32452079-9	2021	Together, we quantified heparin"s antimetastatic effect and proved that it predominantly is related to the blockage of P-selectin.	Heparin	24-31	selectin P	Homo sapiens	119-129
33738401-2	2021	Although conservative treatment options for hereditary AT deficiency-associated VTE such as anticoagulation (warfarin, direct oral anticoagulant, or heparin), intravenous thrombolysis, and recombinant AT are well known, interventional treatment options have not been reported so far.	Heparin	149-156	serpin family C member 1	Homo sapiens	55-57
33453994-8	2020	We confirmed using immunofluorescence microscopy that heparin prevented uptake of alpha-synuclein PFFs into cells but that chloroquine did not stop alpha-synuclein uptake into lysosomes despite impairing lysosomal function and inhibiting alpha-synuclein toxicity.	Heparin	54-61	synuclein, alpha	Mus musculus	82-97
32853623-7	2020	Further, these substitutions also resulted in attenuation of stability and heparin binding affinity in the canine IL8 as compared to its human counterpart.	Heparin	75-82	C-X-C motif chemokine ligand 8	Canis lupus familiaris	114-117
33031793-8	2020	By using surface plasmon resonance assays, the equilibrium dissociation constants of both the open and closed conformations of beta2GPI showed a similar and strong affinity to isolated anti-beta2GPI autoantibodies (Kd closed beta2GPI = 5.17 x 10-8 M, Kd open beta2GPI = 5.56 x 10-8 M) and the open form had one order of magnitude stronger affinity to heparin (Kd = 0.30 x 10-6 M) compared to the closed conformation (Kd = 3.50 x 10-6 M).	Heparin	351-358	apolipoprotein H	Homo sapiens	127-135
33718796-0	2021	Timed Controlled Repeated Rotation of the CAR-170-C NXSTAGE Chronic Cartridge Hemodialysis Filter: A Novel Approach to Enabling Heparin-Free Frequent Daily Home Hemodialysis.	Heparin	128-135	CXADR pseudogene 1	Homo sapiens	42-45
32907762-3	2020	Clinical efficacy of heparin is due to its interaction with antithrombin (AT) that may be decreased in COVID-19.	Heparin	21-28	serpin family C member 1	Homo sapiens	60-72
32304324-2	2020	D-Glucuronyl C5-epimerase (C5-epi) is an enzyme acting on a heparin precursor, N-sulfoheparosan, catalyzing the reversible epimerization of D-glucuronic acid (GlcA) to L-iduronic acid (IdoA).	Heparin	60-67	glucuronic acid epimerase	Homo sapiens	0-25
32718661-4	2020	The prototypical heparin-binding protein is antithrombin III (AT), responsible for heparin"s anticoagulant/antithrombotic activity.	Heparin	17-24	serpin family C member 1	Homo sapiens	44-60
32897051-0	2020	Mapping the Structural and Dynamic Determinants of pH-sensitive Heparin Binding to Granulocyte Macrophage-colony Stimulating Factor.	Heparin	64-71	colony stimulating factor 2	Homo sapiens	83-131
32897051-2	2020	GMCSF is known to interact with other clinically important molecules, such as heparin, suggesting that endogenous and administered GMCSF has the potential to modulate orthogonal treatment outcomes.	Heparin	78-85	colony stimulating factor 2	Homo sapiens	0-5
32897051-2	2020	GMCSF is known to interact with other clinically important molecules, such as heparin, suggesting that endogenous and administered GMCSF has the potential to modulate orthogonal treatment outcomes.	Heparin	78-85	colony stimulating factor 2	Homo sapiens	131-136
32897051-4	2020	Here, we dissect the biophysical factors that facilitate the GMCSF-heparin interaction, previously shown to be pH-dependent, using NMR spectroscopy, SPR, and molecular dynamics simulations.	Heparin	67-74	colony stimulating factor 2	Homo sapiens	61-66
32897051-5	2020	We find that the affinity of GMCSF to bind heparin increases not only with a transition to acidic pH but also with an increase in heparin chain length.	Heparin	43-50	colony stimulating factor 2	Homo sapiens	29-34
32897051-5	2020	We find that the affinity of GMCSF to bind heparin increases not only with a transition to acidic pH but also with an increase in heparin chain length.	Heparin	130-137	colony stimulating factor 2	Homo sapiens	29-34
33005203-7	2020	Treatment with heparin significantly inhibited the upregulation of CD40, NF-kappaB, and HIF-1alpha induced by asphyxial CA.	Heparin	15-22	CD40 molecule	Rattus norvegicus	67-71
31977357-5	2020	The UFH rate decreased after the administration of both types of ATIII.	Heparin	4-7	serpin family C member 1	Homo sapiens	65-70
32404633-14	2020	Comprehensive cost analysis that includes anticoagulant, laboratories, and antithrombin III cost, showed that heparin anticoagulation therapy total cost was significantly higher than bivalirudin (1,184 dollars per day in heparin group vs 494 dollars per day in bivalirudin group; p = 0.03).	Heparin	110-117	serpin family C member 1	Homo sapiens	75-91
32229688-6	2020	Biochemical studies by heparin affinity chromatography and colocalization studies further supported a role of heparan sulphate proteoglycan in lipocalin uptake.	Heparin	23-30	glypican 3	Homo sapiens	110-139
32824699-3	2020	Previous reports have suggested that the glycosaminoglycan heparin is a ligand for the natural cytotoxicity receptors NKp30, NKp44 (human), and NKp46 (both human and mouse).	Heparin	59-66	natural cytotoxicity triggering receptor 3	Homo sapiens	118-123
32681841-3	2020	We have reported previously that a region of tau (297-391), referred to as dGAE, assembles spontaneously in physiological conditions to form paired helical filament-like fibres in vitro in the absence of additives such as heparin.	Heparin	222-229	microtubule associated protein tau	Homo sapiens	45-48
33005889-6	2020	As compared to tau filaments induced by heparin, those induced by dextran sulphate showed higher thioflavin T fluorescence and lower resistance to guanidine hydrochloride, which suggests that the two types of filaments have distinct conformational features.	Heparin	40-47	microtubule associated protein tau	Homo sapiens	15-18
32600401-16	2020	Timed-pregnant rats given a continuous infusion of unfractionated heparin exhibited an increased mean arterial pressure as well as decreased bioavailable VEGF compared to vehicle-treated animals.	Heparin	66-73	vascular endothelial growth factor A	Rattus norvegicus	154-158
32469847-1	2020	BACKGROUND Heparin, often used as an anticoagulant, acts by binding to antithrombin III.	Heparin	11-18	serpin family C member 1	Homo sapiens	71-87
32469847-2	2020	Indeed, heparin binds to a variety of proteins other than antithrombin III.	Heparin	8-15	serpin family C member 1	Homo sapiens	58-74
32402428-10	2020	This also has clinical implications: in the era of generics and biosimilars where biosimilar heparins begin to appear, it is important to know that accordingly to FDA and EMEA rules: their biosimilarity is judged only on the "classical" anticoagulation effect cofactor of antithrombin (anti-IIa/anti-Xa) but that all glycan effects that are potentially beneficial or potentially deleterious are not taken into consideration in their assessment.	Heparin	93-101	serpin family C member 1	Homo sapiens	272-284
33528157-2	2021	Unfractionated heparin (UFH) is commonly used, which depends on native antithrombin (AT) function to exert anticoagulant effects.	Heparin	15-22	serpin family C member 1	Homo sapiens	71-83
33528157-2	2021	Unfractionated heparin (UFH) is commonly used, which depends on native antithrombin (AT) function to exert anticoagulant effects.	Heparin	24-27	serpin family C member 1	Homo sapiens	71-83
33125521-3	2021	METHODS: Capitalising on the IL-2-binding capabilities of heparin, an injectable hydrogel incorporating clinical-grade heparin, collagen and hyaluronan polymers was used to deliver IL-2.	Heparin	58-65	interleukin 2	Mus musculus	29-33
33125521-3	2021	METHODS: Capitalising on the IL-2-binding capabilities of heparin, an injectable hydrogel incorporating clinical-grade heparin, collagen and hyaluronan polymers was used to deliver IL-2.	Heparin	58-65	interleukin 2	Mus musculus	181-185
33317395-7	2020	To visualize the polymorphisms of Tau and cysteine mutants under different aggregation conditions anionic cofactor, heparin was employed.	Heparin	116-123	microtubule associated protein tau	Homo sapiens	34-37
33343739-6	2021	Experience with low serum albumin levels and antithrombin III activity in nephrotic patients helps to point out the decreasing effects of loop diuretics and heparin to other specialist disciplines.	Heparin	157-164	serpin family C member 1	Homo sapiens	45-61
32799002-5	2020	Because heparin relies on AT to augment its physiologic function, patients with ATD often exhibit profound heparin resistance.	Heparin	8-15	serpin family C member 1	Homo sapiens	26-28
32799002-5	2020	Because heparin relies on AT to augment its physiologic function, patients with ATD often exhibit profound heparin resistance.	Heparin	107-114	serpin family C member 1	Homo sapiens	26-28
32945907-1	2020	The 3-O sulfate-modified -GlcNS3S6S- monosaccharide in heparin and heparan sulfate glycosaminoglycans (HSGAGs) is a relatively rare yet important modification that facilitates HSGAG-antithrombin binding and subsequent anticoagulant activity.	Heparin	55-62	serpin family C member 1	Homo sapiens	182-194
32682802-8	2020	Fifteen minutes after intravenous heparin injection (30 U/kg), her serum TG, LPL and HL concentrations turned to 14.1 mmol/l, 20 ng/ml and 660 ng/ml, respectively.	Heparin	34-41	lipoprotein lipase	Homo sapiens	77-80
32947474-1	2020	OBJECTIVES: Supplementation of antithrombin might decrease the amount of heparin needed to achieve a given anticoagulation target during extracorporeal membrane oxygenation.	Heparin	73-80	serpin family C member 1	Homo sapiens	31-43
32947474-3	2020	We conceived a study to evaluate the effect of antithrombin supplementation in adult patients requiring venovenous extracorporeal membrane oxygenation for respiratory failure on heparin dose, adequacy of anticoagulation, and safety.	Heparin	178-185	serpin family C member 1	Homo sapiens	47-59
33019549-7	2020	However, digitonin and heparin stimulated the conversion of PrP 91-104 into PrPSc 91-104 even after incubation with RML- and 22L-PrPSc-prions.	Heparin	23-30	PRP@	Bos taurus	60-63
31686597-1	2020	The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa.	Heparin	79-86	serpin family C member 1	Homo sapiens	16-28
31686597-1	2020	The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa.	Heparin	79-86	serpin family C member 1	Homo sapiens	30-32
31686597-1	2020	The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa.	Heparin	91-98	serpin family C member 1	Homo sapiens	16-28
31686597-1	2020	The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa.	Heparin	91-98	serpin family C member 1	Homo sapiens	30-32
31686597-8	2020	We could also confirm the high stability of helix P in non-activated AT conformations, such states might play an important role in heparin binding.	Heparin	131-138	serpin family C member 1	Homo sapiens	69-71
31608625-4	2020	These oligosaccharides must contain a Delta4,5-unsaturated uronic acid (DeltaUA) residue at the non-reducing end, which is due to the depolymerization reaction cata-lyzed by heparin lyases used during the compositional analysis procedure.	Heparin	174-181	delta like canonical Notch ligand 4	Homo sapiens	44-46
32388896-2	2020	Because these tetrasaccharides are derived from antithrombin III-binding sites of heparin, we examined whether this method could be applied to estimate the anticoagulant activity of heparin.	Heparin	82-89	serpin family C member 1	Homo sapiens	48-64
32452976-1	2020	OBJECTIVES: Antithrombin is a cofactor in the coagulation cascade with mild anticoagulant activity and facilitates the action of heparin as an anticoagulant.	Heparin	129-136	serpin family C member 1	Homo sapiens	12-24
32733248-8	2020	Heparin also inhibits cathepsin G, blocks P-selectin and L-selectin, hinders ligand binding to the receptor for advanced glycation endproducts, and impedes histone acetyltransferase activity which dampens cytokine transcription and High Mobility Group Box 1 release.	Heparin	0-7	cathepsin G	Homo sapiens	22-33
32733248-8	2020	Heparin also inhibits cathepsin G, blocks P-selectin and L-selectin, hinders ligand binding to the receptor for advanced glycation endproducts, and impedes histone acetyltransferase activity which dampens cytokine transcription and High Mobility Group Box 1 release.	Heparin	0-7	selectin P	Homo sapiens	42-52
32733248-8	2020	Heparin also inhibits cathepsin G, blocks P-selectin and L-selectin, hinders ligand binding to the receptor for advanced glycation endproducts, and impedes histone acetyltransferase activity which dampens cytokine transcription and High Mobility Group Box 1 release.	Heparin	0-7	selectin L	Homo sapiens	57-67
32347711-5	2020	When applied to a paradigmatic heparin/antithrombin system, the new method generates a series of oligomers with surprisingly distinct sulfation levels.	Heparin	31-38	serpin family C member 1	Homo sapiens	39-51
32336028-0	2020	Repairing peripheral nerve defects with revascularized tissue-engineered nerve based on a VEGF-heparin sustained release system.	Heparin	95-102	vascular endothelial growth factor A	Rattus norvegicus	90-94
32336028-1	2020	To enhance the angiogenic capacity of tissue-engineered peripheral nerves, we have constructed revascularized tissue-engineered nerves based on a Vascular endothelial growth factor (VEGF)-heparin sustained release system.	Heparin	188-195	vascular endothelial growth factor A	Rattus norvegicus	146-180
32336028-1	2020	To enhance the angiogenic capacity of tissue-engineered peripheral nerves, we have constructed revascularized tissue-engineered nerves based on a Vascular endothelial growth factor (VEGF)-heparin sustained release system.	Heparin	188-195	vascular endothelial growth factor A	Rattus norvegicus	182-186
32336028-5	2020	The results showed that the tissue-engineered peripheral nerve based on a VEGF-heparin sustained release system can achieve early vascularization and restore blood supply in the nerve graft area.	Heparin	79-86	vascular endothelial growth factor A	Rattus norvegicus	74-78
32413029-3	2020	As a heparan sulfate proteoglycan, perlecan (HSPG2) stores and stabilizes growth factors, including heparin-binding Wnt3A, a positive regulator of PCa cell growth.	Heparin	100-107	heparan sulfate proteoglycan 2	Homo sapiens	45-50
32410995-3	2020	Here, kaempferol was shown to bind with vascular endothelial growth factor (VEGF), probably in the heparin binding domain of VEGF: this binding potentiated the angiogenic functions of VEGF in various culture models.	Heparin	99-106	vascular endothelial growth factor A	Rattus norvegicus	76-80
32277030-0	2020	ZNF263 is a transcriptional regulator of heparin and heparan sulfate biosynthesis.	Heparin	41-48	zinc finger protein 263	Homo sapiens	0-6
32277030-7	2020	CRISPR-mediated targeting and siRNA knockdown of ZNF263 in mammalian cell lines and human primary cells led to dramatically increased expression levels of HS3ST1, a key enzyme involved in imparting anticoagulant activity to heparin, and HS3ST3A1, another glucosaminyl 3-O-sulfotransferase expressed in cells.	Heparin	224-231	zinc finger protein 263	Homo sapiens	49-55
32353952-0	2020	Low-Molecular-Weight Heparin Reduces Ventilation-Induced Lung Injury through Hypoxia Inducible Factor-1alpha in a Murine Endotoxemia Model.	Heparin	21-28	hypoxia inducible factor 1, alpha subunit	Mus musculus	77-108
31950133-10	2020	These data suggest that the antithrombin-binding regions of low molecular weight heparin is required to confer its protective effects on fetal growth and placental development.	Heparin	81-88	serpin family C member 1	Homo sapiens	28-40
32232808-2	2020	Laboratory values showed a homozygous mutation of factor V Leiden and we treated her initially with heparin, then with coumadin.	Heparin	100-107	coagulation factor V	Homo sapiens	50-65
32110917-6	2020	Light transmission aggregometry and ATP release assays confirmed that only those heparin derivatives with P-selectin blocking capacities were able to attenuate breast cancer cell-induced platelet activation, while pentasaccharide fondaparinux was without effects.	Heparin	81-88	selectin P	Homo sapiens	106-116
32069798-7	2020	Both NIH3T3 and A549 cells adhered to heparin/chitosan (HEP/CHI) film because HEP has an affinity for integrin through fibronectin.	Heparin	38-45	fibronectin 1	Mus musculus	119-130
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	heparin binding EGF like growth factor	Homo sapiens	134-140
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	insulin like growth factor binding protein 1	Homo sapiens	360-367
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	insulin like growth factor binding protein 1	Homo sapiens	369-413
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	LIF interleukin 6 family cytokine	Homo sapiens	415-418
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	LIF interleukin 6 family cytokine	Homo sapiens	420-446
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	interleukin 1 alpha	Homo sapiens	448-456
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	proteasome 26S subunit ubiquitin receptor, non-ATPase 4	Homo sapiens	551-555
31979118-6	2020	The highest affinity interaction was with the 30-kDa (heparin-binding) FN fragment, which also showed the greatest colocalization in cells and accommodated both HSP90 and heparin in the complex.	Heparin	54-61	heat shock protein 90 alpha family class A member 1	Homo sapiens	161-166
33214783-0	2020	Evaluation of Heparin Anti-Factor Xa Levels Following Antithrombin Supplementation in Pediatric Patients Supported With Extracorporeal Membrane Oxygenation.	Heparin	14-21	serpin family C member 1	Homo sapiens	54-66
33214783-2	2020	Heparin works by potentiating the effects of antithrombin (AT), which may be deficient in critically ill patients and can be replaced.	Heparin	0-7	serpin family C member 1	Homo sapiens	45-57
31797980-1	2019	Heparin is a widely used anticoagulant which inhibits factor Xa and thrombin through potentiation of antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	101-113
31232851-14	2019	Unfractionated heparin dose and baseline antithrombin activity level should be considered when dosing antithrombin in pediatric ventricular assist device patients.	Heparin	15-22	serpin family C member 1	Homo sapiens	102-114
31803745-4	2019	Consequently, the therapeutic potency of a heparin is determined by its aIIa activity, i.e., the concentration of a domain in which 12 sugar flank the high affinity antithrombin-binding pentasaccharide (HA5) at one side.	Heparin	43-50	serpin family C member 1	Homo sapiens	165-177
31634932-0	2019	Use of Antithrombin Concentrate for Acquired Antithrombin Deficiency in Acutely Unwell Children Receiving Unfractionated Heparin.	Heparin	121-128	serpin family C member 1	Homo sapiens	7-19
31351252-2	2019	Heparin-binding growth factor (HBGF) gradients are established in living systems by proteoglycans including the extracellular matrix heparan sulfate proteoglycan, perlecan/HSPG2.	Heparin	0-7	heparan sulfate proteoglycan 2	Homo sapiens	172-177
31471526-6	2019	Adoptively transferred Treg cells prevented spontaneous production of PF4/heparin-specific Abs in Foxp3-deficient mice and inhibited PF4/heparin complex-induced production of PF4/heparin-specific IgGs in wild-type mice.	Heparin	74-81	forkhead box P3	Mus musculus	98-103
31358628-4	2019	However, in vitro heparin-fibrillized 2N4R tau, which contains all four microtubule-binding repeats (4R), was recently found to adopt polymorphic structures.	Heparin	18-25	microtubule associated protein tau	Homo sapiens	43-46
31358628-5	2019	Here we use solid-state NMR spectroscopy to investigate the global fold and dynamics of heparin-fibrillized 0N4R tau.	Heparin	88-95	microtubule associated protein tau	Homo sapiens	113-116
31033049-9	2019	We found that a positive feedback loop of heparin-binding epidermal growth factor-like growth factor (HBEGF) and epidermal growth factor receptor (EGFR) signaling regulates astrocytes maturation.	Heparin	42-49	heparin binding EGF like growth factor	Homo sapiens	102-107
31336723-5	2019	This review will focus on HARE/Stabilin-2 and its interactions with hyaluronan, heparin, and phosphorothioate antisense oligonucleotides and what is known about how this receptor participates in signaling upon ligand binding.	Heparin	80-87	stabilin 2	Homo sapiens	26-30
31336723-5	2019	This review will focus on HARE/Stabilin-2 and its interactions with hyaluronan, heparin, and phosphorothioate antisense oligonucleotides and what is known about how this receptor participates in signaling upon ligand binding.	Heparin	80-87	stabilin 2	Homo sapiens	31-41
30986390-18	2019	BEST PRACTICE ADVICE 10: Systemic heparin infusion is recommended for symptomatic deep vein thrombosis and portal and mesenteric vein thrombosis, but there are unresolved issues regarding monitoring with both the anti-Xa assay and the partial thromboplastin time due to cirrhosis-related antithrombin deficiency (heparin cofactor).	Heparin	34-41	serpin family C member 1	Homo sapiens	288-300
1673023-3	1991	Administration of 1 ml of Intralipid (500 microliters at -30 min and 500 microliters at -25 min) plus heparin (50 IU at -15 min) induced a marked decrease in GH responses to both 1 and 5 micrograms/kg of GHRH (p less than 0.01 at 5, 10 and 15 min for GHRH alone vs. GHRH plus Intralipid).	Heparin	102-109	growth hormone releasing hormone	Rattus norvegicus	251-255
1673023-3	1991	Administration of 1 ml of Intralipid (500 microliters at -30 min and 500 microliters at -25 min) plus heparin (50 IU at -15 min) induced a marked decrease in GH responses to both 1 and 5 micrograms/kg of GHRH (p less than 0.01 at 5, 10 and 15 min for GHRH alone vs. GHRH plus Intralipid).	Heparin	102-109	growth hormone releasing hormone	Rattus norvegicus	251-255
1658969-4	1991	We have earlier reported that the extrinsic pathway inhibitor (EPI) is released to the blood after heparin injection.	Heparin	99-106	tissue factor pathway inhibitor	Homo sapiens	34-61
31018591-0	2019	Soluble Heparin and Heparan Sulfate Glycosaminoglycans Interfere with Sonic Hedgehog Solubilization and Receptor Binding.	Heparin	8-15	sonic hedgehog signaling molecule	Homo sapiens	70-84
31018591-6	2019	Consistent with the established binding of soluble heparin or HS to the Shh CW target motif, both polysaccharides impaired proteolytic Shh processing and release from source cells.	Heparin	51-58	sonic hedgehog signaling molecule	Homo sapiens	72-75
31018591-7	2019	We also show that HS and heparin bind to, and block, another set of basic amino acids required for unimpaired Shh binding to Ptc receptors on receiving cells.	Heparin	25-32	sonic hedgehog signaling molecule	Homo sapiens	110-113
2266131-4	1990	In contrast, binding and activation of hLS2 by heparin seem to be determined mainly by the positive charge density of the involved inhibitor segment.	Heparin	47-54	serpin family D member 1	Homo sapiens	39-43
30660005-6	2019	Docking and molecular dynamics analysis of a molecular model of HB-EGF led to the identification of residues in the heparin-binding domain of the protein being essential for the recognition of GAG derivatives.	Heparin	116-123	heparin binding EGF like growth factor	Homo sapiens	64-70
30660009-4	2019	In our study, a unique growth factor delivery vehicle composed of heparin and the synthetic polycation poly(ethylene argininylaspartate diglyceride) (PEAD) was used to sustain GDF5 release.	Heparin	66-73	myotrophin	Rattus norvegicus	23-36
30660009-11	2019	In our study, a unique growth factor delivery vehicle comprised of heparin and the synthetic polycation poly(ethylene argininylaspartate diglyceride) (PEAD) was used to sustain the release of GDF-5.	Heparin	67-74	myotrophin	Rattus norvegicus	23-36
30659446-4	2019	Heparin, a polysaccharide closely related to HS, also reduced the Hsp90-stimulated migration and invasion of cells.	Heparin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	66-71
2096488-1	1990	Heparin cofactor II (HCII) is a thrombin inhibitor present in human plasma whose activity is enhanced by heparin.	Heparin	105-112	serpin family D member 1	Homo sapiens	0-19
30406694-4	2019	The OppA sequence showed five potential domains for glycosaminoglycan-binding, and structural modelling of the protein showed that two of them were located in the vicinity of an OppA superficial groove whose width approached the diameter of the helical form of heparin in solution.	Heparin	261-268	OppA	Lactococcus lactis	4-8
30406694-4	2019	The OppA sequence showed five potential domains for glycosaminoglycan-binding, and structural modelling of the protein showed that two of them were located in the vicinity of an OppA superficial groove whose width approached the diameter of the helical form of heparin in solution.	Heparin	261-268	OppA	Lactococcus lactis	178-182
2096488-1	1990	Heparin cofactor II (HCII) is a thrombin inhibitor present in human plasma whose activity is enhanced by heparin.	Heparin	105-112	serpin family D member 1	Homo sapiens	21-25
2403299-8	1990	Injection of radioactive heparin confirmed that it does cross into the interstitial space in sufficient concentrations to displace lipase from peripheral cells.	Heparin	25-32	pancreatic lipase related protein 1	Canis lupus familiaris	131-137
30720432-0	2019	Heparin-induced tau filaments are polymorphic and differ from those in Alzheimer"s and Pick"s diseases.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	16-19
30720432-6	2019	The heparin-induced tau filaments differ from those of Alzheimer"s or Pick"s disease, which have larger cores with different repeat compositions.	Heparin	4-11	microtubule associated protein tau	Homo sapiens	20-23
30720432-6	2019	The heparin-induced tau filaments differ from those of Alzheimer"s or Pick"s disease, which have larger cores with different repeat compositions.	Heparin	4-11	protein interacting with PRKCA 1	Homo sapiens	70-74
2403299-9	1990	We conclude that most of the lipase found in lymph after heparin injection is derived from peripheral cells and not from plasma.	Heparin	57-64	pancreatic lipase related protein 1	Canis lupus familiaris	29-35
2143417-3	1990	The Km of plasmin formation is unaltered by the presence of either heparin or heparan.	Heparin	67-74	plasminogen	Homo sapiens	10-17
30377735-6	2019	Adding the anti-sFRP1 antibody (0.5 microg/ml) and inhibiting sFRP1 secretion by caffeine (5 mM) both relieved Dox-induced cardiotoxicity through activating Wnt/beta-catenin signaling, whereas increasing the secretion of sFRP1 by heparin (100 microg/ml) had the opposite effect.	Heparin	230-237	secreted frizzled-related protein 1	Rattus norvegicus	16-21
2143417-5	1990	Additionally, the lipoproteins lipoprotein(a) [Lp(a)] and low-density lipoprotein (LDL) inhibit the heparin enhancement of Pg activation.	Heparin	100-107	lipoprotein(a)	Homo sapiens	47-52
1974459-6	1990	Analysis of the primary structure of apoJ predicts the existence of amphiphilic helices, which may account for the association of apoJ with lipoproteins, and heparin-binding motifs in both subunits.	Heparin	158-165	clusterin	Homo sapiens	37-41
30056611-1	2019	U3-1565 is a monoclonal antibody directed against heparin-binding epidermal growth factor-like growth factor (HB-EGF), which mediates angiogenesis via induction of vascular endothelial growth factor (VEGF-A).	Heparin	50-57	heparin binding EGF like growth factor	Homo sapiens	110-116
2110916-4	1990	Therefore, the authors wished to see if diamine oxidase could be released by a low and safe dose of heparin (5000 U) and if the resultant area under the concentration-time curve would provide a noninvasive marker of segmental intestinal disease.	Heparin	100-107	amine oxidase copper containing 1	Homo sapiens	40-55
30303710-1	2019	Extracellular superoxide dismutase 3 (SOD3), one member of the antioxidant defense system and a superoxide scavenger, has been noted to be downregulated in the kidneys of diabetic mice and is characterized by a heparin-binding domain that can anchor the protein to the endothelium and extracellular matrix.	Heparin	211-218	superoxide dismutase 3, extracellular	Mus musculus	38-42
30218657-0	2018	An automated method for measuring lipoprotein lipase and hepatic triglyceride lipase activities in post-heparin plasma.	Heparin	104-111	lipoprotein lipase	Homo sapiens	34-52
2223005-2	1990	The lectin, which closely resembles those from chicken and rat tissues, was purified by heparin-affinity chromatography.	Heparin	88-95	galectin 3	Gallus gallus	4-10
30218657-3	2018	METHODS: The automated kinetic colorimetric method was used for assaying LPL and HTGL activity in the post-heparin plasma using the natural long-chain fatty acid 2-diglyceride as a substrate.	Heparin	107-114	lipoprotein lipase	Homo sapiens	73-76
30218657-8	2018	The measurement range of LPL activity in the post-heparin plasma was 30-153 U/L, while HTGL activity was 135-431 U/L in normal controls.	Heparin	50-57	lipoprotein lipase	Homo sapiens	25-28
30218657-9	2018	CONCLUSIONS: The L PL and HTGL activity assays are applicable to quantitating the LPL and HTGL activity in the post-heparin plasma.	Heparin	116-123	lipoprotein lipase	Homo sapiens	82-85
2310758-9	1990	The antibody R377, but not R385, interfered with the interaction of the enzyme with heparin, which is one of the characteristic properties of rat platelet phospholipase A2.	Heparin	84-91	phospholipase A2 group IIA	Rattus norvegicus	146-171
2106377-3	1990	At 96 hours, heparin 5, 25, and 125 micrograms/ml decreased [3H]proline incorporation into CDP by 41, 48, and 32%, respectively, with no significant change in NCP.	Heparin	13-20	cut-like homeobox 1	Rattus norvegicus	91-94
30253213-0	2018	Binding and structure-kinetic relationship analysis of selective TLR4-targeted immunosuppressive self-assembling heparin nanoparticles.	Heparin	113-120	toll like receptor 4	Homo sapiens	65-69
2106377-4	1990	To evaluate the possible role of PGE2 in these inhibitory responses, media PGE2 concentration was measured and the effects of heparin on CDP labeling and DNA synthesis were tested in the presence of indomethacin, piroxicam, and flurbiprofen to inhibit endogenous prostaglandin E2 (PGE2) production and in the presence of a high concentration (10(-7) M) of exogenous PGE2.	Heparin	126-133	cut-like homeobox 1	Rattus norvegicus	137-140
30253213-1	2018	Self-assembling aliphatic heparin derivatives were shown to inhibit the immune system by antagonizing Toll-like receptor 4/myeloid differentiation protein 2 (TLR4/MD2).	Heparin	26-33	toll like receptor 4	Homo sapiens	158-162
2106377-9	1990	Moreover, addition of heparin produced a further inhibition of CDP and DNA content and finally, heparin decreased CDP labeling by 71% in the presence of PGE2.	Heparin	22-29	cut-like homeobox 1	Rattus norvegicus	63-66
2106377-9	1990	Moreover, addition of heparin produced a further inhibition of CDP and DNA content and finally, heparin decreased CDP labeling by 71% in the presence of PGE2.	Heparin	96-103	cut-like homeobox 1	Rattus norvegicus	114-117
2331791-8	1990	Heparin-affinity high performance liquid chromatography (HPLC) showed a proportionately greater increase in levels of aFGF than bFGF between the tenth and fortieth postnatal days.	Heparin	0-7	fibroblast growth factor 2	Rattus norvegicus	128-132
30412630-9	2018	Low baseline EV-TF predicted a worse survival in the low molecular weight heparin as compared with the control group (HR 1.42; 95% CI 1.04-1.95; P = 0.03; P for interaction = 0.12).	Heparin	74-81	coagulation factor III, tissue factor	Homo sapiens	16-18
2302416-2	1990	Binding was linear up to a concentration of 0.5 microgram/ml (10 nM) enzyme used in this study, and equilibrium was achieved after 2 h of incubation with bovine 125I-LPL at 4 degrees C. Heparin and heparan sulfate effectively inhibited the binding of LPL to extracellular-matrix-coated plates; chondroitin sulfate had no effect, while high concentrations of dermatan sulfate or keratan sulfate inhibited binding of LPL to extracellular matrix by only 40%.	Heparin	186-193	lipoprotein lipase	Bos taurus	166-169
30118980-5	2018	As proof of principle, we generated alkyne-modified heparin, immobilized it onto azide-incorporated acellular lungs, and demonstrated its bioactivity by Antithrombin III immobilization and Factor Xa inhibition.	Heparin	52-59	serpin family C member 1	Homo sapiens	153-169
32254606-4	2018	In the present study, we designed a facile synthesis method to prepare near-infrared emitting denatured bovine serum albumin-templated copper nanoclusters (dBSA-Cu NCs) for the trace detection of heparin.	Heparin	196-203	albumin	Bos taurus	111-124
32254606-9	2018	Hence, the dBSA-Cu NCs can be used as a probe for the trace detection of heparin with a very low limit of detection (LOD) of 0.26 ng mL-1 in a linear range from 1.25 ng mL-1 to 250 ng mL-1.	Heparin	73-80	L1 cell adhesion molecule	Mus musculus	133-137
32254606-9	2018	Hence, the dBSA-Cu NCs can be used as a probe for the trace detection of heparin with a very low limit of detection (LOD) of 0.26 ng mL-1 in a linear range from 1.25 ng mL-1 to 250 ng mL-1.	Heparin	73-80	L1 cell adhesion molecule	Mus musculus	169-173
32254606-9	2018	Hence, the dBSA-Cu NCs can be used as a probe for the trace detection of heparin with a very low limit of detection (LOD) of 0.26 ng mL-1 in a linear range from 1.25 ng mL-1 to 250 ng mL-1.	Heparin	73-80	L1 cell adhesion molecule	Mus musculus	169-173
2156335-5	1990	The release of HL activity was equal with both heparins in man, but greater with unfractionated heparin in the rat.	Heparin	47-55	lipase C, hepatic type	Homo sapiens	15-17
29999301-1	2018	Factor Xa (fXa) inhibition by antithrombin (AT) enabled by heparin or heparan sulfate is critical for controlling blood coagulation.	Heparin	59-66	serpin family C member 1	Homo sapiens	30-42
30181723-1	2018	OBJECTIVES: Determine the effect of exogenous antithrombin III administration on low molecular weight heparin anti-Xa levels in the context of enoxaparin dosing in infants.	Heparin	102-109	serpin family C member 1	Homo sapiens	46-62
2156335-5	1990	The release of HL activity was equal with both heparins in man, but greater with unfractionated heparin in the rat.	Heparin	47-54	lipase C, hepatic type	Homo sapiens	15-17
2156335-8	1990	In liver tissue homogenate the two heparins showed the same ability to release HL activity.	Heparin	35-43	lipase C, hepatic type	Homo sapiens	79-81
32397894-6	2020	The aims of this work were (1) to convey increased awareness to clinicians who may experience defaulted, expected effect after antithrombin supplementation in, for example, heparin anticoagulation during extracorporeal life support and (2) to urge manufacturers to assess and disclose latent antithrombin content in their products.	Heparin	173-180	serpin family C member 1	Homo sapiens	127-139
32397894-6	2020	The aims of this work were (1) to convey increased awareness to clinicians who may experience defaulted, expected effect after antithrombin supplementation in, for example, heparin anticoagulation during extracorporeal life support and (2) to urge manufacturers to assess and disclose latent antithrombin content in their products.	Heparin	173-180	serpin family C member 1	Homo sapiens	292-304
29921298-7	2018	Post-heparin LPL activity and mass were also lower in the patient.	Heparin	5-12	lipoprotein lipase	Homo sapiens	13-16
2151097-4	1990	The obtained results call attention to the importance of final concentration of Mn2+ ions at HDL2 precipitation with DS from heparin-Mn2+ supernate containing HDL.	Heparin	125-132	junctophilin 3	Homo sapiens	93-97
29664486-0	2018	Heparin-induced tau filaments are structurally heterogeneous and differ from Alzheimer"s disease filaments.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	16-19
29664486-3	2018	This study shows that heparin-induced tau filaments are markedly different from the AD filaments and are highly heterogeneous.	Heparin	22-29	microtubule associated protein tau	Homo sapiens	38-41
32251304-8	2020	The effect of K18 on the yeast ribosome can be mitigated in the presence of cellular polyanions like heparin and tRNA, thereby indicating the electrostatic nature of the aggregation process.	Heparin	101-108	keratin 18	Homo sapiens	14-17
2322419-0	1990	Effects of different heparins on the enhancement of the thrombin-antithrombin reaction.	Heparin	21-29	coagulation factor II, thrombin	Sus scrofa	56-64
32231194-1	2020	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a member of the epidermal growth factor family and has a variety of physiological and pathophysiological functions.	Heparin	0-7	heparin binding EGF like growth factor	Homo sapiens	60-66
29340361-5	2018	Gel retardation and heparin competition assays showed that DP-Cur formed stable complexes with miR21ASO.	Heparin	20-27	microRNA 21	Homo sapiens	95-103
2322419-4	1990	Thus, the slow reactions in the case of bovine and pig HA-heparins were probably due to preferential binding of the two HA-heparins to thrombin rather than to ATIII, thus causing the HA-heparins to be inhibitory for the reaction by reducing the turnover rates of the polysaccharides as catalysts.	Heparin	58-66	coagulation factor II, thrombin	Sus scrofa	135-143
2322419-4	1990	Thus, the slow reactions in the case of bovine and pig HA-heparins were probably due to preferential binding of the two HA-heparins to thrombin rather than to ATIII, thus causing the HA-heparins to be inhibitory for the reaction by reducing the turnover rates of the polysaccharides as catalysts.	Heparin	123-131	coagulation factor II, thrombin	Sus scrofa	135-143
2322419-6	1990	Since the strength of the interactions of these HA-heparins with thrombin was in the order, pig greater than or equal to bovine greater than whale, the faster reactions were probably due to higher associations of the enzyme with the essential HA-heparin-ATIII complex.	Heparin	51-59	coagulation factor II, thrombin	Sus scrofa	65-73
32000579-6	2020	Cleaved osteopontin was higher in plasma from patients with aortic stenosis receiving crystalloid compared with blood cardioplegia, likely because of less heparin-induced inhibition of thrombin.	Heparin	155-162	secreted phosphoprotein 1	Homo sapiens	8-19
2124565-0	1990	Is the intestine the sole source of heparin-stimulated plasma diamine oxidase?	Heparin	36-43	amine oxidase, copper containing 1	Rattus norvegicus	62-77
27624738-0	2018	Antithrombin Administration During Intravenous Heparin Anticoagulation in the Intensive Care Unit: A Single-Center Matched Retrospective Cohort Study.	Heparin	47-54	serpin family C member 1	Homo sapiens	0-12
27624738-1	2018	Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition.	Heparin	15-22	serpin family C member 1	Homo sapiens	122-134
27624738-1	2018	Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition.	Heparin	15-22	serpin family C member 1	Homo sapiens	136-138
2124565-7	1990	Total enterectomy virtually abolished the post-heparin rise in plasma DAO, the mean AUC falling from 55.3 +/- (SEM) 10.2 in controls to 2.1 +/- 1.1 after enterectomy (p less than 0.001).	Heparin	47-54	amine oxidase, copper containing 1	Rattus norvegicus	70-73
27624738-1	2018	Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition.	Heparin	24-27	serpin family C member 1	Homo sapiens	122-134
1694154-2	1990	Since it was shown that the inhibition of coagulation and complement activity attributed to PAPP-A was in fact due to a contamination by heparin occurring during the purification process, we undertook the present study to see whether the reported PAPP-A-induced inhibition of human leukocyte elastase (HLE) could also be attributed to heparin contamination.	Heparin	137-144	pappalysin 1	Homo sapiens	92-98
27624738-1	2018	Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition.	Heparin	24-27	serpin family C member 1	Homo sapiens	136-138
27624738-2	2018	In suspected heparin resistance (HR) during cardiopulmonary bypass, AT activity may be decreased and AT supplementation helps restore UFH responsiveness.	Heparin	13-20	serpin family C member 1	Homo sapiens	68-70
27624738-2	2018	In suspected heparin resistance (HR) during cardiopulmonary bypass, AT activity may be decreased and AT supplementation helps restore UFH responsiveness.	Heparin	13-20	serpin family C member 1	Homo sapiens	101-103
28301908-1	2018	Thrombate III is a human plasma-derived antithrombin III (AT-III) often utilized in patients on extracorporeal membrane oxygenation (ECMO) with suspected AT-III-mediated heparin resistance.	Heparin	170-177	serpin family C member 1	Homo sapiens	40-56
27898513-1	2017	: The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH.	Heparin	45-52	serpin family C member 1	Homo sapiens	128-140
27898513-1	2017	: The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH.	Heparin	54-57	serpin family C member 1	Homo sapiens	128-140
27898513-1	2017	: The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH.	Heparin	84-91	serpin family C member 1	Homo sapiens	128-140
27898513-1	2017	: The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH.	Heparin	235-238	serpin family C member 1	Homo sapiens	128-140
27898513-10	2017	Plasmin generation may be mildly inhibited by heparin-based anticoagulants; however, heparin-catalyzed antithrombin activity is not a major inhibitor of plasmin, as compared to its natural inhibitors alpha2-AP and alpha2-M.	Heparin	85-92	serpin family C member 1	Homo sapiens	103-115
31729495-8	2020	The heparin layer served as a VEGF reservoir with an in vitro VEGF release for at least four weeks.	Heparin	4-11	vascular endothelial growth factor A	Rattus norvegicus	30-34
31729495-8	2020	The heparin layer served as a VEGF reservoir with an in vitro VEGF release for at least four weeks.	Heparin	4-11	vascular endothelial growth factor A	Rattus norvegicus	62-66
31959232-5	2020	One aspect of anticoagulation therapy that is particularly challenging is the use of antithrombin (AT) supplementation for heparin resistance.	Heparin	123-130	serpin family C member 1	Homo sapiens	85-97
32128502-9	2020	Discussion : Patients with AT III deficiency are likely to be heparin-resistant and will require higher heparin doses or the administration of AT III replacement therapy for the treatment of thrombosis, both of which are associated with an increased risk for haemorrhagic complications.	Heparin	62-69	serpin family C member 1	Homo sapiens	27-33
32128502-9	2020	Discussion : Patients with AT III deficiency are likely to be heparin-resistant and will require higher heparin doses or the administration of AT III replacement therapy for the treatment of thrombosis, both of which are associated with an increased risk for haemorrhagic complications.	Heparin	104-111	serpin family C member 1	Homo sapiens	27-33
1694154-2	1990	Since it was shown that the inhibition of coagulation and complement activity attributed to PAPP-A was in fact due to a contamination by heparin occurring during the purification process, we undertook the present study to see whether the reported PAPP-A-induced inhibition of human leukocyte elastase (HLE) could also be attributed to heparin contamination.	Heparin	137-144	pappalysin 1	Homo sapiens	247-253
31861225-2	2019	Various biological activities of heparin/HS are attributed to their specific interaction and regulation with various heparin-binding cytokines, antithrombin (AT), and extracellular matrix (ECM) biomolecules.	Heparin	33-40	serpin family C member 1	Homo sapiens	144-156
28425077-2	2017	We compared the effect of hemodialysis (HD) with enoxaparin as an anticoagulant and without systemic anticoagulation (heparin-grafted membrane-Evodial) on the release of monocyte chemoattractant protein 1 (MCP-1), endostatin (ES) and activin A (Act-A).	Heparin	118-125	C-C motif chemokine ligand 2	Homo sapiens	170-204
1694154-2	1990	Since it was shown that the inhibition of coagulation and complement activity attributed to PAPP-A was in fact due to a contamination by heparin occurring during the purification process, we undertook the present study to see whether the reported PAPP-A-induced inhibition of human leukocyte elastase (HLE) could also be attributed to heparin contamination.	Heparin	335-342	pappalysin 1	Homo sapiens	247-253
31898566-0	2019	[Effect of heparin on histone-mediated the expression of von Willebrand factor and fibrinogen in lung tissue].	Heparin	11-18	Von Willebrand factor	Mus musculus	57-78
1694154-3	1990	PAPP-A was purified from maternal pregnancy EDTA plasma by a method which was previously shown to eliminate contaminating heparin: this preparation was inactive in the HLE assay.	Heparin	122-129	pappalysin 1	Homo sapiens	0-6
31898566-15	2019	Immunohistochemistry showed that high vWF expressions of lung tissue were observed in the histone group while there was almost no positive expression in the control group, and the vWF expression in the histone+heparin group was significantly reduced, indicating that heparin protected mice against histone-induced endothelial cell injury.	Heparin	210-217	Von Willebrand factor	Mus musculus	180-183
31898566-15	2019	Immunohistochemistry showed that high vWF expressions of lung tissue were observed in the histone group while there was almost no positive expression in the control group, and the vWF expression in the histone+heparin group was significantly reduced, indicating that heparin protected mice against histone-induced endothelial cell injury.	Heparin	267-274	Von Willebrand factor	Mus musculus	180-183
1694154-4	1990	But PAPP-A isolated by heparin-Sepharose chromatography, or a PAPP-A-free washing of the heparin-Sepharose column were both inhibitors of HLE.	Heparin	23-30	pappalysin 1	Homo sapiens	4-10
28331220-4	2017	Although these phenotypes overlap considerably with some known SEMDs, they had a novel causal gene, exostosin-like glycosyltransferase 3 (EXTL3), that encodes a glycosyltransferase involved in the synthesis of heparin and heparan sulfate.	Heparin	210-217	exostosin like glycosyltransferase 3	Homo sapiens	100-136
28331220-4	2017	Although these phenotypes overlap considerably with some known SEMDs, they had a novel causal gene, exostosin-like glycosyltransferase 3 (EXTL3), that encodes a glycosyltransferase involved in the synthesis of heparin and heparan sulfate.	Heparin	210-217	exostosin like glycosyltransferase 3	Homo sapiens	138-143
1694154-4	1990	But PAPP-A isolated by heparin-Sepharose chromatography, or a PAPP-A-free washing of the heparin-Sepharose column were both inhibitors of HLE.	Heparin	89-96	elastase, neutrophil expressed	Homo sapiens	138-141
1694154-5	1990	Furthermore the inactive PAPP-A preparation, when incubated with the PAPP-A-free washing of the heparin-Sepharose column, yielded a high molecular weight preparation which inhibited HLE.	Heparin	96-103	pappalysin 1	Homo sapiens	25-31
28671597-6	2017	For all heparins, potentiation of thrombin inhibition by antithrombin and heparin cofactor II was preferentially neutralized over antithrombin-mediated inhibition of factor Xa or plasma clotting time.	Heparin	8-16	serpin family D member 1	Bos taurus	74-93
31636315-4	2019	Copper ions are shown to induce a distinct amyloid-like aggregation pathway of GAPR-1 in the presence of heparin.	Heparin	105-112	GLI pathogenesis related 2	Homo sapiens	79-85
31162225-0	2019	Non-Antithrombin-Mediated Heparin Resistance During Cardiac Surgery: Two Case Reports.	Heparin	26-33	serpin family C member 1	Homo sapiens	4-16
31162225-1	2019	It is well known that antithrombin (AT) deficiency results in decreased heparin sensitivity, also known as "heparin resistance."	Heparin	72-79	serpin family C member 1	Homo sapiens	22-34
31162225-1	2019	It is well known that antithrombin (AT) deficiency results in decreased heparin sensitivity, also known as "heparin resistance."	Heparin	108-115	serpin family C member 1	Homo sapiens	22-34
1694154-5	1990	Furthermore the inactive PAPP-A preparation, when incubated with the PAPP-A-free washing of the heparin-Sepharose column, yielded a high molecular weight preparation which inhibited HLE.	Heparin	96-103	pappalysin 1	Homo sapiens	69-75
1694154-5	1990	Furthermore the inactive PAPP-A preparation, when incubated with the PAPP-A-free washing of the heparin-Sepharose column, yielded a high molecular weight preparation which inhibited HLE.	Heparin	96-103	elastase, neutrophil expressed	Homo sapiens	182-185
31279893-2	2019	The anticoagulant process is mainly mediated by the interaction of heparin with antithrombin followed by inhibition of clotting factors IIa (FIIa) and Xa (FXa).	Heparin	67-74	serpin family C member 1	Homo sapiens	80-92
1694154-6	1990	It is concluded that PAPP-A is not an inhibitor of HLE and that the inhibition of HLE previously attributed to PAPP-A was due to contaminating heparin.	Heparin	143-150	elastase, neutrophil expressed	Homo sapiens	82-85
2200451-3	1990	Recombinant aFGF was mitogenic for BHK21 cells and its activity was stimulated by heparin.	Heparin	82-89	fibroblast growth factor 1	Mesocricetus auratus	12-16
31002379-4	2019	Furthermore, the LPS-neutralizing ability of heparin (5 mug mL-1 )-LL37 (10 mumol L-1 ) complexes, which were found to be less cytotoxic for hDPCs with undiminished antimicrobial ability, was investigated.	Heparin	45-52	L1 cell adhesion molecule	Mus musculus	60-64
31002379-4	2019	Furthermore, the LPS-neutralizing ability of heparin (5 mug mL-1 )-LL37 (10 mumol L-1 ) complexes, which were found to be less cytotoxic for hDPCs with undiminished antimicrobial ability, was investigated.	Heparin	45-52	L1 cell adhesion molecule	Mus musculus	61-64
31002379-8	2019	LL37 (10 mumol L-1 ) binding to heparin within a limited concentration range (2~6 mug mL-1 ) eliminated the cytotoxicity for hDPCs (P &lt; 0.01) whilst exerting potent antimicrobial effects against Streptococcus mutans, Streptococcus sobrinus, Streptococcus salivarius, Aggegatibacter actinomycetemcomitans and Escherichia coli.	Heparin	32-39	L1 cell adhesion molecule	Mus musculus	15-18
31002379-8	2019	LL37 (10 mumol L-1 ) binding to heparin within a limited concentration range (2~6 mug mL-1 ) eliminated the cytotoxicity for hDPCs (P &lt; 0.01) whilst exerting potent antimicrobial effects against Streptococcus mutans, Streptococcus sobrinus, Streptococcus salivarius, Aggegatibacter actinomycetemcomitans and Escherichia coli.	Heparin	32-39	L1 cell adhesion molecule	Mus musculus	86-90
2136880-3	1990	We now demonstrate that C4BP contains heparin-binding fragments, which are located within the C4b binding domain.	Heparin	38-45	complement C4B (Chido blood group)	Homo sapiens	94-97
2136880-8	1990	In addition, heparin blocked the binding of 125I-C4BP to C4b and vice versa.	Heparin	13-20	complement C4B (Chido blood group)	Homo sapiens	57-60
2136880-9	1990	It is therefore likely that the heparin-binding fragments are localized on or close to the C4b-binding site of C4BP.	Heparin	32-39	complement C4B (Chido blood group)	Homo sapiens	91-94
33819813-5	2021	We applied (3-Aminopropyl)triethoxysilane (APTES) as an organosilicate was used for amine-functionalized BCP and (collagen/heparin)5 film was used to delay and sustain BMP-2 release.	Heparin	123-130	bone morphogenetic protein 2	Homo sapiens	168-173
31242089-6	2019	In solution, BMP-1-FN interactions and BMP-1 cleavage of procollagen I were both enhanced by the presence of heparin, suggesting a role for heparin in complex formation during proteolysis.	Heparin	109-116	bone morphogenetic protein 1	Homo sapiens	13-18
31242089-6	2019	In solution, BMP-1-FN interactions and BMP-1 cleavage of procollagen I were both enhanced by the presence of heparin, suggesting a role for heparin in complex formation during proteolysis.	Heparin	109-116	bone morphogenetic protein 1	Homo sapiens	39-44
31242089-6	2019	In solution, BMP-1-FN interactions and BMP-1 cleavage of procollagen I were both enhanced by the presence of heparin, suggesting a role for heparin in complex formation during proteolysis.	Heparin	140-147	bone morphogenetic protein 1	Homo sapiens	13-18
31242089-7	2019	Indeed, addition of heparin enhanced the rate of procollagen cleavage by matrix-bound BMP-1.	Heparin	20-27	bone morphogenetic protein 1	Homo sapiens	86-91
33234593-6	2021	We previously examined the reaction products of human 3OST isoforms and identified five 3-O-sulfated components, including three non-AT-binding disaccharides and two AT-binding tetrasaccharides, as digestion products of heparin lyases.	Heparin	220-227	heparan sulfate-glucosamine 3-sulfotransferase 1	Homo sapiens	54-58
31100600-0	2019	Single conical track-etched nanopore for a free-label detection of OSCS contaminants in heparin.	Heparin	88-95	APC membrane recruitment protein 1	Homo sapiens	67-71
31100600-1	2019	The heparin contamination by oversulfated chondroitin (OSCS) was at the origin of one major sanitary problem of last decade.	Heparin	4-11	APC membrane recruitment protein 1	Homo sapiens	55-59
33034200-0	2020	Studies on Tissue Factor Pathway Inhibitor Antigen Release by Bovine, Ovine and Porcine Heparins Following Intravenous Administration to Non-Human Primates.	Heparin	88-96	tissue factor pathway inhibitor	Bos taurus	11-42
31100600-2	2019	Here we propose a novel strategy to detect OSCS from heparin solution based on conical nanopore functionalized with poly-L-lysine deposition to ensure its re-usability.	Heparin	53-60	APC membrane recruitment protein 1	Homo sapiens	43-47
31100600-5	2019	The sensor is sensitive to the inhibition of heparinase by OSCS until a concentration of 200 pg/ml representing 0.01% in weight in a heparin.	Heparin	45-52	APC membrane recruitment protein 1	Homo sapiens	59-63
33034200-9	2020	These studies demonstrated that IV administration of equigravemetric dosages of PMH and ovine mucosal heparin (OMH) to non-human primates resulted in comparable TFPI antigen release from endothelial cells.	Heparin	102-109	tissue factor pathway inhibitor	Homo sapiens	161-165
25525049-1	2015	Low-molecular-weight heparins (LMWHs) have several positive therapeutic effects and can also form immunostimulatory complexes with plasma proteins, such as platelet factor 4 (PF4).	Heparin	21-29	platelet factor 4	Homo sapiens	175-178
31048599-2	2019	Acquired antithrombin deficiency was suspected due to a refractory response to therapeutic anticoagulation with enoxaparin, unfractionated heparin, and fondaparinux, and a reduced antithrombin antigen level.	Heparin	139-146	serpin family C member 1	Homo sapiens	9-21
25525049-4	2015	Production of tissue factor pathway inhibitor (TFPI), a physiologic heparin-induced inhibitor of tissue factor-induced coagulation that was used as a functional readout of biological activity of enoxaparins in these assays, was heightened in the presence of branded enoxaparin complexes, but its levels were variable in cultures treated with complexes containing US-generic enoxaparins.	Heparin	68-75	tissue factor pathway inhibitor	Homo sapiens	14-45
30714261-6	2019	Maintenance of patient-specific heparin concentrations during bypass is another key goal, since neonates have lower baseline antithrombin concentrations and, therefore, a higher risk for inadequate thrombin inhibition and postoperative bleeding.	Heparin	32-39	serpin family C member 1	Homo sapiens	125-137
30723159-6	2019	Moreover, a low heparin concentration under high-glucose conditions blocked glucose uptake by 1 h into G1 Of note, glucose transporter 4 (glut4) localized on the RMC surface at G0/G1 and was internalized into G1 cells under normal glucose conditions with or without heparin within 30 min.	Heparin	16-23	solute carrier family 2 member 4	Rattus norvegicus	115-136
30723159-6	2019	Moreover, a low heparin concentration under high-glucose conditions blocked glucose uptake by 1 h into G1 Of note, glucose transporter 4 (glut4) localized on the RMC surface at G0/G1 and was internalized into G1 cells under normal glucose conditions with or without heparin within 30 min.	Heparin	16-23	solute carrier family 2 member 4	Rattus norvegicus	138-143
30723159-6	2019	Moreover, a low heparin concentration under high-glucose conditions blocked glucose uptake by 1 h into G1 Of note, glucose transporter 4 (glut4) localized on the RMC surface at G0/G1 and was internalized into G1 cells under normal glucose conditions with or without heparin within 30 min.	Heparin	266-273	solute carrier family 2 member 4	Rattus norvegicus	115-136
30723159-6	2019	Moreover, a low heparin concentration under high-glucose conditions blocked glucose uptake by 1 h into G1 Of note, glucose transporter 4 (glut4) localized on the RMC surface at G0/G1 and was internalized into G1 cells under normal glucose conditions with or without heparin within 30 min.	Heparin	266-273	solute carrier family 2 member 4	Rattus norvegicus	138-143
30723159-7	2019	We also noted that, under high-glucose conditions, glut4 remained on the RMC surface for at least 2 h into G1 and was internalized by 4 h without heparin and within 1 h with heparin.	Heparin	146-153	solute carrier family 2 member 4	Rattus norvegicus	51-56
30723159-7	2019	We also noted that, under high-glucose conditions, glut4 remained on the RMC surface for at least 2 h into G1 and was internalized by 4 h without heparin and within 1 h with heparin.	Heparin	174-181	solute carrier family 2 member 4	Rattus norvegicus	51-56
25525049-4	2015	Production of tissue factor pathway inhibitor (TFPI), a physiologic heparin-induced inhibitor of tissue factor-induced coagulation that was used as a functional readout of biological activity of enoxaparins in these assays, was heightened in the presence of branded enoxaparin complexes, but its levels were variable in cultures treated with complexes containing US-generic enoxaparins.	Heparin	68-75	tissue factor pathway inhibitor	Homo sapiens	47-51
23859593-0	2013	Synthetic ePTFE grafts coated with an anti-CD133 antibody-functionalized heparin/collagen multilayer with rapid in vivo endothelialization properties.	Heparin	73-80	prominin 1	Homo sapiens	43-48
30850549-3	2019	Of note, however, in those studies the LPL had been incubated with heparin, a polyanionic substance that binds and stabilizes LPL.	Heparin	67-74	lipoprotein lipase	Homo sapiens	39-42
30850549-3	2019	Of note, however, in those studies the LPL had been incubated with heparin, a polyanionic substance that binds and stabilizes LPL.	Heparin	67-74	lipoprotein lipase	Homo sapiens	126-129
30850549-7	2019	In the presence of heparin, LPL size increased, overlapping with a 97.2-kDa standard.	Heparin	19-26	lipoprotein lipase	Homo sapiens	28-31
30850549-8	2019	We also used density gradient ultracentrifugation to characterize the LPL within the high-salt and low-salt peaks from a heparin-Sepharose column.	Heparin	121-128	lipoprotein lipase	Homo sapiens	70-73
23859593-8	2013	The success of the anti-CD133 antibody-functionalized heparin/collagen multilayer will provide an effective selection system for the surface modification of synthetic vascular grafts and improve their use in clinical applications.	Heparin	54-61	prominin 1	Homo sapiens	24-29
11372675-0	2001	Plasma levels of total and free tissue factor pathway inhibitor (TFPI) as individual pharmacological parameters of various heparins.	Heparin	123-131	tissue factor pathway inhibitor	Homo sapiens	32-63
30814314-2	2019	(Bioscience Reports, (2019) 39, pii:BSR20182345] described a small but significant conformational change that occurs upon zinc binding and results in initiation of the amyloidogenic aggregation cascade of Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1) in the presence of heparin.	Heparin	287-294	GLI pathogenesis related 2	Homo sapiens	205-258
30814314-2	2019	(Bioscience Reports, (2019) 39, pii:BSR20182345] described a small but significant conformational change that occurs upon zinc binding and results in initiation of the amyloidogenic aggregation cascade of Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1) in the presence of heparin.	Heparin	287-294	GLI pathogenesis related 2	Homo sapiens	260-266
30814314-4	2019	For GAPR-1 in the present study, these steps are provided by zinc binding causing the required conformational change enhancing accessibility of amyloidogenic regions, and heparin providing a template or scaffold in turn increasing the local protein concentration.	Heparin	171-178	GLI pathogenesis related 2	Homo sapiens	4-10
11372675-0	2001	Plasma levels of total and free tissue factor pathway inhibitor (TFPI) as individual pharmacological parameters of various heparins.	Heparin	123-131	tissue factor pathway inhibitor	Homo sapiens	65-69
11372675-1	2001	The release of circulating tissue factor pathway inhibitor (TFPI) into plasma by heparins is thought to contribute to their overall antithrombotic activity.	Heparin	81-89	tissue factor pathway inhibitor	Homo sapiens	27-58
30529119-11	2019	Number of days needed for wound healing was significantly lower in the heparin group than the conventional group (SPTB 14+-1 vs. 20+-4 days; P-value &lt;0.000 and for DPTB, 15+-3 vs. 19+-2 days; P-value &lt;0.003).	Heparin	71-78	spectrin beta, erythrocytic	Homo sapiens	114-118
30529119-12	2019	Mean pain score was also lower in the heparin group (for both SPTB and DPTB 3+-1 vs. 7+-1; P-value &lt;0.000).	Heparin	38-45	spectrin beta, erythrocytic	Homo sapiens	62-66
11372675-1	2001	The release of circulating tissue factor pathway inhibitor (TFPI) into plasma by heparins is thought to contribute to their overall antithrombotic activity.	Heparin	81-89	tissue factor pathway inhibitor	Homo sapiens	60-64
30529119-13	2019	Similarly, total consumption of analgesic medication was significantly less in the heparin group (53+-27 vs. 119+-15mg; P-value &lt;0.000 for SPTB and 46+-6 vs. 126+-12mg; P-value &lt;0.000 for DPTB).	Heparin	83-90	spectrin beta, erythrocytic	Homo sapiens	142-146
11372675-2	2001	In the presented study in healthy volunteers, we measured the heparin-induced increase of circulating total and free TFPI antigen and the aXa- and aIIa activity after subcutaneous (s.c.) injection of 9000 aXa-U of four different heparins: unfractionated heparin (UFH) (13.0 kDa), a medium molecular weight (MW) heparin with a narrow MW range (HF) (10.5 kDa), certoparin (6.0 kDa) and enoxaparin (4.5 kDa).	Heparin	62-69	tissue factor pathway inhibitor	Homo sapiens	117-121
11372675-5	2001	However, the AUC of released free TFPI significantly increased in the order: enoxaparin &lt; UFH &lt; certoparin &lt; HF, showing MW dependency with the exception of UFH.	Heparin	93-96	tissue factor pathway inhibitor	Homo sapiens	34-38
11372675-9	2001	Although the ex vivo aIIa activity of the heparins increased in the same order like the release of free TFPI, there was no clear correlation.	Heparin	42-50	tissue factor pathway inhibitor	Homo sapiens	104-108
30891093-2	2019	Therapeutic low molecular weight heparin is recommended, but it can be difficult to attain sufficient anticoagulation since low molecular weight heparin requires antithrombin to exert its anticoagulant effect.	Heparin	145-152	serpin family C member 1	Homo sapiens	162-174
30891093-3	2019	We carried out a multicentre case-series assessing the dose of low molecular weight heparin required to achieve therapeutic anti-activated factor X levels in pregnant women with antithrombin deficiency.	Heparin	84-91	serpin family C member 1	Homo sapiens	178-190
30672921-8	2019	This can be attributed to the strong interaction of protamine with heparin and the limit of detection was calculated as 0.0406 ng mL-1.	Heparin	67-74	L1 cell adhesion molecule	Mus musculus	130-134
11372675-10	2001	This is attributed to the fact that the aIIa activity of heparin is not only dependent on the MW, but, in contrast to its TFPI releasing effect, also on the percentage of material with high affinity to AT.	Heparin	57-64	tissue factor pathway inhibitor	Homo sapiens	122-126
11372675-11	2001	In conclusion, besides the aXa- and aIIa activity, the TFPI releasing effect of heparins is an additional parameter of their individual pharmacological profile.	Heparin	80-88	tissue factor pathway inhibitor	Homo sapiens	55-59
34694067-0	2022	Delivery of MiR335-5p-Pendant Tetrahedron DNA Nanostructures Using an Injectable Heparin Lithium Hydrogel for Challenging Bone Defects in Steroid-Associated Osteonecrosis.	Heparin	81-88	microRNA 335	Homo sapiens	12-18
30332317-5	2019	Heparin affinity chromatography and mass spectrometry were used to identify Annexin-A2 (ANXA2) as having differential nucleic acid-binding activity.	Heparin	0-7	annexin A2	Rattus norvegicus	76-86
30332317-5	2019	Heparin affinity chromatography and mass spectrometry were used to identify Annexin-A2 (ANXA2) as having differential nucleic acid-binding activity.	Heparin	0-7	annexin A2	Rattus norvegicus	88-93
31167211-13	2019	CONCLUSIONS: These results suggest that LSG independently increases pre-heparin LPL level beyond BW reduction in obese patients.	Heparin	72-79	lipoprotein lipase	Homo sapiens	80-83
34735039-1	2022	BACKGROUND: Heparin management in hemophilia A (HA) patients with a factor VIII (FVIII) inhibitor can be challenging due to severe activated clotting time (ACT) prolongations.	Heparin	12-19	coagulation factor VIII	Homo sapiens	68-79
29953200-4	2018	Here we have used single molecule fluorescence techniques combined with mechanistic modeling to study the heparin-induced aggregation of the repeat region of tau, which forms the core region of neurofibrillary tangles found in Alzheimer"s disease.	Heparin	106-113	microtubule associated protein tau	Homo sapiens	158-161
34735039-1	2022	BACKGROUND: Heparin management in hemophilia A (HA) patients with a factor VIII (FVIII) inhibitor can be challenging due to severe activated clotting time (ACT) prolongations.	Heparin	12-19	coagulation factor VIII	Homo sapiens	81-86
30389911-0	2018	Suppressive effect of syndecan ectodomains and N-desulfated heparins on osteoclastogenesis via direct binding to macrophage-colony stimulating factor.	Heparin	60-68	colony stimulating factor 1	Homo sapiens	113-149
34743814-3	2021	Heparan sulfate (HS)/heparin, a key factor in coagulation process, was found to bind SARS-CoV-2 S protein with high affinity.	Heparin	21-28	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	96-97
34887403-6	2021	We also present the structure of the HHIP C-terminal domain in complex with the GAG heparin.	Heparin	84-91	hedgehog interacting protein	Homo sapiens	37-41
29173042-1	2018	Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate.	Heparin	126-133	serpin family C member 1	Homo sapiens	0-12
29701427-4	2017	Heparin resistance was considered and treated with 1000 UI of antithrombin III concentrate.	Heparin	0-7	serpin family C member 1	Homo sapiens	62-78
29504410-6	2018	Meticulous handling of RA and the use of appropriate hemostatic devices and techniques along with sufficient heparin dose appear important measures to reduce RAO rates.	Heparin	109-116	amine oxidase copper containing 2	Homo sapiens	158-161
34901357-4	2021	The first is competitive inhibition of the SARS-CoV-2 spike glycoprotein (SGP) trimer binding to its human angiotensin converting enzyme 2 (ACE2) receptor by unfractionated heparin (UFH).	Heparin	173-180	angiotensin converting enzyme 2	Homo sapiens	107-138
29717364-3	2018	The heparin effect on EC adhesion molecule (ICAM-1, VCAM-1, E-selectin) expression was also assessed.	Heparin	4-11	selectin E	Homo sapiens	60-70
28322799-2	2017	The anticoagulant activity of target heparin was evaluated by measuring the competitive antithrombin III binding of analyte heparin in the solution phase and USP heparin immobilized on chip surface.	Heparin	37-44	serpin family C member 1	Homo sapiens	88-104
28322799-2	2017	The anticoagulant activity of target heparin was evaluated by measuring the competitive antithrombin III binding of analyte heparin in the solution phase and USP heparin immobilized on chip surface.	Heparin	124-131	serpin family C member 1	Homo sapiens	88-104
28322799-2	2017	The anticoagulant activity of target heparin was evaluated by measuring the competitive antithrombin III binding of analyte heparin in the solution phase and USP heparin immobilized on chip surface.	Heparin	124-131	serpin family C member 1	Homo sapiens	88-104
34901357-4	2021	The first is competitive inhibition of the SARS-CoV-2 spike glycoprotein (SGP) trimer binding to its human angiotensin converting enzyme 2 (ACE2) receptor by unfractionated heparin (UFH).	Heparin	173-180	angiotensin converting enzyme 2	Homo sapiens	140-144
34901357-4	2021	The first is competitive inhibition of the SARS-CoV-2 spike glycoprotein (SGP) trimer binding to its human angiotensin converting enzyme 2 (ACE2) receptor by unfractionated heparin (UFH).	Heparin	182-185	angiotensin converting enzyme 2	Homo sapiens	107-138
34901357-4	2021	The first is competitive inhibition of the SARS-CoV-2 spike glycoprotein (SGP) trimer binding to its human angiotensin converting enzyme 2 (ACE2) receptor by unfractionated heparin (UFH).	Heparin	182-185	angiotensin converting enzyme 2	Homo sapiens	140-144
28402449-1	2017	STUDY QUESTION: Does low molecular weight heparin (LMWH) require heparin-binding epidermal growth factor (EGF)-like growth factor (HBEGF) signaling to induce extravillous trophoblast differentiation and decrease apoptosis during oxidative stress?	Heparin	42-49	heparin binding EGF like growth factor	Homo sapiens	131-136
29993233-7	2018	Mechanistically, PKR is activated in a heparin-dependent manner.	Heparin	39-46	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	17-20
34536674-3	2021	To enhance growth factor (GF) availability in DFUs, heparin (HN)-mimetic alginate sulfate/polycaprolactone (AlgSulf/PCL) double emulsion nanoparticles (NPs) with high affinity and sustained release of CTGF and IGF-I were synthesized.	Heparin	52-59	cellular communication network factor 2	Homo sapiens	201-205
34536674-3	2021	To enhance growth factor (GF) availability in DFUs, heparin (HN)-mimetic alginate sulfate/polycaprolactone (AlgSulf/PCL) double emulsion nanoparticles (NPs) with high affinity and sustained release of CTGF and IGF-I were synthesized.	Heparin	61-63	cellular communication network factor 2	Homo sapiens	201-205
28539925-6	2017	Compared to CXCL9(74-103), CXCL9(74-93) showed equally high affinity for heparin and heparan sulfate (HS), but lower affinity for binding to chondroitin sulfate (CS) and cellular GAGs.	Heparin	73-80	chemokine (C-X-C motif) ligand 9	Mus musculus	27-32
28174207-7	2017	Heparan sulfate proteoglycans and heparin derivatives further enhance HBEGF-induced differentiation by forming a complex with the epidermal growth factor receptor, leading to activation of the ERK1/2 and STAT3 pathways and up-regulation of the inhibitor of DNA binding transcription factor.	Heparin	34-41	heparin binding EGF like growth factor	Homo sapiens	70-75
28445754-8	2017	Antithrombin (2.6 muM) plus heparin (4 U/mL) inhibits 72% of the active clot-bound thrombin after ~10 min at 92 s-1, while no inhibition is observed in the absence of heparin.	Heparin	167-174	serpin family C member 1	Homo sapiens	0-12
30026593-6	2018	VWF-erythrocyte adhesion was attenuated by heparin and the VWF-specific protease ADAMTS13.	Heparin	43-50	Von Willebrand factor	Mus musculus	0-3
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	96-103	signal transducer and activator of transcription 5A	Homo sapiens	38-43
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	96-103	heparin binding EGF like growth factor	Homo sapiens	55-61
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	96-103	heparin binding EGF like growth factor	Homo sapiens	179-185
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	140-147	signal transducer and activator of transcription 5A	Homo sapiens	38-43
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	140-147	heparin binding EGF like growth factor	Homo sapiens	55-61
29274275-7	2018	The phosphorylation of EGFR-Y1045 and Stat5 induced by HB-EGF was prevented by sequestering the heparin-binding domain, suggesting that the heparin-binding domain is critical for HB-EGF-mediated signaling and cellular responses.	Heparin	140-147	heparin binding EGF like growth factor	Homo sapiens	179-185
29274275-8	2018	In conclusion, the heparin-binding domain of HB-EGF was responsible for EGFR-mediated Stat5 activation, resulting in a more potent cellular proliferation, and migration than that mediated by EGF.	Heparin	19-26	heparin binding EGF like growth factor	Homo sapiens	45-51
34370931-2	2021	Tetrameric PF4 has a high affinity for extracellular DNA, which is a key component of neutrophil extracellular traps (NETs); therefore, the interactions between anti-heparin/PF4 antibodies and NETs can contribute to prothrombotic events.	Heparin	166-173	platelet factor 4	Homo sapiens	11-14
29274275-8	2018	In conclusion, the heparin-binding domain of HB-EGF was responsible for EGFR-mediated Stat5 activation, resulting in a more potent cellular proliferation, and migration than that mediated by EGF.	Heparin	19-26	signal transducer and activator of transcription 5A	Homo sapiens	86-91
29274275-8	2018	In conclusion, the heparin-binding domain of HB-EGF was responsible for EGFR-mediated Stat5 activation, resulting in a more potent cellular proliferation, and migration than that mediated by EGF.	Heparin	19-26	epidermal growth factor	Homo sapiens	48-51
28397746-2	2017	In fact, heparins are strong suppressors of hepcidin expression in hepatic cell lines that act by inhibiting the phosphorylation of SMAD1/5/8 proteins elicited by the BMPs.	Heparin	9-17	SMAD family member 1	Mus musculus	132-139
28397746-6	2017	Moreover, the alteration of endogenous heparan sulfates has been found to cause a reduction in hepcidin expression in vitro and in vivo, indicating that heparins act by interfering with the interaction between BMPs and components of the complex involved in the activation of the BMP/SMAD1/5/8 pathway.	Heparin	153-161	SMAD family member 1	Mus musculus	283-290
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	interleukin 1 alpha	Homo sapiens	39-47
34370931-2	2021	Tetrameric PF4 has a high affinity for extracellular DNA, which is a key component of neutrophil extracellular traps (NETs); therefore, the interactions between anti-heparin/PF4 antibodies and NETs can contribute to prothrombotic events.	Heparin	166-173	platelet factor 4	Homo sapiens	174-177
34370931-5	2021	Results: The frequency of anti-heparin/PF4 antibodies was significantly higher in incident HD patients compared to prevalent HD patients (23.6% vs. 7.7%).	Heparin	31-38	platelet factor 4	Homo sapiens	39-42
34370931-6	2021	Serum nucleosome levels, as well as the white blood cell counts, neutrophil counts, and high-sensitivity C-reactive protein levels, were significantly higher in anti-heparin/PF4 antibody-positive patients compared to the control.	Heparin	166-173	platelet factor 4	Homo sapiens	174-177
34370931-7	2021	Platelet counts tended to be lower in the patients with anti-heparin/PF4 of >1.8 than in the controls.	Heparin	61-68	platelet factor 4	Homo sapiens	69-72
29907123-0	2018	Overcoming heparin resistance in pregnant women with antithrombin deficiency: a case report and review of the literature.	Heparin	11-18	serpin family C member 1	Homo sapiens	53-65
28209711-7	2017	Binding of Hic to hTSP-1 is inhibited by heparin and chondroitin sulfate A, indicating binding to the N-terminal globular domain or type I repeats of hTSP-1.	Heparin	41-48	MyoD family inhibitor domain containing	Homo sapiens	11-14
34370931-8	2021	Relative risk calculations showed that the presence of anti-heparin/PF4 antibodies increased the risk of primary functional patency failure by 4.28-fold, and this risk increased further with higher nucleosome levels.	Heparin	60-67	platelet factor 4	Homo sapiens	68-71
34370931-9	2021	Furthermore, in the anti-heparin/PF4 antibody-positive group, the time to first vascular intervention was much shorter, and the risk of repeated intervention was higher, compared to the controls.	Heparin	25-32	platelet factor 4	Homo sapiens	33-36
34370931-10	2021	Conclusion: In incident HD patients, the presence of anti-heparin/PF4 antibodies was associated with increased NET formation; this could be a strong predictor of vascular access complications.	Heparin	58-65	platelet factor 4	Homo sapiens	66-69
34912330-17	2021	Recent studies have assumed a mechanism that is assimilable to heparin-induced thrombocytopenia, with protagonist antibodies against the PF4-polyanion complex.	Heparin	63-70	platelet factor 4	Homo sapiens	137-140
28480430-11	2017	There was significant decrease in concentration of IL-Iotabeta and D-dimer and activity of amylase and lipase in SS and heparin treated group than negative control group.	Heparin	120-127	lipase G, endothelial type	Rattus norvegicus	103-109
29451788-10	2018	Overall agreement of the relative protein quantification between the sample pairs demonstrated that shotgun proteomics using workflows such as the ASAP2 is suitable in analyzing heparin-plasma and that such sample type may be considered in large-scale clinical research studies.	Heparin	178-185	ArfGAP with SH3 domain, ankyrin repeat and PH domain 2	Homo sapiens	147-152
29292168-7	2018	It was found that heparin microparticles bound insulin-like growth factor binding proteins (IGFBP)-3 and 5.	Heparin	18-25	insulin-like growth factor binding protein 3	Mus musculus	47-106
29307667-5	2018	The majority of the LPL in non-heparin plasma was found in RLP as an RLP-LPL complex and released into the circulation after hydrolysis.	Heparin	31-38	lipoprotein lipase	Homo sapiens	20-23
28722442-4	2017	When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles.	Heparin	100-107	serpin family C member 1	Homo sapiens	58-75
28722442-4	2017	When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles.	Heparin	100-107	serpin family C member 1	Homo sapiens	77-83
28722442-4	2017	When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles.	Heparin	100-107	serpin family C member 1	Homo sapiens	129-135
34647745-1	2021	Cellular binding and entry of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are mediated by its spike glycoprotein (S protein), which binds with not only the human angiotensin-converting enzyme 2 (ACE2) receptor but also glycosaminoglycans such as heparin.	Heparin	263-270	angiotensin converting enzyme 2	Homo sapiens	179-210
28036320-1	2017	Acquired antithrombin (AT) deficiency is not uncommon in cardiothoracic surgery because of heparin exposure and dilutional or consumptive losses.	Heparin	91-98	serpin family C member 1	Homo sapiens	9-21
27585400-2	2017	We reported that 2-O, 3-O desulfated heparin (ODSH) inhibits the release of HMGB1 from murine macrophages triggered by neutrophil elastase both in vivo and in vitro.	Heparin	37-44	elastase, neutrophil expressed	Mus musculus	119-138
27418639-0	2017	Lessons From the EThIGII Trial: Proper Putative Benefit Assessment of Low-Molecular-Weight Heparin Treatment in M2/ANXA5 Haplotype Carriers.	Heparin	91-98	annexin A5	Homo sapiens	115-120
29175954-2	2018	Low molecular weight hyaluronan (LMWH) acts at both peptidergic and nonpeptidergic nociceptors to induce mechanical hyperalgesia that is prevented by intrathecal oligodeoxynucleotide antisense to CD44 mRNA, which also prevents hyperalgesia induced by a CD44 receptor agonist, A6.	Heparin	33-37	CD44 molecule (Indian blood group)	Rattus norvegicus	196-200
29175954-2	2018	Low molecular weight hyaluronan (LMWH) acts at both peptidergic and nonpeptidergic nociceptors to induce mechanical hyperalgesia that is prevented by intrathecal oligodeoxynucleotide antisense to CD44 mRNA, which also prevents hyperalgesia induced by a CD44 receptor agonist, A6.	Heparin	33-37	CD44 molecule (Indian blood group)	Rattus norvegicus	253-257
28301908-1	2018	Thrombate III is a human plasma-derived antithrombin III (AT-III) often utilized in patients on extracorporeal membrane oxygenation (ECMO) with suspected AT-III-mediated heparin resistance.	Heparin	170-177	serpin family C member 1	Homo sapiens	58-64
34647745-1	2021	Cellular binding and entry of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are mediated by its spike glycoprotein (S protein), which binds with not only the human angiotensin-converting enzyme 2 (ACE2) receptor but also glycosaminoglycans such as heparin.	Heparin	263-270	angiotensin converting enzyme 2	Homo sapiens	212-216
34657233-0	2022	Unfractionated Heparin Attenuated Histone-Induced Pulmonary Syndecan-1 Degradation in Mice: a Preliminary Study on the Roles of Heparinase Pathway.	Heparin	15-22	syndecan 1	Mus musculus	60-70
29066620-8	2017	Finally, these AutoAbs enhance tumor growth in mice bearing human prostate cancer xenografts, and heparin derivatives specifically abrogate this effect by blocking AutoAb binding to cell-surface GRP78 and decreasing TF expression/activity.	Heparin	98-105	coagulation factor III, tissue factor	Homo sapiens	216-218
29285085-6	2017	The in vivo data indicated that UFH preconditioning attenuated the decline in circulating activated protein C following LPS administration, and also reduced LPS-induced shedding of TM and EPCR.	Heparin	32-35	thrombomodulin	Homo sapiens	181-183
28825541-0	2017	Determination of Bovine Lactoferrin in Food by HPLC with a Heparin Affinity Column for Sample Preparation.	Heparin	59-66	lactotransferrin	Bos taurus	24-35
34657233-11	2022	UFH treatment markedly inhibited pulmonary glycocalyx degradation by reducing the histone-induced decrease in the levels of lung syndecan-1 mRNA and protein.	Heparin	0-3	syndecan 1	Mus musculus	129-139
28804827-3	2017	Acting alone, AT inhibits coagulation factors, but does this very slowly; however, when coupled with heparin as a cofactor, the speed of inhibition is increased many fold.	Heparin	101-108	serpin family C member 1	Homo sapiens	14-16
28804827-4	2017	The AT/Heparin complex is the most powerful naturally occurring anticoagulant in blood.	Heparin	7-14	serpin family C member 1	Homo sapiens	4-6
34261860-1	2021	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	0-7	platelet factor 4	Homo sapiens	140-143
29031112-1	2017	The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin.	Heparin	200-207	serpin family C member 1	Homo sapiens	4-20
29031112-1	2017	The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin.	Heparin	200-207	serpin family C member 1	Homo sapiens	22-27
29031112-2	2017	Undergoing the chemical depolymerization process, the preservation of the ATIII-binding site in low molecular weight heparins (LMWHs) are varied leading to the fluctuation of the anticoagulant activity.	Heparin	117-125	serpin family C member 1	Homo sapiens	74-79
34261860-1	2021	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	68-75	platelet factor 4	Homo sapiens	140-143
34261860-1	2021	Heparin-induced thrombocytopenia (HIT) is an immune complication of heparin therapy caused by antibodies to complexes of platelet factor 4 (PF4) and heparin.	Heparin	149-156	platelet factor 4	Homo sapiens	140-143
27810279-0	2016	Synthesis and characterisation of magnetised Dacron-heparin composite employed for antithrombin affinity purification.	Heparin	52-59	serpin family C member 1	Homo sapiens	83-95
34629931-6	2022	After vaccination, using sera from patients who experienced thrombocytopenia and thrombosis showed increased reactivity in anti-PF4/heparin enzyme immunoassays and substantial platelet-activating antibodies (positive).	Heparin	132-139	platelet factor 4	Homo sapiens	128-131
27533909-12	2016	Additionally, only low dose UFH (75 U/kg) improved GNT at both 24 and 48 hours after TBI.	Heparin	28-31	glucosaminyl (N-acetyl) transferase family member 7	Mus musculus	51-54
29105331-1	2017	In current PCI practice, anticoagulation with either bivalirudin or unfractionated heparin in patients with ACS share comparable efficacy and safety.	Heparin	83-90	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	108-111
28693359-11	2017	Incorporating individual variation, age and antithrombin activity in a model with heparin dose explained less than 50% of the variation in test results.	Heparin	82-89	serpin family C member 1	Homo sapiens	44-56
28880550-12	2017	Finally, fluorescence and ELISA experiments show that UHRA disrupts antithrombin-UFH complexes to neutralize heparin"s activity.	Heparin	109-116	serpin family C member 1	Homo sapiens	68-80
28230633-14	2017	Interleukin-4 increased in heparin Ice group that was in comparison with TNF-alpha reduction.	Heparin	27-34	tumor necrosis factor	Oryctolagus cuniculus	73-82
27862941-4	2016	In 1976, three teams independently found that a specific structure in heparin binds tightly to antithrombin.	Heparin	70-77	serpin family C member 1	Homo sapiens	95-107
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	37-44	serpin family C member 1	Homo sapiens	81-93
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	37-44	serpin family C member 1	Homo sapiens	145-157
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	37-44	serpin family C member 1	Homo sapiens	145-157
34629931-7	2022	In some sera of individuals suffering from heparin-induced thrombocytopenia (HIT), it has been observed that platelet-activating antibodies resulting from vaccination tend to bind to non-complexed PF4 alone.	Heparin	43-50	platelet factor 4	Homo sapiens	197-200
34611669-0	2021	Anti-PF4 VITT antibodies are oligoclonal and variably inhibited by heparin.	Heparin	67-74	platelet factor 4	Homo sapiens	5-8
28261626-0	2016	Influence of heparin molecular size on the induction of C- terminal unfolding in beta2-microglobulin.	Heparin	13-20	beta-2-microglobulin	Homo sapiens	81-100
28261626-10	2016	We also investigated whether heparin could induce beta2m to have an amyloidogenic conformation.	Heparin	29-36	beta-2-microglobulin	Homo sapiens	50-56
29042831-1	2017	OBJECTIVES: To determine the percentage of patients with &gt;10% reduction in heparin infusion rate within 48 hours of antithrombin III (ATIII) administration.	Heparin	78-85	serpin family C member 1	Homo sapiens	119-135
29042831-1	2017	OBJECTIVES: To determine the percentage of patients with &gt;10% reduction in heparin infusion rate within 48 hours of antithrombin III (ATIII) administration.	Heparin	78-85	serpin family C member 1	Homo sapiens	137-142
29042831-6	2017	58.3% of the patients (n = 7) had a &gt;=10% reduction from the baseline heparin infusion rate within 48 hours of ATIII administration.	Heparin	73-80	serpin family C member 1	Homo sapiens	114-119
29042831-9	2017	CONCLUSIONS: Administration of ATIII is associated with &gt;10% decrease in heparin requirements in more than half of the patients identified.	Heparin	76-83	serpin family C member 1	Homo sapiens	31-36
34778697-4	2021	Aim of our retrospective study was to compare the concordance between HIPA and SRA in HIT suspected-patients with positive anti-PF4/heparin antibodies between October 2010 and October 2015.	Heparin	132-139	platelet factor 4	Homo sapiens	128-131
30787791-5	2017	Anticoagulants such as anti-Xa and antithrombin have been found to be effective and safe as compared with the standard of care using low-molecular-weight heparin and warfarin.	Heparin	154-161	serpin family C member 1	Homo sapiens	35-47
27867754-5	2016	Approach: A chimeric fibronectin fragment was produced by inserting the integrin-binding Arg-Gly-Asp (RGD) loop from the tenth type III repeat of fibronectin (FNIII10) into the analogous site within the heparin-binding, bioactive fragment of the first type III repeat (FNIII1H).	Heparin	203-210	fibronectin 1	Mus musculus	21-32
27867754-5	2016	Approach: A chimeric fibronectin fragment was produced by inserting the integrin-binding Arg-Gly-Asp (RGD) loop from the tenth type III repeat of fibronectin (FNIII10) into the analogous site within the heparin-binding, bioactive fragment of the first type III repeat (FNIII1H).	Heparin	203-210	fibronectin 1	Mus musculus	146-157
34477104-0	2021	Heparin-binding motif mutations of human diamine oxidase allow the development of a first-in-class histamine-degrading biopharmaceutical.	Heparin	0-7	amine oxidase copper containing 1	Homo sapiens	41-56
27655335-2	2016	The current monitoring practice for heparin in plasma, such as the chromogenic anti-factor Xa assay, relies on heparin-triggered activation of antithrombin, an inhibitor of coagulation proteases.	Heparin	36-43	serpin family C member 1	Homo sapiens	143-155
27655335-2	2016	The current monitoring practice for heparin in plasma, such as the chromogenic anti-factor Xa assay, relies on heparin-triggered activation of antithrombin, an inhibitor of coagulation proteases.	Heparin	111-118	serpin family C member 1	Homo sapiens	143-155
28667866-1	2017	Using an illustrative case of a patient with antithrombin (AT) deficiency who developed a recurrent venous thromboembolism (VTE) in pregnancy despite therapeutic low-molecular-weight heparin (LMWH), we highlight what is known in the literature and address areas of controversy through a series of questions around the case.	Heparin	183-190	serpin family C member 1	Homo sapiens	45-57
30279820-4	2017	Patients with low antithrombin III activity may have resistance to heparin therapy, leading to insufficient anticoagulation during the acute phase of thromboembolism.	Heparin	67-74	serpin family C member 1	Homo sapiens	18-34
27566697-3	2016	Aims of the present study are (1) to evaluate a possible role of low-molecular-weight-heparins (LMWHs) in the modulation of the expression of TF, TFPI, TFPI2 and VEGF in placentae from thrombophilic women and (2) to study the possible role of endothelium in the placental expression of markers involved in haemostasis and angiogenesis.	Heparin	86-94	coagulation factor III, tissue factor	Homo sapiens	142-144
34184370-8	2021	ROR indicated a lower than average risk for salbutamol, angiotensin receptor antagonists, oral anticoagulants, thrombocytic function inhibitors and heparins.	Heparin	148-156	long intergenic non-protein coding RNA, regulator of reprogramming	Homo sapiens	0-3
27301751-1	2016	Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma.	Heparin	15-22	serpin family C member 1	Homo sapiens	58-70
27301751-1	2016	Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma.	Heparin	24-27	serpin family C member 1	Homo sapiens	58-70
34175640-6	2021	Positive detection of anti-PF4-heparin-antibodies confirmed vaccine-induced immune thrombotic thrombocytopenia diagnosis.	Heparin	31-38	platelet factor 4	Homo sapiens	27-30
27351139-0	2016	ECM-mimetic heparin glycosamioglycan-functionalized surface favors constructing functional vascular smooth muscle tissue in vitro.	Heparin	12-19	multimerin 1	Homo sapiens	0-3
28943821-9	2017	Compared with nonprotocolized intermittent dosing, the use of a continuous infusion ATIII protocol demonstrated increased time within goal ACT range at a lower heparin dose, no increase in hemostatic complications, and trends toward fewer heparin changes and lower blood product usage.	Heparin	160-167	serpin family C member 1	Homo sapiens	84-89
28943821-9	2017	Compared with nonprotocolized intermittent dosing, the use of a continuous infusion ATIII protocol demonstrated increased time within goal ACT range at a lower heparin dose, no increase in hemostatic complications, and trends toward fewer heparin changes and lower blood product usage.	Heparin	239-246	serpin family C member 1	Homo sapiens	84-89
27858202-0	2017	Computational drill down on FGF1-heparin interactions through methodological evaluation.	Heparin	33-40	LOW QUALITY PROTEIN: fibroblast growth factor 1	Mandrillus leucophaeus	28-32
28402449-0	2017	Enhancement of trophoblast differentiation and survival by low molecular weight heparin requires heparin-binding EGF-like growth factor.	Heparin	80-87	heparin binding EGF like growth factor	Homo sapiens	97-135
27479819-0	2016	Identification of a new potential mechanism responsible for severe bleeding in myeloma: immunoglobulins bind the heparin binding domain of antithrombin activating this endogenous anticoagulant.	Heparin	113-120	serpin family C member 1	Homo sapiens	139-151
34433435-2	2021	Fibroblast growth factor-2 (FGF-2), a leading member of the FGF family of heparin-binding growth factors, contributes to normal as well as pathological angiogenesis.	Heparin	74-81	fibroblast growth factor 2	Danio rerio	60-63
27497655-2	2016	The antithrombotic activity of heparin is mediated mainly through its activation of antithrombin (AT) and subsequent inhibition of coagulation factors.	Heparin	31-38	serpin family C member 1	Homo sapiens	84-96
28242144-0	2017	Supplemental Antithrombin Is Effective in Achieving Adequate Anticoagulation in Infants and Children With an Inadequate Response to Heparin.	Heparin	132-139	serpin family C member 1	Homo sapiens	13-25
28242144-1	2017	OBJECTIVE: To demonstrate that supplemental antithrombin (AT) is effective in establishing adequate anticoagulation in infants and children with initially inadequate responses to heparin.	Heparin	179-186	serpin family C member 1	Homo sapiens	44-56
28242144-1	2017	OBJECTIVE: To demonstrate that supplemental antithrombin (AT) is effective in establishing adequate anticoagulation in infants and children with initially inadequate responses to heparin.	Heparin	179-186	serpin family C member 1	Homo sapiens	58-60
34233346-6	2021	Using biolayer interferometry, we demonstrated VITT anti-PF4 antibodies had a stronger binding response against PF4 and PF4/heparin complexes than HIT antibodies; albeit, with similar dissociation rates.	Heparin	124-131	platelet factor 4	Homo sapiens	57-60
28242144-13	2017	CONCLUSION: AT was effective in achieving adequate anticoagulation in a small cohort of infants and children undergoing cardiac surgery who initially were poorly responsive to heparin.	Heparin	176-183	serpin family C member 1	Homo sapiens	12-14
34233346-6	2021	Using biolayer interferometry, we demonstrated VITT anti-PF4 antibodies had a stronger binding response against PF4 and PF4/heparin complexes than HIT antibodies; albeit, with similar dissociation rates.	Heparin	124-131	platelet factor 4	Homo sapiens	120-123
28554992-6	2017	For LPL and HL, the use of heparin and low molecular weight heparin as anticoagulation during hemodialysis (HD) initiate a loss of these enzymes from their binding sites and degradation, causing a temporary dysregulation in triglyceride breakdown.	Heparin	27-34	lipoprotein lipase	Homo sapiens	4-7
28554992-6	2017	For LPL and HL, the use of heparin and low molecular weight heparin as anticoagulation during hemodialysis (HD) initiate a loss of these enzymes from their binding sites and degradation, causing a temporary dysregulation in triglyceride breakdown.	Heparin	60-67	lipoprotein lipase	Homo sapiens	4-7
27364950-6	2016	We found that heparin enhanced cell survival in LPS-treated uterine explants and that this effect was mediated by increasing uterine FAAH activity.	Heparin	14-21	fatty acid amide hydrolase	Mus musculus	133-137
34233346-7	2021	Our data indicates VITT antibodies can mimic the effect of heparin by binding to a similar site on PF4, allowing PF4 tetramers to cluster and form immune complexes, which in turn cause FcgammaRIIa-dependent platelet activation.	Heparin	59-66	platelet factor 4	Homo sapiens	99-102
28486961-6	2017	Heparin reduced the expression of pro-inflammatory markers (TNF-alpha and IL-6) in hAM and deactivated the NF-kss pathway in hATII, diminishing the expression of IRAK1 and MyD88 and their effectors, IL-6, MCP-1 and IL-8.	Heparin	0-7	C-C motif chemokine ligand 2	Homo sapiens	205-210
34233346-7	2021	Our data indicates VITT antibodies can mimic the effect of heparin by binding to a similar site on PF4, allowing PF4 tetramers to cluster and form immune complexes, which in turn cause FcgammaRIIa-dependent platelet activation.	Heparin	59-66	platelet factor 4	Homo sapiens	113-116
34436245-6	2021	The possible binding sites on both S-protein"s RBD and ACE2 were determined based on how they bind to heparin, which has been reported to exhibit significant antiviral activity against SARS CoV-2 through binding to RBD, preventing the virus from affecting ACE2.	Heparin	102-109	angiotensin converting enzyme 2	Homo sapiens	55-59
28207959-5	2017	Heparin-releasable LPL activity was measured in muscle and adipose tissue biopsies.	Heparin	0-7	lipoprotein lipase	Homo sapiens	19-22
28439042-0	2017	Correction: Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif.	Heparin	53-60	gremlin 2, DAN family BMP antagonist	Homo sapiens	47-52
27178931-1	2016	A heparin-based hydrogel sheet composed of thiolated heparin and diacrylated poly (ethylene glycol) was prepared via photo polymerization and human epidermal growth factor (hEGF) were loaded into it for the purpose of wound healing.	Heparin	2-9	epidermal growth factor	Homo sapiens	148-171
27178931-1	2016	A heparin-based hydrogel sheet composed of thiolated heparin and diacrylated poly (ethylene glycol) was prepared via photo polymerization and human epidermal growth factor (hEGF) were loaded into it for the purpose of wound healing.	Heparin	2-9	epidermal growth factor	Homo sapiens	173-177
27178931-6	2016	In conclusion, the delivery of hEGF using the heparin-based hydrogel could accelerate the skin wound healing process.	Heparin	46-53	epidermal growth factor	Homo sapiens	31-35
34436245-6	2021	The possible binding sites on both S-protein"s RBD and ACE2 were determined based on how they bind to heparin, which has been reported to exhibit significant antiviral activity against SARS CoV-2 through binding to RBD, preventing the virus from affecting ACE2.	Heparin	102-109	angiotensin converting enzyme 2	Homo sapiens	256-260
27980562-1	2016	Low molecular weight heparin-modified isoliquiritigenin-loaded solid lipid nanoparticle (LMWH-ISL-SLN) was developed for injective application.	Heparin	21-28	sarcolipin	Homo sapiens	98-101
27980562-12	2016	In conclusion, low molecular weight heparin-modified SLN system is a promising carrier for the intravenous delivery of ISL.	Heparin	36-43	sarcolipin	Homo sapiens	53-56
34436245-7	2021	Moreover, our modeling results illustrate that heparin can also bind to and block ACE2, acting as a competitor and protective agent against SARS CoV-2 infection.	Heparin	47-54	angiotensin converting enzyme 2	Homo sapiens	82-86
34212822-1	2022	Objectives: Syndecan-1 (SDC-1), a transmembrane heparin sulphate proteoglycan predominantly expressed on epithelial cells, also exists in a soluble form through ectodomain shedding.	Heparin	48-55	syndecan 1	Homo sapiens	12-22
27304216-5	2016	In vitro solid phase binding assays using pure proteins revealed that wild-type Fibulin-5 does not bind to Ang-1 or TIE-2 proteins but strongly binds to heparin.	Heparin	153-160	fibulin 5	Homo sapiens	80-89
28007564-2	2017	The mechanism for heparin"s anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa.	Heparin	18-25	serpin family C member 1	Homo sapiens	122-138
28282887-1	2017	Low Molecular Weight Heparins (LMWH) are complex anticoagulant drugs that mainly inhibit the blood coagulation cascade through indirect interaction with antithrombin.	Heparin	21-29	serpin family C member 1	Homo sapiens	153-165
27270881-4	2016	The inhibitory process required the activation of antithrombin by heparin, and the reactive center loop and the heparin binding domain were essential.	Heparin	66-73	serpin family C member 1	Homo sapiens	50-62
27270881-4	2016	The inhibitory process required the activation of antithrombin by heparin, and the reactive center loop and the heparin binding domain were essential.	Heparin	112-119	serpin family C member 1	Homo sapiens	50-62
34212822-1	2022	Objectives: Syndecan-1 (SDC-1), a transmembrane heparin sulphate proteoglycan predominantly expressed on epithelial cells, also exists in a soluble form through ectodomain shedding.	Heparin	48-55	syndecan 1	Homo sapiens	24-29
34286513-1	2021	BACKGROUND: Syndecan-1 (Sdc1) is a heparin sulfate proteoglycan expressed in intestinal epithelium, which plays a crucial role in inflammation and epithelial repair.	Heparin	35-42	syndecan 1	Homo sapiens	24-28
27258428-10	2016	Polysialic acid and heparin reversed the histone-induced TF up-regulation and TM down-regulation.	Heparin	20-27	coagulation factor III, tissue factor	Homo sapiens	57-59
27258428-10	2016	Polysialic acid and heparin reversed the histone-induced TF up-regulation and TM down-regulation.	Heparin	20-27	thrombomodulin	Homo sapiens	78-80
34230926-6	2021	This last mutation affects S protein processing, transforms the unprocessed furin cleavage site into the heparin-binding peptide and makes viruses less capable of syncytia formation.	Heparin	105-112	furin, paired basic amino acid cleaving enzyme	Homo sapiens	76-81
26822178-9	2016	Additionally, SP and heparin/SP grafts showed the existence of CD90(+) and CD105(+) MSCs and induced a large number of M2 macrophages to infiltrate the graft wall compared with that observed with the control group.	Heparin	21-28	Thy-1 cell surface antigen	Homo sapiens	63-67
27068534-0	2016	Heparin interacts with the adhesion GPCR GPR56, reduces receptor shedding, and promotes cell adhesion and motility.	Heparin	0-7	adhesion G protein-coupled receptor G1	Homo sapiens	41-46
34200372-0	2021	ACE2-Independent Interaction of SARS-CoV-2 Spike Protein with Human Epithelial Cells Is Inhibited by Unfractionated Heparin.	Heparin	116-123	angiotensin converting enzyme 2	Homo sapiens	0-4
27068534-4	2016	In this study, we identify heparin as a glycosaminoglycan interacting partner of GPR56.	Heparin	27-34	adhesion G protein-coupled receptor G1	Homo sapiens	81-86
27068534-6	2016	Interestingly, the GPR56-heparin interaction is modulated by collagen III but not TG2, even though both ligands are also heparin-binding proteins.	Heparin	25-32	adhesion G protein-coupled receptor G1	Homo sapiens	19-24
27068534-7	2016	Finally, we show that the interaction with heparin reduces GPR56 receptor shedding, and enhances cell adhesion and motility.	Heparin	43-50	adhesion G protein-coupled receptor G1	Homo sapiens	59-64
34200372-0	2021	ACE2-Independent Interaction of SARS-CoV-2 Spike Protein with Human Epithelial Cells Is Inhibited by Unfractionated Heparin.	Heparin	116-123	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	43-48
34200372-7	2021	As the spike protein has previously been shown to bind heparin, a soluble glycosaminoglycan, we tested the effects of various heparins on ACE2-independent spike protein interaction with cells.	Heparin	55-62	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	7-12
34200372-8	2021	Unfractionated heparin inhibited spike protein interaction with an IC50 value of <0.05 U/mL, whereas two low-molecular-weight heparins were less effective.	Heparin	15-22	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	33-38
34200372-9	2021	A mutant form of the spike protein, lacking the arginine-rich putative furin cleavage site, interacted only weakly with cells and had a lower affinity for unfractionated and low-molecular-weight heparin than the wild-type spike protein.	Heparin	195-202	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	21-26
26884418-7	2016	Heparin is commonly used to treat pregnant women with aPL; however, as thrombotic events do not occur in the placentae of all women with aPL, it may exert a protective effect by preventing the binding of aPL to beta2GPI or by acting through non-thrombotic pathways.	Heparin	0-7	apolipoprotein H	Homo sapiens	211-219
34200372-9	2021	A mutant form of the spike protein, lacking the arginine-rich putative furin cleavage site, interacted only weakly with cells and had a lower affinity for unfractionated and low-molecular-weight heparin than the wild-type spike protein.	Heparin	195-202	furin, paired basic amino acid cleaving enzyme	Homo sapiens	71-76
34200372-10	2021	This suggests that the furin cleavage site might also be a heparin-binding site and potentially important for interactions with host cells.	Heparin	59-66	furin, paired basic amino acid cleaving enzyme	Homo sapiens	23-28
35183674-9	2022	Following the enhancement/inhibition of HSPGs via heparin/siRNA treatment, heparin increased the migratory characteristics of MCF-7 cells while KD of SDC1 increased cell migration in both MCF-7 and MDA-MB-231 cells when compared to scramble negative control conditions.	Heparin	50-57	syndecan 1	Homo sapiens	150-154
27100626-0	2016	Activation of ERK and NF-kappaB during HARE-Mediated Heparin Uptake Require Only One of the Four Endocytic Motifs.	Heparin	53-60	stabilin 2	Homo sapiens	39-43
27100626-1	2016	Fifteen different ligands, including heparin (Hep), are cleared from lymph and blood by the Hyaluronan (HA) Receptor for Endocytosis (HARE; derived from Stabilin-2 by proteolysis), which contains four endocytic motifs (M1-M4).	Heparin	37-44	stabilin 2	Homo sapiens	134-138
27100626-1	2016	Fifteen different ligands, including heparin (Hep), are cleared from lymph and blood by the Hyaluronan (HA) Receptor for Endocytosis (HARE; derived from Stabilin-2 by proteolysis), which contains four endocytic motifs (M1-M4).	Heparin	37-44	stabilin 2	Homo sapiens	153-163
27100626-12	2016	NF-kappaB activation by HARE-mediated uptake of Hep, HA, dermatan sulfate or acetylated LDL was unaffected in single-motif deletion mutants lacking M1, M2 or M4.	Heparin	48-51	stabilin 2	Homo sapiens	24-28
35339716-9	2022	The antiplatelet factor 4 (anti-PF4) antibody positivity rate was 91% (95% CI 88-94, I2=0%) and the overall mortality was 32% (95% CI 24-41, I2=69%), and no significant difference was observed between heparin- and non-heparin-based anticoagulation treatments (risk ratio 0.84, 95% CI 0.47-1.50, I2=0%).	Heparin	201-208	platelet factor 4	Homo sapiens	32-35
26998583-7	2016	OBJECTIVES: To assess whether the prophylactic administration of antithrombin (started within the first 24 hours after birth) reduces the incidence of germinal matrix-intraventricular hemorrhage in very preterm neonates when compared to placebo, no treatment, or heparin.	Heparin	263-270	serpin family C member 1	Homo sapiens	65-77
35339716-9	2022	The antiplatelet factor 4 (anti-PF4) antibody positivity rate was 91% (95% CI 88-94, I2=0%) and the overall mortality was 32% (95% CI 24-41, I2=69%), and no significant difference was observed between heparin- and non-heparin-based anticoagulation treatments (risk ratio 0.84, 95% CI 0.47-1.50, I2=0%).	Heparin	218-225	platelet factor 4	Homo sapiens	32-35
35609563-9	2022	These findings suggest EIA assays that can directly detect antibodies to PF4 or PF4/heparin have excellent performance characteristics and may be useful as a diagnostic test if the PF4-SRA is unavailable.	Heparin	84-91	platelet factor 4	Homo sapiens	80-83
26661689-0	2016	Extracellular matrix fibronectin initiates endothelium-dependent arteriolar dilatation via the heparin-binding, matricryptic RWRPK sequence of the first type III repeat of fibrillar fibronectin.	Heparin	95-102	fibronectin 1	Mus musculus	21-32
26661689-0	2016	Extracellular matrix fibronectin initiates endothelium-dependent arteriolar dilatation via the heparin-binding, matricryptic RWRPK sequence of the first type III repeat of fibrillar fibronectin.	Heparin	95-102	fibronectin 1	Mus musculus	182-193
26661689-3	2016	This vasodilatory signal requires the heparin-binding matricryptic RWRPK sequence in the first type III repeat of fibrillar fibronectin.	Heparin	38-45	fibronectin 1	Mus musculus	124-135
26661689-6	2016	Here we test the hypotheses that (i) the matricryptic heparin-binding region of the first type III repeat of fibrillar FN (FNIII1H) mediates vasodilatation, and (ii) this response is EC dependent.	Heparin	54-61	fibronectin 1	Mus musculus	119-121
26661689-6	2016	Here we test the hypotheses that (i) the matricryptic heparin-binding region of the first type III repeat of fibrillar FN (FNIII1H) mediates vasodilatation, and (ii) this response is EC dependent.	Heparin	54-61	fibronectin 1	Mus musculus	123-130
26661689-8	2016	Both FNIII1H,8-10 and FNIII1H induced dilatations (12.2 +- 1.7 mum, n = 12 and 17.2 +- 2.4 mum, n = 14, respectively) whereas mutation of the active sequence (R(613) WRPK) of the heparin binding region significantly diminished the dilatation (3.2 +- 1.8 mum, n = 10).	Heparin	179-186	fibronectin 1	Mus musculus	22-29
26955355-0	2015	High Sulfation and a High Molecular Weight Are Important for Anti-hepcidin Activity of Heparin.	Heparin	87-94	hepcidin antimicrobial peptide	Homo sapiens	66-74
26955355-1	2015	Heparins are efficient inhibitors of hepcidin expression even in vivo, where they induce an increase of systemic iron availability.	Heparin	0-8	hepcidin antimicrobial peptide	Homo sapiens	37-45
26955355-2	2015	Heparins seem to act by interfering with BMP6 signaling pathways that control the expression of liver hepcidin, causing the suppression of SMAD1/5/8 phosphorylation.	Heparin	0-8	hepcidin antimicrobial peptide	Homo sapiens	102-110
26955355-8	2015	The high sulfation and high molecular weight properties for efficient anti-hepcidin activity suggest that heparin is involved in multiple binding sites.	Heparin	106-113	hepcidin antimicrobial peptide	Homo sapiens	75-83
26431853-2	2016	The primary aim of this study was to evaluate the relationship between preoperative antithrombin (AT) activity and heparin responsiveness in neonates and infants undergoing congenital cardiac surgery.	Heparin	115-122	serpin family C member 1	Homo sapiens	84-96
35334413-3	2022	In this study, we modified the amino acid sequence of PEDF to increase its affinity for heparin and hyaluronic acid (HA), which are negatively charged extracellular matrix (ECM) molecules.	Heparin	88-95	serpin family F member 1	Homo sapiens	54-58
26431853-2	2016	The primary aim of this study was to evaluate the relationship between preoperative antithrombin (AT) activity and heparin responsiveness in neonates and infants undergoing congenital cardiac surgery.	Heparin	115-122	serpin family C member 1	Homo sapiens	98-100
26672027-2	2016	The anticoagulant activity of heparin is mainly attributable to the action of a specific pentasaccharide sequence that acts in concert with antithrombin, a plasma coagulation factor inhibitor.	Heparin	30-37	serpin family C member 1	Homo sapiens	140-152
35334413-6	2022	Using in vitro binding assays, we demonstrate that ePEDF had higher affinity for heparin and HA than wild-type PEDF (wtPEDF).	Heparin	81-88	serpin family F member 1	Homo sapiens	111-115
35551912-0	2022	Heparin activation of protein Z-dependent protease inhibitor (ZPI) allosterically blocks protein Z activation through an extended heparin binding site.	Heparin	0-7	serpin family A member 10	Homo sapiens	62-65
26374846-8	2015	Recombinant Tau-CTF24 accelerated heparin-induced aggregation and lost the ability to promote microtubule assembly.	Heparin	34-41	microtubule associated protein tau	Homo sapiens	12-15
35551912-0	2022	Heparin activation of protein Z-dependent protease inhibitor (ZPI) allosterically blocks protein Z activation through an extended heparin binding site.	Heparin	130-137	serpin family A member 10	Homo sapiens	62-65
35551912-2	2022	ZPI is also activated by heparin to inhibit free FXa at a physiologically significant rate.	Heparin	25-32	serpin family A member 10	Homo sapiens	0-3
35551912-3	2022	Here we show that heparin binding to ZPI antagonizes PZ binding to and activation of ZPI.	Heparin	18-25	serpin family A member 10	Homo sapiens	37-40
26156753-11	2015	This is the first study to demonstrate that kallistatin"s heparin-binding site is crucial for preventing TGF-beta-induced miR-21 and oxidative stress, while its active site is key for stimulating the expression of antioxidant genes via interaction with an endothelial surface tyrosine kinase.	Heparin	58-65	microRNA 21	Homo sapiens	122-128
35551912-3	2022	Here we show that heparin binding to ZPI antagonizes PZ binding to and activation of ZPI.	Heparin	18-25	serpin family A member 10	Homo sapiens	85-88
35551912-4	2022	Virtual docking of heparin to ZPI showed that a heparin binding site near helix H close to the PZ binding site as well as a previously mapped site in helix C were both favored.	Heparin	19-26	serpin family A member 10	Homo sapiens	30-33
35551912-4	2022	Virtual docking of heparin to ZPI showed that a heparin binding site near helix H close to the PZ binding site as well as a previously mapped site in helix C were both favored.	Heparin	48-55	serpin family A member 10	Homo sapiens	30-33
35551912-6	2022	The binding of heparin chains 72 to 5-saccharides in length to ZPI were similarly effective in antagonizing PZ binding and in inducing Trp fluorescence changes in ZPI.	Heparin	15-22	serpin family A member 10	Homo sapiens	63-66
25483839-1	2015	While antithrombin (AT) has small basal inhibitory activity, it reaches its full inhibitory potential against activated blood coagulation factors, FXa, FIXa, and FIIa (thrombin), via an allosteric and/or template (bridging) mechanism by the action of heparin, heparan sulfate, or heparin-mimetic pentasaccharides (PS).	Heparin	251-258	serpin family C member 1	Homo sapiens	6-18
35551912-6	2022	The binding of heparin chains 72 to 5-saccharides in length to ZPI were similarly effective in antagonizing PZ binding and in inducing Trp fluorescence changes in ZPI.	Heparin	15-22	serpin family A member 10	Homo sapiens	163-166
25998703-0	2015	Heparin inhibits lipopolysaccharide-induced inflammation via inducing caveolin-1 and activating the p38/mitogen-activated protein kinase pathway in murine peritoneal macrophages.	Heparin	0-7	caveolin 1, caveolae protein	Mus musculus	70-80
35551912-8	2022	Together, these findings suggest that heparin binding to a site on ZPI extending from helix C to helix H promotes ZPI inhibition of FXa and allosterically antagonizes PZ binding to ZPI through long-range conformational changes.	Heparin	38-45	serpin family A member 10	Homo sapiens	67-70
35551912-8	2022	Together, these findings suggest that heparin binding to a site on ZPI extending from helix C to helix H promotes ZPI inhibition of FXa and allosterically antagonizes PZ binding to ZPI through long-range conformational changes.	Heparin	38-45	serpin family A member 10	Homo sapiens	114-117
35551912-8	2022	Together, these findings suggest that heparin binding to a site on ZPI extending from helix C to helix H promotes ZPI inhibition of FXa and allosterically antagonizes PZ binding to ZPI through long-range conformational changes.	Heparin	38-45	serpin family A member 10	Homo sapiens	181-184
35551912-9	2022	Heparin antagonism of PZ binding to ZPI may serve to spare limiting PZ and allow PZ and heparin cofactors to target FXa at different sites of action.	Heparin	0-7	serpin family A member 10	Homo sapiens	36-39
26188924-8	2015	A direct FXa inhibitor, edoxaban, and an antithrombin-dependent anticoagulant, unfractionated heparin (UFH), did not increase, but simply decreased TG under each condition in a concentration dependent manner.	Heparin	103-106	serpin family C member 1	Homo sapiens	41-53
25811451-8	2015	However, activation of FV with rhFIIa was approximately 25% more effective than with pdhFIIa and heparin-enhanced inhibition of rhFIIa by antithrombin was significantly more efficient compared with pdhFIIa with 10% higher inhibition both at steady state and at initial rate conditions.	Heparin	97-104	serpin family C member 1	Homo sapiens	138-150
35551912-9	2022	Heparin antagonism of PZ binding to ZPI may serve to spare limiting PZ and allow PZ and heparin cofactors to target FXa at different sites of action.	Heparin	88-95	serpin family A member 10	Homo sapiens	36-39
35438981-4	2022	To this end, we produced heparin-doped polypyrrole (PPy/Hep) electrodes of different surface roughness, with Ra values from 5.5 to 17.6 nm, by varying the charge densities during electrochemical synthesis.	Heparin	25-32	pancreatic polypeptide	Homo sapiens	52-55
25913486-5	2015	The effect of heparin-binding epidermal growth factor-like growth factor (HB-EGF) on macrophage polarization was determined by flow cytometry with M1/M2 markers and real time polymerase chain reaction.	Heparin	14-21	heparin binding EGF like growth factor	Homo sapiens	74-80
25851619-9	2015	Dual mutations in the heparin exosite or combined mutations in both exosites synergistically reduced the inhibition rate for antithrombin-heparin.	Heparin	22-29	serpin family C member 1	Homo sapiens	125-137
35038779-1	2022	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a prothrombotic, immune-mediated adverse drug reaction associated with high rates of thrombosis-related morbidity and mortality caused by FcgammaRIIa-activating pathogenic antibodies to PF4-heparin.	Heparin	12-19	platelet factor 4	Homo sapiens	240-243
35038779-1	2022	BACKGROUND: Heparin-induced thrombocytopenia (HIT) is a prothrombotic, immune-mediated adverse drug reaction associated with high rates of thrombosis-related morbidity and mortality caused by FcgammaRIIa-activating pathogenic antibodies to PF4-heparin.	Heparin	244-251	platelet factor 4	Homo sapiens	240-243
25765603-6	2015	The ability of heparin-based NCs to bind to antithrombin (AT III) was investigated using isothermal titration calorimetry and dynamic light scattering experiments.	Heparin	15-22	serpin family C member 1	Homo sapiens	44-64
35419157-1	2022	Heparin-induced thrombocytopenia (HIT) is a prothrombotic state caused by autoantibodies against platelet factor 4 (PF4)-heparin complexes.	Heparin	121-128	platelet factor 4	Homo sapiens	116-119
35244123-4	2022	Based on the long-term stability and modifiable properties of TLA coatings, heparin was introduced by an amide reaction to provide anticoagulant activity (TLH).	Heparin	76-83	procollagen-lysine,2-oxoglutarate 5-dioxygenase 2	Homo sapiens	155-158
25817684-4	2015	Liquid chromatography-mass spectrometry and nuclear magnetic resonance spectroscopy analysis confirms an abundance of heparin"s characteristic trisulfated disaccharide, as well as 3-O-sulfo containing residues critical for heparin binding to antithrombin III and its anticoagulant activity.	Heparin	118-125	serpin family C member 1	Homo sapiens	242-258
25817684-4	2015	Liquid chromatography-mass spectrometry and nuclear magnetic resonance spectroscopy analysis confirms an abundance of heparin"s characteristic trisulfated disaccharide, as well as 3-O-sulfo containing residues critical for heparin binding to antithrombin III and its anticoagulant activity.	Heparin	223-230	serpin family C member 1	Homo sapiens	242-258
35253140-9	2022	At baseline, 3.2% of the ChAdOx1 cohort and 1.6% BNT162b2 cohort were positive for PF4/heparin antibodies with a stable titre through T1 and T2.	Heparin	87-94	platelet factor 4	Homo sapiens	83-86
25945799-2	2015	In this paper, we report on the fabrication of albumin/heparin (Alb/Hep) assemblies for controlled binding of basic fibroblast growth factor (FGF-2).	Heparin	55-62	albumin	Bos taurus	64-67
34980833-11	2022	On admission, 64 patients tested positive for PF4-Heparin ELISA assay (80%).	Heparin	50-57	platelet factor 4	Homo sapiens	46-49
25938566-13	2015	Preventing fibrin network formation with heparin suppressed the prosurvival effect of Reg3alpha.	Heparin	41-48	regenerating islet-derived 3 alpha	Mus musculus	86-95
35215487-8	2022	In response to HEC with Intralipid/heparin infusion, OPG decreased (p < 0.001) and BNP increased (p < 0.001).	Heparin	35-42	TNF receptor superfamily member 11b	Homo sapiens	53-56
25633564-4	2015	Dorsomorphin, heparin, and cobalt chloride, known inhibitors of hepcidin expression, significantly suppressed green fluorescence intensity, and these inhibitory effects were more prominent when the cells were stimulated with BMP-6.	Heparin	14-21	hepcidin antimicrobial peptide	Homo sapiens	64-72
35215487-8	2022	In response to HEC with Intralipid/heparin infusion, OPG decreased (p < 0.001) and BNP increased (p < 0.001).	Heparin	35-42	natriuretic peptide B	Homo sapiens	83-86
35202331-7	2022	In addition, monocytes from heparin blood showed higher expression levels of the cell surface markers CD14, CD163, and MHCII when compared to cells from EDTA blood.	Heparin	28-35	scavenger receptor cysteine-rich type 1 protein M130	Camelus dromedarius	108-113
26073395-9	2015	The high- and low-dose effects differed significantly for heparin-precipitated apoC-III, LpB, LpA-I, and apoB/apoA-I ratio (P &lt; .05).	Heparin	58-65	apolipoprotein C3	Homo sapiens	79-87
26131136-3	2015	They were intervened by heparin and the expression levels of soluble thrombomodulin (sTM) and serum activated protein C (APC) were detected by ELISA, the regulatory mechanism of heparin improving vascular endothelial cells injury induced by TNFalpha was detected by Western Blotting method, the methylation of histone in the gene promoter region of endothelial nitric oxide synthase (eNOS) and monocyte chemotactic protein-1 (MCP-1) were detected using chromatin immunoprecipitation method.	Heparin	178-185	thrombomodulin	Homo sapiens	69-83
26131136-3	2015	They were intervened by heparin and the expression levels of soluble thrombomodulin (sTM) and serum activated protein C (APC) were detected by ELISA, the regulatory mechanism of heparin improving vascular endothelial cells injury induced by TNFalpha was detected by Western Blotting method, the methylation of histone in the gene promoter region of endothelial nitric oxide synthase (eNOS) and monocyte chemotactic protein-1 (MCP-1) were detected using chromatin immunoprecipitation method.	Heparin	178-185	C-C motif chemokine ligand 2	Homo sapiens	394-424
26131136-3	2015	They were intervened by heparin and the expression levels of soluble thrombomodulin (sTM) and serum activated protein C (APC) were detected by ELISA, the regulatory mechanism of heparin improving vascular endothelial cells injury induced by TNFalpha was detected by Western Blotting method, the methylation of histone in the gene promoter region of endothelial nitric oxide synthase (eNOS) and monocyte chemotactic protein-1 (MCP-1) were detected using chromatin immunoprecipitation method.	Heparin	178-185	C-C motif chemokine ligand 2	Homo sapiens	426-431
26131136-4	2015	Results Heparin could inhibit the secretion of sTM and APC protein and the expression of MCP-1 gene which involved in NF-kappaB signal pathway.	Heparin	8-15	C-C motif chemokine ligand 2	Homo sapiens	89-94
35169535-1	2022	The heparin polysaccharide nanoparticles block the interaction between heparan sulfate/S protein and inhibit the infection of both wild-type SARS-CoV-2 pseudovirus and the mutated strains through pulmonary delivery.Image 1.	Heparin	4-11	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	87-88
25367817-3	2015	Heparin has been shown to inhibit P-selectin and as a consequence it blunts metastasis and inflammation.	Heparin	0-7	selectin P	Homo sapiens	34-44
25367817-4	2015	Some heparin analogs obtained from marine invertebrates are P-selectin inhibitors and do not induce bleeding effects.	Heparin	5-12	selectin P	Homo sapiens	60-70
25367817-10	2015	These data suggest that the mollusk HS is a potential alternative to heparin for inhibiting P-selectin-mediated events such as metastasis and inflammatory cell recruitment.	Heparin	69-76	selectin P	Homo sapiens	92-102
25811371-9	2015	AT purified from patient"s plasma on hi-trap heparin column showed a marked decrease in heparin affinity and thrombin inhibition rates.	Heparin	45-52	serpin family C member 1	Homo sapiens	0-2
25811371-9	2015	AT purified from patient"s plasma on hi-trap heparin column showed a marked decrease in heparin affinity and thrombin inhibition rates.	Heparin	88-95	serpin family C member 1	Homo sapiens	0-2
27805412-3	2017	We used R213G mice expressing a naturally occurring single-nucleotide polymorphism, rs1799895, within the heparin-binding domain of SOD3, which results in an amino acid substitution at position 213 to test the hypothesis that the redistribution of SOD3 into the extracellular fluids would impart protection against bleomycin-induced lung fibrosis and secondary pulmonary hypertension (PH).	Heparin	106-113	superoxide dismutase 3, extracellular	Mus musculus	132-136
27527263-5	2017	RESULTS: Stimulation with anti-IgE or IL-3 resulted in strong upregulation of basophil CD203c in samples collected in EDTA or heparin, stored at 4 C, and analyzed 24 hours after sample collection.	Heparin	126-133	interleukin 3	Homo sapiens	38-42
28722442-4	2017	When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles.	Heparin	170-177	serpin family C member 1	Homo sapiens	58-75
28722442-4	2017	When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles.	Heparin	170-177	serpin family C member 1	Homo sapiens	77-83
28722442-4	2017	When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles.	Heparin	170-177	serpin family C member 1	Homo sapiens	129-135
27759896-12	2017	Anti-PRT/heparin antibodies induced P-selectin expression in the presence of NPH-insulin in a heparin-dependent way (median mean fluorescence intensity in the presence of NPH-insulin: 55, 95% confidence interval [CI] 18.7-100.5 vs. NPH-insulin and heparin: 204, 95% CI 106.5-372.8).	Heparin	9-16	selectin P	Homo sapiens	36-46
27759896-12	2017	Anti-PRT/heparin antibodies induced P-selectin expression in the presence of NPH-insulin in a heparin-dependent way (median mean fluorescence intensity in the presence of NPH-insulin: 55, 95% confidence interval [CI] 18.7-100.5 vs. NPH-insulin and heparin: 204, 95% CI 106.5-372.8).	Heparin	94-101	selectin P	Homo sapiens	36-46
25581634-11	2015	For those who received antithrombin concentrate, heparin infusion rates decreased by an average of 10.2 U/kg/hr for at least 12 hours following administration.	Heparin	49-56	serpin family C member 1	Homo sapiens	23-35
25581634-14	2015	Patients who received antithrombin concentrate also had decreased heparin requirements for at least 12 hours after dosing.	Heparin	66-73	serpin family C member 1	Homo sapiens	22-34
35068341-0	2022	Specificity protein 1-induced serine peptidase inhibitor, Kunitz Type 1 antisense RNA1 regulates colorectal cancer cell proliferation, migration, invasion and apoptosis through targeting heparin binding growth factor via sponging microRNA-214.	Heparin	187-194	serine peptidase inhibitor, Kunitz type 1	Homo sapiens	30-71
25239670-2	2015	METHODS: Healthy volunteers were injected with heparin for LPL and HTGL determination in the fasting (8:00) and postprandial (20:00) plasma on the same day.	Heparin	47-54	lipoprotein lipase	Homo sapiens	59-62
25239670-4	2015	RESULTS: LPL activity and concentration in the post-heparin plasma exhibited a significant inverse correlation with TG, RLP-C, RLP-TG, and RLP particle size estimated as RLP-TG/RLP-C ratio and sdLDL-C, and positively correlated with HDL-C. HTGL was only inversely correlated with HDL-C. LPL concentration in the pre-heparin plasma was also inversely correlated with the RLP-TG/RLP-C ratio and other lipoprotein parameters.	Heparin	52-59	lipoprotein lipase	Homo sapiens	9-12
28170190-6	2017	Delivery of IFN-gamma via heparin-microparticles within MSC aggregates induced sustained IDO expression during 1 week of culture, whereas IDO expression by IFN-gamma-pretreated MSC spheroids rapidly decreased during 2 days.	Heparin	26-33	indoleamine 2,3-dioxygenase 1	Homo sapiens	89-92
35126147-3	2021	Such knowledge gaps include the identity of a HIT immunogen, the intrinsic roles of various cell types and their interactions, and the molecular basis that distinguishes pathogenic and non-pathogenic PF4/heparin antibodies.	Heparin	204-211	platelet factor 4	Homo sapiens	200-203
27782377-7	2016	On the other hand, the observation that the enhancer activity of KKN1 is superstimulated in the presence of heparin is explained by the fact KKN1, latent myostatin, and BMP1 have affinity for heparin and these interactions with heparin increase the local concentrations of the reactants thereby facilitating the action of BMP1.	Heparin	108-115	bone morphogenetic protein 1	Homo sapiens	169-173
27782377-7	2016	On the other hand, the observation that the enhancer activity of KKN1 is superstimulated in the presence of heparin is explained by the fact KKN1, latent myostatin, and BMP1 have affinity for heparin and these interactions with heparin increase the local concentrations of the reactants thereby facilitating the action of BMP1.	Heparin	108-115	bone morphogenetic protein 1	Homo sapiens	322-326
25239670-4	2015	RESULTS: LPL activity and concentration in the post-heparin plasma exhibited a significant inverse correlation with TG, RLP-C, RLP-TG, and RLP particle size estimated as RLP-TG/RLP-C ratio and sdLDL-C, and positively correlated with HDL-C. HTGL was only inversely correlated with HDL-C. LPL concentration in the pre-heparin plasma was also inversely correlated with the RLP-TG/RLP-C ratio and other lipoprotein parameters.	Heparin	52-59	lipoprotein lipase	Homo sapiens	287-290
25239670-7	2015	Those results suggest that LPL concentration in pre-heparin plasma can take the place of LPL activity in the post-heparin plasma.	Heparin	52-59	lipoprotein lipase	Homo sapiens	27-30
27782377-7	2016	On the other hand, the observation that the enhancer activity of KKN1 is superstimulated in the presence of heparin is explained by the fact KKN1, latent myostatin, and BMP1 have affinity for heparin and these interactions with heparin increase the local concentrations of the reactants thereby facilitating the action of BMP1.	Heparin	192-199	bone morphogenetic protein 1	Homo sapiens	169-173
2482548-11	1989	Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups.	Heparin	40-47	serpin family C member 1	Homo sapiens	101-106
27782377-7	2016	On the other hand, the observation that the enhancer activity of KKN1 is superstimulated in the presence of heparin is explained by the fact KKN1, latent myostatin, and BMP1 have affinity for heparin and these interactions with heparin increase the local concentrations of the reactants thereby facilitating the action of BMP1.	Heparin	192-199	bone morphogenetic protein 1	Homo sapiens	322-326
27782377-7	2016	On the other hand, the observation that the enhancer activity of KKN1 is superstimulated in the presence of heparin is explained by the fact KKN1, latent myostatin, and BMP1 have affinity for heparin and these interactions with heparin increase the local concentrations of the reactants thereby facilitating the action of BMP1.	Heparin	192-199	bone morphogenetic protein 1	Homo sapiens	169-173
27782377-7	2016	On the other hand, the observation that the enhancer activity of KKN1 is superstimulated in the presence of heparin is explained by the fact KKN1, latent myostatin, and BMP1 have affinity for heparin and these interactions with heparin increase the local concentrations of the reactants thereby facilitating the action of BMP1.	Heparin	192-199	bone morphogenetic protein 1	Homo sapiens	322-326
27405066-9	2016	Finally, TF activity was increased on monocytes exposed to plasma from septic patients, an effect that was attenuated in plasma from patients receiving unfractionated heparin (UFH).	Heparin	167-174	coagulation factor III, tissue factor	Homo sapiens	9-11
27405066-9	2016	Finally, TF activity was increased on monocytes exposed to plasma from septic patients, an effect that was attenuated in plasma from patients receiving unfractionated heparin (UFH).	Heparin	176-179	coagulation factor III, tissue factor	Homo sapiens	9-11
27429124-9	2016	Fibroblast growth factor-1 (FGF-1) in combination with heparin decreased the expression of alpha-SMA and increased the expression of EDA-FN in the cells on plastic.	Heparin	55-62	actin gamma 2, smooth muscle	Rattus norvegicus	91-100
27601475-6	2016	S-guanylated tau inhibited heparin-induced tau aggregation in a thioflavin T assay.	Heparin	27-34	microtubule associated protein tau	Homo sapiens	13-16
27601475-6	2016	S-guanylated tau inhibited heparin-induced tau aggregation in a thioflavin T assay.	Heparin	27-34	microtubule associated protein tau	Homo sapiens	43-46
27534383-2	2016	Two fluorophore-functionalized cationic oligopeptides HS 1 and HS 2 were developed to monitor heparin ratiometrically in aqueous media.	Heparin	94-101	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	54-58
27534383-2	2016	Two fluorophore-functionalized cationic oligopeptides HS 1 and HS 2 were developed to monitor heparin ratiometrically in aqueous media.	Heparin	94-101	spectrin beta, erythrocytic	Homo sapiens	63-67
27534383-3	2016	Upon binding to heparin, HS 1 and HS 2 undergo a conformational change from an open form to a folded form, which leads to a distinct change in the fluorescence properties.	Heparin	16-23	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	25-29
27534383-3	2016	Upon binding to heparin, HS 1 and HS 2 undergo a conformational change from an open form to a folded form, which leads to a distinct change in the fluorescence properties.	Heparin	16-23	spectrin beta, erythrocytic	Homo sapiens	34-38
27534383-7	2016	HS 1 and HS 2 could also detect heparin ratiometrically in diluted bovine serum.	Heparin	32-39	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	0-4
27534383-7	2016	HS 1 and HS 2 could also detect heparin ratiometrically in diluted bovine serum.	Heparin	32-39	spectrin beta, erythrocytic	Homo sapiens	9-13
27534383-9	2016	Addition of the polycationic protein protamine releases both HS 1 and HS 2 from their heparin complex, which simultaneously restores pyrene monomer emission for the first case and decreases the FRET process for the latter case, respectively.	Heparin	86-93	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	61-65
27534383-9	2016	Addition of the polycationic protein protamine releases both HS 1 and HS 2 from their heparin complex, which simultaneously restores pyrene monomer emission for the first case and decreases the FRET process for the latter case, respectively.	Heparin	86-93	spectrin beta, erythrocytic	Homo sapiens	70-74
27534383-10	2016	Dynamic light scattering (DLS) and AFM studies confirm aggregate formation of heparin with HS 1 and HS 2.	Heparin	78-85	eukaryotic translation elongation factor 1 alpha 2	Homo sapiens	91-95
27534383-10	2016	Dynamic light scattering (DLS) and AFM studies confirm aggregate formation of heparin with HS 1 and HS 2.	Heparin	78-85	spectrin beta, erythrocytic	Homo sapiens	100-104
27011369-6	2016	Unfractionated heparin as well as tinzaparin attenuated the IL-1beta-mediated induction of IL-6, IL-11, and LIF on protein and messenger RNA (mRNA) levels.	Heparin	15-22	interleukin 11	Homo sapiens	97-102
27011369-6	2016	Unfractionated heparin as well as tinzaparin attenuated the IL-1beta-mediated induction of IL-6, IL-11, and LIF on protein and messenger RNA (mRNA) levels.	Heparin	15-22	LIF interleukin 6 family cytokine	Homo sapiens	108-111
27366296-1	2016	We report a challenging case of cerebral venous sinus thrombosis (multiple etiologic factors) that was complicated by heparin resistance secondary to suspected antithrombin III (ATIII) deficiency.	Heparin	118-125	serpin family C member 1	Homo sapiens	160-176
27366296-1	2016	We report a challenging case of cerebral venous sinus thrombosis (multiple etiologic factors) that was complicated by heparin resistance secondary to suspected antithrombin III (ATIII) deficiency.	Heparin	118-125	serpin family C member 1	Homo sapiens	178-183
27366296-7	2016	Deficiency of ATIII was suspected as a possible etiology of her heparin resistance.	Heparin	64-71	serpin family C member 1	Homo sapiens	14-19
27069129-0	2016	Unfractionated Heparin Selectively Modulates the Expression of CXCL8, CCL2 and CCL5 in Endometrial Carcinoma Cells.	Heparin	15-22	C-C motif chemokine ligand 2	Homo sapiens	70-74
27069129-5	2016	UFH attenuated the secretion of CXCL8 and CCL2, and enhanced that of CCL5.	Heparin	0-3	C-C motif chemokine ligand 2	Homo sapiens	42-46
27069129-7	2016	CONCLUSION: UFH has selective modulating effects on the secretion of CXCL8, CCL2 and CCL5 in different endometrial adenocarcinoma cell lines.	Heparin	12-15	C-C motif chemokine ligand 2	Homo sapiens	76-80
27161720-7	2016	RESULTS: Unfractionated heparin (UFH) and low molecular weight heparin (LMWH) both strongly inhibited migration as well as adhesion of SCLC cells to fibronectin and stromal cells.	Heparin	24-31	fibronectin 1	Mus musculus	149-160
27161720-7	2016	RESULTS: Unfractionated heparin (UFH) and low molecular weight heparin (LMWH) both strongly inhibited migration as well as adhesion of SCLC cells to fibronectin and stromal cells.	Heparin	33-36	fibronectin 1	Mus musculus	149-160
27161720-7	2016	RESULTS: Unfractionated heparin (UFH) and low molecular weight heparin (LMWH) both strongly inhibited migration as well as adhesion of SCLC cells to fibronectin and stromal cells.	Heparin	63-70	fibronectin 1	Mus musculus	149-160
26769965-0	2016	Heparin Decreases in Tumor Necrosis Factor alpha (TNFalpha)-induced Endothelial Stress Responses Require Transmembrane Protein 184A and Induction of Dual Specificity Phosphatase 1.	Heparin	0-7	transmembrane protein 184A	Homo sapiens	105-131
26708018-1	2016	In previous studies Sulf2 has been evidenced to play an important role in tumor progression through editing sulfate moieties on heparan sulfate proteoglycans (HSPGs) and modulating heparin binding growth factors.	Heparin	181-188	sulfatase 2	Homo sapiens	20-25
27030175-3	2016	Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry.	Heparin	119-127	fibroblast growth factor 6	Homo sapiens	66-70
27030175-3	2016	Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry.	Heparin	119-127	fibroblast growth factor 17	Homo sapiens	79-84
27030175-3	2016	Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry.	Heparin	119-127	fibroblast growth factor 20	Homo sapiens	86-91
27088203-20	2016	We supposed that the heparin was ineffective due to an antithrombin deficiency.	Heparin	21-28	serpin family C member 1	Homo sapiens	55-67
26578266-1	2016	The antithrombin activity of unfractionated heparin (UFH) is offset by extracellular histones, which, along with DNA, represent a novel mediator of thrombosis and a structural component of thrombi.	Heparin	44-51	serpin family C member 1	Homo sapiens	4-16
26578266-1	2016	The antithrombin activity of unfractionated heparin (UFH) is offset by extracellular histones, which, along with DNA, represent a novel mediator of thrombosis and a structural component of thrombi.	Heparin	53-56	serpin family C member 1	Homo sapiens	4-16
26554332-0	2016	Oxidized antithrombin is a dual inhibitor of coagulation and angiogenesis: Importance of low heparin affinity.	Heparin	93-100	serpin family C member 1	Homo sapiens	9-21
26554332-7	2016	Latent and cleaved conformations of AT shows an increase in alpha-helical content in the presence of unfractionated heparin, but not the oxidized AT.	Heparin	116-123	serpin family C member 1	Homo sapiens	36-38
26554332-9	2016	The results of our study establish that active conformation of AT can become antiangiogenic while maintaining its anticoagulant activity possibly through chelation of low affinity heparin in the vicinity of endothelial cell.	Heparin	180-187	serpin family C member 1	Homo sapiens	63-65
26998625-8	2016	Attenuating intracellular calcium concentration with EGTA, heparin or procaine decreased POX-induced upregulation of calpain 1, calpain 2, caspase-12 and caspase-3, and reduced POX-induced cyt c release.	Heparin	59-66	calpain 2	Mus musculus	128-137
26359493-0	2015	Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States.	Heparin	111-118	serpin family C member 1	Homo sapiens	30-42
26359493-1	2015	Past studies have suggested that a key feature of the mechanism of heparin allosteric activation of the anticoagulant serpin, antithrombin, is the release of the reactive center loop P14 residue from a native state stabilizing interaction with the hydrophobic core.	Heparin	67-74	serpin family C member 1	Homo sapiens	126-138
26342034-8	2015	In agreement with this, the absence of Ctr2 caused a skewed ratio between proteoglycans of heparin and chondroitin sulfate type, with increased amounts of heparin accompanied by a reduction of chondroitin sulfate.	Heparin	91-98	solute carrier family 31 member 2	Homo sapiens	39-43
26342034-8	2015	In agreement with this, the absence of Ctr2 caused a skewed ratio between proteoglycans of heparin and chondroitin sulfate type, with increased amounts of heparin accompanied by a reduction of chondroitin sulfate.	Heparin	155-162	solute carrier family 31 member 2	Homo sapiens	39-43
26349809-5	2015	Among cell types assayed, adhesion persistence to P-selectin was specifically reduced in metastatic but not leukocyte-like cells in response to a low dose of heparin.	Heparin	158-165	selectin P	Homo sapiens	50-60
26396244-3	2015	Here, atomic force microscopy (AFM) of a single BAD-1 molecule interacting with immobilized heparin revealed that binding is enhanced upon treatment with protein disulfide isomerase and dithiothreitol (PDI/DTT).	Heparin	92-99	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	202-205
26396244-5	2015	Inhibition of PDI in murine macrophages blunted BAD-1 binding to heparin in vitro.	Heparin	65-72	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	14-17
26396244-8	2015	Mass spectroscopy of the tandem repeat revealed that the PDI-induced interaction with heparin is characterized by ruptured disulfide bonds and that cysteine thiols remain reduced.	Heparin	86-93	prolyl 4-hydroxylase, beta polypeptide	Mus musculus	57-60
26199422-7	2015	We also show that the vaspin-inhibition rate for KLK7 can be modestly increased by heparin and demonstrate that vaspin is a heparin-binding serpin.	Heparin	83-90	kallikrein related peptidase 7	Homo sapiens	49-53
26148660-0	2015	Antithrombin Concentrate Use in Children Receiving Unfractionated Heparin for Acute Thrombosis.	Heparin	66-73	serpin family C member 1	Homo sapiens	0-12
26148660-1	2015	OBJECTIVE: To characterize features of antithrombin concentrate (ATC) use in children receiving unfractionated heparin (UFH) therapy for acute thrombosis.	Heparin	111-118	serpin family C member 1	Homo sapiens	39-51
26148660-1	2015	OBJECTIVE: To characterize features of antithrombin concentrate (ATC) use in children receiving unfractionated heparin (UFH) therapy for acute thrombosis.	Heparin	120-123	serpin family C member 1	Homo sapiens	39-51
25998703-5	2015	Caveolin-1 participated in the anti-inflammatory process and it was able to be induced by heparin.	Heparin	90-97	caveolin 1, caveolae protein	Mus musculus	0-10
25998703-6	2015	Transfection of small interfering RNA of caveolin-1 into murine peritoneal macrophages attenuated the anti-inflammatory effects of heparin.	Heparin	131-138	caveolin 1, caveolae protein	Mus musculus	41-51
25998703-7	2015	Furthermore, following caveolin-1 silencing, the p38/mitogen-activated protein kinase (MAPK) pathway was still able to be activated by heparin, while the extracellular signal-regulated kinase and c-Jun N-terminal kinase pathways were inhibited.	Heparin	135-142	caveolin 1, caveolae protein	Mus musculus	23-33
25998703-8	2015	In conclusion, these results suggested that heparin inhibits LPS-induced inflammation via inducing caveolin-1 and activating the p38/MAPK pathway in murine peritoneal macrophages.	Heparin	44-51	caveolin 1, caveolae protein	Mus musculus	99-109
26186963-1	2015	INTRODUCTION: beta-antithrombin, the minor antithrombin glycoform in plasma, is probably the major thrombin inhibitor in vivo because of its high heparin affinity.	Heparin	146-153	serpin family C member 1	Homo sapiens	19-31
26188924-8	2015	A direct FXa inhibitor, edoxaban, and an antithrombin-dependent anticoagulant, unfractionated heparin (UFH), did not increase, but simply decreased TG under each condition in a concentration dependent manner.	Heparin	94-101	serpin family C member 1	Homo sapiens	41-53
26251446-0	2015	Mapping the heparin-binding site of the BMP antagonist gremlin by site-directed mutagenesis based on predictive modelling.	Heparin	12-19	bone morphogenetic protein 1	Homo sapiens	40-43
25147059-0	2015	Structural and binding studies of SAP-1 protein with heparin.	Heparin	53-60	protein tyrosine phosphatase receptor type H	Homo sapiens	34-39
25147059-5	2015	Therefore, we have employed surface plasmon resonance (SPR) to improve our understanding of the binding interaction between heparin and SAP-1 (protease inhibitor).	Heparin	124-131	protein tyrosine phosphatase receptor type H	Homo sapiens	136-141
25147059-6	2015	SPR data suggest that SAP-1 binds to heparin with a significant affinity (KD = 158 nm).	Heparin	37-44	protein tyrosine phosphatase receptor type H	Homo sapiens	22-27
25147059-7	2015	SPR solution competition studies using heparin oligosaccharides showed that the binding of SAP-1 to heparin is dependent on chain length.	Heparin	39-46	protein tyrosine phosphatase receptor type H	Homo sapiens	91-96
25147059-9	2015	Further to get insight into the structural aspect of interactions between SAP-1 and heparin, we used modelled structure of the SAP-1 and docked with heparin and heparin-derived polysaccharides.	Heparin	84-91	protein tyrosine phosphatase receptor type H	Homo sapiens	74-79
25147059-9	2015	Further to get insight into the structural aspect of interactions between SAP-1 and heparin, we used modelled structure of the SAP-1 and docked with heparin and heparin-derived polysaccharides.	Heparin	84-91	protein tyrosine phosphatase receptor type H	Homo sapiens	127-132
25147059-9	2015	Further to get insight into the structural aspect of interactions between SAP-1 and heparin, we used modelled structure of the SAP-1 and docked with heparin and heparin-derived polysaccharides.	Heparin	149-156	protein tyrosine phosphatase receptor type H	Homo sapiens	74-79
25147059-9	2015	Further to get insight into the structural aspect of interactions between SAP-1 and heparin, we used modelled structure of the SAP-1 and docked with heparin and heparin-derived polysaccharides.	Heparin	149-156	protein tyrosine phosphatase receptor type H	Homo sapiens	127-132
25723475-0	2015	Low molecular weight heparin (LMWH) improves peritoneal function and inhibits peritoneal fibrosis possibly through suppression of HIF-1alpha, VEGF and TGF-beta1.	Heparin	21-28	vascular endothelial growth factor A	Rattus norvegicus	142-146
25708982-5	2015	N-terminal extension of the isolated FNIII EDA with its neighboring FNIII repeats (FNIII 9-10-11) enhanced its activity in agonizing TLR4, while C-terminal extension with the native FNIII 12-13-14 heparin-binding domain abrogated it.	Heparin	197-204	ectodysplasin-A	Mus musculus	43-46
25497737-6	2015	Ca(2+) flux, chemotaxis, and heparin binding assays showed that the monomer form of XCL2 is responsible for G protein-coupled receptor activation while the dimeric form is important for GAG binding.	Heparin	29-36	X-C motif chemokine ligand 2	Homo sapiens	84-88
25665603-0	2015	[Unfractionated heparin inhibits lipopolysaccharide-induced expression of granulocyte colony-stimulating factor in human endothelial cells through Toll-like receptor 4 signaling pathway].	Heparin	16-23	colony stimulating factor 3	Homo sapiens	74-111
25665603-0	2015	[Unfractionated heparin inhibits lipopolysaccharide-induced expression of granulocyte colony-stimulating factor in human endothelial cells through Toll-like receptor 4 signaling pathway].	Heparin	16-23	toll like receptor 4	Homo sapiens	147-167
25486437-1	2015	Heparan sulfate (HS) 3-O-sulfation determines the binding specificity of HS/heparin for antithrombin III and plays a key role in herpes simplex virus (HSV) infection.	Heparin	76-83	serpin family C member 1	Homo sapiens	88-104
25966765-6	2015	There was more production of APC-PCI and platelet-derived PAI-1 in the filter after 10 min in the heparin group than in other groups.	Heparin	98-105	serpin family E member 1	Homo sapiens	58-63
25966765-7	2015	In clotting filters, production of APC-PCI and PAI was also higher with heparin than citrate.	Heparin	72-79	serpin family E member 1	Homo sapiens	35-50
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	158-163
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-194
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class B member 1	Homo sapiens	199-208
26651243-3	2015	We showed that treatment of human glioblastoma A-172 and fibrosarcoma HT1080 cells with sodium chlorate, heparinase, and heparin causes a prominent loss of 2 Hsp90 cytosolic isoforms, Hsp90alpha and Hsp90beta, from the cell surface and strongly inhibits the binding of exogenous Hsp90 to cells.	Heparin	105-112	heat shock protein 90 alpha family class A member 1	Homo sapiens	184-189
26651243-4	2015	We revealed that Hsp90alpha and Hsp90beta are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.	Heparin	174-181	heat shock protein 90 alpha family class A member 1	Homo sapiens	17-27
26651243-4	2015	We revealed that Hsp90alpha and Hsp90beta are partly colocalized with heparan sulfate proteoglycans (HSPGs) on the cell surface and that this colocalization was sensitive to heparin.	Heparin	174-181	heat shock protein 90 alpha family class B member 1	Homo sapiens	32-41
25466846-0	2015	Development of a novel, rapid assay for detection of heparin-binding defect antithrombin deficiencies: the heparin-antithrombin binding (HAB) ratio.	Heparin	53-60	serpin family C member 1	Homo sapiens	76-88
25466846-3	2015	PATIENTS/METHODS: Extended heparin incubation in antithrombin activity assays can overestimate levels in patients with HBDs.	Heparin	27-34	serpin family C member 1	Homo sapiens	49-61
25441837-1	2014	Bone morphogenetic protein 1 (BMP1) was originally isolated from bone with other BMPs due to its affinity for heparin.	Heparin	110-117	bone morphogenetic protein 1	Homo sapiens	0-28
25441837-1	2014	Bone morphogenetic protein 1 (BMP1) was originally isolated from bone with other BMPs due to its affinity for heparin.	Heparin	110-117	bone morphogenetic protein 1	Homo sapiens	30-34
25312341-0	2014	Identification of a new SERPINC1 mutation in a Kazak family that alters the heparin binding capacity of antithrombin.	Heparin	76-83	serpin family C member 1	Homo sapiens	24-32
25312341-0	2014	Identification of a new SERPINC1 mutation in a Kazak family that alters the heparin binding capacity of antithrombin.	Heparin	76-83	serpin family C member 1	Homo sapiens	104-116
25312341-1	2014	INTRODUCTION: Given its central role in mediating heparin-induced anti-coagulation, antithrombin (AT) gene mutations may result in heparin resistance.	Heparin	50-57	serpin family C member 1	Homo sapiens	84-96
25312341-1	2014	INTRODUCTION: Given its central role in mediating heparin-induced anti-coagulation, antithrombin (AT) gene mutations may result in heparin resistance.	Heparin	131-138	serpin family C member 1	Homo sapiens	84-96
25202017-2	2014	Previous investigations have shown that ATIII is degraded by Staphylococcus aureus V8 protease, leading to release of heparin binding fragments derived from its D helix.	Heparin	118-125	serpin family C member 1	Homo sapiens	40-45
25202017-5	2014	Correspondingly, the heparin-binding, helix D-derived, peptide FFFAKLNCRLYRKANKSSKLV (FFF21) of human ATIII, was found to be antimicrobial against particularly the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa.	Heparin	21-28	serpin family C member 1	Homo sapiens	102-107
25284680-3	2014	The aggregation mechanism of tau in the presence of inducers such as heparin, deciphered using probes such as thioflavin T/S fluorescence, light scattering, and electron microscopy assays, has been shown to conform to ligand-induced nucleation-dependent polymerization.	Heparin	69-76	microtubule associated protein tau	Homo sapiens	29-32
25284680-5	2014	In this study, UV resonance Raman spectroscopy is employed to look directly at signatures of changes in secondary structure and side-chain packing during fibril formation by the four repeat functional domain of tau in the presence of the inducer heparin, at pH 7 and at 37  C. Changes in the positions and intensities of the amide Raman bands are shown to occur in two distinct stages during the fibril formation process.	Heparin	246-253	microtubule associated protein tau	Homo sapiens	211-214
24993449-8	2014	Although a 3-fold higher initial bolus of heparin was administered with cPE/HD, the heparin dose per hour was similar with both modalities and the total heparin load was only slightly lower with cPE/HD, with a median 2939 IU/m(2) per session (interquartile range, 1868, 4189) versus 3341 IU/m(2) per session (interquartile range, 2126, 4792).	Heparin	42-49	carboxypeptidase E	Homo sapiens	72-75
25191939-7	2014	Inhibition of complement by C1-inh was potentiated by ~10-fold by polysulfated macromolecules including heparin and dextran sulfate.	Heparin	104-111	serpin family G member 1	Rattus norvegicus	28-34
25191939-8	2014	In rats, intravenous C1-inh at a dose 30-fold greater than that approved to treat HAE inhibited serum complement activity by &lt;5%, even when supplemented with heparin.	Heparin	161-168	serpin family G member 1	Rattus norvegicus	21-27
25108113-9	2014	Despite this substitution, MPXV A29 bound to heparin with similar affinity to that of VACV A27 protein, suggesting flexibility of this motif for heparin binding.	Heparin	45-52	immunoglobulin kappa variable 2-18 (pseudogene)	Homo sapiens	32-35
25108113-10	2014	Although binding of mAb 69-126-3-7 to MPXV A29 prevented interaction with heparin, it did not have any effect on the infectivity of MPXV.	Heparin	74-81	immunoglobulin kappa variable 2-18 (pseudogene)	Homo sapiens	43-46
24984153-7	2014	One of the selected compounds, 50F10, was directly shown to preserve the active homodimer structure of LPL, as demonstrated by heparin-Sepharose chromatography.	Heparin	127-134	lipoprotein lipase	Homo sapiens	103-106
24522239-1	2014	Antithrombin (AT) is a heparin-binding serpin in plasma which regulates the proteolytic activity of procoagulant proteases of the clotting cascade.	Heparin	23-30	serpin family C member 1	Homo sapiens	0-12
24994735-4	2014	Heparin resistance is very rare in these patients, especially when antithrombin levels are near normal.	Heparin	0-7	serpin family C member 1	Homo sapiens	67-79
24835176-4	2014	Our glycan microarray showed a unique affinity profile of chemokine CCL20 to substructures of heparin and heparin-like oligo/di/monosaccharides.	Heparin	94-101	chemokine (C-C motif) ligand 20	Mus musculus	68-73
24835176-4	2014	Our glycan microarray showed a unique affinity profile of chemokine CCL20 to substructures of heparin and heparin-like oligo/di/monosaccharides.	Heparin	106-113	chemokine (C-C motif) ligand 20	Mus musculus	68-73
24357546-5	2014	Heparin increased gene expression of chain initiation and modification enzymes including EXT1 and NDST1, as well as core proteins SDC2 and GPC6.	Heparin	0-7	N-deacetylase and N-sulfotransferase 1	Homo sapiens	98-103
24354788-8	2014	RT-PCR showed an increase in the epiregulin and heparin-binding EGF levels from day 0 to day 3 after the release of the duct obstruction.	Heparin	48-55	epidermal growth factor	Mus musculus	64-67
24832898-6	2014	In the presence of heparin, a well-known activator of FGF signaling, cystic morphology with lumen expansion was observed in cultures containing FGF1, FGF7, or FGF10, but growth arrest was observed in cultures containing FGF2 or FGF9.	Heparin	19-26	fibroblast growth factor 7	Mus musculus	150-154
24604825-2	2014	Here we show by a combination of NMR and EPR spectroscopy that the binding of the cytokine osteopontin (OPN) to its natural ligand, heparin, is accompanied by thermodynamically compensating structural adaptations.	Heparin	132-139	secreted phosphoprotein 1	Homo sapiens	91-102
24604825-2	2014	Here we show by a combination of NMR and EPR spectroscopy that the binding of the cytokine osteopontin (OPN) to its natural ligand, heparin, is accompanied by thermodynamically compensating structural adaptations.	Heparin	132-139	secreted phosphoprotein 1	Homo sapiens	104-107
24604825-4	2014	This "unfolding-upon-binding" is governed primarily through electrostatic interactions between heparin and charged patches along the protein backbone and compensates for entropic penalties due to heparin-OPN binding.	Heparin	95-102	secreted phosphoprotein 1	Homo sapiens	204-207
24325600-5	2014	In this report, we demonstrate the efficacy of a 2-O, 3-O-desulfated heparin (ODSH), a modified heparin with minimal anticoagulant activity, to inhibit NE activity and to block NE-induced airway inflammation.	Heparin	69-76	elastase, neutrophil expressed	Mus musculus	152-154
24325600-5	2014	In this report, we demonstrate the efficacy of a 2-O, 3-O-desulfated heparin (ODSH), a modified heparin with minimal anticoagulant activity, to inhibit NE activity and to block NE-induced airway inflammation.	Heparin	69-76	elastase, neutrophil expressed	Mus musculus	177-179
24325600-5	2014	In this report, we demonstrate the efficacy of a 2-O, 3-O-desulfated heparin (ODSH), a modified heparin with minimal anticoagulant activity, to inhibit NE activity and to block NE-induced airway inflammation.	Heparin	96-103	elastase, neutrophil expressed	Mus musculus	152-154
24325600-5	2014	In this report, we demonstrate the efficacy of a 2-O, 3-O-desulfated heparin (ODSH), a modified heparin with minimal anticoagulant activity, to inhibit NE activity and to block NE-induced airway inflammation.	Heparin	96-103	elastase, neutrophil expressed	Mus musculus	177-179
24508514-1	2014	A synthesis to L-iduronic derivatives, major components of heparin derived pentasaccharides was accomplished by formal inversion of configuration at C-5 of a D-glucuronic acid derivative through radical formation at C-5 using Barton decarboxylation followed by intramolecular radical addition on an acetylenic tether at O-4 giving exclusively a bicyclic sugar of L-ido configuration.	Heparin	59-66	complement C5	Homo sapiens	149-152
24508514-1	2014	A synthesis to L-iduronic derivatives, major components of heparin derived pentasaccharides was accomplished by formal inversion of configuration at C-5 of a D-glucuronic acid derivative through radical formation at C-5 using Barton decarboxylation followed by intramolecular radical addition on an acetylenic tether at O-4 giving exclusively a bicyclic sugar of L-ido configuration.	Heparin	59-66	complement C5	Homo sapiens	216-219
24398330-4	2014	Four nonanticoagulant heparins inhibited hepcidin expression in hepatic HepG2 cells and primary hepatocytes.	Heparin	22-30	hepcidin antimicrobial peptide	Homo sapiens	41-49
24529131-9	2014	The association of purified decorin with human LDL in an in vitro microassay was blocked by serum albumin and heparin suggesting anti-atherogenic roles for these proteins in vivo.	Heparin	110-117	decorin	Homo sapiens	28-35
24365672-3	2014	CPE was characterized as glycoprotein by Periodic Acid Schiff (PAS) staining and treating with deglycosylating enzyme N-glycosidase F. The interaction of CPE with heparin was illustrated by surface plasmon resonance (SPR) and in silico interaction analysis.	Heparin	163-170	carboxypeptidase E	Homo sapiens	0-3
24365672-3	2014	CPE was characterized as glycoprotein by Periodic Acid Schiff (PAS) staining and treating with deglycosylating enzyme N-glycosidase F. The interaction of CPE with heparin was illustrated by surface plasmon resonance (SPR) and in silico interaction analysis.	Heparin	163-170	carboxypeptidase E	Homo sapiens	154-157
24365672-4	2014	The association constant (KA) and dissociation constant (KD) of CPE with heparin was determined by SPR and found to be 1.06 x 10(5)M and 9.46 x 10(-6)M, respectively.	Heparin	73-80	carboxypeptidase E	Homo sapiens	64-67
24365672-7	2014	We suggest that CPE might act not only in the innate immunity of male reproductive tract but also regulate sperm fertilization process by interacting heparin.	Heparin	150-157	carboxypeptidase E	Homo sapiens	16-19
24412695-7	2014	The results indicate that lithium-heparin plasma samples are suitable for measurement of equine SAA using this method.	Heparin	34-41	serum amyloid A protein	Equus caballus	96-99
24438898-7	2014	The plasma components of hPL necessitate addition of anticoagulants such as heparins to prevent gelatinization of hPL medium, and their concentration must be standardized.	Heparin	76-84	galectin 1	Homo sapiens	25-28
24438898-7	2014	The plasma components of hPL necessitate addition of anticoagulants such as heparins to prevent gelatinization of hPL medium, and their concentration must be standardized.	Heparin	76-84	galectin 1	Homo sapiens	114-117
25594496-2	2015	The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation.	Heparin	88-95	serpin family C member 1	Homo sapiens	126-142
25594496-2	2015	The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation.	Heparin	88-95	serpin family C member 1	Homo sapiens	144-146
25863018-0	2015	A fast capillary electrophoresis method to assess the binding affinity of recombinant antithrombin toward heparin directly from cell culture supernatants.	Heparin	106-113	serpin family C member 1	Homo sapiens	86-98
25863018-1	2015	With the aim to determine the binding affinity of a new generation of recombinant antithrombin (AT) toward heparin, we developed a dynamic equilibrium-affinity capillary electrophoresis (DE-ACE) method.	Heparin	107-114	serpin family C member 1	Homo sapiens	82-94
24911927-0	2014	Heparin responses in vascular smooth muscle cells involve cGMP-dependent protein kinase (PKG).	Heparin	0-7	protein kinase cGMP-dependent 1	Homo sapiens	89-92
25387410-0	2014	Inflammatory response to heparinoid and heparin in a patient with tumor necrosis factor receptor-associated periodic syndrome: the second case with a T61I mutation in the TNFRSF1A gene.	Heparin	25-32	TNF receptor superfamily member 1A	Homo sapiens	171-179
25093806-5	2014	Reduction of hepatic hepcidin through administration of heparin restrained tumorigenic properties of breast tumor cells.	Heparin	56-63	hepcidin antimicrobial peptide	Homo sapiens	21-29
25023776-0	2014	Unfractionated heparin suppresses lipopolysaccharide-induced monocyte chemoattractant protein-1 expression in human microvascular endothelial cells by blocking Kruppel-like factor 5 and nuclear factor-kappaB pathway.	Heparin	15-22	C-C motif chemokine ligand 2	Homo sapiens	61-95
24901804-0	2014	Antithrombin concentrate in pediatric patients requiring unfractionated heparin anticoagulation: a retrospective cohort study.	Heparin	72-79	serpin family C member 1	Homo sapiens	0-12
27526536-11	2014	This is done to avoid the influence of LPL activity on heparin treatment for cardiovascular disease patients.	Heparin	55-62	lipoprotein lipase	Homo sapiens	39-42
25034023-0	2014	Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assembly.	Heparin	0-7	fibrillin 1	Homo sapiens	33-55
25127119-8	2014	In addition, the HSulf2 preferentially digests the oligosaccharide domain located at the non-reducing end (NRE) of the HS and heparin chain.	Heparin	126-133	sulfatase 2	Homo sapiens	17-23
24704550-2	2014	S447X carriers have higher LPL levels in the pre- and post-heparin plasma, raising the possibility that the S447X polymorphism leads to higher LPL levels within capillaries.	Heparin	59-66	lipoprotein lipase	Homo sapiens	27-30
24704550-2	2014	S447X carriers have higher LPL levels in the pre- and post-heparin plasma, raising the possibility that the S447X polymorphism leads to higher LPL levels within capillaries.	Heparin	59-66	lipoprotein lipase	Homo sapiens	143-146
24801362-2	2014	The capacity of antithrombin to inhibit thrombin is known to increase a 1000-fold whilst in the presence of unfractionated heparin.	Heparin	123-130	serpin family C member 1	Homo sapiens	16-28
24801362-3	2014	beta-antithrombin is an isoform of antithrombin with a high affinity for unfractionated heparin.	Heparin	88-95	serpin family C member 1	Homo sapiens	5-17
24801362-3	2014	beta-antithrombin is an isoform of antithrombin with a high affinity for unfractionated heparin.	Heparin	88-95	serpin family C member 1	Homo sapiens	35-47
24671416-0	2014	Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing alpha-synuclein oligomeric species toxicity.	Heparin	31-38	synuclein alpha	Homo sapiens	112-127
24470361-6	2014	RESULTS: Fusion of heparin-binding domain with IGF-1 prolonged retention in articular and meniscal cartilage from &lt;1 day to 8 days after injection.	Heparin	19-26	insulin-like growth factor 1	Rattus norvegicus	47-52
24616065-1	2014	The anticoagulant properties of heparin stem in part from high-affinity binding to antithrombin-III (AT-III) inducing a 300-fold increase in its inhibitory activity against the coagulation protease factor Xa.	Heparin	32-39	serpin family C member 1	Homo sapiens	83-99
24616065-1	2014	The anticoagulant properties of heparin stem in part from high-affinity binding to antithrombin-III (AT-III) inducing a 300-fold increase in its inhibitory activity against the coagulation protease factor Xa.	Heparin	32-39	serpin family C member 1	Homo sapiens	101-107
24616065-3	2014	ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra).	Heparin	103-111	serpin family C member 1	Homo sapiens	49-55
24979990-4	2014	A glycoarray assay showed that recombinant p23 proteins from the three genotypes bound to heparin, indicating that p23 is a heparin-binding Theileria surface molecule.	Heparin	90-97	cyclin dependent kinase 5 regulatory subunit 1	Bos taurus	43-46
24979990-4	2014	A glycoarray assay showed that recombinant p23 proteins from the three genotypes bound to heparin, indicating that p23 is a heparin-binding Theileria surface molecule.	Heparin	90-97	cyclin dependent kinase 5 regulatory subunit 1	Bos taurus	115-118
24979990-4	2014	A glycoarray assay showed that recombinant p23 proteins from the three genotypes bound to heparin, indicating that p23 is a heparin-binding Theileria surface molecule.	Heparin	124-131	cyclin dependent kinase 5 regulatory subunit 1	Bos taurus	43-46
24979990-4	2014	A glycoarray assay showed that recombinant p23 proteins from the three genotypes bound to heparin, indicating that p23 is a heparin-binding Theileria surface molecule.	Heparin	124-131	cyclin dependent kinase 5 regulatory subunit 1	Bos taurus	115-118
24297394-13	2014	LDL receptor blocking agent heparin decreased lipid droplets induced by LPS significantly in THP-1 macrophages and VSMCs.	Heparin	28-35	low density lipoprotein receptor	Homo sapiens	0-12
24005342-1	2014	UNLABELLED: Recombinant soluble human thrombomodulin (TM-alpha) has been shown to be useful in the treatment of disseminated intravascular coagulation (DIC) in a heparin-controlled study and has been available for clinical use in Japan since 2008.	Heparin	162-169	thrombomodulin	Homo sapiens	38-62
24326668-9	2014	The MST lines express N-acetylglucosamine N-deacetylase/N-sulfotransferase-1, uronosyl 2-O-sulfotransferase and glucosaminyl 6-O-sulfotransferase-1, which are sufficient to make the highly sulfated HP.	Heparin	198-200	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	42-107
24193793-4	2014	Heparin has been shown to interfere with the binding of the integrin Very Late Antigen 4 (VLA-4) to its ligand Vascular Cell Adhesion Molecule 1 (VCAM-1) and in a recent paper the laboratory of Bendas (Thrombosis and Haemostasis, Prepublished online) demonstrated that CCN1 binds to VLA-4 and interference in this binding by heparin results in reduced strength of the VLA-4/VCAM-1 binding.	Heparin	0-7	cellular communication network factor 1	Homo sapiens	269-273
24779124-1	2014	Acquired antithrombin (AT) deficiency has been associated with patients on extracorporeal membrane oxygenation (ECMO) as a result of hemodilution, blood coagulation activation, and the use of heparin.	Heparin	192-199	serpin family C member 1	Homo sapiens	9-21
24485402-8	2014	CONCLUSIONS: These data not only confirm the role played by PAI-1 activity and by the 4G/5G SNP of the PAI-1 gene, but also suggest that current therapeutic protocols, recommending the administration of low weight molecular heparin and oral anticoagulant for the treatment of deep vein thrombosis, could be non sufficient for patients genetically predisposed to a less efficient clot lysis.	Heparin	224-231	serpin family E member 1	Homo sapiens	103-108
24148803-7	2014	In parallel experiments heparin was shown to have minor inhibitory effects on fibulin-5 interactions with tropoelastin and LTBP-2.	Heparin	24-31	fibulin 5	Homo sapiens	78-87
24287143-6	2014	Both heparin treatments decreased the accumulation of T cells and macrophages (P &lt; .03), and the activation of NF-kappaB and pERK (P &lt; .04) in the diverted colon.	Heparin	5-12	eukaryotic translation initiation factor 2 alpha kinase 3	Homo sapiens	128-132
24014620-5	2014	Antithrombin (AT) binds to heparin and increases the rate at which it binds to thrombin.	Heparin	27-34	serpin family C member 1	Homo sapiens	0-12
24014620-6	2014	The levels of antithrombin in the blood are an important aspect of the heparin dose-response curve.	Heparin	71-78	serpin family C member 1	Homo sapiens	14-26
24014620-8	2014	Heparin resistance is usually treated with a combination of supplementary heparin, fresh frozen plasma (FFP) or antithrombin III concentrate.	Heparin	0-7	serpin family C member 1	Homo sapiens	112-128
24014620-11	2014	Antithrombin (AT) concentrate is a safe and efficient treatment for heparin resistance to elevate the activated clotting time (ACT).	Heparin	68-75	serpin family C member 1	Homo sapiens	0-12
24014620-13	2014	Antithrombin concentrates are more expensive than fresh frozen plasma and may put patients at risk of heparin rebound in the early postoperative period.	Heparin	102-109	serpin family C member 1	Homo sapiens	0-12
24678194-0	2014	Elucidating the specificity of non-heparin-based conformational activators of antithrombin for factor Xa inhibition.	Heparin	35-42	serpin family C member 1	Homo sapiens	78-90
24678194-1	2014	INTRODUCTION: Antithrombin, the principal inhibitor of coagulation proteases, requires allosteric activation by its physiological cofactor, heparin or heparin sulfate to achieve physiologically permissible rates.	Heparin	140-147	serpin family C member 1	Homo sapiens	14-26
23855665-10	2014	c) An isozyme specific antithrombin study showed the structural basis of improved heparin binding to beta antithrombin as compared to alpha-antithrombin.	Heparin	82-89	serpin family C member 1	Homo sapiens	23-35
23855665-10	2014	c) An isozyme specific antithrombin study showed the structural basis of improved heparin binding to beta antithrombin as compared to alpha-antithrombin.	Heparin	82-89	serpin family C member 1	Homo sapiens	106-118
23855665-10	2014	c) An isozyme specific antithrombin study showed the structural basis of improved heparin binding to beta antithrombin as compared to alpha-antithrombin.	Heparin	82-89	serpin family C member 1	Homo sapiens	106-118
24068708-0	2013	The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin.	Heparin	100-107	serpin family C member 1	Homo sapiens	42-54
24068708-0	2013	The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin.	Heparin	100-107	serpin family C member 1	Homo sapiens	212-224
24171489-8	2013	Cell behavior was highly dependent on pH during multilayer formation with heparin as polyanion and was closely related to fibronectin adsorption.	Heparin	74-81	fibronectin 1	Mus musculus	122-133
32261185-6	2013	Interestingly, on addition of 0.5 mug mL-1 heparin into aggregated FA-AuNPs, the absorption maximum attained a blue shift and the wine red color reverted back.	Heparin	43-50	L1 cell adhesion molecule	Mus musculus	38-42
24124146-0	2013	The superiority of anti-FXa assay over anti-FIIa assay in detecting heparin-binding site antithrombin deficiency.	Heparin	68-75	serpin family C member 1	Homo sapiens	89-101
24124146-9	2013	CONCLUSIONS: Anti-FXa antithrombin assay is recommended as a first-line test to detect type II heparin-binding site antithrombin deficiency.	Heparin	95-102	serpin family C member 1	Homo sapiens	22-34
24124146-9	2013	CONCLUSIONS: Anti-FXa antithrombin assay is recommended as a first-line test to detect type II heparin-binding site antithrombin deficiency.	Heparin	95-102	serpin family C member 1	Homo sapiens	116-128
24121110-1	2013	Antithrombin III (ATIII) performs a critical anticoagulant function by precluding the activation of blood clotting proteinases, aided by its two cofactors, heparin and heparan sulfate.	Heparin	156-163	serpin family C member 1	Homo sapiens	18-23
24121110-6	2013	We found that heparin binding basic residues, hD helix, three pairs of Cys-Cys salt bridges, N-glycosylation sites, serpin motifs and inhibitory reactive center loop (RCL) of ATIII protein are highly conserved.	Heparin	14-21	serpin family C member 1	Homo sapiens	175-180
24095600-2	2013	The anticoagulation process is mainly caused by the interaction of heparin with antithrombin followed by inhibition of anticoagulant factor IIa and factor Xa.	Heparin	67-74	serpin family C member 1	Homo sapiens	80-92
23793991-1	2013	PURPOSE: Our objective was to develop novel nanocarriers (protected graft copolymer, PGC) that improve the stability of heparin binding EGF (HBEGF) and gastrin and then to use PGC-formulated HBEGF (PGC-HBEGF) and Omeprazole (+/- PGC-gastrin) for normalizing fasting blood glucose (FBG) and improving islet function in diabetic mice.	Heparin	120-127	epidermal growth factor	Mus musculus	136-139
23793991-1	2013	PURPOSE: Our objective was to develop novel nanocarriers (protected graft copolymer, PGC) that improve the stability of heparin binding EGF (HBEGF) and gastrin and then to use PGC-formulated HBEGF (PGC-HBEGF) and Omeprazole (+/- PGC-gastrin) for normalizing fasting blood glucose (FBG) and improving islet function in diabetic mice.	Heparin	120-127	heparin-binding EGF-like growth factor	Mus musculus	141-146
24163620-6	2013	The critical concentrations of 4RMBD and its S305N mutant are 5.26 muM and 4.04 muM respectively, indicating point mutation S305N, which is associated with FTDP-17, appear to enhance the heparin-induced tau aggregation in vitro.	Heparin	187-194	microtubule associated protein tau	Homo sapiens	156-163
23752481-0	2013	Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots.	Heparin	0-7	serpin family C member 1	Homo sapiens	50-62
23597922-0	2013	STAT1 requirement for PKR-induced cell cycle arrest in vascular smooth muscle cells in response to heparin.	Heparin	99-106	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	22-25
23597922-9	2013	In order to understand the mechanism of heparin-induced stabilization of p27(kip1) in VSMC, we examined the involvement of the Signal Transducer and Activator of Transcription-1 (STAT1), which is an important player in mediating antiproliferative effects of IFNs.	Heparin	40-47	cyclin dependent kinase inhibitor 1B	Homo sapiens	77-81
23597922-11	2013	PKR activation induced by antiproliferative agent heparin leads to phosphorylation of STAT1 on serine 727, which is essential for the cell cycle block.	Heparin	50-57	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	0-3
23597922-12	2013	STAT1 null VSMCs are largely defective in heparin-induced cell cycle arrest and in PKR null cells the STAT1 phosphorylation in response to heparin was absent.	Heparin	139-146	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	83-86
23597922-13	2013	These results establish that heparin causes STAT1 phosphorylation on serine 727 via activation of PKR and that this event is required for the G1 arrest in VSMC.	Heparin	29-36	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	98-101
23110868-6	2013	In the second protocol, insulin was accompanied by Intralipid, which is mainly a mixture of triacylglycerols, and heparin, given as an activator of lipoprotein lipase, inducing insulin resistance.	Heparin	114-121	lipoprotein lipase	Homo sapiens	148-166
23974171-6	2013	A cell cultivation system using heparin-functionalized thermoresponsive cell culture surface is versatile for immobilizing other heparin-binding proteins such as vascular endothelial growth factor, fibronectin, antithrombin III, and hepatocyte growth factor, etc.	Heparin	32-39	serpin family C member 1	Homo sapiens	211-227
23875127-10	2013	Finally, the calculated concentration of IL-24 was increased in ethylenediaminetetraacetic acid (EDTA) plasma compared to heparin plasma and serum and decreased with repetitive freeze/thaw cycles of the samples illustrating how sample handling could additionally contribute to the variations reported by different laboratories in measurement of the same analyte.	Heparin	122-129	interleukin 24	Homo sapiens	41-46
23581397-1	2013	BACKGROUND: Heparin and its analogs, mediating their anticoagulant activity through antithrombin (AT) activation, remain largely used for the preventive and curative treatment of thrombosis.	Heparin	12-19	serpin family C member 1	Homo sapiens	84-96
23581397-1	2013	BACKGROUND: Heparin and its analogs, mediating their anticoagulant activity through antithrombin (AT) activation, remain largely used for the preventive and curative treatment of thrombosis.	Heparin	12-19	serpin family C member 1	Homo sapiens	98-100
23581397-4	2013	To secure administration of AT-mediated anticoagulants and counteract bleeding disorders, we previously designed a recombinant inactive AT as an antidote to heparin derivatives.	Heparin	157-164	serpin family C member 1	Homo sapiens	28-30
23581397-4	2013	To secure administration of AT-mediated anticoagulants and counteract bleeding disorders, we previously designed a recombinant inactive AT as an antidote to heparin derivatives.	Heparin	157-164	serpin family C member 1	Homo sapiens	136-138
23581397-5	2013	OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs.	Heparin	190-197	serpin family C member 1	Homo sapiens	70-72
23581397-5	2013	OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs.	Heparin	190-197	serpin family C member 1	Homo sapiens	165-167
23581397-5	2013	OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs.	Heparin	228-235	serpin family C member 1	Homo sapiens	70-72
23581397-5	2013	OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs.	Heparin	228-235	serpin family C member 1	Homo sapiens	165-167
23581397-8	2013	RESULTS: AT treated by butanedione and selected for its high heparin affinity (AT-BD) was indeed modified on reactive Arg393 and thus exhibited decreased anticoagulant activity and increased heparin affinity.	Heparin	61-68	serpin family C member 1	Homo sapiens	9-11
23581397-8	2013	RESULTS: AT treated by butanedione and selected for its high heparin affinity (AT-BD) was indeed modified on reactive Arg393 and thus exhibited decreased anticoagulant activity and increased heparin affinity.	Heparin	61-68	serpin family C member 1	Homo sapiens	79-81
23581397-9	2013	AT-BD was able to neutralize anticoagulant activity of heparin derivatives in vitro and in vivo and was devoid of intrinsic anticoagulant activity, as assessed by activated partial thromboplastin time assay.	Heparin	55-62	serpin family C member 1	Homo sapiens	0-2
23494009-0	2013	Covalently linking heparin to antithrombin enhances prothrombinase inhibition on activated platelets.	Heparin	19-26	serpin family C member 1	Homo sapiens	30-42
23374371-0	2013	Neutralizing the anticoagulant activity of ultra-low-molecular-weight heparins using N-acetylglucosamine 6-sulfatase.	Heparin	70-78	glucosamine (N-acetyl)-6-sulfatase	Homo sapiens	85-116
23102903-1	2013	OBJECTIVES: Purified antithrombin supplementation in cardiac surgery has been suggested for the treatment of heparin resistance and the prevention of thromboembolic complications.	Heparin	109-116	serpin family C member 1	Homo sapiens	21-33
23102903-7	2013	Heparin resistance rate was significantly (P = .001) higher in the control group (38.2%) versus the antithrombin group (17%).	Heparin	0-7	serpin family C member 1	Homo sapiens	100-112
23102903-10	2013	CONCLUSIONS: Preoperative antithrombin supplementation prevents heparin resistance and avoids excessive postoperative decrease of antithrombin activity.	Heparin	64-71	serpin family C member 1	Homo sapiens	26-38
23601319-0	2013	Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes.	Heparin	12-19	fibroblast growth factor receptor 2	Homo sapiens	106-111
23307015-6	2013	A mouse osteoporotic model was used to test the ability of BMP6 to improve the bone quality in vivo in the presence of heparin, followed by DEXA and muCT analyses.	Heparin	119-126	bone morphogenetic protein 6	Mus musculus	59-63
23307015-9	2013	After 48 and 72 hours of treatment, heparin inhibited BMP6-induced ALP and OC expression in C2C12 cells.	Heparin	36-43	bone morphogenetic protein 6	Mus musculus	54-58
23307015-10	2013	Heparin dose dependently inhibited BMP6-induced new bone and cartilage formation in the rat ectopic bone formation assay, while in osteoporotic mice heparin inhibited the BMP6 potential to improve the bone quality as evidenced by decreased bone mineral density and trabecular bone parameters.	Heparin	149-156	bone morphogenetic protein 6	Mus musculus	171-175
32260841-8	2013	The sensing protocol was successfully applied to the determination of heparin in a HEPES buffer and in a buffer containing fetal bovine serum, for the concentration ranges of 0.30-5.35 U mL-1 and 0.67-4.33 U mL-1 respectively, which covers most part of therapeutic level.	Heparin	70-77	L1 cell adhesion molecule	Mus musculus	187-191
32260841-8	2013	The sensing protocol was successfully applied to the determination of heparin in a HEPES buffer and in a buffer containing fetal bovine serum, for the concentration ranges of 0.30-5.35 U mL-1 and 0.67-4.33 U mL-1 respectively, which covers most part of therapeutic level.	Heparin	70-77	L1 cell adhesion molecule	Mus musculus	208-212
23959669-2	2013	We aimed to compare the effect of unfractionated heparin (UFH) and enoxaparin used as anticoagulants during hemodialysis (HD) on circulating levels of heparin-binding, anti-angiogenic Endostatin, pro-inflammatory RANTES (Regulated upon Activation, Normal T cell Expressed and Secreted), and MCP-1 (Monocyte Chemoattractant Protein-1).	Heparin	49-56	collagen type XVIII alpha 1 chain	Homo sapiens	184-194
23959669-2	2013	We aimed to compare the effect of unfractionated heparin (UFH) and enoxaparin used as anticoagulants during hemodialysis (HD) on circulating levels of heparin-binding, anti-angiogenic Endostatin, pro-inflammatory RANTES (Regulated upon Activation, Normal T cell Expressed and Secreted), and MCP-1 (Monocyte Chemoattractant Protein-1).	Heparin	58-61	collagen type XVIII alpha 1 chain	Homo sapiens	184-194
23349855-4	2013	Among local growth factors known to be present at the time of implantation, heparin-binding epidermal growth factor-like growth factor (HB-EGF) triggered chemotaxis (directed locomotion), whereas platelet-derived growth factor (PDGF)-BB elicited both chemotaxis and chemokinesis (non-directed locomotion) of endometrial stromal cells.	Heparin	76-83	heparin binding EGF like growth factor	Homo sapiens	136-142
23578459-7	2013	The mutation of 13th base pair decreases the distance between AT and heparin.	Heparin	69-76	serpin family C member 1	Homo sapiens	62-64
23177153-6	2012	Through a 200 mum long heparin affinity column microfabricated inside a channel of 50 mum width and 20 mum height, the binding constant of each G-CSF-polysaccharide binding pair can be obtained within 1h, around one sixth of time needed by traditional capillary electrophoresis based method.	Heparin	23-30	colony stimulating factor 3	Homo sapiens	144-149
22824487-1	2012	Heparin is a glycosaminoglycan known to bind bone morphogenetic proteins (BMPs) and the growth and differentiation factors (GDFs) and has strong and variable effects on BMP osteogenic activity.	Heparin	0-7	bone morphogenetic protein 1	Homo sapiens	74-77
22824487-9	2012	Taken together, non-conserved amino acid residues in the N-terminus and residues protruding from the beta sheet (not overlapping with the receptor binding sites and the dimeric interface) and not C-terminal are found to be important for heparin-BMP interactions.	Heparin	237-244	bone morphogenetic protein 1	Homo sapiens	245-248
22862794-7	2012	RESULTS: We judged that samples of whole blood with 2K-EDTA were suitable for CD62P expression assay as functional assessments of platelet activity, because platelets treated with anticoagulants such as sodium citrate and heparin were extremely damaged after stimulation, and it was difficult to measure the CD62P expression by flow cytometry.	Heparin	222-229	selectin P	Homo sapiens	308-313
23355938-11	2012	The case illustrates the differential diagnosis of skin necrosis and limb gangrene in patients on warfarin and heparin, and also the clinical complexities that can occur in a FVL heterozygote.	Heparin	111-118	coagulation factor V	Homo sapiens	175-178
22672269-5	2012	HARP was shown to compete with both antithrombin and thrombin for binding to heparin and to OTR4120, respectively.	Heparin	77-84	serpin family C member 1	Homo sapiens	36-48
22963465-5	2012	Heparin mimetic nanofibers were shown to bind to vascular endothelial growth factor (VEGF) and direct endothelial cells to angiogenesis.	Heparin	0-7	vascular endothelial growth factor A	Rattus norvegicus	49-83
22963465-5	2012	Heparin mimetic nanofibers were shown to bind to vascular endothelial growth factor (VEGF) and direct endothelial cells to angiogenesis.	Heparin	0-7	vascular endothelial growth factor A	Rattus norvegicus	85-89
22963465-8	2012	We observed that heparin mimetic peptide nanofibers demonstrate better binding profiles to VEGF, hepatocyte growth factor (HGF), and fibroblast growth factor-2 (FGF-2) than control peptide nanofibers.	Heparin	17-24	vascular endothelial growth factor A	Rattus norvegicus	91-95
22963465-9	2012	We also identified that the heparin-binding domain of VEGF is critical for its interaction with these nanofibers.	Heparin	28-35	vascular endothelial growth factor A	Rattus norvegicus	54-58
22983394-6	2012	Treatment of the rabbits with the high dose of heparin also effectively improved the hemostatic parameters, ameliorated liver and renal injuries, and reduced the plasma level of TNF-alpha, and significantly reduced the mortality (33.3%).	Heparin	47-54	tumor necrosis factor	Oryctolagus cuniculus	178-187
22641607-0	2012	Polyurethane modified with an antithrombin-heparin complex via polyethylene oxide linker/spacers: influence of PEO molecular weight and PEO-ATH bond on catalytic and direct anticoagulant functions.	Heparin	43-50	serpin family C member 1	Homo sapiens	30-42
22641607-9	2012	On PEO-ATH surfaces fibrinogen adsorption was minimal while AT adsorption was high showing the selectivity of the heparin moiety of ATH for AT.	Heparin	114-121	serpin family C member 1	Homo sapiens	7-9
22641607-9	2012	On PEO-ATH surfaces fibrinogen adsorption was minimal while AT adsorption was high showing the selectivity of the heparin moiety of ATH for AT.	Heparin	114-121	serpin family C member 1	Homo sapiens	60-62
22912486-8	2012	Activation experiments reveal that short dsRNAs compete with 5"-triphosphate RNAs and heparin for activation, and likewise gel-shift assays reveal that activating 5"-triphosphate RNAs and heparin compete with short dsRNAs for binding to PKR"s dsRBD.	Heparin	188-195	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	237-240
22912486-9	2012	The dsRBD thus plays a critical role in the activation of PKR by ppp-ssRNA and even heparin.	Heparin	84-91	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	58-61
22759380-4	2012	In vitro maturation of cumulus oocyte complexes in the presence of exogenous heparin, which antagonizes HSPG signaling, prevented cumulus expansion and blocked the induction of cumulus-specific matrix genes, Has2 and Tnfaip6, whereas conversely, the mural granulosa-specific genes, Lhcgr and Cyp11a1, were strongly up-regulated.	Heparin	77-84	luteinizing hormone/choriogonadotropin receptor	Homo sapiens	282-287
23010571-9	2012	Affinity-chromatography demonstrated heparin-binding of ADAMTSL5 through its NTR-module.	Heparin	37-44	ADAMTS-like 5	Mus musculus	56-64
22820186-4	2012	The mechanisms for inactivation of LPL by ANGPTL4 was studied in THP-1 macrophages where active LPL is associated with cell surfaces in a heparin-releasable form, while LPL in the culture medium is mostly inactive.	Heparin	138-145	lipoprotein lipase	Homo sapiens	35-38
22820186-4	2012	The mechanisms for inactivation of LPL by ANGPTL4 was studied in THP-1 macrophages where active LPL is associated with cell surfaces in a heparin-releasable form, while LPL in the culture medium is mostly inactive.	Heparin	138-145	angiopoietin like 4	Homo sapiens	42-49
22820186-4	2012	The mechanisms for inactivation of LPL by ANGPTL4 was studied in THP-1 macrophages where active LPL is associated with cell surfaces in a heparin-releasable form, while LPL in the culture medium is mostly inactive.	Heparin	138-145	lipoprotein lipase	Homo sapiens	96-99
22820186-4	2012	The mechanisms for inactivation of LPL by ANGPTL4 was studied in THP-1 macrophages where active LPL is associated with cell surfaces in a heparin-releasable form, while LPL in the culture medium is mostly inactive.	Heparin	138-145	lipoprotein lipase	Homo sapiens	96-99
22820186-5	2012	The PPARdelta agonist GW501516 had no effect on LPL mRNA, but increased ANGPTL4 mRNA and caused a marked reduction of the heparin-releasable LPL activity concomitantly with accumulation of inactive, monomeric LPL in the medium.	Heparin	122-129	lipoprotein lipase	Homo sapiens	141-144
22820186-5	2012	The PPARdelta agonist GW501516 had no effect on LPL mRNA, but increased ANGPTL4 mRNA and caused a marked reduction of the heparin-releasable LPL activity concomitantly with accumulation of inactive, monomeric LPL in the medium.	Heparin	122-129	lipoprotein lipase	Homo sapiens	141-144
22820186-6	2012	Intracellular ANGPTL4 was monomeric, while dimers and tetramers of ANGPTL4 were present in the heparin-releasable fraction and medium.	Heparin	95-102	angiopoietin like 4	Homo sapiens	67-74
22504297-5	2012	Furthermore, rat embryonic fibroblasts (REFs) plated on fibronectin fragments lacking the heparin-binding domain that interacts with syndecan-4 showed much lower RhoA activation than that in cells plated on full-length fibronectin, indicating that RhoA is involved in syndecan-4-mediated cell adhesion signaling.	Heparin	90-97	fibronectin 1	Rattus norvegicus	56-67
22504297-5	2012	Furthermore, rat embryonic fibroblasts (REFs) plated on fibronectin fragments lacking the heparin-binding domain that interacts with syndecan-4 showed much lower RhoA activation than that in cells plated on full-length fibronectin, indicating that RhoA is involved in syndecan-4-mediated cell adhesion signaling.	Heparin	90-97	fibronectin 1	Rattus norvegicus	219-230
23022759-0	2012	Perioperative PAI-1 values in surgically treated colorectal carcinoma patients under low molecular weight heparin thromboprophylaxis.	Heparin	106-113	serpin family E member 1	Homo sapiens	14-19
22762190-5	2012	HBPs like lactoferrin (LF), fibronectin fragment (FNIII), semenogelinI (SGI) and prostate specific antigen (PSA) all bind heparin with different binding kinetics and affinities.	Heparin	122-129	kallikrein related peptidase 3	Homo sapiens	81-106
22762190-5	2012	HBPs like lactoferrin (LF), fibronectin fragment (FNIII), semenogelinI (SGI) and prostate specific antigen (PSA) all bind heparin with different binding kinetics and affinities.	Heparin	122-129	kallikrein related peptidase 3	Homo sapiens	108-111
22762190-6	2012	Kinetic data suggests that FNIII binds heparin with a high affinity (KD=3.2 nM), while PSA binds heparin with a micromolar affinity (KD=11.1 muM).	Heparin	97-104	kallikrein related peptidase 3	Homo sapiens	87-90
22762190-7	2012	Preincubation of SGI with heparin inhibits the binding of SGI to immobilized PSA in a dose-dependent manner, while FNIII incubated with heparin binds with an increased affinity to PSA.	Heparin	26-33	kallikrein related peptidase 3	Homo sapiens	77-80
22762190-7	2012	Preincubation of SGI with heparin inhibits the binding of SGI to immobilized PSA in a dose-dependent manner, while FNIII incubated with heparin binds with an increased affinity to PSA.	Heparin	136-143	kallikrein related peptidase 3	Homo sapiens	180-183
22618708-0	2012	Crystal structures of protease nexin-1 in complex with heparin and thrombin suggest a 2-step recognition mechanism.	Heparin	55-62	serpin family E member 2	Homo sapiens	22-38
22516065-3	2012	Coinjection of low doses of morpholinos for beta-neurexin 1a and neuroligin 1 together or in combination with morpholinos targeting the -heparin--binding isoforms of vascular endothelial growth factor A (encoded by the VEGFAb gene) recapitulates the observed abnormalities, suggesting synergistic activity of these molecules.	Heparin	137-144	vascular endothelial growth factor Aa	Danio rerio	166-202
22888520-0	2012	Preparation, characterization and anti-angiogenesis activity of endostatin covalently modified by polysulfated heparin.	Heparin	111-118	collagen type XVIII alpha 1 chain	Homo sapiens	64-74
22669117-0	2012	Roles of vimentin and 14-3-3 zeta/delta in the inhibitory effects of heparin on PC-3M cell proliferation and B16-F10-luc-G5 cells metastasis.	Heparin	69-76	vimentin	Homo sapiens	9-33
22669117-18	2012	Heparin 125 mug/mL decreased vimentin and E-cadherin mRNA transcription while increased TGF-beta mRNA transcription in the PC-3M cells, but the differences were not significant.	Heparin	0-7	vimentin	Homo sapiens	29-37
22488107-4	2012	A proof-of-principle study established that doses of heparin lower than what are used for anticoagulation but sufficient to block P-selectin improved microvascular blood flow inpatients with SCD.	Heparin	53-60	selectin P	Homo sapiens	130-140
22522458-5	2012	We subsequently showed how heparin and a high-molecular-weight Escherichia coli K5-derived heparin-like polysaccharide (K5-NSOS) inhibited TGF-beta-induced IL-11 production in MDA-MB-231(SA) cells.	Heparin	27-34	interleukin 11	Homo sapiens	156-161
22522458-5	2012	We subsequently showed how heparin and a high-molecular-weight Escherichia coli K5-derived heparin-like polysaccharide (K5-NSOS) inhibited TGF-beta-induced IL-11 production in MDA-MB-231(SA) cells.	Heparin	91-98	interleukin 11	Homo sapiens	156-161
22155502-8	2012	Although both approaches resulted in a phenotype consistent with CD56(bright) stage IV NK cells, heparin-based cultures favored the development of CD56(+)CD16(+) cells, whereas stroma produced more NK cell immunoglobulin-like receptor-expressing NK cells, both of which are markers of terminal maturation.	Heparin	97-104	neural cell adhesion molecule 1	Homo sapiens	147-151
22467748-6	2012	De novo expression of heparin-binding epidermal growth factor-like growth factor (HB-EGF) in glomerular epithelial cells is found specifically in human glomerulonephritis with proliferation of these cells and dedifferentiation of podocytes.	Heparin	22-29	epidermal growth factor	Homo sapiens	38-61
22467748-6	2012	De novo expression of heparin-binding epidermal growth factor-like growth factor (HB-EGF) in glomerular epithelial cells is found specifically in human glomerulonephritis with proliferation of these cells and dedifferentiation of podocytes.	Heparin	22-29	heparin binding EGF like growth factor	Homo sapiens	82-88
22035631-6	2012	RESULTS: We found that heparin significantly improved LPS-induced lung pathological changes, inhibited myeloperoxidase (MPO) activity, and reduced malondialdehyde (MDA) level and lung wet/dry weight ratio.	Heparin	23-30	myeloperoxidase	Rattus norvegicus	103-118
22035631-6	2012	RESULTS: We found that heparin significantly improved LPS-induced lung pathological changes, inhibited myeloperoxidase (MPO) activity, and reduced malondialdehyde (MDA) level and lung wet/dry weight ratio.	Heparin	23-30	myeloperoxidase	Rattus norvegicus	120-123
22035631-8	2012	Additionally, heparin decreased the expression of transforming growth factor-beta1 (TGF-beta1), p-Smad 2, and p-Smad 3, which are all important molecules of the TGF-beta1/Smad signaling pathway.	Heparin	14-21	SMAD family member 2	Rattus norvegicus	98-104
22315264-3	2012	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes.	Heparin	0-3	serpin family C member 1	Homo sapiens	66-78
22214372-1	2012	OBJECTIVE: The aims of this study were to examine the effects of prophylactic heparin treatment during taurocholate-induced pancreatitis in rats and its impact on serum VEGF levels and local VEGF contents within the pancreas.	Heparin	78-85	vascular endothelial growth factor A	Rattus norvegicus	169-173
22214372-1	2012	OBJECTIVE: The aims of this study were to examine the effects of prophylactic heparin treatment during taurocholate-induced pancreatitis in rats and its impact on serum VEGF levels and local VEGF contents within the pancreas.	Heparin	78-85	vascular endothelial growth factor A	Rattus norvegicus	191-195
22214372-9	2012	Prophylactic heparin treatment significantly improved the morphologic changes, myeloperoxidase (MPO), TNF-alpha and malondialdehyde (MDA) activities.	Heparin	13-20	myeloperoxidase	Rattus norvegicus	79-94
22214372-9	2012	Prophylactic heparin treatment significantly improved the morphologic changes, myeloperoxidase (MPO), TNF-alpha and malondialdehyde (MDA) activities.	Heparin	13-20	myeloperoxidase	Rattus norvegicus	96-99
22466566-1	2012	Natural cytotoxicity receptor 2 (NCR2 or natural killer (NK)p44) and NCR3 (NKp30) bind to heparin and heparin sulfate; however, other natural ligands have yet to be identified.	Heparin	90-97	natural cytotoxicity triggering receptor 3	Homo sapiens	69-73
22466566-1	2012	Natural cytotoxicity receptor 2 (NCR2 or natural killer (NK)p44) and NCR3 (NKp30) bind to heparin and heparin sulfate; however, other natural ligands have yet to be identified.	Heparin	90-97	natural cytotoxicity triggering receptor 3	Homo sapiens	75-80
22382418-2	2012	Low-molecular-weight (LMW) heparin mimetics that potentiate antithrombin III (AT) action are also valuable as anti-thrombotics.	Heparin	27-34	serpin family C member 1	Homo sapiens	60-76
22482044-4	2012	A recombinant soluble form of thrombomodulin has been approved to treat patients suffering from disseminated intravascular coagulation (DIC) and has thus far shown greater therapeutic potential than heparin.	Heparin	199-206	thrombomodulin	Homo sapiens	30-44
22088204-1	2012	OBJECTIVE: To evaluate the effects of low-molecular-weight heparins (LMWHs) on decidual heparin-binding epidermal growth factor-like growth factor (HB-EGF) expression/secretion and on TNF-alpha-induced decidual apoptosis.	Heparin	59-67	heparin binding EGF like growth factor	Homo sapiens	148-154
22566220-1	2012	The molecular basis for the anticoagulant action of heparin lies in its ability to bind to and enhance the inhibitory activity of the plasma protein antithrombin against several serine proteases of the coagulation system, most importantly factors IIa (thrombin), Xa and IXa.	Heparin	52-59	serpin family C member 1	Homo sapiens	149-161
22566220-2	2012	Two major mechanisms underlie heparin"s potentiation of antithrombin.	Heparin	30-37	serpin family C member 1	Homo sapiens	56-68
22566220-3	2012	The conformational changes induced by heparin binding cause both expulsion of the reactive loop and exposure of exosites of the surface of antithrombin, which bind directly to the enzyme target; and a template mechanism exists in which both inhibitor and enzyme bind to the same heparin molecule.	Heparin	38-45	serpin family C member 1	Homo sapiens	139-151
22566220-3	2012	The conformational changes induced by heparin binding cause both expulsion of the reactive loop and exposure of exosites of the surface of antithrombin, which bind directly to the enzyme target; and a template mechanism exists in which both inhibitor and enzyme bind to the same heparin molecule.	Heparin	279-286	serpin family C member 1	Homo sapiens	139-151
22566226-2	2012	Heparin exerts its antithrombotic effects by facilitating the ability of antithrombin (AT), a plasma serum protease inhibitor, to inhibit thrombin (factor IIa) and factor Xa.	Heparin	0-7	serpin family C member 1	Homo sapiens	73-85
22566226-2	2012	Heparin exerts its antithrombotic effects by facilitating the ability of antithrombin (AT), a plasma serum protease inhibitor, to inhibit thrombin (factor IIa) and factor Xa.	Heparin	0-7	serpin family C member 1	Homo sapiens	87-89
22566227-3	2012	Nonbleeding complications of heparins are caused by binding of heparin molecules to proteins other than antithrombin and to cells, which is generally more pronounced with unfractionated heparin than with low-molecular-weight heparins.	Heparin	29-37	serpin family C member 1	Homo sapiens	104-116
21997473-5	2012	We were interested in studying the C-terminal heparin-binding region of FN since it mediates aggrecan and type II collagen breakdown in cartilage, but the specific FN domains responsible for proteolytic enzyme activity and their receptors in cartilage are unknown.	Heparin	46-53	fibronectin 1	Mus musculus	72-74
21997473-7	2012	We found that the FN III 13-14 domains in the C-terminal heparin-binding region of FN are potent inducers of aggrecanase activity in articular cartilage.	Heparin	57-64	fibronectin 1	Mus musculus	18-20
22252637-1	2012	Serglycin is a proteoglycan composed of a relatively small (~17 kDa) core protein to which sulfated glycosaminoglycans of either heparin, heparan sulfate or chondroitin sulfate types are attached.	Heparin	129-136	serglycin	Mus musculus	0-9
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	130-136
21984036-9	2012	When cells were pretreated with both heparin and DMTU, there was a further reduction in ROS content, the mRNA of Duox1, EGFR, and MUC5AC as well as the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with either the PMA group, heparin group, or DMTU group (all P &lt; 0.01).	Heparin	37-44	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	195-201
22235321-4	2012	beta2GPI can be recognized by aPL that, once bound, interfere with both trophoblast functions and with the HEEC differentiation.APS patients can be successfully treated with Low Molecular Weight Heparin (LMWH).	Heparin	195-202	apolipoprotein H	Homo sapiens	0-8
21914461-7	2011	Angiotensin II and LPA induced EGF receptor transactivation as evidenced by Akt/PKB phosphorylation through metalloproteinase-catalyzed membrane shedding of heparin-binding EGF and autocrine/paracrine activation of EGF receptors.	Heparin	157-164	epidermal growth factor	Homo sapiens	31-34
21682942-6	2011	We treated C2C12 cells with LMWF and/or heparin during MyoD.	Heparin	40-47	myogenic differentiation 1	Mus musculus	55-59
21682942-10	2011	Heparin was used as a positive control because it has been reported to activate MyoD.	Heparin	0-7	myogenic differentiation 1	Mus musculus	80-84
21851968-13	2011	4) The UFH-pretreated group exhibited significantly lower levels of ALT and CRE at 6h.	Heparin	7-10	glutamic pyruvic transaminase, soluble	Mus musculus	68-71
22012070-5	2011	In this assay, direct factor Xa (FXa) inhibitors such as edoxaban and antithrombin (AT)-dependent anticoagulants such as heparin did not increase, but simply suppressed TG.	Heparin	121-128	serpin family C member 1	Homo sapiens	70-82
21978664-8	2011	Analytical ultracentrifugation measurements support a thermodynamic linkage model where heparin binding allosterically enhances PKR dimerization, thereby activating the kinase.	Heparin	88-95	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	128-131
22105014-19	2011	In this report, we will demonstrate the endocytic activity of SECs in the intact organ using radio-labeled heparin for hyaluronan for the SEC-specific Stabilin-2 receptor.	Heparin	107-114	stabilin 2	Homo sapiens	151-161
21931955-8	2011	The binding affinities of these heparins to antithrombin III and thrombin were evaluated by using a surface plasmon resonance competitive binding assay.	Heparin	32-40	serpin family C member 1	Homo sapiens	44-60
21771212-2	2011	This in vitro study was conducted to assess the manner in which heparin-binding epidermal growth factor-like growth factor (HB-EGF) and epiregulin cooperatively participate in the wound-healing process in the gingival epithelial and fibroblast cells of the oral mucosa.	Heparin	64-71	heparin binding EGF like growth factor	Homo sapiens	124-130
21744268-0	2011	Synthetic peptide fragment (65-76) of monocyte chemotactic protein-1 (MCP-1) inhibits MCP-1 binding to heparin and possesses anti-inflammatory activity in stable angina patients after coronary stenting.	Heparin	103-110	C-C motif chemokine ligand 2	Homo sapiens	38-68
21744268-0	2011	Synthetic peptide fragment (65-76) of monocyte chemotactic protein-1 (MCP-1) inhibits MCP-1 binding to heparin and possesses anti-inflammatory activity in stable angina patients after coronary stenting.	Heparin	103-110	C-C motif chemokine ligand 2	Homo sapiens	70-75
21744268-0	2011	Synthetic peptide fragment (65-76) of monocyte chemotactic protein-1 (MCP-1) inhibits MCP-1 binding to heparin and possesses anti-inflammatory activity in stable angina patients after coronary stenting.	Heparin	103-110	C-C motif chemokine ligand 2	Homo sapiens	86-91
21723287-6	2011	After enterokinase digestion and heparin affinity chromatography, high yields of enzymatic and biologically active human grB were obtained.	Heparin	33-40	granzyme B	Homo sapiens	121-124
24196373-1	2014	Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE).	Heparin	78-85	serpin family C member 1	Homo sapiens	17-29
24196373-1	2014	Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE).	Heparin	78-85	serpin family C member 1	Homo sapiens	31-33
24196373-1	2014	Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE).	Heparin	78-85	serpin family C member 1	Homo sapiens	67-69
24627861-2	2014	Heparin resistance was defined as at least one activated clothing time &lt;400 seconds after heparinization and/or the need for purified antithrombin III (AT-III) administration.	Heparin	0-7	serpin family C member 1	Homo sapiens	137-153
24627861-2	2014	Heparin resistance was defined as at least one activated clothing time &lt;400 seconds after heparinization and/or the need for purified antithrombin III (AT-III) administration.	Heparin	0-7	serpin family C member 1	Homo sapiens	155-161
24296776-0	2014	Antithrombin III supplementation on extracorporeal membrane oxygenation: impact on heparin dose and circuit life.	Heparin	83-90	serpin family C member 1	Homo sapiens	0-16
24296776-3	2014	We hypothesized that ATIII supplementation would reduce heparin infusion rates, increase unfractionated heparin anti-Xa levels, and prolong ECMO circuit life.	Heparin	56-63	serpin family C member 1	Homo sapiens	21-26
24296776-3	2014	We hypothesized that ATIII supplementation would reduce heparin infusion rates, increase unfractionated heparin anti-Xa levels, and prolong ECMO circuit life.	Heparin	104-111	serpin family C member 1	Homo sapiens	21-26
24296776-6	2014	The primary outcome was whether the heparin infusion rate was reduced by 10% or more as a result of ATIII administration.	Heparin	36-43	serpin family C member 1	Homo sapiens	100-105
25036482-6	2014	These results indicate that heparin increases the activity and stability of MMP-7, while CS decreases them.	Heparin	28-35	matrix metallopeptidase 7	Homo sapiens	76-81
24266905-0	2014	Early heparin administration attenuates tissue factor-mediated thrombin generation during simulated cardiopulmonary bypass.	Heparin	6-13	coagulation factor III, tissue factor	Homo sapiens	40-53
24266905-1	2014	BACKGROUND: We tested the hypothesis that heparin administration prior to the emergence of tissue factor (TF) would increase plasma TF pathway inhibitor (TFPI) and attenuate TF-mediated thrombin generation during simulated cardiopulmonary bypass (CPB).	Heparin	42-49	coagulation factor III, tissue factor	Homo sapiens	106-108
24266905-1	2014	BACKGROUND: We tested the hypothesis that heparin administration prior to the emergence of tissue factor (TF) would increase plasma TF pathway inhibitor (TFPI) and attenuate TF-mediated thrombin generation during simulated cardiopulmonary bypass (CPB).	Heparin	42-49	coagulation factor III, tissue factor	Homo sapiens	132-134
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	serpin family C member 1	Homo sapiens	57-69
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	serpin family C member 1	Homo sapiens	156-168
24266905-10	2014	CONCLUSIONS: Heparin-induced TFPI elevation attenuates TF-mediated thrombin generation.	Heparin	13-20	coagulation factor III, tissue factor	Homo sapiens	29-31
23510717-1	2013	The heparin sulfate proteoglycan Terribly Reduced Optic Lobes (Trol) is the Drosophila melanogaster homolog of the vertebrate protein Perlecan.	Heparin	4-11	terribly reduced optic lobes	Drosophila melanogaster	63-67
23510717-1	2013	The heparin sulfate proteoglycan Terribly Reduced Optic Lobes (Trol) is the Drosophila melanogaster homolog of the vertebrate protein Perlecan.	Heparin	4-11	terribly reduced optic lobes	Drosophila melanogaster	134-142
24048327-3	2013	We have developed a covalent conjugate of antithrombin (AT) and heparin (ATH) with superior anticoagulant properties compared with UFH.	Heparin	131-134	serpin family C member 1	Homo sapiens	42-54
24220340-3	2013	This resulted in higher levels of LPL activity both on cell surfaces (heparin-releasable) and in the medium, while LPL activity within the cells remained unaffected.	Heparin	70-77	lipoprotein lipase	Homo sapiens	34-37
32261185-9	2013	In contrast, addition of 65 pg mL-1 heparin into aggregated FA-AuNPs enhanced their emission intensity at 780 nm in the presence of 1040-fold higher concentrations of the above-mentioned interferences.	Heparin	36-43	L1 cell adhesion molecule	Mus musculus	31-35
32261185-11	2013	The lowest detection limits were found to be 4.8 x 10-15 g mL-1 for protamine and 12.6 x 10-15 g mL-1 for heparin (S/N = 3).	Heparin	106-113	L1 cell adhesion molecule	Mus musculus	97-101
23942551-10	2013	These data indicate a role for Src in a high glucose-Src-TACE-heparin-binding epidermal growth factor-EGFR-MAPK-signaling pathway to collagen accumulation.	Heparin	62-69	Rous sarcoma oncogene	Mus musculus	31-34
23942551-10	2013	These data indicate a role for Src in a high glucose-Src-TACE-heparin-binding epidermal growth factor-EGFR-MAPK-signaling pathway to collagen accumulation.	Heparin	62-69	Rous sarcoma oncogene	Mus musculus	53-56
23942551-10	2013	These data indicate a role for Src in a high glucose-Src-TACE-heparin-binding epidermal growth factor-EGFR-MAPK-signaling pathway to collagen accumulation.	Heparin	62-69	epidermal growth factor receptor	Mus musculus	102-106
23856814-9	2013	This data showed that a certain lipoprotein that includes apolipoprotein A-I might precipitate with canine LDL when using heparin manganese chloride solution.	Heparin	122-129	apolipoprotein A1	Canis lupus familiaris	58-76
24009013-0	2013	Cyr61 is a target for heparin in reducing MV3 melanoma cell adhesion and migration via the integrin VLA-4.	Heparin	22-29	cellular communication network factor 1	Homo sapiens	0-5
24009013-2	2013	We could recently show that heparin can block VLA-4 binding, which contributes, next to blocking P- and L-selectin, to the understanding of antimetastatic activities of heparin.	Heparin	28-35	selectin L	Homo sapiens	104-114
24009013-2	2013	We could recently show that heparin can block VLA-4 binding, which contributes, next to blocking P- and L-selectin, to the understanding of antimetastatic activities of heparin.	Heparin	169-176	selectin L	Homo sapiens	104-114
24009013-6	2013	Since Cyr61 possesses heparin binding capabilities, Cyr61 can be supposed as potential target for heparin to indirectly interfere with integrin functions.	Heparin	22-29	cellular communication network factor 1	Homo sapiens	6-11
24009013-6	2013	Since Cyr61 possesses heparin binding capabilities, Cyr61 can be supposed as potential target for heparin to indirectly interfere with integrin functions.	Heparin	22-29	cellular communication network factor 1	Homo sapiens	52-57
24009013-6	2013	Since Cyr61 possesses heparin binding capabilities, Cyr61 can be supposed as potential target for heparin to indirectly interfere with integrin functions.	Heparin	98-105	cellular communication network factor 1	Homo sapiens	6-11
24009013-6	2013	Since Cyr61 possesses heparin binding capabilities, Cyr61 can be supposed as potential target for heparin to indirectly interfere with integrin functions.	Heparin	98-105	cellular communication network factor 1	Homo sapiens	52-57
24009013-7	2013	The present in vitro studies address (i) the existence of a Cyr61/VLA-4 axis and (ii) the functional relevance of heparin interference via Cyr61.	Heparin	114-121	cellular communication network factor 1	Homo sapiens	139-144
24009013-11	2013	The low-molecular-weight heparin tinzaparin, but not the pentasaccharide fondaparinux, binds module IV of Cyr61 with micromolar affinity.	Heparin	25-32	cellular communication network factor 1	Homo sapiens	106-111
24009013-12	2013	But tinzaparin cannot interfere with Cyr61 accumulation onto syndecan-4, indicating different Cyr61 binding sites for heparin and other GAGs.	Heparin	118-125	cellular communication network factor 1	Homo sapiens	94-99
24033133-3	2013	In contrast, tau amyloids formed with heparin as an inducing agent-a common biochemical model of tau misfolding-are structurally distinct from brain-derived PHFs.	Heparin	38-45	microtubule associated protein tau	Homo sapiens	13-16
24033133-3	2013	In contrast, tau amyloids formed with heparin as an inducing agent-a common biochemical model of tau misfolding-are structurally distinct from brain-derived PHFs.	Heparin	38-45	microtubule associated protein tau	Homo sapiens	97-100
24033133-5	2013	Tau fibrils produced by incubating recombinant tau with heparin had significantly narrower fibrils with a longer periodicity, higher chemical stability, and distinct secondary structure compared to AD PHFs.	Heparin	56-63	microtubule associated protein tau	Homo sapiens	0-3
24033133-5	2013	Tau fibrils produced by incubating recombinant tau with heparin had significantly narrower fibrils with a longer periodicity, higher chemical stability, and distinct secondary structure compared to AD PHFs.	Heparin	56-63	microtubule associated protein tau	Homo sapiens	47-50
24033133-6	2013	The addition of heparin to the reaction of recombinant tau and AD PHFs also corrupted the templating process, resulting in a mixture of fibril conformations.	Heparin	16-23	microtubule associated protein tau	Homo sapiens	55-58
24273488-7	2013	CONCLUSION: Heparin can significantly enhance the stimulating effects of a combination of TPO, SCF, FL, IL-6, and IL-11 supplemented with autologous serum on CFU-MK, MK, and platelet production from CB CD34+ cells.	Heparin	12-19	interleukin 11	Homo sapiens	114-119
23843463-1	2013	The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)).	Heparin	44-51	serpin family C member 1	Homo sapiens	4-16
23843463-1	2013	The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)).	Heparin	77-85	serpin family C member 1	Homo sapiens	4-16
23897813-8	2013	Our data identify CD82 as a new regulator of c-Cbl, which discriminatively controls the activity of this E3 ubiquitin ligase toward heparin-binding ligand-EGFR pairs.	Heparin	132-139	Cbl proto-oncogene	Homo sapiens	45-50
23475997-2	2013	Recently, we identified a PDI from Chlamydomonas reinhardtii (CrPDI2) by a mass spectrometry approach that is specifically enriched by heparin affinity chromatography in samples taken during the night phase.	Heparin	135-142	uncharacterized protein	Chlamydomonas reinhardtii	62-68
23475997-5	2013	By immunoblots, we confirm a high-amplitude change in abundance of the heparin-bound CrPDI2 during subjective night.	Heparin	71-78	uncharacterized protein	Chlamydomonas reinhardtii	85-91
23903049-14	2013	In conclusion, in antithrombin deficiency the use of low-molecular-weight heparin in pregnancy and puerperium with antithrombin concentrate pre-delivery was associated with successful pregnancy outcome; rates of VTE appear to be lower than previously reported, but remain elevated.	Heparin	74-81	serpin family C member 1	Homo sapiens	18-30
23903049-14	2013	In conclusion, in antithrombin deficiency the use of low-molecular-weight heparin in pregnancy and puerperium with antithrombin concentrate pre-delivery was associated with successful pregnancy outcome; rates of VTE appear to be lower than previously reported, but remain elevated.	Heparin	74-81	serpin family C member 1	Homo sapiens	115-127
2482548-11	1989	Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups.	Heparin	40-47	alpha-2-macroglobulin	Homo sapiens	111-119
2482548-11	1989	Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups.	Heparin	40-47	serpin family C member 1	Homo sapiens	222-227
23824188-9	2013	The recombinant protein expressed in Escherichia coli showed epimerization activity toward substrates generated from heparin and the E. coli K5 capsular polysaccharide, thereby providing the first evidence for bacterial D-glucuronyl C5-epimerase activity.	Heparin	117-124	glucuronic acid epimerase	Homo sapiens	220-245
2692853-2	1989	This protein (RBP1) has been partially purified by means of heparin-agarose chromatography and protects 20 bp in the rDNA enhancer, and 25 bp in the initiation region, against DNase I in an in vitro footprinting assay.	Heparin	60-67	Sgn1p	Saccharomyces cerevisiae S288C	14-18
23752481-1	2013	We presented a homogeneous heparin-mediated fluorescence anisotropy (FA) assay of antithrombin (AT) based on long-lived luminescent polyethyleneimine capped Mn-doped ZnS (PEI-Mn-ZnS) QDs.	Heparin	27-34	serpin family C member 1	Homo sapiens	82-94
2592856-1	1989	Inhibition of thrombin by heparin is mediated by at least two plasma proteins, antithrombin III, and heparin cofactor II.	Heparin	26-33	serpin family C member 1	Homo sapiens	79-95
25206517-5	2013	Hb9 and choline acetyltransferase expression was high following inductive with heparin combined with basic fibroblast growth factor.	Heparin	79-86	motor neuron and pancreas homeobox 1	Homo sapiens	0-3
2609289-0	1989	Identification and characterisation of an antithrombin III mutant (AT Dublin 2) with marginally decreased heparin reactivity.	Heparin	106-113	serpin family C member 1	Homo sapiens	42-58
23773695-6	2013	RESULTS: Serum and plasma anticoagulated with citrate or heparin had equivalent ADAMTS13 activity with FRETS-rVWF71.	Heparin	57-64	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	80-88
2609289-6	1989	Mutant plasma ATIII showed reduced thrombin reactivity at low concentrations of thrombin and demonstrated decreased reactivity with heparin over a range of heparin concentrations.	Heparin	132-139	serpin family C member 1	Homo sapiens	14-19
2609289-6	1989	Mutant plasma ATIII showed reduced thrombin reactivity at low concentrations of thrombin and demonstrated decreased reactivity with heparin over a range of heparin concentrations.	Heparin	156-163	serpin family C member 1	Homo sapiens	14-19
2609289-7	1989	This was confirmed using a modified ATIII heparin cofactor activity assay with varying heparin concentrations.	Heparin	42-49	serpin family C member 1	Homo sapiens	36-41
23720451-4	2013	Flow experiments with VWF deletion mutants and heparin indicate a contribution of the A-type domains of VWF to bacterial binding.	Heparin	47-54	Von Willebrand factor	Mus musculus	104-107
23917140-2	2013	As perioperative anticoagulation, AT III was administered to have its activity&gt;=70% in addition to heparin.	Heparin	102-109	serpin family C member 1	Homo sapiens	34-40
2609289-8	1989	The abnormal ATIII was also found to elute from heparin agarose at a lower ionic strength than normal ATIII.	Heparin	48-55	serpin family C member 1	Homo sapiens	13-18
2632043-9	1989	ATIII antigenicity was altered in the presence of both heparin and TP but not in the presence of TP alone.	Heparin	55-62	serpin family C member 1	Homo sapiens	0-5
23530033-1	2013	The hyaluronan (HA) receptor for endocytosis (HARE; Stabilin-2) binds and clears 14 different ligands, including HA and heparin, via clathrin-mediated endocytosis.	Heparin	120-127	stabilin 2	Homo sapiens	46-50
2688761-2	1989	The anticoagulant heparin greatly accelerates the rate of inactivation of proteinases by antithrombin, predominantly through its well defined, highly specific binding reaction with the inhibitor, but also through a less strictly defined interaction with some of the proteinases (such as thrombin).	Heparin	18-25	serpin family C member 1	Homo sapiens	89-101
23530033-1	2013	The hyaluronan (HA) receptor for endocytosis (HARE; Stabilin-2) binds and clears 14 different ligands, including HA and heparin, via clathrin-mediated endocytosis.	Heparin	120-127	stabilin 2	Homo sapiens	52-62
23357641-4	2013	Nephronectin bound strongly to heparin and chondroitin sulfate (CS)-E and moderately to heparan sulfate (HS), but failed to bind to CS-A, CS-C, CS-D, dermatan sulfate and hyaluronic acid.	Heparin	31-38	nephronectin	Mus musculus	0-12
23357641-5	2013	Deletion of the MAM domain severely impaired the binding of nephronectin to heparin but not CS-E, whereas deletion of the EGF-like repeats reduced its binding to CS-E but not heparin, suggesting that nephronectin interacts with CS-E and heparin through the EGF-like repeats and MAM domain, respectively.	Heparin	76-83	nephronectin	Mus musculus	60-72
2806479-8	1989	Antithrombin III and fibronectin inhibited platelet response to heparin, suggesting that these proteins may protect platelets from aggregation by heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	0-16
23314760-10	2013	AEPO, but not EPO, expressed heparin affinity in vitro.	Heparin	29-36	erythropoietin	Mus musculus	1-4
21726720-0	2011	Electrochemical impedance spectroscopy as a highly sensitive tool for a dynamic interaction study between heparin and antithrombin: a novel antithrombin sensor.	Heparin	106-113	serpin family C member 1	Homo sapiens	140-152
2621705-6	1989	Heparin binding to the membranes was abolished by a 1-h pretreatment with chymotrypsin, plasmin, pronase or trypsin.	Heparin	0-7	plasminogen	Bos taurus	88-95
21720642-2	2011	We hypothesized that chemically well-defined cell culture substrates could be used to study the influence of sequestered heparin on human mesenchymal stem cell (hMSC) behavior.	Heparin	121-128	musculin	Homo sapiens	161-165
21720642-5	2011	These heparin-sequestering SAMs enhance hMSC proliferation by amplifying endogenous fibroblast growth factor (FGF) signaling, and enhance hMSC osteogenic differentiation by amplifying endogenous bone morphogenetic protein (BMP) signaling.	Heparin	6-13	musculin	Homo sapiens	40-44
21720642-5	2011	These heparin-sequestering SAMs enhance hMSC proliferation by amplifying endogenous fibroblast growth factor (FGF) signaling, and enhance hMSC osteogenic differentiation by amplifying endogenous bone morphogenetic protein (BMP) signaling.	Heparin	6-13	musculin	Homo sapiens	138-142
21720642-5	2011	These heparin-sequestering SAMs enhance hMSC proliferation by amplifying endogenous fibroblast growth factor (FGF) signaling, and enhance hMSC osteogenic differentiation by amplifying endogenous bone morphogenetic protein (BMP) signaling.	Heparin	6-13	bone morphogenetic protein 1	Homo sapiens	195-221
23263338-9	2013	AT was inversely correlated with ACT (r = -0.33), even after adjusting for heparin dose, and positively correlated with antifactor Xa (r = 0.57).	Heparin	75-82	serpin family C member 1	Homo sapiens	0-2
23263338-11	2013	ACT is poorly correlated with antifactor Xa and AT modifies the relationship between ACT and the heparin dose, indicating that results should be interpreted with caution when managing anticoagulation on ECMO.	Heparin	97-104	serpin family C member 1	Homo sapiens	48-50
21720642-5	2011	These heparin-sequestering SAMs enhance hMSC proliferation by amplifying endogenous fibroblast growth factor (FGF) signaling, and enhance hMSC osteogenic differentiation by amplifying endogenous bone morphogenetic protein (BMP) signaling.	Heparin	6-13	bone morphogenetic protein 1	Homo sapiens	223-226
2598315-3	1989	The HA-heparin-catalyzed thrombin/AT III reaction was faster in the presence of 0.1 M NaCl at pH 6.05 than that in the absence of the salt.	Heparin	7-14	serpin family C member 1	Homo sapiens	34-40
2598315-6	1989	Thus, it appears that AT III tends to form a ternary complex with the thrombin-DS or thrombin-LA-heparin complex, even in the presence of 0.1 M NaCl, whereas factor Xa reacts with the AT III-DS or AT III-LA-heparin complex.	Heparin	97-104	serpin family C member 1	Homo sapiens	22-28
2598315-6	1989	Thus, it appears that AT III tends to form a ternary complex with the thrombin-DS or thrombin-LA-heparin complex, even in the presence of 0.1 M NaCl, whereas factor Xa reacts with the AT III-DS or AT III-LA-heparin complex.	Heparin	207-214	serpin family C member 1	Homo sapiens	22-28
23100269-0	2013	Inhibition of the prothrombinase complex on red blood cells by heparin and covalent antithrombin-heparin complex.	Heparin	97-104	serpin family C member 1	Homo sapiens	84-96
21793788-9	2011	At 1 dyn/cm(2) shear stress, 60 nM of P-selectin aptamer had antiadhesion activity similar to heparin, a known inhibitor of SS-RBC adhesion to P-selectin.	Heparin	94-101	selectin P	Homo sapiens	38-48
2598315-7	1989	These results indicate that HA-heparin is the only substance having the ability to catalyze the thrombin/AT III reaction, and that its turnover rate is markedly elevated in the presence of strongly electropositive and electronegative ions because of the decreased affinity of the enzyme for heparin under such conditions.	Heparin	31-38	serpin family C member 1	Homo sapiens	105-111
23100269-4	2013	Therefore, this study examines the ability of heparin and a covalent antithrombin-heparin complex (ATH) to inhibit the RBC-prothrombinase system.	Heparin	82-89	serpin family C member 1	Homo sapiens	69-81
2598315-7	1989	These results indicate that HA-heparin is the only substance having the ability to catalyze the thrombin/AT III reaction, and that its turnover rate is markedly elevated in the presence of strongly electropositive and electronegative ions because of the decreased affinity of the enzyme for heparin under such conditions.	Heparin	291-298	serpin family C member 1	Homo sapiens	105-111
2501315-1	1989	Secretion of urokinase-type plasminogen activator (uPA) by RAW264.7 cells was stimulated by heparin in a dose- and time-dependent manner.	Heparin	92-99	plasminogen activator, urokinase	Mus musculus	13-49
22999468-6	2012	In our bilayer hydrogel construct, the top layer contains heparin (HP)-decorated, HA-based hydrogel particles (HGPs) capable of releasing heparin-binding epidermal growth factor-like growth factor (HB-EGF) in a sustained manner at a rate of 2.5 wt%/day cumulatively.	Heparin	58-65	heparin binding EGF like growth factor	Homo sapiens	198-204
22999468-6	2012	In our bilayer hydrogel construct, the top layer contains heparin (HP)-decorated, HA-based hydrogel particles (HGPs) capable of releasing heparin-binding epidermal growth factor-like growth factor (HB-EGF) in a sustained manner at a rate of 2.5 wt%/day cumulatively.	Heparin	67-69	heparin binding EGF like growth factor	Homo sapiens	198-204
22999468-6	2012	In our bilayer hydrogel construct, the top layer contains heparin (HP)-decorated, HA-based hydrogel particles (HGPs) capable of releasing heparin-binding epidermal growth factor-like growth factor (HB-EGF) in a sustained manner at a rate of 2.5 wt%/day cumulatively.	Heparin	138-145	heparin binding EGF like growth factor	Homo sapiens	198-204
23010574-0	2012	Potentiation of anti-angiogenic activity of heparin by blocking the ATIII-interacting pentasaccharide unit and increasing net anionic charge.	Heparin	44-51	serpin family C member 1	Homo sapiens	68-73
22670863-3	2012	Heparin needs to be added as anticoagulant before addition of HPL to culture medium; otherwise, HPL-medium forms a gel within 1 h. Here, we demonstrated that such HPL-gels provide a suitable 3D-matrix for cell culture that-apart from heparin-consists of the same components as the over-layered culture medium.	Heparin	234-241	galectin 1	Homo sapiens	96-99
22670863-3	2012	Heparin needs to be added as anticoagulant before addition of HPL to culture medium; otherwise, HPL-medium forms a gel within 1 h. Here, we demonstrated that such HPL-gels provide a suitable 3D-matrix for cell culture that-apart from heparin-consists of the same components as the over-layered culture medium.	Heparin	234-241	galectin 1	Homo sapiens	96-99
22998648-6	2012	Moreover, we observe that heparin binding induces a distinct two-state structural transition in tau characterized by a loss of long-range contacts and a concomitant compaction of the microtubule binding domain.	Heparin	26-33	microtubule associated protein tau	Homo sapiens	96-99
21120692-7	2011	Furthermore, Tg rabbits showed markedly delayed clearance of plasma triglycerides accompanied with significantly reduced LPL activity in post-heparin plasma compared to that in non-Tg controls.	Heparin	142-149	lipoprotein lipase	Oryctolagus cuniculus	121-124
21781252-1	2011	Thrombomodulin (TM) is an endothelial anticoagulant cofactor that promotes thrombin-mediated activation of protein C. Recently, we conducted a multicentre, double-blind, randomized trial to evaluate the efficacy and safety of recombinant human soluble thrombomodulin (rhsTM, also known as ART-123) for the treatment of disseminated intravascular coagulation (DIC), and found that rhsTM therapy is more effective and safer than low-dose heparin therapy.	Heparin	436-443	thrombomodulin	Homo sapiens	0-14
21781252-1	2011	Thrombomodulin (TM) is an endothelial anticoagulant cofactor that promotes thrombin-mediated activation of protein C. Recently, we conducted a multicentre, double-blind, randomized trial to evaluate the efficacy and safety of recombinant human soluble thrombomodulin (rhsTM, also known as ART-123) for the treatment of disseminated intravascular coagulation (DIC), and found that rhsTM therapy is more effective and safer than low-dose heparin therapy.	Heparin	436-443	thrombomodulin	Homo sapiens	16-18
21518912-6	2011	Here, we report that two LPL missense mutations initially identified in patients with chylomicronemia, C418Y and E421K, abolish LPL"s ability to bind to GPIHBP1 without interfering with LPL catalytic activity or binding to heparin.	Heparin	223-230	lipoprotein lipase	Homo sapiens	25-28
21518912-6	2011	Here, we report that two LPL missense mutations initially identified in patients with chylomicronemia, C418Y and E421K, abolish LPL"s ability to bind to GPIHBP1 without interfering with LPL catalytic activity or binding to heparin.	Heparin	223-230	lipoprotein lipase	Homo sapiens	128-131
21518912-6	2011	Here, we report that two LPL missense mutations initially identified in patients with chylomicronemia, C418Y and E421K, abolish LPL"s ability to bind to GPIHBP1 without interfering with LPL catalytic activity or binding to heparin.	Heparin	223-230	lipoprotein lipase	Homo sapiens	128-131
20558775-0	2011	Heparin inhibits pulmonary artery smooth muscle cell proliferation through guanine nucleotide exchange factor-H1/RhoA/Rho kinase/p27.	Heparin	0-7	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	75-112
20558775-4	2011	We also investigated the effect of guanine nucleotide exchange factor (GEF)-H1, an upstream regulator of RhoA, on heparin inhibition of PASMC proliferation by GEF-H1 cDNA transfection.	Heparin	114-121	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	35-78
20558775-4	2011	We also investigated the effect of guanine nucleotide exchange factor (GEF)-H1, an upstream regulator of RhoA, on heparin inhibition of PASMC proliferation by GEF-H1 cDNA transfection.	Heparin	114-121	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	159-165
22900939-3	2012	Efficient conversions of these to a range of heparin-related gluco-ido disaccharide building blocks (various C-4 protection options) including efficient multigram access to key heparin-building block ido-thioglycoside donors are described.	Heparin	45-52	complement C4A (Rodgers blood group)	Homo sapiens	109-112
2501315-1	1989	Secretion of urokinase-type plasminogen activator (uPA) by RAW264.7 cells was stimulated by heparin in a dose- and time-dependent manner.	Heparin	92-99	plasminogen activator, urokinase	Mus musculus	51-54
21220417-5	2011	Maximal accelerations of ZPI-factor Xa reactions required calcium, which augmented the heparin acceleration by relieving Gla domain inhibition as previously shown for heparin bridging of the antithrombin-factor Xa reaction.	Heparin	87-94	serpin family C member 1	Homo sapiens	191-203
2501315-2	1989	Secretion of uPA was not detected when cells were exposed to heparin at 4 degrees C, indicating that heparin was not simply releasing receptor-bound uPA.	Heparin	101-108	plasminogen activator, urokinase	Mus musculus	13-16
2501315-2	1989	Secretion of uPA was not detected when cells were exposed to heparin at 4 degrees C, indicating that heparin was not simply releasing receptor-bound uPA.	Heparin	101-108	plasminogen activator, urokinase	Mus musculus	149-152
22758787-11	2012	Surprisingly, the insertion resulted in a type II antithrombin deficiency with heparin binding defect.	Heparin	79-86	serpin family C member 1	Homo sapiens	50-62
2501315-4	1989	Low molecular weight and weakly anticoagulant heparins stimulated uPA secretion but less effectively than other heparin fractions.	Heparin	46-54	plasminogen activator, urokinase	Mus musculus	66-69
2501315-4	1989	Low molecular weight and weakly anticoagulant heparins stimulated uPA secretion but less effectively than other heparin fractions.	Heparin	46-53	plasminogen activator, urokinase	Mus musculus	66-69
21193412-8	2011	We show that removal of cell surface glycosaminoglycans (GAGs) by enzymatic or chemical treatment of cells or competition with heparin completely inhibited binding of PSG1.	Heparin	127-134	pregnancy specific beta-1-glycoprotein 1	Homo sapiens	167-171
2501315-5	1989	The observed stimulation in macrophage uPA secretion by heparin is similar to that previously reported for polyanions recognized by the scavenger receptor including fucoidan, polyinosinic acid, dextran sulfate, and acetyl-LDL (Falcone and Ferenc: J.	Heparin	56-63	plasminogen activator, urokinase	Mus musculus	39-42
22777780-5	2012	Protein engineering, or the addition of Cu(2+) ions, sodium dodecyl sulphate, trifluoroethanol, heparin, or protein stabilisers, was employed to perturb the conformational dynamics of beta(2)m.	Heparin	96-103	beta-2-microglobulin	Homo sapiens	184-192
2781529-0	1989	Heparin-induced thrombocytopenia: effects of rabbit IgG, and its Fab and FC fragments on antibody-heparin-platelet interaction.	Heparin	0-7	FA complementation group B	Homo sapiens	65-68
22759275-4	2012	We mutated two cationic heparin-binding motifs responsible for electrostatic interactions of GrB with cell surface structures, and genetically fused the resulting GrBcs derivative to TGFalpha for expression in the yeast Pichia pastoris.	Heparin	24-31	granzyme B	Homo sapiens	93-96
22281439-4	2012	Amyloid fibril formation by tau, a microtubule-associated protein whose aggregation to form neurofibrillary tangles is implicated in Alzheimer"s disease and other tauopathies, in the presence of inducers such as heparin and fatty acid micelles, has always been traditionally described by a ligand-induced NDP model.	Heparin	212-219	regulator of microtubule dynamics 1	Homo sapiens	35-65
21679503-12	2011	UFH or LMWH inhibited tumor necrosis factor alpha (10 ng/mL)-induced secretion of MUC5AC and IL-8 from NCI-H292 cells in a dose-dependent manner (0.01-10 IU/mL).	Heparin	0-3	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	82-88
22977511-0	2011	Low molecular weight heparin suppresses tissue factor-mediated cancer cell invasion and migration in vitro.	Heparin	21-28	coagulation factor III, tissue factor	Homo sapiens	40-53
2544589-2	1989	Human antithrombin III (AT-III) was partially reduced under mild conditions in the absence or presence of low molecular weight heparin.	Heparin	127-134	serpin family C member 1	Homo sapiens	24-30
21327876-5	2011	Since heparin is a conditio sine qua non for cardiopulmonary bypass, rapid consumption of AT-III promoted by heparin may lead to systemic thrombosis.	Heparin	6-13	serpin family C member 1	Homo sapiens	90-96
22498748-0	2012	Amelioration of the severity of heparin-binding antithrombin mutations by posttranslational mosaicism.	Heparin	32-39	serpin family C member 1	Homo sapiens	48-60
22498748-4	2012	These mutations do not modify the folding or secretion of the protein, but abolish the glycosaminoglycan-induced activation of antithrombin by affecting the heparin-binding domain.	Heparin	157-164	serpin family C member 1	Homo sapiens	127-139
22498748-5	2012	We speculated that the natural beta-glycoform of antithrombin might compensate for the effect of heparin-binding mutations.	Heparin	97-104	serpin family C member 1	Homo sapiens	49-61
21327876-5	2011	Since heparin is a conditio sine qua non for cardiopulmonary bypass, rapid consumption of AT-III promoted by heparin may lead to systemic thrombosis.	Heparin	109-116	serpin family C member 1	Homo sapiens	90-96
2544589-7	1989	These results suggest that Cys8-Cys128 is required for the integrity of the heparin binding domain of AT-III and support previous findings that lysyl residues surrounding Cys128 (Lys107, Lys114, Lys125, and Lys136) constitute an important part of the heparin binding site in AT-III.	Heparin	76-83	serpin family C member 1	Homo sapiens	102-108
22498748-10	2012	In conclusion, we identified a new type of mosaicism associated with mutations causing heparin-binding defects in antithrombin.	Heparin	87-94	serpin family C member 1	Homo sapiens	114-126
2473082-0	1989	Transforming growth factor-beta activity is potentiated by heparin via dissociation of the transforming growth factor-beta/alpha 2-macroglobulin inactive complex.	Heparin	59-66	alpha-2-macroglobulin	Homo sapiens	123-144
22618708-6	2012	To address these issues, we determined the crystal structures of PN1 in complex with heparin, and in complex with catalytically inert thrombin.	Heparin	85-92	serpin family E member 2	Homo sapiens	65-68
2473082-8	1989	Heparin increases the electrophoretic mobility of TGF-beta apparently by freeing TGF-beta from its complex with alpha 2-macroglobulin.	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	112-133
21347292-10	2011	The pre-incubation with CB1 or TRPV1 antagonists inhibited heparin-induced sperm capacitation; moreover the activity of FAAH was 30% lower in heparin-capacitated spermatozoa as compared to control conditions.	Heparin	59-66	fatty-acid amide hydrolase 1	Bos taurus	120-124
21347292-10	2011	The pre-incubation with CB1 or TRPV1 antagonists inhibited heparin-induced sperm capacitation; moreover the activity of FAAH was 30% lower in heparin-capacitated spermatozoa as compared to control conditions.	Heparin	142-149	fatty-acid amide hydrolase 1	Bos taurus	120-124
2473082-10	1989	Relatively high, antiproliferative concentrations of heparin (1-100 micrograms/ml) were required to dissociate the TGF-beta/alpha 2-macroglobulin complex.	Heparin	53-60	alpha-2-macroglobulin	Homo sapiens	124-145
2473082-11	1989	Thus, it appears that the antiproliferative effect of heparin may be partially attributed to its ability to potentiate the biological activity of TGF-beta by dissociating it from alpha 2-macroglobulin, which normally renders it inactive.	Heparin	54-61	alpha-2-macroglobulin	Homo sapiens	179-200
22349764-7	2012	In heparin plasma, CN-1 was also poorly detected with the RYSK-based assay.	Heparin	3-10	carnosine dipeptidase 1	Homo sapiens	19-23
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	0-7	serpin family C member 1	Homo sapiens	124-140
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	0-7	serpin family C member 1	Homo sapiens	142-148
21052646-1	2011	Heparin-immobilized microspheres were included in microdialysis sampling perfusion fluids under both in vitro and in vivo conditions to improve the recovery of different cytokines, acidic fibroblast growth factor, vascular endothelial growth factor, monocyte chemoattractant protein-1 (or CCL2), and regulation upon activation normal T cell express sequence (or CCL5).	Heparin	0-7	C-C motif chemokine ligand 2	Rattus norvegicus	250-284
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	12-19	serpin family C member 1	Homo sapiens	124-140
21052646-1	2011	Heparin-immobilized microspheres were included in microdialysis sampling perfusion fluids under both in vitro and in vivo conditions to improve the recovery of different cytokines, acidic fibroblast growth factor, vascular endothelial growth factor, monocyte chemoattractant protein-1 (or CCL2), and regulation upon activation normal T cell express sequence (or CCL5).	Heparin	0-7	C-C motif chemokine ligand 2	Rattus norvegicus	289-293
2781509-2	1989	The variant antithrombin was isolated from plasma of the propositus by chromatography on heparin-Sepharose, followed by passage through thrombin-Sepharose to remove the normal antithrombin component that is present.	Heparin	89-96	serpin family C member 1	Homo sapiens	12-24
21052646-4	2011	Enhanced microdialysis RR of CCL2 using the heparin-immobilized microspheres from microdialysis probes implanted into the peritoneal cavity of a rat was performed to test the in vivo application.	Heparin	44-51	C-C motif chemokine ligand 2	Rattus norvegicus	29-33
21987113-8	2011	Flow cytometric analysis using anti-CD14 (monocyte marker) and anti-CD83 (mature DC marker) revealed that expression of CD14 decreased in MCM plus heparin-treated DC, and the expression of CD83 was increased when heparin and MCM used as a maturation factor.	Heparin	147-154	CD83 molecule	Homo sapiens	68-72
21987113-8	2011	Flow cytometric analysis using anti-CD14 (monocyte marker) and anti-CD83 (mature DC marker) revealed that expression of CD14 decreased in MCM plus heparin-treated DC, and the expression of CD83 was increased when heparin and MCM used as a maturation factor.	Heparin	147-154	CD83 molecule	Homo sapiens	189-193
21987113-8	2011	Flow cytometric analysis using anti-CD14 (monocyte marker) and anti-CD83 (mature DC marker) revealed that expression of CD14 decreased in MCM plus heparin-treated DC, and the expression of CD83 was increased when heparin and MCM used as a maturation factor.	Heparin	213-220	CD83 molecule	Homo sapiens	189-193
20850172-1	2011	INTRODUCTION: Low-molecular-weight heparins (LMWHs) and fondaparinux are antithrombin dependent anticoagulant drugs considered to need no laboratory monitoring because of their reputedly predictable anticoagulant effect.	Heparin	35-43	serpin family C member 1	Homo sapiens	73-85
22454106-7	2012	The antithrombin binding capacity of the immobilized heparin was determined to be 60-80 pmol/cm(2) in an antithrombin uptake assay.	Heparin	53-60	serpin family C member 1	Homo sapiens	4-16
22454106-7	2012	The antithrombin binding capacity of the immobilized heparin was determined to be 60-80 pmol/cm(2) in an antithrombin uptake assay.	Heparin	53-60	serpin family C member 1	Homo sapiens	105-117
22197178-5	2012	We measured the heparin binding affinity of purified alphaIIbbeta3, and of recombinant fragments of alphaIIb and beta3, by surface plasmon resonance.	Heparin	16-23	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	61-66
22197178-7	2012	Heparin binding alone is not sufficient to induce tyrosine phosphorylation of the integrin beta3 cytoplasmic domain, but the presence of heparin increased both beta3 phosphorylation and src kinase activation in response to ligand binding.	Heparin	137-144	eukaryotic translation elongation factor 1 beta 2 pseudogene 2	Homo sapiens	160-165
22406166-11	2012	A similar agreement between the total TGF-beta1 and the LAP ELISA was found with citrate- and heparin-containing plasma.	Heparin	94-101	LAP	Homo sapiens	56-59
22642296-11	2012	Triton X-100 and heparin are important factors in the refolding environment for this mini-enzyme matrilysin.	Heparin	17-24	matrix metallopeptidase 7	Homo sapiens	97-107
2723649-0	1989	Equilibrium binding analysis of neural cell adhesion molecule binding to heparin.	Heparin	73-80	neural cell adhesion molecule 1	Rattus norvegicus	32-61
22227436-3	2012	We demonstrate that HS isolated from a bone marrow stromal cell line (HS-5) and heparin each enhances BMP-2-induced osteogenesis in C2C12 myoblasts through increased ALP activity and osteocalcin mRNA expression.	Heparin	80-87	bone gamma-carboxyglutamate protein	Bos taurus	183-194
21134627-2	2011	We present a case of a female with heterozygous type I antithrombin deficiency who presented with a central nervous system transverse sinus thrombosis in the third trimester of pregnancy despite the use of therapeutic doses of low molecular weight heparin, as venous thromboembolic prophylaxis, since conception.	Heparin	248-255	serpin family C member 1	Homo sapiens	55-67
21050017-2	2010	Here we report the first successful use of solution NMR in mapping the binding sites in arrestin-1 (visual arrestin) for two polyanionic compounds that mimic phosphorylated light-activated rhodopsin: inositol hexaphosphate (IP6) and heparin.	Heparin	233-240	S-antigen visual arrestin	Homo sapiens	88-98
21050017-4	2010	IP6 and heparin appear to bind to the same site on arrestin-1, centered on a positively charged region in the N-domain.	Heparin	8-15	S-antigen visual arrestin	Homo sapiens	51-61
2723649-1	1989	The kinetics of neural cell adhesion molecule (NCAM) binding to heparin were studied in a heparin-Sepharose-based solid-phase binding assay.	Heparin	64-71	neural cell adhesion molecule 1	Rattus norvegicus	16-45
22009636-4	2012	GPIHBP1-deficient mice and humans exhibit severe hypertriglyceridemia and diminished heparin-releasable LPL, pointing to the critical role of GPIHBP1 in regulation of LPL activity.	Heparin	85-92	lipoprotein lipase	Homo sapiens	104-107
22009636-4	2012	GPIHBP1-deficient mice and humans exhibit severe hypertriglyceridemia and diminished heparin-releasable LPL, pointing to the critical role of GPIHBP1 in regulation of LPL activity.	Heparin	85-92	lipoprotein lipase	Homo sapiens	167-170
2723649-1	1989	The kinetics of neural cell adhesion molecule (NCAM) binding to heparin were studied in a heparin-Sepharose-based solid-phase binding assay.	Heparin	64-71	neural cell adhesion molecule 1	Rattus norvegicus	47-51
20945941-1	2010	Supersulfated low molecular weight heparin (ssLMWH) inhibits the intrinsic tenase (factor IXa-factor VIIIa) complex in an antithrombin-independent manner.	Heparin	35-42	serpin family C member 1	Homo sapiens	122-134
2723649-1	1989	The kinetics of neural cell adhesion molecule (NCAM) binding to heparin were studied in a heparin-Sepharose-based solid-phase binding assay.	Heparin	90-97	neural cell adhesion molecule 1	Rattus norvegicus	16-45
2723649-1	1989	The kinetics of neural cell adhesion molecule (NCAM) binding to heparin were studied in a heparin-Sepharose-based solid-phase binding assay.	Heparin	90-97	neural cell adhesion molecule 1	Rattus norvegicus	47-51
22178588-6	2012	All 4 forms of HGF/SF induced similar levels of DNA synthesis in human hepatocytes; 1K1 and NK1 required heparin, an HSPG analogue, for full agonistic activity.	Heparin	105-112	tachykinin receptor 1	Homo sapiens	92-95
2723649-3	1989	A binding constant of 5.2 +/- 1.4 X 10(-8) M is observed for binding of newborn rat NCAM to heparin.	Heparin	92-99	neural cell adhesion molecule 1	Rattus norvegicus	84-88
20692269-2	2010	Here, we provide evidence that, unlike other C-type lectins, human RegIV binds to polysaccharides, mannan, and heparin in the absence of calcium.	Heparin	111-118	regenerating family member 4	Homo sapiens	67-72
2723649-6	1989	Fab" fragments of antibodies to rat NCAM significantly inhibit binding, a result indicating that a specific site on NCAM is involved in binding to heparin.	Heparin	147-154	neural cell adhesion molecule 1	Rattus norvegicus	36-40
2723649-6	1989	Fab" fragments of antibodies to rat NCAM significantly inhibit binding, a result indicating that a specific site on NCAM is involved in binding to heparin.	Heparin	147-154	neural cell adhesion molecule 1	Rattus norvegicus	116-120
22134915-0	2012	Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in alpha-synuclein aggregation.	Heparin	20-27	synuclein alpha	Homo sapiens	131-146
2503646-5	1989	As our patient had multiple risk factors for the development of vitamin K deficiency including malabsorption, decreased food intake, and antibiotic use, we postulate that the small amount of heparin precipitated the coagulopathy by increasing the antiprotease activity of antithrombin III on abnormal factors X and II formed in the vitamin K deficient state.	Heparin	191-198	serpin family C member 1	Homo sapiens	272-288
22134915-9	2012	Taking into account the toxicity of alpha-synuclein prefibrillar species, the heparin-induced glyceraldehyde-3-phosphate dehydrogenase early oligomers might come in useful as a novel therapeutic strategy in Parkinson disease and other synucleinopathies.	Heparin	78-85	synuclein alpha	Homo sapiens	36-51
22161774-0	2012	Heparin-coated colloidal mesoporous silica nanoparticles efficiently bind to antithrombin as an anticoagulant drug-delivery system.	Heparin	0-7	serpin family C member 1	Homo sapiens	77-89
20628058-1	2010	The activation of antithrombin (AT) by heparin facilitates the exosite-dependent interaction of the serpin with factors IXa (FIXa) and Xa (FXa), thereby improving the rate of reactions by 300- to 500-fold.	Heparin	39-46	serpin family C member 1	Homo sapiens	18-30
20628058-1	2010	The activation of antithrombin (AT) by heparin facilitates the exosite-dependent interaction of the serpin with factors IXa (FIXa) and Xa (FXa), thereby improving the rate of reactions by 300- to 500-fold.	Heparin	39-46	serpin family C member 1	Homo sapiens	32-34
20628058-7	2010	The chimeric mutant cleaved a FIXa-specific chromogenic substrate with normal catalytic efficiency, however, the mutant exhibited approximately 5-fold enhanced reactivity with AT specifically in the absence of the cofactor, heparin.	Heparin	224-231	serpin family C member 1	Homo sapiens	176-178
20699357-4	2010	Blocking alpha5beta1 integrin or supplementing cultures with heparin, which both inhibited microfibril assembly, disrupted LTBP-1 deposition and enhanced Smad2 phosphorylation.	Heparin	61-68	latent transforming growth factor beta binding protein 1	Homo sapiens	123-129
20699357-5	2010	Full-length LTBP-1 bound only weakly to N-terminal pro-fibrillin-1, but this association was strongly enhanced by heparin.	Heparin	114-121	latent transforming growth factor beta binding protein 1	Homo sapiens	12-18
20627942-1	2010	BACKGROUND: Antithrombin concentrate (AT) is used to treat heparin resistance (HR) in cardiac surgery.	Heparin	59-66	serpin family C member 1	Homo sapiens	12-24
22028447-2	2012	In this report, we provide evidence that 5-HT induced production of heparin-binding epidermal growth factor-like growth factor (HB-EGF) and caused insulin resistance in 3T3-L1 adipocytes, primary adipocytes, and C2C12 myotubes.	Heparin	68-75	heparin binding EGF like growth factor	Homo sapiens	128-134
2759682-7	1989	Heparin and calcium ionophore induced release of both MBP and histaminase.	Heparin	0-7	myelin basic protein	Cavia porcellus	54-57
22232002-5	2012	The quinolines 2-(4-methylphenyl)-6-methyl quinoline (THQ-4S) and 2-(4-aminophenyl)-6-methylquinoline (THQ-55) inhibited in vitro aggregation of heparin-induced polymers of purified brain tau and aggregates of human recombinant tau.	Heparin	145-152	microtubule associated protein tau	Homo sapiens	188-191
22232002-5	2012	The quinolines 2-(4-methylphenyl)-6-methyl quinoline (THQ-4S) and 2-(4-aminophenyl)-6-methylquinoline (THQ-55) inhibited in vitro aggregation of heparin-induced polymers of purified brain tau and aggregates of human recombinant tau.	Heparin	145-152	microtubule associated protein tau	Homo sapiens	228-231
22052169-0	2012	In vitro determination of apoptotic effect of heparin on lymphoblasts by using flow cytometric DNA analysis and measurements of caspase-9 activation and cytochrome C level.	Heparin	46-53	caspase 9	Homo sapiens	128-137
22052169-9	2012	The mean caspase-9 activity in 20 U/mL heparin concentration was significantly higher than values in 0 and 10 U/mL heparin concentrations at 1 and 2 hours (P&lt;0.05).	Heparin	39-46	caspase 9	Homo sapiens	9-18
20547765-8	2010	Mechanistically, Wnt3a-heparin signaling strongly activates the phosphoinositide 3-kinase/Akt pathway and requires the bone-related transcription factor RUNX2 to stimulate alkaline phosphatase activity, which parallels canonical beta-catenin signaling.	Heparin	23-30	catenin beta 1	Homo sapiens	229-241
20548024-6	2010	DNA and heparin compete for C1q binding but are poor C1 activators compared with immune complexes.	Heparin	8-15	complement C1q A chain	Homo sapiens	28-31
22052169-10	2012	The highest caspase-9 activity was determined in 20 U/mL heparin levels at the first hour.	Heparin	57-64	caspase 9	Homo sapiens	12-21
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	55-62	serpin family C member 1	Homo sapiens	127-143
21984036-11	2012	Heparin can decrease the level of Duox1, ROS production and block the PMA-induced activation of EGFR, thus inhibiting the overexpression of mucin MUC5AC in a dose-dependent manner.	Heparin	0-7	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	146-152
20503388-5	2010	FoxA1 protein was upregulated at early to intermediate time points, where it was strongly elevated by heparin.	Heparin	102-109	forkhead box A1	Homo sapiens	0-5
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	55-62	serpin family C member 1	Homo sapiens	127-143
21984036-12	2012	In addition to reducing ROS production, heparin may also inhibit the expression of MUC5AC through other signal mechanisms.	Heparin	40-47	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	83-89
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	152-159	serpin family C member 1	Homo sapiens	29-45
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	152-159	serpin family C member 1	Homo sapiens	127-143
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	152-159	serpin family C member 1	Homo sapiens	127-143
20375066-7	2010	Studies with fragments indicated that both the RGD-synergy site and the adjacent heparin-binding region of fibronectin were required for full activity in mechanotransduction, but not its ability to self-assemble.	Heparin	81-88	fibronectin 1	Mus musculus	107-118
23152789-2	2012	BACKGROUND: The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively.	Heparin	29-36	serpin family C member 1	Homo sapiens	16-28
2466666-6	1989	If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity.	Heparin	152-159	serpin family C member 1	Homo sapiens	127-143
20351192-7	2010	The interaction of C1 inhibitor and its variants with heparin was investigated by surface plasmon resonance, yielding K(D) values of 16.7 x 10(-8) M (C1 inhibitor), 2.3 x 10(-8) M (C1inhDelta97), and 3.6 x 10(-8) M (C1inhDelta97DM).	Heparin	54-61	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	181-193
2466666-9	1989	Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced.	Heparin	135-142	serpin family C member 1	Homo sapiens	15-31
23133647-7	2012	This finding enabled us to map heparin/heparan sulfate binding to two sites on fibrillin-1 TB5 using a mutagenesis approach.	Heparin	31-38	fibrillin 1	Homo sapiens	79-90
2466666-9	1989	Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced.	Heparin	185-192	serpin family C member 1	Homo sapiens	15-31
22912725-0	2012	Heparin inhibits Hepatocyte Growth Factor induced motility and invasion of hepatocellular carcinoma cells through early growth response protein 1.	Heparin	0-7	early growth response 1	Homo sapiens	114-145
22912725-7	2012	In addition, heparin reduced HGF-induced activation of c-Met and MAPK in a dose-dependent manner, as well as decreased transcriptional activation and expression of Early growth response factor 1 (Egr1).	Heparin	13-20	early growth response 1	Homo sapiens	164-194
22912725-7	2012	In addition, heparin reduced HGF-induced activation of c-Met and MAPK in a dose-dependent manner, as well as decreased transcriptional activation and expression of Early growth response factor 1 (Egr1).	Heparin	13-20	early growth response 1	Homo sapiens	196-200
22049073-0	2011	Lowered expression of heparan sulfate/heparin biosynthesis enzyme N-deacetylase/n-sulfotransferase 1 results in increased sulfation of mast cell heparin.	Heparin	38-45	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	66-100
22049073-0	2011	Lowered expression of heparan sulfate/heparin biosynthesis enzyme N-deacetylase/n-sulfotransferase 1 results in increased sulfation of mast cell heparin.	Heparin	145-152	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	66-100
20035973-5	2010	RESULTS: The specific interaction between low-molecular-weight heparin and the C1q subunit of the C1 complex of the complement cascade allowed the isolation of a small subpopulation of heparin ( 8.03+/-1.20 microg %), with an anti-activated factor X activity more than four times greater than the starting material.	Heparin	185-192	complement C1q A chain	Homo sapiens	79-82
20035973-9	2010	CONCLUSIONS: We concluded that the interaction between low-molecular-weight heparin and C1q could be relevant not only in the complement-dependent, but also in the complement-independent inflammation mechanisms responsible for the prevention of pregnancy loss.	Heparin	76-83	complement C1q A chain	Homo sapiens	88-91
20216984-4	2010	Heparin (H) increases the rate of IIa-TM inhibition by antithrombin (AT) and enhances FV cleavage by APC.	Heparin	0-7	serpin family C member 1	Homo sapiens	55-67
22049073-1	2011	Deficiency of the heparan sulfate biosynthesis enzyme N-deacetylase/N-sulfotransferase 1 (NDST1) in mice causes severely disturbed heparan sulfate biosynthesis in all organs, whereas lack of NDST2 only affects heparin biosynthesis in mast cells (MCs).	Heparin	210-217	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	54-88
2466666-9	1989	Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced.	Heparin	185-192	serpin family C member 1	Homo sapiens	15-31
22049073-1	2011	Deficiency of the heparan sulfate biosynthesis enzyme N-deacetylase/N-sulfotransferase 1 (NDST1) in mice causes severely disturbed heparan sulfate biosynthesis in all organs, whereas lack of NDST2 only affects heparin biosynthesis in mast cells (MCs).	Heparin	210-217	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	90-95
22049073-4	2011	Surprisingly, the relative amount of heparin produced in NDST1(+/-) and NDST1(-/-) MCs is higher ( 30%) than in control MCs where  95% of the (35)S-labeled glycosaminoglycans produced is chondroitin sulfate.	Heparin	37-44	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	57-62
2466846-2	1989	The anticoagulant action of heparin is mediated through antithrombin III, and the postoperative decrease in the plasma concentration of antithrombin III may contribute to the relative ineffectiveness of prophylaxis with low-dose heparin in preventing venous thrombosis after total hip arthroplasty.	Heparin	28-35	serpin family C member 1	Homo sapiens	56-72
22049073-4	2011	Surprisingly, the relative amount of heparin produced in NDST1(+/-) and NDST1(-/-) MCs is higher ( 30%) than in control MCs where  95% of the (35)S-labeled glycosaminoglycans produced is chondroitin sulfate.	Heparin	37-44	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	72-77
22049073-5	2011	Lowered expression of NDST1 also results in a higher sulfate content of the heparin synthesized and is accompanied by increased levels of stored MC proteases.	Heparin	76-83	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	22-27
22049079-4	2011	Here, we have used molecular modeling to examine the heparin-binding domain of sonic hedgehog (Shh).	Heparin	53-60	sonic hedgehog signaling molecule	Homo sapiens	79-93
22049079-4	2011	Here, we have used molecular modeling to examine the heparin-binding domain of sonic hedgehog (Shh).	Heparin	53-60	sonic hedgehog signaling molecule	Homo sapiens	95-98
22049079-8	2011	Mutated hShhs such as K37S/K38S, K178S, and particularly K37S/K38S/K178S that could not interact with heparin efficiently had reduced signaling activity compared with wild type hShh or a control mutation (K74S).	Heparin	102-109	sonic hedgehog signaling molecule	Homo sapiens	8-12
20434009-5	2010	Heparin, apart from its anticoagulant activity contains a variety of biological activities possibly affecting cancer progression, including: inhibition of heparanase, blocking of P- and L-selectin mediated cell adhesion, and inhibition of angiogenesis.	Heparin	0-7	selectin L	Homo sapiens	186-196
20434010-8	2010	As heparins are strong inhibitor of heparanase, in view of the effect of heparanase on TF, the role of heparins anticoagulant-activity may potentially be expanded.	Heparin	3-11	coagulation factor III, tissue factor	Homo sapiens	87-89
20201787-4	2010	We found that butanoylated heparin a) significantly inhibited lung cancer cell proliferation in vitro and lung cancer growth in mice and rats; b) had very low anticoagulant effect; c) had no significant toxicity on heart, liver, kidney and lung; d) significantly although modestly induced apoptosis and decreased expression of the cell proliferation pathway consisting of mutant p53, phospho-Rb and E2F1 expression in the tumor tissues.	Heparin	27-34	Wistar clone pR53P1 p53 pseudogene	Rattus norvegicus	379-382
20201787-4	2010	We found that butanoylated heparin a) significantly inhibited lung cancer cell proliferation in vitro and lung cancer growth in mice and rats; b) had very low anticoagulant effect; c) had no significant toxicity on heart, liver, kidney and lung; d) significantly although modestly induced apoptosis and decreased expression of the cell proliferation pathway consisting of mutant p53, phospho-Rb and E2F1 expression in the tumor tissues.	Heparin	27-34	E2F transcription factor 1	Rattus norvegicus	399-403
2466846-2	1989	The anticoagulant action of heparin is mediated through antithrombin III, and the postoperative decrease in the plasma concentration of antithrombin III may contribute to the relative ineffectiveness of prophylaxis with low-dose heparin in preventing venous thrombosis after total hip arthroplasty.	Heparin	229-236	serpin family C member 1	Homo sapiens	136-152
2492530-14	1989	We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification.	Heparin	71-78	serpin family C member 1	Homo sapiens	101-113
20215909-2	2010	Heparin exerts its major effect via antithrombin, converting antithrombin to a more efficient inhibitor of circulating thrombin (factor IIa), factor Xa, factor IXa, factor XIIa, and kallikrein.	Heparin	0-7	serpin family C member 1	Homo sapiens	36-48
20215909-2	2010	Heparin exerts its major effect via antithrombin, converting antithrombin to a more efficient inhibitor of circulating thrombin (factor IIa), factor Xa, factor IXa, factor XIIa, and kallikrein.	Heparin	0-7	serpin family C member 1	Homo sapiens	61-73
20387539-9	2010	Generation of Slit2 and Ext 1 compound mutants caused disturbed activity of Slit proteins, heparin/heparan sulfate-binding chemorepulsive guidance factors.	Heparin	91-98	slit guidance ligand 2	Homo sapiens	14-19
19906646-7	2010	This property is likely caused by histidine residues in the vicinity of the mapped heparin binding site and could be important for the proposed adhesive function of APL-1.	Heparin	83-90	acireductone dioxygenase 1	Homo sapiens	165-170
21569219-1	2011	Antithrombin inhibits VIIa when bound to cellular tissue factor in the presence of heparin.	Heparin	83-90	serpin family C member 1	Homo sapiens	0-12
21569219-6	2011	There is an approximate twofold increase in measurable VIIa-antithrombin complexes in patients undergoing cardiac surgery, which is apparent after heparin administration.	Heparin	147-154	serpin family C member 1	Homo sapiens	60-72
21795523-6	2011	Using purified active matriptase, we further characterize the formation of matriptase-antithrombin complex and show that heparin can significantly potentiate the inhibitory potency of antithrombin against matriptase.	Heparin	121-128	serpin family C member 1	Homo sapiens	86-98
21795523-6	2011	Using purified active matriptase, we further characterize the formation of matriptase-antithrombin complex and show that heparin can significantly potentiate the inhibitory potency of antithrombin against matriptase.	Heparin	121-128	serpin family C member 1	Homo sapiens	184-196
21795523-7	2011	Second-order rate constants for the inhibition were determined to be 3.9 x 10(3) M(-1)s(-1) in the absence of heparin and 1.2 x 10(5) M(-1)s(-1) in the presence of heparin, a 30-fold increase, consistent with the established role of heparin in activating antithrombin function.	Heparin	110-117	serpin family C member 1	Homo sapiens	255-267
2492530-14	1989	We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification.	Heparin	71-78	serpin family C member 1	Homo sapiens	145-157
19753513-8	2010	Heparin inhibits the activity of aSMase and concomitantly induces the activity of nSMase in each studied muscle.	Heparin	0-7	sphingomyelin phosphodiesterase 2	Rattus norvegicus	82-88
2492530-14	1989	We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification.	Heparin	71-78	serpin family C member 1	Homo sapiens	145-157
22097980-2	2011	Heparin acts by potentiating the anticoagulant effect of antithrombin (ATIII).	Heparin	0-7	serpin family C member 1	Homo sapiens	57-69
2492530-14	1989	We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification.	Heparin	134-141	serpin family C member 1	Homo sapiens	101-113
22097980-2	2011	Heparin acts by potentiating the anticoagulant effect of antithrombin (ATIII).	Heparin	0-7	serpin family C member 1	Homo sapiens	71-76
22097980-3	2011	Acquired ATIII deficiency, common in pediatric patients requiring ECMO, may result in ineffective anticoagulation with heparin.	Heparin	119-126	serpin family C member 1	Homo sapiens	9-14
2492530-14	1989	We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification.	Heparin	134-141	serpin family C member 1	Homo sapiens	145-157
2492530-14	1989	We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification.	Heparin	134-141	serpin family C member 1	Homo sapiens	145-157
20816204-1	2010	Sulf-1 and Sulf-2 are extracellular endoglucosamine 6-sulfatases, which selectively liberate the 6-O-sulfate groups on glucosamines present in N, 6-O, and 2-O trisulfated disaccharides of intact heparan sulfate (HS)/heparin chains.	Heparin	216-223	sulfatase 2	Homo sapiens	11-17
2546277-2	1989	EMT 966 like standard heparin, acts primarily on thrombin formed and not on prothrombinase (S type heparin).	Heparin	22-29	IL2 inducible T cell kinase	Homo sapiens	0-3
20224283-2	2010	BACE1 binds strongly to heparin and other glycosaminoglycans, and there is evidence that the enzyme may interact with proteoglycans in vivo.	Heparin	24-31	beta-site APP cleaving enzyme 1	Mus musculus	0-5
21513424-0	2011	Efficient inhibition of ovarian cancer by truncation mutant of FILIP1L gene delivered by novel biodegradable cationic heparin-polyethyleneimine nanogels.	Heparin	118-125	filamin A interacting protein 1 like	Homo sapiens	63-70
2471858-2	1989	A low-molecular weight peptide (P-1) responsible for releasing histamine was isolated from peptic digests of human serum albumin by affinity chromatography on heparin-Ultrogel and reversed-phase high performance liquid chromatography.	Heparin	159-166	perforin 1	Rattus norvegicus	32-35
21665912-8	2011	CONCLUSIONS: Patient"s age could be a moderate indicator of AT activity drop and low preoperative AT activity could be a sign of reduced anticoagulant efficacy of heparin during CPB.	Heparin	163-170	serpin family C member 1	Homo sapiens	98-100
20224283-4	2010	OBJECTIVE: To determine whether heparin can inhibit Abeta production in cortical neurons by inhibiting BACE1.	Heparin	32-39	beta-site APP cleaving enzyme 1	Mus musculus	103-108
19877579-0	2009	The heparin binding motif of endostatin mediates its interaction with receptor nucleolin.	Heparin	4-11	collagen type XVIII alpha 1 chain	Homo sapiens	29-39
19877579-3	2009	To define the exact role of the heparin binding motif in mediating the interaction between endostatin and its receptor nucleolin, up to six arginine residues (R155, R158, R184, R270, R193, and R194) located in the heparin binding motif of endostatin were substituted by alanine to make double, quadruple, or hexad point mutations, respectively.	Heparin	32-39	collagen type XVIII alpha 1 chain	Homo sapiens	91-101
19877579-4	2009	Contributions of the heparin binding motif to both the interaction with nucleolin and the biological activities of endostatin were investigated from in vitro to in vivo.	Heparin	21-28	collagen type XVIII alpha 1 chain	Homo sapiens	115-125
19877579-5	2009	Here we show that Arg to Ala point mutagenesis of the heparin binding motif does not interrupt the folding of endostatin but significantly impairs the interaction between endostatin and nucleolin.	Heparin	54-61	collagen type XVIII alpha 1 chain	Homo sapiens	171-181
19877579-7	2009	Taken together, the present study demonstrates that the arginine clusters in the heparin binding motif of endostatin significantly contribute to its interaction with receptor nucleolin and mediate the antiangiogenic and antitumor activities of endostatin.	Heparin	81-88	collagen type XVIII alpha 1 chain	Homo sapiens	106-116
21799398-9	2011	ATIII administration increases heparin sensitivity and decreases heparin requirements compared with FFP in patients undergoing CABGS with peroperative NTG infusion.	Heparin	31-38	serpin family C member 1	Homo sapiens	0-5
21799398-9	2011	ATIII administration increases heparin sensitivity and decreases heparin requirements compared with FFP in patients undergoing CABGS with peroperative NTG infusion.	Heparin	65-72	serpin family C member 1	Homo sapiens	0-5
21799398-10	2011	ATIII may be preferred to FFP in patients with heparin resistance due to NTG infusion undergoing CABGS.	Heparin	47-54	serpin family C member 1	Homo sapiens	0-5
21875153-0	2011	Energetics of hydrogen bond switch, residue burial and cavity analysis reveals molecular basis of improved heparin binding to antithrombin.	Heparin	107-114	serpin family C member 1	Homo sapiens	126-138
21875153-2	2011	Anticoagulant activity of ATIII is increased by several thousand folds when activated by vascular wall heparan sulfate proteoglycans (HSPGs) and pharmaceutical heparins.	Heparin	160-168	serpin family C member 1	Homo sapiens	26-31
21875153-3	2011	ATIII isoforms in human plasma, alpha-ATIII and beta-ATIII differ in the amount of glycosylation which is the basis of differences in their heparin binding affinity and function.	Heparin	140-147	serpin family C member 1	Homo sapiens	0-5
21875153-4	2011	Crystal structures and site directed mutagenesis studies have mapped the heparin binding site in ATIII, however the hydrogen bond switch and energetics of interaction during the course of heparin dependent conformational change remains largely unclear.	Heparin	73-80	serpin family C member 1	Homo sapiens	97-102
21875153-5	2011	An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions.	Heparin	15-22	serpin family C member 1	Homo sapiens	54-59
19877579-7	2009	Taken together, the present study demonstrates that the arginine clusters in the heparin binding motif of endostatin significantly contribute to its interaction with receptor nucleolin and mediate the antiangiogenic and antitumor activities of endostatin.	Heparin	81-88	collagen type XVIII alpha 1 chain	Homo sapiens	244-254
19961422-6	2009	The identified proteinases contained heparin-binding motifs inherent in the complex-forming partners of CP, such as lactoferrin, myeloperoxidase, and serprocidines.	Heparin	37-44	ceruloplasmin	Homo sapiens	104-106
19961422-7	2009	Therefore, admixtures of MMPs can be efficiently eliminated from CP preparations by chromatography on heparin-Sepharose as proposed previously.	Heparin	102-109	ceruloplasmin	Homo sapiens	65-67
19748283-8	2009	Further in vitro experiments indicate that heparin prevents the activation of latent TGF-beta into its bioactive form probably by virtue of accelerating the complex-formation between AT-III and thrombin.	Heparin	43-50	serpin family C member 1	Homo sapiens	183-189
21875153-5	2011	An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions.	Heparin	97-104	serpin family C member 1	Homo sapiens	54-59
21875153-5	2011	An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions.	Heparin	97-104	serpin family C member 1	Homo sapiens	54-59
21875153-11	2011	We hypothesize that during the process of conformational change after heparin binding beta form of antithrombin has low energy barrier to form D-helix extension toward N and C-terminal end as compared to alpha isoform.	Heparin	70-77	serpin family C member 1	Homo sapiens	99-111
19929245-5	2009	Compared to baseline and to lepirudin, heparin induced platelet P-selectin expression (p = 0.04).	Heparin	39-46	selectin P	Homo sapiens	64-74
2909522-0	1989	Location of the antithrombin-binding sequence in the heparin chain.	Heparin	53-60	serpin family C member 1	Homo sapiens	16-28
19931793-4	2009	Heparin can then act as an anticoagulant by binding to antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	55-67
2909522-1	1989	The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-.	Heparin	35-42	serpin family C member 1	Homo sapiens	4-16
21784848-11	2011	Compared with the classical mutations and the wild type, the group of neonatal mutations more severely affected the ability of fibrillin-1 to interact with heparin/heparan sulfate, which plays a role in microfibril assembly.	Heparin	156-163	fibrillin 1	Homo sapiens	127-138
2909522-6	1989	Such units were present in small, intermediate-sized as well as large fragments, suggesting that the antithrombin-binding regions were randomly distributed along the heparin chains.	Heparin	166-173	serpin family C member 1	Homo sapiens	101-113
19661062-0	2009	The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.	Heparin	51-58	serpin family C member 1	Homo sapiens	103-115
2909522-8	1989	The molecular weight distributions of such labeled LA-fragments, determined by gel chromatography, again conformed to a random distribution of the antithrombin-binding sequence within the heparin chains.	Heparin	188-195	serpin family C member 1	Homo sapiens	147-159
19661062-1	2009	Heparin and heparan sulfate glycosaminoglycans allosterically activate the serpin, antithrombin, by binding through a specific pentasaccharide sequence containing a critical 3-O-sulfo group.	Heparin	0-7	serpin family C member 1	Homo sapiens	83-95
2909522-15	1989	263, 262-266) which suggest that the antithrombin-binding region is preferentially located at the nonreducing terminus of the heparin molecule.	Heparin	126-133	serpin family C member 1	Homo sapiens	37-49
2786690-4	1989	Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex).	Heparin	118-125	serpin family C member 1	Homo sapiens	79-84
21496084-10	2011	The addition of heparin significantly reduced levels of IGF-1, TNF-alpha and TGF-beta, and significantly elevated levels of IL-1ra.	Heparin	16-23	insulin like growth factor 1	Equus caballus	56-61
2786690-4	1989	Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex).	Heparin	118-125	serpin family C member 1	Homo sapiens	112-117
22477517-1	2009	The unusual clinical presentation, importance of imaging techniques and role of low molecular weight heparin are described for an initial treatment of thrombosis in inferior vena cava agenesis associated with heterozygous factor V Leiden.	Heparin	101-108	coagulation factor V	Homo sapiens	222-237
2786690-4	1989	Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex).	Heparin	118-125	serpin family C member 1	Homo sapiens	112-117
19690236-1	2009	BACKGROUND: Low antithrombin levels may compromise the anticoagulant effect of heparin and heparin-related compounds, such as fondaparinux.	Heparin	79-86	serpin family C member 1	Homo sapiens	16-28
19690236-1	2009	BACKGROUND: Low antithrombin levels may compromise the anticoagulant effect of heparin and heparin-related compounds, such as fondaparinux.	Heparin	91-98	serpin family C member 1	Homo sapiens	16-28
21769943-0	2011	Effects of glycosylation on heparin binding and antithrombin activation by heparin.	Heparin	75-82	serpin family C member 1	Homo sapiens	48-60
21769943-1	2011	Antithrombin (AT), a serine protease inhibitor, circulates in blood in two major isoforms, alpha and beta, which differ in their amount of glycosylation and affinity for heparin.	Heparin	170-177	serpin family C member 1	Homo sapiens	0-12
21769943-1	2011	Antithrombin (AT), a serine protease inhibitor, circulates in blood in two major isoforms, alpha and beta, which differ in their amount of glycosylation and affinity for heparin.	Heparin	170-177	serpin family C member 1	Homo sapiens	14-16
21769943-3	2011	In this process, beta-AT presents the higher affinity for heparin, being suggested as the major AT glycoform inhibitor in vivo.	Heparin	58-65	serpin family C member 1	Homo sapiens	22-24
21769943-3	2011	In this process, beta-AT presents the higher affinity for heparin, being suggested as the major AT glycoform inhibitor in vivo.	Heparin	58-65	serpin family C member 1	Homo sapiens	96-98
21769943-4	2011	However, either the molecular basis demonstrating the differences in heparin binding to both AT isoforms or the mechanism of its conformational activation are not fully understood.	Heparin	69-76	serpin family C member 1	Homo sapiens	93-95
21769943-5	2011	Thus, the present work evaluated the effects of glycosylation and heparin binding on AT structure, function, and dynamics.	Heparin	66-73	serpin family C member 1	Homo sapiens	85-87
21769943-7	2011	Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT.	Heparin	75-82	serpin family C member 1	Homo sapiens	64-66
19664058-8	2009	Heparin was also an effective co-factor for inhibition of FSAP by plasminogen activator inhibitor 1 (PAI-1) and antithrombin, whereas polyphosphate served as co-factor for the inhibition of FSAP by PAI-1 only.	Heparin	0-7	serpin family E member 1	Homo sapiens	66-99
21769943-7	2011	Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT.	Heparin	75-82	serpin family C member 1	Homo sapiens	176-178
2786690-4	1989	Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex).	Heparin	235-242	serpin family C member 1	Homo sapiens	79-84
21769943-9	2011	Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation.	Heparin	50-57	serpin family C member 1	Homo sapiens	72-74
21769943-9	2011	Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation.	Heparin	50-57	serpin family C member 1	Homo sapiens	188-190
19664058-8	2009	Heparin was also an effective co-factor for inhibition of FSAP by plasminogen activator inhibitor 1 (PAI-1) and antithrombin, whereas polyphosphate served as co-factor for the inhibition of FSAP by PAI-1 only.	Heparin	0-7	serpin family E member 1	Homo sapiens	101-106
19664058-8	2009	Heparin was also an effective co-factor for inhibition of FSAP by plasminogen activator inhibitor 1 (PAI-1) and antithrombin, whereas polyphosphate served as co-factor for the inhibition of FSAP by PAI-1 only.	Heparin	0-7	serpin family C member 1	Homo sapiens	112-124
19664058-8	2009	Heparin was also an effective co-factor for inhibition of FSAP by plasminogen activator inhibitor 1 (PAI-1) and antithrombin, whereas polyphosphate served as co-factor for the inhibition of FSAP by PAI-1 only.	Heparin	0-7	serpin family E member 1	Homo sapiens	198-203
21769943-9	2011	Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation.	Heparin	168-175	serpin family C member 1	Homo sapiens	72-74
2786690-4	1989	Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex).	Heparin	235-242	serpin family C member 1	Homo sapiens	112-117
2786690-4	1989	Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex).	Heparin	235-242	serpin family C member 1	Homo sapiens	112-117
2786690-6	1989	The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex.	Heparin	20-27	serpin family C member 1	Homo sapiens	79-84
2786690-6	1989	The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex.	Heparin	20-27	serpin family C member 1	Homo sapiens	196-201
21866614-20	2004	UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide.	Heparin	0-3	serpin family C member 1	Homo sapiens	87-103
19597879-9	2009	CONCLUSIONS: Heparin responsiveness during CPB was significantly reduced in the IE group, and it seems to be associated with preoperative hypercoagulability and reduced antithrombin III activity.	Heparin	13-20	serpin family C member 1	Homo sapiens	169-185
2786690-6	1989	The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex.	Heparin	202-209	serpin family C member 1	Homo sapiens	79-84
2786690-6	1989	The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex.	Heparin	202-209	serpin family C member 1	Homo sapiens	196-201
19706524-5	2009	We show that betaKlotho was essential for FGF19 interaction with FGFRs 1c, 2c, and 3c, but FGF19 was able to interact directly with FGFR4 in the absence of betaKlotho in a heparin-dependent manner.	Heparin	172-179	fibroblast growth factor 15	Mus musculus	91-96
2920011-4	1989	Association rate constants of both gdN and antithrombin III with alpha-thrombin were obtained using unfractionated, low- and high-affinity heparin types.	Heparin	139-146	serpin family E member 2	Homo sapiens	35-38
19172319-6	2009	The modeled structure also shows specific structural differences between AT3 and ZPI in the heparin-binding and flexible N-terminal tail regions.	Heparin	92-99	serpin family C member 1	Homo sapiens	73-76
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	15-22	serpin family C member 1	Homo sapiens	38-50
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	24-27	serpin family C member 1	Homo sapiens	38-50
21416466-2	2011	A new method to follow loss in heparin binding to the serine protease inhibitor, antithrombin III, and the serine protease, thrombin, was developed using a surface plasmon resonance competitive binding assay.	Heparin	31-38	serpin family C member 1	Homo sapiens	81-97
21416466-6	2011	It is this sulfo group loss that probably accounts for a decrease in the binding of autoclaved heparin to antithrombin III and thrombin as well as the observed decrease in its amidolytic activity.	Heparin	95-102	serpin family C member 1	Homo sapiens	106-122
21873163-2	2011	Recently, we showed that heparin-binding epidermal growth factor-like growth factor (HB-EGF), a member of the EGF family, is a promising target for the treatment of various types of cancer.	Heparin	25-32	heparin binding EGF like growth factor	Homo sapiens	85-91
2920011-4	1989	Association rate constants of both gdN and antithrombin III with alpha-thrombin were obtained using unfractionated, low- and high-affinity heparin types.	Heparin	139-146	serpin family C member 1	Homo sapiens	43-59
2917133-4	1989	The antithrombin was isolated by heparin Sepharose affinity chromatography.	Heparin	33-40	serpin family C member 1	Homo sapiens	4-16
21296829-0	2011	Suppression of choroidal neovascularization and quantitative and qualitative inhibition of VEGF and CCL2 by heparin.	Heparin	108-115	C-C motif chemokine ligand 2	Homo sapiens	100-104
21296829-9	2011	Relative decreases in VEGF and CCL2 levels were observed in media of ARPE19 cells at higher heparin concentrations.	Heparin	92-99	C-C motif chemokine ligand 2	Homo sapiens	31-35
21296829-12	2011	Reduced VEGF and CCL2 secretion by RPE cells and suppression of VEGF-VEGFR2 and CCL2-CCR2 interactions at the laser site mediated by heparin may contribute to the pharmacologic effect.	Heparin	133-140	C-C motif chemokine ligand 2	Homo sapiens	80-84
19442507-2	2009	A mutant of GBP was labelled with badan near the binding site, the protein adsorbed to microparticles of CaCO(3) as templates and encapsulated in alternating nano-layers of poly-L-lysine and heparin.	Heparin	191-198	transmembrane protein 132A	Homo sapiens	12-15
2483705-6	1989	The assay is based on the inactivation of factor Xa by antithrombin III which is catalysed by heparin or smaller fragments of it.	Heparin	94-101	serpin family C member 1	Homo sapiens	55-71
19371327-4	2009	Given the complex nature of cell-surface and extracellular matrix glycan structures, this therapeutic site has been neglected for a long time, the only exception being the antithrombin III-glycan interaction which has been successfully targeted by unfractionated and low-molecular weight heparins for many decades.	Heparin	288-296	serpin family C member 1	Homo sapiens	172-188
2483706-0	1989	A new AT III-heparin-complex preparation: in vitro and in vivo characterisation.	Heparin	13-20	serpin family C member 1	Homo sapiens	6-12
21277398-4	2011	Antithrombin (AT) uptake was measured before and after selectively destroying the active pentasaccharide sequence of the heparin moiety, and was found to be predominantly through the active sequence on all of the surfaces.	Heparin	121-128	serpin family C member 1	Homo sapiens	0-12
2483706-1	1989	The in vitro experiments show that the anticoagulant affect of a new AT III-Heparin-complex preparation in plasma is similar to heparin.	Heparin	76-83	serpin family C member 1	Homo sapiens	69-75
2483706-1	1989	The in vitro experiments show that the anticoagulant affect of a new AT III-Heparin-complex preparation in plasma is similar to heparin.	Heparin	128-135	serpin family C member 1	Homo sapiens	69-75
19473011-1	2009	D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized.	Heparin	110-117	serpin family C member 1	Homo sapiens	70-82
2708007-4	1989	3H-heparin binding to peptide F-9 was specific as determined by competition with excess unlabeled heparin, dextran sulfate, and dermatan sulfate.	Heparin	3-10	coagulation factor IX	Mus musculus	30-33
19359419-0	2009	Rat and human HARE/stabilin-2 are clearance receptors for high- and low-molecular-weight heparins.	Heparin	89-97	stabilin 2	Homo sapiens	14-18
19359419-0	2009	Rat and human HARE/stabilin-2 are clearance receptors for high- and low-molecular-weight heparins.	Heparin	89-97	stabilin 2	Homo sapiens	19-29
19359419-1	2009	The human hyaluronic acid (HA) receptor for endocytosis (HARE/stabilin-2) is the primary clearance receptor for systemic HA, chondroitin sulfates, and heparin, but not for heparan sulfate or keratan sulfate (Harris EN, Weigel JA, Weigel PH.	Heparin	151-158	lymphatic vessel endothelial hyaluronan receptor 1	Homo sapiens	10-39
19359419-1	2009	The human hyaluronic acid (HA) receptor for endocytosis (HARE/stabilin-2) is the primary clearance receptor for systemic HA, chondroitin sulfates, and heparin, but not for heparan sulfate or keratan sulfate (Harris EN, Weigel JA, Weigel PH.	Heparin	151-158	stabilin 2	Homo sapiens	57-61
19359419-1	2009	The human hyaluronic acid (HA) receptor for endocytosis (HARE/stabilin-2) is the primary clearance receptor for systemic HA, chondroitin sulfates, and heparin, but not for heparan sulfate or keratan sulfate (Harris EN, Weigel JA, Weigel PH.	Heparin	151-158	stabilin 2	Homo sapiens	62-72
21418450-5	2011	The soluble HB-EGF in culture media was measured by heparin agarose chromatography/Western blot analysis.	Heparin	52-59	heparin binding EGF like growth factor	Homo sapiens	12-18
21348501-0	2011	Heparin binds 8 kDa gelsolin cross-beta-sheet oligomers and accelerates amyloidogenesis by hastening fibril extension.	Heparin	0-7	gelsolin	Homo sapiens	20-28
2708007-4	1989	3H-heparin binding to peptide F-9 was specific as determined by competition with excess unlabeled heparin, dextran sulfate, and dermatan sulfate.	Heparin	98-105	coagulation factor IX	Mus musculus	30-33
3265623-1	1988	The effect of various well-characterized heparin preparations on the inactivation of human Factor XIa by human antithrombin III was studied.	Heparin	41-48	serpin family C member 1	Homo sapiens	111-127
21348501-5	2011	In contrast, 8 kDa gelsolin cross-beta-sheet oligomers and amyloid fibrils bind strongly to heparin, apparently because of electrostatic interactions between the negatively charged polysaccharide and a positively charged region of the 8 kDa gelsolin assemblies.	Heparin	92-99	gelsolin	Homo sapiens	19-27
21348501-5	2011	In contrast, 8 kDa gelsolin cross-beta-sheet oligomers and amyloid fibrils bind strongly to heparin, apparently because of electrostatic interactions between the negatively charged polysaccharide and a positively charged region of the 8 kDa gelsolin assemblies.	Heparin	92-99	gelsolin	Homo sapiens	241-249
21348501-7	2011	Notably, heparin decreases the 8 kDa gelsolin concentration necessary for amyloid fibril formation, likely a consequence of fibril stabilization through heparin binding.	Heparin	9-16	gelsolin	Homo sapiens	37-45
21348501-7	2011	Notably, heparin decreases the 8 kDa gelsolin concentration necessary for amyloid fibril formation, likely a consequence of fibril stabilization through heparin binding.	Heparin	153-160	gelsolin	Homo sapiens	37-45
21348501-9	2011	The addition of GAG mimetics, small molecule sulfonates shown to reduce the amyloid load in animal models of amyloidosis, to a heparin-accelerated 8 kDa gelsolin aggregation reaction mixture neither significantly alters the rate of amyloidogenesis nor prevents oligomers from binding to GAGs, calling into question their commonly accepted mechanism.	Heparin	127-134	gelsolin	Homo sapiens	153-161
21365655-4	2011	The effect of the ionic strength, temperature, and conformation of the protein on the interaction between beta2gpI and heparin has been studied.	Heparin	119-126	apolipoprotein H	Homo sapiens	106-114
21365655-9	2011	We found that (i) the K(D)-values differed by a factor of 60 at the ionic strengths studied (ii) beta2gpI was resistant to denaturation with SDS and ACN, but was partially denatured by urea, and (iii) the K(D) for the beta2gpI-heparin interaction in the presence of urea was ten times higher than the K(D) determined at the same conditions without urea added.	Heparin	227-234	apolipoprotein H	Homo sapiens	97-105
18996625-1	2009	Antithrombin, a plasma glycoprotein serpin, requires conformational activation by heparin to induce an anticoagulant effect, which is mediated through accelerated factor Xa inhibition.	Heparin	82-89	serpin family C member 1	Homo sapiens	0-12
19377079-12	2009	CONCLUSIONS: Our data indicate that LPS-stimulated monocytes inhibit fibrinolysis through a tissue factor-mediated enhancement of thrombin activatable fibrinolysis inhibitor activation and make clots resistant to the profibrinolytic activity of heparins, thus providing an additional mechanism whereby tissue factor-expressing monocytes/macrophages may favor fibrin accumulation and diminish the antithrombotic efficacy of heparins.	Heparin	245-253	coagulation factor III, tissue factor	Homo sapiens	92-105
19377079-12	2009	CONCLUSIONS: Our data indicate that LPS-stimulated monocytes inhibit fibrinolysis through a tissue factor-mediated enhancement of thrombin activatable fibrinolysis inhibitor activation and make clots resistant to the profibrinolytic activity of heparins, thus providing an additional mechanism whereby tissue factor-expressing monocytes/macrophages may favor fibrin accumulation and diminish the antithrombotic efficacy of heparins.	Heparin	423-431	coagulation factor III, tissue factor	Homo sapiens	92-105
19509548-3	2009	In the present study, we demonstrated that chemically modified nonanticoagulation heparin derivate (periodate-oxidized, borohydride-reduced heparin [RO-heparin]) can inhibit the binding of L-selectin to HO-8910 cells, block the adhering of HO-8910 to Chinese hamster ovary cells expressing a transfected human L-selectin complementary DNA, and affect the interactions of neutrophils with HO-8910 cells.	Heparin	140-147	selectin L	Homo sapiens	189-199
19509548-3	2009	In the present study, we demonstrated that chemically modified nonanticoagulation heparin derivate (periodate-oxidized, borohydride-reduced heparin [RO-heparin]) can inhibit the binding of L-selectin to HO-8910 cells, block the adhering of HO-8910 to Chinese hamster ovary cells expressing a transfected human L-selectin complementary DNA, and affect the interactions of neutrophils with HO-8910 cells.	Heparin	140-147	selectin L	Homo sapiens	310-320
21365655-10	2011	Therefore, we conclude that the interaction between beta2gpI and heparin is dependent on electrostatic interactions and on the conformation of beta2gpI.	Heparin	65-72	apolipoprotein H	Homo sapiens	52-60
21349432-7	2011	In contrast, heparin and activated mast cells induced excessive edema in mice deficient in the major inhibitor of factor XII, C1 esterase inhibitor.	Heparin	13-20	serine (or cysteine) peptidase inhibitor, clade G, member 1	Mus musculus	126-147
19509548-3	2009	In the present study, we demonstrated that chemically modified nonanticoagulation heparin derivate (periodate-oxidized, borohydride-reduced heparin [RO-heparin]) can inhibit the binding of L-selectin to HO-8910 cells, block the adhering of HO-8910 to Chinese hamster ovary cells expressing a transfected human L-selectin complementary DNA, and affect the interactions of neutrophils with HO-8910 cells.	Heparin	140-147	selectin L	Homo sapiens	189-199
3265623-4	1988	Enhancement of the rate of inhibition of Factor XIa in the presence of unfractionated heparin correlated to the binding of antithrombin III to heparin.	Heparin	86-93	serpin family C member 1	Homo sapiens	123-139
19509548-3	2009	In the present study, we demonstrated that chemically modified nonanticoagulation heparin derivate (periodate-oxidized, borohydride-reduced heparin [RO-heparin]) can inhibit the binding of L-selectin to HO-8910 cells, block the adhering of HO-8910 to Chinese hamster ovary cells expressing a transfected human L-selectin complementary DNA, and affect the interactions of neutrophils with HO-8910 cells.	Heparin	140-147	selectin L	Homo sapiens	310-320
3265623-4	1988	Enhancement of the rate of inhibition of Factor XIa in the presence of unfractionated heparin correlated to the binding of antithrombin III to heparin.	Heparin	143-150	serpin family C member 1	Homo sapiens	123-139
3265623-7	1988	The rate enhancement achieved in the presence of each of the heparin fractions could also be correlated to the binding of antithrombin III to the heparin.	Heparin	61-68	serpin family C member 1	Homo sapiens	122-138
20129923-1	2011	N-Deacetylase-N-sulfotransferase 1 (Ndst1) catalyzes the initial modification of heparan sulfate and heparin during their biosynthesis by removal of acetyl groups from subsets of N-acetylglucosamine units and subsequent sulfation of the resulting free amino groups.	Heparin	101-108	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	0-34
3265623-8	1988	The binding constant inferred from the kinetic data varied from 0.10 to 0.28 microM and the number of binding sites for antithrombin III varied from 0.06 to 0.74 site per heparin molecule.	Heparin	171-178	serpin family C member 1	Homo sapiens	120-136
20129923-1	2011	N-Deacetylase-N-sulfotransferase 1 (Ndst1) catalyzes the initial modification of heparan sulfate and heparin during their biosynthesis by removal of acetyl groups from subsets of N-acetylglucosamine units and subsequent sulfation of the resulting free amino groups.	Heparin	101-108	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	36-41
3232125-1	1988	Previous theoretical and experimental evidence led to the formulation of a specific pentasaccharide structure which represents the site in heparin for binding to antithrombin III.	Heparin	139-146	serpin family C member 1	Homo sapiens	162-178
19320820-2	2009	OBJECTIVES: The purpose of this study was to investigate the mechanism of the intracellular signaling activities of AT using wild-type and mutant serpins that have reduced anticoagulant activities due to mutations in either the reactive center loop (RCL) or the heparin-binding site.	Heparin	262-269	serpin family C member 1	Homo sapiens	116-118
2973992-4	1988	From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present.	Heparin	332-339	serpin family C member 1	Homo sapiens	214-219
19320820-7	2009	The heparin-binding site mutants, AT-K114E and AT-K125E, did not exhibit any protective activity in either one of these assays, but a potent pro-apoptotic activity was observed for the AT-K114E in endothelial cells.	Heparin	4-11	serpin family C member 1	Homo sapiens	34-36
20964615-14	2011	Different anticoagulants all have the improvement roles on placental fibrin depositions, but heparin and high-dose danshensu"s roles on lowering thrombomodulin expression in placentas are superior to low-dose danshensu and aspirin.	Heparin	93-100	thrombomodulin	Mus musculus	145-159
20816747-0	2010	Kinetic evidence that allosteric activation of antithrombin by heparin is mediated by two sequential conformational changes.	Heparin	63-70	serpin family C member 1	Homo sapiens	47-59
20816747-1	2010	The serpin, antithrombin, requires allosteric activation by a sequence-specific pentasaccharide unit of heparin or heparan sulfate glycosaminoglycans to function as an anticoagulant regulator of blood clotting proteases.	Heparin	104-111	serpin family C member 1	Homo sapiens	12-24
20816747-2	2010	Surprisingly, X-ray structures have shown that the pentasaccharide produces similar induced-fit changes in the heparin binding site of native and latent antithrombin despite large differences in the heparin affinity and global conformation of these two forms.	Heparin	111-118	serpin family C member 1	Homo sapiens	153-165
21204288-3	2010	The anticoagulative effect of heparin is a result of the binding of heparin to the plasma protein antithrombin III and the subsequent inactivation of blood clotting factors (e.g. factor IIa, IXa, Xa, XIa, XIIa).	Heparin	30-37	serpin family C member 1	Homo sapiens	98-114
21204288-3	2010	The anticoagulative effect of heparin is a result of the binding of heparin to the plasma protein antithrombin III and the subsequent inactivation of blood clotting factors (e.g. factor IIa, IXa, Xa, XIa, XIIa).	Heparin	68-75	serpin family C member 1	Homo sapiens	98-114
19299468-7	2009	Exogenous heparin can rescue both the BMP signaling and BMP internalization abnormalities in Ndst1(-/-) lung.	Heparin	10-17	N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1	Mus musculus	93-98
3191150-3	1988	These rat urinary fibronectin-related substances (RUF) were adsorbed on heparin-immobilized gel but hardly at all on gelatin-immobilized gel.	Heparin	72-79	fibronectin 1	Rattus norvegicus	18-29
19302807-12	2009	SIGNIFICANCE: These results suggest that fucoidan acts like heparin by releasing LPL in addition to increasing the intracellular transport and decreasing the degradation of LPL in the medium.	Heparin	60-67	lipoprotein lipase	Homo sapiens	81-84
19302807-12	2009	SIGNIFICANCE: These results suggest that fucoidan acts like heparin by releasing LPL in addition to increasing the intracellular transport and decreasing the degradation of LPL in the medium.	Heparin	60-67	lipoprotein lipase	Homo sapiens	173-176
20586780-2	2010	OBJECTIVES: To examine the potential role of MMP-7 in shedding of heparin-binding epidermal growth factor-like growth factor (HB-EGF) in RDEB-associated and sporadic SCCs.	Heparin	66-73	matrix metallopeptidase 7	Homo sapiens	45-50
20586780-2	2010	OBJECTIVES: To examine the potential role of MMP-7 in shedding of heparin-binding epidermal growth factor-like growth factor (HB-EGF) in RDEB-associated and sporadic SCCs.	Heparin	66-73	heparin binding EGF like growth factor	Homo sapiens	126-132
3183496-7	1988	Heparin recovery in cord plasma was significantly improved by raising the AT-III concentration to normal adult levels in both assays.	Heparin	0-7	serpin family C member 1	Homo sapiens	74-80
20955273-0	2010	Biocompatibility of heparin-grafted hemodialysis membranes: impact on monocyte chemoattractant protein-1 circulating level and oxidative status.	Heparin	20-27	C-C motif chemokine ligand 2	Homo sapiens	70-104
19026722-3	2009	We have compared the interaction of P-selectin with several low molecular weight polysaccharides: fucoidan, heparin and dextran sulfate.	Heparin	108-115	selectin P	Homo sapiens	36-46
2464199-12	1988	This effect is additional to the heparin-like action of PPS, i.e. potentiation of the activity of antithrombin III and/or heparin cofactor II.	Heparin	33-40	serpin family C member 1	Homo sapiens	98-114
18306296-3	2009	Such an inhibitor is antithrombin, the effect of which may be enhanced with heparin.	Heparin	76-83	serpin family C member 1	Homo sapiens	21-33
20547151-9	2010	However, this form of FN differs from other forms as it does not bind tightly to either gelatin or heparin.	Heparin	99-106	fibronectin 1	Mus musculus	22-24
2464201-10	1988	In the chromogenic substrate assay corn Hageman factor inhibitor (CHFI) inhibited the activation of S-2251 cleaving enzyme by GAGPS, pentosan polysulfate, polyanethol sulfate, heparin, and ribonucleic acid near completely.	Heparin	176-183	trypsin/factor XIIA inhibitor	Zea mays	66-70
20608762-7	2010	RESULTS: Heparin, selenium and platelet-derived growth factor (PDGF)-BB were found to be inhibitory for the growth of hMSC, whereas basic fibroblast growth factor (bFGF) was critical and worked synergistically with transforming growth factor (TGF)-beta1 to allow significant cell expansion.	Heparin	9-16	musculin	Homo sapiens	118-122
19013185-9	2009	In myenteric neurons cultured without mast cells the PAR(2) agonist SLIGRL-amide, prostaglandin D(2) and interleukin (IL) 6 reduced neuronal survival while histamine, serotonin, heparin, IL1beta and tumour necrosis factor alpha had no effect; corticosteroid and VIP enhanced neuronal survival.	Heparin	178-185	F2R like trypsin receptor 1	Rattus norvegicus	53-59
3218731-0	1988	Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin.	Heparin	33-41	serpin family C member 1	Homo sapiens	115-131
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	255-262	serpin family C member 1	Homo sapiens	47-52
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	255-262	serpin family C member 1	Homo sapiens	107-112
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	255-262	serpin family C member 1	Homo sapiens	107-112
19689280-4	2009	On the other side, low molecular weight heparins (LMWHs) are too short to be able to form this ternary complex, and mainly exert their anticoagulant effect by binding the factor Xa, always via ATIII.	Heparin	40-48	serpin family C member 1	Homo sapiens	193-198
19627396-6	2010	Accordingly, the peptide hampers the binding of FGF2 to Chinese Hamster ovary cells overexpressing the tyrosine-kinase FGF receptor-1 (FGFR1) and to recombinant FGFR1 immobilized to a BIAcore sensorchip without affecting heparin interaction.	Heparin	221-228	fibroblast growth factor receptor 1	Cricetulus griseus	135-140
20503388-0	2010	Temporal changes in expression of FoxA1 and Wnt7A in isolated adult human alveolar epithelial cells enhanced by heparin.	Heparin	112-119	forkhead box A1	Homo sapiens	34-39
20503388-0	2010	Temporal changes in expression of FoxA1 and Wnt7A in isolated adult human alveolar epithelial cells enhanced by heparin.	Heparin	112-119	Wnt family member 7A	Homo sapiens	44-49
2976685-4	1988	The tip is cooled by a continuous flow of sterile saline containing dextran 40, heparin and urokinase.	Heparin	80-87	TOR signaling pathway regulator	Homo sapiens	4-7
19309545-0	2010	Endogenous tissue plasminogen activator increases hemorrhagic transformation induced by heparin after ischemia reperfusion in rat brains.	Heparin	88-95	plasminogen activator, tissue type	Rattus norvegicus	11-39
19309545-11	2010	In the heparin group, the expressions of endogenous tPA and MMP-9 obviously increased, while their content and activity had significant differences compared with that of the control group (p&lt;0.01).	Heparin	7-14	plasminogen activator, tissue type	Rattus norvegicus	52-55
19309545-12	2010	CONCLUSION: Endogenous tPA, through enhancement of MMP-9 expression and proteolytic activation, plays an important role in the pathogenesis of hemorrhagic transformation after cerebral reperfusion induced by heparin.	Heparin	208-215	plasminogen activator, tissue type	Rattus norvegicus	23-26
20431847-1	2010	Antithrombin (AT), in the presence of heparin, is able to inhibit the catalytic activity of factor VIIa bound to tissue factor (TF) on cell surfaces.	Heparin	38-45	coagulation factor III, tissue factor	Homo sapiens	113-126
20431847-1	2010	Antithrombin (AT), in the presence of heparin, is able to inhibit the catalytic activity of factor VIIa bound to tissue factor (TF) on cell surfaces.	Heparin	38-45	coagulation factor III, tissue factor	Homo sapiens	128-130
19218109-1	2009	OBJECTIVE: To investigate the expression of heparin-binding epidermal growth factor-like growth factor (HB-EGF) in patients with gastric carcinoma in different stages.	Heparin	44-51	heparin binding EGF like growth factor	Homo sapiens	104-110
19035835-7	2008	This contrasts the interaction with native antithrombin and demonstrates that residues flanking the pentasaccharide sequence of heparin are repelled by the latent and cleaved forms.	Heparin	128-135	serpin family C member 1	Homo sapiens	43-55
19035835-8	2008	These findings contribute to delineating the mechanism by which heparin or heparan sulfate mediates antiangiogenic activity of antithrombin.	Heparin	64-71	serpin family C member 1	Homo sapiens	127-139
18722996-4	2008	This on-chip signal amplification platform was successfully demonstrated by probing the heparin microarray with the highly specific heparin-binding protein antithrombin III (AT III).	Heparin	88-95	serpin family C member 1	Homo sapiens	156-172
20207734-4	2010	In contrast, we report that the NTR domain within PCPE-1 leads to superstimulation of bone morphogenetic protein-1 activity in the presence of heparin and heparan sulfate.	Heparin	143-150	bone morphogenetic protein 1	Homo sapiens	86-114
3174644-3	1988	For example, intestinal brush border membranes containing heparin bind homogeneous human pancreatic 125I-labeled cholesterol esterase (100 kDa) and 125I-labeled triglyceride lipase (52 kDa).	Heparin	58-65	carboxyl ester lipase	Homo sapiens	113-133
19962139-9	2010	RESULT(S): Heparin dose- and time-dependently delayed the production of IGFBP-1 and amplified the levels of PRL and IGF-I in ESCs during decidualization in vitro.	Heparin	11-18	insulin like growth factor binding protein 1	Homo sapiens	72-79
18722996-4	2008	This on-chip signal amplification platform was successfully demonstrated by probing the heparin microarray with the highly specific heparin-binding protein antithrombin III (AT III).	Heparin	88-95	serpin family C member 1	Homo sapiens	174-180
18829766-16	2008	Preincubation of KSHV with soluble heparin and alpha3beta1 significantly inhibited this association, suggesting that the first contact with HS and integrin is an essential element in subsequent CD98-xCT interactions.	Heparin	35-42	solute carrier family 3 member 2	Homo sapiens	194-198
18829766-16	2008	Preincubation of KSHV with soluble heparin and alpha3beta1 significantly inhibited this association, suggesting that the first contact with HS and integrin is an essential element in subsequent CD98-xCT interactions.	Heparin	35-42	solute carrier family 7 member 11	Homo sapiens	199-202
3169232-0	1988	New carbohydrate site in mutant antithrombin (7 Ile----Asn) with decreased heparin affinity.	Heparin	75-82	serpin family C member 1	Homo sapiens	32-44
18708078-4	2008	InsP3R antagonists (heparin, xestospongin C) as well as an inositol monophosphatase inhibitor (LiCl) showed an antidepressant activity of intensity comparable to clinically used antidepressants.	Heparin	20-27	inositol 1,4,5-trisphosphate receptor 1	Mus musculus	0-6
20378948-1	2010	Heparin is a potent anticoagulant agent that interacts strongly with antithrombin III to prevent the formation of fibrin clots.	Heparin	0-7	serpin family C member 1	Homo sapiens	69-85
3056863-0	1988	Beta-2-microglobulin adsorption and release in-vitro: influence of membrane material, osmolality and heparin.	Heparin	101-108	beta-2-microglobulin	Homo sapiens	0-20
20096680-10	2010	We observed maximum reversal of heparin anticoagulation at protamine to heparin ratios of 1.4:1 from TC1 (P=0.6) and 1.2:1 from theta (P=0.55).	Heparin	32-39	transcobalamin 1	Homo sapiens	101-104
20096680-10	2010	We observed maximum reversal of heparin anticoagulation at protamine to heparin ratios of 1.4:1 from TC1 (P=0.6) and 1.2:1 from theta (P=0.55).	Heparin	72-79	transcobalamin 1	Homo sapiens	101-104
3401503-2	1988	A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III).	Heparin	31-38	serpin family C member 1	Homo sapiens	195-211
19132244-12	2008	To our knowledge, this is the first time that heparin is shown to interfere with the VLA-4/VCAM-1 interaction leading to the suggestion of a novel heparin target.	Heparin	46-53	vascular cell adhesion molecule 1	Mus musculus	91-97
19132244-12	2008	To our knowledge, this is the first time that heparin is shown to interfere with the VLA-4/VCAM-1 interaction leading to the suggestion of a novel heparin target.	Heparin	147-154	vascular cell adhesion molecule 1	Mus musculus	91-97
3401503-2	1988	A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III).	Heparin	31-38	serpin family C member 1	Homo sapiens	213-219
3408687-7	1988	Moreover, the unexpectedly normal level of AT III provides a theoretical basis for the use of heparin to enhance the inactivation of those serine proteases present before antivenom administration.	Heparin	94-101	serpin family C member 1	Homo sapiens	43-49
18786816-4	2008	In this study we have coated PET with heparin and show that this decreases PET hydrophobicity and the presence of the fibrinogen P2 epitope on the material surface.	Heparin	38-45	fibrinogen gamma chain	Gallus gallus	118-128
18786816-5	2008	In addition, we show that heparin-induced reduction of PET hydrophobicity correlates with decreased exposure of the fibrinogen P2 epitope and reduced adhesion of monocytes.	Heparin	26-33	fibrinogen gamma chain	Gallus gallus	116-126
20440757-7	2010	Residual particle-extracellular fibronectin matrix binding and 2 degrees transfer can be competitively disrupted by heparin exposure without affecting murine progenitor homing and repopulation.	Heparin	116-123	fibronectin 1	Mus musculus	32-43
20381830-6	2010	The inhibitory effects of F-Q and heparin on thrombin activity were strikingly enhanced by either antithrombin (AT) or heparin cofactor II (HCII).	Heparin	34-41	serpin family D member 1	Rattus norvegicus	119-138
20381830-6	2010	The inhibitory effects of F-Q and heparin on thrombin activity were strikingly enhanced by either antithrombin (AT) or heparin cofactor II (HCII).	Heparin	34-41	serpin family D member 1	Rattus norvegicus	140-144
3391345-7	1988	On the basis of these data, it is concluded that glycosylated antithrombin III with 50% depressed heparin cofactor activity is three times weaker than normal antithrombin III as an inhibitor of thrombin.	Heparin	98-105	serpin family C member 1	Homo sapiens	62-78
20437787-9	2010	In addition, recent studies suggest that children need larger doses of heparin than adults, because they have lower antithrombin levels, and they metabolize heparin more rapidly.	Heparin	71-78	serpin family C member 1	Homo sapiens	116-128
20005946-11	2010	The congenic mouse plasma ecSOD activity before and after heparin administration recapitulates the differences reported in the founder mice.	Heparin	58-65	superoxide dismutase 3, extracellular	Mus musculus	26-31
19959474-5	2010	The presence of heparin accelerated inhibition of cathepsin L by both serpins, and in the case of SCCA-1, heparin increased the second order inhibition rate constant from 5.4 x 10(5) to &gt;10(8), indicating a rate enhancement of at least 180-fold.	Heparin	106-113	serpin family B member 3	Homo sapiens	98-104
19959474-7	2010	Furthermore, SCCA-1 inhibition of cathepsin L-like proteolytic activity secreted from breast and melanoma cancer cell lines was significantly enhanced by heparin.	Heparin	154-161	serpin family B member 3	Homo sapiens	13-19
18950270-4	2008	Using radioiodine labeling, the effect of heparin on the binding of ANG to the scaffold was studied.	Heparin	42-49	angiogenin	Oryctolagus cuniculus	68-71
18669635-1	2008	Fibrillin-1 N- and C-terminal heparin binding sites have been characterized.	Heparin	30-37	fibrillin 1	Homo sapiens	0-11
18669635-5	2008	Within domains encoded by exons 59-62 near the fibrillin-1 C terminus are novel conformation-dependent high affinity heparin and tropoelastin binding sites.	Heparin	117-124	fibrillin 1	Homo sapiens	47-58
18669635-7	2008	Thus, fibrillin-1 N-terminal interactions with heparin/heparan sulfate directly influence cell behavior, whereas C-terminal interactions with heparin/heparan sulfate regulate elastin deposition.	Heparin	47-54	fibrillin 1	Homo sapiens	6-17
18669635-8	2008	These data highlight how heparin/heparan sulfate controls fibrillin-1 interactions.	Heparin	25-32	fibrillin 1	Homo sapiens	58-69
18806070-0	2008	Does preoperative level of antithrombin III predict heparin resistance during extracorporeal circulation?	Heparin	52-59	serpin family C member 1	Homo sapiens	27-43
19900405-1	2010	Heparan sulfate 6-O-endosufatases Sulf1 and Sulf2 hydrolyze the 6-O-sulfate of the glucosamine residues in heparin and heparan sulfate, thereby regulating multiple signaling pathways.	Heparin	107-114	sulfatase 1	Rattus norvegicus	34-39
2455726-5	1988	Here, it is demonstrated that the power of fibronectin to bring about this change in the differentiated properties of the smooth muscle cells resides in a 105-kD cell-binding fragment, whereas a 70-kD collagen-binding fragment and a 31-kD heparin-binding fragment are inactive in this respect.	Heparin	239-246	fibronectin 1	Rattus norvegicus	43-54
20110603-3	2010	These ligands appear to be a powerful tool to tag brain-isolated tau-aggregates and heparin-induced polymers of recombinant tau.	Heparin	84-91	microtubule associated protein tau	Homo sapiens	124-127
18832918-2	2008	Specifically, activated coagulation time values are obtained with devices that utilize contact protein activators to generate thrombin and assess the efficacy of heparin-mediated antithrombin activation, with an activated coagulation time value of 480 s considered "safe".	Heparin	162-169	serpin family C member 1	Homo sapiens	179-191
18758089-1	2008	BACKGROUND: The aim of this analysis was to define the risk factors associated with the problematic dose titration of unfractionated heparin (UFH) in high-risk non-ST-segment elevation acute coronary syndrome (NSTE ACS) patients.	Heparin	133-140	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	215-218
20807641-0	2010	Glucuronyl C5-epimerase an enzyme converting glucuronic acid to iduronic acid in heparan sulfate/heparin biosynthesis.	Heparin	97-104	glucuronyl C5-epimerase	Mus musculus	0-23
3413737-8	1988	This is the first reported ATIII variant in which a molecular abnormality produces a lack of affinity for heparin but no changes in its isoelectric point.	Heparin	106-113	serpin family C member 1	Homo sapiens	27-32
20807641-1	2010	The glucuronyl C5 epimerase (HSepi) is one of the modification enzymes involved in biosynthesis of heparan sulfate (HS) and heparin, catalyzing the epimerization of D-glucuronic acid (GlcA) to L-iduronic acid (IdoA) at polymer level.	Heparin	124-131	glucuronyl C5-epimerase	Mus musculus	4-27
20807641-1	2010	The glucuronyl C5 epimerase (HSepi) is one of the modification enzymes involved in biosynthesis of heparan sulfate (HS) and heparin, catalyzing the epimerization of D-glucuronic acid (GlcA) to L-iduronic acid (IdoA) at polymer level.	Heparin	124-131	glucuronyl C5-epimerase	Mus musculus	29-34
20807641-7	2010	Recombinant HSepi is used to generate HS/heparin related compounds having potential to be used for therapeutic purposes.	Heparin	41-48	glucuronyl C5-epimerase	Mus musculus	12-17
18758089-1	2008	BACKGROUND: The aim of this analysis was to define the risk factors associated with the problematic dose titration of unfractionated heparin (UFH) in high-risk non-ST-segment elevation acute coronary syndrome (NSTE ACS) patients.	Heparin	142-145	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	215-218
18758089-2	2008	METHODS AND RESULTS: The study group comprised 267 patients with high-risk NSTE ACS managed with an early invasive strategy and treated with the recommended dose of UFH.	Heparin	165-168	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	80-83
3284386-2	1988	Our data suggest the presence of two types of binding sites, i.e., heparin-sensitive sites that bind primarily the catalytically active form of the lipase and are present at the endothelium in all blood vessels and heparin-insensitive sites that bind both active and inactive forms and are present only within the sinusoids.	Heparin	67-74	lipase G, endothelial type	Rattus norvegicus	148-154
18321693-10	2008	OD had significantly lower fasting and postprandial adipose tissue heparin-releasable LPL activity than O and C. CONCLUSIONS: In insulin-resistant conditions of obesity, with and without diabetes, large VLDL are increased after a fat-rich meal.	Heparin	67-74	lipoprotein lipase	Homo sapiens	86-89
20196517-9	2010	In cases of resistance to heparin, additional doses of the drug were injected, in combination with plasma or antithrombin in 29% and 12% of the hospitals, respectively.	Heparin	26-33	serpin family C member 1	Homo sapiens	109-121
3284386-2	1988	Our data suggest the presence of two types of binding sites, i.e., heparin-sensitive sites that bind primarily the catalytically active form of the lipase and are present at the endothelium in all blood vessels and heparin-insensitive sites that bind both active and inactive forms and are present only within the sinusoids.	Heparin	215-222	lipase G, endothelial type	Rattus norvegicus	148-154
3355847-11	1988	Heparin-releasable membrane-bound anti-LPL antibody was demonstrated.	Heparin	0-7	lipoprotein lipase	Homo sapiens	39-42
20223119-0	2009	[Recombinant polypeptide of N-terminal heparin-binding domain of fibronectin antagonizes hepatic failure induced by endotoxin in mice].	Heparin	39-46	fibronectin 1	Mus musculus	65-76
20223119-1	2009	OBJECTIVE: To study the preventive effect of recombinant polypeptide of N-terminal heparin-binding domain of fibronectin on hepatic failure induced by endotoxin in mice.	Heparin	83-90	fibronectin 1	Mus musculus	109-120
18593710-6	2008	Analysis of ECP mt1 (R34A/W35A/R36A/K38A) showed that these charged and aromatic residues were involved in ECP binding to heparin and the cell surface.	Heparin	122-129	metallothionein 1I, pseudogene	Homo sapiens	16-19
3400080-4	1988	Our results suggested that heparin-like glycosaminoglycans on endothelial cells play as important a role as heparin does in the regulation of antithrombin activity.	Heparin	27-34	serpin family C member 1	Homo sapiens	142-154
18685429-11	2008	These findings suggest that long-term thromboprophylaxis with low-molecular-weight heparin is associated with a low rate of HPF4-As seroconversion in pregnancy.	Heparin	83-90	zinc finger protein 85	Homo sapiens	124-128
18022801-9	2008	After the heparin was immobilized on the BA-PEG-grafted 316L SS surface by SP, the surface showed an improvement in antithrombrin III (AT III) binding ability, its anticoagulant property, and hemocompatibility in comparison with heparin grafted by 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide.	Heparin	10-17	serpin family C member 1	Homo sapiens	116-133
18022801-9	2008	After the heparin was immobilized on the BA-PEG-grafted 316L SS surface by SP, the surface showed an improvement in antithrombrin III (AT III) binding ability, its anticoagulant property, and hemocompatibility in comparison with heparin grafted by 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide.	Heparin	10-17	serpin family C member 1	Homo sapiens	135-141
18041724-3	2008	The coatings containing heparin were tested for their ability to potentiate thrombin inhibition by antithrombin and its dependence on the layer arrangement.	Heparin	24-31	serpin family C member 1	Homo sapiens	99-111
18449905-6	2008	Further, heparin bound to both BMP-2 and BMP receptor (BMPR).	Heparin	9-16	bone morphogenetic protein 1	Homo sapiens	31-34
18449906-5	2008	Interestingly, heparin induces glycogen synthase kinase-3beta (GSK-3beta) inhibition, beta-catenin stabilization and morphological differentiation in both N2a cells and in rat primary hippocampal neuronal cultures.	Heparin	15-22	glycogen synthase kinase 3 beta	Mus musculus	63-72
19542565-4	2009	ANGPTL4 potently inhibited nonstabilized LPL as well as heparin-stabilized LPL but not GPIHBP1-stabilized LPL.	Heparin	56-63	angiopoietin-like 4	Mus musculus	0-7
19818773-4	2009	We propose a quite different mechanism in which heparin activates antithrombin by mitigating an unfavorable surface interaction, by altering its nature, and by moving the attached proteinase away from the site of the unfavorable interaction through RCL expulsion.	Heparin	48-55	serpin family C member 1	Homo sapiens	66-78
19540231-16	2009	Heparin abolished responses to Vn, IGFBP-5 and non-glycosylated IGFBP-3, but only partially inhibited the response to glycosylated IGFBP-3.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	64-71
19540231-16	2009	Heparin abolished responses to Vn, IGFBP-5 and non-glycosylated IGFBP-3, but only partially inhibited the response to glycosylated IGFBP-3.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	131-138
19888514-4	2009	We recently demonstrated that heparin interferes with the integrin VLA-4 on murine melanoma cells binding to VCAM-1.	Heparin	30-37	vascular cell adhesion molecule 1	Mus musculus	109-115
18565684-13	2008	By regulating the ratio of heparin to BMP, BMP release can be predominantly by gel network biodegradation rather than by simple diffusion.	Heparin	27-34	bone morphogenetic protein 1	Homo sapiens	43-46
3378053-0	1988	Purification of a form of protease nexin 1 that binds heparin with a low affinity.	Heparin	54-61	serpin family E member 2	Homo sapiens	26-42
19888521-0	2009	Structural features of low-molecular-weight heparins affecting their affinity to antithrombin.	Heparin	44-52	serpin family C member 1	Homo sapiens	81-93
3378053-1	1988	A form of protease nexin 1 (PN-1) that binds heparin with a low affinity (L-PN-1) was purified and studies since altered interactions with glycosaminoglycans could affect its inhibition of certain serine proteases.	Heparin	45-52	serpin family E member 2	Homo sapiens	10-26
19555665-4	2009	We found that rNKG2Dlec and rCD94lec bind in a dose-dependent manner to plates coated with heparin-conjugated bovine serum albumin (heparin-BSA).	Heparin	91-98	killer cell lectin like receptor D1	Rattus norvegicus	28-33
3378053-1	1988	A form of protease nexin 1 (PN-1) that binds heparin with a low affinity (L-PN-1) was purified and studies since altered interactions with glycosaminoglycans could affect its inhibition of certain serine proteases.	Heparin	45-52	serpin family E member 2	Homo sapiens	28-32
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	41-48	serpin family E member 2	Homo sapiens	147-151
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	41-48	serpin family E member 2	Homo sapiens	170-174
18499864-4	2008	The human hyaluronan receptor for endocytosis [HARE/Stabilin-2] is a systemic clearance receptor for heparin.	Heparin	101-108	stabilin 2	Homo sapiens	47-51
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	41-48	serpin family E member 2	Homo sapiens	170-174
18499864-4	2008	The human hyaluronan receptor for endocytosis [HARE/Stabilin-2] is a systemic clearance receptor for heparin.	Heparin	101-108	stabilin 2	Homo sapiens	52-62
18499864-10	2008	(125)I-AcLDL binding to HARE was partially competed by Hep and dextran sulfate, but not competed by HA.	Heparin	55-58	stabilin 2	Homo sapiens	24-28
19502598-3	2009	We used surface plasmon resonance assays to characterize interactions between endostatin, integrins, and heparin/heparan sulfate.	Heparin	105-112	collagen type XVIII alpha 1 chain	Homo sapiens	78-88
19502598-5	2009	Two arginine residues (Arg27 and Arg139) are crucial for the binding of endostatin to integrins and to heparin/heparan sulfate, suggesting that endostatin would not bind simultaneously to integrins and to heparan sulfate.	Heparin	103-110	collagen type XVIII alpha 1 chain	Homo sapiens	72-82
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	41-48	serpin family E member 2	Homo sapiens	170-174
19502598-9	2009	The direct binding between integrins and heparin/heparan sulfate might explain why both heparan sulfate and alpha5beta1 integrin are required for the localization of endostatin in endothelial cell lipid rafts.	Heparin	41-48	collagen type XVIII alpha 1 chain	Homo sapiens	166-176
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	147-151
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	170-174
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	170-174
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	72-77
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	72-77
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
19456850-6	2009	Binding of APRIL or TACI-Fc was abrogated by heparin or cell pretreatment with heparitinase, which cleaves heparan sulfate chains.	Heparin	45-52	TNF receptor superfamily member 13B	Homo sapiens	20-24
19468011-1	2009	Aims We examined the specific effects of unfractionated heparin and bivalirudin on thrombin-inducible platelet PAR-1 in patients undergoing percutaneous coronary intervention (PCI).	Heparin	56-63	Prader Willi/Angelman region RNA 1	Homo sapiens	111-116
19708998-4	2009	Further, during each dialysis treatment, the use of heparin (or low molecular weight heparin) induces a release of LPL from its normal binding sites at the plasma membrane of endothelial cells.	Heparin	52-59	lipoprotein lipase	Homo sapiens	115-118
19708998-4	2009	Further, during each dialysis treatment, the use of heparin (or low molecular weight heparin) induces a release of LPL from its normal binding sites at the plasma membrane of endothelial cells.	Heparin	85-92	lipoprotein lipase	Homo sapiens	115-118
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	246-253	chemokine like factor	Homo sapiens	83-88
3378053-5	1988	Studies on activities that depend on the heparin binding domain revealed that heparin equally accelerated the rate of formation of 125I-thrombin-L-PN-1 and 125I-thrombin-PN-1 complexes even when the ratio of heparin to L-PN-1 or PN-1 was varied from 0.01 to 100.	Heparin	78-85	serpin family E member 2	Homo sapiens	170-174
19415899-3	2009	The relative heparin-binding affinity of recombinant laminin alpha chain LG45 proteins was as follows: alpha5 &gt; alpha4 &gt; alpha1 &gt; alpha2 and alpha3.	Heparin	13-20	adrenoceptor alpha 1D	Homo sapiens	127-133
3348170-6	1988	After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference.	Heparin	91-98	serpin family C member 1	Homo sapiens	108-114
18558718-5	2008	Paramagnetic relaxation enhancement (PRE) of (15)N-tau by interaction with MTSL- (14)N-tau allowed identification of low molecular weight oligomers of tau (187) that formed in response to heparin-induced aggregation.	Heparin	188-195	microtubule associated protein tau	Homo sapiens	51-54
18558718-5	2008	Paramagnetic relaxation enhancement (PRE) of (15)N-tau by interaction with MTSL- (14)N-tau allowed identification of low molecular weight oligomers of tau (187) that formed in response to heparin-induced aggregation.	Heparin	188-195	microtubule associated protein tau	Homo sapiens	87-90
18558718-7	2008	We propose that soluble oligomers of tau (187) are generated via intermolecular interactions at these motifs triggered by heparin addition.	Heparin	122-129	microtubule associated protein tau	Homo sapiens	37-40
19533051-5	2009	The main clinically relevant situations in which AT-dependent HR occurs, with possible indication of AT substitution, are congenital AT deficiency, asparaginase therapy, disseminated intravascular coagulation (DIC) and administration of high doses of heparin during extracorporeal circulation, where it is significant, due to the need to maintain a very high ACT (&gt; 400 s), that use of heart-lung machines is associated with an HR incidence of approximately 20%.	Heparin	251-258	serpin family C member 1	Homo sapiens	49-51
19533051-8	2009	Under normalized and stable AT activity, the UFH dose should be adjusted such that aPTT is within a range of 60-100 s. If anticoagulation over a longer term is indicated, then overlapping anticoagulation with a vitamin K antagonist should be started as quickly as possible.	Heparin	45-48	serpin family C member 1	Homo sapiens	28-30
19359419-6	2009	In this study, we demonstrate that anti-HARE antibodies specifically block the uptake of LMWH and UFH by isolated rat liver SECs and by human 293 cells expressing recombinant human HARE (hHARE).	Heparin	98-101	stabilin 2	Homo sapiens	181-185
19359419-10	2009	We conclude that both UFH and LMWH are cleared by HARE/Stab2 and that the differences in the affinities of HARE binding to LMWH and UFH likely explain the longer in vivo circulating half-life of LMWH compared with UFH.	Heparin	22-25	stabilin 2	Homo sapiens	50-54
19359419-10	2009	We conclude that both UFH and LMWH are cleared by HARE/Stab2 and that the differences in the affinities of HARE binding to LMWH and UFH likely explain the longer in vivo circulating half-life of LMWH compared with UFH.	Heparin	22-25	stabilin 2	Homo sapiens	55-60
19359419-10	2009	We conclude that both UFH and LMWH are cleared by HARE/Stab2 and that the differences in the affinities of HARE binding to LMWH and UFH likely explain the longer in vivo circulating half-life of LMWH compared with UFH.	Heparin	22-25	stabilin 2	Homo sapiens	107-111
19359419-10	2009	We conclude that both UFH and LMWH are cleared by HARE/Stab2 and that the differences in the affinities of HARE binding to LMWH and UFH likely explain the longer in vivo circulating half-life of LMWH compared with UFH.	Heparin	132-135	stabilin 2	Homo sapiens	107-111
19359419-10	2009	We conclude that both UFH and LMWH are cleared by HARE/Stab2 and that the differences in the affinities of HARE binding to LMWH and UFH likely explain the longer in vivo circulating half-life of LMWH compared with UFH.	Heparin	132-135	stabilin 2	Homo sapiens	107-111
18467328-11	2008	Instead, PLP-J interacts with heparin-containing molecules, including syndecan-1, which is expressed in gestation day 8.5 pregnant uteri, as well as in uterine stromal cells and endothelial cells.	Heparin	30-37	syndecan 1	Rattus norvegicus	70-80
19086324-8	2008	CONCLUSIONS: The anti-inflammatory mechanisms of heparin in ALI may be inhibiting p38 MAPK and NF-kappaB activities, and then TNF-alpha overexpression, thus alleviating the inflammatory reaction.	Heparin	49-56	tumor necrosis factor	Oryctolagus cuniculus	126-135
19254961-2	2009	Exogenous heparin polymer and some octasaccharides inhibited FGF-2-induced phosphorylation both of FGFR-1 and of extracellular signal-regulated kinase (ERK1/2) in Chinese hamster ovary (CHO)-K1 cells transfected with FGFR-1, which present HS on their cell surface.	Heparin	10-17	fibroblast growth factor receptor 1	Cricetulus griseus	99-105
3422166-8	1988	Antithrombin III alpha alone had no effect, but antithrombin III alpha with heparin abrogated the TF inhibition.	Heparin	76-83	coagulation factor III, tissue factor	Homo sapiens	98-100
19254961-2	2009	Exogenous heparin polymer and some octasaccharides inhibited FGF-2-induced phosphorylation both of FGFR-1 and of extracellular signal-regulated kinase (ERK1/2) in Chinese hamster ovary (CHO)-K1 cells transfected with FGFR-1, which present HS on their cell surface.	Heparin	10-17	fibroblast growth factor receptor 1	Cricetulus griseus	217-223
19377079-0	2009	Tissue factor-expressing monocytes inhibit fibrinolysis through a TAFI-mediated mechanism, and make clots resistant to heparins.	Heparin	119-127	coagulation factor III, tissue factor	Homo sapiens	0-13
19377079-11	2009	Finally, the profibrinolytic effect of unfractionated heparin and enoxaparin was markedly lower (approximately 50%) in the presence of LPS-MNC than in the presence of a thromboplastin preparation displaying an identical tissue factor activity.	Heparin	54-61	coagulation factor III, tissue factor	Homo sapiens	220-233
18454939-2	2008	We believe the cause of the elevation is mainly due to a temporary depletion of lipoprotein lipase caused by heparin.	Heparin	109-116	lipoprotein lipase	Homo sapiens	80-98
2963012-6	1988	Binding via the cell surface PG was to the COOH-terminal heparin binding domain of fibronectin.	Heparin	57-64	fibronectin 1	Mus musculus	83-94
18413297-3	2008	Thrombin cleavage of OPN was inhibited by unsulfated hirugen (IC(50) = 1.2 +/- 0.2 microm), unfractionated heparin (IC(50) = 56.6 +/- 8.4 microg/ml) and low molecular weight (5 kDa) heparin (IC(50) = 31.0 +/- 7.9 microg/ml), indicating the involvement of both anion-binding exosite I (ABE-I) and anion-binding exosite II (ABE-II).	Heparin	107-114	secreted phosphoprotein 1	Homo sapiens	21-24
18413297-3	2008	Thrombin cleavage of OPN was inhibited by unsulfated hirugen (IC(50) = 1.2 +/- 0.2 microm), unfractionated heparin (IC(50) = 56.6 +/- 8.4 microg/ml) and low molecular weight (5 kDa) heparin (IC(50) = 31.0 +/- 7.9 microg/ml), indicating the involvement of both anion-binding exosite I (ABE-I) and anion-binding exosite II (ABE-II).	Heparin	182-189	secreted phosphoprotein 1	Homo sapiens	21-24
19284310-7	2009	We identified two aptamers, WT-15 and SM-20, that disrupt the interactions between PAI-1 and heparin, as well as PAI-1 and vitronectin, without affecting the antiprotease activity of PAI-1.	Heparin	93-100	serpin family E member 1	Homo sapiens	83-88
19500510-7	2009	There are significant positive correlation between TF or PAI-1 secretion of HUVEC and corresponding serum TNFalpha level in the group without heparin, the coefficient correlation is 0.902 and 0.939(P&lt;0.05)respectively.	Heparin	142-149	serpin family E member 1	Homo sapiens	57-62
2963012-9	1988	These results indicate that the mammary epithelial cells have at least two distinct cell surface receptors for fibronectin: a trypsin-resistant molecule that binds cells to the sequence RGD and a trypsin-labile, heparan sulfate-rich PG that binds cells to the COOH-terminal heparin binding domain.	Heparin	274-281	fibronectin 1	Mus musculus	111-122
19509548-0	2009	Chemically modified heparin inhibits in vitro L-selectin-mediated human ovarian carcinoma cell adhesion.	Heparin	20-27	selectin L	Homo sapiens	46-56
19509548-3	2009	In the present study, we demonstrated that chemically modified nonanticoagulation heparin derivate (periodate-oxidized, borohydride-reduced heparin [RO-heparin]) can inhibit the binding of L-selectin to HO-8910 cells, block the adhering of HO-8910 to Chinese hamster ovary cells expressing a transfected human L-selectin complementary DNA, and affect the interactions of neutrophils with HO-8910 cells.	Heparin	82-89	selectin L	Homo sapiens	189-199
18541909-4	2008	Diffusion measurements in free solution, supported by confocal imaging and binding assays with cultured cells, were used to characterize the properties of a fluorescently labeled protein, lactoferrin (Lf), and its association with heparin and heparan sulfate in vitro.	Heparin	231-238	lactotransferrin	Rattus norvegicus	188-199
18541909-4	2008	Diffusion measurements in free solution, supported by confocal imaging and binding assays with cultured cells, were used to characterize the properties of a fluorescently labeled protein, lactoferrin (Lf), and its association with heparin and heparan sulfate in vitro.	Heparin	231-238	lactotransferrin	Rattus norvegicus	201-203
19509548-3	2009	In the present study, we demonstrated that chemically modified nonanticoagulation heparin derivate (periodate-oxidized, borohydride-reduced heparin [RO-heparin]) can inhibit the binding of L-selectin to HO-8910 cells, block the adhering of HO-8910 to Chinese hamster ovary cells expressing a transfected human L-selectin complementary DNA, and affect the interactions of neutrophils with HO-8910 cells.	Heparin	82-89	selectin L	Homo sapiens	310-320
18498854-1	2008	Heparin resistance occurs in up to 22% of patients undergoing cardiac surgery requiring cardiopulmonary bypass and it is associated with decreased levels of antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	157-169
18498854-2	2008	Treatment options for heparin resistance include administration of antithrombin or fresh frozen plasma.	Heparin	22-29	serpin family C member 1	Homo sapiens	67-79
18498854-4	2008	Thus, the aim of this review is to discuss the limited number of published reports assessing antithrombin or fresh frozen plasma in managing heparin resistance and to present emerging data regarding fresh frozen plasma safety issues and practical considerations for antithrombin treatment in patients with heparin resistance undergoing cardiopulmonary bypass.	Heparin	141-148	serpin family C member 1	Homo sapiens	93-105
3276727-9	1988	IGF-I and a high insulin concentration (70 nM) stimulated only the heparin-releasable (HR) component of LPL activity and immunoreactive mass, and neither IGF-I nor insulin affected LPL specific activity.	Heparin	67-74	lipoprotein lipase	Homo sapiens	104-107
18574277-8	2008	In addition to aspirin and other antiplatelet therapies, we recommend the use of antithrombin therapy (eg, unfractionated heparin (UFH), enoxaparin, or fondaparinux) over no antithrombin therapy (Grade 1A), including for those patients receiving fibrinolysis (and regardless of which lytic agent is administered), primary PCI, or patients not receiving reperfusion therapy.	Heparin	122-129	serpin family C member 1	Homo sapiens	81-93
18574277-8	2008	In addition to aspirin and other antiplatelet therapies, we recommend the use of antithrombin therapy (eg, unfractionated heparin (UFH), enoxaparin, or fondaparinux) over no antithrombin therapy (Grade 1A), including for those patients receiving fibrinolysis (and regardless of which lytic agent is administered), primary PCI, or patients not receiving reperfusion therapy.	Heparin	131-134	serpin family C member 1	Homo sapiens	81-93
19569526-6	2009	We propose that Ingramon might interfere with MCP-1-heparin/heparan sulphate binding on cell surface.	Heparin	52-59	C-C motif chemokine ligand 2	Homo sapiens	46-51
2843005-2	1988	Heparin activates lipoprotein lipase (LPL) and hepatic lipase (HL), enhances plasma lipolytic activity and elevates plasma levels of free fatty acids (FFA).	Heparin	0-7	lipoprotein lipase	Homo sapiens	18-36
19167525-2	2009	Recombinant rat Protease Nexin-1 (rPN-1) was efficiently produced in Escherichia coli using a T7 RNA polymerase based expression system and purified by heparin-sepharose affinity chromatography yielding 3 mg of protein per liter of cell culture.	Heparin	152-159	serpin family E member 2	Rattus norvegicus	16-32
2843005-2	1988	Heparin activates lipoprotein lipase (LPL) and hepatic lipase (HL), enhances plasma lipolytic activity and elevates plasma levels of free fatty acids (FFA).	Heparin	0-7	lipoprotein lipase	Homo sapiens	38-41
19167525-2	2009	Recombinant rat Protease Nexin-1 (rPN-1) was efficiently produced in Escherichia coli using a T7 RNA polymerase based expression system and purified by heparin-sepharose affinity chromatography yielding 3 mg of protein per liter of cell culture.	Heparin	152-159	serpin family E member 2	Rattus norvegicus	34-39
19167525-5	2009	Fluorescence titration of rPN-1 with heparin indicated that rPN-1 binds heparin with high affinity.	Heparin	37-44	serpin family E member 2	Rattus norvegicus	26-31
18520877-14	2008	Heparin in complex with chitosan has the ability to stabilize or activate the growth factor in vivo and induce the generation of new bone in good yields.	Heparin	0-7	myotrophin	Rattus norvegicus	78-91
2843005-16	1988	The complex-binding between heparin and LPL is dependent on the degree of sulphation or ionic strength of the heparin.	Heparin	28-35	lipoprotein lipase	Homo sapiens	40-43
19167525-5	2009	Fluorescence titration of rPN-1 with heparin indicated that rPN-1 binds heparin with high affinity.	Heparin	37-44	serpin family E member 2	Rattus norvegicus	60-65
19167525-5	2009	Fluorescence titration of rPN-1 with heparin indicated that rPN-1 binds heparin with high affinity.	Heparin	72-79	serpin family E member 2	Rattus norvegicus	26-31
2843005-16	1988	The complex-binding between heparin and LPL is dependent on the degree of sulphation or ionic strength of the heparin.	Heparin	110-117	lipoprotein lipase	Homo sapiens	40-43
19167525-5	2009	Fluorescence titration of rPN-1 with heparin indicated that rPN-1 binds heparin with high affinity.	Heparin	72-79	serpin family E member 2	Rattus norvegicus	60-65
2962557-3	1988	Antithrombin III inhibits the serine proteases (factors II, IX, X, XI, and XII); its anticoagulant action is dramatically enhanced by heparin.	Heparin	134-141	serpin family C member 1	Homo sapiens	0-16
18378683-9	2008	This study provides a complete account of the gp120 residues involved in heparin binding and identified several binding surfaces that constitute potential target for viral entry inhibition.	Heparin	73-80	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	46-51
18451252-2	2008	Compelling data suggest that heparin exhibits critical antimetastatic effects via interference with P-selectin-mediated cell-cell binding.	Heparin	29-36	selectin P	Homo sapiens	100-110
2840374-5	1988	Studying the ADP-induced fibrinogen binding to platelets in vivo, we were able to show that the effect of heparin on platelets is antibody- and antithrombin-III-independent.	Heparin	106-113	serpin family C member 1	Homo sapiens	144-160
21475829-0	2009	Inhibitory effects of chemically modified heparin on the P-selectin-mediated adhesion of breast cancer cells in vitro.	Heparin	42-49	selectin P	Homo sapiens	57-67
21475829-2	2009	Heparin or chemically modified heparins with decreased anticoagulant activities exhibit marked inhibitory effects on P-selectin-mediated adhesion.	Heparin	0-7	selectin P	Homo sapiens	117-127
3121830-5	1988	Lipoprotein lipase activity rose more with the high heparin dose and equally at either infusion rate.	Heparin	52-59	lipoprotein lipase	Homo sapiens	0-18
21475829-2	2009	Heparin or chemically modified heparins with decreased anticoagulant activities exhibit marked inhibitory effects on P-selectin-mediated adhesion.	Heparin	31-39	selectin P	Homo sapiens	117-127
21475829-3	2009	Here, we prepared chemically modified heparins with reduced anticoagulant activities and investigated whether they effectively inhibited P-selectin binding to breast cancer cells under static and flow conditions.	Heparin	38-46	selectin P	Homo sapiens	137-147
21475829-4	2009	The results indicated that P-selectin binding to ZR-75-30 cells was attenuated by chemically modified heparins in a sulfation-dependent manner under static and flow conditions.	Heparin	102-110	selectin P	Homo sapiens	27-37
18424754-5	2008	C3a and C4a were best generated from C3 and C4, respectively, by monomeric beta-tryptase in the presence of low molecular weight dextran sulfate or heparin at acidic pH.	Heparin	148-155	complement C4A (Rodgers blood group)	Homo sapiens	8-11
18318435-1	2008	UNLABELLED: It has been shown that the heparin-degrading endosulfatase, sulfatase 1 (SULF1), functions as a liver tumor suppressor, but the role of the related sulfatase, sulfatase 2 (SULF2), in liver carcinogenesis remains to be elucidated.	Heparin	39-46	sulfatase 2	Homo sapiens	171-182
18318435-1	2008	UNLABELLED: It has been shown that the heparin-degrading endosulfatase, sulfatase 1 (SULF1), functions as a liver tumor suppressor, but the role of the related sulfatase, sulfatase 2 (SULF2), in liver carcinogenesis remains to be elucidated.	Heparin	39-46	sulfatase 2	Homo sapiens	184-189
18182153-6	2008	In addition, heparin shows stronger effect than sodium sulfate on sensitizing endostatin against acid, and very limited stabilizing effect against urea.	Heparin	13-20	collagen type XVIII alpha 1 chain	Homo sapiens	78-88
18182153-7	2008	The loose structure of endostatin upon heparin binding may imply that the physiologically favorable structure for endostatin exerting its biological functions is not as compact as what was reported.	Heparin	39-46	collagen type XVIII alpha 1 chain	Homo sapiens	23-33
18182153-7	2008	The loose structure of endostatin upon heparin binding may imply that the physiologically favorable structure for endostatin exerting its biological functions is not as compact as what was reported.	Heparin	39-46	collagen type XVIII alpha 1 chain	Homo sapiens	114-124
19178150-0	2009	Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor.	Heparin	22-29	serpin family C member 1	Homo sapiens	156-168
19178150-0	2009	Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor.	Heparin	95-102	serpin family C member 1	Homo sapiens	156-168
19178150-1	2009	Heparin accelerates inhibition of factor XIa (fXIa) by the serpins antithrombin (AT) and C1-inhibitor (C1-INH) by more than 2 orders of magnitude.	Heparin	0-7	serpin family C member 1	Homo sapiens	67-79
19196184-0	2009	Natural cytotoxicity receptors NKp30, NKp44 and NKp46 bind to different heparan sulfate/heparin sequences.	Heparin	88-95	natural cytotoxicity triggering receptor 3	Homo sapiens	31-36
19196184-8	2009	The affinity of NKp30 and NKp44 for synthetic HS/heparin is approximately one order of magnitude higher than the affinity of NKp46.	Heparin	49-56	natural cytotoxicity triggering receptor 3	Homo sapiens	16-21
3481885-0	1987	Antithrombin III binding to surface immobilized heparin and its relation to F Xa inhibition.	Heparin	48-55	serpin family C member 1	Homo sapiens	0-16
19010776-1	2009	We have previously shown that residues Tyr-253 and Glu-255 in the serpin antithrombin function as exosites to promote the inhibition of factor Xa and factor IXa when the serpin is conformationally activated by heparin.	Heparin	210-217	serpin family C member 1	Homo sapiens	73-85
18288776-0	2008	Further characterization of the binding of heparin to granulocyte colony-stimulating factor: importance of sulfate groups.	Heparin	43-50	colony stimulating factor 3	Homo sapiens	54-91
18288776-2	2008	Previously, we have shown that standard heparin binds to granulocyte colony-stimulating factor (G-CSF) with an affinity of 4.8 x 10(5) M(-1).	Heparin	40-47	colony stimulating factor 3	Homo sapiens	57-94
18288776-2	2008	Previously, we have shown that standard heparin binds to granulocyte colony-stimulating factor (G-CSF) with an affinity of 4.8 x 10(5) M(-1).	Heparin	40-47	colony stimulating factor 3	Homo sapiens	96-101
18288776-3	2008	To further study the structural features in heparin that are responsible for this interaction, we studied the bindings of G-CSF and N-desulfated and 2,3-O-desulfated heparin by CZE.	Heparin	44-51	colony stimulating factor 3	Homo sapiens	122-127
18288776-4	2008	Results showed that the N-desulfated heparin had a similar affinity for G-CSF ((5.4 +/- 0.9) x 10(5) M(-1)), but the 2,3-O-desulfated heparin had a 1000-fold lower affinity ((3.4 +/- 1.2) x 10(2) M(-1)) in comparison to standard heparin.	Heparin	37-44	colony stimulating factor 3	Homo sapiens	72-77
3481885-2	1987	Affinity chromatography revealed that one fourth of the heparin used in surface coating had high affinity for antithrombin III (AT).	Heparin	56-63	serpin family C member 1	Homo sapiens	110-126
19028676-7	2009	Furthermore, heparin was able to overcome the inhibitory effect of ANGPTL3 on LPL but not that of ANGPTL4.	Heparin	13-20	lipoprotein lipase	Homo sapiens	78-81
3481885-2	1987	Affinity chromatography revealed that one fourth of the heparin used in surface coating had high affinity for antithrombin III (AT).	Heparin	56-63	serpin family C member 1	Homo sapiens	128-130
18082175-0	2008	In situ growth of nanogold on quartz crystal microbalance and its application in the interaction between heparin and antithrombin III.	Heparin	105-112	serpin family C member 1	Homo sapiens	117-133
18082175-7	2008	After that, both the immobilized amount of heparin and the sensor response to AT III decreased gradually.	Heparin	43-50	serpin family C member 1	Homo sapiens	78-84
3481885-3	1987	The heparin surface adsorbed AT from both human plasma and solutions of purified AT.	Heparin	4-11	serpin family C member 1	Homo sapiens	29-31
18082175-8	2008	Compared with the directly immobilized large nanogold particles, the in situ grown particles with the same size occupy more sensor surface, resulting in higher frequency shifts to AT III in the interaction study between heparin and AT III.	Heparin	220-227	serpin family C member 1	Homo sapiens	180-186
3481885-3	1987	The heparin surface adsorbed AT from both human plasma and solutions of purified AT.	Heparin	4-11	serpin family C member 1	Homo sapiens	81-83
3481885-8	1987	With AT adsorbed on both high and low affinity heparin the surface had the capacity to inhibit several consecutive aliquots of F Xa exposed to the surface.	Heparin	47-54	serpin family C member 1	Homo sapiens	5-7
19758969-1	2009	PURPOSE: Endostatin (ES) is a potent inhibitor of angiogenesis and neoangiogenesis, and interestingly its activity is modified by heparin.	Heparin	130-137	collagen type XVIII alpha 1 chain	Homo sapiens	9-19
19758969-1	2009	PURPOSE: Endostatin (ES) is a potent inhibitor of angiogenesis and neoangiogenesis, and interestingly its activity is modified by heparin.	Heparin	130-137	collagen type XVIII alpha 1 chain	Homo sapiens	21-23
3481885-10	1987	It was demonstrated that the density of AT on both high and low affinity heparin determines the F Xa inhibition capacity whereas the amount of AT on high affinity sites limits the rate of the reaction.	Heparin	73-80	serpin family C member 1	Homo sapiens	40-42
18088351-13	2008	CONCLUSIONS: These observations suggest that AT might inhibit LPS-induced production of TNF-alpha by inhibiting the increase in Egr-1 expression in monocytes via interaction with heparin-like substances expressed on the cell surface.	Heparin	179-186	early growth response 1	Homo sapiens	128-133
18327412-2	2008	In these patients, exogenous AT may be used in association with heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	29-31
3481885-12	1987	The ability of the immobilized heparin to catalyze inhibition of F Xa is likely to be an important component for the thromboresistant properties of a heparin coating with non-compromised AT binding sequences.	Heparin	31-38	serpin family C member 1	Homo sapiens	187-189
19775523-3	2009	Heparin did not affect the viability of ASCs for at least 24 h. The injection of heparin into the caudal tail vein decreased slightly the activities of the alanine aminotransferase (ALT), asparate aminotransferase (AST), and lactate dehydrogenase (LDH) in plasma.	Heparin	81-88	glutamic pyruvic transaminase, soluble	Mus musculus	156-180
3448104-5	1987	The well-proven antimicrobial agent, lactoferrin, was isolated from sweet whey by heparin-attached Sepharose.	Heparin	82-89	lactotransferrin	Bos taurus	37-48
19775523-3	2009	Heparin did not affect the viability of ASCs for at least 24 h. The injection of heparin into the caudal tail vein decreased slightly the activities of the alanine aminotransferase (ALT), asparate aminotransferase (AST), and lactate dehydrogenase (LDH) in plasma.	Heparin	81-88	glutamic pyruvic transaminase, soluble	Mus musculus	182-185
19055319-1	2008	Heparins can be contaminated with oversulfated chondroitin sulfate, OSCS, the impurity being linked to adverse clinical events that certain lots of heparins have had on humans.	Heparin	0-8	APC membrane recruitment protein 1	Homo sapiens	68-72
19055319-1	2008	Heparins can be contaminated with oversulfated chondroitin sulfate, OSCS, the impurity being linked to adverse clinical events that certain lots of heparins have had on humans.	Heparin	148-156	APC membrane recruitment protein 1	Homo sapiens	68-72
18845535-11	2008	This may explain how GDNF.GFR alpha 1 can mediate cell adhesion and how heparin might inhibit GDNF signaling through RET.	Heparin	72-79	ret proto-oncogene	Homo sapiens	117-120
18206177-3	2008	Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity.	Heparin	98-105	serpin family C member 1	Homo sapiens	0-12
18206177-3	2008	Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity.	Heparin	98-105	serpin family C member 1	Homo sapiens	236-248
18006516-9	2008	These results highlight a new difference between the plant PM Ca(2+)-ATPase and its animal counterpart, which is inhibited by heparin.	Heparin	126-133	autoinhibited Ca2+-ATPase 1	Arabidopsis thaliana	62-75
2962194-3	1987	Both snRNP (the presumed human homologue of the U7 snRNP of the sea urchin) and the heat-labile factor described above show closely similar properties when fractionated on DEAE, heparin, and Mono Q columns.	Heparin	178-185	LSM2 homolog, U6 small nuclear RNA and mRNA degradation associated	Homo sapiens	5-10
18226138-1	2008	We present a case of a pregnant woman with hereditary antithrombin III deficiency and deep vein thrombosis of the left lower extremity managed by perinatal unfractionated heparin injection with antithrombin III replacement as well as by intrapartum placement of a temporary inferior vena cava filter.	Heparin	171-178	serpin family C member 1	Homo sapiens	54-70
19086847-2	2008	Two recently identified human heparin-degrading endosulfatases, named sulfatase 1 (SULF1) and sulfatase 2 (SULF2), have been found to be involved in liver carcinogenesis.	Heparin	30-37	sulfatase 2	Homo sapiens	94-105
19086847-2	2008	Two recently identified human heparin-degrading endosulfatases, named sulfatase 1 (SULF1) and sulfatase 2 (SULF2), have been found to be involved in liver carcinogenesis.	Heparin	30-37	sulfatase 2	Homo sapiens	107-112
3666316-5	1987	LPL activity was measured as activity secreted into the culture medium (CM), released from cells by heparin (HR), and extracted from cell digests (EXT).	Heparin	100-107	lipoprotein lipase	Homo sapiens	0-3
19035406-9	2008	The reversed polarity CE-LIF disaccharide analysis protocol yields baseline resolution and quantification of heparin/heparan sulfate and CS/dermatan sulfate disaccharides from both standard preparations and biologically relevant proteoglycan samples.	Heparin	109-116	LIF interleukin 6 family cytokine	Homo sapiens	25-28
18006589-3	2008	In the present study, we complement our results by showing direct binding of recombinant NKp30 to immobilized heparin.	Heparin	110-117	natural cytotoxicity triggering receptor 3	Homo sapiens	89-94
18721140-5	2008	The release of the 35 k Da annexin II by matrilysin was significantly enhanced in the presence of serotonin or heparin.	Heparin	111-118	annexin A2	Homo sapiens	27-37
2958379-3	1987	First, in the presence of soluble heparin, the rate at which embryos attach and outgrow on laminin, fibronectin, or monolayers of uterine epithelial cells is reduced considerably.	Heparin	34-41	fibronectin 1	Mus musculus	100-111
18721140-5	2008	The release of the 35 k Da annexin II by matrilysin was significantly enhanced in the presence of serotonin or heparin.	Heparin	111-118	matrix metallopeptidase 7	Homo sapiens	41-51
18653779-4	2008	Prolactin and the ErbB4/HER4 ligand heparin-binding epidermal growth factor each induced STAT5A tyrosine phosphorylation and nuclear translocation; each pathway required the intracellular tyrosine kinase Janus kinase 2 (JAK2).	Heparin	36-43	erb-b2 receptor tyrosine kinase 4	Mus musculus	18-23
18179175-3	2008	The FGF19 subfamily has reduced heparin binding resulting from a disrupted beta-trefoil domain.	Heparin	32-39	fibroblast growth factor 15	Mus musculus	4-9
2958379-4	1987	In the case of fibronectin, the rate of outgrowth in the presence of the heparin is slower than in the presence of the Arg-Gly-Asp-Ser-containing peptide that is recognized by a fibronectin receptor.	Heparin	73-80	fibronectin 1	Mus musculus	15-26
18653779-4	2008	Prolactin and the ErbB4/HER4 ligand heparin-binding epidermal growth factor each induced STAT5A tyrosine phosphorylation and nuclear translocation; each pathway required the intracellular tyrosine kinase Janus kinase 2 (JAK2).	Heparin	36-43	erb-b2 receptor tyrosine kinase 4	Mus musculus	24-28
18653779-4	2008	Prolactin and the ErbB4/HER4 ligand heparin-binding epidermal growth factor each induced STAT5A tyrosine phosphorylation and nuclear translocation; each pathway required the intracellular tyrosine kinase Janus kinase 2 (JAK2).	Heparin	36-43	signal transducer and activator of transcription 5A	Mus musculus	89-95
2958379-4	1987	In the case of fibronectin, the rate of outgrowth in the presence of the heparin is slower than in the presence of the Arg-Gly-Asp-Ser-containing peptide that is recognized by a fibronectin receptor.	Heparin	73-80	fibronectin 1	Mus musculus	178-189
18653779-4	2008	Prolactin and the ErbB4/HER4 ligand heparin-binding epidermal growth factor each induced STAT5A tyrosine phosphorylation and nuclear translocation; each pathway required the intracellular tyrosine kinase Janus kinase 2 (JAK2).	Heparin	36-43	Janus kinase 2	Mus musculus	204-218
17985932-10	2007	Glycosaminoglycan binding by IGFBPs can affect their IGF binding although the effects appear to differ among different IGFBPs; here, we found that heparin bound to the IGF-I.N-BP-2.C-BP-2 ternary complex, but did not cause it to dissociate.	Heparin	147-154	insulin like growth factor binding protein 1	Homo sapiens	29-35
18653779-4	2008	Prolactin and the ErbB4/HER4 ligand heparin-binding epidermal growth factor each induced STAT5A tyrosine phosphorylation and nuclear translocation; each pathway required the intracellular tyrosine kinase Janus kinase 2 (JAK2).	Heparin	36-43	Janus kinase 2	Mus musculus	220-224
17985932-10	2007	Glycosaminoglycan binding by IGFBPs can affect their IGF binding although the effects appear to differ among different IGFBPs; here, we found that heparin bound to the IGF-I.N-BP-2.C-BP-2 ternary complex, but did not cause it to dissociate.	Heparin	147-154	insulin like growth factor binding protein 1	Homo sapiens	119-125
3317985-5	1987	However, heparin (1-10 ug/ml) strongly accelerated the rate of antithrombin III inactivation and slightly protected heparin cofactor II, thus reversing the order of inactivation.	Heparin	9-16	serpin family C member 1	Homo sapiens	63-79
17985932-10	2007	Glycosaminoglycan binding by IGFBPs can affect their IGF binding although the effects appear to differ among different IGFBPs; here, we found that heparin bound to the IGF-I.N-BP-2.C-BP-2 ternary complex, but did not cause it to dissociate.	Heparin	147-154	NUBP iron-sulfur cluster assembly factor 2, cytosolic	Homo sapiens	174-180
18940719-11	2008	Other studies have shown that heparin inhibited P-selectin- and soluble-TSP-mediated sickle erythrocyte adhesion to endothelial cells.	Heparin	30-37	selectin P	Homo sapiens	48-58
18640975-2	2008	The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)).	Heparin	52-60	serpin family C member 1	Homo sapiens	100-112
18640975-2	2008	The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)).	Heparin	52-60	synuclein alpha	Homo sapiens	166-169
18449905-0	2008	Heparin inhibits BMP-2 osteogenic bioactivity by binding to both BMP-2 and BMP receptor.	Heparin	0-7	bone morphogenetic protein 1	Homo sapiens	17-20
18449905-2	2008	However, the role of heparin in the biological activity of bone morphogenetic protein (BMP) remains unclear.	Heparin	21-28	bone morphogenetic protein 1	Homo sapiens	59-85
18449905-2	2008	However, the role of heparin in the biological activity of bone morphogenetic protein (BMP) remains unclear.	Heparin	21-28	bone morphogenetic protein 1	Homo sapiens	87-90
18057711-4	2007	OR-heparin also inhibited high glucose-activated ERK1/2 phosphorylation, induced p27(Kip1) expression, and suppressed reactive oxygen species (ROS) accumulation in a dose-dependent manner.	Heparin	3-10	cyclin dependent kinase inhibitor 1B	Homo sapiens	85-89
17933553-8	2007	A protocol was developed to purify recombinant endostatin in the fermentation supernatant to a yield of 24mg/L and 98% purity by the use of SP Sepharose FF cation exchange chromatography, Sepharose-heparin Hi Trap affinity chromatography and gel filtration chromatography.	Heparin	198-205	collagen type XVIII alpha 1 chain	Homo sapiens	47-57
3690577-0	1987	Synthesis of heparin fragments: a methyl alpha-pentaoside with high affinity for antithrombin III.	Heparin	13-20	serpin family C member 1	Homo sapiens	81-97
17944804-1	2007	The keratinocyte growth factor receptor (KGFR)/fibroblast growth factor receptor 2b is activated by high-affinity-specific interaction with two different ligands, keratinocyte growth factor (KGF)/fibroblast growth factor (FGF)7 and FGF10/KGF2, which are characterized by an opposite requirement of heparan sulfate proteoglycans and heparin for binding to the receptor.	Heparin	332-339	fibroblast growth factor receptor 2	Homo sapiens	4-39
17944804-1	2007	The keratinocyte growth factor receptor (KGFR)/fibroblast growth factor receptor 2b is activated by high-affinity-specific interaction with two different ligands, keratinocyte growth factor (KGF)/fibroblast growth factor (FGF)7 and FGF10/KGF2, which are characterized by an opposite requirement of heparan sulfate proteoglycans and heparin for binding to the receptor.	Heparin	332-339	fibroblast growth factor receptor 2	Homo sapiens	41-45
17944804-1	2007	The keratinocyte growth factor receptor (KGFR)/fibroblast growth factor receptor 2b is activated by high-affinity-specific interaction with two different ligands, keratinocyte growth factor (KGF)/fibroblast growth factor (FGF)7 and FGF10/KGF2, which are characterized by an opposite requirement of heparan sulfate proteoglycans and heparin for binding to the receptor.	Heparin	332-339	fibroblast growth factor receptor 2	Homo sapiens	47-82
18556661-4	2008	In this study, we show that Arabidopsis HFR1 can be phosphorylated by recombinant casein kinase II (CKII) and plant extract in vitro and that phosphorylation of HFR1 can be effectively reduced by treatments with two CKII-specific inhibitors, 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole (DRB) and heparin.	Heparin	302-309	Protein kinase superfamily protein	Arabidopsis thaliana	82-98
18556661-4	2008	In this study, we show that Arabidopsis HFR1 can be phosphorylated by recombinant casein kinase II (CKII) and plant extract in vitro and that phosphorylation of HFR1 can be effectively reduced by treatments with two CKII-specific inhibitors, 5,6-dichloro-1-beta-d-ribofuranosyl-benzimidazole (DRB) and heparin.	Heparin	302-309	Protein kinase superfamily protein	Arabidopsis thaliana	100-104
3690577-1	1987	The synthesis is described of the methyl alpha-glycoside of the pentasaccharide which represents the sequence in heparin responsible for binding and activation of the anticoagulant protein Antithrombin III.	Heparin	113-120	serpin family C member 1	Homo sapiens	189-205
2442161-0	1987	Neutralization and binding of heparin by S protein/vitronectin in the inhibition of factor Xa by antithrombin III.	Heparin	30-37	serpin family C member 1	Homo sapiens	97-113
18599591-3	2008	ErbB-1 may protect the heart against stress-induced injury and its ligand; epidermal growth factor (EGF) increases myocardial contractility, whereas heparin-binding EGF is essential for normal cardiac function.	Heparin	149-156	epidermal growth factor receptor	Mus musculus	0-4
17706192-5	2007	We were interested in the in vivo effects of amitriptyline on the diamine oxidase release into guinea pig plasma after heparin stimulation and in effects on the activity and gene expression of both histamine degrading enzymes in different guinea pig tissues.	Heparin	119-126	amiloride-sensitive amine oxidase [copper-containing]	Cavia porcellus	66-81
17706192-8	2007	The results showed that amitriptyline in vivo changed the profile of the heparin-induced diamine oxidase release, which could be due to changes in at least three processes: diamine oxidase release into plasma, protein synthesis and enzyme activity at the molecular level.	Heparin	73-80	amiloride-sensitive amine oxidase [copper-containing]	Cavia porcellus	89-104
17706192-8	2007	The results showed that amitriptyline in vivo changed the profile of the heparin-induced diamine oxidase release, which could be due to changes in at least three processes: diamine oxidase release into plasma, protein synthesis and enzyme activity at the molecular level.	Heparin	73-80	amiloride-sensitive amine oxidase [copper-containing]	Cavia porcellus	173-188
18602100-3	2008	The peptides of 18 amino acid residues derived from IGFBP-3 and IGFBP-5, which involve heparin-binding regions, mediated cellular delivery of an exogenous protein into NIH3T3 and HeLa cells.	Heparin	87-94	insulin-like growth factor binding protein 3	Mus musculus	52-59
2442161-2	1987	The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system.	Heparin	105-112	serpin family C member 1	Homo sapiens	162-178
18602100-5	2008	Heparin inhibited the uptake of the fusion proteins with IGFBP-3 and IGFBP-5, indicating that the delivery pathway is heparin-dependent endocytosis, similar to that of HIV-Tat.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	57-64
2442161-4	1987	Using purified components in the presence of heparin, S protein induced a concentration-dependent reduction of the inhibition rate of factor Xa by antithrombin III.	Heparin	45-52	serpin family C member 1	Homo sapiens	147-163
18338323-0	2008	Analysis of the interactions between the peptides from secreted human CKLF1 and heparin using capillary zone electrophoresis.	Heparin	80-87	chemokine like factor	Homo sapiens	70-75
18338323-3	2008	In this study, a selective high-performance analytical method based on capillary zone electrophoresis (CZE) to investigate interactions between heparin and CKLF1-C27/CKLF1-C19 was developed.	Heparin	144-151	chemokine like factor	Homo sapiens	156-161
17875649-1	2007	Heparin activates the serpin, antithrombin, to inhibit its target blood-clotting proteases by generating new protease interaction exosites.	Heparin	0-7	serpin family C member 1	Homo sapiens	30-42
2442161-12	1987	These data provide evidence that the heparin-binding domain of S protein appears to be unique in binding to heparin and thereby neutralizing its anticoagulant activity in the inhibition of coagulation factors by antithrombin III.	Heparin	37-44	serpin family C member 1	Homo sapiens	212-228
17621651-13	2007	Our findings suggest that the safety of antithrombin therapy with low molecular weight heparin during PCI requires further evaluation.	Heparin	87-94	serpin family C member 1	Homo sapiens	40-52
17766586-0	2007	Fibroblast growth factor-binding protein and N-deacetylase/N-sulfotransferase-1 expression in type II cells is modulated by heparin and extracellular matrix.	Heparin	124-131	N-deacetylase and N-sulfotransferase 1	Rattus norvegicus	45-79
18338323-3	2008	In this study, a selective high-performance analytical method based on capillary zone electrophoresis (CZE) to investigate interactions between heparin and CKLF1-C27/CKLF1-C19 was developed.	Heparin	144-151	chemokine like factor	Homo sapiens	166-171
18338323-6	2008	The binding constants of the interactions between CKLF1-C27/CKLF1-C19 and heparin were calculated as (3.38 +/- 0.49) x 10(5) M(-1) and (1.10 +/- 0.02) x 10(5) M(-1) by Scatchard analysis.	Heparin	74-81	chemokine like factor	Homo sapiens	50-55
18338323-6	2008	The binding constants of the interactions between CKLF1-C27/CKLF1-C19 and heparin were calculated as (3.38 +/- 0.49) x 10(5) M(-1) and (1.10 +/- 0.02) x 10(5) M(-1) by Scatchard analysis.	Heparin	74-81	chemokine like factor	Homo sapiens	60-65
18338323-7	2008	To study structural requirements, CKLF1-C19pm and CKLF1-C19km have been synthesized, and their interactions with heparin have been studied by CZE.	Heparin	113-120	chemokine like factor	Homo sapiens	34-39
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	164-171	chemokine like factor	Homo sapiens	72-77
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	164-171	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	164-171	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	164-171	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	164-171	chemokine like factor	Homo sapiens	83-88
18338323-8	2008	We found that the Pro or Lys to Ala substitution within the residues of CKLF1-C19 (CKLF1-C19pm or CKLF1-C19km) strongly decreased or abolished its interaction with heparin, suggesting that the residues of Pro affect the affinity of CKLF1-C19 for heparin, and the residues of Lys of CKLF1-C19 play the important role for the interaction of CKLF1-C19 and heparin, respectively.	Heparin	164-171	chemokine like factor	Homo sapiens	83-88
17766586-7	2007	NDST-1 expression in ATII cells was most sensitive to the amount of sulfation in medium and ECM and enhanced by fully sulfated heparin.	Heparin	127-134	N-deacetylase and N-sulfotransferase 1	Rattus norvegicus	0-6
3305015-14	1987	The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin.	Heparin	294-301	serpin family C member 1	Homo sapiens	255-271
17644519-6	2007	In studies of glycosaminoglycan binding, MIP-1beta-A10C binds to a heparin-Sepharose column as tightly as the wild type protein and more tightly than monomeric variants.	Heparin	67-74	C-C motif chemokine ligand 4	Homo sapiens	41-50
17580303-4	2007	We have localized critical domains in the N terminus of LTBP1 that are required for co-localization with fibronectin in osteoblast cultures and have identified heparin binding sites in the N terminus of LTBP1 between residues 345 and 487.	Heparin	160-167	latent transforming growth factor beta binding protein 1	Homo sapiens	203-208
17580303-6	2007	Heparin coupled to bovine serum albumin (heparin-BSA) was able to mediate binding between fibronectin and LTBP1.	Heparin	0-7	latent transforming growth factor beta binding protein 1	Homo sapiens	106-111
18452898-1	2008	2-O-Sulfo-alpha-l-iduronic acid (IdoA2S) is one of the main components of heparin, an anticoagulant and antithrombotic polysaccharide able to potentiate the inhibitory effect of antithrombin over plasma serine proteases.	Heparin	74-81	serpin family C member 1	Homo sapiens	178-190
18549262-12	2008	In summary, we describe heparin affinity fractionation enrichment (HAFE) as a prefractionation tool for the study of the human primary tissue proteome and the discovery of PSB7, PRDX1, and SRP9 up-regulation as candidate biomarkers of colon cancer.	Heparin	24-31	proteasome 20S subunit beta 7	Homo sapiens	172-176
18549262-12	2008	In summary, we describe heparin affinity fractionation enrichment (HAFE) as a prefractionation tool for the study of the human primary tissue proteome and the discovery of PSB7, PRDX1, and SRP9 up-regulation as candidate biomarkers of colon cancer.	Heparin	24-31	peroxiredoxin 1	Homo sapiens	178-183
17580303-7	2007	Treatment of primary osteoblast cultures with heparin or heparin-BSA but not with chondroitin sulfate impaired LTBP1 deposition onto fibronectin without inhibiting expression of LTBP1.	Heparin	46-53	latent transforming growth factor beta binding protein 1	Homo sapiens	111-116
3305015-15	1987	Both high-affinity and low-affinity antithrombin-III-binding heparins were shown to inhibit the V8 protease digestion of native antithrombin III, but the high-affinity sample exhibited a higher inhibition activity than the low-affinity heparin.	Heparin	61-69	serpin family C member 1	Homo sapiens	128-144
17580303-7	2007	Treatment of primary osteoblast cultures with heparin or heparin-BSA but not with chondroitin sulfate impaired LTBP1 deposition onto fibronectin without inhibiting expression of LTBP1.	Heparin	57-64	latent transforming growth factor beta binding protein 1	Homo sapiens	111-116
3305015-15	1987	Both high-affinity and low-affinity antithrombin-III-binding heparins were shown to inhibit the V8 protease digestion of native antithrombin III, but the high-affinity sample exhibited a higher inhibition activity than the low-affinity heparin.	Heparin	61-68	serpin family C member 1	Homo sapiens	128-144
3305015-16	1987	These findings (a) imply that the segment containing residues 34-51 is among the most exposed region of native antithrombin III and (b) support the previous conclusions that this region may play a pivotal role in the heparin binding.	Heparin	217-224	serpin family C member 1	Homo sapiens	111-127
17849067-0	2007	Report of a novel kindred with antithrombin heparin-binding site variant (47 Arg to His): demand for an automated progressive antithrombin assay to detect molecular variants with low thrombotic risk.	Heparin	44-51	serpin family C member 1	Homo sapiens	31-43
17849067-0	2007	Report of a novel kindred with antithrombin heparin-binding site variant (47 Arg to His): demand for an automated progressive antithrombin assay to detect molecular variants with low thrombotic risk.	Heparin	44-51	serpin family C member 1	Homo sapiens	126-138
25392850-7	2008	We show the benefits of the instance-based methods on two real-world detection problems: detection of unusual admission decisions for patients with the community-acquired pneumonia and detection of unusual orders of an HPF4 test that is used to confirm Heparin induced thrombocytopenia - a life-threatening condition caused by the Heparin therapy.	Heparin	253-260	zinc finger protein 85	Homo sapiens	219-223
25392850-7	2008	We show the benefits of the instance-based methods on two real-world detection problems: detection of unusual admission decisions for patients with the community-acquired pneumonia and detection of unusual orders of an HPF4 test that is used to confirm Heparin induced thrombocytopenia - a life-threatening condition caused by the Heparin therapy.	Heparin	331-338	zinc finger protein 85	Homo sapiens	219-223
18448283-6	2008	We measured HL and LPL activity in post-heparin normal human plasma in the presence and absence of the drugs by measuring the release of fatty acids from radiolabeled triolein.	Heparin	40-47	lipoprotein lipase	Homo sapiens	19-22
18448283-9	2008	LPL activity in post-heparin normal human plasma was suppressed following the co-incubation with CsA, RAPA, FK-506 or MMF whereas HL activity remained unaffected.	Heparin	21-28	lipoprotein lipase	Homo sapiens	0-3
17447896-6	2007	Centerin also bound DNA and unfractionated heparin, although there was no functionally significant impact on the rate of inhibition.	Heparin	43-50	serpin family A member 9	Homo sapiens	0-8
3649921-0	1987	Heparin promotes the inactivation of antithrombin by neutrophil elastase.	Heparin	0-7	serpin family C member 1	Homo sapiens	37-49
18434317-0	2008	The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin.	Heparin	101-108	stabilin 2	Homo sapiens	10-45
3649921-1	1987	Heparin is an acceleratory cofactor for antithrombin, a circulating inhibitor of blood coagulation enzymes.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-52
18434317-0	2008	The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin.	Heparin	101-108	stabilin 2	Homo sapiens	47-51
18434317-0	2008	The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a systemic clearance receptor for heparin.	Heparin	101-108	stabilin 2	Homo sapiens	52-62
3649921-3	1987	In apparent opposition to this function, heparin was found to greatly accelerate the in vitro inactivation of antithrombin by neutrophil elastase.	Heparin	41-48	serpin family C member 1	Homo sapiens	110-122
18434317-4	2008	Here we report that the 190- and 315-kDa HARE isoforms, expressed stably either in Flp-In 293 cell lines or as soluble ectodomains, specifically bind heparin (Hep).	Heparin	150-157	stabilin 2	Homo sapiens	41-45
17476032-7	2007	Another novel double mutation, Lys312insC + Asn291Ser, resulted in the loss of the catalytic ability of LPL attributable to the complete loss of the C-terminal domain and alteration in the heparin association site.	Heparin	189-196	lipoprotein lipase	Homo sapiens	104-107
3649921-5	1987	Although the data suggest that a heparin-antithrombin complex is essential for the inactivation by elastase to occur, the enzyme itself interacts tightly with heparin.	Heparin	33-40	serpin family C member 1	Homo sapiens	41-53
18434317-4	2008	Here we report that the 190- and 315-kDa HARE isoforms, expressed stably either in Flp-In 293 cell lines or as soluble ectodomains, specifically bind heparin (Hep).	Heparin	159-162	stabilin 2	Homo sapiens	41-45
3621492-3	1987	In this study, induction of ornithine decarboxylase (ODC) activity was used as a marker of SMC entry into the cell cycle in an attempt to localize the site of heparin action during the initial hours after rat carotid injury.	Heparin	159-166	ornithine decarboxylase 1	Rattus norvegicus	28-51
18375953-5	2008	Here, we show that the previously characterized prelatent antithrombin is a mixture of native antithrombin and a modified, true prelatent antithrombin that are resolvable by heparin-agarose chromatography.	Heparin	174-181	serpin family C member 1	Homo sapiens	58-70
17536781-0	2007	Frontal analysis capillary electrophoresis hyphenated to electrospray ionization mass spectrometry for the characterization of the antithrombin/heparin pentasaccharide complex.	Heparin	144-151	serpin family C member 1	Homo sapiens	131-143
17536781-5	2007	This FACE-MS coupling was applied to the analysis of the complex between antithrombin and the sulfated pentasaccharide reproducing the antithrombin-binding sequence in heparin.	Heparin	168-175	serpin family C member 1	Homo sapiens	73-85
3621492-3	1987	In this study, induction of ornithine decarboxylase (ODC) activity was used as a marker of SMC entry into the cell cycle in an attempt to localize the site of heparin action during the initial hours after rat carotid injury.	Heparin	159-166	ornithine decarboxylase 1	Rattus norvegicus	53-56
17536781-5	2007	This FACE-MS coupling was applied to the analysis of the complex between antithrombin and the sulfated pentasaccharide reproducing the antithrombin-binding sequence in heparin.	Heparin	168-175	serpin family C member 1	Homo sapiens	135-147
17536781-7	2007	The intact noncovalent complex antithrombin/heparin pentasaccharide was detected on-line by ESIMS in positive ionization mode and in nondenaturing sheath liquid conditions.	Heparin	44-51	serpin family C member 1	Homo sapiens	31-43
18375953-7	2008	Purified prelatent antithrombin had reduced anticoagulant function compared with native antithrombin, due to a reduced heparin affinity and consequent impaired ability of heparin to either bridge prelatent antithrombin and coagulation proteases in a ternary complex or to induce full conformational activation of the serpin.	Heparin	119-126	serpin family C member 1	Homo sapiens	19-31
18375953-7	2008	Purified prelatent antithrombin had reduced anticoagulant function compared with native antithrombin, due to a reduced heparin affinity and consequent impaired ability of heparin to either bridge prelatent antithrombin and coagulation proteases in a ternary complex or to induce full conformational activation of the serpin.	Heparin	171-178	serpin family C member 1	Homo sapiens	19-31
17629851-0	2007	Affinity and kinetics of different heparins binding to P- and L-selectin.	Heparin	35-43	selectin L	Homo sapiens	62-72
18375953-9	2008	The prelatent form was conformationally altered from native antithrombin as judged from an attenuation of tryptophan fluorescence changes following heparin activation and a reduced thermal stability.	Heparin	148-155	serpin family C member 1	Homo sapiens	60-72
3428662-0	1987	[Effect of heparin treatment on antithrombin III (AT III) activity].	Heparin	11-18	serpin family C member 1	Homo sapiens	32-48
17629851-2	2007	The anti-inflammatory and antimetastatic activities of heparins have been related partly to their ability to interact with P- and L-selectin.	Heparin	55-63	selectin L	Homo sapiens	130-140
17537059-10	2007	The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process.	Heparin	35-42	serpin family C member 1	Homo sapiens	23-26
17537059-10	2007	The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process.	Heparin	47-54	serpin family C member 1	Homo sapiens	23-26
17511500-3	2007	Thiol functionalization of heparin carboxylic groups was controlled from 10% to 60% of the available COOH groups, and the retained bioactivity of the modified heparin, characterized by its binding affinity to antithrombin III, decreased with increasing functionalization.	Heparin	27-34	serpin family C member 1	Homo sapiens	209-225
17511500-3	2007	Thiol functionalization of heparin carboxylic groups was controlled from 10% to 60% of the available COOH groups, and the retained bioactivity of the modified heparin, characterized by its binding affinity to antithrombin III, decreased with increasing functionalization.	Heparin	159-166	serpin family C member 1	Homo sapiens	209-225
18272520-11	2008	Treatment with heparin rescued a pool of apoB in cells expressing the endocytic mutant, indicating that reuptake of VLDL via apoE still occurs with this mutant.	Heparin	15-22	apolipoprotein B	Mus musculus	41-45
18231993-6	2008	Heparin suppressed TRAP-positive multinucleated cell formation and TRAP activity induced by RANKL, whereas the other GAGs showed no effects on osteoclast differentiation.	Heparin	0-7	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	92-97
18231993-9	2008	However, heparin reduced the level of c-Src protein in RAW 264.7 cells stimulated with RANKL.	Heparin	9-16	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	87-92
18231993-11	2008	Western blotting analysis revealed the expression of RANKL in the fraction bound to heparin.	Heparin	84-91	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	53-58
18231993-12	2008	The binding of RANKL and heparin was confirmed by quartz-crystal microbalance.	Heparin	25-32	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	15-20
18231993-13	2008	These results indicate that the inhibitory effect of heparin toward osteoclastogenesis induced by RANKL is due to the binding of heparin to RANKL.	Heparin	53-60	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	98-103
18231993-13	2008	These results indicate that the inhibitory effect of heparin toward osteoclastogenesis induced by RANKL is due to the binding of heparin to RANKL.	Heparin	53-60	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	140-145
3428662-0	1987	[Effect of heparin treatment on antithrombin III (AT III) activity].	Heparin	11-18	serpin family C member 1	Homo sapiens	50-56
18231993-13	2008	These results indicate that the inhibitory effect of heparin toward osteoclastogenesis induced by RANKL is due to the binding of heparin to RANKL.	Heparin	129-136	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	98-103
2442830-3	1987	The sulfated xylans were more effective than heparin or SP-54 in potentiating the AT-III inhibition of amidolysis of H-D-Phe-Pip-Arg-pNa (S-2238) by thrombin (IIa) or amidolysis of Bz-Ile-Glu-Gly-Arg-pNa (S-2222) by Xa.	Heparin	45-52	serpin family C member 1	Homo sapiens	82-88
18231993-13	2008	These results indicate that the inhibitory effect of heparin toward osteoclastogenesis induced by RANKL is due to the binding of heparin to RANKL.	Heparin	129-136	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	140-145
17878960-4	2007	However, other intriguing properties of ANXA5 potentially contributing to its antithrombotic function, especially downregulation of surface expressed tissue factor, or interaction with additional ligands involved in hemostasis such as sulfatide and heparin, as well as upregulation of urokinase-type plasminogen activator were reported.	Heparin	249-256	annexin A5	Homo sapiens	40-45
18287332-7	2008	Exposure of neutrophils to heparin attenuated binding of xanthine oxidase to the cell surface as well as interactions with TLR4.	Heparin	27-34	toll like receptor 4	Homo sapiens	123-127
3609301-5	1987	Chromatography of total tryptic digests on concanavalin A-Sepharose confirmed that the high heparin affinity form of antithrombin lacked an oligosaccharide moiety at Asn 135.	Heparin	92-99	serpin family C member 1	Homo sapiens	117-129
17409095-8	2007	Activin-induced binding of heparin is unique to the FS315 isoform and may stimulate clearance of FS315 complexes.	Heparin	27-34	inhibin subunit beta E	Homo sapiens	0-7
18162523-8	2008	A COOH-terminal region in IGFBP-3 (residues 215-232) contains a nuclear localization signal, and binding domains for RXR-alpha and heparin (HBD).	Heparin	131-138	insulin like growth factor binding protein 3	Homo sapiens	26-33
3109497-1	1987	The interactions of antithrombin III with two heparin-dye conjugates have been compared using their fluorescence anisotropy.	Heparin	46-53	serpin family C member 1	Homo sapiens	20-36
17705152-7	2008	Heparin and dextran sulfate inhibit porcine somatotropin (pST) and bovine somatotropin (bST) aggregation to the greatest extent, as compared to phytic acid and SOS, while decreasing secondary and tertiary structural stability as measured by the temperature dependence of their circular dichroism and intrinsic fluorescence.	Heparin	0-7	somatotropin	Bos taurus	44-56
17394193-1	2007	BACKGROUND: Cleavage of membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields a soluble HB-EGF isoform (sHB-EGF), which is an activating epidermal growth factor receptor (EGFR) ligand and a C-terminal fragment HB-EGF-C acting directly in the nucleus.	Heparin	42-49	heparin binding EGF like growth factor	Homo sapiens	105-111
17394193-1	2007	BACKGROUND: Cleavage of membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields a soluble HB-EGF isoform (sHB-EGF), which is an activating epidermal growth factor receptor (EGFR) ligand and a C-terminal fragment HB-EGF-C acting directly in the nucleus.	Heparin	42-49	heparin binding EGF like growth factor	Homo sapiens	130-136
17485301-7	2007	Recent studies have confirmed that HPF4 antibody generation (seroconversion) is common after cardiac surgery and suggest that patients receiving bovine heparin are more likely to generate functional (pathogenic) HPF4 antibodies of the IgG subclass.	Heparin	152-159	zinc finger protein 85	Homo sapiens	35-39
17705152-7	2008	Heparin and dextran sulfate inhibit porcine somatotropin (pST) and bovine somatotropin (bST) aggregation to the greatest extent, as compared to phytic acid and SOS, while decreasing secondary and tertiary structural stability as measured by the temperature dependence of their circular dichroism and intrinsic fluorescence.	Heparin	0-7	somatotropin	Bos taurus	74-86
17485301-7	2007	Recent studies have confirmed that HPF4 antibody generation (seroconversion) is common after cardiac surgery and suggest that patients receiving bovine heparin are more likely to generate functional (pathogenic) HPF4 antibodies of the IgG subclass.	Heparin	152-159	zinc finger protein 85	Homo sapiens	212-216
3109497-2	1987	The first, heparin labelled with 5-isothiocyanatofluorescein, where the dye was mostly bound to unsulphated glucosamine residues, exhibited binding which was characteristic of heparin with a low affinity for antithrombin III.	Heparin	11-18	serpin family C member 1	Homo sapiens	208-224
3109497-2	1987	The first, heparin labelled with 5-isothiocyanatofluorescein, where the dye was mostly bound to unsulphated glucosamine residues, exhibited binding which was characteristic of heparin with a low affinity for antithrombin III.	Heparin	176-183	serpin family C member 1	Homo sapiens	208-224
3109497-4	1987	However, when the heparin was treated with an amino group blocking agent prior to labelling with DENMT, the resultant heparin-dye conjugate showed binding behaviour, the strength of which was consistent with heparin molecules having both high and low affinity for antithrombin III.	Heparin	18-25	serpin family C member 1	Homo sapiens	264-280
17497280-6	2007	The study showed that the incidence of ischemic events in patients with ACS receiving tirofiban+heparin was lower when compared with that of patients who received only heparin and aspirin, suggesting that tirofiban might be of special value in the treatment of ACS.	Heparin	96-103	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	72-75
17497280-6	2007	The study showed that the incidence of ischemic events in patients with ACS receiving tirofiban+heparin was lower when compared with that of patients who received only heparin and aspirin, suggesting that tirofiban might be of special value in the treatment of ACS.	Heparin	96-103	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	261-264
18160297-2	2008	In this study, we investigated their interactions with synthetic heparin-binding peptides, derived from human antithrombin III (hAT III) and heparin-interacting protein (HIP), using surface noncovalent affinity mass spectrometry.	Heparin	65-72	serpin family C member 1	Homo sapiens	110-126
18160297-2	2008	In this study, we investigated their interactions with synthetic heparin-binding peptides, derived from human antithrombin III (hAT III) and heparin-interacting protein (HIP), using surface noncovalent affinity mass spectrometry.	Heparin	65-72	serpin family C member 1	Homo sapiens	128-135
18160297-3	2008	We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6.	Heparin	40-47	serpin family C member 1	Homo sapiens	183-190
18160297-3	2008	We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6.	Heparin	222-229	serpin family C member 1	Homo sapiens	183-190
18243143-0	2008	Uteroglobin interacts with the heparin-binding site of fibronectin and prevents fibronectin-IgA complex formation found in IgA-nephropathy.	Heparin	31-38	secretoglobin family 1A member 1	Homo sapiens	0-11
18082175-8	2008	Compared with the directly immobilized large nanogold particles, the in situ grown particles with the same size occupy more sensor surface, resulting in higher frequency shifts to AT III in the interaction study between heparin and AT III.	Heparin	220-227	serpin family C member 1	Homo sapiens	232-238
17393024-8	2007	Additional experiments revealed a slight influence of heparin on platelet P-selectin expression but excluded an effect of this anticoagulant on the other evaluated parameters.	Heparin	54-61	selectin P	Homo sapiens	74-84
18082175-9	2008	The obtained constants of AT III binding to immobilized heparin are k(ass)=(1.65+/-0.12)x10(3) L/mols, k diss=(2.63+/-0.18)x10(-2) 1/s and K(A)=(6.27+/-0.42)x10(4) L/mol.	Heparin	56-63	serpin family C member 1	Homo sapiens	26-32
3109497-4	1987	However, when the heparin was treated with an amino group blocking agent prior to labelling with DENMT, the resultant heparin-dye conjugate showed binding behaviour, the strength of which was consistent with heparin molecules having both high and low affinity for antithrombin III.	Heparin	118-125	serpin family C member 1	Homo sapiens	264-280
3109497-4	1987	However, when the heparin was treated with an amino group blocking agent prior to labelling with DENMT, the resultant heparin-dye conjugate showed binding behaviour, the strength of which was consistent with heparin molecules having both high and low affinity for antithrombin III.	Heparin	118-125	serpin family C member 1	Homo sapiens	264-280
17107942-4	2007	Upon PTH stimulation, metalloprotease cleavage of membrane-bound heparin-binding fragment (HB-EGF) induced EGFR transactivation of ERK.	Heparin	65-72	heparin binding EGF like growth factor	Homo sapiens	91-97
3109497-5	1987	Heparin molecules with a high affinity for antithrombin III did not possess free amino groups.	Heparin	0-7	serpin family C member 1	Homo sapiens	43-59
18292505-9	2008	Heparin treatment of cultures induces many of the same biological effects as treatment with heparan sulfate, including elevated pERK levels in preBCR+ cells.	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 3	Homo sapiens	128-132
3664518-0	1987	Conformation of the pentasaccharide corresponding to the binding site of heparin to antithrombin-III.	Heparin	73-80	serpin family C member 1	Homo sapiens	84-100
17557562-0	2007	Utility of the clinical practice of administering thrombophilic screening and antithrombotic prophylaxis with low-molecular-weight heparin to healthy donors treated with G-CSF for mobilization of peripheral blood stem cells.	Heparin	131-138	colony stimulating factor 3	Homo sapiens	170-175
17376263-5	2007	Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI.	Heparin	43-50	serpin family C member 1	Homo sapiens	130-142
17376263-5	2007	Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI.	Heparin	75-82	serpin family C member 1	Homo sapiens	130-142
18056266-0	2008	Heparin strongly enhances the formation of beta2-microglobulin amyloid fibrils in the presence of type I collagen.	Heparin	0-7	beta-2-microglobulin	Homo sapiens	43-62
3656435-5	1987	DNA binding assays using partially purified mutant proteins indicate that mutations in two widely separated regions of the protein each result in loss of heparin-resistant complexes between Cre and a loxP site.	Heparin	154-161	site-specific integrase	Escherichia phage P1	190-193
18303934-4	2008	Although unfractionated heparin (UFH) has been the mainstay of antithrombin therapy in the past, it has numerous clinical and biochemical limitations, including substantial protein binding (leading to inconsistent bioavailability), a need for frequent monitoring and adjustment, unreliable and variable degrees of anticoagulation, significant platelet activation, risk of heparin-induced thrombocytopenia, and the inability to block clot bound thrombin.	Heparin	24-31	serpin family C member 1	Homo sapiens	63-75
3110143-0	1987	Identification of a lysyl residue in antithrombin which is essential for heparin binding.	Heparin	73-80	serpin family C member 1	Homo sapiens	37-49
18303934-4	2008	Although unfractionated heparin (UFH) has been the mainstay of antithrombin therapy in the past, it has numerous clinical and biochemical limitations, including substantial protein binding (leading to inconsistent bioavailability), a need for frequent monitoring and adjustment, unreliable and variable degrees of anticoagulation, significant platelet activation, risk of heparin-induced thrombocytopenia, and the inability to block clot bound thrombin.	Heparin	33-36	serpin family C member 1	Homo sapiens	63-75
18284938-0	2008	Heparin and low molecular weight heparins as scaffolds for assembling antithrombin and serine proteases.	Heparin	0-7	serpin family C member 1	Homo sapiens	70-82
18284938-0	2008	Heparin and low molecular weight heparins as scaffolds for assembling antithrombin and serine proteases.	Heparin	33-41	serpin family C member 1	Homo sapiens	70-82
17135256-8	2007	Heparin diminishes the avidity of colon carcinoma cells for P- and L-selectin, which may compromise integrin-mediated firm adhesion to host cells and mitigate metastasis.	Heparin	0-7	selectin L	Homo sapiens	67-77
17251460-5	2007	Wound- and LPA-induced shedding of HB-EGF was assessed by measuring the release of alkaline phosphatase (AP) in a stable THCE cell line that expressed HB-EGF with AP inserted in the heparin-binding site.	Heparin	182-189	heparin binding EGF like growth factor	Homo sapiens	35-41
17251460-5	2007	Wound- and LPA-induced shedding of HB-EGF was assessed by measuring the release of alkaline phosphatase (AP) in a stable THCE cell line that expressed HB-EGF with AP inserted in the heparin-binding site.	Heparin	182-189	heparin binding EGF like growth factor	Homo sapiens	151-157
18070750-9	2007	Finally, addition of CM of heparin- or insulin-treated adipocytes to HAECs stimulated monocyte adhesion to these cells, an effect that was abrogated by an anti-LPL antibody.	Heparin	27-34	lipoprotein lipase	Homo sapiens	160-163
3110143-1	1987	Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent pyridoxal 5"-phosphate.	Heparin	88-95	serpin family C member 1	Homo sapiens	51-63
3110143-5	1987	Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin.	Heparin	72-79	serpin family C member 1	Homo sapiens	29-41
17597201-5	2007	Aminated CarboSil can also be employed to initially couple heparin to the surface, and then the carboxylic acid groups on heparin can be further used to anchor TM.	Heparin	122-129	thrombomodulin	Homo sapiens	160-162
17600786-8	2007	Although the mechanism of heparin binding involves covalent boronate ester formation, it can be completely reversed by protamine addition, similar to heparin"s complex formation with antithrombin III.	Heparin	26-33	serpin family C member 1	Homo sapiens	183-199
17600786-8	2007	Although the mechanism of heparin binding involves covalent boronate ester formation, it can be completely reversed by protamine addition, similar to heparin"s complex formation with antithrombin III.	Heparin	150-157	serpin family C member 1	Homo sapiens	183-199
3110143-5	1987	Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin.	Heparin	72-79	serpin family C member 1	Homo sapiens	123-135
3110143-5	1987	Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin.	Heparin	154-161	serpin family C member 1	Homo sapiens	29-41
17337889-7	2007	E-Cadherin expression in the metastatic tissue of animals treated with taurolidine/heparin was significantly decreased (p = 0.016).	Heparin	83-90	cadherin 1	Rattus norvegicus	0-10
3110143-5	1987	Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin.	Heparin	154-161	serpin family C member 1	Homo sapiens	29-41
3110143-10	1987	Additionally, phosphopyridoxylation of antithrombin in the presence of added heparin indicated that several other lysyl residues were "protected" from modification.	Heparin	77-84	serpin family C member 1	Homo sapiens	39-51
17576819-4	2007	Antisense oligonucleotides against VEGF-receptor 2 (VEGF-R2) prevented the permeability-inducing activity of extracellular RNA and heparin completely.	Heparin	131-138	kinase insert domain receptor	Rattus norvegicus	35-50
3110143-11	1987	Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein.	Heparin	43-50	serpin family C member 1	Homo sapiens	141-153
17576819-4	2007	Antisense oligonucleotides against VEGF-receptor 2 (VEGF-R2) prevented the permeability-inducing activity of extracellular RNA and heparin completely.	Heparin	131-138	kinase insert domain receptor	Rattus norvegicus	52-59
17482241-2	2007	INTRODUCTION: A heparin preparation with low antithrombin activity and different disaccharide composition than mammalian heparin was isolated from the body of the ascidian Styela plicata (Chordata-Tunicata).	Heparin	16-23	serpin family C member 1	Homo sapiens	45-57
3110143-11	1987	Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein.	Heparin	115-122	serpin family C member 1	Homo sapiens	141-153
17482241-9	2007	CONCLUSION: The antithrombin-mediated anticoagulant activity of heparin polymers is not directly related to antithrombotic potency in the arterio-venous shunt.	Heparin	64-71	serpin family C member 1	Homo sapiens	16-28
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	serpin family C member 1	Homo sapiens	57-73
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	serpin family C member 1	Homo sapiens	75-81
17656819-6	2007	Although Al induced tau aggregation in a heparin-induced tau assembly assay, these aggregates were neither thioflavin T positive nor did they resemble tau fibrils seen in human AD brains.	Heparin	41-48	microtubule associated protein tau	Homo sapiens	57-60
3660328-8	1987	The decrease of AT III induced by heparin administrated during dialysis is likely to account for this relative decrease of AT III activity.	Heparin	34-41	serpin family C member 1	Homo sapiens	16-22
17656819-6	2007	Although Al induced tau aggregation in a heparin-induced tau assembly assay, these aggregates were neither thioflavin T positive nor did they resemble tau fibrils seen in human AD brains.	Heparin	41-48	microtubule associated protein tau	Homo sapiens	57-60
16919351-2	2006	A heparin-based delivery system (HBDS) was used to immobilize NT-3 within fibrin scaffolds via non-covalent interactions.	Heparin	2-9	neurotrophin 3	Rattus norvegicus	62-66
3660328-8	1987	The decrease of AT III induced by heparin administrated during dialysis is likely to account for this relative decrease of AT III activity.	Heparin	34-41	serpin family C member 1	Homo sapiens	123-129
3663126-2	1987	All these proteins, like EF-2, were selectively retained by a heparin-Sepharose column, which we used as an affinity-chromatography step.	Heparin	62-69	eukaryotic translation elongation factor 2	Homo sapiens	25-29
17068295-7	2006	Competition and direct binding assays indicate that the strong interaction of ANGPTL4 with the ECM is heparin/heparan sulfate proteoglycan dependent.	Heparin	102-109	angiopoietin like 4	Homo sapiens	78-85
17893975-7	2007	Also, interaction of ANXA5 with ligands involved in hemostasis, such as sulfatide and heparin, has been demonstrated.	Heparin	86-93	annexin A5	Homo sapiens	21-26
3473488-7	1987	In a two-stage chromogenic thrombin inactivation assay, under pseudo-first-order conditions, at 16 nM antithrombin III the t1/2 was 74 min and 50 min for plasma and COS cell-derived antithrombin III, respectively, in the absence of heparin.	Heparin	232-239	serpin family C member 1	Homo sapiens	102-118
17489664-1	2007	Enoxaparin is a low-molecular-weight heparin (LMWH) derivative that exerts its anticoagulant activity through antithrombin III, an endogenous inhibitor of factor Xa and thrombin IIa.	Heparin	37-44	serpin family C member 1	Homo sapiens	110-126
17348690-4	2007	SPR analysis shows that heparin binds with different affinities to active fragments of the proteins Hedgehog (Hh), Interference Hedgehog (Ihog), Cam-related/Down-regulated by Oncogenes (CDO), and Sonic Hedgehog (Shh).	Heparin	24-31	sonic hedgehog signaling molecule	Homo sapiens	196-210
18221095-6	2006	These drugs do not rely on blocking serine proteases nor do they require a co-factor (antithrombin III) like unfractionated heparin (UFH) or low molecular weight heparin (LMWH).	Heparin	124-131	serpin family C member 1	Homo sapiens	86-102
18221095-6	2006	These drugs do not rely on blocking serine proteases nor do they require a co-factor (antithrombin III) like unfractionated heparin (UFH) or low molecular weight heparin (LMWH).	Heparin	133-136	serpin family C member 1	Homo sapiens	86-102
16824188-6	2006	This Fg/VWF-independent aggregation was blocked by thrombin inhibitors (heparin, hirudin, PPACK), and thrombin or thrombin receptor activation peptide (AYPGKF-NH(2)) induced aggregation of gel-filtered Fg/VWF(-/-) platelets in 1 mm Ca(2+) PIPES buffer.	Heparin	72-79	Von Willebrand factor	Mus musculus	8-11
17348690-4	2007	SPR analysis shows that heparin binds with different affinities to active fragments of the proteins Hedgehog (Hh), Interference Hedgehog (Ihog), Cam-related/Down-regulated by Oncogenes (CDO), and Sonic Hedgehog (Shh).	Heparin	24-31	sonic hedgehog signaling molecule	Homo sapiens	212-215
3473488-7	1987	In a two-stage chromogenic thrombin inactivation assay, under pseudo-first-order conditions, at 16 nM antithrombin III the t1/2 was 74 min and 50 min for plasma and COS cell-derived antithrombin III, respectively, in the absence of heparin.	Heparin	232-239	serpin family C member 1	Homo sapiens	182-198
3038185-3	1987	Heparin-like structures of the vessel wall have been proposed as another regulatory mechanism catalyzing the inhibition of thrombin by antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	135-151
17110602-5	2007	In vitro, ANGPTL3 inhibited the phospholipase activity of endothelial lipase (EL), which hydrolyzes HDL-PL and hence decreases plasma HDL levels, through a putative heparin-binding site in the N-terminal domain of ANGPTL3.	Heparin	165-172	lipase, endothelial	Mus musculus	58-76
18688288-7	2007	Osteopontin and core binding factor alpha1 gene expression was 6-fold and 4-fold greater for hMSCs exposed to fluvastatin in the presence of the heparin functionalities, respectively.	Heparin	145-152	secreted phosphoprotein 1	Homo sapiens	0-11
16809550-1	2006	OBJECTIVE: Extracellular superoxide dismutase (EC-SOD) is a secreted antioxidant enzyme that binds to the outer plasma membrane and extracellular matrix through its heparin-binding domain (HBD).	Heparin	165-172	superoxide dismutase 3, extracellular	Mus musculus	11-45
16809550-1	2006	OBJECTIVE: Extracellular superoxide dismutase (EC-SOD) is a secreted antioxidant enzyme that binds to the outer plasma membrane and extracellular matrix through its heparin-binding domain (HBD).	Heparin	165-172	superoxide dismutase 3, extracellular	Mus musculus	47-53
16763062-4	2006	IGF-I and heparin blocked binding of IGFBP-3 to matrix when added with the binding protein but were unable to displace IGFBP-3 already bound to the matrix.	Heparin	10-17	insulin like growth factor binding protein 3	Homo sapiens	37-44
3038185-4	1987	In the present study, the interaction of antithrombin III with the thrombin-TM complex and its interference with heparin and polycations were investigated by using human components and TM isolated from the microvasculature of rabbit lung.	Heparin	113-120	serpin family C member 1	Homo sapiens	41-57
16763062-6	2006	Mutation of the C-terminal basic domain of IGFBP-3 (228KGRKR--&gt;MDGEA) resulted in markedly reduced binding to matrix compared with wild-type IGFBP-3, whereas mutation of the adjacent consensus heparin-binding domain (220KKK--&gt;HSR) had relatively little effect.	Heparin	196-203	insulin like growth factor binding protein 3	Homo sapiens	43-50
3567355-0	1987	Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His.	Heparin	0-7	serpin family C member 1	Homo sapiens	32-48
16837648-10	2007	Treatment of IC BUC with heparin-binding epidermal growth factor-like growth factor (HB-EGF), previously shown to be secreted in lower amounts by IC BUC, significantly increased inward potassium current.	Heparin	25-32	epidermal growth factor	Homo sapiens	41-64
16837648-10	2007	Treatment of IC BUC with heparin-binding epidermal growth factor-like growth factor (HB-EGF), previously shown to be secreted in lower amounts by IC BUC, significantly increased inward potassium current.	Heparin	25-32	heparin binding EGF like growth factor	Homo sapiens	85-91
16897046-7	2006	Rational initial empiric treatment in acute CAD to prevent secondary embolism is partial thromboplastin time-guided anticoagulation by intravenous heparin followed by anticoagulation with warfarin.	Heparin	147-154	aconitate decarboxylase 1	Homo sapiens	44-47
3567355-1	1987	Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity.	Heparin	126-133	serpin family C member 1	Homo sapiens	0-16
16754660-2	2006	We found recently that heparin stimulates BMP activity in vitro (Takada, T., Katagiri, T., Ifuku, M., Morimura, N., Kobayashi, M., Hasegawa, K., Ogamo, A., and Kamijo, R. (2003) J. Biol.	Heparin	23-30	bone morphogenetic protein 1	Homo sapiens	42-45
3567355-1	1987	Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity.	Heparin	126-133	serpin family C member 1	Homo sapiens	18-24
16754660-5	2006	In the present study, we examined whether heparin enhances bone formation induced by BMPs in vivo and attempted to determine the molecular mechanism by which heparin stimulates BMP activity using C2C12 myoblasts.	Heparin	42-49	bone morphogenetic protein 1	Homo sapiens	85-88
16963119-2	2007	Heparin-functionalized hydrogels supported hMSC viability, as quantified through live/dead imaging, and induced osteogenic differentiation, as measured by increased alkaline phosphatase (ALP) production and osteopontin (OPN) and collagen I (COL I) gene expression over the 5-week study.	Heparin	0-7	secreted phosphoprotein 1	Homo sapiens	207-218
16754660-10	2006	These findings clearly indicate that heparin enhances BMP-induced osteoblast differentiation not only in vitro but also in vivo.	Heparin	37-44	bone morphogenetic protein 1	Homo sapiens	54-57
3567355-1	1987	Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity.	Heparin	126-133	serpin family C member 1	Homo sapiens	57-69
16754660-11	2006	This study indicates that heparin enhances BMP-induced osteoblast differentiation in vitro and in vivo by protecting BMPs from degradation and inhibition by BMP antagonists.	Heparin	26-33	bone morphogenetic protein 1	Homo sapiens	43-46
16963119-2	2007	Heparin-functionalized hydrogels supported hMSC viability, as quantified through live/dead imaging, and induced osteogenic differentiation, as measured by increased alkaline phosphatase (ALP) production and osteopontin (OPN) and collagen I (COL I) gene expression over the 5-week study.	Heparin	0-7	secreted phosphoprotein 1	Homo sapiens	220-223
3567355-4	1987	By heparin-Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl.	Heparin	3-10	serpin family C member 1	Homo sapiens	37-43
16754660-11	2006	This study indicates that heparin enhances BMP-induced osteoblast differentiation in vitro and in vivo by protecting BMPs from degradation and inhibition by BMP antagonists.	Heparin	26-33	bone morphogenetic protein 1	Homo sapiens	117-120
3494808-5	1987	Serum, LDL, HDL, and heparin inhibit the hemolytic activity of PFP by blocking its binding to lipid membranes.	Heparin	21-28	perforin 1	Homo sapiens	63-66
16820297-3	2006	The regulatory advantages provided by structural mobility are best illustrated by the heparin activation mechanisms of the plasma serpins antithrombin and heparin cofactor II.	Heparin	86-93	serpin family C member 1	Homo sapiens	138-150
16720575-0	2006	Heparin synergistically enhances interleukin-11 signaling through up-regulation of the MAPK pathway.	Heparin	0-7	interleukin 11	Homo sapiens	33-47
16720575-2	2006	Furthermore, we found that, although heparin alone has no effect, it is able to synergistically enhance Interleukin-11 (IL-11)-induced signal transducer and activator of transcription 3 (STAT3) activation and thus increase osteoclast formation in vitro.	Heparin	37-44	interleukin 11	Homo sapiens	104-118
16720575-2	2006	Furthermore, we found that, although heparin alone has no effect, it is able to synergistically enhance Interleukin-11 (IL-11)-induced signal transducer and activator of transcription 3 (STAT3) activation and thus increase osteoclast formation in vitro.	Heparin	37-44	interleukin 11	Homo sapiens	120-125
16720575-3	2006	In the present study, we examine the effect of various serine kinase inhibitors on the ability of heparin to act synergistically with IL-11.	Heparin	98-105	interleukin 11	Homo sapiens	134-139
16817162-0	2006	Binding of Ca2+, Mg2+, and heparin by human serum amyloid P component in affinity capillary electrophoresis.	Heparin	27-34	amyloid P component, serum	Homo sapiens	44-69
17059423-1	2007	BACKGROUND: Soluble thrombomodulin is a promising therapeutic natural anticoagulant that is comparable to antithrombin, tissue factor pathway inhibitor and activated protein C. OBJECTIVES: We conducted a multicenter, double-blind, randomized, parallel-group trial to compare the efficacy and safety of recombinant human soluble thrombomodulin (ART-123) to those of low-dose heparin for the treatment of disseminated intravascular coagulation (DIC) associated with hematologic malignancy or infection.	Heparin	374-381	thrombomodulin	Homo sapiens	20-34
16555944-7	2007	Similarly, LPL activity measured in the plasma after intravenous injection of heparin at the end of the experiments was 16 % lower (p&lt;0.05) after glucose administration.	Heparin	78-85	lipoprotein lipase	Homo sapiens	11-14
17917621-8	2007	UFH is likely to be replaced by more effective and safer antithrombin agents, such as DTIs.	Heparin	0-3	serpin family C member 1	Homo sapiens	57-69
16817162-4	2006	We now work out conditions to characterize the binding of Ca(2+) and Mg(2+) and the binding of heparin to SAP in the presence of divalent metal ions by ACE.	Heparin	95-102	amyloid P component, serum	Homo sapiens	106-109
2443128-1	1987	Heparin catalyses the inhibition of two key enzymes of blood coagulation, namely Factor Xa and thrombin, by enhancing the antiproteinase activities of plasma antithrombin III and heparin cofactor II.	Heparin	0-7	serpin family C member 1	Homo sapiens	158-174
16515805-0	2007	Heparin chain-length dependence of factor Xa inhibition by antithrombin in plasma.	Heparin	0-7	serpin family C member 1	Homo sapiens	59-71
16794256-8	2006	SP-C and AQP-5 mRNA levels were increased by heparin alone in a dose- and sulfation-dependent manner, while all FGFs lacked effect on SP-C or AQP-5 mRNA levels.	Heparin	45-52	aquaporin 5	Homo sapiens	9-14
2443128-12	1987	Reversal of the inhibitory effects of heparin and pentosan polysulphate was associated with the accelerated formation of 125I-thrombin-antithrombin III and 125I-thrombin-heparin cofactor complexes respectively.	Heparin	38-45	serpin family C member 1	Homo sapiens	135-151
16790765-8	2006	This phosphorylation was inhibited by the CKII inhibitors heparin and 4,5,6,7,-tetrabromo-2-azabenzimidazole.	Heparin	58-65	casein kinase 2 alpha 1	Homo sapiens	42-46
3606717-2	1987	LPL from post-heparin plasma was first purified by heparin Sepharose 4B affinity chromatography.	Heparin	14-21	lipoprotein lipase	Homo sapiens	0-3
16922281-1	2006	The interactions between granulocyte-macrophage colony-stimulating factor (GM-CSF) and heparin or low-molecular weight heparin (LMWH) were studied by CZE.	Heparin	87-94	colony stimulating factor 2	Homo sapiens	75-81
16922281-2	2006	It was found that GM-CSF could bind to both heparin and LMWH.	Heparin	44-51	colony stimulating factor 2	Homo sapiens	18-24
17146553-2	2006	A heparin-like substance with an anticoagulant activity equivalent to 10% of mammalian heparin and about 5% as potent as the mammalian counterpart for the inhibition of thrombin by antithrombin was isolated from the oocyte test cells.	Heparin	2-9	serpin family C member 1	Homo sapiens	181-193
3472589-5	1987	The effects of thrombin and heparin on the mutant ATIII were similar to controls.	Heparin	28-35	serpin family C member 1	Homo sapiens	50-55
16922281-4	2006	The specificity of the interaction between GM-CSF and heparin was also studied by employing another sulfated K carrageenan oligosaccharide as a control.	Heparin	54-61	colony stimulating factor 2	Homo sapiens	43-49
16922281-5	2006	Results showed that K carrageenan oligosaccharide could not interact with GM-CSF, indicating that GM-CSF could specifically interact with heparin.	Heparin	138-145	colony stimulating factor 2	Homo sapiens	98-104
16709175-5	2006	Thus the presence of heparin increases the potency of HGF/SF in experiments with cells in culture leading to elevated downstream signalling effects and, although not vital for the Met-HGF/SF interaction, heparin or heparan sulphate is essential for the activity of certain isoforms of HGF/SF, such as NK1 and NK2.	Heparin	21-28	tachykinin receptor 1	Homo sapiens	301-304
3615614-1	1987	The systematic search for a deficiency in antithrombin III must be considered in case of: venous thrombosis in a young patient, recurrent venous thrombosis especially if these occurred under Heparin, venous mesenteric infarction since this type of thrombosis is rare and seems relatively frequent in case of congenital deficiency in antithrombin III, familial past history of venous thrombosis in a woman desiring to undergo estrogen-progesterone therapy.	Heparin	191-198	serpin family C member 1	Homo sapiens	42-58
16675258-10	2006	Heparin was given during cardiopulmonary bypass to maintain an activated clotting time above 480 s. RESULTS: Patients in the enoxaparin group needed more heparin to maintain an activated clotting time above 480 s, and had higher heparin concentrations and lower antithrombin values compared with control patients.	Heparin	0-7	serpin family C member 1	Homo sapiens	262-274
16997938-0	2006	Investigation of the effects of heparin and low molecular weight heparin on E-cadherin and laminin expression in rat pregnancy by immunohistochemistry.	Heparin	65-72	cadherin 1	Rattus norvegicus	76-86
16997938-2	2006	This study was designed to investigate the effects of heparin and LMWHs, enoxaparin and tinzaparin, on E-cadherin and laminin expression in placental and decidual tissues in rat pregnancy.	Heparin	54-61	cadherin 1	Rattus norvegicus	103-113
16997938-5	2006	RESULTS: E-cadherin placental staining score of heparin group was significantly lower and E-cadherin decidual staining score of heparin and enoxaparin groups were significantly lower than control group.	Heparin	48-55	cadherin 1	Rattus norvegicus	9-19
16997938-5	2006	RESULTS: E-cadherin placental staining score of heparin group was significantly lower and E-cadherin decidual staining score of heparin and enoxaparin groups were significantly lower than control group.	Heparin	128-135	cadherin 1	Rattus norvegicus	90-100
16997938-7	2006	CONCLUSIONS: Heparin and enoxaparin can reduce E-cadherin expression but not laminin expression in rat pregnancy.	Heparin	13-20	cadherin 1	Rattus norvegicus	47-57
3494653-5	1987	The androgen receptor was also partially purified using heparin-sepharose chromatography The involvement of the anddrogen receptor in the mode of action of trenbolone is discussed.	Heparin	56-63	androgen receptor	Ovis aries	4-21
16945929-2	2006	The LG4-5 module at the C terminus of laminin alpha1 contains major binding sites for heparin, sulfatide, and alpha-dystroglycan and plays a critical role in early embryonic development.	Heparin	86-93	laminin subunit alpha 1	Homo sapiens	38-52
16683212-4	2006	METHODS: Using data from the CRUSADE Initiative, we evaluated LMWH and UFH in high-risk NSTE ACS patients (positive cardiac markers and/or ischemic ST-segment changes) who had received early (&lt; 24 hours) GP IIb/IIIa inhibitor therapy and underwent early invasive management.	Heparin	71-74	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	93-96
16683212-16	2006	Our results support the current ACC/AHA guidelines recommendations but raise concerns about the safety and efficacy of UFH in the setting of background use of upstream GP IIb/IIIa inhibitors for patients with NSTE ACS in routine clinical practice.	Heparin	119-122	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	214-217
16676077-0	2006	Benefit/risk profile of high-dose antithrombin in patients with severe sepsis treated with and without concomitant heparin.	Heparin	115-122	serpin family C member 1	Homo sapiens	34-46
16567083-0	2006	Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity.	Heparin	0-7	serpin family C member 1	Homo sapiens	73-85
16882661-4	2006	The common heparin-binding site is situated at the convex face of domain IV of annexin A2.	Heparin	11-18	annexin A2	Homo sapiens	79-89
16567083-1	2006	The durability and functionality of a heparin coating on artificial heart valve leaflets were evaluated with X-ray photoelectron spectroscopy (XPS) and by the coatings" capacity to bind antithrombin.	Heparin	38-45	serpin family C member 1	Homo sapiens	186-198
3590093-1	1987	The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III).	Heparin	22-29	serpin family C member 1	Homo sapiens	195-211
16567083-4	2006	It was found that the heparin coating was stable and wear resistant enough to still be present after 3 weeks and to have about the same antithrombin uptake as coatings not exposed to circulating plasma.	Heparin	22-29	serpin family C member 1	Homo sapiens	136-148
16882661-11	2006	The combined data provide a clear basis for the calcium dependence of heparin binding to annexin A2.	Heparin	70-77	annexin A2	Homo sapiens	89-99
3590093-1	1987	The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III).	Heparin	22-29	serpin family C member 1	Homo sapiens	213-219
3565746-14	1987	125I-Fluoresceinamine-derivatized heparin retains its ability to interact specifically with heparin-binding proteins such as human protease nexin-I and antithrombin III.	Heparin	34-41	serpin family E member 2	Homo sapiens	131-147
16963080-11	2006	Surface plasmon resonance measurements also indicate that this domain binds heparin, a known ligand of domain IV in the full-length annexin A2, although with lower affinity.	Heparin	76-83	annexin A2	Homo sapiens	132-142
16575261-0	2006	Antithrombin Nagasaki (Ser 116 to Pro): a rare antithrombin variant with abnormal heparin binding presenting during pregnancy.	Heparin	82-89	serpin family C member 1	Homo sapiens	0-12
16575261-0	2006	Antithrombin Nagasaki (Ser 116 to Pro): a rare antithrombin variant with abnormal heparin binding presenting during pregnancy.	Heparin	82-89	serpin family C member 1	Homo sapiens	47-59
3565746-14	1987	125I-Fluoresceinamine-derivatized heparin retains its ability to interact specifically with heparin-binding proteins such as human protease nexin-I and antithrombin III.	Heparin	34-41	serpin family C member 1	Homo sapiens	152-168
16575261-2	2006	Studies suggest, however, that individuals heterozygous for missense mutations involving the heparin-binding site of antithrombin do not have a significantly increased thrombotic risk.	Heparin	93-100	serpin family C member 1	Homo sapiens	117-129
16575261-4	2006	We report here the case of a pregnant woman with an exceptionally rare Type II heparin-binding site antithrombin variant.	Heparin	79-86	serpin family C member 1	Homo sapiens	100-112
16982928-6	2006	Finally, simultaneous cell incubation with the polyanion molecules, poly-L-glutamic acid or heparin, restored MMP-1 gene expression but incompletely inhibited MBP- and EPO-induced transcriptional effects as well as endothelin-1 and PDGF-AB release, suggesting that cationic proteins act partially through their cationic charge.	Heparin	92-99	matrix metallopeptidase 1	Homo sapiens	110-115
3791206-0	1987	Heparin binding affinity of rat prostatic growth factor in normal and cancerous prostates: partial purification and characterization of rat prostatic growth factor in the Dunning tumor.	Heparin	0-7	myotrophin	Rattus norvegicus	42-55
16880140-3	2006	Heparin concentration recovery, in vitro, was dependent on the plasma antithrombin concentration for all 3 assays.	Heparin	0-7	serpin family C member 1	Homo sapiens	70-82
16648575-4	2006	Flow cytometry revealed heparin-binding activity in the AbFPs containing IL-12 and IL-2, although this activity seems to be decreased in the bi-AbFPs.	Heparin	24-31	interleukin 2	Mus musculus	83-87
3791206-0	1987	Heparin binding affinity of rat prostatic growth factor in normal and cancerous prostates: partial purification and characterization of rat prostatic growth factor in the Dunning tumor.	Heparin	0-7	myotrophin	Rattus norvegicus	150-163
16880140-4	2006	The antithrombin-supplemented assay demonstrated improved heparin recovery in direct correlation to the heparin concentration in the plasma.	Heparin	58-65	serpin family C member 1	Homo sapiens	4-16
16880140-4	2006	The antithrombin-supplemented assay demonstrated improved heparin recovery in direct correlation to the heparin concentration in the plasma.	Heparin	104-111	serpin family C member 1	Homo sapiens	4-16
16601834-0	2006	Less pronounced enhancement of thrombin-dependent inactivation of plasminogen activator inhibitor type 1 by low molecular weight heparin compared with unfractionated heparin.	Heparin	129-136	serpin family E member 1	Homo sapiens	66-104
3427899-2	1987	An attempt was made to purify lipoprotein lipase (LpL) from the flight muscle of the migratory locust based on affinity for heparin, which is known to avidly bind mammalian LpL.	Heparin	124-131	lipoprotein lipase	Homo sapiens	50-53
16601834-1	2006	Plasminogen activator inhibitor type 1 (PAI-1), the primary inhibitor of plasminogen activators, also forms high molecular weight complexes with either thrombin or factor Xa (FXa) in the presence of heparin, resulting in the loss of mutual activities of enzyme and inhibitor.	Heparin	199-206	serpin family E member 1	Homo sapiens	0-38
16601834-1	2006	Plasminogen activator inhibitor type 1 (PAI-1), the primary inhibitor of plasminogen activators, also forms high molecular weight complexes with either thrombin or factor Xa (FXa) in the presence of heparin, resulting in the loss of mutual activities of enzyme and inhibitor.	Heparin	199-206	serpin family E member 1	Homo sapiens	40-45
16601834-3	2006	In the present study, we compared the effects of low molecular weight (LMW)- and unfractionated-heparin on the interaction between PAI-1 and either thrombin or FXa.	Heparin	96-103	serpin family E member 1	Homo sapiens	131-136
16601834-4	2006	Both types of heparin enhanced the inhibition of thrombin activity by PAI-1 with a bell-shaped pattern, though the magnitude of the enhancement was significantly weaker with LMW-heparin.	Heparin	14-21	serpin family E member 1	Homo sapiens	70-75
16601834-6	2006	In the presence of vitronectin (Vn), the inhibition of thrombin and FXa by PAI-1 was further promoted by both types of heparin but to a significantly lesser extent with LMW-heparin.	Heparin	119-126	serpin family E member 1	Homo sapiens	75-80
16601834-8	2006	As a consequence of thrombin-dependent inactivation of PAI-1, tPA-induced fibrin clot lysis time in the presence of PAI-1 was shortened by unfractionated-heparin as well as by LMW-heparin with lesser extent, which was further enhanced by Vn.	Heparin	154-161	serpin family E member 1	Homo sapiens	55-60
16601834-8	2006	As a consequence of thrombin-dependent inactivation of PAI-1, tPA-induced fibrin clot lysis time in the presence of PAI-1 was shortened by unfractionated-heparin as well as by LMW-heparin with lesser extent, which was further enhanced by Vn.	Heparin	154-161	serpin family E member 1	Homo sapiens	116-121
16470783-7	2006	However, binding of folate induced a distinct increase in FBP-peak symmetry, and using heparin as an affinity displacer, the free FBP in equilibrium with folate-FBP complexes could readily be separated from the complexes.	Heparin	87-94	folate receptor alpha	Bos taurus	130-133
16880140-7	2006	Classification of the clinical adequacy of patient heparin levels showed agreement of 80% or more between the antithrombin-supplemented and nonsupplemented assays.	Heparin	51-58	serpin family C member 1	Homo sapiens	110-122
16969073-1	2006	An N-glycosylated 60-kDa PV-1 protein that binds heparin was detected in mouse lung from a single mRNA transcript.	Heparin	49-56	plasmalemma vesicle associated protein	Mus musculus	25-29
16780802-2	2006	The anti-inflammatory activities of heparin have partly been related to inhibition of P-selectin binding.	Heparin	36-43	selectin P	Homo sapiens	86-96
16699957-0	2006	The apoptotic endonuclease DFF40/CAD is inhibited by RNA, heparin and other polyanions.	Heparin	58-65	aconitate decarboxylase 1	Homo sapiens	33-36
16699957-3	2006	In addition, other anionic polymers, like poly-glutamic acid and heparin also inhibit DFF40/CAD, the latter one being highly effective at nanomolar concentrations.	Heparin	65-72	aconitate decarboxylase 1	Homo sapiens	92-95
16470783-7	2006	However, binding of folate induced a distinct increase in FBP-peak symmetry, and using heparin as an affinity displacer, the free FBP in equilibrium with folate-FBP complexes could readily be separated from the complexes.	Heparin	87-94	folate receptor alpha	Bos taurus	130-133
3427899-2	1987	An attempt was made to purify lipoprotein lipase (LpL) from the flight muscle of the migratory locust based on affinity for heparin, which is known to avidly bind mammalian LpL.	Heparin	124-131	lipoprotein lipase	Homo sapiens	173-176
16470783-9	2006	The heparin interaction fractionated FBP into distinct subfractions, and the CE approach thus promises to be useful for unraveling the complex oligomerization behavior of FBP isoforms as well as for evaluating the FBP affinity for various species and analogs of glycosaminoglycans and folate.	Heparin	4-11	folate receptor alpha	Bos taurus	37-40
16470783-9	2006	The heparin interaction fractionated FBP into distinct subfractions, and the CE approach thus promises to be useful for unraveling the complex oligomerization behavior of FBP isoforms as well as for evaluating the FBP affinity for various species and analogs of glycosaminoglycans and folate.	Heparin	4-11	folate receptor alpha	Bos taurus	171-174
3609485-3	1987	Moderately reduced ATIII activity before or immediately after surgery is neither sensitive nor specific for a high risk of postoperative venous thromboembolism (VTE), while moderately reduced ATIII activity during heparin treatment for VTE fails to indicate an unusually large heparin requirement or to predict recurrence.	Heparin	214-221	serpin family C member 1	Homo sapiens	192-197
16470783-9	2006	The heparin interaction fractionated FBP into distinct subfractions, and the CE approach thus promises to be useful for unraveling the complex oligomerization behavior of FBP isoforms as well as for evaluating the FBP affinity for various species and analogs of glycosaminoglycans and folate.	Heparin	4-11	folate receptor alpha	Bos taurus	171-174
16954536-0	2006	Structural effects of a covalent linkage between antithrombin and heparin: covalent N-terminus attachment of heparin enhances the maintenance of antithrombin"s activated state.	Heparin	66-73	serpin family C member 1	Homo sapiens	145-157
16954536-0	2006	Structural effects of a covalent linkage between antithrombin and heparin: covalent N-terminus attachment of heparin enhances the maintenance of antithrombin"s activated state.	Heparin	109-116	serpin family C member 1	Homo sapiens	49-61
3692172-6	1987	A likely candidate for the heparin-binding site is a 9-aa stretch containing five positive charges, analogous to the consensus sequence for receptor-binding sites on apolipoproteins E and B.	Heparin	27-34	apolipoprotein E	Cavia porcellus	166-189
16954536-0	2006	Structural effects of a covalent linkage between antithrombin and heparin: covalent N-terminus attachment of heparin enhances the maintenance of antithrombin"s activated state.	Heparin	109-116	serpin family C member 1	Homo sapiens	145-157
16954536-2	2006	This study was designed to elucidate the covalent linkage point(s) for heparin on antithrombin and conformational properties of the ATH molecule.	Heparin	71-78	serpin family C member 1	Homo sapiens	82-94
16954536-8	2006	The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin.	Heparin	25-32	serpin family C member 1	Homo sapiens	72-84
16954536-8	2006	The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin.	Heparin	25-32	serpin family C member 1	Homo sapiens	183-195
16525583-0	2006	The ability of different forms of heparins to suppress P-selectin function in vitro correlates to their inhibitory capacity on bloodborne metastasis in vivo.	Heparin	34-42	selectin P	Homo sapiens	55-65
16525583-1	2006	Ample evidence suggests that many of the in vivo anti-metastatic effects by heparins reflect their actions on P-selectin-mediated binding.	Heparin	76-84	selectin P	Homo sapiens	110-120
16525583-2	2006	We hypothesized that the ability of widely used heparins and derivatives to interfere with P-selectin-dependent tumour cell interactions under flow in vitro could be used to identify anticoagulants with advanced inhibitory functions on experimental blood-borne metastasis in vivo.	Heparin	48-56	selectin P	Homo sapiens	91-101
16525583-5	2006	Importantly, the superior inhibitory capacity on P-selectin function of unfractionated heparin and LMWH nadroparin as opposed to LMWH enoxaparin and synthetic heparin pentasaccharide fondaparinux strongly correlated to the inhibitory potency of each in inhibiting experimental lung metastasis in vivo.	Heparin	87-94	selectin P	Homo sapiens	49-59
16954536-8	2006	The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin.	Heparin	157-164	serpin family C member 1	Homo sapiens	72-84
16954536-8	2006	The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin.	Heparin	157-164	serpin family C member 1	Homo sapiens	183-195
3111953-3	1987	In the presence of heparin, AT III is converted from its progressive activity state to an immediate activity state.	Heparin	19-26	serpin family C member 1	Homo sapiens	28-34
16728399-3	2006	Recently we showed that a mixture of undersulfated octasaccharides exhibiting 7 and 8 sulfates (7,8-S-OctaF7) generated from heparin had the highest affinity for FGF7 monitored by salt resistance (&gt;0.60 M salt) of octasaccharide-FGF7 complexes.	Heparin	125-132	fibroblast growth factor 7	Mus musculus	162-166
16737974-1	2006	In this study, we present multiple lines of evidence to support a critical role for heparin-bound EGF (epidermal growth factor)-like growth factor (HB-EGF) and tumor necrosis factor-alpha-converting enzyme (TACE) (ADAM17) in the transactivation of EGF receptor (EGFR), ERK phosphorylation, and cellular proliferation induced by the 5-HT(2A) receptor in renal mesangial cells.	Heparin	84-91	heparin binding EGF like growth factor	Homo sapiens	148-154
16737974-1	2006	In this study, we present multiple lines of evidence to support a critical role for heparin-bound EGF (epidermal growth factor)-like growth factor (HB-EGF) and tumor necrosis factor-alpha-converting enzyme (TACE) (ADAM17) in the transactivation of EGF receptor (EGFR), ERK phosphorylation, and cellular proliferation induced by the 5-HT(2A) receptor in renal mesangial cells.	Heparin	84-91	EPH receptor B2	Homo sapiens	269-272
16475811-0	2006	Heparin accelerates gelsolin amyloidogenesis.	Heparin	0-7	gelsolin	Homo sapiens	20-28
16493483-4	2006	The purpose of this study was to compare the effects of low (LMW) or high molecular weight (HMW) fucoidans to those of standard heparin and LMW heparin on PN-1 properties.	Heparin	144-151	serpin family E member 2	Homo sapiens	155-159
16493483-7	2006	Moreover, the formation of PN-1/(125)I-thrombin complex was increased in the presence of heparin, HMW and LMW fucoidans, but barely by LMW heparin.	Heparin	89-96	serpin family E member 2	Homo sapiens	27-31
16493483-10	2006	PN-1 was detached by fucoidans and heparins and was still able to inhibit thrombin.	Heparin	35-43	serpin family E member 2	Homo sapiens	0-4
16417632-0	2006	HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: effects on VEGF, FGF-1, and SDF-1.	Heparin	77-84	sulfatase 2	Homo sapiens	0-7
16417632-4	2006	We previously cloned a cDNA encoding a novel human endosulfatase, HSulf-2, which removes 6-O-sulfate groups on glucosamine from subregions of intact heparin.	Heparin	149-156	sulfatase 2	Homo sapiens	66-73
16417632-6	2006	To determine whether HSulf-2 modulates the interactions between heparin-binding factors and heparin, we developed an ELISA, in which soluble factors were allowed to bind to immobilized heparin.	Heparin	64-71	sulfatase 2	Homo sapiens	21-28
2828272-1	1987	In order to obtain a radioiodinated antithrombin III (AT III) with a good labelling yield and optimal biological properties towards heparin, thrombin and its anti-AT III monoclonal antibodies, we compared the classical labelling methods and found them wanting.	Heparin	132-139	serpin family C member 1	Homo sapiens	36-52
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	113-120	sulfatase 2	Homo sapiens	190-197
16413239-1	2006	We hypothesized that infusion of recombinant human antithrombin without concomitant heparin would have dose-dependent anticoagulant properties and potentially decrease endotoxin (lipopolysaccharide [LPS])-induced cytokine production.	Heparin	84-91	serpin family C member 1	Homo sapiens	51-63
16672689-0	2006	Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin-independent mechanism.	Heparin	48-55	serpin family C member 1	Homo sapiens	105-117
16505491-6	2006	This was surprising because IGFBP-5 reportedly interacts with PAI-1 via its heparin-binding domain.	Heparin	76-83	serine (or cysteine) peptidase inhibitor, clade E, member 1	Mus musculus	62-67
2828272-1	1987	In order to obtain a radioiodinated antithrombin III (AT III) with a good labelling yield and optimal biological properties towards heparin, thrombin and its anti-AT III monoclonal antibodies, we compared the classical labelling methods and found them wanting.	Heparin	132-139	serpin family C member 1	Homo sapiens	54-60
2834484-2	1987	A diagnosis of heparin induced thrombocytopenia (HIT) in the 26 patients was based on: 1. normal platelet count prior to heparin administration; 2. its fall to less than 100 Giga/l (m = 46 +/- 23) at time of first sample collection for test to detect a platelet aggregation factor (PAF); 3.	Heparin	15-22	peroxisomal biogenesis factor 12	Homo sapiens	253-289
16289605-0	2006	A novel application of multi-wavelength TIRF spectroscopy for real time monitoring of antithrombin interactions with immobilized heparin.	Heparin	129-136	serpin family C member 1	Homo sapiens	86-98
16244492-4	2006	Our case shows that a combined treatment with antithrombin substitution and a prophylactic, body-weight-adjusted dose of low-molecular-weight heparin may be successful in preventing pregnancy loss and thromboembolism in antithrombin deficiency during pregnancy, although other complications, such as preeclampsia and intrauterine growth restriction cannot always be prevented.	Heparin	142-149	serpin family C member 1	Homo sapiens	220-232
17113870-5	2006	Sulf-1 and Sulf-2 have been cloned and identified as sulfatases that release sulfate groups on the C-6 position of GlcNAc residue from an internal subdomain in intact heparin.	Heparin	167-174	extracellular sulfatase Sulf-1	Cricetulus griseus	0-6
16289605-1	2006	Real time interactions of antithrombin (AT) with Corline Heparin Surfaces (CHS) with one and two layers of heparin conjugate have been examined using a multi-wavelength TIRF spectroscopy technique with continuous flow.	Heparin	107-114	serpin family C member 1	Homo sapiens	26-38
16289605-1	2006	Real time interactions of antithrombin (AT) with Corline Heparin Surfaces (CHS) with one and two layers of heparin conjugate have been examined using a multi-wavelength TIRF spectroscopy technique with continuous flow.	Heparin	107-114	serpin family C member 1	Homo sapiens	40-42
3332689-5	1987	Glycosaminoglycans (heparin) inhibit nerve fiber growth on fibronectin substrata.	Heparin	20-27	fibronectin 1	Rattus norvegicus	59-70
16289605-2	2006	Fluorescently labeled AT, adsorbed from citrated human blood plasma, showed significantly higher signals on CHS compared to the cationic surface used to attach the heparin conjugate.	Heparin	164-171	serpin family C member 1	Homo sapiens	22-24
16289605-3	2006	The AT binding to CHS was very stable, also after exposure to soluble heparin at a concentration of 1.5 IU/mL.	Heparin	70-77	serpin family C member 1	Homo sapiens	4-6
16289605-5	2006	In contrast, larger amounts of the freshly added AT had adsorbed to the surfaces, especially to the surface with two layers of heparin conjugate, indicating the presence of unsaturated AT binding sites.	Heparin	127-134	serpin family C member 1	Homo sapiens	49-51
16051347-5	2005	This ATIII adsorption was mediated by the heparin layer, since surfaces modified with PEG only did not adsorb significant quantities of AT.	Heparin	42-49	serpin family C member 1	Homo sapiens	5-10
16338497-6	2005	These data indicate that heparin as effective cofactor for TPO and IL-11 promotes expansion of MK progenitor cells from CB CD34(+) cells.	Heparin	25-32	interleukin 11	Homo sapiens	67-72
2431720-8	1986	The mechanism of heparin-induced increase in lipoprotein lipase secretion was explored.	Heparin	17-24	lipase, endothelial	Mus musculus	57-63
16437314-2	2005	UFH is still the recommended antithrombin as soon as percutaneous coronary interventions (PCI) are performed, although the results of different trials clearly have demonstrated the benefit of enoxaparin also in interventional cardiology.	Heparin	0-3	serpin family C member 1	Homo sapiens	29-41
16291163-1	2005	PURPOSE: We have previously demonstrated that heparin-binding epidermal growth factor-like growth factor (HB-EGF) is an intestinal cytoprotective agent.	Heparin	46-53	heparin binding EGF like growth factor	Homo sapiens	106-112
16357320-4	2006	TACI binding appears to require heparan sulfate posttranslational modifications of syndecan-2, because free heparin or pretreatment with heparitinase blocked the interaction.	Heparin	108-115	TNF receptor superfamily member 13B	Homo sapiens	0-4
16613771-3	2006	Up-to-date antithrombin therapy consists of vitamin K antagonists, unfractionated and low molecular heparins, direct thrombin inhibitors and selective inhibitors of factor Xa.	Heparin	100-108	serpin family C member 1	Homo sapiens	11-23
3798418-2	1986	The interaction between the immobilized heparin, added thrombin, and antithrombin III [AT] was investigated.	Heparin	40-47	serpin family C member 1	Homo sapiens	69-85
16360204-4	2006	The entrapment of heparin molecules was confirmed by a negatively increased zeta potential value and the specific binding affinity to antithrombin III.	Heparin	18-25	serpin family C member 1	Homo sapiens	134-150
16100390-8	2005	The upregulated expression of these fibroblast marker proteins was significantly inhibited by heparin, but not by an integrin inhibitor, indicating that a heparin-binding motif in the extracellular domain might be an active site of osteoactivin.	Heparin	94-101	glycoprotein (transmembrane) nmb	Mus musculus	232-244
3596677-5	1986	The binding of SAP to Fn was selectively inhibited by a monoclonal antibody specific for the mid-molecule region of Fn, by soluble gelatin, and by heparin in the presence of 3mM Ca++.	Heparin	147-154	amyloid P component, serum	Homo sapiens	15-18
16100390-8	2005	The upregulated expression of these fibroblast marker proteins was significantly inhibited by heparin, but not by an integrin inhibitor, indicating that a heparin-binding motif in the extracellular domain might be an active site of osteoactivin.	Heparin	155-162	glycoprotein (transmembrane) nmb	Mus musculus	232-244
16111491-5	2005	Exogenous heparin or chondroitin sulfate impaired, in a dose-dependent manner the attachment of C6 glioma cell line to laminin and fibronectin, but not to type IV collagen.	Heparin	10-17	fibronectin 1	Rattus norvegicus	131-142
16111491-8	2005	Furthermore, heparin and chondroitin sulfate impaired C6 cells proliferation on fibronectin, but not on type IV collagen or laminin.	Heparin	13-20	fibronectin 1	Rattus norvegicus	80-91
16368135-4	2006	The capacity of surface bound heparin to promote ATIII-mediated thrombin inactivation was investigated in a parallel plate flow chamber under simulated venous and arterial wall shear rates of 50 and 500 s(-1), respectively.	Heparin	30-37	serpin family C member 1	Homo sapiens	49-54
16376423-7	2006	These studies are the first to demonstrate the additive effect of surface bound heparin and TM as a combined interactive strategy to limit TF-induced thrombin formation.	Heparin	80-87	coagulation factor III, tissue factor	Homo sapiens	139-141
3798412-6	1986	This suggests that Factor Xa and antithrombin III have similar affinities for this immobilized heparin, unlike the situation for thrombin (Thromb-Res., 20, 543-554, 1980).	Heparin	95-102	serpin family C member 1	Homo sapiens	33-49
16331491-0	2006	Chemically modified heparin inhibits the in vitro adhesion of nonsmall cell lung cancer cells to P-selectin.	Heparin	20-27	selectin P	Homo sapiens	97-107
16331491-2	2006	The mechanism of inhibition by the heparin derivatives in part accounts for the interference of tumor cell-platelet interaction mediated by P-selectin.	Heparin	35-42	selectin P	Homo sapiens	140-150
16331491-3	2006	METHODS: In the present study, we demonstrated that both heparin and chemically modified heparins inhibited the adhesion of nonsmall cell lung cancer (NSCLC) cells to P-selectin under static or flow conditions in vitro.	Heparin	57-64	selectin P	Homo sapiens	167-177
15985216-8	2005	Taken as a whole, our results demonstrate that there is a direct connection between the dependence of endostatin activity on heparin-like glycosaminoglycans and its ability to antagonize bFGF.	Heparin	125-132	collagen type XVIII alpha 1 chain	Homo sapiens	102-112
16331491-3	2006	METHODS: In the present study, we demonstrated that both heparin and chemically modified heparins inhibited the adhesion of nonsmall cell lung cancer (NSCLC) cells to P-selectin under static or flow conditions in vitro.	Heparin	89-97	selectin P	Homo sapiens	167-177
3790695-8	1986	Antithrombin III, a natural thrombin inhibitor, did not significantly reduce the thrombin concentrations, but antithrombin III accelerated by heparin greatly reduced the local thrombin concentrations.	Heparin	142-149	serpin family C member 1	Homo sapiens	110-126
3766461-7	1986	The anti-Factor Xa activity of heparin was measured using chromogenic substrate S-2251, purified Factor Xa, and excess antithrombin III.	Heparin	31-38	serpin family C member 1	Homo sapiens	119-135
16322097-4	2006	The results presented in this study demonstrate that this heparin binding domain (HBD) is the region of Vn that binds to the cysteine loop region of beta3 and that this region is sufficient to mediate the positive effects of Vn on IGF-I signaling.	Heparin	58-65	basic helix-loop-helix family member e22	Homo sapiens	149-154
16026276-8	2005	Some patients with very low AT levels may be resistant to heparin therapy and may require increased doses of heparin or AT concentrates.	Heparin	58-65	serpin family C member 1	Homo sapiens	28-30
16026276-8	2005	Some patients with very low AT levels may be resistant to heparin therapy and may require increased doses of heparin or AT concentrates.	Heparin	109-116	serpin family C member 1	Homo sapiens	28-30
3767984-2	1986	We report here that a synthetic heparin pentasaccharide with high affinity for antithrombin III has the same effect as heparin at about the same concentration.	Heparin	32-39	serpin family C member 1	Homo sapiens	79-95
3756191-8	1986	First, post-heparin plasma lipoprotein lipase activity and immunoreactivity detected by an enzyme-linked immunosorbent assay (ELISA) co-eluted during heparin-agarose and phenyl-Sepharose chromatography.	Heparin	12-19	lipoprotein lipase	Homo sapiens	27-45
16034135-3	2005	We have previously demonstrated that heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) decreases proinflammatory cytokine IL-8 and NO production in cytokine-stimulated intestinal epithelial cells by interfering with the NF-kappaB signaling pathway.	Heparin	37-44	heparin binding EGF like growth factor	Homo sapiens	103-109
16532012-0	2006	Heparan sulfate C5-epimerase is essential for heparin biosynthesis in mast cells.	Heparin	46-53	glucuronyl C5-epimerase	Mus musculus	0-28
16532012-3	2006	We have generated Hsepi-null mouse mutant mast cells, and we show that the same enzyme catalyzes the generation of IdoA in heparin and that "heparin" lacking IdoA shows a distorted O-sulfation pattern.	Heparin	123-130	glucuronyl C5-epimerase	Mus musculus	18-23
16532012-3	2006	We have generated Hsepi-null mouse mutant mast cells, and we show that the same enzyme catalyzes the generation of IdoA in heparin and that "heparin" lacking IdoA shows a distorted O-sulfation pattern.	Heparin	141-148	glucuronyl C5-epimerase	Mus musculus	18-23
3755846-6	1986	In the presence of heparin, measurement of the rate of inhibition under pseudo first order conditions can be made only when the NaCl concentration is at least 0.3 M. The significance of the presented data for designing a functional assay of AT III is discussed.	Heparin	19-26	serpin family C member 1	Homo sapiens	241-247
16307734-3	2006	It is the vascular endothelial-bound LPL that determines the rate of plasma TG clearance, and, hence, it is also called heparin-releasable (HR) "functional" LPL.	Heparin	120-127	lipoprotein lipase	Homo sapiens	37-40
16307734-3	2006	It is the vascular endothelial-bound LPL that determines the rate of plasma TG clearance, and, hence, it is also called heparin-releasable (HR) "functional" LPL.	Heparin	120-127	lipoprotein lipase	Homo sapiens	157-160
16542481-5	2006	Preclinical research has demonstrated partial interference of heparin--administered even at low doses--with the therapeutic effects of antithrombin, and has confirmed--at the level of cellular mechanisms--a regulatory role for antithrombin in DIC.	Heparin	62-69	serpin family C member 1	Homo sapiens	135-147
16310171-0	2006	Interactions of low-molecular-weight semi-synthetic sulfated heparins with human leukocyte elastase and human Cathepsin G.	Heparin	61-69	cathepsin G	Homo sapiens	110-121
16028903-1	2005	HRMAS NMR of tau paired helical fragments assembled with heparin show an intensity decrease for those amino acids that are incorporated into the rigid core region, whereas the N-terminal amino acids maintain their full mobility.	Heparin	57-64	microtubule associated protein tau	Homo sapiens	13-16
15967359-1	2005	In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III).	Heparin	226-233	serpin family C member 1	Homo sapiens	336-352
15967359-1	2005	In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III).	Heparin	226-233	serpin family C member 1	Homo sapiens	354-360
15967359-5	2005	The interactions between immobilized heparin and AT III were studied with various concentrations under various conditions.	Heparin	37-44	serpin family C member 1	Homo sapiens	49-55
15878877-9	2005	When LPL was first bound to the heparin-coated chip, apoA-V-enriched chylomicrons showed binding.	Heparin	32-39	lipoprotein lipase	Homo sapiens	5-8
16310171-4	2006	A non-linear relationship was found between degree of sulfation and binding affinity or enzyme inhibition properties, showing a composite correlation between heparin charge density and interference with EL/CatG activity.	Heparin	158-165	cathepsin G	Homo sapiens	206-210
3775688-1	1986	A qualitative defect of antithrombin III (AT III) was demonstrated in four members of a large Tunisian family by the discrepancy between a normal amount of antigen and decreased or absent heparin cofactor activity.	Heparin	188-195	serpin family C member 1	Homo sapiens	24-40
16475731-10	2006	CONCLUSION: Our results suggest that heparin can promote the proliferation and up-regulation of c-Myc protein expression in gastric cancer cells.	Heparin	37-44	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	96-101
16701827-0	2005	Heparin functionalized PEG gels that modulate protein adsorption for hMSC adhesion and differentiation.	Heparin	0-7	progestagen associated endometrial protein	Homo sapiens	23-26
16701827-4	2005	Results demonstrate that methacrylate-modified heparin retained its ability to bind heparin-binding proteins both in solution and when copolymerized with dimethacrylated PEG in a hydrogel.	Heparin	47-54	progestagen associated endometrial protein	Homo sapiens	170-173
3775688-1	1986	A qualitative defect of antithrombin III (AT III) was demonstrated in four members of a large Tunisian family by the discrepancy between a normal amount of antigen and decreased or absent heparin cofactor activity.	Heparin	188-195	serpin family C member 1	Homo sapiens	42-48
15922935-2	2005	Inspired by the ternary complex formation of heparin with antithrombin III and thrombin, the active pentasaccharide fondaparinux has been succeeded by several clinical candidates, such as SR123781, that have tailor-made factor Xa and thrombin inhibitory activities combined with less aspecific binding (e.g. binding to platelet factor 4 involved in thrombocytopenia).	Heparin	45-52	serpin family C member 1	Homo sapiens	58-74
17170521-6	2006	Pretreatment of cells with heparin, a non-selective inhibitor of G protein-coupled receptor kinases (GRKs), prevented the observed attenuation of SKF 38393-induced inhibition of Cl-/HCO3- exchange.	Heparin	27-34	G protein-coupled receptor kinase 4	Rattus norvegicus	101-105
3775688-4	1986	Anti-F. Xa activity was also absent when using low molecular weight heparin or a synthetic pentasaccharide, representing the binding site to AT III.	Heparin	68-75	serpin family C member 1	Homo sapiens	141-147
3775688-5	1986	The lack of affinity of the propositus AT III for heparin was demonstrated by two-dimensional immunoelectrophoresis and chromatography on heparin-Sepharose.	Heparin	50-57	serpin family C member 1	Homo sapiens	39-45
16542495-1	2006	INTRODUCTION: Acquired antithrombin III (AT) deficiency may induce heparin resistance and premature membrane clotting during continuous renal replacement therapy (CRRT).	Heparin	67-74	serpin family C member 1	Homo sapiens	23-39
15957976-5	2005	Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned.	Heparin	34-37	serpin family C member 1	Homo sapiens	0-12
3775688-6	1986	The parents, first cousins, and the sister of the propositus also demonstrated a qualitative abnormality of AT III, with levels of heparin cofactor activity close to 50% of the normal range.	Heparin	131-138	serpin family C member 1	Homo sapiens	108-114
15957976-5	2005	Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned.	Heparin	245-248	serpin family C member 1	Homo sapiens	0-12
3730415-6	1986	Most of the injected lipase located in the liver, and could be released back into circulation by injection of heparin.	Heparin	110-117	lipase, endothelial	Mus musculus	21-27
16226436-2	2006	Several BMPs bind strongly to heparin, and heparan sulfate proteoglycans (HSPGs) at the cell surface or in the extracellular matrix have recently been implicated as modulators of BMP signaling in some developing systems.	Heparin	30-37	bone morphogenetic protein 1	Homo sapiens	8-11
15797889-0	2005	A single bolus of a low molecular weight heparin to patients on haemodialysis depletes lipoprotein lipase stores and retards triglyceride clearing.	Heparin	41-48	lipoprotein lipase	Homo sapiens	87-105
3800906-0	1986	A fragment of antithrombin that binds both heparin and thrombin.	Heparin	43-50	serpin family C member 1	Homo sapiens	14-26
15797889-3	2005	Evidence from in vitro studies and from animal experiments indicate, however, that both types of heparin preparations have the same ability to release endothelial LPL, but LMWH are less effective in preventing uptake and degradation of LPL in the liver.	Heparin	97-104	lipoprotein lipase	Homo sapiens	163-166
16139336-0	2006	Increased expression of platelet P-selectin and formation of platelet-leukocyte aggregates in blood from patients treated with unfractionated heparin plus eptifibatide compared with bivalirudin.	Heparin	142-149	selectin P	Homo sapiens	33-43
17323590-1	2006	The antithrombin binding sequence of heparin, a pentasaccharide, has been synthesized as fondaparinux, an indirect, selective, and reversible factor Xa inhibitor.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
16338497-5	2005	In vivo, transfusion of CD34(+) cells expanded with TPO + IL-11 + heparin into irradiated nonobese diabetic/severe combined immunodeficient mice significantly accelerated platelet recovery.	Heparin	66-73	CD34 antigen	Mus musculus	24-28
15735670-3	2005	We previously found that heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a growth factor for malignant plasma cells.	Heparin	25-32	heparin binding EGF like growth factor	Homo sapiens	85-91
15924156-9	2005	Antithrombin concentrate is used in patients with antithrombin deficiency treated with heparin for acute venous thrombosis or embolism, extracorporeal circulation procedures or other invasive procedures.	Heparin	87-94	serpin family C member 1	Homo sapiens	0-12
3800906-2	1986	These fragments did not exhibit direct thrombin-neutralizing activity; however, one unique fragment was found to bind to heparin-Sepharose and also to interfere with the inhibition of thrombin by intact antithrombin.	Heparin	121-128	serpin family C member 1	Homo sapiens	203-215
15924156-9	2005	Antithrombin concentrate is used in patients with antithrombin deficiency treated with heparin for acute venous thrombosis or embolism, extracorporeal circulation procedures or other invasive procedures.	Heparin	87-94	serpin family C member 1	Homo sapiens	50-62
15924157-5	2005	Treatment with antithrombin and heparin resulted in a considerable increase in bleeding complications and on the other hand, may have antagonized the expected effect of antithrombin on the patient"s prognosis.	Heparin	32-39	serpin family C member 1	Homo sapiens	169-181
16303928-4	2005	METHODS: Solid-phase opticin binding assays were performed with immobilized type XVIII collagen and heparin albumin.	Heparin	100-107	opticin	Homo sapiens	21-28
3800906-4	1986	At a concentration of 46 nM, this product decreased the heparin-enhanced thrombin-inhibitory activity of antithrombin by half, and completely abolished this inhibition when above 300 nM.	Heparin	56-63	serpin family C member 1	Homo sapiens	105-117
16303928-7	2005	SPR showed that opticin bound to porcine intestinal mucosa HS and heparin with moderately high affinity (K(D) 73 and 43 nM, respectively).	Heparin	66-73	opticin	Homo sapiens	16-23
16303928-8	2005	Binding inhibition studies showed that hexasaccharides of heparin had a lower affinity for opticin than larger oligosaccharides; the sulfate groups of heparin contributed variably to opticin binding, with the group at ring position two of iduronate contributing least; and chondroitin sulfate A and B bound to opticin, whereas binding to chondroitin sulfate C and hyaluronan was not observed.	Heparin	58-65	opticin	Homo sapiens	91-98
3800906-9	1986	It is concluded that this peptide possesses portions of the antithrombin molecule that bind to heparin as well as to a site on thrombin.	Heparin	95-102	serpin family C member 1	Homo sapiens	60-72
3738858-4	1986	The accelerating effect of heparin or potassium polyvinylsulfate for the inhibitory action of AT III is abolished by charge equivalent amounts of polycation.	Heparin	27-34	serpin family C member 1	Homo sapiens	94-100
16146701-0	2005	Insights into the induced fit mechanism in antithrombin-heparin interaction using molecular dynamics simulations.	Heparin	56-63	serpin family C member 1	Homo sapiens	43-55
15710745-3	2005	In the current study, we found that EMAP II-alpha-ATP synthase interaction could be inhibited by excess heparin, whereas the interaction could be enhanced by a low concentration of heparin.	Heparin	104-111	aminoacyl tRNA synthetase complex interacting multifunctional protein 1	Homo sapiens	36-43
15710745-4	2005	Both EMAP II and alpha-ATP synthase could specifically interact with heparin, and this interaction was increased under acidic conditions.	Heparin	69-76	aminoacyl tRNA synthetase complex interacting multifunctional protein 1	Homo sapiens	5-12
15710745-5	2005	In addition, EMAP II and alpha-ATP synthase were found to contain the heparin binding motifs determined by analysis using site-directed mutant forms.	Heparin	70-77	aminoacyl tRNA synthetase complex interacting multifunctional protein 1	Homo sapiens	13-20
15710745-9	2005	Furthermore, the enhanced inhibitory effects of EMAP II could be abrogated by excess heparin or heparinase treatment.	Heparin	85-92	aminoacyl tRNA synthetase complex interacting multifunctional protein 1	Homo sapiens	48-55
15878772-5	2005	The patient LPL purified from post heparin plasma scarcely hydrolyzed VLDL-triglyceride and also triolein emulsified with Triton X-100 or phosphatidylcholine.	Heparin	35-42	lipoprotein lipase	Homo sapiens	12-15
3750270-1	1986	Serum amyloid P component (SAP), and its acute phase homologue C-reactive protein (CRP), prolonged activated partial thromboplastin times (APTT) in cell free plasma when assayed at physiological concentrations in the presence of heparin.	Heparin	229-236	amyloid P component, serum	Homo sapiens	0-25
3750270-1	1986	Serum amyloid P component (SAP), and its acute phase homologue C-reactive protein (CRP), prolonged activated partial thromboplastin times (APTT) in cell free plasma when assayed at physiological concentrations in the presence of heparin.	Heparin	229-236	amyloid P component, serum	Homo sapiens	27-30
3754869-4	1986	Functionally, S-protein in the presence of low concentrations of heparin, protects thrombin from inactivation by ATIII.	Heparin	65-72	serpin family C member 1	Homo sapiens	113-118
16234627-3	2005	There are developments in the role of low-molecular-weight heparin agents in management of acute coronary syndromes in the modern treatment era, in which early coronary revascularization and use of other potent antiplatelet and antithrombin agents are common.	Heparin	59-66	serpin family C member 1	Homo sapiens	228-240
15860994-6	2005	Fibrinolytic therapy, in combination with adjunctive antithrombin therapy that is simpler and quicker to administer (e.g., tenecteplase with enoxaparin), may be more efficacious and easier to use than regimens involving unfractionated heparin.	Heparin	235-242	serpin family C member 1	Homo sapiens	53-65
3699029-12	1986	These findings not only indicate a direct interaction of S protein with heparin in the onset of the inhibition of thrombin by antithrombin-III--heparin, but also a contribution of S protein during enzyme-inhibitor complex formation.	Heparin	72-79	serpin family C member 1	Homo sapiens	126-142
16124952-3	2005	METHODS: SYNERGY was an international, multicenter, randomized, open-label trial that compared enoxaparin with UFH in high-risk NSTE ACS patients managed with an early invasive strategy.	Heparin	111-114	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	133-136
3013215-5	1986	The residual anticoagulant activity of periodate-oxidized heparins obtained from preparations - such as those from beef lung - rich in trisulfated disaccharide sequences is discussed in terms of the influence of charge density on heparin-protease interactions not mediated by antithrombin.	Heparin	58-66	serpin family C member 1	Homo sapiens	276-288
15644496-3	2005	Soluble glycosaminoglycans such as heparin and heparan sulfate bind gp120 via V3 and, possibly, a CD4-induced domain.	Heparin	35-42	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	68-80
15644496-6	2005	Here, using surface plasmon resonance, we observed an inverse relationship between heparin binding by gp120 and its thiol content.	Heparin	83-90	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	102-107
15644496-7	2005	In vitro, and in conditions in which gp120 could bind CD4, heparin and heparan sulfate reduced PDI-mediated gp120 reduction by approximately 80%.	Heparin	59-66	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	37-42
15644496-7	2005	In vitro, and in conditions in which gp120 could bind CD4, heparin and heparan sulfate reduced PDI-mediated gp120 reduction by approximately 80%.	Heparin	59-66	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	108-113
15752359-0	2005	Identification of the heparin-binding domains of the interferon-induced protein kinase, PKR.	Heparin	22-29	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	88-91
15752359-7	2005	In addition to dsRNA, polyanionic agents such as heparin can also activate PKR.	Heparin	49-56	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	75-78
15752359-8	2005	In contrast to dsRNA-induced activation of PKR, heparin-dependent PKR activation has so far remained uncharacterized.	Heparin	48-55	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	66-69
15887238-8	2005	Inhibitors and neutralizing antibodies against heparin-binding epidermal growth factor-like growth factor (HB-EGF), and to a lesser extent transforming growth factor-alpha, reduced imatinib-mediated mitogen activated protein kinase (MAPK) activation.	Heparin	47-54	heparin binding EGF like growth factor	Homo sapiens	107-113
15812639-3	2005	We present experimental results using SPR for the interaction of insulin-like growth factor-I (IGF-I) with one of its binding proteins, IGF binding protein-3 (IGFBP-3), and show that the dissociation, even with the addition of soluble heparin in the dissociation phase, does not exhibit the expected exponential decay characteristic of a 1:1 binding reaction.	Heparin	235-242	insulin like growth factor binding protein 3	Homo sapiens	159-166
16181411-0	2005	Modulation of the homophilic interaction between the first and second Ig modules of neural cell adhesion molecule by heparin.	Heparin	117-124	neural cell adhesion molecule 1	Homo sapiens	84-113
16107729-6	2005	We also show that GrB-mediated cytotoxicity is abrogated by heparin and that target cells deficient in cell surface sulfate or glycosaminoglycans resist GrB.	Heparin	60-67	granzyme B	Homo sapiens	18-21
15752359-9	2005	In order to understand the mechanism of heparin-induced PKR activation, we have mapped the heparin-binding domains of PKR.	Heparin	40-47	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	56-59
3956877-9	1986	Liver perfusion studies showed that the heparin-releasable phospholipase A2 activity in the perfusate was significantly decreased in the diabetic rats when compared with control and controlled diabetic animals.	Heparin	40-47	phospholipase A2 group IB	Rattus norvegicus	59-75
15752359-9	2005	In order to understand the mechanism of heparin-induced PKR activation, we have mapped the heparin-binding domains of PKR.	Heparin	40-47	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	118-121
15752359-9	2005	In order to understand the mechanism of heparin-induced PKR activation, we have mapped the heparin-binding domains of PKR.	Heparin	91-98	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	56-59
15752359-9	2005	In order to understand the mechanism of heparin-induced PKR activation, we have mapped the heparin-binding domains of PKR.	Heparin	91-98	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	118-121
15752359-10	2005	Our results indicate that PKR has two heparin-binding domains that are nonoverlapping with its dsRNA-binding domains.	Heparin	38-45	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	26-29
15752359-12	2005	Point mutations created within these domains rendered PKR defective in heparin-binding, thereby confirming their essential role.	Heparin	71-78	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	54-57
2419721-2	1986	The lipase binds to Sepharose-heparin columns from which it can be eluted by 0.8 to 0.9 M NaCl.	Heparin	30-37	lipase G, endothelial type	Rattus norvegicus	4-10
15980072-0	2005	Fibrillin-1 interactions with heparin.	Heparin	30-37	fibrillin 1	Homo sapiens	0-11
15980072-3	2005	We have used BIAcore technology to investigate fibrillin-1 interactions with heparin and with heparin saccharides that are analogous to S-domains of heparan sulfate.	Heparin	77-84	fibrillin 1	Homo sapiens	47-58
15980072-4	2005	We have identified four high affinity heparin-binding sites on fibrillin-1, localized three of these sites, and defined their binding kinetics.	Heparin	38-45	fibrillin 1	Homo sapiens	63-74
3964663-2	1986	Interfacial catalysis of hepatic triacylglycerol lipase (H-TGL) and lipoprotein lipase (LpL) isolated from human post-heparin plasma was investigated with mixed monolayers of trioleoylglycerol (TO) and egg phosphatidylcholine.	Heparin	118-125	lipoprotein lipase	Homo sapiens	88-91
15980072-5	2005	Heparin binding to the fibrillin-1 N terminus has particularly rapid kinetics.	Heparin	0-7	fibrillin 1	Homo sapiens	23-34
3947650-0	1986	The catalysis by heparin of the reaction between thrombin and antithrombin.	Heparin	17-24	serpin family C member 1	Homo sapiens	62-74
15843596-4	2005	The method was applied to assay for the heparin substrate specificity of a newly discovered human extracellular endosulfatase, HSulf-2, which has been implicated in tumorigenesis.	Heparin	40-47	sulfatase 2	Homo sapiens	127-134
3947650-2	1986	The heparin-catalysed combination of thrombin and antithrombin is saturable with respect to both thrombin and antithrombin.	Heparin	4-11	serpin family C member 1	Homo sapiens	50-62
3947650-2	1986	The heparin-catalysed combination of thrombin and antithrombin is saturable with respect to both thrombin and antithrombin.	Heparin	4-11	serpin family C member 1	Homo sapiens	110-122
16102051-2	2005	Novel parenteral agents include synthetic analogs of the pentasaccharide sequence of heparin that mediates its interaction with antithrombin.	Heparin	85-92	serpin family C member 1	Homo sapiens	128-140
3947650-4	1986	The kinetics observed can be explained by proposing that the catalyst of the reaction is not heparin alone but a complex of heparin and antithrombin (bound at the high-affinity site).	Heparin	93-100	serpin family C member 1	Homo sapiens	136-148
3947172-4	1986	In vitro, only the combination of protamine sulfate and heparin, and neither alone, resulted in increased C3a and C4a.	Heparin	56-63	complement C4A (Rodgers blood group)	Homo sapiens	114-117
16004430-3	2005	The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity.	Heparin	38-45	serpin family C member 1	Homo sapiens	65-81
16004430-3	2005	The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity.	Heparin	38-45	serpin family C member 1	Homo sapiens	83-88
3718405-6	1986	Heparin seems to form a ternary complex with AT III and activated coagulation factors, so acting as a catalyst.	Heparin	0-7	serpin family C member 1	Homo sapiens	45-51
18555318-0	1986	Application of immobilized heparins for isolation of human antithrombin III.	Heparin	27-35	serpin family C member 1	Homo sapiens	59-75
15999048-0	2005	Recombinant human antithrombin III restores heparin responsiveness and decreases activation of coagulation in heparin-resistant patients during cardiopulmonary bypass.	Heparin	44-51	serpin family C member 1	Homo sapiens	18-34
15999048-0	2005	Recombinant human antithrombin III restores heparin responsiveness and decreases activation of coagulation in heparin-resistant patients during cardiopulmonary bypass.	Heparin	110-117	serpin family C member 1	Homo sapiens	18-34
15999048-1	2005	OBJECTIVES: We sought to evaluate the efficacy of recombinant human antithrombin III for restoration of heparin responsiveness in heparin-resistant patients scheduled for cardiac surgery.	Heparin	104-111	serpin family C member 1	Homo sapiens	68-84
15999048-1	2005	OBJECTIVES: We sought to evaluate the efficacy of recombinant human antithrombin III for restoration of heparin responsiveness in heparin-resistant patients scheduled for cardiac surgery.	Heparin	130-137	serpin family C member 1	Homo sapiens	68-84
15999048-13	2005	CONCLUSION: Treatment with recombinant human antithrombin III in a dose of 75 U/kg is effective in restoring heparin responsiveness and promoting therapeutic anticoagulation for cardiopulmonary bypass in the majority of heparin-resistant patients.	Heparin	109-116	serpin family C member 1	Homo sapiens	45-61
15999048-13	2005	CONCLUSION: Treatment with recombinant human antithrombin III in a dose of 75 U/kg is effective in restoring heparin responsiveness and promoting therapeutic anticoagulation for cardiopulmonary bypass in the majority of heparin-resistant patients.	Heparin	220-227	serpin family C member 1	Homo sapiens	45-61
15964810-5	2005	To address this, we developed a sensitive and quantitative assay for snRNP assembly, the formation of high-salt- and heparin-resistant stable Sm cores, that is strictly dependent on the SMN complex.	Heparin	117-124	LSM2 homolog, U6 small nuclear RNA and mRNA degradation associated	Homo sapiens	69-74
18555318-1	1986	Immobilized heparins were prepared by six different methods, and these were utilized for affinity purification of human antithrombin III (AT-III).	Heparin	12-20	serpin family C member 1	Homo sapiens	120-136
18555318-1	1986	Immobilized heparins were prepared by six different methods, and these were utilized for affinity purification of human antithrombin III (AT-III).	Heparin	12-20	serpin family C member 1	Homo sapiens	138-144
16296580-9	2005	MANAGEMENT OF THROMBOPHILIA: Treatment of patients with congenital AT III deficiency includes intravenous heparin and AT III concentrate (dosage 50 U/ kgbw).	Heparin	106-113	serpin family C member 1	Homo sapiens	67-73
18555318-2	1986	Affinity support capacities (mg AT-III/g support) were strongly influenced by immobilized active heparin concentrations.	Heparin	97-104	serpin family C member 1	Homo sapiens	32-38
3080419-2	1986	Antithrombin III Basel is a hereditary abnormal antithrombin with normal progressive inhibition activity (normal reactive site) and reduced heparin cofactor activity (impaired heparin binding site).	Heparin	140-147	serpin family C member 1	Homo sapiens	0-16
16113788-4	2005	Heparin, however, partially relieves this protective effect and at the same time it facilitates the inhibition of the intrinsic thrombin activity by antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	149-161
15681706-3	2005	Incubation of myocytes with LPA (1-100 nM) increased basal and heparin-releasable LPL (HR-LPL), an effect that was independent of shifts in LPL mRNA.	Heparin	63-70	lipoprotein lipase	Homo sapiens	82-85
3080419-2	1986	Antithrombin III Basel is a hereditary abnormal antithrombin with normal progressive inhibition activity (normal reactive site) and reduced heparin cofactor activity (impaired heparin binding site).	Heparin	140-147	serpin family C member 1	Homo sapiens	48-60
15681706-3	2005	Incubation of myocytes with LPA (1-100 nM) increased basal and heparin-releasable LPL (HR-LPL), an effect that was independent of shifts in LPL mRNA.	Heparin	63-70	lipoprotein lipase	Homo sapiens	90-93
3080419-6	1986	This substitution is close to an Arg (residue 47) and a Trp (residue 49) which have previously been shown to be critical for heparin binding by antithrombin III.	Heparin	125-132	serpin family C member 1	Homo sapiens	144-160
3080419-8	1986	These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41.	Heparin	33-40	serpin family C member 1	Homo sapiens	57-73
15882280-5	2005	After adjustment for illness severity, antithrombin-III levels increased significantly more over the period of study in the citrate as compared to the heparin group (P= 0.038).	Heparin	151-158	serpin family C member 1	Homo sapiens	39-55
3080419-8	1986	These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41.	Heparin	33-40	serpin family C member 1	Homo sapiens	184-200
3080419-8	1986	These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41.	Heparin	155-162	serpin family C member 1	Homo sapiens	57-73
3080419-8	1986	These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41.	Heparin	155-162	serpin family C member 1	Homo sapiens	184-200
3000827-0	1986	The heparin-binding site(s) of histidine-rich glycoprotein as suggested by sequence homology with antithrombin III.	Heparin	4-11	serpin family C member 1	Homo sapiens	98-114
15705969-2	2005	Although the EGFR ligand, heparin-binding epidermal growth factor-like growth factor (HB-EGF), is known to be released as a result of this stimulation, whether compressive stress enhances expression of other EGFR ligands, and the duration of mechanical compression required to initiate this response, is not known.	Heparin	26-33	heparin binding EGF like growth factor	Homo sapiens	86-92
15785094-6	2005	Gel mobility shift assays using oligonucleotides encoding the ET-1 AP-1 and ET-1 GATA sites confirmed that both AP-1 and GATA binding activities in BAEC nuclear extract were markedly inhibited by heparin.	Heparin	196-203	glutaminyl-tRNA amidotransferase subunit QRSL1	Homo sapiens	81-85
15785094-6	2005	Gel mobility shift assays using oligonucleotides encoding the ET-1 AP-1 and ET-1 GATA sites confirmed that both AP-1 and GATA binding activities in BAEC nuclear extract were markedly inhibited by heparin.	Heparin	196-203	glutaminyl-tRNA amidotransferase subunit QRSL1	Homo sapiens	121-125
3000827-1	1986	A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located.	Heparin	174-181	serpin family C member 1	Homo sapiens	129-145
3000827-1	1986	A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located.	Heparin	174-181	serpin family C member 1	Homo sapiens	147-153
15718352-0	2005	Higher concentrations of heparin and hirudin are required to inhibit thrombin generation in tissue factor-activated cord plasma than in adult plasma.	Heparin	25-32	coagulation factor III, tissue factor	Homo sapiens	92-105
15718352-5	2005	After strong activation with high amounts of TF (30 microM), the thrombin potential was significantly more suppressed in cord plasma compared with adult plasma in the presence of 0.4 IE/mL heparin (-92 versus -75%; p &lt; 0.01) and in the presence of 2 IE/mL hirudin (-18 versus -8%; p &lt; 0.01).	Heparin	189-196	coagulation factor III, tissue factor	Homo sapiens	45-47
15718352-6	2005	In contrast, after weak activation with low amounts of TF (30 pM), the thrombin potential was significantly more suppressed in adult plasma compared with neonatal plasma in the presence of 0.025 IE/mL heparin (-93 versus -8%; p &lt; 0.01) and in the presence of 2 IE/mL hirudin (-89 versus -48%; p &lt; 0.01).	Heparin	201-208	coagulation factor III, tissue factor	Homo sapiens	55-57
15731113-0	2005	Regulation of vascular smooth muscle proliferation by heparin: inhibition of cyclin-dependent kinase 2 activity by p27(kip1).	Heparin	54-61	cyclin dependent kinase inhibitor 1B	Homo sapiens	119-123
15731113-5	2005	Our results indicate that the heparin-induced block in G(1) to S phase transition is imposed by p27(kip1)-mediated inhibition of cyclin-dependent kinase 2 activity.	Heparin	30-37	cyclin dependent kinase inhibitor 1B	Homo sapiens	100-104
15731113-6	2005	Further analysis of p27(kip1) mRNA levels showed that the increase in p27(kip1) protein levels in heparin-treated VSMC occurs at posttranscriptional levels.	Heparin	98-105	cyclin dependent kinase inhibitor 1B	Homo sapiens	24-28
15731113-6	2005	Further analysis of p27(kip1) mRNA levels showed that the increase in p27(kip1) protein levels in heparin-treated VSMC occurs at posttranscriptional levels.	Heparin	98-105	cyclin dependent kinase inhibitor 1B	Homo sapiens	74-78
15731113-7	2005	We present evidence that heparin causes stabilization of p27(kip1) protein during G(1) phase and thereby prevents activation of cyclin-dependent kinase 2.	Heparin	25-32	cyclin dependent kinase inhibitor 1B	Homo sapiens	57-65
3000827-1	1986	A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located.	Heparin	174-181	serpin family C member 1	Homo sapiens	198-204
3000827-2	1986	The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG.	Heparin	99-106	serpin family C member 1	Homo sapiens	66-72
15741074-5	2005	Consecutive binding of the thrombin inhibitors heparin, antithrombin III or the heparin-antithrombin III complex to the immobilized thrombin molecules, and binding of a ternary complex of heparin, anithrombin III, and thrombin to aptamers was evaluated.	Heparin	80-87	serpin family C member 1	Homo sapiens	88-104
15741074-7	2005	Binding of heparin activated the formation of the inhibitory complex of antithrombin III with thrombin about 2.7-fold.	Heparin	11-18	serpin family C member 1	Homo sapiens	72-88
3000827-3	1986	These observations strongly suggest that the heparin-binding sites of HRG and AT III are evolutionarily related.	Heparin	45-52	serpin family C member 1	Homo sapiens	78-84
3940539-7	1986	Our data strongly suggest that the heparin-resistant neutral triacylglycerol lipase activity may not be the only determinant of endogenous lipolysis in the isolated rat heart and indicate that lipolysis may additionally be mediated by the lysosomal, acid lipase in concert with the microsomal mono-and diacylglycerol lipase.	Heparin	35-42	lipase G, endothelial type	Rattus norvegicus	77-83
16052301-4	2005	Heparins are the cornerstone of antithrombotic therapy in the current management of NSTE-ACS.	Heparin	0-8	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	89-92
3940539-7	1986	Our data strongly suggest that the heparin-resistant neutral triacylglycerol lipase activity may not be the only determinant of endogenous lipolysis in the isolated rat heart and indicate that lipolysis may additionally be mediated by the lysosomal, acid lipase in concert with the microsomal mono-and diacylglycerol lipase.	Heparin	35-42	lipase G, endothelial type	Rattus norvegicus	255-261
3940539-7	1986	Our data strongly suggest that the heparin-resistant neutral triacylglycerol lipase activity may not be the only determinant of endogenous lipolysis in the isolated rat heart and indicate that lipolysis may additionally be mediated by the lysosomal, acid lipase in concert with the microsomal mono-and diacylglycerol lipase.	Heparin	35-42	lipase G, endothelial type	Rattus norvegicus	255-261
3739751-7	1986	Post-heparin plasma activity of hepatic lipase was virtually absent and that of lipoprotein lipase was reduced by 50%.	Heparin	5-12	lipoprotein lipase	Homo sapiens	80-98
15736971-0	2005	The factor IXa heparin-binding exosite is a cofactor interactive site: mechanism for antithrombin-independent inhibition of intrinsic tenase by heparin.	Heparin	15-22	serpin family C member 1	Homo sapiens	85-97
15736971-1	2005	Therapeutic heparin concentrations selectively inhibit the intrinsic tenase complex in an antithrombin-independent manner.	Heparin	12-19	serpin family C member 1	Homo sapiens	90-102
15699163-7	2005	Fondaparinux, which is identical with the antithrombin III-binding pentasaccharide in heparin, did not bind to LBP or alter LBP function.	Heparin	86-93	serpin family C member 1	Homo sapiens	42-58
3583099-0	1986	Heparin preserves antithrombin III biological activity from hyperglycemia-induced alterations in insulin-dependent diabetics.	Heparin	0-7	serpin family C member 1	Homo sapiens	18-34
3583099-3	1986	The subcutaneous and endovenous heparin administration restores ATIII activity, but does not modify its plasma concentration in diabetics.	Heparin	32-39	serpin family C member 1	Homo sapiens	64-69
3583099-4	1986	Moreover, heparin treatment preserves ATIII activity from glycemia-induced alterations.	Heparin	10-17	serpin family C member 1	Homo sapiens	38-43
15644062-8	2005	IDH-NADP decreased its activity 50% in spermatozoa capacitated with heparin and acrosome reacted with progesterone (P &lt; 0.05).	Heparin	68-75	isocitrate dehydrogenase (NADP(+)) 2	Bos taurus	0-3
3583099-6	1986	Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII.	Heparin	37-44	serpin family C member 1	Homo sapiens	71-76
3583099-6	1986	Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII.	Heparin	37-44	serpin family C member 1	Homo sapiens	267-272
3733300-1	1986	The anticoagulant activity of heparin is dependent on its affinity for antithrombin III (AT III) and on its molecular weight.	Heparin	30-37	serpin family C member 1	Homo sapiens	71-87
15661045-3	2005	We have shown that uptake and activation of DC by VLP involves proteoglycan receptors and can be inhibited by heparin.	Heparin	110-117	VHL like	Homo sapiens	50-53
15661045-4	2005	Heparin has been shown to activate DC by signalling through Toll-like receptor 4 (TLR4) and nuclear factor (NF)-kappaB.	Heparin	0-7	toll like receptor 4	Homo sapiens	60-80
3733300-1	1986	The anticoagulant activity of heparin is dependent on its affinity for antithrombin III (AT III) and on its molecular weight.	Heparin	30-37	serpin family C member 1	Homo sapiens	89-95
15661045-4	2005	Heparin has been shown to activate DC by signalling through Toll-like receptor 4 (TLR4) and nuclear factor (NF)-kappaB.	Heparin	0-7	toll like receptor 4	Homo sapiens	82-86
15661045-8	2005	VLP-induced induction of costimulatory molecule expression, RelB activation and cytokine secretion by DC was blocked by inhibition of NF-kappaB activation, heparin or TLR4 mAb.	Heparin	156-163	VHL like	Homo sapiens	0-3
16178272-9	2005	The increase in cell adhesion was observed on plastic dishes, albumin, as well as on fibronectin pre-coated ones suggesting that heparin effect is substratum independent.	Heparin	129-136	fibronectin 1	Mus musculus	85-96
4063384-3	1985	Three significant quantitative differences were observed for the mollusc heparin when compared with the ones from mammalian origin, namely, a higher degree of binding with antithrombin III (45%), higher molecular weight (27-43 kDa) and higher anticoagulant activity (320 I.U./mg).	Heparin	73-80	serpin family C member 1	Homo sapiens	172-188
15604266-0	2004	The minimal active domain of endostatin is a heparin-binding motif that mediates inhibition of tumor vascularization.	Heparin	45-52	collagen type XVIII alpha 1 chain	Homo sapiens	29-39
15604266-2	2004	In the present study, we have investigated the role of the heparin-binding sites in the in vivo mechanism of action of endostatin.	Heparin	59-66	collagen type XVIII alpha 1 chain	Homo sapiens	119-129
15604266-3	2004	The majority of the heparin binding is mediated by arginines 155/158/184/270 in endostatin, but there is also a minor site constituted by arginines 193/194.	Heparin	20-27	collagen type XVIII alpha 1 chain	Homo sapiens	80-90
15604266-4	2004	Using endostatin mutants lacking either of these two sites, we show that inhibition of fibroblast growth factor-2-induced angiogenesis in the chicken chorioallantoic membrane requires both heparin-binding sites.	Heparin	189-196	collagen type XVIII alpha 1 chain	Homo sapiens	6-16
15604266-5	2004	In contrast, inhibition of vascular endothelial growth factor-A-induced chorioallantoic membrane angiogenesis by endostatin was only dependent on the minor heparin-binding site (R193/194).	Heparin	156-163	collagen type XVIII alpha 1 chain	Homo sapiens	113-123
15604266-7	2004	Moreover, we show that a synthetic peptide corresponding to amino acids 180-199 of human endostatin (which covers the minor heparin-binding site) inhibits endothelial cell chemotaxis and reduces tumor vascularization in vivo.	Heparin	124-131	collagen type XVIII alpha 1 chain	Homo sapiens	89-99
4043407-0	1985	Heparin binding to lipoprotein lipase and low density lipoproteins.	Heparin	0-7	lipoprotein lipase	Homo sapiens	19-37
15604266-9	2004	These data show an essential role for heparin binding in the antiangiogenic action of endostatin.	Heparin	38-45	collagen type XVIII alpha 1 chain	Homo sapiens	86-96
4043407-1	1985	Heparin was fractionated on an affinity column of bovine milk lipoprotein lipase (LpL) immobilized to Affi-Gel-15.	Heparin	0-7	lipoprotein lipase	Homo sapiens	62-80
15381701-5	2004	Here, we demonstrate that mammalian Chordin binds heparin with an affinity similar to that of factors known to functionally interact with heparan sulfate proteoglycans (HSPGs) in tissues.	Heparin	50-57	chordin	Homo sapiens	36-43
4043407-2	1985	The bound heparin, designated high-reactive heparin (HRH), enhanced LpL activity, presumably by stabilizing the enzyme against denaturation.	Heparin	10-17	lipoprotein lipase	Homo sapiens	68-71
4043407-2	1985	The bound heparin, designated high-reactive heparin (HRH), enhanced LpL activity, presumably by stabilizing the enzyme against denaturation.	Heparin	44-51	lipoprotein lipase	Homo sapiens	68-71
4043407-6	1985	Since LpL and LDL both bind to heparin-like molecules at the surface of the arterial wall, we suggest that their similar heparin-binding specificity may have physiological consequences as it relates to the development of atherosclerosis.	Heparin	31-38	lipoprotein lipase	Homo sapiens	6-9
4043407-6	1985	Since LpL and LDL both bind to heparin-like molecules at the surface of the arterial wall, we suggest that their similar heparin-binding specificity may have physiological consequences as it relates to the development of atherosclerosis.	Heparin	121-128	lipoprotein lipase	Homo sapiens	6-9
15253930-8	2004	The rNDST-1 was partially purified on heparin Sepharose CL-6B.	Heparin	38-45	N-deacetylase and N-sulfotransferase 1	Rattus norvegicus	4-11
4033424-1	1985	Two enzymes, lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL), are released into human plasma after intravenous injection of heparin.	Heparin	140-147	lipoprotein lipase	Homo sapiens	13-31
15371417-2	2004	The antithrombotic effect of heparin, however, is due primarily to the specific interaction of a fraction of heparin chains with the related serpin antithrombin (AT).	Heparin	29-36	serpin family C member 1	Homo sapiens	148-160
4033424-1	1985	Two enzymes, lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL), are released into human plasma after intravenous injection of heparin.	Heparin	140-147	lipoprotein lipase	Homo sapiens	33-36
15371417-2	2004	The antithrombotic effect of heparin, however, is due primarily to the specific interaction of a fraction of heparin chains with the related serpin antithrombin (AT).	Heparin	109-116	serpin family C member 1	Homo sapiens	148-160
4082101-2	1985	Both anti-activated factor X (anti Xa) and antithrombin activity were decreased, in the absence and in the presence of heparin, while protein concentration was normal in an immunological assay.	Heparin	119-126	serpin family C member 1	Homo sapiens	43-55
4082101-3	1985	The abnormal AT III copurified with functional AT III using insolubilized heparin affinity chromatography.	Heparin	74-81	serpin family C member 1	Homo sapiens	13-19
4082101-3	1985	The abnormal AT III copurified with functional AT III using insolubilized heparin affinity chromatography.	Heparin	74-81	serpin family C member 1	Homo sapiens	47-53
15535971-2	2004	As a result of the identification of FN fragment responsible for TNF-alpha secretion, a 30-kDa fragment derived from the carboxyl-terminal heparin-binding (Hep 2) domain of FN was isolated from the FN digest.	Heparin	139-146	fibronectin 1	Rattus norvegicus	37-39
4026027-8	1985	In addition, transfusion of AT III-rich donor plasma may be necessary when low plasma AT III reduces the effects of heparin.	Heparin	116-123	serpin family C member 1	Homo sapiens	28-34
15535971-2	2004	As a result of the identification of FN fragment responsible for TNF-alpha secretion, a 30-kDa fragment derived from the carboxyl-terminal heparin-binding (Hep 2) domain of FN was isolated from the FN digest.	Heparin	139-146	fibronectin 1	Rattus norvegicus	173-175
15535971-2	2004	As a result of the identification of FN fragment responsible for TNF-alpha secretion, a 30-kDa fragment derived from the carboxyl-terminal heparin-binding (Hep 2) domain of FN was isolated from the FN digest.	Heparin	139-146	fibronectin 1	Rattus norvegicus	173-175
4026027-8	1985	In addition, transfusion of AT III-rich donor plasma may be necessary when low plasma AT III reduces the effects of heparin.	Heparin	116-123	serpin family C member 1	Homo sapiens	86-92
4043133-3	1985	The mean rise of AT III activity by 40 U/kg per day heparin was 8.7%.	Heparin	52-59	serpin family C member 1	Homo sapiens	17-23
15544705-0	2004	Effects of heparin on the uptake of lipoprotein lipase in rat liver.	Heparin	11-18	lipase G, endothelial type	Rattus norvegicus	48-54
15544705-11	2004	When heparin was injected before the lipase, the initial immunostaining along sinusoids was weaker, whereas staining over Kupffer cells was enhanced.	Heparin	5-12	lipase G, endothelial type	Rattus norvegicus	37-43
4043133-4	1985	If AT III concentrate (40 U/kg per day) was activated with 200 U/kg per day heparin, excessive anticoagulation effect was only observed in one child.	Heparin	76-83	serpin family C member 1	Homo sapiens	3-9
15331606-1	2004	Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of growth factors that has a high affinity for heparin and heparan sulfate.	Heparin	125-132	heparin binding EGF like growth factor	Homo sapiens	0-38
15331606-1	2004	Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of growth factors that has a high affinity for heparin and heparan sulfate.	Heparin	125-132	heparin binding EGF like growth factor	Homo sapiens	40-46
15331606-1	2004	Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of growth factors that has a high affinity for heparin and heparan sulfate.	Heparin	125-132	epidermal growth factor	Homo sapiens	16-19
15331606-2	2004	While interactions with heparin are thought to modulate the biological activity of HB-EGF, the precise role of the heparin-binding domain has remained unclear.	Heparin	24-31	heparin binding EGF like growth factor	Homo sapiens	83-89
15331606-6	2004	The binding affinity of HB-EGF for DT was increased by addition of exogenous heparin and reached the level close to the affinity of DeltaHB, whereas that of DeltaHB was not affected.	Heparin	77-84	heparin binding EGF like growth factor	Homo sapiens	24-30
15570242-6	2004	Similar dose-dependent mobilization of TFPI and lipoprotein lipase (LPL), another glucosaminoglycan (GAG)-anchored protein of the endothelial membrane, was observed after both subcutaneous and intravenous administration of heparins.	Heparin	223-231	lipoprotein lipase	Homo sapiens	48-66
15570242-6	2004	Similar dose-dependent mobilization of TFPI and lipoprotein lipase (LPL), another glucosaminoglycan (GAG)-anchored protein of the endothelial membrane, was observed after both subcutaneous and intravenous administration of heparins.	Heparin	223-231	lipoprotein lipase	Homo sapiens	68-71
15570242-7	2004	However, UFH induced a more efficient release of both TFPI and LPL into plasma than did LMWH at equivalent anti-Xa levels, indicating molecular-weight dependence of the release reactions.	Heparin	9-12	lipoprotein lipase	Homo sapiens	63-66
15292258-0	2004	Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV.	Heparin	16-23	dipeptidyl peptidase 4	Homo sapiens	125-153
15292258-5	2004	We report here that heparin and HS specifically prevent the processing of SDF-1 by DPP IV expressed by Caco-2 cells.	Heparin	20-27	dipeptidyl peptidase 4	Homo sapiens	83-89
15230691-0	2004	Effect of intravenous heparin on serum levels of endostatin, VEGF and HGF: author"s reply.	Heparin	22-29	collagen type XVIII alpha 1 chain	Homo sapiens	49-59
15230692-0	2004	Effect of intravenous heparin on serum levels of endostatin, VEGF and HGF.	Heparin	22-29	collagen type XVIII alpha 1 chain	Homo sapiens	49-59
2864335-3	1985	Heparin inhibited the phosphorylation of phosvitin but not that of C-48.	Heparin	0-7	casein kinase 2 beta	Bos taurus	41-50
15281096-6	2004	PN-1 secreted by smooth muscle cells remained essentially associated to cell-surface glycosaminoglycans and was released from the cell surface by heparin.	Heparin	146-153	serpin family E member 2	Rattus norvegicus	0-4
15281096-7	2004	A lower amount of PN-1 was released by heparin from TRAP-stimulated versus unstimulated cells and correlated with a decreased capacity to inhibit thrombin.	Heparin	39-46	serpin family E member 2	Rattus norvegicus	18-22
15641292-7	2004	The great majority of the patients (99%) received oral antiplatelets during hospitalization and low molecular weight heparins were the preferred antithrombin therapy.	Heparin	117-125	serpin family C member 1	Homo sapiens	145-157
15664348-5	2005	This column is highly specific as described by the dissociation constant of the complex of immobilized heparin and AT III, which was 2.83 x 10(-5)mol/L.	Heparin	103-110	serpin family C member 1	Homo sapiens	115-121
15671997-7	2005	In villous trophoblast, heparin increased Bcl-2 and cytokeratin 18 protein expression.	Heparin	24-31	keratin 18	Homo sapiens	52-66
4010229-4	1985	Selective and partial inhibition of cell attachment to type I collagen, and, to a lesser extent, fibronectin, occurred upon preincubating these substrates with the sulfated glycosaminoglycans, heparin and heparan sulfate, at concentrations of 1 to 100 micrograms/ml; for 3T3 cells heparin was significantly more inhibitory (mean maximal inhibition of approximately 40%) than were two heparan sulfate fractions.	Heparin	193-200	fibronectin 1	Mus musculus	97-108
15714867-4	2005	Heparin therapy of acute coronary syndromes and the eventual ensuing interventional coronary procedure may employ NFH or LMWH.	Heparin	0-7	neurofilament heavy chain	Homo sapiens	114-117
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	46-53	serpin family C member 1	Homo sapiens	33-45
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	46-53	serpin family C member 1	Homo sapiens	33-45
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	46-53	serpin family C member 1	Homo sapiens	33-45
15178583-1	2004	A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin.	Heparin	37-44	serpin family C member 1	Homo sapiens	75-87
15178583-1	2004	A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin.	Heparin	37-44	serpin family C member 1	Homo sapiens	262-274
15178583-6	2004	These results suggest that structural differences in the autolysis loop of coagulation proteases play a key role in their differential reactivity with the native and heparin-activated conformations of antithrombin.	Heparin	166-173	serpin family C member 1	Homo sapiens	201-213
15311268-1	2004	Antithrombin, the principal physiological inhibitor of the blood coagulation proteinase thrombin, requires heparin as a cofactor.	Heparin	107-114	serpin family C member 1	Homo sapiens	0-12
15311268-5	2004	The 16-mer oligosaccharide is just long enough to form the predicted bridge between the high-affinity pentasaccharide-binding site on antithrombin and the highly basic exosite 2 on thrombin, validating the design strategy for this synthetic heparin.	Heparin	241-248	serpin family C member 1	Homo sapiens	134-146
15311269-0	2004	Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.	Heparin	39-46	serpin family C member 1	Homo sapiens	17-29
4049307-0	1985	Antithrombin III "Northwick Park": a variant antithrombin with normal affinity for heparin but reduced heparin cofactor activity.	Heparin	83-90	serpin family C member 1	Homo sapiens	0-16
15311269-0	2004	Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.	Heparin	103-110	serpin family C member 1	Homo sapiens	17-29
15311269-2	2004	Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans.	Heparin	127-134	serpin family C member 1	Homo sapiens	0-12
15311269-3	2004	The anticoagulant properties of therapeutic heparin are mediated by its interaction with antithrombin, although the structural basis for this interaction is unclear.	Heparin	44-51	serpin family C member 1	Homo sapiens	89-101
15311269-5	2004	The structure reveals a template mechanism with antithrombin and thrombin bound to the same heparin chain.	Heparin	92-99	serpin family C member 1	Homo sapiens	48-60
15339877-6	2004	These include fondaparinux and idraparinux, synthetic analogs of the pentasaccharide sequence that mediates the interaction of heparin and LMWH with antithrombin, and ximelagatran, an orally active inhibitor of thrombin.	Heparin	127-134	serpin family C member 1	Homo sapiens	149-161
15264226-7	2004	UH-treated rats showed smaller infarctions than rats treated with vehicle, as well as higher IL-10 plasma levels and HO-1 brain expression and lower endothelial VCAM-1 induction.	Heparin	0-2	interleukin 10	Rattus norvegicus	93-98
15607575-5	2005	Moreover, infusion of triglycerides with heparin - inducing a marked increase in free fatty acids - has been shown to induce a rapid increase in plasma PAI-1.	Heparin	41-48	serpin family E member 1	Homo sapiens	152-157
15668190-0	2005	Potentiation of platelet aggregation by heparin in human whole blood is attenuated by P2Y12 and P2Y1 antagonists but not aspirin.	Heparin	40-47	purinergic receptor P2Y1	Homo sapiens	86-90
15485805-8	2004	Heparin or heparinase treatment inhibited EL-mediated increases of monocyte adhesion in a dose-dependent manner.	Heparin	0-7	lipase, endothelial	Mus musculus	42-44
4049307-0	1985	Antithrombin III "Northwick Park": a variant antithrombin with normal affinity for heparin but reduced heparin cofactor activity.	Heparin	83-90	serpin family C member 1	Homo sapiens	45-57
15246840-0	2004	Heparin stabilizes FGF-2 and modulates striatal precursor cell behavior in response to EGF.	Heparin	0-7	epidermal growth factor	Homo sapiens	87-90
4049307-6	1985	Further studies confirmed that the abnormal AT III binds completely to heparin but has no heparin cofactor or progressive antithrombin activity.	Heparin	71-78	serpin family C member 1	Homo sapiens	44-50
2408688-3	1985	These derivatives exhibit a heparin-like antithrombic activity which requires the presence of antithrombin III; however they are less effective than heparin on a weight basis.	Heparin	28-35	serpin family C member 1	Homo sapiens	94-110
15328291-1	2004	The peptidoglycan recognition protein, PGRP, known as an intracellular component of neutrophils, has been isolated from camel (Camelus dromedarius) milk by acid precipitation followed by heparin-sepharose affinity chromatography of the supernatant.	Heparin	187-194	LOW QUALITY PROTEIN: peptidoglycan recognition protein 1	Camelus dromedarius	39-43
15315969-1	2004	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	117-124	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
15315969-1	2004	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	117-124	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
4037242-4	1985	These findings suggest that the administration of AT-III concentrates may significantly enhance the therapeutic efficacy of heparin, and that the use of AT-III concentrates with heparin is a safe and effective regimen for the treatment of childhood DIC.	Heparin	124-131	serpin family C member 1	Homo sapiens	50-56
15219850-5	2004	Inhibitors of matrix metalloproteinase and heparin bound-EGF prevented the CaR-mediated increases of pERK and PTHrP, consistent with a "triple-membrane-spanning signaling" requirement for transactivation of the EGFR by the CaR.	Heparin	43-50	eukaryotic translation initiation factor 2 alpha kinase 3	Homo sapiens	101-105
3838304-2	1985	Heparin cofactor II and antithrombin III are functionally similar in that both proteins have been shown to inhibit thrombin at accelerated rates in the presence of heparin.	Heparin	164-171	serpin family C member 1	Homo sapiens	24-40
23570202-1	2004	Unfractionated heparin (UFH) does not effectively inhibit clot-bound thrombin and increases platelet reactivity, expression of P-selectin and inflammatory responses.	Heparin	15-22	selectin P	Homo sapiens	127-137
23570202-1	2004	Unfractionated heparin (UFH) does not effectively inhibit clot-bound thrombin and increases platelet reactivity, expression of P-selectin and inflammatory responses.	Heparin	24-27	selectin P	Homo sapiens	127-137
3838304-8	1985	While the similarities in primary structure suggest that heparin cofactor II may be an additional member of the superfamily of proteins consisting of antithrombin III, alpha 1-antitrypsin, alpha 1-antichymotrypsin and ovalbumin, the differences in structure could account for differences in protease specificity and reactivity toward thrombin.	Heparin	57-64	serpin family C member 1	Homo sapiens	150-166
15133030-0	2004	Modified heparin inhibits P-selectin-mediated cell adhesion of human colon carcinoma cells to immobilized platelets under dynamic flow conditions.	Heparin	9-16	selectin P	Homo sapiens	26-36
3838304-9	1985	In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II.	Heparin	163-170	serpin family C member 1	Homo sapiens	88-104
15133030-1	2004	Accumulating evidence indicates that the formation of tumor cell platelet emboli complexes in the blood stream is a very important step during metastases and that the anti-metastasis effects of heparin are partially due to a blockade of P-selectin on platelets.	Heparin	194-201	selectin P	Homo sapiens	237-247
15133030-2	2004	In this study, heparin and chemically modified heparins were tested as inhibitors of three human colon carcinoma cell lines (COLO320, LS174T, and CW-2) binding to P-selectin, adhering to CHO cells expressing a transfected human P-selectin cDNA, and adhering to surface-anchored platelets expressing P-selectin under static and flow conditions.	Heparin	15-22	selectin P	Homo sapiens	163-173
3838304-9	1985	In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II.	Heparin	245-252	serpin family C member 1	Homo sapiens	88-104
15133030-2	2004	In this study, heparin and chemically modified heparins were tested as inhibitors of three human colon carcinoma cell lines (COLO320, LS174T, and CW-2) binding to P-selectin, adhering to CHO cells expressing a transfected human P-selectin cDNA, and adhering to surface-anchored platelets expressing P-selectin under static and flow conditions.	Heparin	47-55	selectin P	Homo sapiens	163-173
15133030-6	2004	Our findings suggested that the 6-O-sulfate group of glucosamine units in heparin is critical for the inhibition of P-selectin-mediated tumor cell adhesion.	Heparin	74-81	selectin P	Homo sapiens	116-126
15522821-7	2004	Monomeric LPL was bound to the cells mostly in a heparin-resistant fashion.	Heparin	49-56	lipoprotein lipase	Homo sapiens	10-13
3838304-9	1985	In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II.	Heparin	245-252	serpin family C member 1	Homo sapiens	88-104
15133030-8	2004	Some chemically modified heparins with low anticoagulant activities, such as 2/3ODS-heparin, may have potential value as therapeutic agents that block P-selectin-mediated cell adhesion and prevent tumor metastasis.	Heparin	25-33	selectin P	Homo sapiens	151-161
15133030-8	2004	Some chemically modified heparins with low anticoagulant activities, such as 2/3ODS-heparin, may have potential value as therapeutic agents that block P-selectin-mediated cell adhesion and prevent tumor metastasis.	Heparin	25-32	selectin P	Homo sapiens	151-161
15170430-3	2004	Because of a severe antithombin deficiency, regular infusions of antithrombin concentrates were necessary until delivery to ensure effective anticoagulation by heparin.	Heparin	160-167	serpin family C member 1	Homo sapiens	65-77
15331606-8	2004	These results indicate that the heparin-binding domain suppresses the activity of the EGF-like domain of HB-EGF and that association of heparin with HB-EGF via this domain removes the suppressive effect.	Heparin	32-39	epidermal growth factor	Homo sapiens	86-89
15331606-8	2004	These results indicate that the heparin-binding domain suppresses the activity of the EGF-like domain of HB-EGF and that association of heparin with HB-EGF via this domain removes the suppressive effect.	Heparin	32-39	heparin binding EGF like growth factor	Homo sapiens	105-111
15331606-8	2004	These results indicate that the heparin-binding domain suppresses the activity of the EGF-like domain of HB-EGF and that association of heparin with HB-EGF via this domain removes the suppressive effect.	Heparin	136-143	heparin binding EGF like growth factor	Homo sapiens	105-111
15331606-8	2004	These results indicate that the heparin-binding domain suppresses the activity of the EGF-like domain of HB-EGF and that association of heparin with HB-EGF via this domain removes the suppressive effect.	Heparin	136-143	heparin binding EGF like growth factor	Homo sapiens	149-155
15522270-10	2004	Incubation of myocytes with LPA, a phospholipase D (PLD) mediated breakdown metabolite of PLPC, significantly enhanced basal and heparin-releasable myocyte LPL activity, an effect that was duplicated by co-incubation of control myocytes with exogenous PLD and PLPC.	Heparin	129-136	lipoprotein lipase	Homo sapiens	156-159
15543318-8	2004	The conformational change of antithrombin induced both by the pentasaccharides and longer heparins contributes substantially, approximately 150-500-fold, to accelerating the inactivation of factors Xa, IXa and VIIa and moderately, approximately 50-fold, to that of factor XIIa and tissue plasminogen activator inhibition.	Heparin	90-98	serpin family C member 1	Homo sapiens	29-41
15543318-9	2004	The bridging effect due to binding of antithrombin and proteinase to the same, long heparin chain is dominating, approximately 1000-3000-fold, for thrombin inhibition and is appreciably smaller, although up to approximately 250-350-fold, for the inactivation of factors IXa and XIa.	Heparin	84-91	serpin family C member 1	Homo sapiens	38-50
3838304-10	1985	This observation provides an initial indication that while the reported kinetic mechanisms of action of heparin in accelerating the heparin cofactor II/thrombin and antithrombin III/thrombin reactions are similar, the mechanisms and effects of heparin binding to the two inhibitors may be different.	Heparin	104-111	serpin family C member 1	Homo sapiens	165-181
15353914-4	2004	Hemodilution associated with ANH may reduce the effectiveness of heparin anticoagulation due to dilution of antithrombin.	Heparin	65-72	serpin family C member 1	Homo sapiens	108-120
2578296-3	1985	Heparin fractions of different molecular weight and affinity for antithrombin III showed similar kinetic parameters in catalysis of the thrombin-antithrombin III reaction when these parameters were expressed on the basis of antithrombin III-binding heparin.	Heparin	249-256	serpin family C member 1	Homo sapiens	65-81
2578296-4	1985	The latter was determined by stoichiometric titration of the antithrombin III fluorescence change by the heparin preparation.	Heparin	105-112	serpin family C member 1	Homo sapiens	61-77
15149315-3	2004	The aims of this study of murine autosomal-recessive polycystic kidney disease (ARPKD) were (1) to characterize amphiregulin and heparin-binding EGF expression in cystic versus normal kidneys and cells; and (2) to identify the functional effects of abnormal EGF-related growth factor expression.	Heparin	129-136	epidermal growth factor	Mus musculus	145-148
2578296-6	1985	This indicated that functional heparin molecules had similar kinetic properties regardless of size or antithrombin III-binding affinity and is possible because the Km for antithrombin III is determined by diffusion rather than by binding affinity.	Heparin	31-38	serpin family C member 1	Homo sapiens	102-118
15166006-7	2004	Pretreatment of cells with heparin (1 microM), a nonselective G protein-coupled receptor kinase (GRK) inhibitor, prevented the loss of effects on NHE activity after 25 min exposure to SKF-38393.	Heparin	27-34	G protein-coupled receptor kinase 4	Rattus norvegicus	97-100
15149315-4	2004	METHODS: Amphiregulin and heparin-binding-EGF expression were examined by immunohistology and Western blot of kidneys and conditionally-immortalized collecting tubule cells obtained from cystic bpk mice (a murine model of ARPKD) and normal littermates.	Heparin	26-33	epidermal growth factor	Mus musculus	42-45
2578296-6	1985	This indicated that functional heparin molecules had similar kinetic properties regardless of size or antithrombin III-binding affinity and is possible because the Km for antithrombin III is determined by diffusion rather than by binding affinity.	Heparin	31-38	serpin family C member 1	Homo sapiens	171-187
15149315-5	2004	EGF, TGF-alpha, amphiregulin, and heparin-binding EGF in vitro effects on cystic and control collecting tubule cells were assessed by cell proliferation, cyst fluid mitogenicity, and EGFR activation.	Heparin	34-41	epidermal growth factor	Mus musculus	50-53
15149315-6	2004	RESULTS: By immunohistology, amphiregulin and heparin-binding EGF localized to apical and basolateral surfaces of proximal tubule cysts &gt; normal proximal tubules.	Heparin	46-53	epidermal growth factor	Mus musculus	62-65
3965464-0	1985	Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding.	Heparin	109-116	serpin family C member 1	Homo sapiens	37-53
15149315-7	2004	In cystic collecting tubules, heparin-binding EGF (but not amphiregulin) localized to both apical and basolateral surfaces; whereas in normal collecting tubules, amphiregulin and heparin-binding EGF localized to the basolateral surface only.	Heparin	30-37	epidermal growth factor	Mus musculus	46-49
15149315-7	2004	In cystic collecting tubules, heparin-binding EGF (but not amphiregulin) localized to both apical and basolateral surfaces; whereas in normal collecting tubules, amphiregulin and heparin-binding EGF localized to the basolateral surface only.	Heparin	179-186	epidermal growth factor	Mus musculus	46-49
15149315-7	2004	In cystic collecting tubules, heparin-binding EGF (but not amphiregulin) localized to both apical and basolateral surfaces; whereas in normal collecting tubules, amphiregulin and heparin-binding EGF localized to the basolateral surface only.	Heparin	179-186	epidermal growth factor	Mus musculus	195-198
15149315-8	2004	Increased amphiregulin and heparin-binding EGF expression by Western blot was seen in cystic vs. normal kidneys and increased heparin-binding EGF (but not amphiregulin) expression was present in cystic collecting tubule cell lines vs. controls.	Heparin	27-34	epidermal growth factor	Mus musculus	43-46
15505366-4	2004	Likewise, the results of electron microscopy showed that Abeta 25-35 increases the tau peptide polymerization observed in the presence of polyanions like heparin.	Heparin	154-161	microtubule associated protein tau	Homo sapiens	83-86
15149315-10	2004	Immunoprecipitation of EGF and TGF-alpha reduced cyst fluid mitogenicity by almost 80%, whereas heparin-binding EGF and amphiregulin immunoprecipitations had minimal effects.	Heparin	96-103	epidermal growth factor	Mus musculus	112-115
15149315-11	2004	Differential receptor activation was also seen: Heparin-binding EGF markedly activated EGFR (&gt;EGF = TGF-alpha &gt; amphiregulin), with a greater effect seen in cystic vs. control collecting tubule cells.	Heparin	48-55	epidermal growth factor	Mus musculus	64-67
15149315-11	2004	Differential receptor activation was also seen: Heparin-binding EGF markedly activated EGFR (&gt;EGF = TGF-alpha &gt; amphiregulin), with a greater effect seen in cystic vs. control collecting tubule cells.	Heparin	48-55	epidermal growth factor receptor	Mus musculus	87-91
15149315-11	2004	Differential receptor activation was also seen: Heparin-binding EGF markedly activated EGFR (&gt;EGF = TGF-alpha &gt; amphiregulin), with a greater effect seen in cystic vs. control collecting tubule cells.	Heparin	48-55	epidermal growth factor	Mus musculus	87-90
15149315-11	2004	Differential receptor activation was also seen: Heparin-binding EGF markedly activated EGFR (&gt;EGF = TGF-alpha &gt; amphiregulin), with a greater effect seen in cystic vs. control collecting tubule cells.	Heparin	48-55	transforming growth factor alpha	Mus musculus	103-112
15149315-13	2004	In particular, newly identified abnormalities in heparin-binding EGF expression in cystic kidneys and cells may have important implications for disease pathogenesis.	Heparin	49-56	epidermal growth factor	Mus musculus	65-68
15516868-4	2004	The APTT was prolonged on the PU-C-H and PU-P-H, suggesting the binding of immobilized heparin to the antithrombin III.	Heparin	87-94	serpin family C member 1	Homo sapiens	102-118
15383472-2	2004	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors.	Heparin	0-3	serpin family C member 1	Homo sapiens	66-78
15588409-3	2004	Our aim is to achieve this goal by covalently incorporating heparin into collagen matrices and by physically immobilizing angiogenic vascular endothelial growth factor (VEGF) to the heparin.	Heparin	182-189	vascular endothelial growth factor A	Rattus norvegicus	133-167
3965464-1	1985	Two distinct forms of antithrombin III were isolated by chromatography of normal human plasma on heparin-Sepharose.	Heparin	97-104	serpin family C member 1	Homo sapiens	22-38
15588409-3	2004	Our aim is to achieve this goal by covalently incorporating heparin into collagen matrices and by physically immobilizing angiogenic vascular endothelial growth factor (VEGF) to the heparin.	Heparin	182-189	vascular endothelial growth factor A	Rattus norvegicus	169-173
14996843-10	2004	6) Sulfated galactan and heparin bind to different sites on antithrombin.	Heparin	25-32	serpin family C member 1	Homo sapiens	60-72
14996843-11	2004	7) Sulfated galactans are less effective than heparin at promoting antithrombin conformational activation.	Heparin	46-53	serpin family C member 1	Homo sapiens	67-79
15588409-13	2004	It is apparent that the physical binding of VEGF to heparin allows for a release that is beneficial to angiogenesis.	Heparin	52-59	vascular endothelial growth factor A	Rattus norvegicus	44-48
3975871-3	1985	Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site.	Heparin	0-7	serpin family C member 1	Homo sapiens	121-127
15265919-0	2004	Histidines are critical for heparin-dependent activation of mast cell tryptase.	Heparin	28-35	tryptase alpha/beta 1	Mus musculus	70-78
15196003-5	2004	Low molecular weight heparin accelerates the inhibition of trypsin by antithrombin by a factor of 16 [d(t)=0.36 s].	Heparin	21-28	serpin family C member 1	Homo sapiens	70-82
3975871-3	1985	Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site.	Heparin	37-44	serpin family C member 1	Homo sapiens	121-127
15265919-3	2004	Previous studies have shown that tryptase binds tightly to heparin, and that heparin is required in the assembly of the tryptase tetramer as well as for stabilization of the active tetramer.	Heparin	59-66	tryptase alpha/beta 1	Mus musculus	33-41
3975871-3	1985	Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site.	Heparin	148-155	serpin family C member 1	Homo sapiens	121-127
2409857-8	1985	Follicular PP5, like antithrombin III, interacted reversibly with heparin and thrombin affinity matrices, suggesting a potential biological role as a follicular anticoagulant, whereas PAPP-A, a specific and potent inhibitor of leukocyte elastase, contributes to the maintenance of proteolytic homeostasis and the protection of spermatozoa and embryo against proteolytic attack originating from the maternal leukocytes.	Heparin	66-73	serpin family C member 1	Homo sapiens	21-37
15282457-6	2004	Heparin bound nonspecifically to plasma proteins was measured after displacement with a chemically altered heparin with low affinity to antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	136-148
15282457-6	2004	Heparin bound nonspecifically to plasma proteins was measured after displacement with a chemically altered heparin with low affinity to antithrombin.	Heparin	107-114	serpin family C member 1	Homo sapiens	136-148
15116263-0	2004	Binding of heparin to plasma proteins and endothelial surfaces is inhibited by covalent linkage to antithrombin.	Heparin	11-18	serpin family C member 1	Homo sapiens	99-111
15116263-3	2004	Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH.	Heparin	36-43	serpin family C member 1	Homo sapiens	20-32
15116263-3	2004	Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH.	Heparin	114-117	serpin family C member 1	Homo sapiens	20-32
15116263-3	2004	Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH.	Heparin	173-176	serpin family C member 1	Homo sapiens	20-32
15116263-8	2004	Although ATH is polydisperse, the covalently-linked antithrombin may shield a portion of the heparin chain from association with plasma or endothelial cell surface proteins.	Heparin	93-100	serpin family C member 1	Homo sapiens	52-64
3967057-8	1985	This lipase can be stimulated by heparin (100 micrograms/ml) by about 10-25% in newborn and adult animals.	Heparin	33-40	lipase G, endothelial type	Rattus norvegicus	5-11
15219196-0	2004	Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin.	Heparin	129-136	serpin family C member 1	Homo sapiens	116-128
3965218-5	1985	Oleate decreased the values, indicating that intravenous heparin, which releases endothelial lipase, causing in vitro lipolysis, should be avoided if indwelling catheters are used for sampling, e.g., during provocation tests for gastrin release.	Heparin	57-64	gastrin	Homo sapiens	229-236
15007070-4	2004	By use of Me-Indoxam and the cell-impermeable, secreted phospholipase A(2) trapping agent heparin, it is shown that hGIIA liberates free arachidonate prior to secretion from the cell.	Heparin	90-97	glucosidase II alpha subunit	Homo sapiens	116-121
14707039-8	2004	The functionality of immobilized heparin was confirmed by specific uptake of antithrombin, 13.5+/-4.7 pmol/cm2 and 1.95+/-0.21 pmol/cm2 for mildly and heavily periodated heparin, respectively.	Heparin	33-40	serpin family C member 1	Homo sapiens	77-89
14707039-8	2004	The functionality of immobilized heparin was confirmed by specific uptake of antithrombin, 13.5+/-4.7 pmol/cm2 and 1.95+/-0.21 pmol/cm2 for mildly and heavily periodated heparin, respectively.	Heparin	170-177	serpin family C member 1	Homo sapiens	77-89
14623882-2	2004	In the structure of native antithrombin, the reactive center loop is restrained due to the insertion of its hinge region into the main beta-sheet A, whereas in the heparin-activated state the reactive center loop is freed from beta-sheet A.	Heparin	164-171	serpin family C member 1	Homo sapiens	27-39
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	serpin family C member 1	Homo sapiens	214-230
14624766-4	2003	In the presence of IGF-II, IGFBP-2 bound with high affinity to heparin-Sepharose, but not to type I collagen, fibronectin, or laminin.	Heparin	63-70	insulin like growth factor 2	Homo sapiens	19-25
14624766-5	2003	Furthermore, heparin and heparan sulfate, but not chondroitin sulfate, inhibited IGFBP-2/IGF-II binding to ECM.	Heparin	13-20	insulin like growth factor 2	Homo sapiens	89-95
15253542-2	2004	Platinum coils were prepared by successive deposition of cationic polyethyleneimine and anionic heparin, and VEGF was immobilized through affinity interaction with heparin.	Heparin	164-171	vascular endothelial growth factor A	Rattus norvegicus	109-113
14963717-8	2004	In contrast, the mitogenic effects of the platelet-derived and the heparin-binding epidermal growth factors were dependent on p44/p42 MAPK activation and independent of activation of p38 MAPK.	Heparin	67-74	cyclin dependent kinase 20	Homo sapiens	130-133
4007636-2	1985	Significant increases of AT-III (p less than 0.025) measured as heparin cofactor activity were noted in 1 female and 1 male patient.	Heparin	64-71	serpin family C member 1	Homo sapiens	25-31
14967813-2	2004	The time course of LPL activity in the postprandial state following a single meal has never been studied, because its determination required heparin injection.	Heparin	141-148	lipoprotein lipase	Homo sapiens	19-22
14580209-4	2003	The rec-alpha1G protein promoted both cell attachment and heparin binding (K(D) = 19 nM).	Heparin	58-65	calcium channel, voltage-dependent, T type, alpha 1G subunit	Mus musculus	8-15
14580209-5	2003	Cell attachment to the rec-alpha1G protein was inhibited 60% by heparin and 30% by EDTA.	Heparin	64-71	calcium channel, voltage-dependent, T type, alpha 1G subunit	Mus musculus	27-34
14580209-6	2003	The heparin binding sites were identified by competing heparin binding to the rec-alpha1G protein with 110 synthetic peptides in solution.	Heparin	4-11	calcium channel, voltage-dependent, T type, alpha 1G subunit	Mus musculus	82-89
2579436-1	1985	There is now considerable evidence that the antithrombotic and the hemorrhagic effects of heparin can be dissociated by using low molecular weight heparins and by using heparin with low affinity to AT III.	Heparin	90-97	serpin family C member 1	Homo sapiens	198-204
14580209-6	2003	The heparin binding sites were identified by competing heparin binding to the rec-alpha1G protein with 110 synthetic peptides in solution.	Heparin	55-62	calcium channel, voltage-dependent, T type, alpha 1G subunit	Mus musculus	82-89
14580209-7	2003	Only two peptides, AG73 (IC(50) = 147 microM) and AG75 (IC(50) = 206 microM), inhibited heparin binding to rec-alpha1G.	Heparin	88-95	calcium channel, voltage-dependent, T type, alpha 1G subunit	Mus musculus	111-118
14993245-7	2004	Inhibiting calcium signaling using 1,2-bis(2-aminophenoxy)-ethane-N,N,N",N"-tetraacetic acid and heparin decreased the expression of E-selectin.	Heparin	97-104	selectin E	Homo sapiens	133-143
3975640-1	1985	Affinity for antithrombin III and anti-Xa activity of selectively carboxyl esterified heparin.	Heparin	86-93	serpin family C member 1	Homo sapiens	13-29
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	40-47	serpin family C member 1	Homo sapiens	79-85
15162900-2	2004	Unfractionated heparin and low-molecular-weight heparins may not provide effective anticoagulation since they require antithrombin for activity.	Heparin	48-56	serpin family C member 1	Homo sapiens	118-130
14585904-9	2003	Patients homozygous for both the ACE D and PAI-1 4G alleles may benefit from the application of low molecular weight heparin as early as possible in the pregnancy in order to prevent uteroplacental microthromboses.	Heparin	117-124	serpin family E member 1	Homo sapiens	43-48
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	40-47	serpin family C member 1	Homo sapiens	149-155
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family C member 1	Homo sapiens	79-85
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family C member 1	Homo sapiens	149-155
12829607-8	2003	In contrast, heparin but not LY311727 abrogated the binding of hGIIA to cellular HSPGs.	Heparin	13-20	glucosidase II alpha subunit	Homo sapiens	63-68
15073698-0	2004	Decreased concentration of antithrombin after preoperative therapeutic heparin does not cause heparin resistance during cardiopulmonary bypass.	Heparin	71-78	serpin family C member 1	Homo sapiens	27-39
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family C member 1	Homo sapiens	79-85
15073698-1	2004	OBJECTIVE: To determine if preoperative heparin therapy causes an increase in the incidence of intraoperative heparin resistance by reducing the concentration of antithrombin in plasma.	Heparin	40-47	serpin family C member 1	Homo sapiens	162-174
12837131-0	2003	Fibrillin-1 and -2 contain heparin-binding sites important for matrix deposition and that support cell attachment.	Heparin	27-34	fibrillin 1	Homo sapiens	0-18
15073698-1	2004	OBJECTIVE: To determine if preoperative heparin therapy causes an increase in the incidence of intraoperative heparin resistance by reducing the concentration of antithrombin in plasma.	Heparin	110-117	serpin family C member 1	Homo sapiens	162-174
12837131-3	2003	Additionally, we have narrowed the location of heparin-binding activity previously identified in fibrillin-1 to the last 17 residues of the mature proteolytically processed protein.	Heparin	47-54	fibrillin 1	Homo sapiens	97-108
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family C member 1	Homo sapiens	149-155
15073698-9	2004	Comparison of heparin-resistant and heparin-responsive POHI patients showed that the concentration of antithrombin did not differ before bypass (82.4% and 79.8%, respectively, p = 0.53) or during bypass (51.8% and 51.4%, respectively, p = 0.91).	Heparin	36-43	serpin family C member 1	Homo sapiens	102-114
15073698-10	2004	In fact, antithrombin concentrations were slightly higher in the heparin-resistant POHI patients (not significant).	Heparin	65-72	serpin family C member 1	Homo sapiens	9-21
15073698-12	2004	CONCLUSIONS: Preoperative heparin causes an increased incidence of heparin resistance and reduced antithrombin concentrations.	Heparin	26-33	serpin family C member 1	Homo sapiens	98-110
15064342-6	2004	RESULTS: The addition of soluble CD39 to heparinized blood inhibited platelet deposition to an extent greater than that of heparin alone (P =.04).	Heparin	41-48	ectonucleoside triphosphate diphosphohydrolase 1	Homo sapiens	33-37
14519117-5	2003	M27 blocked the ability of antithrombin to inhibit thrombin as well as antithrombin cleavage, both in the presence and absence of heparin.	Heparin	130-137	serpin family C member 1	Homo sapiens	27-39
14502551-8	2003	This may provide a novel cost-effective, bioaffinity-based alternative to antithrombin for concurrent enrichment and recovery of anticoagulant and nonanticoagulant heparin from the same heparin mixture.	Heparin	164-171	serpin family C member 1	Homo sapiens	74-86
6593229-2	1984	The high activity of CKII in transformed cells and in established cell lines was reduced to about the same basic level after treatment with heparin, a highly specific inhibitor of CKII activity.	Heparin	140-147	casein kinase 2 alpha 1	Homo sapiens	21-25
14578460-2	2003	We designed a novel vascular-targeting fusion construct designated as GrB/vascular endothelial growth factor (VEGF)121, which is composed of a non-heparin-binding isoform of VEGF and the proapoptotic pathway enzyme GrB fused via a short, flexible tether (G4S).	Heparin	147-154	granzyme B	Homo sapiens	70-73
12927798-3	2003	We show that HS and heparin chains specifically bind to BMP-7.	Heparin	20-27	bone morphogenetic protein 7	Rattus norvegicus	56-61
15045703-3	2004	We measured the LPL mass before and 15 minutes after the injection of heparin in 164 subjects with hyperlipidemia.	Heparin	70-77	lipoprotein lipase	Homo sapiens	16-19
6593229-2	1984	The high activity of CKII in transformed cells and in established cell lines was reduced to about the same basic level after treatment with heparin, a highly specific inhibitor of CKII activity.	Heparin	140-147	casein kinase 2 alpha 1	Homo sapiens	180-184
12927798-6	2003	Addition of exogenous heparin to ROS 17/2.8 cells prevents BMP-7-mediated Smad phosphorylation rather than enhances the BMP-7 signal, suggesting that HS should be anchored on the plasma membrane for BMP signaling.	Heparin	22-29	bone morphogenetic protein 7	Rattus norvegicus	59-64
14711523-0	2004	Separation of latent, prelatent, and native forms of human antithrombin by heparin affinity high-performance liquid chromatography.	Heparin	75-82	serpin family C member 1	Homo sapiens	59-71
12927798-7	2003	Moreover, BMP-7 binding to ROS 17/2.8 cells is inhibited by chlorate treatment and exogenous application of heparin.	Heparin	108-115	bone morphogenetic protein 7	Rattus norvegicus	10-15
6509363-0	1984	Effects of heparin fractions of different affinities to antithrombin III and thrombin on the inactivation of thrombin and factor Xa by antithrombin III.	Heparin	11-18	serpin family C member 1	Homo sapiens	56-72
12941037-9	2003	Moreover, both heparin and SanOrg123781A significantly inhibited fibrinopeptide A generated by the action of clot-bound thrombin on fibrinogen but also by free thrombin generated from prothrombin by clot-bound FXa with IC50 values of 4 +/- 0.6 and 1 +/- 0.1 micro g mL-1, respectively.	Heparin	15-22	L1 cell adhesion molecule	Mus musculus	266-270
6509363-0	1984	Effects of heparin fractions of different affinities to antithrombin III and thrombin on the inactivation of thrombin and factor Xa by antithrombin III.	Heparin	11-18	serpin family C member 1	Homo sapiens	135-151
6509363-2	1984	There was a good correlation between heparin affinity for antithrombin III and its ability to enhance the inactivation of thrombin and factor Xa.	Heparin	37-44	serpin family C member 1	Homo sapiens	58-74
15085469-1	2004	The 87-year history of heparin began in 1916 when a 26-year-old medical student named Jay McLean startled his mentor William Howell, Professor of Physiology at Johns Hopkins University, by proclaiming that he had discovered "antithrombin."	Heparin	23-30	serpin family C member 1	Homo sapiens	225-237
6509363-3	1984	In addition, there was a good correlation between affinity of heparin for thrombin and its catalytic activity on the inactivation of thrombin by antithrombin III.	Heparin	62-69	serpin family C member 1	Homo sapiens	145-161
15085469-12	2004	The first synthetic product was called the pentasaccharide, named for the five critical sugar units in heparin that bind to antithrombin (1983).	Heparin	103-110	serpin family C member 1	Homo sapiens	124-136
12873131-0	2003	Crystal structure of antithrombin in a heparin-bound intermediate state.	Heparin	39-46	serpin family C member 1	Homo sapiens	21-33
6509363-7	1984	A heparin fraction with very low affinity to thrombin and high affinity to antithrombin III was prepared by repeated fractionation of a low molecular weight heparin on the two affinity columns.	Heparin	2-9	serpin family C member 1	Homo sapiens	75-91
12873131-2	2003	The binding of heparin induces a global conformational change in antithrombin which results in the freeing of its reactive center loop for interaction with target proteases and a 1000-fold increase in heparin affinity.	Heparin	15-22	serpin family C member 1	Homo sapiens	65-77
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	98-105	serpin family C member 1	Homo sapiens	158-174
12873131-2	2003	The binding of heparin induces a global conformational change in antithrombin which results in the freeing of its reactive center loop for interaction with target proteases and a 1000-fold increase in heparin affinity.	Heparin	201-208	serpin family C member 1	Homo sapiens	65-77
12873131-3	2003	The allosteric mechanism by which the properties of antithrombin are altered by its interactions with the specific pentasaccharide sequence of heparin is of great interest to the medical and protein biochemistry communities.	Heparin	143-150	serpin family C member 1	Homo sapiens	52-64
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	207-214	serpin family C member 1	Homo sapiens	158-174
12873131-4	2003	Heparin binding has previously been characterized as a two-step, three-state mechanism where, after an initial weak interaction, antithrombin undergoes a conformational change to its high-affinity state.	Heparin	0-7	serpin family C member 1	Homo sapiens	129-141
15125386-10	2004	Low molecular weight heparins by their action on lipoprotein lipase serve as an additional factor that suppresses development of atherosclerotic plaque in dialysis patients.	Heparin	21-29	lipoprotein lipase	Homo sapiens	49-67
6509363-9	1984	The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III.	Heparin	207-214	serpin family C member 1	Homo sapiens	238-254
6520110-0	1984	A method to determine the affinity of heparin to thrombin and antithrombin III on equilibrium gel permeation chromatography.	Heparin	38-45	serpin family C member 1	Homo sapiens	62-78
14699222-6	2004	Low-dose (0.03 mg/kg/hour) rTPA with heparin is an acceptable and safe alternative to high-dose rTPA infusion for intracardiac thrombi in children.	Heparin	37-44	plasminogen activator, tissue type	Rattus norvegicus	27-31
15507263-3	2004	Although the exact physiological function of beta2GPI has not been fully elucidated, several interactions have been described with other proteins and with negatively charged surfaces, such as anionic phospholipids, dextran and heparin.	Heparin	227-234	apolipoprotein H	Homo sapiens	45-53
12721300-6	2003	By contrast, Arg143 and Lys147 mutants reacted normally with antithrombin (AT) in both the absence and presence of the cofactor, heparin.	Heparin	129-136	serpin family C member 1	Homo sapiens	61-73
12773140-0	2003	Intralipid/heparin infusion suppresses serum leptin in humans.	Heparin	11-18	leptin	Homo sapiens	45-51
12801846-8	2003	With long periods of incubation (24-48h), both unfractionated heparin and enoxaparin significantly increased TFPI release (control vs. unfractionated heparin, p&lt;0.05-0.001; control vs. enoxaparin, p&lt;0.01-0.001) and also reduced the release of vWF in the culture medium, though no variations in endothelial cell procoagulant activity or TF content were observed.	Heparin	62-69	coagulation factor III, tissue factor	Homo sapiens	109-111
6520110-1	1984	Equilibrium gel permeation chromatography was employed to determine the ability of heparin to form complexes with thrombin and antithrombin III.	Heparin	83-90	serpin family C member 1	Homo sapiens	127-143
6487338-2	1984	The binding affinity toward antithrombin III decreases in the following order: Heparin greater than heparin methyl ester greater than heparinylglycine greater than heparinylglycine methyl ester.	Heparin	79-86	serpin family C member 1	Homo sapiens	28-44
12743035-4	2003	Moreover, AR gene silencing by siRNA or inhibition of AR biological activity by neutralizing antibodies and heparin prevents GPCR-induced EGFR tyrosine phosphorylation, downstream mitogenic signalling events, cell proliferation, migration and activation of the survival mediator Akt/PKB.	Heparin	108-115	C-X-C motif chemokine receptor 6	Homo sapiens	125-129
14532267-1	2003	We have previously shown that exosites in antithrombin outside the P6-P3" reactive loop region become available upon heparin activation to promote rapid inhibition of the target proteases, factor Xa and factor IXa.	Heparin	117-124	serpin family C member 1	Homo sapiens	42-54
14532267-3	2003	All chimeras bound heparin with a high affinity similar to wild-type, underwent heparin-induced fluorescence changes indicative of normal conformational activation, and were able to form SDS-stable complexes with thrombin, factor Xa, and factor IXa and inhibit these proteases with stoichiometries minimally altered from those of wild-type antithrombin.	Heparin	19-26	serpin family C member 1	Homo sapiens	340-352
12571234-9	2003	Mutations of charged and uncharged residues in the loop regions of residues 20-24 and 46-47, which caused reduced heparin binding, also resulted in reduced CXCR3 binding and signaling.	Heparin	114-121	chemokine (C-X-C motif) receptor 3	Mus musculus	156-161
6496919-0	1984	[Antithrombin III substitution for optimization of the heparin effect during extracorporeal circulation in heart surgery].	Heparin	55-62	serpin family C member 1	Homo sapiens	1-17
12907439-0	2003	Heparin-induced substrate behavior of antithrombin Cambridge II.	Heparin	0-7	serpin family C member 1	Homo sapiens	38-50
6235872-2	1984	In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III.	Heparin	22-29	serpin family C member 1	Homo sapiens	66-82
12907439-3	2003	Antithrombin Cambridge II was found to be normal in its affinity for heparin, its ability to form sodium dodecyl sulfate-stable complexes with factor Xa and thrombin, and its uncatalyzed stoichiometries and rates of inhibition.	Heparin	69-76	serpin family C member 1	Homo sapiens	0-12
14652650-13	2003	From our results, we can conclude that endotoxin-induced adhesion of leukocytes to endothelium can be reversed by ligation of syndecan-4 with antithrombin"s heparin-binding site and interferences with stress response signaling events in endothelium.	Heparin	157-164	serpin family C member 1	Homo sapiens	142-154
12701115-4	2003	Moreover, eosinophil peroxidase by itself functioned as a powerful procoagulant and also inhibited the anticoagulant actions of heparin in a chromogenic assay for antithrombin III/factor Xa activity.	Heparin	128-135	serpin family C member 1	Homo sapiens	163-179
6235872-2	1984	In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III.	Heparin	22-29	serpin family C member 1	Homo sapiens	189-205
6235872-2	1984	In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III.	Heparin	34-41	serpin family C member 1	Homo sapiens	66-82
12556525-5	2003	The binding of L-selectin to isolated collagen XVIII was specifically inhibited by an anti-L-selectin monoclonal antibody, EDTA, treatment of the collagen XVIII with heparitinase or heparin but not by chemically desulfated heparin.	Heparin	182-189	collagen type XVIII alpha 1 chain	Homo sapiens	38-52
14568190-0	2003	Tamoxifen might influence the affinity of LPL for heparin-sepharose.	Heparin	50-57	lipoprotein lipase	Homo sapiens	42-45
14568190-3	2003	METHODS: Lipoprotein lipase in post-heparin plasma usually exists in both monomeric and dimeric forms, which may be separated on a heparin-Sepharose column with different salt concentrations.	Heparin	36-43	lipoprotein lipase	Homo sapiens	9-27
6235872-2	1984	In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III.	Heparin	34-41	serpin family C member 1	Homo sapiens	189-205
14568190-3	2003	METHODS: Lipoprotein lipase in post-heparin plasma usually exists in both monomeric and dimeric forms, which may be separated on a heparin-Sepharose column with different salt concentrations.	Heparin	131-138	lipoprotein lipase	Homo sapiens	9-27
14568190-4	2003	Lipoprotein lipase in post-heparin plasma from postmenopausal patients with hypertriglyceridemia treated with or without tamoxifen was incubated with or without 4-hydroxy-tamoxifen (4-OHT), the monomers and dimers were separated on a heparin-Sepharose column and their masses were measured.	Heparin	27-34	lipoprotein lipase	Homo sapiens	0-18
6495266-1	1984	Antithrombin III was purified from normal plasma by DEAE-Sephadex chromatography and heparin affinity chromatography; the protein was subsequently radiolabelled with 125I.	Heparin	85-92	serpin family C member 1	Homo sapiens	0-16
14568190-4	2003	Lipoprotein lipase in post-heparin plasma from postmenopausal patients with hypertriglyceridemia treated with or without tamoxifen was incubated with or without 4-hydroxy-tamoxifen (4-OHT), the monomers and dimers were separated on a heparin-Sepharose column and their masses were measured.	Heparin	234-241	lipoprotein lipase	Homo sapiens	0-18
14568190-6	2003	Monomeric LPL of tamoxifen-treated patients passed more slowly through the heparin-Sepharose column compared with that of control subjects.	Heparin	75-82	lipoprotein lipase	Homo sapiens	10-13
14568190-8	2003	In addition, monomeric LPL incubated with 4-OHT passed more slowly through the heparin-Sepharose column compared with that incubated without 4-OHT.	Heparin	79-86	lipoprotein lipase	Homo sapiens	23-26
14568192-1	2003	BACKGROUND: Lipoprotein lipase (LPL) mass is present in pre-heparin serum, although its activity is rarely detected.	Heparin	60-67	lipoprotein lipase	Homo sapiens	12-30
14568192-1	2003	BACKGROUND: Lipoprotein lipase (LPL) mass is present in pre-heparin serum, although its activity is rarely detected.	Heparin	60-67	lipoprotein lipase	Homo sapiens	32-35
14585398-6	2003	Co-incubation of CTGF with heparin or perturbation of cell surface HSPGs with heparinase or sodium chlorate completely blocked adhesion of activated HSCs to all CTGF isoforms.	Heparin	27-34	cellular communication network factor 2	Rattus norvegicus	17-21
12682480-3	2003	Heparin has immunomodulatory properties and effectively inhibits L- and P-selectin binding in vitro.	Heparin	0-7	selectin P	Homo sapiens	72-82
12682480-12	2003	Of note, however, unfractionated heparin reduced L-selectin down-regulation and lymphocytopenia.	Heparin	33-40	selectin L	Homo sapiens	49-59
12674336-4	2003	To mimic activated signaling by mutated FGF receptors, we used heparin acrylic beads to deliver FGF ligands to mouse calvaria and demonstrated increased Msx2, Runx2, Bsp, and Osteocalcin gene expression, decreased cell proliferation, and suture obliteration and fusion.	Heparin	63-70	runt related transcription factor 2	Mus musculus	159-164
12674336-4	2003	To mimic activated signaling by mutated FGF receptors, we used heparin acrylic beads to deliver FGF ligands to mouse calvaria and demonstrated increased Msx2, Runx2, Bsp, and Osteocalcin gene expression, decreased cell proliferation, and suture obliteration and fusion.	Heparin	63-70	black spleen	Mus musculus	166-169
12674336-4	2003	To mimic activated signaling by mutated FGF receptors, we used heparin acrylic beads to deliver FGF ligands to mouse calvaria and demonstrated increased Msx2, Runx2, Bsp, and Osteocalcin gene expression, decreased cell proliferation, and suture obliteration and fusion.	Heparin	63-70	bone gamma-carboxyglutamate protein 2	Mus musculus	175-186
12697737-4	2003	All three mutations cause reduced binding to the central complement component C3b/C3d to heparin, as well as to endothelial cells.	Heparin	89-96	endogenous retrovirus group K member 13	Homo sapiens	82-85
6495266-4	1984	In semilogarithmic plots 125I-antithrombin III disappeared according to a double exponential curve with a half-life in the second phase of 56.8 hr in the absence of heparin and of 33.7 hr in the presence of heparin.	Heparin	165-172	serpin family C member 1	Homo sapiens	30-46
14511765-1	2003	In the blood coagulation cascade, human antithrombin III (hAT III) acts as an inhibitor of serine proteases such as thrombin and factor Xa, and this anticoagulatory glycoprotein requires the binding of heparin for its activation.	Heparin	202-209	serpin family C member 1	Homo sapiens	40-56
14511765-1	2003	In the blood coagulation cascade, human antithrombin III (hAT III) acts as an inhibitor of serine proteases such as thrombin and factor Xa, and this anticoagulatory glycoprotein requires the binding of heparin for its activation.	Heparin	202-209	serpin family C member 1	Homo sapiens	58-65
6495266-4	1984	In semilogarithmic plots 125I-antithrombin III disappeared according to a double exponential curve with a half-life in the second phase of 56.8 hr in the absence of heparin and of 33.7 hr in the presence of heparin.	Heparin	207-214	serpin family C member 1	Homo sapiens	30-46
14511765-2	2003	In this study, we synthesized the polypeptides corresponding to the proposed heparin-binding sites including the (41-49), (286-301) and (123-139) regions of hAT III, and examined their interactions with heparin by means of physicochemical and biochemical methods.	Heparin	77-84	serpin family C member 1	Homo sapiens	157-164
6495266-6	1984	These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III.	Heparin	36-43	serpin family C member 1	Homo sapiens	102-118
14511765-2	2003	In this study, we synthesized the polypeptides corresponding to the proposed heparin-binding sites including the (41-49), (286-301) and (123-139) regions of hAT III, and examined their interactions with heparin by means of physicochemical and biochemical methods.	Heparin	203-210	serpin family C member 1	Homo sapiens	157-164
14511765-4	2003	In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin.	Heparin	56-63	serpin family C member 1	Homo sapiens	13-20
12905705-3	2003	LPL mass and activity in post-heparin plasma and in in vitro expression were investigated.	Heparin	30-37	lipoprotein lipase	Homo sapiens	0-3
12905705-7	2003	They led to reduced LPL mass and enzyme activities in both post-heparin plasma and in vitro expression.	Heparin	64-71	lipoprotein lipase	Homo sapiens	20-23
6495266-6	1984	These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III.	Heparin	36-43	serpin family C member 1	Homo sapiens	144-160
14511765-4	2003	In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin.	Heparin	56-63	serpin family C member 1	Homo sapiens	85-92
14511765-4	2003	In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin.	Heparin	56-63	serpin family C member 1	Homo sapiens	85-92
6495266-6	1984	These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III.	Heparin	63-70	serpin family C member 1	Homo sapiens	102-118
14511765-4	2003	In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin.	Heparin	200-207	serpin family C member 1	Homo sapiens	13-20
14511765-4	2003	In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin.	Heparin	200-207	serpin family C member 1	Homo sapiens	85-92
6495266-6	1984	These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III.	Heparin	63-70	serpin family C member 1	Homo sapiens	144-160
14511765-4	2003	In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin.	Heparin	200-207	serpin family C member 1	Homo sapiens	85-92
14511765-5	2003	On the basis of these results, we prepared novel hAT III (123-139)-related derivatives as potent heparin antagonist candidates, and examined the influence of several modifications on their activity in vitro.	Heparin	97-104	serpin family C member 1	Homo sapiens	49-56
12820388-1	2003	BACKGROUND: The effects of three members of the heparin binding growth factor family, FGF-8, FGF-9 and KGF, on the human embryonal carcinoma-derived cells line tera 2 were examined.	Heparin	48-55	fibroblast growth factor 8	Homo sapiens	86-91
6495266-7	1984	Immuno-reactive antithrombin III decreased from 100% to 85-90% immediately after injection of 125I-antithrombin III in the presence of heparin and returned to normal values within 30 min.	Heparin	135-142	serpin family C member 1	Homo sapiens	16-32
12626998-10	2003	MEASUREMENTS AND MAIN RESULTS: Expression of GP IIb-IIIa and P-selectin on adenosine diphosphate-activated platelets and platelet-leukocyte aggregation were significantly lower after the passage of blood through the hemofilter in patients receiving an extracorporeal infusion of prostacyclin plus heparin when compared with control patients receiving heparin only.	Heparin	297-304	selectin P	Homo sapiens	61-71
12626998-10	2003	MEASUREMENTS AND MAIN RESULTS: Expression of GP IIb-IIIa and P-selectin on adenosine diphosphate-activated platelets and platelet-leukocyte aggregation were significantly lower after the passage of blood through the hemofilter in patients receiving an extracorporeal infusion of prostacyclin plus heparin when compared with control patients receiving heparin only.	Heparin	351-358	selectin P	Homo sapiens	61-71
12535750-10	2003	There was a significant and independent inverse association between insulin resistance (homeostasis model assessment insulin resistance (HOMA-IR) index) vs post-heparin plasma LPL activity and postprandial triglyceride levels, respectively.	Heparin	161-168	lipoprotein lipase	Homo sapiens	176-179
14511765-6	2003	The results provided new findings about the structure-activity relationship of hAT III (123-139), and led us to the successful development of a potent antagonist for heparin.	Heparin	166-173	serpin family C member 1	Homo sapiens	79-86
14563580-6	2003	In the heparin group, plasma PAI activity (IU/ml, median value [range]) was increased continuously from 8 to 24 h after thrombolysis and peaked at 24 h (30.9 [11.3 to 38.5]); on the other hand, it was not increased in the APC group at 24 h after thrombolysis (11.3 [0.0 to 31.0], p &lt; 0.01 vs. heparin group).	Heparin	7-14	serpin family E member 1	Homo sapiens	29-32
14563580-6	2003	In the heparin group, plasma PAI activity (IU/ml, median value [range]) was increased continuously from 8 to 24 h after thrombolysis and peaked at 24 h (30.9 [11.3 to 38.5]); on the other hand, it was not increased in the APC group at 24 h after thrombolysis (11.3 [0.0 to 31.0], p &lt; 0.01 vs. heparin group).	Heparin	296-303	serpin family E member 1	Homo sapiens	29-32
14564303-1	2003	BACKGROUND: Unfractionated heparin has been the cornerstone of antithrombin therapy in the treatment of non-ST-segment elevation acute coronary syndromes for more than a decade.	Heparin	27-34	serpin family C member 1	Homo sapiens	63-75
6495266-7	1984	Immuno-reactive antithrombin III decreased from 100% to 85-90% immediately after injection of 125I-antithrombin III in the presence of heparin and returned to normal values within 30 min.	Heparin	135-142	serpin family C member 1	Homo sapiens	99-115
12893682-6	2003	Both free and heparin-releasable ecSOD activities in the 129P3/J strain are more than 3-fold higher than those in the C57Bl/6 mice.	Heparin	14-21	superoxide dismutase 3, extracellular	Mus musculus	33-38
6382135-4	1984	Fifteen minutes after an intravenous heparin bolus of 100 IU/kg, mean lipoprotein lipase activity in infants (16.0 mumol free fatty acids/ml/h) was as in adults.	Heparin	37-44	lipoprotein lipase	Homo sapiens	70-88
12837765-10	2003	Commercial heparin was found to be a powerful inhibitor (I50 approximately 20 nM expressed as disaccharide unit, approximately 0.7 nM polysaccharide) of heparanase action toward antithrombin-binding oligosaccharides.	Heparin	11-18	serpin family C member 1	Homo sapiens	178-190
12565822-4	2003	In addition, expression of a dominant-negative form of Ras, which abolished the activities of epidermal growth factor (EGF) and heparin-binding EGF, had no affect on PFNP-induced DNA synthesis.	Heparin	128-135	epidermal growth factor	Mus musculus	144-147
12627673-15	2003	In addition, binding oligosaccharides are conjugated with antithrombin agents to mimic the anti-Xa/anti-IIa activities of heparin.	Heparin	122-129	serpin family C member 1	Homo sapiens	58-70
6740570-6	1984	The bound heparin (HRH2) had a high affinity for AT-III and precipitated LDL in the presence of Ca2+.	Heparin	10-17	serpin family C member 1	Homo sapiens	49-55
12871518-0	2003	Two new antithrombin variants support a role for K114 and R13 in heparin binding.	Heparin	65-72	serpin family C member 1	Homo sapiens	8-20
6740570-10	1984	Denatured AT-III did not bind HRH2, indicating that its heparin recognition site may depend on conformation.	Heparin	56-63	serpin family C member 1	Homo sapiens	10-16
12939144-0	2003	Introduction of a mutation in the shutter region of antithrombin (Phe77 --&gt; Leu) increases affinity for heparin and decreases thermal stability.	Heparin	107-114	serpin family C member 1	Homo sapiens	52-64
6375731-4	1984	Lipase activity and 14C-labeled protein co-eluted from heparin-Sepharose 4B at 1.2 M NaCl and were inhibited and precipitated by preincubation with anti-lipoprotein lipase gamma-globulins.	Heparin	55-62	lipase G, endothelial type	Rattus norvegicus	0-6
12939144-8	2003	Previous studies on shutter region mutations that destabilize antithrombin revealed that such variants possess enhanced affinity for both heparin pentasaccharide and full-length heparin.	Heparin	138-145	serpin family C member 1	Homo sapiens	62-74
12939144-10	2003	We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions.	Heparin	208-215	serpin family C member 1	Homo sapiens	101-113
12765778-0	2003	1976-1983, a critical period in the history of heparin: the discovery of the antithrombin binding site.	Heparin	47-54	serpin family C member 1	Homo sapiens	77-89
6375731-4	1984	Lipase activity and 14C-labeled protein co-eluted from heparin-Sepharose 4B at 1.2 M NaCl and were inhibited and precipitated by preincubation with anti-lipoprotein lipase gamma-globulins.	Heparin	55-62	lipase G, endothelial type	Rattus norvegicus	165-171
12765778-1	2003	Heparin inhibits blood coagulation by binding to the protease inhibitor antithrombin, thus promoting inactivation of the protease "factors" of the coagulation cascade mechanism.	Heparin	0-7	serpin family C member 1	Homo sapiens	72-84
12939144-10	2003	We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions.	Heparin	208-215	serpin family C member 1	Homo sapiens	195-207
12765778-2	2003	The article provides an overview of the studies, by different research groups, that led to the structural elucidation of the antithrombin-binding region of heparin.	Heparin	156-163	serpin family C member 1	Homo sapiens	125-137
6202346-0	1984	In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. A large number of negatively charged macromolecules, including DNA, glycosaminoglycans, and proteoglycans, were tested as possible activators of the contact (Hageman factor) system in vitro.	Heparin	72-79	coagulation factor XII	Rattus norvegicus	36-50
12765778-3	2003	These studies were triggered by the finding that only a fraction of heparin molecules were capable of binding with high affinity to antithrombin, and further that this fraction essentially accounted for the anticoagulant activity of the unfractionated material.	Heparin	68-75	serpin family C member 1	Homo sapiens	132-144
13129403-5	2003	Since conjugation of Fab" to PEG-PEI might influence complex stability, this issue was addressed by incubating the complexes with increasing amounts of heparin.	Heparin	152-159	FA complementation group B	Homo sapiens	21-24
14521318-9	2003	The use of antithrombin III is one way of preventing heparin resistance.	Heparin	53-60	serpin family C member 1	Homo sapiens	11-27
12587674-0	2003	Muscle reinnervation and IGF-I synthesis are affected by exposure to heparin: an effect partially antagonized by anti-growth hormone-releasing hormone.	Heparin	69-76	insulin-like growth factor 1	Rattus norvegicus	25-30
12587674-4	2003	In addition, treatment with heparin increased markedly insulin-like growth factor-I levels in denervated muscles.	Heparin	28-35	insulin-like growth factor 1	Rattus norvegicus	55-83
12941037-4	2003	In buffer, heparin and SanOrg123781A inhibited FXa and thrombin at similar concentrations [concentration inhibiting 50% (IC50) of Xa and IIa activity were, respectively: heparin 120 +/- 7 and 3 +/- 1 ng mL-1; SanOrg123781A 77 +/- 5 and 4 +/- 1 ng mL-1].	Heparin	11-18	L1 cell adhesion molecule	Mus musculus	203-207
12941037-4	2003	In buffer, heparin and SanOrg123781A inhibited FXa and thrombin at similar concentrations [concentration inhibiting 50% (IC50) of Xa and IIa activity were, respectively: heparin 120 +/- 7 and 3 +/- 1 ng mL-1; SanOrg123781A 77 +/- 5 and 4 +/- 1 ng mL-1].	Heparin	11-18	L1 cell adhesion molecule	Mus musculus	247-251
12941037-7	2003	We showed that heparin and SanOrg123781A were able to inhibit fragment F1+2 generation induced by clot-bound FXa with IC50 values of 2 +/- 0.5 micro g mL-1 and 0.6 +/- 0.2 micro g mL-1, respectively.	Heparin	15-22	L1 cell adhesion molecule	Mus musculus	151-163
12941037-7	2003	We showed that heparin and SanOrg123781A were able to inhibit fragment F1+2 generation induced by clot-bound FXa with IC50 values of 2 +/- 0.5 micro g mL-1 and 0.6 +/- 0.2 micro g mL-1, respectively.	Heparin	15-22	L1 cell adhesion molecule	Mus musculus	151-155
12941037-8	2003	Both compounds also inhibited clot-bound thrombin activity, the IC50 values of heparin and SanOrg123781A being 1 +/- 0.01 micro g mL-1 and 0.1 +/- 0.1 micro g mL-1, respectively.	Heparin	79-86	L1 cell adhesion molecule	Mus musculus	130-163
12441904-12	2002	Accordingly, the supplementation of AT without concomitant heparin may be beneficial in disorders with inflammatory characteristics, which has to be demonstrated in further clinical studies.	Heparin	59-66	serpin family C member 1	Homo sapiens	36-38
6733045-0	1984	The inhibition of the anticoagulant activity of heparin by platelets, brain phospholipids, and tissue factor.	Heparin	48-55	coagulation factor III, tissue factor	Homo sapiens	95-108
14531265-6	2003	Several recent articles have reported that heparin resistance was corrected with antithrombin III concentrates, fresh frozen plasma, or argatroban.	Heparin	43-50	serpin family C member 1	Homo sapiens	81-97
6724150-0	1984	Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation.	Heparin	14-21	serpin family C member 1	Homo sapiens	38-54
12466191-8	2002	IGFBP-3 and -5 have carboxyl-terminal basic motifs incorporating heparin-binding and additional basic residues that interact with the cell surface and matrix, the nuclear transporter importin-beta, and other proteins.	Heparin	65-72	insulin like growth factor binding protein 3	Homo sapiens	0-14
12384988-6	2002	In contrast, cell adhesion to fibronectin was inhibited by NH and modified heparins in a size-dependent manner with the lowest effect by the smallest compound.	Heparin	75-83	fibronectin 1	Rattus norvegicus	30-41
13677267-13	2003	In patients who have hereditary antithrombin deficiency, antiphospholipid antibodies, a combined abnormality or a history of a severe thrombotic event (pulmonary embolism, extended deep vein thrombosis) should be advised to use prophylactic heparin during pregnancy, starting during the first trimester.	Heparin	241-248	serpin family C member 1	Homo sapiens	32-44
6724150-2	1984	The effect of nonenzymatic glycosylation on the biologic function of human antithrombin III was evaluated using a chromogenic thrombin substrate assay in the presence of catalytic amounts of heparin.	Heparin	191-198	serpin family C member 1	Homo sapiens	75-91
12889008-7	2003	Moreover, the experiments performed on leukocytes and on CD14-positive Chinese hamster ovary cells indicated that heparin inhibited LPS binding.	Heparin	114-121	LOW QUALITY PROTEIN: monocyte differentiation antigen CD14	Cricetulus griseus	57-61
6724150-4	1984	This glycosylation-induced inhibition of heparin-catalyzed antithrombin III activity was completely reversible by preassay incubation with excess sodium heparin.	Heparin	41-48	serpin family C member 1	Homo sapiens	59-75
6724150-4	1984	This glycosylation-induced inhibition of heparin-catalyzed antithrombin III activity was completely reversible by preassay incubation with excess sodium heparin.	Heparin	146-160	serpin family C member 1	Homo sapiens	59-75
6204398-6	1984	Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel.	Heparin	70-77	serpin family C member 1	Homo sapiens	104-116
12960955-0	2003	Lower plasma levels of lipoprotein lipase after infusion of low molecular weight heparin than after administration of conventional heparin indicate more rapid catabolism of the enzyme.	Heparin	81-88	lipoprotein lipase	Homo sapiens	23-41
12960955-0	2003	Lower plasma levels of lipoprotein lipase after infusion of low molecular weight heparin than after administration of conventional heparin indicate more rapid catabolism of the enzyme.	Heparin	131-138	lipoprotein lipase	Homo sapiens	23-41
12960955-4	2003	Low molecular weight (LMW) heparin preparations are widely used in the clinic and are supposed to release less LPL.	Heparin	27-34	lipoprotein lipase	Homo sapiens	111-114
12530914-1	2002	Sp17 was originally proposed to be a sperm-specific protein and thought to play a role in sperm-egg interactions by binding to the zona pellucida via two conserved heparin-binding motifs.	Heparin	164-171	sperm autoantigenic protein 17	Homo sapiens	0-4
12472678-7	2002	Finally, as an estimate of function, SAP from SLE patients appeared to have the same affinity for heparin and nucleosomes as SAP from normal individuals, when analysed by crossed affinity immunoelectrophoresis and enzyme-linked immunosorbent capture assay (ELISA).	Heparin	98-105	amyloid P component, serum	Homo sapiens	37-40
12960955-7	2003	When a bolus of heparin was given after 4 hours" infusion of LMW or conventional heparin, only relatively small, and similar, amounts of LPL entered plasma.	Heparin	16-23	lipoprotein lipase	Homo sapiens	137-140
6204398-6	1984	Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel.	Heparin	70-77	serpin family C member 1	Homo sapiens	153-165
12960955-8	2003	This suggests that the difference between LMW and conventional heparin lay in the ability to retain LPL in the circulating blood, not in the ability to release the lipase.	Heparin	63-70	lipoprotein lipase	Homo sapiens	100-103
6204398-6	1984	Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel.	Heparin	171-178	serpin family C member 1	Homo sapiens	104-116
12536119-0	2002	Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases.	Heparin	0-7	serpin family C member 1	Homo sapiens	18-30
6204398-7	1984	It was concluded that molecular alteration of the antithrombin molecule seemed to affect only the heparin binding site thus preventing from any rate enhancement of thrombin inactivation.	Heparin	98-105	serpin family C member 1	Homo sapiens	50-62
12536119-2	2002	Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex.	Heparin	0-7	serpin family C member 1	Homo sapiens	18-30
12536119-2	2002	Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex.	Heparin	0-7	serpin family C member 1	Homo sapiens	209-221
12536119-3	2002	Although x-ray structures of antithrombin, free and complexed with heparin, have suggested that exposure of a reactive proteinase binding loop is a key feature of conformational activation, mutagenesis of reactive loop residues indicates that the function of this structural change is not to present an optimal loop sequence to target clotting proteinases.	Heparin	67-74	serpin family C member 1	Homo sapiens	29-41
12395090-7	2002	Expression of early response genes such as c-fos or Egr1 increased and sustained in the presence of heparin more than that without heparin.	Heparin	100-107	early growth response 1	Homo sapiens	52-56
12911595-1	2003	We previously localized the heparin binding region on high molecular weight kininogen to domain 5 (D5) by quantifying the binding using surface plasmon resonance of D5 fused at its N-terminal to glutathione-S-transferase.	Heparin	28-35	glutathione S-transferase kappa 1	Homo sapiens	195-220
12911595-8	2003	Both H483-K497 and G486-K502 were effective in neutralizing the accelerated inhibition by heparin of thrombin by antithrombin in the absence of Zn++.	Heparin	90-97	serpin family C member 1	Homo sapiens	113-125
12888879-0	2003	Affinity and kinetics of P-selectin binding to heparin.	Heparin	47-54	selectin P	Homo sapiens	25-35
12888879-2	2003	It also binds to heparin and heparan sulfate proteoglycans (HSPGs), which attenuates P-selectin mediated adhesions of leukocytes and cancer cells.	Heparin	17-24	selectin P	Homo sapiens	85-95
12888879-5	2003	Heparin inhibited the adhesion of A375 cells to immobilized P-selectin under flow (IC(50) = 3 microM heparin) and neutralized the binding of P-selectin to A375 cells (IC50 = 4 microM heparin).	Heparin	0-7	selectin P	Homo sapiens	60-70
12888879-5	2003	Heparin inhibited the adhesion of A375 cells to immobilized P-selectin under flow (IC(50) = 3 microM heparin) and neutralized the binding of P-selectin to A375 cells (IC50 = 4 microM heparin).	Heparin	0-7	selectin P	Homo sapiens	141-151
12888879-5	2003	Heparin inhibited the adhesion of A375 cells to immobilized P-selectin under flow (IC(50) = 3 microM heparin) and neutralized the binding of P-selectin to A375 cells (IC50 = 4 microM heparin).	Heparin	101-108	selectin P	Homo sapiens	60-70
12369826-0	2002	Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding.	Heparin	86-93	serpin family C member 1	Homo sapiens	70-82
12888879-6	2003	Using surface plasmon resonance technique, we found that P-selectin bound to heparin with a dissociation constant (K(d)) of 115 +/- 6 nM.	Heparin	77-84	selectin P	Homo sapiens	57-67
6378216-6	1984	Intravenous administration of heparin led to a substantial decrease of immunodetectable LPL in vessels, whereas the enzyme in adipocytes and connective tissue cells was unaffected.	Heparin	30-37	lipoprotein lipase	Homo sapiens	88-91
12359775-4	2002	In all four cell lines, AdtrEGFR markedly attenuated EGF and heparin-binding EGF-dependent cell growth, EGFR family tyrosine phosphorylation, and phosphorylation of MAPK, c-Jun NH2-terminal kinase, p38 MAPK, and activating transcription factor 2.	Heparin	61-68	epidermal growth factor	Homo sapiens	28-31
12846563-0	2003	Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites.	Heparin	0-7	serpin family C member 1	Homo sapiens	46-58
6729779-5	1984	But the high amount of thrombin needed to obtain a 50% reduction of the circulating AT III required a corresponding high amount of protective heparin.	Heparin	142-149	serpin family C member 1	Homo sapiens	84-90
12846563-2	2003	Here we show that antithrombin is essentially unreactive with factor IXa in the absence of heparin (k(ass) approximately 10 M(-1) s(-1)) but undergoes a remarkable approximately 1 million-fold enhancement in reactivity with this proteinase to the physiologically relevant range (k(ass) approximately 10(7) M(-1) s(-1)) when activated by heparin in the presence of physiologic levels of calcium.	Heparin	91-98	serpin family C member 1	Homo sapiens	18-30
12846563-2	2003	Here we show that antithrombin is essentially unreactive with factor IXa in the absence of heparin (k(ass) approximately 10 M(-1) s(-1)) but undergoes a remarkable approximately 1 million-fold enhancement in reactivity with this proteinase to the physiologically relevant range (k(ass) approximately 10(7) M(-1) s(-1)) when activated by heparin in the presence of physiologic levels of calcium.	Heparin	337-344	serpin family C member 1	Homo sapiens	18-30
12846563-3	2003	This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length).	Heparin	126-133	serpin family C member 1	Homo sapiens	90-102
12846563-3	2003	This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length).	Heparin	126-133	serpin family C member 1	Homo sapiens	265-277
12846563-3	2003	This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length).	Heparin	245-252	serpin family C member 1	Homo sapiens	90-102
12176868-7	2002	We propose that this binding fragment may wrap around the MIP1alpha dimer in a horseshoe shape, facilitating the interaction of the S-domains with the heparin-binding domains on each monomer.	Heparin	151-158	C-C motif chemokine ligand 3	Homo sapiens	58-67
12846563-4	2003	Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity.	Heparin	258-265	serpin family C member 1	Homo sapiens	48-60
6704544-1	1984	High and low affinity heparin (HA and LA heparin) were prepared from commercial heparin by affinity chromatography to insolubilized antithrombin III.	Heparin	22-29	serpin family C member 1	Homo sapiens	132-148
12846563-4	2003	Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity.	Heparin	286-293	serpin family C member 1	Homo sapiens	48-60
6704544-4	1984	LA heparin failed to induce anticoagulant activity but released the hepatic triglyceride lipase (H-TGL) and lipoprotein lipase (LPL) activities normally.	Heparin	3-10	lipoprotein lipase	Homo sapiens	128-131
12821548-6	2003	The mitogenic effect of BSDL was associated with an activation of the extracellular signal-regulated kinase 1/2 mitogen-activated protein kinase pathway, which was inhibited by heparin, and involved several mechanisms, among them diacylglycerol and oleic acid production as well as a rapid basic fibroblast growth factor release.	Heparin	177-184	carboxyl ester lipase	Homo sapiens	24-28
12799194-2	2003	We have studied the mechanism whereby heparin directs FGF-2-induced FGF receptor-1 (FGFR-1) signal transduction.	Heparin	38-45	fibroblast growth factor receptor 1	Cricetulus griseus	68-82
12799194-2	2003	We have studied the mechanism whereby heparin directs FGF-2-induced FGF receptor-1 (FGFR-1) signal transduction.	Heparin	38-45	fibroblast growth factor receptor 1	Cricetulus griseus	84-90
12799194-8	2003	Our data imply that tyrosine 463 is phosphorylated and able to transduce signals in response to FGF-2 treatment alone; furthermore, we suggest that FGFR-1 dimerization/kinase activation is stabilized by heparin.	Heparin	203-210	fibroblast growth factor receptor 1	Cricetulus griseus	148-154
12871328-1	2003	Antithrombin and its cofactor, heparin, target both the product of prothrombin activation by prothrombinase, thrombin, as well as the enzyme responsible for the reaction, factor (F)Xa.	Heparin	31-38	serpin family C member 1	Homo sapiens	0-12
12871328-9	2003	Therefore, in the presence of unfractionated heparin, fondaparinux, or enoxaparin, prothrombinase is profoundly protected from antithrombin.	Heparin	45-52	serpin family C member 1	Homo sapiens	127-139
12350245-1	2002	Low-molecular-weight heparins (LMWH) are efficacious agents that offer clinical and pharmacoeconomic advantages over unfractionated heparin (UFH) for the treatment of ACS and venous thromboembolism.	Heparin	21-29	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	167-170
12350245-1	2002	Low-molecular-weight heparins (LMWH) are efficacious agents that offer clinical and pharmacoeconomic advantages over unfractionated heparin (UFH) for the treatment of ACS and venous thromboembolism.	Heparin	21-28	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	167-170
12353073-0	2002	Antithrombin "DREUX" (Lys 114Glu): a variant with complete loss of heparin affinity.	Heparin	67-74	serpin family C member 1	Homo sapiens	0-12
6704544-12	1984	On the basis of these kinetics, we suggest that, after intravenous administration of heparin, the two lipolytic enzymes present in plasma are complexed with heparin, analogous to the heparin-antithrombin III complex.	Heparin	85-92	serpin family C member 1	Homo sapiens	191-207
12147226-3	2002	Site-directed mutagenesis indicated that the heparin-binding domain of EC-SOD functions as the nuclear localization signal.	Heparin	45-52	superoxide dismutase 3, extracellular	Mus musculus	71-77
6704544-12	1984	On the basis of these kinetics, we suggest that, after intravenous administration of heparin, the two lipolytic enzymes present in plasma are complexed with heparin, analogous to the heparin-antithrombin III complex.	Heparin	157-164	serpin family C member 1	Homo sapiens	191-207
12147226-4	2002	These results suggest that the mechanism of the nuclear transport of EC-SOD involves a series of N-terminal signal peptide- and C-terminal heparin-binding domain-dependent processes of secretion, re-uptake and the subsequent nuclear translocation.	Heparin	139-146	superoxide dismutase 3, extracellular	Mus musculus	69-75
12948833-1	2003	In the blood coagulation cascade, heparin activates human plasma antithrombin III (hAT III), resulting in the inhibition of factor Xa.	Heparin	34-41	serpin family C member 1	Homo sapiens	65-81
12948833-1	2003	In the blood coagulation cascade, heparin activates human plasma antithrombin III (hAT III), resulting in the inhibition of factor Xa.	Heparin	34-41	serpin family C member 1	Homo sapiens	83-90
6721831-7	1984	An octadecasaccharide is therefore the smallest heparin fragment (prepared by nitrous acid depolymerization) that can accelerate thrombin inhibition by antithrombin III.	Heparin	48-55	serpin family C member 1	Homo sapiens	152-168
12626499-8	2003	Finally, although these residues lie within a major heparin-binding site in IGFBP-5 and -3, we also show that the mutations in C-Term have no effect on heparin binding.	Heparin	52-59	insulin-like growth factor binding protein 5	Rattus norvegicus	76-90
12034712-5	2002	We show that the ectodomains of FGFR1 IIIc and FGFR2 IIIc exhibit specific interactions with different characteristics for both heparin and porcine mucosal HS.	Heparin	128-135	fibroblast growth factor receptor 2	Homo sapiens	47-52
12034712-8	2002	FGFR1 and FGFR2 bind heparin with mean association rate constants of 1.9 x 10(5) and 2.1 x 10(6) m(-1)s(-1), respectively, and dissociation rate constants of 1.2 x 10(-2) and 2.7 x 10(-2) s(-1), respectively.	Heparin	21-28	fibroblast growth factor receptor 2	Homo sapiens	10-15
12034712-10	2002	Hence, FGFR1 and FGFR2 bind to heparin chains with markedly different kinetics and affinities.	Heparin	31-38	fibroblast growth factor receptor 2	Homo sapiens	17-22
6721831-10	1984	Such binding results in either steric interference with the formation of antithrombin III-proteinase complexes or in displacement of the antithrombin III molecule from the heparin chain.	Heparin	172-179	serpin family C member 1	Homo sapiens	137-153
6722255-1	1984	The inhibition of thrombin by antithrombin III is known to be accelerated by heparin through the formation of complexes between the muccopolysaccharide and both proteins.	Heparin	77-84	serpin family C member 1	Homo sapiens	30-46
12223091-3	2002	Methyl-beta-cyclodextrin and some osmolytes, such as glycerol, sucrose, proline, glycine, and heparin, could effectively prevent the aggregation, implying an artificial chaperone role of those substances during fatty acid synthase unfolding.	Heparin	94-101	fatty acid synthase	Gallus gallus	211-230
6747369-1	1984	Heparin anticoagulation during extracorporeal circulation in an antithrombin III deficit patient].	Heparin	0-7	serpin family C member 1	Homo sapiens	64-80
12244479-1	2002	NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution.	Heparin	41-48	serpin family C member 1	Homo sapiens	74-86
12244479-4	2002	The pentasaccharide corresponding to the active site of heparin/heparan sulfate for antithrombin (AT) adopts in the complex with the protein a conformation different from that in the absence of the protein.	Heparin	56-63	serpin family C member 1	Homo sapiens	84-96
12244482-0	2002	Effects of calcium ions on the interactions between antithrombin and factor Xa mediated by variously sulfated, semisynthetic low-molecular-weight heparins.	Heparin	146-154	serpin family C member 1	Homo sapiens	52-64
12244482-1	2002	A homogeneous set of low-molecular weight heparins, chemically modified to yield different degrees of sulfation, were investigated for their ability to interfere with the antithrombin (AT)-factor Xa (FXa) interaction process in the presence or absence of physiological concentrations of calcium ions.	Heparin	42-50	serpin family C member 1	Homo sapiens	171-183
12739991-3	2003	Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases.	Heparin	0-7	serpin family C member 1	Homo sapiens	165-177
12739991-3	2003	Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases.	Heparin	50-58	serpin family C member 1	Homo sapiens	165-177
12691755-6	2003	We demonstrate experimentally that D.melanogaster TSP is assembled as a pentamer, has heparin-binding activity and is a component of extracellular matrix (ECM).	Heparin	86-93	Thrombospondin	Drosophila melanogaster	50-53
12591924-0	2003	Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis.	Heparin	121-128	serpin family C member 1	Homo sapiens	35-47
12591924-0	2003	Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis.	Heparin	121-128	serpin family C member 1	Homo sapiens	57-69
12591924-3	2003	The abnormal antithrombin was separated from the normal inhibitor by complexing the latter with thrombin followed by heparin-agarose affinity chromatography.	Heparin	117-124	serpin family C member 1	Homo sapiens	13-25
12591924-4	2003	The purified variant, antithrombin London, was completely inactive as a thrombin or factor Xa inhibitor even after heparin activation.	Heparin	115-122	serpin family C member 1	Homo sapiens	22-34
12591924-7	2003	Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction.	Heparin	39-46	serpin family C member 1	Homo sapiens	70-82
12591924-7	2003	Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction.	Heparin	134-141	serpin family C member 1	Homo sapiens	70-82
12591924-7	2003	Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction.	Heparin	134-141	serpin family C member 1	Homo sapiens	171-183
12591924-9	2003	The unusually severe thrombosis associated with the heterozygous mutation may be explained by the ability of antithrombin London to bind endogenous heparan sulfate or heparin molecules with high affinity and to thereby block activation of the normal inhibitor.	Heparin	167-174	serpin family C member 1	Homo sapiens	109-121
12048130-0	2002	Activity and concentration of lipoprotein lipase in post-heparin plasma and the extent of coronary artery disease.	Heparin	57-64	lipoprotein lipase	Homo sapiens	30-48
12048130-3	2002	We quantitated activity and concentration of LPL in post-heparin plasma from 194 male patients undergoing coronary angiography.	Heparin	57-64	lipoprotein lipase	Homo sapiens	45-48
12361208-0	2002	Direct antithrombin agents ameliorate disseminated intravascular coagulation in suspected heparin-induced thrombocytopenia thrombosis syndrome.	Heparin	90-97	serpin family C member 1	Homo sapiens	7-19
12361208-1	2002	This is a case series of 5 patients who were treated with the direct antithrombin agents (lepirudin or argatroban) for known or suspected heparin-induced thrombocytopenia thrombosis syndrome (HITTs).	Heparin	138-145	serpin family C member 1	Homo sapiens	69-81
6719385-7	1984	However, Sepharose-coupled thrombin mixed with plasma in the presence of heparin produced outstanding quantities of residual immunoreactive AT III devoid of inhibitory activity.	Heparin	73-80	serpin family C member 1	Homo sapiens	140-146
12161073-0	2002	Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants.	Heparin	60-67	serpin family C member 1	Homo sapiens	82-94
12161073-2	2002	The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin.	Heparin	67-74	serpin family C member 1	Homo sapiens	104-116
12161073-2	2002	The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin.	Heparin	227-234	serpin family C member 1	Homo sapiens	104-116
12551943-11	2003	Tissue LPL activity decreased by about 10% in 2 min and by 50% in 1 h. Heparin released mainly the active form of the lipase.	Heparin	71-78	lipase G, endothelial type	Rattus norvegicus	118-124
6319400-6	1984	The purified Cre protein binds to loxP-containing DNA and makes complexes that are resistant to heparin.	Heparin	96-103	site-specific integrase	Escherichia phage P1	13-16
12655575-7	2003	They led to reduced LPL mass and enzyme activities in both post-heparin plasma and in vitro expression.	Heparin	64-71	lipoprotein lipase	Homo sapiens	20-23
12161073-2	2002	The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin.	Heparin	227-234	serpin family C member 1	Homo sapiens	104-116
12161073-5	2002	The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active.	Heparin	91-98	serpin family C member 1	Homo sapiens	147-159
12161073-5	2002	The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active.	Heparin	125-132	serpin family C member 1	Homo sapiens	55-67
12161073-5	2002	The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active.	Heparin	125-132	serpin family C member 1	Homo sapiens	147-159
12161073-5	2002	The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active.	Heparin	125-132	serpin family C member 1	Homo sapiens	55-67
12161073-5	2002	The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active.	Heparin	125-132	serpin family C member 1	Homo sapiens	147-159
12603746-5	2003	Three B. burgdorferi surface proteins, Bgp, DbpA and DbpB, have been demonstrated previously to bind to GAGs or to GAG-containing molecules, and we show here that recombinant derivatives of each of these proteins were able to bind to purified heparin and dermatan sulphate.	Heparin	243-250	Y-box binding protein 3	Homo sapiens	44-48
6691921-1	1984	Long-term warfarin therapy was changed to subcutaneous heparin to cover a planned pregnancy in a patient with congenital antithrombin III (AT III) deficiency.	Heparin	55-62	serpin family C member 1	Homo sapiens	121-137
12535860-3	2003	Antithrombin hyperactivation is mediated by inhibition of platelet factor 4 release from alpha-granules, leading to higher heparin availability.	Heparin	123-130	serpin family C member 1	Homo sapiens	0-12
12544739-1	2003	Anti-heparin platelet factor 4 (anti-HPF4) antibodies have been demonstrated to play a pathogenetic role in the development of heparin-induced thrombocytopenia.	Heparin	5-12	zinc finger protein 85	Homo sapiens	37-41
12119116-10	2002	This residue is conserved in LPL from all mammals and has been shown to be critical for enzyme stability at 37 degrees C. On chromatography on heparin-Sepharose trout and chicken LPL eluted at higher salt concentration than bovine (or other mammalian) LPL.	Heparin	143-150	lipoprotein lipase	Homo sapiens	29-32
12119116-11	2002	The C-terminal end of LPL has been implied in heparin binding and the higher heparin affinity of the trout and chicken enzymes may be because they have 17 and 15 extra amino acid residues at the C-terminal end, of which three residues are positively charged.	Heparin	46-53	lipoprotein lipase	Homo sapiens	22-25
12119116-11	2002	The C-terminal end of LPL has been implied in heparin binding and the higher heparin affinity of the trout and chicken enzymes may be because they have 17 and 15 extra amino acid residues at the C-terminal end, of which three residues are positively charged.	Heparin	77-84	lipoprotein lipase	Homo sapiens	22-25
11920660-4	2002	The results showed that fucan, dextran derivatives, and heparin differentially (1) triggered interleukin-1alpha, tumor necrosis factor alpha, interleukin-6, and interleukin-8 production by monocytes in a dose-dependent manner, (2) modulated cytokine production by LPS-stimulated monocytes, and (3) specifically inhibited the binding of biotinylated LPS to monocyte membranes.	Heparin	56-63	interleukin 1 alpha	Homo sapiens	93-140
19498968-6	2002	We partially purified OBIF with successive three-step chromatography by heparin affinity, anion exchange, and reverse-phase columns.	Heparin	72-79	transmembrane protein 119	Mus musculus	22-26
6420409-0	1984	Pyridoxylation of essential lysines in the heparin-binding site of antithrombin III.	Heparin	43-50	serpin family C member 1	Homo sapiens	67-83
12634318-6	2003	Comparison of various HS preparations and the unsulfated K5 polysaccharide as substrates indicate that both NDST-1 and -2 can differentially N-sulfate polysaccharides already modified to some extent by various other enzymes involved in HS/heparin synthesis.	Heparin	239-246	N-deacetylase and N-sulfotransferase 1	Homo sapiens	108-121
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	160-167	serpin family C member 1	Homo sapiens	56-72
12891293-12	2003	CONCLUSION: Compared with controls the use of ticlopidine in patients with NSTEACS treated with aspirin and UFH was associated with less pronounced lowering of PAI activity and lower level of D-dimer.	Heparin	108-111	serpin family E member 1	Homo sapiens	160-163
12073179-6	2002	Based on studies of the heparin binding site of antithrombin, this novel pentasaccharide has superior pharmacokinetics and bioavailability when compared with LMWH and can be administered once daily.	Heparin	24-31	serpin family C member 1	Homo sapiens	48-60
6693405-2	1984	Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol.	Heparin	160-167	serpin family C member 1	Homo sapiens	56-72
6434227-1	1984	Lactoferrin from human milk, pancreatic juice and bovine milk were purified by heparin-Sepharose affinity chromatography procedure.	Heparin	79-86	lactotransferrin	Bos taurus	0-11
11973346-6	2002	Heparin-agarose-purified p33/30 was identified as histone H1.	Heparin	0-7	inhibitor of growth family member 1	Homo sapiens	25-28
12729069-0	2003	Lipoprotein lipase during heparin infusion: lower activity in hemodialysis patients.	Heparin	26-33	lipoprotein lipase	Homo sapiens	0-18
12729069-10	2003	CONCLUSIONS: During hemodialysis with heparin, there is a peak in LPL activity as well as a reduction in triglycerides during the first hour.	Heparin	38-45	lipoprotein lipase	Homo sapiens	66-69
6083907-4	1984	In acquired AT III defects the anticoagulant activity of heparin is not necessarily decreased.	Heparin	57-64	serpin family C member 1	Homo sapiens	12-18
6083907-5	1984	After continuous infusion of doses below 500 USP in patients with DICFS and after administration of heparin doses of 750 USP/h/70 kg in patients undergoing fibrinolytic therapy the AT III content rather increases continuously.	Heparin	100-107	serpin family C member 1	Homo sapiens	181-187
11981148-1	2002	BACKGROUND: Acquired antithrombin III (AT) deficiency may render heparin less effective during cardiac surgery and cardiopulmonary bypass (CPB).	Heparin	65-72	serpin family C member 1	Homo sapiens	21-37
6083907-6	1984	After extremely high heparin doses during extracorporeal circulation in the heart-lung machine transitorily decreased AT III values return to normal.	Heparin	21-28	serpin family C member 1	Homo sapiens	118-124
12540961-2	2003	Here, the anti-fXa and anti-prothrombinase activities of DX-9065a which is an active-site directed inhibitor of fXa, and therapeutic heparins which are dependent on antithrombin (AT) for their anticoagulant function, were studied in amidolytic and proteolytic activity assays.	Heparin	133-141	serpin family C member 1	Homo sapiens	165-177
6083907-7	1984	In certain risk situations, however, such as after bolus injection of comparatively high heparin doses in patients with greatly reduced AT III values, a lowered anticoagulant effect of high heparin doses must be expected.	Heparin	89-96	serpin family C member 1	Homo sapiens	136-142
6083907-7	1984	In certain risk situations, however, such as after bolus injection of comparatively high heparin doses in patients with greatly reduced AT III values, a lowered anticoagulant effect of high heparin doses must be expected.	Heparin	190-197	serpin family C member 1	Homo sapiens	136-142
12007569-5	2002	In vitro studies indicated that HSA-modified with heparin 6 or 13 kD displayed anti-HIV activity (IC50=660 and 37 nM, respectively) and exhibited affinity for gp120-V3 loop, although the activity was lower than that of Suc-HSA.	Heparin	50-57	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	159-164
6083907-9	1984	However, when enhanced heparin resistance is suspected or diagnosed, treatment with AT III concentrates is justified only when the diagnosis is based on laboratory findings.	Heparin	23-30	serpin family C member 1	Homo sapiens	84-90
6378816-1	1984	The activity of lipoprotein-lipase in heparin-eluates of adipose tissue (AT-LPLA) of three body regions was measured in 22 obese and 18 nonobese females under basal conditions.	Heparin	38-45	lipoprotein lipase	Homo sapiens	16-34
12029263-6	2002	Moreover, patients pre-treated with heparin reach the operating theater with reduced levels of circulating antithrombin III; this may lead to the heparin resistance phenomenon and may further increase the risk for postoperative thrombotic complications.	Heparin	36-43	serpin family C member 1	Homo sapiens	107-123
12029263-6	2002	Moreover, patients pre-treated with heparin reach the operating theater with reduced levels of circulating antithrombin III; this may lead to the heparin resistance phenomenon and may further increase the risk for postoperative thrombotic complications.	Heparin	146-153	serpin family C member 1	Homo sapiens	107-123
11832488-7	2002	These results suggest the essential roles of DEXT3, its human ortholog EXTL3, and the C. elegans ortholog rib-2 in the biosynthesis of heparan sulfate and heparin, if present, in the respective organisms.	Heparin	155-162	exostosin like glycosyltransferase 3	Homo sapiens	71-76
11939772-1	2002	The anticoagulant sulfated polysaccharide, heparin, binds to the plasma coagulation proteinase inhibitor, antithrombin, and activates it by a conformational change that results in a greatly increased rate of inhibition of target proteinases.	Heparin	43-50	serpin family C member 1	Homo sapiens	106-118
12487777-7	2002	The increase of CD62p expression within the first 5 min was 2.5-times higher in systems with uncoated stents and 1.7-times higher in the control than in systems with heparin-coated stents (P&lt;0.05).	Heparin	166-173	selectin P	Homo sapiens	16-21
12626202-0	2002	Cell adhesion and tissue factor upregulation in oxygenators used during coronary artery bypass grafting are modified by the Corline Heparin Surface.	Heparin	132-139	coagulation factor III, tissue factor	Homo sapiens	18-31
12626202-8	2002	The coated group with high level of heparin showed higher surface-expression of TF with low levels of TFmRNA.	Heparin	36-43	coagulation factor III, tissue factor	Homo sapiens	80-82
12626202-9	2002	CONCLUSION: The CHS was most biocompatible with the standard level of heparin used during CABG whereas elevation of systemic heparin rather increased the activation and TF upregulation in monocytes from oxygenators.	Heparin	125-132	coagulation factor III, tissue factor	Homo sapiens	169-171
12393591-0	2002	Heparin inhibits the flow adhesion of sickle red blood cells to P-selectin.	Heparin	0-7	selectin P	Homo sapiens	64-74
12393591-5	2002	We postulated that the adhesion of sickle cells to P-selectin might be the pathway blocked by unfractionated heparin.	Heparin	109-116	selectin P	Homo sapiens	51-61
12393591-9	2002	These findings and the general role of P-selectin in initiating adhesion of blood cells to the endothelium suggest that unfractionated heparin may be useful in preventing painful vascular occlusion.	Heparin	135-142	selectin P	Homo sapiens	39-49
11939772-2	2002	Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin.	Heparin	258-265	serpin family C member 1	Homo sapiens	10-22
11939772-2	2002	Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin.	Heparin	258-265	serpin family C member 1	Homo sapiens	175-187
6317042-3	1983	The activity of liver lipase, an enzyme that can be released from the liver by heparin, varies under several hormonal conditions.	Heparin	79-86	lipase G, endothelial type	Rattus norvegicus	22-28
11939772-2	2002	Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin.	Heparin	258-265	serpin family C member 1	Homo sapiens	175-187
11939772-3	2002	Replacement of Lys125 with Met or Gln in this work reduced the affinity of antithrombin for full-length heparin or the pentasaccharide by 150-600-fold at I = 0.15, corresponding to a loss of 25-33% of the total binding energy.	Heparin	104-111	serpin family C member 1	Homo sapiens	75-87
11939772-4	2002	The affinity decrease was due both to disruption of approximately three ionic interactions, indicating that Lys125 and two other basic residues of antithrombin act cooperatively in binding to heparin, and to weakened nonionic interactions.	Heparin	192-199	serpin family C member 1	Homo sapiens	147-159
11939772-5	2002	The mutations caused a 10-17-fold decrease in the affinity of the initial, weak binding step of the two-step mechanism of heparin binding to antithrombin.	Heparin	122-129	serpin family C member 1	Homo sapiens	141-153
11939772-7	2002	Lys125 is thus a major heparin-binding residue of antithrombin, contributing an amount of binding energy comparable to that of Arg129, but less energy than Lys114.	Heparin	23-30	serpin family C member 1	Homo sapiens	50-62
11939772-8	2002	It is the first residue identified so far that has a critical role in the initial recognition of heparin by antithrombin, but also appreciably stabilizes the heparin-induced activated state of the inhibitor.	Heparin	97-104	serpin family C member 1	Homo sapiens	108-120
11939772-8	2002	It is the first residue identified so far that has a critical role in the initial recognition of heparin by antithrombin, but also appreciably stabilizes the heparin-induced activated state of the inhibitor.	Heparin	158-165	serpin family C member 1	Homo sapiens	108-120
12399441-4	2002	Pancreatic expression of EGF, TGF-alpha, heparin-binding EGF, betacellulin (BTC), and NRG-4 was detected as early as embryonic d 13 (E13).	Heparin	41-48	epidermal growth factor	Mus musculus	57-60
12357148-11	2002	The generation of fibrin even in the presence of high heparin concentrations most likely has to be attributed to the reduced antithrombin III concentrations or reduced inhibition of clot-bound thrombin.	Heparin	54-61	serpin family C member 1	Homo sapiens	125-141
6317700-4	1983	In addition, whereas the ability of PN-I to link to thrombin is strongly modulated by heparin, PN-II and PN-III are essentially unaffected by heparin.	Heparin	86-93	serpin family E member 2	Homo sapiens	36-40
12239166-8	2002	Heparin was also found to enhance IL-11"s ability to induce the expression of both receptor activator of nuclear factor-kappaB ligand (RANKL) and glycoprotein (gp) 130.	Heparin	0-7	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	83-133
12239166-8	2002	Heparin was also found to enhance IL-11"s ability to induce the expression of both receptor activator of nuclear factor-kappaB ligand (RANKL) and glycoprotein (gp) 130.	Heparin	0-7	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	135-140
11942921-7	2002	Polylysine also interacts with myosin filaments, causing enhancement of their size and the numbers, and this could be reversed by heparin.	Heparin	130-137	myosin heavy chain 14	Homo sapiens	31-37
6643466-11	1983	However, the tryptophan-ascribed fluorescence enhancement and absorption difference spectrum which occur when heparin binds to antithrombin III are reduced by 70%.	Heparin	110-117	serpin family C member 1	Homo sapiens	127-143
6631483-11	1983	Our studies suggest that the growth of nerve fibers on fibronectin substrates results from direct interaction with a specific portion of the fibronectin molecule and that this interaction can be inhibited by heparin and possibly other glycosaminoglycans.	Heparin	208-215	fibronectin 1	Gallus gallus	55-66
11919156-6	2002	We regenerated the binding sites for AT-III on completely desulfated N-resulfated heparin and revealed the critical modification enzymes.	Heparin	82-89	serpin family C member 1	Homo sapiens	37-43
12451678-3	2002	It is well-known that serum levels of lipoprotein lipase(LPL, EC 3.1.1.34) and hepatic triglyceride lipase(HTL, EC 3.1.1.3) show a significant increase after the administration of heparin in hemodialysis patients, and even larger quantities of heparin are administered before cardioangiography for ACS.	Heparin	180-187	lipoprotein lipase	Homo sapiens	57-60
12451678-3	2002	It is well-known that serum levels of lipoprotein lipase(LPL, EC 3.1.1.34) and hepatic triglyceride lipase(HTL, EC 3.1.1.3) show a significant increase after the administration of heparin in hemodialysis patients, and even larger quantities of heparin are administered before cardioangiography for ACS.	Heparin	244-251	lipoprotein lipase	Homo sapiens	57-60
12451678-4	2002	Moreover, inhibitors of LPL and HTL induce almost complete reduction of increased LIP activity in post-heparin serum as measured by enzymatic assays.	Heparin	103-110	lipoprotein lipase	Homo sapiens	24-27
12586136-0	2002	Tissue factor regulation and cytokine expression in monocyte-endothelial cell co-cultures: effects of a statin, an ACE-inhibitor and a low-molecular-weight heparin.	Heparin	156-163	coagulation factor III, tissue factor	Homo sapiens	0-13
12013428-0	2002	Heparin-induced diamine oxidase release into the circulation in pigs.	Heparin	0-7	amine oxidase copper containing 1	Sus scrofa	16-31
6631483-11	1983	Our studies suggest that the growth of nerve fibers on fibronectin substrates results from direct interaction with a specific portion of the fibronectin molecule and that this interaction can be inhibited by heparin and possibly other glycosaminoglycans.	Heparin	208-215	fibronectin 1	Gallus gallus	141-152
6651824-4	1983	These results confirm that the synthetic pentasaccharide with the above structure corresponds to the actual minimal sequence required in heparin for binding to AT-III.	Heparin	137-144	serpin family C member 1	Homo sapiens	160-166
11881992-1	2002	Conformational activation of antithrombin is a critical mechanism for the inhibition of factor Xa, a proteinase of the blood coagulation cascade, and is typically achieved with heparin, a polyanionic polysaccharide clinically used for anticoagulation.	Heparin	177-184	serpin family C member 1	Homo sapiens	29-41
12165435-5	2002	Monoclonal antibody E11 appeared to bind to the arginine-rich N-terminus of hLF, which is the binding site for heparin, bacterial lipopolysaccharide, human lysozyme, DNA and receptors.	Heparin	111-118	HLF transcription factor, PAR bZIP family member	Homo sapiens	76-79
6604220-7	1983	The independence of the new thrombin inhibitor from heparin control explains the bleeding disorder; it also indicates that heparin normally acts directly on antithrombin III, revealing its inherent inhibitory activity.	Heparin	123-130	serpin family C member 1	Homo sapiens	157-173
12077148-2	2002	We have investigated the structural requirements for heparin/heparan sulfate in binding and activation of FGF8 (splice variant b).	Heparin	53-60	fibroblast growth factor 8	Homo sapiens	106-110
12009874-2	2002	Although gC from HSV-1 (gC1) and from HSV-2 (gC2) bind to heparin, gC2 is believed to play a less significant role than gC1 in attachment of virus to cells.	Heparin	58-65	solute carrier family 25 member 22	Homo sapiens	24-27
11741963-1	2002	Antithrombin requires allosteric activation by heparin for efficient inhibition of its target protease, factor Xa.	Heparin	47-54	serpin family C member 1	Homo sapiens	0-12
6886628-3	1983	We have investigated this further by studying the effect of SAP upon clot times in both the absence and presence of heparin, a suggested ligand for SAP and itself a modulator of coagulation processes.	Heparin	116-123	amyloid P component, serum	Homo sapiens	148-151
11741963-2	2002	A pentasaccharide sequence found in heparin activates antithrombin by inducing conformational changes that affect the reactive center of the inhibitor resulting in optimal recognition by factor Xa.	Heparin	36-43	serpin family C member 1	Homo sapiens	54-66
12172461-2	2002	The drug replicates the sulphated antithrombin-binding pentasaccharide sequence in heparin and induces potent and specific antithrombin-mediated anti-Xa activity with excellent bioavailability and a long circulating half-life of 18 hours that makes it ideal for once-daily subcutaneous dosing.	Heparin	83-90	serpin family C member 1	Homo sapiens	34-46
6886628-8	1983	In the presence of heparin, substantial synergism was observed with maximal reductions of approximately 70% in FPA production requiring only 25-50 micrograms/ml SAP.	Heparin	19-26	amyloid P component, serum	Homo sapiens	161-164
11893776-3	2002	Mutant LPL proteins from post-heparin plasma from patients homozygous for missense mutations at amino acid positions 176, 188, 194, 205, and 207, and from COS cells transiently transfected with the corresponding cDNAs were quantified and characterized, in an attempt to determine which aspect of enzyme function was affected by each specific mutation.	Heparin	30-37	lipoprotein lipase	Homo sapiens	7-10
12230584-7	2002	To dissect the structure-function relationships of the LPL carboxyl-terminal domain, several residues predicted by the model structure to be essential for the functions of heparin binding and substrate recognition were mutagenized.	Heparin	172-179	lipoprotein lipase	Homo sapiens	55-58
6615439-0	1983	Properties of antithrombin-thrombin complex formed in the presence and in the absence of heparin.	Heparin	89-96	serpin family C member 1	Homo sapiens	14-26
13679666-15	2002	In patients who have hereditary antithrombin deficiency, antiphospholipid antibodies, a combined abnormality or a history of a severe thrombotic event (pulmonary embolism, extended deep vein thrombosis) should be advised to use prophylactic heparin during pregnancy, starting during the first trimester.	Heparin	241-248	serpin family C member 1	Homo sapiens	32-44
6615439-1	1983	Purification of antithrombin-thrombin complex by ion-exchange chromatography on DEAE-agarose resulted in predominantly monomeric complex, whereas purification on matrix-linked heparin produced large amounts of aggregated complex.	Heparin	176-183	serpin family C member 1	Homo sapiens	16-28
6615439-2	1983	Monomeric antithrombin-thrombin complexes formed in the presence and in the absence of heparin had similar conformations and heparin affinities.	Heparin	87-94	serpin family C member 1	Homo sapiens	10-22
6615439-2	1983	Monomeric antithrombin-thrombin complexes formed in the presence and in the absence of heparin had similar conformations and heparin affinities.	Heparin	125-132	serpin family C member 1	Homo sapiens	10-22
6636045-6	1983	On crossed immunoelectrophoresis (CIE) containing heparin in the first dimension agarose, patient"s AT-III showed no increase in electrophoretic mobility compared to that in the absence of heparin, suggesting that the patient"s AT-III has no affinity for heparin.	Heparin	50-57	serpin family C member 1	Homo sapiens	100-106
12211411-3	2002	Understanding the heparin structure led to the development of LMWHs, synthetic heparinomimetics, antithrombin and anti-Factor Xa agents.	Heparin	18-25	serpin family C member 1	Homo sapiens	97-109
6354782-9	1983	These findings suggest that some NIDD subjects have a defect in heparin releasable lipoprotein lipase activity, which is reversed with improved glycemic control.	Heparin	64-71	lipoprotein lipase	Homo sapiens	83-101
12062645-0	2002	Characterisation of Ag1, the major species-specific contaminant of bovine crude heparin, and its identification as an aprotinin/heparin complex.	Heparin	128-135	pancreatic trypsin inhibitor	Bos taurus	118-127
11956950-0	2002	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) regulates survival of midbrain dopaminergic neurons.	Heparin	0-7	heparin binding EGF like growth factor	Homo sapiens	60-66
6846326-2	1983	To date, much work has been done to elucidate the interaction of heparin with thrombin and its physiologic inhibitor, Antithrombin III (ATIII).	Heparin	65-72	serpin family C member 1	Homo sapiens	118-134
11956950-1	2002	Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is a member of the EGF-family of ligands signaling via the EGF-receptor tyrosine kinase.	Heparin	0-7	heparin binding EGF like growth factor	Homo sapiens	60-66
11866879-11	2002	CONCLUSION: Heparin and ADM appear to interact in a synergistic manner, which may be related to the over-expression of p53 and p21 mRNA and the elevated ratio of Bax/Bcl-2 mRNA.	Heparin	12-19	H3 histone pseudogene 16	Homo sapiens	127-130
12491369-2	2002	Heparin is widely used as an anticoagulant drug based on its ability to accelerate the rate at which antithrombin inhibits serine proteases in the blood coagulation cascade.	Heparin	0-7	serpin family C member 1	Homo sapiens	101-113
12062645-9	2002	Ag1 was then partly sequenced and identified as an aprotinin/heparin complex.	Heparin	61-68	pancreatic trypsin inhibitor	Bos taurus	51-60
12062645-10	2002	Aprotinin, also known as the bovine pancreatic trypsin inhibitor (BPTI), is present with heparin in mast cells, and is very resistant to heat, pH, chemical treatments and proteolytic digestion.	Heparin	89-96	pancreatic trypsin inhibitor	Bos taurus	0-9
12062645-10	2002	Aprotinin, also known as the bovine pancreatic trypsin inhibitor (BPTI), is present with heparin in mast cells, and is very resistant to heat, pH, chemical treatments and proteolytic digestion.	Heparin	89-96	pancreatic trypsin inhibitor	Bos taurus	29-64
12062645-10	2002	Aprotinin, also known as the bovine pancreatic trypsin inhibitor (BPTI), is present with heparin in mast cells, and is very resistant to heat, pH, chemical treatments and proteolytic digestion.	Heparin	89-96	pancreatic trypsin inhibitor	Bos taurus	66-70
12036876-9	2002	Pretreatment of monocytes with heparin or heparinase I resulted in partial inhibition of cell adhesion to Cyr61.	Heparin	31-38	cellular communication network factor 1	Homo sapiens	106-111
12036876-10	2002	However, monocytes, but not fibroblasts, were capable of adhering to a Cyr61 mutant deficient in heparin binding activity.	Heparin	97-104	cellular communication network factor 1	Homo sapiens	71-76
6846326-2	1983	To date, much work has been done to elucidate the interaction of heparin with thrombin and its physiologic inhibitor, Antithrombin III (ATIII).	Heparin	65-72	serpin family C member 1	Homo sapiens	136-141
12355033-6	2002	RESULTS: Platelet reactivity was greater in blood treated with UFH than in blood anticoagulated with bivalirudin with respect to both the capacity to bind fibrinogen (by 4 +/- 1.8%, p = 0.01) and P-selectin expression (by 7.7 +/- 0.7%, p, &lt; 0.0001) in response to 1 microM ADP.	Heparin	63-66	selectin P	Homo sapiens	196-206
11806943-0	2002	Hydration effects of heparin on antithrombin probed by osmotic stress.	Heparin	21-28	serpin family C member 1	Homo sapiens	32-44
11806943-2	2002	Heparin binding to antithrombin induces conformational transitions distal to the binding site.	Heparin	0-7	serpin family C member 1	Homo sapiens	19-31
6307613-9	1983	Heparin-releasable adipose tissue LPL activity was not influenced by a high-CHO diet.	Heparin	0-7	lipoprotein lipase	Homo sapiens	34-37
11857048-7	2002	Heparin-induced activities of LPL or HL or the response of serum total or LDL-C to the reduced fat diet did not differ between the groups.	Heparin	0-7	lipoprotein lipase	Homo sapiens	30-33
12355033-7	2002	Platelet reactivity was greater in blood treated with UFH than in blood exposed to enoxaparin with respect to P-selectin expression (by 7 +/- 1.1%, p, &lt; 0.0001) in response to 1 microM ADP.	Heparin	54-57	selectin P	Homo sapiens	110-120
11854268-2	2002	Antithrombin requires the co-factor, heparin, to efficiently inhibit target proteinases.	Heparin	37-44	serpin family C member 1	Homo sapiens	0-12
11854268-3	2002	A specific pentasaccharide sequence (H5) in high affinity heparin induces a conformational change in antithrombin that is particularly important for factor Xa (fXa) inhibition.	Heparin	58-65	serpin family C member 1	Homo sapiens	101-113
6862515-2	1983	Despite their differing morphology, all of these cell lines secrete lipoprotein lipase in response to heparin.	Heparin	102-109	lipase G, endothelial type	Rattus norvegicus	80-86
11811556-6	2002	OBIF was purified by successive three-step chromatography by heparin affinity, anion exchange, and reversed-phase columns.	Heparin	61-68	transmembrane protein 119	Mus musculus	0-4
6870832-0	1983	Electrostatic interactions in the heparin-enhanced reaction between human thrombin and antithrombin.	Heparin	34-41	serpin family C member 1	Homo sapiens	87-99
11953369-4	2002	However, the possibility existed that radioiodinated DT-HB-EGF complexes associate with cells due to the binding of the heparin-binding domain of recombinant HB-EGF to cell surface heparan sulfate proteoglycans.	Heparin	120-127	heparin binding EGF like growth factor	Homo sapiens	56-62
11953369-4	2002	However, the possibility existed that radioiodinated DT-HB-EGF complexes associate with cells due to the binding of the heparin-binding domain of recombinant HB-EGF to cell surface heparan sulfate proteoglycans.	Heparin	120-127	heparin binding EGF like growth factor	Homo sapiens	158-164
6870832-1	1983	Binding of heparin to thrombin is monitored by means of an aqueous two-phase partition system, and binding of heparin to antithrombin is monitored by means of heparin induced enhancement of the intrinsic fluorescence of the protein.	Heparin	110-117	serpin family C member 1	Homo sapiens	121-133
11953369-6	2002	A recombinant truncated HB-EGF (residues 106 to 149), which lacks most of the heparin-binding domain, showed an essentially heparin-independent binding of radioiodinated DT to cells.	Heparin	78-85	heparin binding EGF like growth factor	Homo sapiens	24-30
11953369-6	2002	A recombinant truncated HB-EGF (residues 106 to 149), which lacks most of the heparin-binding domain, showed an essentially heparin-independent binding of radioiodinated DT to cells.	Heparin	124-131	heparin binding EGF like growth factor	Homo sapiens	24-30
11833091-9	2002	After the preincubation with heparin, the Ca2+ increases were 62+/-23% and 23+/-19% induced by ACh and CCK, as for preincubation with procaine they were 72+/-28% and 85+/-37% induced by ACh and CCK, respectively.	Heparin	29-36	cholecystokinin	Oryctolagus cuniculus	103-106
11833091-9	2002	After the preincubation with heparin, the Ca2+ increases were 62+/-23% and 23+/-19% induced by ACh and CCK, as for preincubation with procaine they were 72+/-28% and 85+/-37% induced by ACh and CCK, respectively.	Heparin	29-36	cholecystokinin	Oryctolagus cuniculus	194-197
6870832-1	1983	Binding of heparin to thrombin is monitored by means of an aqueous two-phase partition system, and binding of heparin to antithrombin is monitored by means of heparin induced enhancement of the intrinsic fluorescence of the protein.	Heparin	110-117	serpin family C member 1	Homo sapiens	121-133
11711550-3	2002	Although heparin is routinely used in the treatment and prophylaxis of APS patients, the primary heparin-binding site within beta2-GPI has not been identified.	Heparin	97-104	apolipoprotein H	Homo sapiens	125-134
11711550-7	2002	Lys(284), Lys(286), and Lys(287) in this domain are essential for the interaction of beta2-GPI with heparin.	Heparin	100-107	apolipoprotein H	Homo sapiens	85-94
6870832-3	1983	Heparin is displaced from thrombin at lower concentrations of electrolyte than those necessary for its displacement from antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	121-133
11711550-8	2002	These data indicate that beta2-GPI binds to heparin in a relatively specific manner even though the affinity for the interaction is rather low.	Heparin	44-51	apolipoprotein H	Homo sapiens	25-34
6870832-5	1983	The kinetics of the reaction between thrombin and antithrombin in the presence of heparin were studied by using an assay where synthetic peptide substrate is present in the reaction mixture during the reaction between proteinase and inhibitor.	Heparin	82-89	serpin family C member 1	Homo sapiens	50-62
11711550-10	2002	Surprisingly, heparin at concentrations that can be achieved in vivo during anticoagulation therapy greatly enhances the plasmin-mediated cleavage of the Lys(317)-Thr(318) site in beta2-GPI.	Heparin	14-21	apolipoprotein H	Homo sapiens	180-189
11790126-1	2002	beta(2)-Glycoprotein I (beta(2)-GPI) is a plasma protein that binds to negatively charged substances such as DNA, heparin, and anionic phospholipids.	Heparin	114-121	apolipoprotein H	Homo sapiens	0-22
11790126-1	2002	beta(2)-Glycoprotein I (beta(2)-GPI) is a plasma protein that binds to negatively charged substances such as DNA, heparin, and anionic phospholipids.	Heparin	114-121	apolipoprotein H	Homo sapiens	24-35
12017388-2	2002	Its aetiology often recognizes a decrease in circulating antithrombin III (AT III) due to a preoperative heparin treatment.	Heparin	105-112	serpin family C member 1	Homo sapiens	57-73
12017388-2	2002	Its aetiology often recognizes a decrease in circulating antithrombin III (AT III) due to a preoperative heparin treatment.	Heparin	105-112	serpin family C member 1	Homo sapiens	75-81
12017388-8	2002	This subgroup significantly differs from the AT III-dependent heparin-resistant group being affected by a less severe degree of HR and including less patients pretreated with heparin.	Heparin	62-69	serpin family C member 1	Homo sapiens	45-51
12017388-8	2002	This subgroup significantly differs from the AT III-dependent heparin-resistant group being affected by a less severe degree of HR and including less patients pretreated with heparin.	Heparin	175-182	serpin family C member 1	Homo sapiens	45-51
12182916-0	2002	Separation of active and inactive forms of human antithrombin by heparin affinity chromatography.	Heparin	65-72	serpin family C member 1	Homo sapiens	49-61
11839780-7	2002	As we showed that the two N-terminal immunoglobulin modules of NCAM, which are known to bind to heparin, were responsible for this inhibition, we presume that this receptor is a heparan sulfate proteoglycan.	Heparin	96-103	neural cell adhesion molecule 1	Homo sapiens	63-67
6870832-7	1983	The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin.	Heparin	57-64	serpin family C member 1	Homo sapiens	68-80
6870832-7	1983	The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin.	Heparin	195-202	serpin family C member 1	Homo sapiens	68-80
11971193-2	2002	We show here that mutated diphtheria toxin, a specific inhibitor of heparin-binding epidermal growth factor-like growth factor (HB-EGF), blocked the IL-6-induced growth of two myeloma cell lines (XG-1 and XG-14) and did not significantly affect that of two other cell lines (XG-6 and XG-13).	Heparin	68-75	heparin binding EGF like growth factor	Homo sapiens	128-134
6870832-7	1983	The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin.	Heparin	195-202	serpin family C member 1	Homo sapiens	68-80
11971193-5	2002	They also overexpressed CD9, a tetraspanin that binds to the heparin-binding domain of HB-EGF and is critical for promoting ErbB1 activation by HB-EGF.	Heparin	61-68	heparin binding EGF like growth factor	Homo sapiens	87-93
6832015-0	1983	[Perioperative plasma antithrombin activity with "low-dose" heparin prophylaxis.	Heparin	60-67	serpin family C member 1	Homo sapiens	22-34
11707451-1	2002	Native antithrombin (AT) has an inactive reactive site loop conformation unless it is activated by a unique pentasaccharide fragment of heparin (H(5)).	Heparin	136-143	serpin family C member 1	Homo sapiens	7-19
6832015-2	1983	Antithrombin III activity was estimated using a chromogenic substrate perioperatively in the plasma of 200 patients undergoing major elective abdominal surgery during low-dose heparin prophylaxis.	Heparin	176-183	serpin family C member 1	Homo sapiens	0-16
11809775-4	2002	Previously, we showed that during fasting there is a shift in the distribution of lipase protein toward an inactive form with low heparin affinity.	Heparin	130-137	lipase G, endothelial type	Rattus norvegicus	82-88
6859531-3	1983	The methodologies were extended to investigations on the effects of heparin in the interaction between thrombin and antithrombin III.	Heparin	68-75	serpin family C member 1	Homo sapiens	116-132
11908641-3	2002	In addition, DNA, bacterial lipopolysaccharide, and heparin can displace CP from its complex with LF.	Heparin	52-59	ceruloplasmin	Homo sapiens	73-75
6571800-0	1983	Antithrombin III and anti-activated factor X activity in patients with acute promyelocytic leukemia and disseminated intravascular coagulation treated with heparin.	Heparin	156-163	serpin family C member 1	Homo sapiens	0-16
11867875-7	2002	Our standard anticoagulant is unfractionated heparin, where the primary mode of action is potentiation of endogenous AT-III.	Heparin	45-52	serpin family C member 1	Homo sapiens	117-123
11923090-5	2002	In comparison with the LPL of other animals, the deduced amino acid sequence shows a high degree of similarity with a conservation of functional domains, e.g. catalytic triad, N-glycosylation sites, lipid and heparin binding regions.	Heparin	209-216	lipoprotein lipase	Homo sapiens	23-26
11741012-3	2002	According to electron microscopy data, an elevation of free heparin in the substratum leads to a decrease of the N-CAM content and changing of its distribution on the membrane of cultured hippocampal neurons.	Heparin	60-67	neural cell adhesion molecule 1	Homo sapiens	113-118
11741012-6	2002	Heparin added to the substratum in a concentration of 40 microg/ml decreased the 2D N-CAM labelling density by 50% - 39.8 labels/microm(2) compared with the control values of 88.9 labels/microm(2).	Heparin	0-7	neural cell adhesion molecule 1	Homo sapiens	84-89
6845286-0	1983	Antithrombin III-binding capacity of heparin-sepharose as a function of activation temperature and duration.	Heparin	37-44	serpin family C member 1	Homo sapiens	0-16
11991242-7	2002	PAI-1 levels increased after the cultures had been supplemented with either Bemiparin or UFH at both doses.	Heparin	89-92	serpin family E member 1	Homo sapiens	0-5
11991242-9	2002	Both doses of UFH, but not Bemiparin, induced an important increase in TF secretion.	Heparin	14-17	coagulation factor III, tissue factor	Homo sapiens	71-73
11985057-2	2002	When measured in the presence of heparin, plasma antithrombin activity includes heparin cofactor II activity as about 20-30% of the total activity.	Heparin	33-40	serpin family C member 1	Homo sapiens	49-61
6822493-0	1983	Two-substrate reaction model for the heparin-catalyzed bovine antithrombin/protease reaction.	Heparin	37-44	serpin family C member 1	Homo sapiens	62-74
11805133-1	2002	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin.	Heparin	135-142	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
11805133-1	2002	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin rapidly in the presence of dermatan sulfate, heparan sulfate, or heparin.	Heparin	135-142	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
6822493-2	1983	In this model, heparin is the catalyst; while antithrombin is the first substrate and the protease is the second substrate.	Heparin	15-22	serpin family C member 1	Homo sapiens	46-58
11854515-1	2002	P-selectin facilitates human carcinoma metastasis in immunodeficient mice by mediating early interactions of platelets with bloodborne tumor cells via their cell surface mucins, and this process can be blocked by heparin [Borsig, L., Wong, R., Feramisco, J., Nadeau, D. R., Varki, N. M. &amp; Varki, A.	Heparin	213-220	selectin P	Homo sapiens	0-10
11831891-1	2002	Despite the lack of structural information on the heparin-binding (HB) epidermal growth factor (EGF) shedding putative target enzyme, the design of potent HB-EGF shedding inhibitors has been attempted by means of comparative molecular field analysis (CoMFA), a well-established 3D-QSAR technique.	Heparin	50-57	heparin binding EGF like growth factor	Homo sapiens	155-161
11895454-7	2002	RESULTS: Postprandial triglyceride excursions (evaluated by the incremental area under the curve during the metabolic meal profile) were inversely correlated to adipose tissue LPL mRNA levels (rho = -0.43, P &lt; 0.03) as well as to adipose tissue LPL heparin-releasable activity (rho = -0.58, P &lt; 0.01).	Heparin	252-259	lipoprotein lipase	Homo sapiens	176-179
11735695-1	2001	Hirudin is one of the new synthetic antithrombin agents, which is most commonly used in patients with type II heparin-induced thrombocytopenia and in patients with hypersensitivity reactions to unfractionated heparin as well as low-molecular-weight heparins.	Heparin	110-117	serpin family C member 1	Homo sapiens	36-48
11735695-1	2001	Hirudin is one of the new synthetic antithrombin agents, which is most commonly used in patients with type II heparin-induced thrombocytopenia and in patients with hypersensitivity reactions to unfractionated heparin as well as low-molecular-weight heparins.	Heparin	209-216	serpin family C member 1	Homo sapiens	36-48
6667245-11	1983	The antithrombotic effect of heparin therapy is determined by FPA as an immediate index and by Fbg, FDP, and AT III as a slow index.	Heparin	29-36	serpin family C member 1	Homo sapiens	109-115
11876557-4	2001	In the present study, glutaminase purified from human ovarian cancer ascites fluid was used in experimental solid and ascites mice model alone and in combination with Cu-Sulphate and heparin.	Heparin	183-190	glutaminase	Homo sapiens	22-33
11849388-9	2002	Both heparin and non-anti-coagulant heparin blocked the accumulation of pFN-FITC, indicating that the protective effect of heparin in the trapping of FN is independent of its anticoagulant properties, and probably results from preventing direct binding of FN in the sclerotic lesions.	Heparin	5-12	fibronectin 1	Mus musculus	73-75
11849388-9	2002	Both heparin and non-anti-coagulant heparin blocked the accumulation of pFN-FITC, indicating that the protective effect of heparin in the trapping of FN is independent of its anticoagulant properties, and probably results from preventing direct binding of FN in the sclerotic lesions.	Heparin	36-43	fibronectin 1	Mus musculus	73-75
6667252-2	1983	About 60% of these 21 patients were effectively treated with AT III concentrates by enhancing the effect of heparin and alleviating the burden of excessive plasma transfusions on the cardiovascular system.	Heparin	108-115	serpin family C member 1	Homo sapiens	61-67
11849388-9	2002	Both heparin and non-anti-coagulant heparin blocked the accumulation of pFN-FITC, indicating that the protective effect of heparin in the trapping of FN is independent of its anticoagulant properties, and probably results from preventing direct binding of FN in the sclerotic lesions.	Heparin	36-43	fibronectin 1	Mus musculus	73-75
11849388-13	2002	CONCLUSIONS: We hypothesize that the protective effect of heparin treatment may be the result of steric hindrance of the specific binding sites, that is, the I1-5 and/or III1 self-assembly sites of FN.	Heparin	58-65	nischarin	Mus musculus	158-162
11763451-0	2001	Synthesis of conformationally locked L-iduronic acid derivatives: direct evidence for a critical role of the skew-boat 2S0 conformer in the activation of antithrombin by heparin.	Heparin	170-177	serpin family C member 1	Homo sapiens	154-166
11763451-1	2001	We have used organic synthesis to understand the role of L-iduronic acid conformational flexibility in the activation of antithrombin by heparin.	Heparin	137-144	serpin family C member 1	Homo sapiens	121-133
11849389-11	2002	CPR levels in plasma were about threefold higher in rats treated with RHS-TM compared to those in rats treated with heparin.	Heparin	116-123	carboxypeptidase B2	Rattus norvegicus	0-3
6833877-3	1983	They appeared to have an inhibitor to lipoprotein lipase activity in their whole plasma that inhibited that activity eluted from adipose tissue with heparin and that activity present in postheparin plasma of normals.	Heparin	149-156	lipoprotein lipase	Homo sapiens	38-56
11763451-2	2001	Among known synthetic analogues of the genuine pentasaccharidic sequence representing the antithrombin binding site of heparin, we have selected as a reference compound the methylated anti-factor Xa pentasaccharide 1.	Heparin	119-126	serpin family C member 1	Homo sapiens	90-102
11763451-11	2001	These results clearly establish the critical importance of the 2S0 conformation of L-iduronic acid in the activation of antithrombin by heparin.	Heparin	136-143	serpin family C member 1	Homo sapiens	120-132
11714697-1	2002	It has been shown previously that the long chain fragments of heparin bind to the beta-strand cationic belt of the three-finger cobra cardiotoxin (or cytotoxin, CTX) and hence enhance its penetration into phospholipid monolayer under physiological ionic conditions.	Heparin	62-69	cytochrome P450 family 27 subfamily A member 1	Homo sapiens	161-164
6402859-0	1983	The antithrombin III content of cryoprecipitate prepared from blood collected with and without heparin.	Heparin	95-102	serpin family C member 1	Homo sapiens	4-20
11714697-2	2002	By taking lysophosphatidylcholine (LPC) micelles as a membrane model, we have shown by (1)H NMR study that the binding of heparin-derived hexasaccharide (Hep-6) to CTX at the beta-strand region can induce conformational changes of CTX near its membrane binding loops and promote the binding activity of CTX toward LPC.	Heparin	122-129	cytochrome P450 family 27 subfamily A member 1	Homo sapiens	164-167
11714697-2	2002	By taking lysophosphatidylcholine (LPC) micelles as a membrane model, we have shown by (1)H NMR study that the binding of heparin-derived hexasaccharide (Hep-6) to CTX at the beta-strand region can induce conformational changes of CTX near its membrane binding loops and promote the binding activity of CTX toward LPC.	Heparin	122-129	cytochrome P450 family 27 subfamily A member 1	Homo sapiens	231-234
11714697-2	2002	By taking lysophosphatidylcholine (LPC) micelles as a membrane model, we have shown by (1)H NMR study that the binding of heparin-derived hexasaccharide (Hep-6) to CTX at the beta-strand region can induce conformational changes of CTX near its membrane binding loops and promote the binding activity of CTX toward LPC.	Heparin	122-129	cytochrome P450 family 27 subfamily A member 1	Homo sapiens	231-234
11606753-3	2001	These signal end complexes were distinct from various precleavage RAG1/2 signal complexes in that they were resistant to treatment with heparin.	Heparin	136-143	recombination activating 1	Homo sapiens	66-70
6402859-6	1983	Using the fluorogenic assay, we also determined the effect of adding heparin to blood on the cryoprecipitation of AT III.	Heparin	69-76	serpin family C member 1	Homo sapiens	114-120
7142182-2	1982	The results have shown that the reaction is saturable with respect to both thrombin (KT = 3.6 x 10(-8) M) and antithrombin III (KAT = 1.0 x 10(-7) M) when the heparin concentration is low relative to the initial protein concentrations.	Heparin	159-166	serpin family C member 1	Homo sapiens	110-126
11704710-3	2001	However, low-molecular-weight heparins (LMWHs) have practical and clinical advantages over UFH and can be considered an effective alternative in the medical treatment of ACS and in patients proceeding to surgical interventions.	Heparin	30-38	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	170-173
11686222-9	2001	The missing matrix localization of LTBP-1D indicates that the hinge region containing a heparin-binding site is essential for the binding of LTBP-1 in the extracellular matrix.	Heparin	88-95	latent transforming growth factor beta binding protein 1	Homo sapiens	35-41
11597289-13	2001	In patients receiving antithrombin III and concomitant heparin, a significantly increased bleeding incidence was observed (23.8% for antithrombin III group vs 13.5% for placebo group; P&lt;.001).	Heparin	55-62	serpin family C member 1	Homo sapiens	133-149
11597289-15	2001	High-dose antithrombin III was associated with an increased risk of hemorrhage when administered with heparin.	Heparin	102-109	serpin family C member 1	Homo sapiens	10-26
11597998-1	2001	NK1 is a splice variant of the polypeptide growth factor HGF/SF, which consists of the N-terminal (N) and first kringle (K) domain and requires heparan sulfate or soluble heparin for activity.	Heparin	171-178	tachykinin receptor 1	Homo sapiens	0-3
11597998-2	2001	We describe two X-ray crystal structures of NK1-heparin complexes that define a heparin-binding site in the N domain, in which a major role is played by R73, with further contributions from main chain atoms of T61, K63 and G79 and the side chains of K60, T61, R76, K62 and K58.	Heparin	48-55	tachykinin receptor 1	Homo sapiens	44-47
11597998-2	2001	We describe two X-ray crystal structures of NK1-heparin complexes that define a heparin-binding site in the N domain, in which a major role is played by R73, with further contributions from main chain atoms of T61, K63 and G79 and the side chains of K60, T61, R76, K62 and K58.	Heparin	80-87	tachykinin receptor 1	Homo sapiens	44-47
11739083-1	2002	Insulin-like growth factor-binding protein (IGFBP)-3 contains a highly basic COOH-terminal heparin-binding region, the P3 region, which is thought to be important in the binding of IGFBP-3 to endothelial cells.	Heparin	91-98	insulin like growth factor binding protein 3	Homo sapiens	181-188
11817586-1	2002	OBJECTIVE: To examine the effects of a fibronectin (FN) fragment containing the COOH-terminal heparin-binding domain (HBFN-f) on chondrocyte-mediated type II collagen (CII) cleavage by collagenase and proteoglycan (PG) degradation in articular cartilage in explant culture.	Heparin	94-101	fibronectin 1	Bos taurus	52-54
11893078-6	2002	Removal of heparin chains from the various matrices by pretreatment of the ECM with heparinase resulted in reduction of glucose-6-phosphatase and DPP IV in adult hepatocytes.	Heparin	11-18	dipeptidyl peptidase 4	Homo sapiens	146-152
11597998-3	2001	Mutagenesis experiments demonstrate that heparin binding to this site is essential for dimerization in solution and biological activity of NK1.	Heparin	41-48	tachykinin receptor 1	Homo sapiens	139-142
7142182-6	1982	When the heparin-enhanced antithrombin III/thrombin reaction was studied under conditions where the heparin concentration was high relative to the initial protein concentrations the overall reaction was second order.	Heparin	9-16	serpin family C member 1	Homo sapiens	26-42
11597998-7	2001	We exploit the interaction between heparin and the K domain site in order to engineer NK1 as a potent receptor agonist and suggest that dual (positive and negative) control may be a general mechanism of heparan sulfate-dependent regulation of growth factor activity.	Heparin	35-42	tachykinin receptor 1	Homo sapiens	86-89
11862716-3	2002	The resulting mRNA codes for the short form of HB-EGF (SF HB-EGF), which retains the signal peptide, the propeptide, and the heparin-binding domain.	Heparin	125-132	heparin binding EGF like growth factor	Homo sapiens	47-53
11862716-3	2002	The resulting mRNA codes for the short form of HB-EGF (SF HB-EGF), which retains the signal peptide, the propeptide, and the heparin-binding domain.	Heparin	125-132	heparin binding EGF like growth factor	Homo sapiens	58-64
11862716-5	2002	Structural analysis suggested that SF HB-EGF is a secreted polypeptide that has high affinity for heparin, but weakly, if at all, interacts with EGFR.	Heparin	98-105	heparin binding EGF like growth factor	Homo sapiens	38-44
11668417-0	2001	Effects of sulfation on antithrombin-thrombin/factor Xa interactions in semisynthetic low molecular weight heparins.	Heparin	107-115	serpin family C member 1	Homo sapiens	24-36
6957257-0	1982	Antithrombin III and anti-activated factor X activity in patients with acute promyelocytic leukemia and disseminated intravascular coagulation treated with heparin.	Heparin	156-163	serpin family C member 1	Homo sapiens	0-16
11668417-2	2001	To gain insight into structure-activity relationships, we investigated quantitatively the interactions of a series of sulfated LMW heparins of similar molecular weights (derived from statistical desulfation of a supersulfated heparin) with the target enzymes human antithrombin (AT) and thrombin (T).	Heparin	131-138	serpin family C member 1	Homo sapiens	265-277
11686316-1	2001	We report 5 children from 3 families with homozygous antithrombin deficiency type II affecting the heparin binding site (99 Leu to Phe mutation).	Heparin	99-106	serpin family C member 1	Homo sapiens	53-65
12688145-6	2002	We means, that especially in cases with longer tourniquet time (more than 30 min) is better, when we give some type of Heparin (best is LMWH) as prevention of DVT, because in laboratory results we found significant increase of PAI-1.	Heparin	119-126	serpin family E member 1	Homo sapiens	227-232
7164033-3	1982	This latter inhibitory action of heparin occurs independently of antithrombin III.	Heparin	33-40	serpin family C member 1	Homo sapiens	65-81
11677228-1	2001	Measurement of water transfer during antithrombin activation by heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	37-49
7164033-4	1982	A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin.	Heparin	2-9	serpin family C member 1	Homo sapiens	40-56
11677228-3	2001	Heparin triggers conformational changes in, and the functional activation of, the serine proteinase inhibitor antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	110-122
11677228-7	2001	The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa.	Heparin	54-61	serpin family C member 1	Homo sapiens	41-53
11677228-7	2001	The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa.	Heparin	54-61	serpin family C member 1	Homo sapiens	173-185
11551226-8	2001	Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin.	Heparin	113-120	serpin family C member 1	Homo sapiens	56-72
11551226-8	2001	Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin.	Heparin	113-120	serpin family C member 1	Homo sapiens	74-79
11677228-7	2001	The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa.	Heparin	160-167	serpin family C member 1	Homo sapiens	41-53
11677228-7	2001	The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa.	Heparin	160-167	serpin family C member 1	Homo sapiens	173-185
11584015-1	2001	Cyr61 is a heparin-binding, extracellular matrix-associated protein of the CCN family, which also includes connective tissue growth factor, Nov, WISP-1, WISP-2, and WISP-3.	Heparin	11-18	cellular communication network factor 1	Homo sapiens	0-5
11584015-6	2001	Cyr61-mediated gene expression requires heparin binding activity of Cyr61, cellular de novo transcription, and protein synthesis and is largely dependent on the activation of p42/p44 MAPKs.	Heparin	40-47	cellular communication network factor 1	Homo sapiens	0-5
11584015-6	2001	Cyr61-mediated gene expression requires heparin binding activity of Cyr61, cellular de novo transcription, and protein synthesis and is largely dependent on the activation of p42/p44 MAPKs.	Heparin	40-47	cellular communication network factor 1	Homo sapiens	68-73
11521878-4	2001	Micellar electrokinetic chromatography was used to analytically separate these AT III variants, which differ in their affinity to the polysaccharide heparin.	Heparin	149-156	serpin family C member 1	Homo sapiens	79-85
11437366-2	2001	Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments.	Heparin	20-27	microtubule associated protein tau	Homo sapiens	38-41
7164033-4	1982	A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin.	Heparin	2-9	serpin family C member 1	Homo sapiens	122-138
11437366-2	2001	Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments.	Heparin	20-27	microtubule associated protein tau	Homo sapiens	76-79
11437366-2	2001	Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments.	Heparin	20-27	microtubule associated protein tau	Homo sapiens	76-79
7164033-4	1982	A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin.	Heparin	84-91	serpin family C member 1	Homo sapiens	40-56
11437366-2	2001	Previous studies on heparin-dependent tau polymerization, using recombinant tau isoforms lacking Cys-291, suggest that tau dimerization via Cys-322 is critical for initiation of assembly of soluble tau into filaments.	Heparin	20-27	microtubule associated protein tau	Homo sapiens	76-79
11755958-10	2001	Antithrombin inhibited protein C activation with an IC(50) value of 290+/-10 nmol/l, which was enhanced fourfold (IC(50) 60 nmol/l) by the addition of heparin 0.5 U/ml.	Heparin	151-158	serpin family C member 1	Homo sapiens	0-12
11755958-11	2001	Heparin alone, up to a concentration of 1 U/ml, had no effect on the activation of protein C. Small direct thrombin inhibitors thus inhibited both free and TM-bound thrombin and therefore also inhibited the activation of protein C. Whether this will influence their clinical efficacy or safety versus heparin and warfarin, which also inhibit protein activation, respectively, lowers the concentration of protein C, remains to be studied in clinical trials.	Heparin	0-7	thrombomodulin	Homo sapiens	156-158
11437366-3	2001	We report heparin-dependent in vitro polymerization of human recombinant tau (1-383 isoform), containing both Cys-291 and Cys-322, into paired helical filaments as characterized by electron microscopy.	Heparin	10-17	microtubule associated protein tau	Homo sapiens	73-76
7164033-5	1982	The low affinity heparin fraction and the unfractionated heparin had equivalent inhibitory effects on prothrombin activation in antithrombin III depleted plasma.	Heparin	17-24	serpin family C member 1	Homo sapiens	128-144
11437366-5	2001	To understand the molecular basis for heparin-induced tau polymerization, we expressed and purified C291A, C322A, and C291A/C322A tau mutants.	Heparin	38-45	microtubule associated protein tau	Homo sapiens	54-57
11437366-5	2001	To understand the molecular basis for heparin-induced tau polymerization, we expressed and purified C291A, C322A, and C291A/C322A tau mutants.	Heparin	38-45	microtubule associated protein tau	Homo sapiens	130-133
11755958-11	2001	Heparin alone, up to a concentration of 1 U/ml, had no effect on the activation of protein C. Small direct thrombin inhibitors thus inhibited both free and TM-bound thrombin and therefore also inhibited the activation of protein C. Whether this will influence their clinical efficacy or safety versus heparin and warfarin, which also inhibit protein activation, respectively, lowers the concentration of protein C, remains to be studied in clinical trials.	Heparin	301-308	thrombomodulin	Homo sapiens	156-158
7164033-5	1982	The low affinity heparin fraction and the unfractionated heparin had equivalent inhibitory effects on prothrombin activation in antithrombin III depleted plasma.	Heparin	57-64	serpin family C member 1	Homo sapiens	128-144
11390981-0	2001	Human tumor suppressor EXT gene family members EXTL1 and EXTL3 encode alpha 1,4- N-acetylglucosaminyltransferases that likely are involved in heparan sulfate/ heparin biosynthesis.	Heparin	159-166	exostosin like glycosyltransferase 3	Homo sapiens	57-62
7164033-9	1982	The antithrombin III independent effect of heparin is unlikely to be important therapeutically, however, if this property of heparin is shared by other naturally occurring glycosaminoglycans, it could be important in maintaining the fluidity of blood under physiological conditions.	Heparin	43-50	serpin family C member 1	Homo sapiens	4-20
11279105-9	2001	An exonuclease competition assay was designed using heparin as a nonsubstrate inhibitor with a series of partial duplex DNAs to delineate the substrate structure preferences for 3" nucleotide excision by Trex1 and TREX2.	Heparin	52-59	three prime repair exonuclease 2	Homo sapiens	214-219
11718706-4	2001	LPL mass in the pre-heparin plasma was measured by a sandwich enzyme immunoassay.	Heparin	20-27	lipoprotein lipase	Homo sapiens	0-3
7164033-9	1982	The antithrombin III independent effect of heparin is unlikely to be important therapeutically, however, if this property of heparin is shared by other naturally occurring glycosaminoglycans, it could be important in maintaining the fluidity of blood under physiological conditions.	Heparin	125-132	serpin family C member 1	Homo sapiens	4-20
11718706-6	2001	LPL mass in the pre-heparin plasma did not change significantly by this treatment during this period.	Heparin	20-27	lipoprotein lipase	Homo sapiens	0-3
7158775-0	1982	Preparation of three types of heparin-sepharose and their binding activities to thrombin and antithrombin III.	Heparin	30-37	serpin family C member 1	Homo sapiens	93-109
11304685-9	2001	In tumor xenografts and in tumor cells, we detected a pattern of specific FGF-BP-immunoreactive high molecular weight forms, which presumably represent stable covalent complexes of FGF-BP and show marked differences in their occurrence in different tumors and in their heparin binding affinity.	Heparin	269-276	fibroblast growth factor binding protein 1	Homo sapiens	74-80
11304685-9	2001	In tumor xenografts and in tumor cells, we detected a pattern of specific FGF-BP-immunoreactive high molecular weight forms, which presumably represent stable covalent complexes of FGF-BP and show marked differences in their occurrence in different tumors and in their heparin binding affinity.	Heparin	269-276	fibroblast growth factor binding protein 1	Homo sapiens	181-187
11322919-2	2001	Hirudin is a powerful, direct, and specific antithrombin agent that can be used in many therapeutic scenarios in which heparin is routinely used.	Heparin	119-126	serpin family C member 1	Homo sapiens	44-56
11787776-5	2001	Western blot analysis showed that levels of bcl-2, bax and c-myc were significantly overexpressed by treatment with the increase of heparin concentrations.	Heparin	132-139	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	59-64
11903489-1	2001	OBJECTIVE: To study the effect of fasting on lipoprotein lipase (LPL) activity in human post-heparin plasma, representing the functional pool of LPL.	Heparin	93-100	lipoprotein lipase	Homo sapiens	45-63
11903489-1	2001	OBJECTIVE: To study the effect of fasting on lipoprotein lipase (LPL) activity in human post-heparin plasma, representing the functional pool of LPL.	Heparin	93-100	lipoprotein lipase	Homo sapiens	65-68
11903489-6	2001	Post-heparin LPL activity increased from 79 +/- 6.4 mU mL-1 in the fed state to 112 +/- 10 mU mL-1 in the fasted state (P &lt; 0.01), while LPL mass was 361 +/- 29 in the fed state and 383 +/- 28 in the fasted state, respectively (P = 0.6).	Heparin	5-12	lipoprotein lipase	Homo sapiens	13-16
11903489-6	2001	Post-heparin LPL activity increased from 79 +/- 6.4 mU mL-1 in the fed state to 112 +/- 10 mU mL-1 in the fasted state (P &lt; 0.01), while LPL mass was 361 +/- 29 in the fed state and 383 +/- 28 in the fasted state, respectively (P = 0.6).	Heparin	5-12	L1 cell adhesion molecule	Mus musculus	55-59
11903489-6	2001	Post-heparin LPL activity increased from 79 +/- 6.4 mU mL-1 in the fed state to 112 +/- 10 mU mL-1 in the fasted state (P &lt; 0.01), while LPL mass was 361 +/- 29 in the fed state and 383 +/- 28 in the fasted state, respectively (P = 0.6).	Heparin	5-12	L1 cell adhesion molecule	Mus musculus	94-98
6812990-8	1982	Plasma from 14 of 16 patients with disseminated intravascular coagulopathy showed a decrease in AT III of from 17 to 51% of normal before and during heparin therapy.	Heparin	149-156	serpin family C member 1	Homo sapiens	96-102
11806438-5	2001	This acquired heparin resistance was attributed to an antithrombin (AT III) deficiency, and was treated with fresh frozen plasma (FFP) to restore adequate anticoagulation.	Heparin	14-21	serpin family C member 1	Homo sapiens	54-66
11806438-8	2001	Future treatment with AT III concentrate rather than FFP may reduce heparin requirements that will, in turn, reduce protamine reversal dose, postoperative bleeding attributable to heparin rebound, and its associated complications.	Heparin	68-75	serpin family C member 1	Homo sapiens	22-28
11806438-8	2001	Future treatment with AT III concentrate rather than FFP may reduce heparin requirements that will, in turn, reduce protamine reversal dose, postoperative bleeding attributable to heparin rebound, and its associated complications.	Heparin	180-187	serpin family C member 1	Homo sapiens	22-28
11344214-3	2001	The interaction of IGFBP-3 with FN and the 40-kDa heparin-binding carboxyl-terminal fragment of FN was confirmed using Western ligand blotting.	Heparin	50-57	insulin like growth factor binding protein 3	Homo sapiens	19-26
11344214-6	2001	Competitive inhibition of IGFBP-3 binding to FN was observed in the presence of IGFBP-5 and heparin.	Heparin	92-99	insulin like growth factor binding protein 3	Homo sapiens	26-33
11517600-4	2001	The expressed endostatin in P. pastoris was purified by heparin-sapherose affinity chromatography.	Heparin	56-63	collagen type XVIII alpha 1 chain	Homo sapiens	14-24
11800084-0	2001	Experimental study using heparin-immobilized adsorbent of EDA(+)fibronectin.	Heparin	25-32	fibronectin 1	Rattus norvegicus	64-75
6816616-1	1982	The lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle and from post-heparin plasma of sixty-five males with hypertriglyceridaemia and of seventy males with normal serum lipid levels.	Heparin	58-65	lipoprotein lipase	Homo sapiens	4-22
11567021-1	2001	Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin.	Heparin	138-145	serpin family C member 1	Homo sapiens	57-69
11322944-4	2001	By solid-phase assays, we showed that dermatan sulfate chains of decorin bind to the heparin-binding site included within the fibronectin-type III domains 10 and 11 of TN-X.	Heparin	85-92	tenascin XB	Homo sapiens	168-172
6816616-1	1982	The lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle and from post-heparin plasma of sixty-five males with hypertriglyceridaemia and of seventy males with normal serum lipid levels.	Heparin	58-65	lipoprotein lipase	Homo sapiens	24-27
11134031-0	2001	Hypersulfated low molecular weight heparin with reduced affinity for antithrombin acts as an anticoagulant by inhibiting intrinsic tenase and prothrombinase.	Heparin	35-42	serpin family C member 1	Homo sapiens	69-81
11567021-1	2001	Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin.	Heparin	138-145	serpin family C member 1	Homo sapiens	211-223
11567021-1	2001	Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin.	Heparin	275-282	serpin family C member 1	Homo sapiens	57-69
6816616-1	1982	The lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle and from post-heparin plasma of sixty-five males with hypertriglyceridaemia and of seventy males with normal serum lipid levels.	Heparin	126-133	lipoprotein lipase	Homo sapiens	24-27
11567021-1	2001	Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin.	Heparin	275-282	serpin family C member 1	Homo sapiens	211-223
11567021-2	2001	In the present work, substitution of Lys(114) by Ala or Met was shown to decrease the affinity of antithrombin for heparin and the pentasaccharide by approximately 10(5)-fold at I 0.15, corresponding to a reduction in binding energy of approximately 50%.	Heparin	115-122	serpin family C member 1	Homo sapiens	98-110
7157229-6	1982	The inactivation of thrombin or factor Xa by antithrombin is catalysed by the presence in the mixture of these insoluble materials as it is with soluble heparin.	Heparin	153-160	serpin family C member 1	Homo sapiens	45-57
11533057-0	2001	Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin.	Heparin	42-49	tryptase alpha/beta 1	Mus musculus	102-110
11533057-0	2001	Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin.	Heparin	42-49	tryptase alpha/beta 1	Mus musculus	160-168
11533057-0	2001	Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin.	Heparin	218-225	tryptase alpha/beta 1	Mus musculus	102-110
11533057-1	2001	Mast cell tryptase is stored as an active tetramer in complex with heparin in mast cell secretory granules.	Heparin	67-74	tryptase alpha/beta 1	Mus musculus	10-18
11533057-2	2001	Previously, we demonstrated the dependence on heparin for the activation/tetramer formation of a recombinant tryptase.	Heparin	46-53	tryptase alpha/beta 1	Mus musculus	109-117
11533057-4	2001	The ability of heparin-related saccharides to activate a recombinant murine tryptase, mouse mast cell protease-6 (mMCP-6), was strongly dependent on anionic charge density and size.	Heparin	15-22	tryptase alpha/beta 1	Mus musculus	76-84
11533057-5	2001	The dose-response curve for heparin-induced mMCP-6 activation displayed a bell-shaped appearance, indicating that heparin acts by binding to more than one tryptase monomer simultaneously.	Heparin	28-35	tryptase alpha/beta 1	Mus musculus	155-163
11533057-5	2001	The dose-response curve for heparin-induced mMCP-6 activation displayed a bell-shaped appearance, indicating that heparin acts by binding to more than one tryptase monomer simultaneously.	Heparin	114-121	tryptase alpha/beta 1	Mus musculus	155-163
11533057-10	2001	Our results suggest a model for tryptase tetramer formation that involves bridging of tryptase monomers by heparin or other highly sulfated polysaccharides of sufficient chain length.	Heparin	107-114	tryptase alpha/beta 1	Mus musculus	32-40
12577350-4	2001	In the heparin group, level of PT and APTT prolonged, FIB decreased, t-PA activity elevated and PAI activity lowered, and APC unchanged.	Heparin	7-14	serpin family E member 1	Homo sapiens	96-99
11113116-5	2001	The region we maintained corresponds to amino acids 80-265 of mature human PAI-1 containing binding sites for vitronectin, heparin (partial), uPA, tPA, fibrin, thrombin, and the helix F region.	Heparin	123-130	serpin family E member 1	Homo sapiens	75-80
11197503-1	2001	Heparin is a potent anticoagulant agent that interacts strongly with antithrombin III to prevent the formation of fibrin clot.	Heparin	0-7	serpin family C member 1	Homo sapiens	69-85
11174739-2	2001	However, heparins are associated with the risk of formation of heparin/platelet factor 4 antibodies (HPF4/A) and the development of heparin-associated thromboemboli.	Heparin	9-17	zinc finger protein 85	Homo sapiens	101-107
11174739-3	2001	We analyzed the occurrence of HPF4/A and thromboembolism in patients with heparin-coated and noncoated VADs.	Heparin	74-81	zinc finger protein 85	Homo sapiens	30-34
14728009-1	2001	Enoxaparin (enoxaparin sodium) is a low-molecular-weight heparin that binds to and increases the activity of antithrombin III.	Heparin	57-64	serpin family C member 1	Homo sapiens	109-125
7110603-2	1982	More specifically, it is shown that a change in these enzymatic systems could determine "functional kidnapping" of heparin or other substances (glicosaminoglycans) engaged in the activation of Antithrombin III, with noteworthy haemorrheological consequences mediated by a variety of mechanisms.	Heparin	115-122	serpin family C member 1	Homo sapiens	193-209
11133602-16	2001	In Group A patients with decreased AT activity, 18% demonstrated an inadequate ACT response-defined as ACT &lt;400 s-to the first bolus injection of heparin.	Heparin	149-156	serpin family C member 1	Homo sapiens	35-37
11685164-7	2001	The number of circulating P-selectin-positive platelets was increased by unfractionated heparin but not dalteparin, and abciximab reversed this increase.	Heparin	88-95	selectin P	Homo sapiens	26-36
11772296-9	2001	TFPI can be administered exogenously in high doses to suppress TF-mediated effects, alternatively high amounts of TFPI can be released from intravascular stores by other drugs, such as heparin and low molecular weight heparins (LMWH).	Heparin	218-226	coagulation factor III, tissue factor	Homo sapiens	0-2
11133602-19	2001	These results suggest that preoperative diminished AT activity causes reduced response to heparin in adult but not in infant patients.	Heparin	90-97	serpin family C member 1	Homo sapiens	51-53
7107605-7	1982	This enzyme has now been found to attack also the beta-glucuronidic linkage in the antithrombin-binding region of the heparin molecule.	Heparin	118-125	serpin family C member 1	Homo sapiens	83-95
11133602-21	2001	Measurement of preoperative AT activity identifies adult patients at risk of reduced sensitivity to heparin.	Heparin	100-107	serpin family C member 1	Homo sapiens	28-30
11133602-24	2001	In contrast, in patients older than one year of age and adult patients decreased preoperative AT activity is mainly caused by preoperative heparin therapy and causes insufficient response to heparin anticoagulation with a standard heparin dosage.	Heparin	139-146	serpin family C member 1	Homo sapiens	94-96
11133602-24	2001	In contrast, in patients older than one year of age and adult patients decreased preoperative AT activity is mainly caused by preoperative heparin therapy and causes insufficient response to heparin anticoagulation with a standard heparin dosage.	Heparin	191-198	serpin family C member 1	Homo sapiens	94-96
11133602-24	2001	In contrast, in patients older than one year of age and adult patients decreased preoperative AT activity is mainly caused by preoperative heparin therapy and causes insufficient response to heparin anticoagulation with a standard heparin dosage.	Heparin	191-198	serpin family C member 1	Homo sapiens	94-96
11597998-0	2001	Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.	Heparin	26-33	tachykinin receptor 1	Homo sapiens	22-25
11597998-0	2001	Crystal structures of NK1-heparin complexes reveal the basis for NK1 activity and enable engineering of potent agonists of the MET receptor.	Heparin	26-33	tachykinin receptor 1	Homo sapiens	65-68
11820460-1	2001	We analyzed the influence of heparins (unfractionated heparin, UFH and low molecular weight heparin certoparin) on the generation of IL-1ra, IL-6, IL-10, and IL-12p40 and from leukocyte fractions in vitro.	Heparin	29-37	interleukin 1 receptor antagonist	Homo sapiens	133-139
7135347-0	1982	On the reliability of the use of heparin immobilized on agarose for the study of the interactions among heparin, thrombin and antithrombin.	Heparin	33-40	serpin family C member 1	Homo sapiens	126-138
11820460-1	2001	We analyzed the influence of heparins (unfractionated heparin, UFH and low molecular weight heparin certoparin) on the generation of IL-1ra, IL-6, IL-10, and IL-12p40 and from leukocyte fractions in vitro.	Heparin	29-36	interleukin 1 receptor antagonist	Homo sapiens	133-139
11820460-1	2001	We analyzed the influence of heparins (unfractionated heparin, UFH and low molecular weight heparin certoparin) on the generation of IL-1ra, IL-6, IL-10, and IL-12p40 and from leukocyte fractions in vitro.	Heparin	54-61	interleukin 1 receptor antagonist	Homo sapiens	133-139
11163598-5	2001	Immunoblotting revealed that the predominant molecular species of VEGF concentrated with heparin-sepharose beads was VEGF(188).	Heparin	89-96	vascular endothelial growth factor A	Rattus norvegicus	66-70
11163598-5	2001	Immunoblotting revealed that the predominant molecular species of VEGF concentrated with heparin-sepharose beads was VEGF(188).	Heparin	89-96	vascular endothelial growth factor A	Rattus norvegicus	117-121
11936856-5	2001	Our results confirmed, in opposition to almost all early literature, that under very strict conditions of pH 6.0, calcium chloride concentration (2 mM), and very low ionic strength (25 mM), the first component of the human complement cascade recognize heparin fractions "enriched" in the high affinity sequence for the antithrombin III.	Heparin	252-259	serpin family C member 1	Homo sapiens	319-335
11190907-1	2001	A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism.	Heparin	110-117	serpin family C member 1	Homo sapiens	65-81
11190907-1	2001	A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism.	Heparin	110-117	serpin family C member 1	Homo sapiens	83-88
11461921-0	2001	Interactions of fibrillin-1 with heparin/heparan sulfate, implications for microfibrillar assembly.	Heparin	33-40	fibrillin 1	Homo sapiens	16-27
11461921-2	2001	Here we identify, characterize, and localize heparin/heparan sulfate-binding sites in fibrillin-1 and report on the role of such glycosaminoglycans in the assembly of fibrillin-1.	Heparin	45-52	fibrillin 1	Homo sapiens	86-97
11461921-2	2001	Here we identify, characterize, and localize heparin/heparan sulfate-binding sites in fibrillin-1 and report on the role of such glycosaminoglycans in the assembly of fibrillin-1.	Heparin	45-52	fibrillin 1	Homo sapiens	167-178
11461921-3	2001	By using different binding assays, we localize two calcium-independent heparin-binding sites to the N-terminal (Arg(45)-Thr(450)) and C-terminal (Asp(1528)-Arg(2731)) domains of fibrillin-1.	Heparin	71-78	fibrillin 1	Homo sapiens	178-189
11461921-6	2001	When heparin or heparan sulfate was added to cultures of skin fibroblasts, the assembly of fibrillin-1 into a microfibrillar network was significantly reduced.	Heparin	5-12	fibrillin 1	Homo sapiens	91-102
7135347-1	1982	The extent of inhibition of thrombin was re-examined as a consequence of the sequence of addition of thrombin and antithrombin III to a column of heparin immobilized on agarose.	Heparin	146-153	serpin family C member 1	Homo sapiens	114-130
11558632-1	2001	BACKGROUND: Previous studies demonstrated that heparin-binding epidermal growth factor-like growth factor (HB-EGF) contributes to carcinogenesis and carcinoma progression.	Heparin	47-54	heparin binding EGF like growth factor	Homo sapiens	107-113
6809059-1	1982	Ornithine decarboxylase (EC 4.1.1.17) was purified to near homogeneity from the livers of thioacetamide- and DL-alpha-hydrazino-delta aminovaleric acid-treated rats by using three types of affinity chromatography with pyridoxamine phosphate-Sepharose, pyridoxamine phosphate-dipropylenetriamine-Sepharose and heparin-Sepharose.	Heparin	309-316	ornithine decarboxylase 1	Rattus norvegicus	0-23
11853380-3	2001	The APTT was prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III.	Heparin	72-79	serpin family C member 1	Homo sapiens	83-99
11563913-0	2001	The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding.	Heparin	181-188	carboxyl ester lipase	Homo sapiens	45-72
11549250-6	2001	Data suggest that antithrombin regulates neutrophil migration via effects of its heparin-binding site on cell surface syndecan-4.	Heparin	81-88	serpin family C member 1	Homo sapiens	18-30
6179183-4	1982	However, pentosan polysulphate is at least as potent as heparin on a weight basis in producing activation of lipoprotein lipase, shortening of the euglobulin clot lysis time and impairing the generation of factor Xa.	Heparin	56-63	lipoprotein lipase	Homo sapiens	109-127
11509533-2	2001	Here, the association between the lipoprotein lipase (LPL) S447X polymorphism and changes in body mass index, fat mass, percent body fat, abdominal visceral fat measured by computed tomography, and post-heparin plasma LPL activity in response to 20 wk of endurance training was investigated in 741 adult white and black subjects.	Heparin	203-210	lipoprotein lipase	Homo sapiens	34-52
11509533-2	2001	Here, the association between the lipoprotein lipase (LPL) S447X polymorphism and changes in body mass index, fat mass, percent body fat, abdominal visceral fat measured by computed tomography, and post-heparin plasma LPL activity in response to 20 wk of endurance training was investigated in 741 adult white and black subjects.	Heparin	203-210	lipoprotein lipase	Homo sapiens	54-57
11509533-6	2001	These results suggest that the LPL S447X polymorphism influences the training-induced changes in body fat and post-heparin LPL activity in women but not in men.	Heparin	115-122	lipoprotein lipase	Homo sapiens	31-34
11509533-6	2001	These results suggest that the LPL S447X polymorphism influences the training-induced changes in body fat and post-heparin LPL activity in women but not in men.	Heparin	115-122	lipoprotein lipase	Homo sapiens	123-126
11164425-10	2000	However, the post-heparin LPL activity in the HTG patients increased from 153 to 192 U/l (P = 0.025).	Heparin	18-25	lipoprotein lipase	Homo sapiens	26-29
11099402-2	2000	The primary LPL deficiency was diagnosed on the basis of the findings that no LPL activity was detected in post-heparin plasma (PHP) and that the immunoreactive LPL mass in PHP was less than 2% of the control level.	Heparin	112-119	lipoprotein lipase	Homo sapiens	12-15
7112509-0	1982	Preparation of highly stable antithrombin-sepharose and utilization for the fractionation of heparin.	Heparin	93-100	serpin family C member 1	Homo sapiens	29-41
10973954-1	2000	The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor.	Heparin	63-70	serpin family E member 2	Homo sapiens	27-43
11493478-0	2001	Antibodies from patients with heparin-induced thrombocytopenia stimulate monocytic cells to express tissue factor and secrete interleukin-8.	Heparin	30-37	coagulation factor III, tissue factor	Homo sapiens	100-113
7071651-5	1982	We believe the antithrombin III level should be routinely determined for patients receiving heparin therapy.	Heparin	92-99	serpin family C member 1	Homo sapiens	15-31
11507154-10	2001	This activity was inhibited by heparin, an IP(3)R channel blocker, and by mutation of the Ca(2+)-binding sites in parvalbumin.	Heparin	31-38	parvalbumin S homeolog	Xenopus laevis	114-125
10973954-4	2000	Using a sensitive fluorescence-quenched peptide substrate, the K(assoc) of PN1 for FXIa was determined to be 7.9 x 10(4) m(-)(1) s(-)(1) in the absence of heparin.	Heparin	155-162	serpin family E member 2	Homo sapiens	75-78
10973954-5	2000	In the presence of heparin, this rate was accelerated to 1.7 x 10(6), M(-)(1) s(-)(1), making PN1 a far better inhibitor of FXIa than C1 inhibitor, which is the only other SERPIN known to significantly inhibit FXIa.	Heparin	19-26	serpin family E member 2	Homo sapiens	94-97
6977539-4	1982	As in the latter reaction, the formation of the modified antithrombin by Factor Xa was increased in the presence of heparin, while only small amounts were produced by Factor IXa both in the absence and presence of the polysaccharide.	Heparin	116-123	serpin family C member 1	Homo sapiens	57-69
11202230-4	2000	The complexes were dissociated by the SAP ligand heparin and were not demonstrable in EDTA plasma.	Heparin	49-56	amyloid P component, serum	Homo sapiens	38-41
7059522-10	1982	It is concluded that this new sulphated mucopolysaccharide acts as a pure antithrombin with a potency corresponding to 40--50 iu heparin/mg S-Lim.	Heparin	129-136	serpin family C member 1	Homo sapiens	74-86
11369259-2	2000	Binding of a full-length heparin chain to this site of factor Xa in the presence of calcium makes a significant contribution to acceleration of the proteinase inhibition by antithrombin through a ternary complex bridging or template mechanism.	Heparin	25-32	serpin family C member 1	Homo sapiens	173-185
11069186-8	2000	The structure of the FGF1-FGFR2-heparin ternary complex provides a structural basis for the essential role of heparan sulphate in FGF signalling.	Heparin	32-39	fibroblast growth factor receptor 2	Homo sapiens	26-31
11200935-6	2000	Lipoprotein lipase activity and mass in post-heparin plasma from those three subjects tended to increase after treatment with DDAVP, along with the complete disappearance of an unusual lipoprotein between low density lipoprotein (LDL) and very low density lipoprotein (VLDL) as analyzed by polyacrylamide gel electrophoresis.	Heparin	45-52	lipoprotein lipase	Homo sapiens	0-18
11522012-3	2001	Binding to the cell blocked acceleration of the thrombin:antithrombin interaction by heparin.	Heparin	85-92	serpin family C member 1	Homo sapiens	57-69
11429331-15	2001	Antithrombin effects may explain the inhibition of shear activation of platelets by both heparin and protamine.	Heparin	89-96	serpin family C member 1	Homo sapiens	0-12
11440189-4	2001	Unlike its influence on NO level, heparin diminished TNF-alpha production by PBMC and monocytes stimulated with LPS.	Heparin	34-41	tumor necrosis factor	Bos taurus	53-62
11018749-4	2000	AP-d/tPRP bound to virtually all cells and tissues to which it was exposed, consistent with our earlier evidence that d/tPRP binds to heparin-containing molecules.	Heparin	134-141	prolactin family 8, subfamily A, member 2	Rattus norvegicus	3-9
7064134-0	1982	Measurement of the heparin enhanced-antithrombin III/thrombin reaction rate in the presence of synthetic substrate.	Heparin	19-26	serpin family C member 1	Homo sapiens	36-52
11018749-4	2000	AP-d/tPRP bound to virtually all cells and tissues to which it was exposed, consistent with our earlier evidence that d/tPRP binds to heparin-containing molecules.	Heparin	134-141	prolactin family 8, subfamily A, member 2	Rattus norvegicus	118-124
11018749-5	2000	Moreover, we found that co-incubation with heparin or pretreatment with heparitinase greatly decreased the binding of AP-d/tPRP to tissue sections.	Heparin	43-50	prolactin family 8, subfamily A, member 2	Rattus norvegicus	121-127
11507678-4	2001	RESULTS: Pre-heparin plasma LPL mass correlated inversely against intra-abdominal visceral fat area (r = - 0.51, p &lt; 0.0001) and body mass index (r = - 0.46, p = 0.0003), but did not show any significant correlation with subcutaneous fat area.	Heparin	13-20	lipoprotein lipase	Homo sapiens	28-31
7309739-5	1981	Lipoprotein lipase binding to endothelial cells was inhibited 80% by preincubating cells in 0.1% trypsin for 3 min at 37 degrees C, 92% by 0.01% pronase, and 91% by 0.008% proteinase K. Heparin was most efficient in releasing lipoprotein lipase from endothelial cells.	Heparin	186-193	lipoprotein lipase	Homo sapiens	0-18
11382921-14	2001	Together, our data indicate that COP-1 may play a role in the antiproliferative mechanism of action of heparin.	Heparin	103-110	COP1, E3 ubiquitin ligase	Rattus norvegicus	33-38
10893232-1	2000	G domains of the mouse laminin alpha 1 and alpha 4 chains consisting of its five subdomains LG1-LG5 were overexpressed in Chinese hamster ovary cells and purified by heparin chromatography.	Heparin	166-173	laminin, alpha 1	Mus musculus	23-50
11382923-6	2001	Furthermore, heparan sulfate as well as heparin reduced smooth muscle cell adhesion when combined with fibronectin whereas neither hyaluronan nor chondroitin sulfate had any anti-adhesive effects.	Heparin	40-47	fibronectin 1	Rattus norvegicus	103-114
7337233-0	1981	Fractionation of heparin using antithrombin III reversibly bound to concanavalin A-sepharose.	Heparin	17-24	serpin family C member 1	Homo sapiens	31-47
11382923-8	2001	Cell adhesion to the 105- and 120 kDa cell-binding fragments of fibronectin, lacking the main heparin-binding domains, was also inhibited by heparin.	Heparin	94-101	fibronectin 1	Rattus norvegicus	64-75
11382923-8	2001	Cell adhesion to the 105- and 120 kDa cell-binding fragments of fibronectin, lacking the main heparin-binding domains, was also inhibited by heparin.	Heparin	141-148	fibronectin 1	Rattus norvegicus	64-75
11441134-6	2001	The mutant G154V LPL expressed in COS-1 cells was catalytically inactive and hardly released from the cells by heparin.	Heparin	111-118	lipoprotein lipase	Homo sapiens	17-20
11016326-0	2000	A randomized trial of antithrombin concentrate for treatment of heparin resistance.	Heparin	64-71	serpin family C member 1	Homo sapiens	22-34
11016326-6	2000	All patients who failed heparin therapy were successfully treated with AT.	Heparin	24-31	serpin family C member 1	Homo sapiens	71-73
6274149-1	1981	Under specified conditions purified C1q, activated C1r and C1s and C1r-C1s complexes were bound independently of Ca2+, to heparin-Sepharose, and could be eluted by an increasing salt gradient.	Heparin	122-129	complement C1q A chain	Homo sapiens	36-39
6800057-0	1981	Antithrombin III levels during heparin therapy.	Heparin	31-38	serpin family C member 1	Homo sapiens	0-16
10966821-1	2000	The mechanism of activation of antithrombin by heparin.	Heparin	47-54	serpin family C member 1	Homo sapiens	31-43
10816596-3	2000	Chinese hamster ovary cells (CHO677) deficient in heparan sulfate biosynthesis were employed to assess the function of heparin/heparan sulfate in FGF receptor-1 (FGFR-1) signal transduction and biological responses.	Heparin	119-126	fibroblast growth factor receptor 1	Cricetulus griseus	162-168
11410807-1	2001	Previous studies have demonstrated an elevated level of heparin-binding epidermal growth factor-like growth factor (HB-EGF) mRNA in hepatocarcinogenesis in a rodent model and of its protein as well as mRNA in human hepatocellular carcinoma (HCC).	Heparin	56-63	heparin binding EGF like growth factor	Homo sapiens	116-122
6978209-0	1981	The interference of fibrinogen and heparin with the determination of circulating immune complexes in the C1q-binding assay.	Heparin	35-42	complement C1q A chain	Homo sapiens	105-108
10902786-4	2000	A rapid and robust release of activin A and follistatin occurred in the circulation of patients undergoing abdominal aortic aneurysm repair or carotid endarterectomy at the time of vessel clamping and administration of heparin (5000 IU).	Heparin	219-226	inhibin subunit beta E	Homo sapiens	30-37
10902786-6	2000	However, administering heparin (2500 IU) to coronary angiography patients produced a similar activin and follistatin response, whereas placebo-treated angiography patients had no response.	Heparin	23-30	inhibin subunit beta E	Homo sapiens	93-100
10902786-7	2000	These findings illustrate that the routine use of heparin in surgical procedures elicits a rapid and robust release of activin and follistatin.	Heparin	50-57	inhibin subunit beta E	Homo sapiens	119-126
11401583-0	2001	Heparin antagonists are potent inhibitors of mast cell tryptase.	Heparin	0-7	tryptase alpha/beta 1	Mus musculus	55-63
6978209-4	1981	When heparin plasma was used to the assay, heparin itself also induced an increase in 125I-C1q binding that was not based on the presence of immune complexes.	Heparin	5-12	complement C1q A chain	Homo sapiens	91-94
11401583-3	2001	Tryptase is present in a macromolecular complex with heparin proteoglycan where the interaction with heparin is known to be essential for maintaining enzymatic activity.	Heparin	53-60	tryptase alpha/beta 1	Mus musculus	0-8
6978209-4	1981	When heparin plasma was used to the assay, heparin itself also induced an increase in 125I-C1q binding that was not based on the presence of immune complexes.	Heparin	43-50	complement C1q A chain	Homo sapiens	91-94
11401583-7	2001	We show that the heparin antagonists Polybrene and protamine are potent inhibitors of both human lung tryptase and of recombinant mouse tryptase (mouse mast cell protease 6).	Heparin	17-24	tryptase alpha/beta 1	Mus musculus	102-110
11401583-7	2001	We show that the heparin antagonists Polybrene and protamine are potent inhibitors of both human lung tryptase and of recombinant mouse tryptase (mouse mast cell protease 6).	Heparin	17-24	tryptase alpha/beta 1	Mus musculus	136-144
11380262-2	2001	Heparin has been proposed to conformationally activate the serpin, antithrombin, by making the reactive center loop P1 arginine residue accessible to proteinases.	Heparin	0-7	serpin family C member 1	Homo sapiens	67-79
11380262-3	2001	To evaluate this proposal, we determined the effect of mutating the P1 arginine on antithrombin"s specificity for target and nontarget proteinases in both native and heparin-activated states of the serpin.	Heparin	166-173	serpin family C member 1	Homo sapiens	83-95
10861096-7	2000	In the competition assays, heparin, but not other proteoglycans, could abolish the P-selectin recognition.	Heparin	27-34	selectin P	Homo sapiens	83-93
10867020-2	2000	We have previously described thrombin (Th)-protease nexin 1 (PN1) inhibitory complex binding to cell surface heparins and subsequent low density lipid receptor-related protein (LRP)-mediated internalization.	Heparin	109-117	serpin family E member 2	Homo sapiens	61-64
10867020-10	2000	By examining the pH dependence of complex binding in the range of 4.0-7.0, it was determined that the uPA.PN1 inhibitory complexes must specifically bind to endosomal heparins at pH 5.5 to be retained and sorted to lysosomes.	Heparin	167-175	serpin family E member 2	Homo sapiens	106-109
7272219-1	1981	The rate of elimination of injected antithrombin III (AT III) concentrate was investigated by measuring plasma AT III levels in two control subjects and four patients treated with continuous intravenous infusion of heparin.	Heparin	215-222	serpin family C member 1	Homo sapiens	36-52
10828477-10	2000	After heparin the patients released higher amounts of tissue factor pathway inhibitor antigen and activity compared with the control group; however, the difference was not statistically significant.	Heparin	6-13	coagulation factor III, tissue factor	Homo sapiens	54-67
11380262-11	2001	Consequently, determinants other than the P1 residue are responsible for enhancing the specificity of antithrombin for the two proteinases when activated by heparin.	Heparin	157-164	serpin family C member 1	Homo sapiens	102-114
11380263-1	2001	Activation of antithrombin by high-affinity heparin as an inhibitor of factor Xa has been ascribed to an allosteric switch between two conformations of the reactive center loop.	Heparin	44-51	serpin family C member 1	Homo sapiens	14-26
7272219-1	1981	The rate of elimination of injected antithrombin III (AT III) concentrate was investigated by measuring plasma AT III levels in two control subjects and four patients treated with continuous intravenous infusion of heparin.	Heparin	215-222	serpin family C member 1	Homo sapiens	54-60
10891598-1	2000	Using recombinant human tau protein phosphorylated by a brain extract and the glycogen synthase kinase-3beta in the absence or the presence of heparin, we showed that phosphorylation-dependent antibody AD2 recognition only requires phosphorylated Ser-396.	Heparin	143-150	microtubule associated protein tau	Homo sapiens	24-27
7272219-3	1981	Their half-time of AT III elimination was 8.4--13.6 h. The patient in whom AT III concentrate was injected at the start of heparin therapy showed a very rapid decrease of AT III activity with a three-fold increase in the elimination rate constant.	Heparin	123-130	serpin family C member 1	Homo sapiens	19-25
11412826-8	2001	The inhibitory effect was significantly higher when the post-heparin plasma was used from the patient or a subject with the same LPL mutation as an LPL source, compared to that from normal subjects.	Heparin	61-68	lipoprotein lipase	Homo sapiens	129-132
11412826-8	2001	The inhibitory effect was significantly higher when the post-heparin plasma was used from the patient or a subject with the same LPL mutation as an LPL source, compared to that from normal subjects.	Heparin	61-68	lipoprotein lipase	Homo sapiens	148-151
7272219-3	1981	Their half-time of AT III elimination was 8.4--13.6 h. The patient in whom AT III concentrate was injected at the start of heparin therapy showed a very rapid decrease of AT III activity with a three-fold increase in the elimination rate constant.	Heparin	123-130	serpin family C member 1	Homo sapiens	75-81
7261547-2	1981	Significant positive correlations were found between the lipoprotein lipase and hepatic lipase activities of post-heparin plasma samples and plasma high-density-lipoprotein (HDL) cholesterol concentrations in 21 children with hyperlipidaemia and six normal adult males.	Heparin	114-121	lipoprotein lipase	Homo sapiens	57-75
10824912-2	2000	Partial thrombotic obstruction of the pulmonary trunk secondary to Antithrombin III (homozygous defect of heparin binding site) deficiency was subsequently diagnosed.	Heparin	106-113	serpin family C member 1	Homo sapiens	67-83
7031837-3	1981	Lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle before and after insulin infusion.	Heparin	54-61	lipoprotein lipase	Homo sapiens	0-18
10772940-7	2000	The hLPL-transduced myoblasts increasingly overexpressed both heparin-releasable (HR) and intracellular (IN) LPL activity compared to nontransduced myoblasts (P &lt; 0.001 at Day 11) and myoblasts transduced with the control vector (P &lt; 0.001 at Day 11).	Heparin	62-69	lipoprotein lipase	Homo sapiens	4-8
10772940-7	2000	The hLPL-transduced myoblasts increasingly overexpressed both heparin-releasable (HR) and intracellular (IN) LPL activity compared to nontransduced myoblasts (P &lt; 0.001 at Day 11) and myoblasts transduced with the control vector (P &lt; 0.001 at Day 11).	Heparin	62-69	lipoprotein lipase	Homo sapiens	5-8
11357059-0	2001	The carboxy-terminal domain of IGF-binding protein-5 inhibits heparin binding to a site in the central domain.	Heparin	62-69	insulin-like growth factor binding protein 5	Rattus norvegicus	31-52
11357059-1	2001	The IGF-binding protein (IGFBP)-5 protein contains consensus heparin binding motifs in both its carboxy (C)-terminal and central domains, although only the C-terminal site has previously been shown to be functional.	Heparin	61-68	insulin-like growth factor binding protein 5	Rattus norvegicus	4-33
11357059-6	2001	These results demonstrate that the active heparin binding site in BP552 and BP550 is contained within the central domain of IGFBP-5, and that this site is active only in the absence of the C-terminal domain.	Heparin	42-49	insulin-like growth factor binding protein 5	Rattus norvegicus	124-131
11278641-0	2001	Identification and characterization of a conformational heparin-binding site involving two fibronectin type III modules of bovine tenascin-X.	Heparin	56-63	fibronectin 1	Bos taurus	91-102
11278641-3	2001	On the other hand, the two contiguous fibronectin type III repeats b10 and b11 have a predicted positive charge at physiological pH, hence a set of recombinant proteins comprising these domains was tested for interaction with heparin.	Heparin	226-233	fibronectin 1	Bos taurus	38-49
7031837-3	1981	Lipoprotein lipase (LPL) activity was determined from heparin eluates of adipose tissue and skeletal muscle before and after insulin infusion.	Heparin	54-61	lipoprotein lipase	Homo sapiens	20-23
11290592-3	2001	There are conflicting results as to whether anticoagulant heparins can catalyze the antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged membrane surfaces, and calcium ion), which is the physiologically relevant form of the proteinase responsible for the activation of prothrombin to thrombin during the blood coagulation process.	Heparin	58-66	serpin family C member 1	Homo sapiens	84-96
11290592-4	2001	In this study, a novel assay system was developed to compare the catalytic effect of different molecular-weight heparins in the antithrombin inhibition of factor Xa, either in free form or assembled into the prothrombinase complex during the process of prothrombin activation.	Heparin	112-120	serpin family C member 1	Homo sapiens	128-140
11290592-5	2001	This assay takes advantage of the unique property of a recombinant mutant antithrombin, which, similar to the wild-type antithrombin, rapidly inhibits factor Xa, but not thrombin, in the presence of heparin.	Heparin	199-206	serpin family C member 1	Homo sapiens	74-86
11290592-5	2001	This assay takes advantage of the unique property of a recombinant mutant antithrombin, which, similar to the wild-type antithrombin, rapidly inhibits factor Xa, but not thrombin, in the presence of heparin.	Heparin	199-206	serpin family C member 1	Homo sapiens	120-132
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	selectin P	Homo sapiens	23-33
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	serpin family C member 1	Homo sapiens	118-130
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	selectin P	Homo sapiens	219-229
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	167-170	selectin E	Homo sapiens	234-244
10760480-6	2000	These PGs were mainly composed of chondroitin sulfate type and exerted a heparin-like effect on LPL release.	Heparin	73-80	lipoprotein lipase	Homo sapiens	96-99
10931744-4	2000	The addition of a range of concentrations of heparin, induced IGFBP-3 protease activity in NS.	Heparin	45-52	insulin like growth factor binding protein 3	Homo sapiens	62-69
10722716-1	2000	Antithrombin requires heparin for efficient inhibition of the final two proteinases of the blood coagulation cascade, factor Xa and thrombin.	Heparin	22-29	serpin family C member 1	Homo sapiens	0-12
10722716-2	2000	Antithrombin binds heparin via a specific pentasaccharide domain in a two-step mechanism whereby initial weak binding is followed by a conformational change and subsequent tight binding.	Heparin	19-26	serpin family C member 1	Homo sapiens	0-12
6166063-5	1981	Conversely, previous plasma alpha 2 M depletion by immunoabsorption increases the consumption of heparin-cofactor activity by exogenous thrombi.	Heparin	97-104	alpha-2-macroglobulin	Homo sapiens	28-37
10759005-8	2000	The thrombin-based assays also overestimated antithrombin activity in patients under high-dose heparin.	Heparin	95-102	serpin family C member 1	Homo sapiens	45-57
11380605-5	2001	The FC method detects activated platelets induced by heparin-immune complexes using the highly sensitive recombinant probe annexin V and pooled platelets from multiple donors.	Heparin	53-60	annexin A5	Homo sapiens	123-132
11599124-10	2001	These results indicate that heparin and HS inhibited ET-1-induced ERK activation, resulting in suppression of Elk-1 phosphorylation, and lead to inhibition of c-fos gene expression through SRF-independent manner.	Heparin	28-35	serum response factor	Rattus norvegicus	189-192
7471127-0	1981	The antithrombin-binding sequence of heparin studied by n.m.r.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
11336704-6	2001	Furthermore, endostatin selected a specific octasulfated hexasaccharide from a sequence in heparin.	Heparin	91-98	collagen type XVIII alpha 1 chain	Homo sapiens	13-23
10698186-6	2000	In contrast, both heparin and heparan sulfate significantly inhibited the OPN-IGFBP-5 interaction and chondroitin sulfate A, B, and C had no effect.	Heparin	18-25	secreted phosphoprotein 1	Homo sapiens	74-77
11281717-4	2001	The recombinant lactoferrin N-lobe was secreted into the culture medium and partially purified by means of an immobilized heparin column.	Heparin	122-129	lactotransferrin	Bos taurus	16-27
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Heparin	54-61	serpin family C member 1	Homo sapiens	81-87
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	91-98	serpin family C member 1	Homo sapiens	146-158
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	218-225	serpin family C member 1	Homo sapiens	146-158
11238089-6	2001	Initially it was hypothesized that the cause of the disease in this family could be an antithrombin III (AT3) mutation that resulted in a constitutively active AT3 in the absence of heparin binding.	Heparin	182-189	serpin family C member 1	Homo sapiens	87-103
7012055-2	1981	The enzymatic activity of LPL release from fat tissue by heparin rose significantly one hour after glucose in the normal subjects.	Heparin	57-64	lipoprotein lipase	Homo sapiens	26-29
11238089-6	2001	Initially it was hypothesized that the cause of the disease in this family could be an antithrombin III (AT3) mutation that resulted in a constitutively active AT3 in the absence of heparin binding.	Heparin	182-189	serpin family C member 1	Homo sapiens	105-108
10688509-9	2000	Pregnancy loss rate was 70% in pregnancies treated with warfarin, compared with 25% for those switched from warfarin to heparin (RR 2 x 81, 95% CI 1 x 03-7 x 73).	Heparin	120-127	ribonucleotide reductase regulatory subunit M2	Homo sapiens	129-133
10735636-1	2000	We analyzed the molecular defect in the lipoprotein lipase (LPL) gene of a young boy from Sardinia who had primary hyperchylomicronemia, pancreatitis, and a complete LPL deficiency in post-heparin plasma.	Heparin	189-196	lipoprotein lipase	Homo sapiens	40-58
6157479-3	1980	In several ways PN resembles antithrombin III (AT3), a prominent inhibitor of thrombin in serum: PN links thrombin, probably via an ester bond; PN does not link thrombin blocked at its catalytic site serine; PN has a high-affinity heparin-binding site; and heparin greatly accelerates the rate of linkage between soluble PN and thrombin.	Heparin	231-238	serpin family C member 1	Homo sapiens	47-50
10735636-1	2000	We analyzed the molecular defect in the lipoprotein lipase (LPL) gene of a young boy from Sardinia who had primary hyperchylomicronemia, pancreatitis, and a complete LPL deficiency in post-heparin plasma.	Heparin	189-196	lipoprotein lipase	Homo sapiens	60-63
10646636-4	2000	After Ad-LPL administration, active, heparin-releasable huLPL was readily detected along with a 10-fold reduction in plasma TGs, disappearance of plasma TG-rich lipoproteins up to day 14, and enhanced clearance of an excess intravenous fat load on day 9.	Heparin	37-44	lipoprotein lipase	Homo sapiens	9-12
10793628-7	2000	The presence of heparin reduced the uptake of cholesteryl ester from apolipoprotein E vesicles but not with apolipoprotein A-I vesicles, indicating that uptake of apolipoprotein A-I vesicles via a secretion of apolipoprotein E by the cells themselves was not involved.	Heparin	16-23	apolipoprotein A1	Rattus norvegicus	163-181
10600606-2	1999	In its native state, gp120(LAI) is able to elicit specific multimolecular complexes with these membrane ligands at the surface of the cells; most of the interactions are abolished by mannan or heparin but not by dextran.	Heparin	193-200	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	21-26
10613650-15	1999	Rabbit polyclonal antiserum against the basic peptide partially inhibited LPL activity of human post heparin plasma, measured by radioenzymatic assay using triolein substrate.	Heparin	101-108	lipoprotein lipase	Homo sapiens	74-77
10555961-8	1999	A heparin disaccharide analogue, sucrose octasulfate, binds with similar affinity to the N domain and to a naturally occurring HGF isoform, NK1, at nearly the same region as in heparin binding.	Heparin	2-9	tachykinin receptor 1	Homo sapiens	140-143
11231699-2	2001	Important new antiplatelet drugs (glycoprotein IIb-IIIa inhibitors) and antithrombin agents (low-molecular-weight heparin) are currently recommended for patients with unstable angina pectoris/non-ST-segment elevation MI who are at high or intermediate risk on the basis of symptoms, electrocardiographic findings, and the presence or absence of serum markers (eg, troponin I, troponin T, and creatine kinase-MB).	Heparin	114-121	serpin family C member 1	Homo sapiens	72-84
11159540-7	2001	Analyses revealed that the AT III heparin-binding site interacts with neutrophil membrane-associated heparan sulfate proteoglycan receptors.	Heparin	34-41	serpin family C member 1	Homo sapiens	27-33
11035040-0	2001	Altered processing of fibronectin in mice lacking heparin.	Heparin	50-57	fibronectin 1	Mus musculus	22-33
11035040-10	2001	Further experiments showed that the degradation of fibronectin observed in cell cultures from NDST-2(+/+) mice was catalyzed by mast cell chymase in a strongly heparin-dependent manner.	Heparin	160-167	fibronectin 1	Mus musculus	51-62
11133602-0	2001	Low preoperative antithrombin activity causes reduced response to heparin in adult but not in infant cardiac-surgical patients.	Heparin	66-73	serpin family C member 1	Homo sapiens	17-29
11133602-1	2001	UNLABELLED: We evaluated the interaction of preoperative antithrombin (AT) activity and intraoperative response to heparin in cardiac surgery.	Heparin	115-122	serpin family C member 1	Homo sapiens	57-69
11133602-1	2001	UNLABELLED: We evaluated the interaction of preoperative antithrombin (AT) activity and intraoperative response to heparin in cardiac surgery.	Heparin	115-122	serpin family C member 1	Homo sapiens	71-73
11133602-3	2001	Heparin itself has no anticoagulant properties, however it causes a conformational change of the physiologic plasma inhibitor AT that converts this slow-acting serine protease inhibitor into a fast acting one.	Heparin	0-7	serpin family C member 1	Homo sapiens	126-128
11133602-4	2001	Thus, adequate AT activity is a prerequisite for sufficient heparin anticoagulation.	Heparin	60-67	serpin family C member 1	Homo sapiens	15-17
11133602-5	2001	AT activity is reduced by long-term heparin therapy.	Heparin	36-43	serpin family C member 1	Homo sapiens	0-2
10555961-11	1999	On the basis of the NK1 crystal structure, we propose a model in which heparin binds to the two primary binding sites and the N-terminal regions of the N domains and stabilizes an NK1 dimer.	Heparin	71-78	tachykinin receptor 1	Homo sapiens	20-23
10555961-11	1999	On the basis of the NK1 crystal structure, we propose a model in which heparin binds to the two primary binding sites and the N-terminal regions of the N domains and stabilizes an NK1 dimer.	Heparin	71-78	tachykinin receptor 1	Homo sapiens	180-183
11133602-13	2001	In adult patients, preoperative AT activity depended predominantly on preoperative heparin treatment: 62% of the patients with an AT activity &lt;80% were pretreated with heparin.	Heparin	83-90	serpin family C member 1	Homo sapiens	32-34
6157479-3	1980	In several ways PN resembles antithrombin III (AT3), a prominent inhibitor of thrombin in serum: PN links thrombin, probably via an ester bond; PN does not link thrombin blocked at its catalytic site serine; PN has a high-affinity heparin-binding site; and heparin greatly accelerates the rate of linkage between soluble PN and thrombin.	Heparin	257-264	serpin family C member 1	Homo sapiens	47-50
11133602-13	2001	In adult patients, preoperative AT activity depended predominantly on preoperative heparin treatment: 62% of the patients with an AT activity &lt;80% were pretreated with heparin.	Heparin	171-178	serpin family C member 1	Homo sapiens	32-34
10545182-4	1999	Heparin and VN accelerated the second-order association rate constant [k(2) = (7.9 +/- 0.5) x 10(2) M(-)(1) s(-)(1)] of alpha-thrombin with PAI-1 approximately 200- and approximately 240-fold, respectively.	Heparin	0-7	serpin family E member 1	Homo sapiens	140-145
7417461-1	1980	The binding of a heparin-releasable acylglycerol hydrolase from rat liver (liver lipase) to non-parenchymal liver cells was studied in vitro.	Heparin	17-24	lipase G, endothelial type	Rattus norvegicus	81-87
10844403-0	1999	Comparative inhibition of LPS-activated human monocyte-induced thrombin generation by unfractionated heparin and low molecular weight heparins.	Heparin	101-108	interferon regulatory factor 6	Homo sapiens	26-29
10844403-0	1999	Comparative inhibition of LPS-activated human monocyte-induced thrombin generation by unfractionated heparin and low molecular weight heparins.	Heparin	134-142	interferon regulatory factor 6	Homo sapiens	26-29
10844403-9	1999	Our results show that unfractionated and low molecular weight heparins potently inhibit monocytic tissue factor induced thrombin generation.	Heparin	62-70	coagulation factor III, tissue factor	Homo sapiens	98-111
11777389-6	2001	The adsorptivity and its stability in buffer solution, complexation compatibility with antithrombin III (ATIII), were enhanced with larger alkyl-group-derivatized heparins.	Heparin	163-171	serpin family C member 1	Homo sapiens	87-103
7377145-0	1980	Heparin anticoagulation during cardiopulmonary bypass in an antithrombin-III deficient patient.	Heparin	0-7	serpin family C member 1	Homo sapiens	60-76
11777389-6	2001	The adsorptivity and its stability in buffer solution, complexation compatibility with antithrombin III (ATIII), were enhanced with larger alkyl-group-derivatized heparins.	Heparin	163-171	serpin family C member 1	Homo sapiens	105-110
10502303-4	1999	pp52(S6K) was inhibited by fluoride (IC(50) approximately 60 mM), but was relatively insensitive to beta-glycerolphosphate, EGTA, dithiothreitol, spermine, heparin, NaCl, and metal ions such as Mn(2+), Zn(2+), and Ca(2+).	Heparin	156-163	ribosomal protein S6 kinase B1	Homo sapiens	5-8
10545520-5	1999	Immobilized heparin, a mimic for extracellular matrix-associated proteoglycans, binds physiological concentrations of TFPI-1 in a conformation that supports TF-VIIa-dependent cell adhesion.	Heparin	12-19	coagulation factor III, tissue factor	Homo sapiens	118-120
7377145-2	1980	A case of antithrombin-III (AT-III) deficiency was diagnosed on the basis of a diminished anticoagulant effect following the administration of heparin for cardiopulmonary bypass.	Heparin	143-150	serpin family C member 1	Homo sapiens	10-26
6444419-8	1980	The isolated proteoglycan was indistinguishable from commercial heparin when analyzed in terms of its ability to act as a cofactor in the antithrombin III inhibition of thrombin.	Heparin	64-71	serpin family C member 1	Homo sapiens	138-154
10585151-6	1999	Heparin resistance was defined as at least one activated clotting time &lt; 400 s after heparinization and/or the need for purified antithrombin III (AT-III) administration.	Heparin	0-7	serpin family C member 1	Homo sapiens	132-148
10585151-6	1999	Heparin resistance was defined as at least one activated clotting time &lt; 400 s after heparinization and/or the need for purified antithrombin III (AT-III) administration.	Heparin	0-7	serpin family C member 1	Homo sapiens	150-156
10531349-4	1999	The addition of heparin promoted a marked blue shift in the fluorescence emission spectrum of GM-CSF as well as a 30-fold increase in the intensity of light scattering, which indicates formation of large molecular weight complexes between the two molecules.	Heparin	16-23	colony stimulating factor 2	Homo sapiens	94-100
10531349-5	1999	Interestingly, heparin-induced changes in the spectral properties of GM-CSF were only observed at acidic pH.	Heparin	15-22	colony stimulating factor 2	Homo sapiens	69-75
10912118-5	1999	Repeated administration of heparin for anticoagulation during hemodialysis apparently leads to an LPL depletion in the endothelium.	Heparin	27-34	lipoprotein lipase	Homo sapiens	98-101
11824259-3	2001	Administration of AT III in septic patients (KYBERSEPT) reduced the mortality rate solely in patients which were not treated with heparin.	Heparin	130-137	serpin family C member 1	Homo sapiens	18-24
11208491-0	2001	Heparin-induced modulation of insulin like-growth factor-I action on glucose level in control and fasted rats.	Heparin	0-7	insulin-like growth factor 1	Rattus norvegicus	30-58
11208491-4	2001	Since: a) IGF-I plays an important role in glucose counter regulation; b) heparin was shown to alter IGF-I affinity to BPs; and c) fasting is known to change quantity and quality of serum BPs, we decided to measure the in vivo effect of heparin on blood IGF-I, BPs and glucose levels in control and fasted rats.	Heparin	74-81	insulin-like growth factor 1	Rattus norvegicus	101-106
11208491-4	2001	Since: a) IGF-I plays an important role in glucose counter regulation; b) heparin was shown to alter IGF-I affinity to BPs; and c) fasting is known to change quantity and quality of serum BPs, we decided to measure the in vivo effect of heparin on blood IGF-I, BPs and glucose levels in control and fasted rats.	Heparin	74-81	insulin-like growth factor 1	Rattus norvegicus	101-106
11208491-9	2001	The evidence was provided that heparin dissociates IGF-I from HMWBPs complex of control rat serum (predominant one in serum of these animals) and released IGF-I in turn is bound to LMWBPs--known as inhibitors of IGF-I dependent functions.	Heparin	31-38	insulin-like growth factor 1	Rattus norvegicus	51-56
11208491-9	2001	The evidence was provided that heparin dissociates IGF-I from HMWBPs complex of control rat serum (predominant one in serum of these animals) and released IGF-I in turn is bound to LMWBPs--known as inhibitors of IGF-I dependent functions.	Heparin	31-38	insulin-like growth factor 1	Rattus norvegicus	155-160
11208491-9	2001	The evidence was provided that heparin dissociates IGF-I from HMWBPs complex of control rat serum (predominant one in serum of these animals) and released IGF-I in turn is bound to LMWBPs--known as inhibitors of IGF-I dependent functions.	Heparin	31-38	insulin-like growth factor 1	Rattus norvegicus	155-160
11208491-10	2001	In contrast, in fasted rat serum heparin dissociates IGF-I from LMWBPs (predominant complex in serum of these animals) making IGF-I free and available to stimulate IGF-I dependent functions.	Heparin	33-40	insulin-like growth factor 1	Rattus norvegicus	53-58
11208491-10	2001	In contrast, in fasted rat serum heparin dissociates IGF-I from LMWBPs (predominant complex in serum of these animals) making IGF-I free and available to stimulate IGF-I dependent functions.	Heparin	33-40	insulin-like growth factor 1	Rattus norvegicus	126-131
6768161-0	1980	Altered inactivation of trinitrophenylated thrombin by antithrombin III in the presence of heparin.	Heparin	91-98	serpin family C member 1	Homo sapiens	55-71
11208491-10	2001	In contrast, in fasted rat serum heparin dissociates IGF-I from LMWBPs (predominant complex in serum of these animals) making IGF-I free and available to stimulate IGF-I dependent functions.	Heparin	33-40	insulin-like growth factor 1	Rattus norvegicus	126-131
10514513-4	1999	Studies presented here show that IGFBP-3 does indeed bind to fibrinogen and fibrin immobilized on immunocapture plates, with K(d) values = 0.67 and 0.70 nM, respectively, and competitive binding studies suggest that the IGFBP-3 heparin binding domain may participate in this binding.	Heparin	228-235	insulin like growth factor binding protein 3	Homo sapiens	33-40
10512728-3	1999	Chemical crosslinking of radiolabeled FGF4 to the soluble FGF receptors confirms the preferential formation of FGF4-FGFR-2 complexes under restricted heparin availability, with maximal ligand-receptor interactions at almost 20-fold lower heparin concentrations then those required for the affinity labeling of FGFR-1.	Heparin	150-157	fibroblast growth factor receptor 2	Homo sapiens	116-122
10512728-3	1999	Chemical crosslinking of radiolabeled FGF4 to the soluble FGF receptors confirms the preferential formation of FGF4-FGFR-2 complexes under restricted heparin availability, with maximal ligand-receptor interactions at almost 20-fold lower heparin concentrations then those required for the affinity labeling of FGFR-1.	Heparin	238-245	fibroblast growth factor receptor 2	Homo sapiens	116-122
10512728-4	1999	In accordance, HS-deficient cells expressing FGFR-2 proliferate in response to FGF4 at extremely low exogenous heparin concentrations, while FGFR-1 expressing cells are completely unresponsive under the same conditions.	Heparin	111-118	fibroblast growth factor receptor 2	Homo sapiens	45-51
11136935-3	2001	We also determined whether heparin or dextran sulfate releases EC-SOD into CSF.	Heparin	27-34	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	63-69
7191289-5	1980	The amidolytic method using chromogenic substrates S-2222 for factor Xa and S-2238 for thrombin demonstrated that the new heparin was also at least two times more effective than commercial heparin in increasing the rate of inactivation of these serin proteases through antithrombin III.	Heparin	122-129	serpin family C member 1	Homo sapiens	269-285
11136935-11	2001	After gene transfer, CuZnSOD was expressed mainly in tissues, and EC-SOD was released into the CSF, especially after injection of heparin or dextran sulfate.	Heparin	130-137	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	66-72
11150580-2	2000	Heparin is known to exert its antithrombotic effects by accelerating the effect of antithrombin (AT) and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation from vascular endothelium.	Heparin	0-7	serpin family C member 1	Homo sapiens	83-95
11150584-0	2000	Rebound activation of coagulation after treatment with unfractionated heparin and not with low molecular weight heparin is associated with partial depletion of tissue factor pathway inhibitor and antithrombin.	Heparin	70-77	serpin family C member 1	Homo sapiens	196-208
10516111-6	1999	The inhibitory effect of heparin combined with its therapeutic potential could help to clarify the role of phospholipase A(2) in the pathogenesis of several preinflammatory situations.	Heparin	25-32	phospholipase A2 group IB	Rattus norvegicus	107-124
10726041-7	1999	The endothelial damage markers of soluble thrombomodulin, soluble P-selectin (p &lt; 0.05 vs. normal), plasminogen activator inhibitor-1 and tissue factor were elevated in heparin-induced thrombocytopenia and antiphospholipid antibody syndrome patients.	Heparin	172-179	serpin family E member 1	Homo sapiens	103-136
10726041-8	1999	The soluble E-selectin was elevated only in the patients with both heparin-induced thrombocytopenia and antiphospholipid antibody syndrome (p &lt; 0.05 vs. normal).	Heparin	67-74	selectin E	Homo sapiens	12-22
10544909-0	1999	A flow cytometric assay of platelet activation marker P-selectin (CD62P) distinguishes heparin-induced thrombocytopenia (HIT) from HIT with thrombosis (HITT).	Heparin	87-94	selectin P	Homo sapiens	54-64
10544909-0	1999	A flow cytometric assay of platelet activation marker P-selectin (CD62P) distinguishes heparin-induced thrombocytopenia (HIT) from HIT with thrombosis (HITT).	Heparin	87-94	selectin P	Homo sapiens	66-71
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	59-66	lipoprotein lipase	Homo sapiens	33-36
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	59-66	lipoprotein lipase	Homo sapiens	117-120
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	59-66	lipoprotein lipase	Homo sapiens	117-120
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	59-66	lipoprotein lipase	Homo sapiens	117-120
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	171-178	lipoprotein lipase	Homo sapiens	33-36
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	171-178	lipoprotein lipase	Homo sapiens	117-120
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	171-178	lipoprotein lipase	Homo sapiens	117-120
11068186-6	2000	Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein.	Heparin	171-178	lipoprotein lipase	Homo sapiens	117-120
10462449-0	1999	Human selenium-dependent thioredoxin reductase from HeLa cells: properties of forms with differing heparin affinities.	Heparin	99-106	peroxiredoxin 5	Homo sapiens	25-46
10462449-3	1999	At higher aeration, 50% of saturation of dissolved oxygen or 12 ml of oxygen in a liter of medium, HeLa cell growth was slower and additional TrxR forms that bound to heparin were present in purified enzyme preparations.	Heparin	167-174	peroxiredoxin 5	Homo sapiens	142-146
7192096-2	1980	A highly potent heparin (Heparin Schering) was characterized in comparison to commercial heparin by affinity chromatography on antithrombin-III-sepharose.	Heparin	16-23	serpin family C member 1	Homo sapiens	127-143
10462449-4	1999	A minor component, TrxR2, the mitochondrial form of TrxR, was detected in the heparin-bound enzyme fraction.	Heparin	78-85	peroxiredoxin 5	Homo sapiens	19-23
7192096-2	1980	A highly potent heparin (Heparin Schering) was characterized in comparison to commercial heparin by affinity chromatography on antithrombin-III-sepharose.	Heparin	25-32	serpin family C member 1	Homo sapiens	127-143
11089550-8	2000	However, unlike the (1-97)NH2-terminal fragment, the COOH-terminal fragments of IGFBP-3 retained their ability to associate with the cell surface, and this binding was competed by heparin, similar to intact IGFBP-3.	Heparin	180-187	insulin-like growth factor binding protein 3	Mus musculus	80-87
7350242-3	1980	A minor heparin fraction binds free AT III selectively and firmly but not its protease complexes.	Heparin	8-15	serpin family C member 1	Homo sapiens	36-42
11131221-2	2000	Binding of AT-III to heparin dramatically increases its inhibitory effect.	Heparin	21-28	serpin family C member 1	Homo sapiens	11-17
10467078-4	1999	However, local delivery of heparin further increased coronary sinus ATIII activity (P = 0.003, period III vs. period IV).	Heparin	27-34	serpin family C member 1	Homo sapiens	68-73
7376137-0	1980	Effect of monovalent cations on the heparin-enhanced antithrombin III/thrombin reaction.	Heparin	36-43	serpin family C member 1	Homo sapiens	53-69
10980840-2	1999	Heparin has limitations as an antithrombin agent, which has led to clinical investigation of alternative agents.	Heparin	0-7	serpin family C member 1	Homo sapiens	30-42
11131221-3	2000	AT-III deficiency during cardiopulmonary bypass (CPB) can lead to insufficient anticoagulation which cannot be treated by higher doses of heparin.	Heparin	138-145	serpin family C member 1	Homo sapiens	0-6
11131221-8	2000	Heparinization was performed with 400 IU/kg of porcine mucosal heparin, increasing the activated coagulation time (ACT) from a baseline of 115 to 549 s. AT-III activity at that time was above 100% and the plasma D-dimer concentration was 230 ng/l.	Heparin	63-70	serpin family C member 1	Homo sapiens	153-159
11131221-11	2000	Heparin was reversed with 3 mg/kg protamine chloride, decreasing the ACT to 155 s. In the intensive care unit (ICU), the patientreceived prophylactic Fraxiparine and 1500 IU AT-III, increasing the AT-III activity to 84%.	Heparin	0-7	serpin family C member 1	Homo sapiens	174-180
41579-11	1979	Zn2+, Mn2+, heparin, glutathione and p-chloromercuribenzoate inhibit the ribonuclease, while Na+, K+, EDTA and sermidine have only little or no effect.	Heparin	12-19	ribonuclease	Saccharomyces cerevisiae S288C	73-85
11131221-11	2000	Heparin was reversed with 3 mg/kg protamine chloride, decreasing the ACT to 155 s. In the intensive care unit (ICU), the patientreceived prophylactic Fraxiparine and 1500 IU AT-III, increasing the AT-III activity to 84%.	Heparin	0-7	serpin family C member 1	Homo sapiens	197-203
10944532-8	2000	However, in chlorate-treated cells, the addition of heparin or purified HSPGs simultaneously with FGF-2 restored DNA synthesis, the sustained phosphorylation of p42/44(MAPK) and p90(RSK), and the degradation of IkappaBalpha and IkappaBbeta.	Heparin	52-59	NFKB inhibitor alpha	Rattus norvegicus	211-223
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	49-61
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	185-197
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	166-173	serpin family C member 1	Homo sapiens	49-61
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	166-173	serpin family C member 1	Homo sapiens	185-197
10433728-2	1999	The binding occurs in two steps, an initial weak interaction inducing a conformational change of antithrombin that increases the affinity for heparin and activates the inhibitor.	Heparin	142-149	serpin family C member 1	Homo sapiens	97-109
10433728-3	1999	Arg46 and Arg47 of antithrombin have been implicated in heparin binding by studies of natural and recombinant variants and by the crystal structure of a pentasaccharide-antithrombin complex.	Heparin	56-63	serpin family C member 1	Homo sapiens	19-31
10433728-3	1999	Arg46 and Arg47 of antithrombin have been implicated in heparin binding by studies of natural and recombinant variants and by the crystal structure of a pentasaccharide-antithrombin complex.	Heparin	56-63	serpin family C member 1	Homo sapiens	169-181
10400621-8	1999	Formation of the complex was dependent on cell interaction with the heparin binding region in fibronectin and required IL-1/type I IL-1 receptor binding.	Heparin	68-75	interleukin 1 alpha	Homo sapiens	119-123
10400621-8	1999	Formation of the complex was dependent on cell interaction with the heparin binding region in fibronectin and required IL-1/type I IL-1 receptor binding.	Heparin	68-75	interleukin 1 alpha	Homo sapiens	131-135
11009624-0	2000	Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex.	Heparin	17-24	serpin family C member 1	Homo sapiens	42-54
11009624-0	2000	Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex.	Heparin	17-24	serpin family C member 1	Homo sapiens	127-139
10906682-4	2000	To decrease their thrombogenicity, which remains the major obstacle, we have developed polymeric materials endowed with a specific affinity for antithrombin III (ATIII) and thus able, like heparin, to catalyze the inhibition of thrombin by ATIII.	Heparin	189-196	serpin family C member 1	Homo sapiens	240-245
477560-7	1979	Antithrombin III levels should be determined in all cases of increased heparin tolerance.	Heparin	71-78	serpin family C member 1	Homo sapiens	0-16
10964700-5	2000	Mouse EC-SOD exists primarily as a homotetramer composed of a pair of dimers linked through disulfide bonds present in the heparin-binding domains of each subunit.	Heparin	123-130	superoxide dismutase 3, extracellular	Mus musculus	6-12
10470235-10	1999	They might release tumor M2-PK in heparin-plasma and serum samples, but not in EDTA-plasma samples.	Heparin	34-41	pyruvate kinase M1/2	Homo sapiens	19-30
10456457-0	1999	Involvement of Lys 62(217) and Lys 63(218) of human anticoagulant protein C in heparin stimulation of inhibition by the protein C inhibitor.	Heparin	79-86	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	52-75
10456457-1	1999	Inhibition of activated protein C (APC) by protein C inhibitor (PCI) is stimulated by heparin, whereas inhibition by alpha1-antitrypsin (AAT) is heparin-independent.	Heparin	86-93	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	24-33
10456457-1	1999	Inhibition of activated protein C (APC) by protein C inhibitor (PCI) is stimulated by heparin, whereas inhibition by alpha1-antitrypsin (AAT) is heparin-independent.	Heparin	86-93	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	43-52
10456457-2	1999	Three lysine residues located in a positively charged cluster in the serine protease domain of protein C (PC) were mutated to probe their involvement in the heparin stimulation of inhibition by PCI.	Heparin	157-164	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	95-104
10926850-5	2000	Among five transcription factors studied, AP-1, SP-1, ETS-1 and nuclear factor kappaB proved to be sensitive to heparin and heparan sulphate, whereas TFIID was hardly inhibited in either in vitro or in vivo systems.	Heparin	112-119	ETS proto-oncogene 1, transcription factor	Homo sapiens	54-59
476156-0	1979	Evidence for a plasma inhibitor of the heparin accelerated inhibition of factor Xa by antithrombin III.	Heparin	39-46	serpin family C member 1	Homo sapiens	86-102
10821835-7	2000	Either destruction of cell surface HSPGs or prior occupancy of the Cyr61 heparin-binding site completely blocked cell adhesion to Cyr61.	Heparin	73-80	cellular communication network factor 1	Homo sapiens	67-72
10415791-0	1999	Heparin and fragments modulate the expression of collagen-degrading enzymes (matrix metalloproteinases 1 and 2) by human gingival fibroblasts.	Heparin	0-7	matrix metallopeptidase 1	Homo sapiens	49-110
10387091-10	1999	In the presence of heparin, oxidized MPI inhibits cathepsin G via a two-step reaction characterized by Ki = 0.22 microM, k2 = 0.1 s-1, k-2 = 0.023 s-1, and Ki = 42 nM.	Heparin	19-26	cathepsin G	Homo sapiens	50-61
10821835-7	2000	Either destruction of cell surface HSPGs or prior occupancy of the Cyr61 heparin-binding site completely blocked cell adhesion to Cyr61.	Heparin	73-80	cellular communication network factor 1	Homo sapiens	130-135
476156-1	1979	The ability of heparin fractions of different molecular weight to potentiate the action of antithrombin III against the coagulation factors thrombin and Xa has been examined in purified reaction mixtures and in plasma.	Heparin	15-22	serpin family C member 1	Homo sapiens	91-107
10821835-8	2000	A heparin-binding defective mutant of Cyr61 was unable to mediate fibroblast adhesion through integrin alpha(6)beta(1) but still mediated endothelial cell adhesion through integrin alpha(V)beta(3), indicating that endothelial cell adhesion through integrin alpha(V)beta(3) is independent of the heparin-binding activity of Cyr61.	Heparin	2-9	cellular communication network factor 1	Homo sapiens	38-43
10821835-8	2000	A heparin-binding defective mutant of Cyr61 was unable to mediate fibroblast adhesion through integrin alpha(6)beta(1) but still mediated endothelial cell adhesion through integrin alpha(V)beta(3), indicating that endothelial cell adhesion through integrin alpha(V)beta(3) is independent of the heparin-binding activity of Cyr61.	Heparin	2-9	cellular communication network factor 1	Homo sapiens	323-328
469001-3	1979	Although heparin markedly enhanced the antithrombin activity of antithrombin III, dextran sulphate did not activate antithrombin III.	Heparin	9-16	serpin family C member 1	Homo sapiens	39-51
10825225-5	2000	The adsorption of ATIII increased with increasing heparin on the surface.	Heparin	50-57	serpin family C member 1	Homo sapiens	18-23
10410303-1	1999	Lipoprotein lipase (LPL) is known to be attached to the luminal surface of vascular endothelial cells in a complex with membrane-bound heparan sulfate, and released into blood stream by heparin.	Heparin	186-193	lipoprotein lipase	Homo sapiens	0-18
10410303-1	1999	Lipoprotein lipase (LPL) is known to be attached to the luminal surface of vascular endothelial cells in a complex with membrane-bound heparan sulfate, and released into blood stream by heparin.	Heparin	186-193	lipoprotein lipase	Homo sapiens	20-23
469001-3	1979	Although heparin markedly enhanced the antithrombin activity of antithrombin III, dextran sulphate did not activate antithrombin III.	Heparin	9-16	serpin family C member 1	Homo sapiens	64-80
429327-0	1979	Fractionation of low molecular weight heparin species and their interaction with antithrombin.	Heparin	38-45	serpin family C member 1	Homo sapiens	81-93
10407500-1	1999	A major gene hypothesis for heparin releasable plasma lipoprotein lipase (PH-LPL) activity was assessed using segregation analyses of data on 495 members in 98 normolipidemic sedentary families of Caucasian descent who participated in the HERITAGE Family Study.	Heparin	28-35	lipoprotein lipase	Homo sapiens	54-72
10407500-1	1999	A major gene hypothesis for heparin releasable plasma lipoprotein lipase (PH-LPL) activity was assessed using segregation analyses of data on 495 members in 98 normolipidemic sedentary families of Caucasian descent who participated in the HERITAGE Family Study.	Heparin	28-35	lipoprotein lipase	Homo sapiens	77-80
10391608-1	1999	PURPOSE: To report three patients who developed heparin resistance during cardiac surgery which was successfully managed with 1000 U Antithrombin III (AT III).	Heparin	48-55	serpin family C member 1	Homo sapiens	133-149
10391608-1	1999	PURPOSE: To report three patients who developed heparin resistance during cardiac surgery which was successfully managed with 1000 U Antithrombin III (AT III).	Heparin	48-55	serpin family C member 1	Homo sapiens	151-157
10391608-12	1999	CONCLUSION: We recommend that AT III supplementation should be considered to manage heparin resistance prior or during CPB in patients undergoing open heart surgery.	Heparin	84-91	serpin family C member 1	Homo sapiens	30-36
10951616-6	2000	RESULTS: Heparin could obviously reduce HSC growth, inhibit the synthesis of type I procollagen and fibronectin protein, and the gene expressions of type I procollagen, fibronectin and MT-MMP.	Heparin	9-16	fibronectin 1	Rattus norvegicus	100-111
10951616-6	2000	RESULTS: Heparin could obviously reduce HSC growth, inhibit the synthesis of type I procollagen and fibronectin protein, and the gene expressions of type I procollagen, fibronectin and MT-MMP.	Heparin	9-16	fibronectin 1	Rattus norvegicus	169-180
10913257-0	2000	The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139.	Heparin	56-63	serpin family C member 1	Homo sapiens	14-26
10913257-1	2000	The interaction of a well-defined pentasaccharide sequence of heparin with a specific binding site on antithrombin activates the inhibitor through a conformational change.	Heparin	62-69	serpin family C member 1	Homo sapiens	102-114
10913257-3	2000	An extended heparin binding site of antithrombin outside the specific pentasaccharide site has been proposed to account for the higher affinity of the inhibitor for full-length heparin chains by interacting with saccharides adjacent to the pentasaccharide sequence.	Heparin	12-19	serpin family C member 1	Homo sapiens	36-48
10913257-10	2000	Together, these results show that Lys136 forms part of the extended heparin binding site of antithrombin that participates in the binding of full-length heparin chains, whereas Lys139 is located outside this site.	Heparin	68-75	serpin family C member 1	Homo sapiens	92-104
10913257-10	2000	Together, these results show that Lys136 forms part of the extended heparin binding site of antithrombin that participates in the binding of full-length heparin chains, whereas Lys139 is located outside this site.	Heparin	153-160	serpin family C member 1	Homo sapiens	92-104
10902786-0	2000	Release of activin and follistatin during cardiovascular procedures is largely due to heparin administration.	Heparin	86-93	inhibin subunit beta E	Homo sapiens	11-18
10902786-2	2000	As heparin is used routinely in many cardiovascular procedures for its anticoagulation properties, it may also cause the release of heparin-binding growth factors, including activin and follistatin, from the vascular endothelium.	Heparin	3-10	inhibin subunit beta E	Homo sapiens	174-181
10902786-3	2000	We examined the effect of two cardiovascular procedures and the use of heparin directly on the circulating concentrations of activin A and follistatin.	Heparin	71-78	inhibin subunit beta E	Homo sapiens	125-132
10404636-2	1999	Upon activation by at least five genetically distinct ligands (including EGF, transforming growth factor-alpha (TGF alpha) and heparin-binding EGF (HB-EGF)), the intrinsic kinase is activated and EGFR tyrosyl-phosphorylates itself and numerous intermediary effector molecules, including closely-related c-erbB receptor family members.	Heparin	127-134	epidermal growth factor	Homo sapiens	143-146
10404636-2	1999	Upon activation by at least five genetically distinct ligands (including EGF, transforming growth factor-alpha (TGF alpha) and heparin-binding EGF (HB-EGF)), the intrinsic kinase is activated and EGFR tyrosyl-phosphorylates itself and numerous intermediary effector molecules, including closely-related c-erbB receptor family members.	Heparin	127-134	heparin binding EGF like growth factor	Homo sapiens	148-155
429327-5	1979	The binding of highly active heparin to antithrombin is accurately described by a single-site binding model with a KHep-ATDISS of approximately 1 X 10(-7) M. Variations in this binding parameter secondary to changes in environmental variables indicate that charge-charge interactions as well as an increase in entropy are critical to the formation of the highly active heparin-antithrombin complex.	Heparin	29-36	serpin family C member 1	Homo sapiens	40-52
10860838-3	2000	Here we show that when both isolated FGFR2betaIIIb and FGFR2betaIIIc or their common Ig module II are allowed to affinity select heparin from a mixture, the resultant binary complexes bound FGF-1, FGF-2, and FGF-7 with nearly equal affinity.	Heparin	129-136	fibroblast growth factor receptor 2	Homo sapiens	37-42
10860838-5	2000	The results show that in isolation both Ig modules II and III of FGFR2 can interact with heparin and that each exhibits a binding site for FGF.	Heparin	89-96	fibroblast growth factor receptor 2	Homo sapiens	65-70
10375387-0	1999	Heparin induced thrombocytopenia: diagnosis and contemporary antithrombin management.	Heparin	0-7	serpin family C member 1	Homo sapiens	61-73
429327-5	1979	The binding of highly active heparin to antithrombin is accurately described by a single-site binding model with a KHep-ATDISS of approximately 1 X 10(-7) M. Variations in this binding parameter secondary to changes in environmental variables indicate that charge-charge interactions as well as an increase in entropy are critical to the formation of the highly active heparin-antithrombin complex.	Heparin	29-36	serpin family C member 1	Homo sapiens	377-389
429327-7	1979	The ability of the highly active heparin to accelerate the thrombin-antithrombin interaction was also examined.	Heparin	33-40	serpin family C member 1	Homo sapiens	68-80
473117-3	1979	The antithrombin activity of the copolymer corresponded to 1% of grafted heparin.	Heparin	73-80	serpin family C member 1	Homo sapiens	4-16
10427537-1	1999	Colchicine, corticosteroids, daunomycin, fluorouracil, heparin and retinoids have been used in man and show an effect in different stages of the development of PVR.	Heparin	55-62	PVR cell adhesion molecule	Homo sapiens	160-163
10408366-8	1999	The factor H-like protein 1 (FHL-1) or reconectin shares the complement regulatory functions with factor H and interacts with heparin.	Heparin	126-133	four and a half LIM domains 1	Homo sapiens	4-27
10408366-8	1999	The factor H-like protein 1 (FHL-1) or reconectin shares the complement regulatory functions with factor H and interacts with heparin.	Heparin	126-133	four and a half LIM domains 1	Homo sapiens	29-34
10806335-0	2000	Inhibition of binding of lactoferrin to the human promonocyte cell line THP-1 by heparin: the role of cell surface sulphated molecules.	Heparin	81-88	lactotransferrin	Bos taurus	25-36
10806335-3	2000	In the present work we found that heparin caused a dose-dependent inhibition of specific binding of both human and bovine lactoferrin to human monocytic THP-1 cells.	Heparin	34-41	lactotransferrin	Bos taurus	122-133
10806335-7	2000	These results suggest that heparin binding and monocyte/macrophage binding by lactoferrin both involve interactions between basic regions in the N1 domain of lactoferrin and sulphate groups.	Heparin	27-34	lactotransferrin	Bos taurus	158-169
10781455-0	2000	The in vitro effects of antithrombin III on the activated coagulation time in patients on heparin therapy.	Heparin	90-97	serpin family C member 1	Homo sapiens	24-40
10781455-1	2000	UNLABELLED: Heparin requires antithrombin III (AT) to achieve anticoagulation, and patients on continuous small-dose heparin preoperatively experience decreased levels of AT-causing heparin resistance.	Heparin	12-19	serpin family C member 1	Homo sapiens	29-45
10781455-11	2000	IMPLICATIONS: In vitro addition of antithrombin III (0.2 U/mL) to heparinized blood samples (4.1-6.8 units of heparin/mL) from patients on previous heparin therapy increases sensitivity to supplemental heparin as reflected by significantly prolonged activated clotting time.	Heparin	66-73	serpin family C member 1	Homo sapiens	35-51
10781455-11	2000	IMPLICATIONS: In vitro addition of antithrombin III (0.2 U/mL) to heparinized blood samples (4.1-6.8 units of heparin/mL) from patients on previous heparin therapy increases sensitivity to supplemental heparin as reflected by significantly prolonged activated clotting time.	Heparin	110-117	serpin family C member 1	Homo sapiens	35-51
10493548-3	1999	On the other hand, the properties of the IP3 receptors of these channels (IP3R), i.e., the dose-dependent effect of IP3, the IP3 desensitization of the receptor, and the sensitivity to micromolar concentrations of heparin and arachidonic acid were close to those of the endoplasmic reticulum IP3 receptor.	Heparin	214-221	inositol 1,4,5-trisphosphate receptor 1	Mus musculus	74-78
10493548-3	1999	On the other hand, the properties of the IP3 receptors of these channels (IP3R), i.e., the dose-dependent effect of IP3, the IP3 desensitization of the receptor, and the sensitivity to micromolar concentrations of heparin and arachidonic acid were close to those of the endoplasmic reticulum IP3 receptor.	Heparin	214-221	inositol 1,4,5-trisphosphate receptor 1	Mus musculus	41-53
10333081-3	1999	Post-heparin LPL activity (10,000 U) was measured on each occasion 120 minutes post-carbohydrate.	Heparin	5-12	lipoprotein lipase	Homo sapiens	13-16
10781455-11	2000	IMPLICATIONS: In vitro addition of antithrombin III (0.2 U/mL) to heparinized blood samples (4.1-6.8 units of heparin/mL) from patients on previous heparin therapy increases sensitivity to supplemental heparin as reflected by significantly prolonged activated clotting time.	Heparin	110-117	serpin family C member 1	Homo sapiens	35-51
473117-6	1979	The heparin part of the copolymer was responsible for antithrombin III adsorption and for decrease of factor V activity.	Heparin	4-11	serpin family C member 1	Homo sapiens	54-70
420817-4	1979	These spectral results indicate that the thrombin-antithrombin III complex formed in the presence of heparin differs in its conformation from that produced in its absence.	Heparin	101-108	serpin family C member 1	Homo sapiens	50-66
10787434-5	2000	LPL activity in the post-heparin plasma of the heterozygotes was reduced to 49;-79% of the mean observed in normal individuals.	Heparin	25-32	lipoprotein lipase	Homo sapiens	0-3
10193724-0	1999	Antithrombin activity during the period of percutaneous coronary revascularization: relation to heparin use, thrombotic complications and restenosis.	Heparin	96-103	serpin family C member 1	Homo sapiens	0-12
10193724-1	1999	OBJECTIVES: This study evaluated changes in antithrombin (AT) activity around the time of percutaneous transluminal coronary revascularization (PTCR) with unfractionated heparin anticoagulation and the effects these changes had on major thrombotic complications of PTCR.	Heparin	170-177	serpin family C member 1	Homo sapiens	44-56
10037709-0	1999	Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II.	Heparin	76-83	serpin family C member 1	Homo sapiens	108-120
10792070-5	2000	Urine specimens were collected at these two time points and measured for heparin-binding epidermal growth factor-like growth factor (HB-EGF) by enzyme-linked immunosorbent assay and for antiproliferative factor (APF) activity by (3)H-thymidine uptake by normal human bladder urothelial cells.	Heparin	73-80	heparin binding EGF like growth factor	Homo sapiens	133-139
106967-0	1979	alpha-L-iduronidase, beta-D-glucuronidase, and 2-sulfo-L-iduronate 2-sulfatase: preparation and characterization of radioactive substrates from heparin.	Heparin	144-151	alpha-L-iduronidase	Homo sapiens	0-19
10736176-0	2000	Interaction of heparin with a synthetic pentadecapeptide from the C-terminal heparin-binding domain of fibronectin.	Heparin	15-22	fibronectin 1	Bos taurus	103-114
10736176-0	2000	Interaction of heparin with a synthetic pentadecapeptide from the C-terminal heparin-binding domain of fibronectin.	Heparin	77-84	fibronectin 1	Bos taurus	103-114
10029547-0	1999	Heparin is essential for a single keratinocyte growth factor molecule to bind and form a complex with two molecules of the extracellular domain of its receptor.	Heparin	0-7	fibroblast growth factor 7	Mus musculus	34-60
10029547-4	1999	In the presence of low-molecular mass heparin ( approximately 3 kDa), we demonstrate the formation of complexes containing two molecules of sKGFR and one molecule of KGF.	Heparin	38-45	fibroblast growth factor 7	Mus musculus	141-144
10029547-7	1999	Utilizing the highly purified proteins and defined conditions described in this study, we find that heparin is obligatory for formation of a KGF-sKGFR complex.	Heparin	100-107	fibroblast growth factor 7	Mus musculus	141-144
504072-5	1979	Heparin cofactor activity was demonstrated by immediate inactivation of thrombin by antithrombin III in the presence of minute quantities of heparin.	Heparin	0-7	serpin family C member 1	Homo sapiens	84-100
10739940-4	2000	In addition, alpha-L-iduronidase also interacts with heparin, as do some amyloid-forming proteins.	Heparin	53-60	alpha-L-iduronidase	Homo sapiens	13-32
504072-6	1979	It also could be demonstrated that thrombin inactivation by antithrombin III occurs by formation of a bimolecular complex whose rate of formation is markedly enhanced by minute quantities of heparin.	Heparin	191-198	serpin family C member 1	Homo sapiens	60-76
10022829-0	1999	Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins.	Heparin	77-84	laminin, alpha 1	Mus musculus	28-42
743219-1	1978	It is proposed that the anti-coagulant activity of heparin is related to the probability of finding, in a random distribution of different disaccharides, a dodecasaccharide with the sequence required for binding to antithrombin.	Heparin	51-58	serpin family C member 1	Homo sapiens	215-227
10093889-2	1999	The use of the current antithrombotic drugs, namely heparin + chronic aspirin (ASA) +/- oral anticoagulants, is based upon the assumptions that: i) heparin blocks thrombin generation and/or accelerates thrombin inhibition by antithrombin III (ATIII); ii) aspirin acetylates platelet cyclooxygenase, thereby preventing thromboxane A2 (TxA2) synthesis; and iii) oral anticoagulants reduce the availability of vitamin K-dependent procoagulants, thereby reducing the risk of thrombus formation.	Heparin	148-155	serpin family C member 1	Homo sapiens	225-241
10093889-2	1999	The use of the current antithrombotic drugs, namely heparin + chronic aspirin (ASA) +/- oral anticoagulants, is based upon the assumptions that: i) heparin blocks thrombin generation and/or accelerates thrombin inhibition by antithrombin III (ATIII); ii) aspirin acetylates platelet cyclooxygenase, thereby preventing thromboxane A2 (TxA2) synthesis; and iii) oral anticoagulants reduce the availability of vitamin K-dependent procoagulants, thereby reducing the risk of thrombus formation.	Heparin	148-155	serpin family C member 1	Homo sapiens	243-248
9949192-4	1999	Protease nexin-1 bound brain heparan sulfate only 1.8-fold less tightly than heparin (Kdvalues of 35 vs. 20 nM, respectively), whereas NCAM and L1 bound heparin well (Kd approximately 140 nM) but failed to bind detectably to brain heparan sulfate (Kd&gt;3 microM).	Heparin	153-160	neural cell adhesion molecule 1	Rattus norvegicus	135-139
10712595-5	2000	The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135.	Heparin	196-203	serpin family C member 1	Homo sapiens	129-141
10712595-5	2000	The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135.	Heparin	196-203	serpin family C member 1	Homo sapiens	357-369
10709911-5	2000	Unlike heparin-induced stimulation of antithrombin-thrombin interaction, the heparin-induced stimulation of tissue plasminogen activator did not seem to follow a template model.	Heparin	7-14	serpin family C member 1	Homo sapiens	38-50
10660568-1	2000	Heparin regulates the inhibitory activity of antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	45-57
10660568-2	2000	It has been proposed that residues P15 and P14 are expelled from beta-sheet A of antithrombin by heparin binding, permitting better interaction of the reactive center loop with factor Xa.	Heparin	97-104	serpin family C member 1	Homo sapiens	81-93
743219-6	1978	The probability that any randomly chosen dodecasaccharide sequence in heparin should bind to antithrombin was calculated to 0.022.	Heparin	70-77	serpin family C member 1	Homo sapiens	93-105
10660568-4	2000	There is minimal further increase in antithrombin fluorescence upon heparin binding.	Heparin	68-75	serpin family C member 1	Homo sapiens	37-49
10226805-3	1999	This proteolysis was less pronounced for IGFBP-3 containing a mutated heparin binding domain, and was prevented by purifying IGFBP-3 on an IGF-I affinity column in the presence of 2 M sodium chloride, suggesting that the responsible protease(s) binds the IGFBP-3 heparin binding domain.	Heparin	70-77	insulin like growth factor binding protein 3	Homo sapiens	41-48
10226805-3	1999	This proteolysis was less pronounced for IGFBP-3 containing a mutated heparin binding domain, and was prevented by purifying IGFBP-3 on an IGF-I affinity column in the presence of 2 M sodium chloride, suggesting that the responsible protease(s) binds the IGFBP-3 heparin binding domain.	Heparin	70-77	insulin like growth factor binding protein 3	Homo sapiens	125-132
10226805-3	1999	This proteolysis was less pronounced for IGFBP-3 containing a mutated heparin binding domain, and was prevented by purifying IGFBP-3 on an IGF-I affinity column in the presence of 2 M sodium chloride, suggesting that the responsible protease(s) binds the IGFBP-3 heparin binding domain.	Heparin	70-77	insulin like growth factor binding protein 3	Homo sapiens	125-132
743219-10	1978	The activity of high-affinity heparin (i.e. molecules containing high-affinity binding sites for antithrombin), determined either by a whole-blood clotting procedure or by thrombin inactivation in the presence of antithrombin, thus remained dependent on molecular weight.	Heparin	30-37	serpin family C member 1	Homo sapiens	97-109
10226805-3	1999	This proteolysis was less pronounced for IGFBP-3 containing a mutated heparin binding domain, and was prevented by purifying IGFBP-3 on an IGF-I affinity column in the presence of 2 M sodium chloride, suggesting that the responsible protease(s) binds the IGFBP-3 heparin binding domain.	Heparin	263-270	insulin like growth factor binding protein 3	Homo sapiens	125-132
10226805-3	1999	This proteolysis was less pronounced for IGFBP-3 containing a mutated heparin binding domain, and was prevented by purifying IGFBP-3 on an IGF-I affinity column in the presence of 2 M sodium chloride, suggesting that the responsible protease(s) binds the IGFBP-3 heparin binding domain.	Heparin	263-270	insulin like growth factor binding protein 3	Homo sapiens	125-132
743219-10	1978	The activity of high-affinity heparin (i.e. molecules containing high-affinity binding sites for antithrombin), determined either by a whole-blood clotting procedure or by thrombin inactivation in the presence of antithrombin, thus remained dependent on molecular weight.	Heparin	30-37	serpin family C member 1	Homo sapiens	213-225
10656996-0	2000	Overlap of IGF- and heparin-binding sites in rat IGF-binding protein-5.	Heparin	20-27	insulin-like growth factor binding protein 5	Rattus norvegicus	49-70
10656996-1	2000	Using site-directed mutagenesis, we have undertaken a study of a potential IGF-binding site in the C-terminal domain of rat IGFBP-5, lying close to or within a previously described heparin-binding domain (residues 201-218) in this protein.	Heparin	181-188	insulin-like growth factor 1	Rattus norvegicus	75-78
743219-12	1978	One explanation could be a requirement for binding of thrombin to the heparin chain adjacent to antithrombin.	Heparin	70-77	serpin family C member 1	Homo sapiens	96-108
10656996-1	2000	Using site-directed mutagenesis, we have undertaken a study of a potential IGF-binding site in the C-terminal domain of rat IGFBP-5, lying close to or within a previously described heparin-binding domain (residues 201-218) in this protein.	Heparin	181-188	insulin-like growth factor binding protein 5	Rattus norvegicus	124-131
708377-0	1978	Effect of heparin on thrombin inactivation by antithrombin-III.	Heparin	10-17	serpin family C member 1	Homo sapiens	46-62
708377-1	1978	The inactivation of thrombin by heat and by its physiological inhibitor, antithrombin-III, shows quite different dependence on heparin concentration.	Heparin	127-134	serpin family C member 1	Homo sapiens	73-89
10656996-2	2000	After analysis of binding activity using three different methods - ligand blotting, solution phase equilibrium binding and biosensor measurement of real-time on- and off-rates - we report that the mutation of two highly conserved residues within this region (glycine 203 and glutamine 209) reduces the affinity of the binding protein for both IGF-I and IGF-II, while having no effect on heparin binding.	Heparin	387-394	insulin-like growth factor 1	Rattus norvegicus	343-348
708377-5	1978	On the other hand, heparin at 0.125-2.5 microgram/ml accelerates the thrombin-antithrombin-III reaction.	Heparin	19-26	serpin family C member 1	Homo sapiens	78-94
10656996-3	2000	In addition, we confirm that mutation of basic residues within the heparin-binding domain (R201L, K202E, K206Q and R214A) results in a protein that has attenuated heparin binding but shows only a small reduction in affinity for IGF-I and -II.	Heparin	67-74	insulin-like growth factor 1	Rattus norvegicus	228-241
10656996-4	2000	Previous findings have described the reduction in affinity of IGFBP-5 for IGFs that occurs after complexation of the binding protein with heparin or other components of the extracellular matrix (ECM) and have postulated that such an interaction may result in conformational changes in protein structure, affecting subsequent IGF interaction.	Heparin	138-145	insulin-like growth factor binding protein 5	Rattus norvegicus	62-69
10656996-4	2000	Previous findings have described the reduction in affinity of IGFBP-5 for IGFs that occurs after complexation of the binding protein with heparin or other components of the extracellular matrix (ECM) and have postulated that such an interaction may result in conformational changes in protein structure, affecting subsequent IGF interaction.	Heparin	138-145	insulin-like growth factor 1	Rattus norvegicus	62-65
10656996-5	2000	Our data suggesting potential overlap of heparin- and IGF-binding domains argue for a more direct effect of ECM modulation of the affinity of IGFBP-5 for ligand by partial occlusion of the IGF-binding site after interaction with ECM.	Heparin	41-48	insulin-like growth factor binding protein 5	Rattus norvegicus	142-149
10644368-4	2000	Here we demonstrate by monoclonal-antibody inhibition, labeled heparin binding, and surface plasmon resonance studies that a second site, most probably corresponding to the newly defined, highly conserved coreceptor binding region on gp120, forms part of the polyanion binding surface.	Heparin	63-70	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	234-239
10697424-9	1999	High activity of the tissue factor and substances neutralizing heparin may intensify the thrombus growth.	Heparin	63-70	coagulation factor III, tissue factor	Homo sapiens	21-34
10625206-11	1999	In women from symptomatic families with antithrombin deficiency, adjusted dose heparin throughout pregnancy is recommended and warfarin for at least 3 months post partum.	Heparin	79-86	serpin family C member 1	Homo sapiens	40-52
708377-9	1978	On the basis of these data we suggest a mechanism of action of heparin in the thrombin-antithrombin-III reaction which accounts for all the important features of the latter and seems to unify the different hypotheses that have been advanced.	Heparin	63-70	serpin family C member 1	Homo sapiens	87-103
10643050-7	1999	NF1-rich nuclear protein fraction was purified from the rat liver nuclear extract by DEAE-cellulose and heparin-sepharose chromatography.	Heparin	104-111	neurofibromin 1	Rattus norvegicus	0-3
10644732-0	2000	Critical role of the linker region between helix D and strand 2A in heparin activation of antithrombin.	Heparin	68-75	serpin family C member 1	Homo sapiens	90-102
641046-3	1978	Lipoprotein lipase with similar specific activity was prepared from the same plasma samples using heparin and concanavalin A affinity chromatography.	Heparin	98-105	lipoprotein lipase	Homo sapiens	0-18
10617625-2	2000	Mouse mast cell protease (mMCP) 6 and mMCP-7 are homologous tryptases stored in granules as macromolecular complexes with heparin and/or chondroitin sulfate E containing serglycin proteoglycans.	Heparin	122-129	tryptase alpha/beta 1	Mus musculus	38-44
9827576-3	1998	Addition of heparin to cell culture medium 1 hour following IL-1beta decreased MMP and TIMP-1 expression in a dose-dependent manner.	Heparin	12-19	matrix metallopeptidase 1	Homo sapiens	79-82
656058-2	1978	The order of strength of inhibition at pH4 was: heparin greater than chondroitin 4-sulphate = chondroitin 6-sulphate greater than dermatan sulphate.	Heparin	48-55	prolyl 4-hydroxylase, transmembrane	Homo sapiens	39-42
10743240-5	1998	In 16 patients with stable COPD and F1 + 2 greater than 1.65 nmol/L (mean +2s of control), intra-venose heparin therapy (100 mg qd for 10 days) significantly reduced F1 + 2(P &lt; 0.005), vWF (P &lt; 0.05), GMP-140 (P &lt; 0.05), and PaCO2 (P &lt; 0.05).	Heparin	104-111	selectin P	Homo sapiens	207-214
10616837-5	2000	However, sodium heparin treatment resulted in a greater than fourfold increase in media-associated CTGF, suggesting that the majority of CTGF produced was cell- or matrix-bound.	Heparin	9-23	cellular communication network factor 2	Rattus norvegicus	99-103
10616837-5	2000	However, sodium heparin treatment resulted in a greater than fourfold increase in media-associated CTGF, suggesting that the majority of CTGF produced was cell- or matrix-bound.	Heparin	9-23	cellular communication network factor 2	Rattus norvegicus	137-141
10616837-7	2000	TGF-, and high glucose, but not mechanical strain, stimulated the concomitant secretion of CTGF protein, the former also inducing abundant quantities of a small molecular weight form of CTGF (18 kD) containing the heparin-binding domain.	Heparin	214-221	cellular communication network factor 2	Rattus norvegicus	186-190
10537578-1	1998	A retrospective study examined the impact, in heparin resistant patients (HRP), of lyophilized antithrombin III (ATIII) upon five patient outcomes: intensive care unit stay (ICU-S), 24 hour chest tube drainage (CTD in ml), blood and blood product usage (BPU), development of postoperative coagulopathy (PO-Coag), and reoperation for bleeding (Re-Op).	Heparin	46-53	serpin family C member 1	Homo sapiens	95-111
673830-7	1978	Thus, in the polysulphate group, heparin has the highest affinity for antithrombin III, liquoid for fibrinogen and dextran sulphate for beta 2-glycoprotein I.	Heparin	33-40	serpin family C member 1	Homo sapiens	70-86
9916505-4	1998	Affinity purified anti-HPS antibodies inhibited heparin dependent formation of thrombin-antithrombin III complexes.	Heparin	48-55	serpin family C member 1	Homo sapiens	88-104
9916505-8	1998	Further, H16 mAb inhibited the binding of antithrombin III to heparin in a dose dependent manner.	Heparin	62-69	serpin family C member 1	Homo sapiens	42-58
9916505-9	1998	These results indicate that this mAb could recognize antithrombin III-binding sites on vascular endothelial heparan sulfate, leading to procoagulant states through the inhibition of heparin/heparan sulfate dependent anticoagulant process.	Heparin	182-189	serpin family C member 1	Homo sapiens	53-69
10593896-4	1999	At physiological concentrations of FGF-7, heparin was required for high affinity receptor binding and for signaling in BaF/KGFR cells.	Heparin	42-49	fibroblast growth factor receptor 2	Homo sapiens	123-127
10604885-6	1999	UFH and LMWH markedly decreased activation of coagulation caused by LPS, as F(1+2) and TpP levels only slightly increased; TF expression on monocytes was also markedly reduced by UFH.	Heparin	0-3	coagulation factor III, tissue factor	Homo sapiens	123-125
10604885-6	1999	UFH and LMWH markedly decreased activation of coagulation caused by LPS, as F(1+2) and TpP levels only slightly increased; TF expression on monocytes was also markedly reduced by UFH.	Heparin	179-182	coagulation factor III, tissue factor	Homo sapiens	123-125
10604885-7	1999	TF pathway inhibitor values increased after either heparin infusion (P&lt;0.01).	Heparin	51-58	coagulation factor III, tissue factor	Homo sapiens	0-2
26436-4	1978	Activation of the DNA and RNA synthesis in the eucaryotic cells, their nuclei and chromatin under the effect of low heparin doses should be associated not with the H1 histone dissociation, but with the dissociation of histones moderately rich in lysine--H2a, and, probably, H2b.	Heparin	116-123	H2B clustered histone 21	Homo sapiens	274-277
10617008-1	1999	BACKGROUND: To evaluate the effectiveness of intraoperative administration of antithrombin III (AT III) to improve anticoagulation and preserve the hemostatic mechanisms during cardiopulmonary bypass (CPB) in patients with unstable angina under heparin treatment.	Heparin	245-252	serpin family C member 1	Homo sapiens	78-94
10617008-1	1999	BACKGROUND: To evaluate the effectiveness of intraoperative administration of antithrombin III (AT III) to improve anticoagulation and preserve the hemostatic mechanisms during cardiopulmonary bypass (CPB) in patients with unstable angina under heparin treatment.	Heparin	245-252	serpin family C member 1	Homo sapiens	96-102
9817840-11	1998	CONCLUSIONS: A cluster of exposed lysine and arginine residues in or near the hairpin-loop region of the N domain might form part of the NK1 heparin-binding site.	Heparin	141-148	tachykinin receptor 1	Homo sapiens	137-140
9848674-1	1998	A new approach for separation, capillary affinity chromatography, is introduced for studying the interaction of heparin with antithrombin III and secretory leukocyte proteinase inhibitor.	Heparin	112-119	serpin family C member 1	Homo sapiens	125-141
9988527-0	1998	Analysis of heparin-binding sites in human lipoprotein lipase using synthetic peptides.	Heparin	12-19	lipoprotein lipase	Homo sapiens	43-61
10614876-2	1999	We have established vascular smooth muscle cells culture conditions in which heparin, in the presence of endothelial cell growth supplement, promotes cell proliferation and inhibits interleukin-1 and matrix protein expression.	Heparin	77-84	interleukin 1 alpha	Homo sapiens	182-195
10536969-7	1999	Heparin affinity chromatography caused a high loss of tryptase and residual protein contamination.	Heparin	0-7	tryptase alpha/beta 1	Mus musculus	54-62
627827-0	1978	Effect of hypothyroidism on the heparin-stimulated release of lipase from the isolated perfused rat liver.	Heparin	32-39	lipase G, endothelial type	Rattus norvegicus	62-68
10497166-4	1999	Surprisingly, the enhanced thrombin specificity of the mutant antithrombin was attenuated when a full-length bridging heparin was the activator, due both to a reduced rate of covalent reaction of the mutant serpin and thrombin and preferred reaction of the mutant serpin as a substrate.	Heparin	118-125	serpin family C member 1	Homo sapiens	62-74
10497166-5	1999	These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex.	Heparin	282-289	serpin family C member 1	Homo sapiens	120-132
10497166-5	1999	These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex.	Heparin	282-289	serpin family C member 1	Homo sapiens	241-253
10497166-5	1999	These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex.	Heparin	282-289	serpin family C member 1	Homo sapiens	241-253
9748646-2	1998	The four PLRP1s were identified using microsequencing methods after performing gel filtration on Ultrogel AcA-54 followed by chromatography on Heparin-Sepharose cation-exchanger.	Heparin	143-150	pancreatic lipase related protein 1	Homo sapiens	9-14
9722560-0	1998	Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding.	Heparin	143-150	serpin family C member 1	Homo sapiens	61-73
9722560-1	1998	Heparin causes an allosterically transmitted conformational change in the reactive center loop of antithrombin and a 40% enhancement of tryptophan fluorescence.	Heparin	0-7	serpin family C member 1	Homo sapiens	98-110
720957-2	1978	When factor Xa was added to a system containing antithrombin III in excess and heparin in low concentration, the amount of factor Xa immediately inactivated was found to be a function of the concentration of heparin.	Heparin	208-215	serpin family C member 1	Homo sapiens	48-64
9722560-5	1998	Trp-49 and Trp-225 underwent spectral shifts of 15 nm to blue and 5 nm to red, respectively, in the antithrombin-heparin complex.	Heparin	113-120	serpin family C member 1	Homo sapiens	100-112
9722560-8	1998	The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution.	Heparin	223-230	serpin family C member 1	Homo sapiens	81-93
10596996-8	1999	RESULTS: In the Hepcon group, the sensitivity to heparin was correlated with coagulation time (r = -0.78) and antithrombin III levels (r = 0.70), and individual difference of sensitivity resulted in a wide range of dosage (160 to 490 IU/kg).	Heparin	49-56	serpin family C member 1	Homo sapiens	110-126
73931-0	1977	Effect of heparin and warfarin on antithrombin III.	Heparin	10-17	serpin family C member 1	Homo sapiens	34-50
10598348-1	1999	OBJECTIVE: The utilization, during pregnancy, of low molecular weight heparin (enoxaparine) for obstetric thromboprophylaxis for patients with activated protein C resistance, following Factor V Leiden mutation.	Heparin	70-77	coagulation factor V	Homo sapiens	185-200
10499250-4	1999	Heparin and insulin stimulate LPL activity.	Heparin	0-7	lipoprotein lipase	Homo sapiens	30-33
9793617-4	1998	As this test is designed for heparin plasma levels, transformation of the chromophore occurred only after adding heparin AT III complex, which is usually present in plasma.	Heparin	113-120	serpin family C member 1	Homo sapiens	121-127
72924-0	1977	Heparin-induced decrease in circulating antithrombin-III.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-56
9716571-6	1998	Mast cell-conditioned medium added to stromal cell culture medium in vitro along with added heparin (which stabilizes tryptase activity) resulted in the appearance of molecular weight forms indicative of active MMP-3 and MMP-1.	Heparin	92-99	matrix metallopeptidase 1	Homo sapiens	221-226
10512636-14	1999	When incubated with HF and cycloheximide or HF and heparin, the cell growth was inhibited, suggesting that the mechanism of action of HF is similar to that of VEGF.	Heparin	51-58	vascular endothelial growth factor A	Rattus norvegicus	159-163
912599-1	1977	The stereochemical course of in vivo hydrolysis of triacylglycerols by lipoprotein lipase was investigated by determining the structure of diacylglycerol intermediates in postheparin plasma of rats which had been fed [3H]glycerol-labeled Intralipid 2 h before an injection of heparin or had been given an injection of a mixture of [3H]glycerol-Intralipid and heparin.	Heparin	276-283	lipase G, endothelial type	Rattus norvegicus	83-89
579490-6	1977	This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex.	Heparin	139-146	serpin family C member 1	Homo sapiens	201-207
10468144-4	1999	Recent data are reviewed here from clinical trials supporting the use of the specific antithrombin agents in the treatment of acute cardiac ischemic syndromes, the prevention and treatment of venous thromboembolism, and the management of heparin-induced thrombocytopenia.	Heparin	238-245	serpin family C member 1	Homo sapiens	86-98
9805364-2	1998	The polysaccharide, which is regarded as a homopolysaccharide, was 6-fold more antithrombin-active than the heparin standard.	Heparin	108-115	serpin family C member 1	Homo sapiens	79-91
579490-7	1977	These results suggest that acceleration of binding and increased utilization of binding capacity are the two regular effects of heparin on thrombin-involving reactions of AT III.	Heparin	128-135	serpin family C member 1	Homo sapiens	171-177
579490-8	1977	Both of these effects may be abolished by quantitative binding of heparin to thrombin-AT III complex.	Heparin	66-73	serpin family C member 1	Homo sapiens	86-92
9791728-7	1998	Blot overlay assays have shown that perlecan binds alpha-DG in a calcium and heparin-sensitive manner.	Heparin	77-84	heparan sulfate proteoglycan 2 L homeolog	Xenopus laevis	36-44
9759611-3	1998	Heparin infusion, well known to inhibit thrombin generation by fostering antithrombin activity, inhibits the formation of platelet-derived procoagulant microparticles, probably by decreasing the formation of free thrombin, which, under our circumstances, is the main platelet activator.	Heparin	0-7	serpin family C member 1	Homo sapiens	73-85
10465290-8	1999	Furthermore, IGFBP-3, mutated on its heparin-binding domain, was not able to inhibit IGFBP-4 proteolytic degradation.	Heparin	37-44	insulin like growth factor binding protein 3	Homo sapiens	13-20
10465290-9	1999	So, in ovine preovulatory follicles, IGFBP-4 proteolytic degradation both 1) depends on IGFs, and 2) is inhibited by IGFBP-3 via its C-terminal heparin-binding domain as well as by heparin-binding domain containing peptides.	Heparin	144-151	insulin like growth factor binding protein 3	Homo sapiens	117-124
10465290-12	1999	This inhibition might be partly mediated by direct interaction of IGFBP-4 proteinase(s) and heparin-binding domain within the C-terminal region from IGFBP-3 and -5.	Heparin	92-99	insulin like growth factor binding protein 3	Homo sapiens	149-163
10456887-3	1999	The mechanism involves specific bacterial recruitment of heparin, glycosaminoglycans, or related sulfated polysaccharides, which in turn serve as universal binding sites for a diverse array of mammalian heparin binding proteins, including adhesive glycoproteins (vitronectin and fibronectin), inflammatory (MCP-3, PF-4, and MIP-1alpha) and immunomodulatory (gamma interferon) intermediates, and fibroblast growth factor.	Heparin	57-64	C-C motif chemokine ligand 3	Homo sapiens	324-334
579491-2	1977	In the first step of the preparation, using heparin-agarose chromatography, we observed that the complexed form of AT III bound less strongly to the gel than the free form and that about half of the AT III was free.	Heparin	44-51	serpin family C member 1	Homo sapiens	115-121
884118-6	1977	The release of these four histones (H2A, H2B, H3, and H4) is coordinate and occurs in a highly cooperative manner, as indicated by (1) dependence of the initial kinetics of histone removal upon heparin concentration, (2) analysis of DNA and histones in the fractions obtained from differential sedimentation of heparin-treated nuclei, and (3) analysis of the products from heparin-treated nuclei by equilibrium centrifugation in metrizamide density gradients.	Heparin	194-201	H2B clustered histone 21	Homo sapiens	41-56
10614708-7	1999	Ligands of scavenger receptors, which are receptors for oxidized LDL, such as dextran sulphate, polyinosinic acid, heparin and acetylated LDL also significantly induced M-CSF production from human monocytes, although this was at levels below 2 ng/ml.	Heparin	115-122	colony stimulating factor 1	Homo sapiens	169-174
9729296-0	1998	Opposing actions of the EGF family and opioids: heparin binding-epidermal growth factor (HB-EGF) protects mouse cerebellar neuroblasts against the antiproliferative effect of morphine.	Heparin	48-55	heparin-binding EGF-like growth factor	Mus musculus	89-95
884118-6	1977	The release of these four histones (H2A, H2B, H3, and H4) is coordinate and occurs in a highly cooperative manner, as indicated by (1) dependence of the initial kinetics of histone removal upon heparin concentration, (2) analysis of DNA and histones in the fractions obtained from differential sedimentation of heparin-treated nuclei, and (3) analysis of the products from heparin-treated nuclei by equilibrium centrifugation in metrizamide density gradients.	Heparin	311-318	H2B clustered histone 21	Homo sapiens	41-56
9716464-1	1998	Cytochemically detectable activity of endogenous beta-galactosidase was found at pH 6.0 in Swiss 3T3 cells after long-term incubation in low serum or in the presence of heparin concentrations known to reversibly inhibit cell proliferation.	Heparin	169-176	galactosidase, beta 1	Mus musculus	49-67
884004-0	1977	The effect of treatment with clofibrate on hepatic triglyceride and lipoprotein lipase activities of post heparin plasma in male patients with hyperlipoproteinemia.	Heparin	106-113	lipoprotein lipase	Homo sapiens	68-86
9736420-0	1998	Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy.	Heparin	45-52	serpin family C member 1	Homo sapiens	105-117
9736420-0	1998	Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy.	Heparin	72-79	serpin family C member 1	Homo sapiens	105-117
9736420-2	1998	Heparin exerts its function by potentiating antithrombin and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation.	Heparin	0-7	serpin family C member 1	Homo sapiens	44-56
9736420-6	1998	Infusion of UFH, but not subcutaneous LMWH, was found to attenuate the antithrombotic defense by a selective decrease of both circulating antithrombin (-21+/-7%, p&lt;0.0001) and of free and endothelial-bound TFPI.	Heparin	12-15	serpin family C member 1	Homo sapiens	138-150
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Heparin	26-33	insulin-like growth factor binding protein 5	Rattus norvegicus	66-73
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Heparin	26-33	insulin-like growth factor 1	Rattus norvegicus	144-149
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Heparin	26-33	insulin-like growth factor binding protein 5	Rattus norvegicus	257-264
9736420-8	1998	The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis.	Heparin	27-30	serpin family C member 1	Homo sapiens	43-55
884004-4	1977	Post heparin plasma lipoprotein lipase activity isolated and partially purified by heparin Sepharose affinity chromatography was determined quantitatively.	Heparin	5-12	lipoprotein lipase	Homo sapiens	20-38
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Heparin	26-33	insulin-like growth factor 1	Rattus norvegicus	269-274
65284-0	1977	Metabolism of antithrombin III (heparin cofactor) in man: effects of venous thrombosis and of heparin administration.	Heparin	32-39	serpin family C member 1	Homo sapiens	14-30
9642241-0	1998	Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism.	Heparin	17-24	serpin family C member 1	Homo sapiens	42-54
9642241-2	1998	It is believed that heparin accelerates factor Xa (FXa) inactivation by antithrombin (AT) by conformationally activating the inhibitor rather than by bridging AT and FXa in a ternary complex (template effect).	Heparin	20-27	serpin family C member 1	Homo sapiens	72-84
9616153-2	1998	Because the serine proteinase of the natural anticoagulant pathway, activated protein C, can bind heparin, it was reasonable to think that these compounds may also bind protein C (PC) and accelerate its activation by thrombin or other heparin binding plasma serine proteinases by a similar mechanism.	Heparin	98-105	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	78-87
9616153-2	1998	Because the serine proteinase of the natural anticoagulant pathway, activated protein C, can bind heparin, it was reasonable to think that these compounds may also bind protein C (PC) and accelerate its activation by thrombin or other heparin binding plasma serine proteinases by a similar mechanism.	Heparin	98-105	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	169-178
9616153-2	1998	Because the serine proteinase of the natural anticoagulant pathway, activated protein C, can bind heparin, it was reasonable to think that these compounds may also bind protein C (PC) and accelerate its activation by thrombin or other heparin binding plasma serine proteinases by a similar mechanism.	Heparin	98-105	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	180-182
9596664-1	1998	beta2-Glycoprotein I (beta2GPI) is a highly glycosylated plasma protein with the ability to bind negatively charged substances such as DNA, heparin, dextran sulfate, and negatively charged phospholipids.	Heparin	140-147	apolipoprotein H	Homo sapiens	0-20
9596664-1	1998	beta2-Glycoprotein I (beta2GPI) is a highly glycosylated plasma protein with the ability to bind negatively charged substances such as DNA, heparin, dextran sulfate, and negatively charged phospholipids.	Heparin	140-147	apolipoprotein H	Homo sapiens	22-30
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	237-244	coagulation factor III, tissue factor	Homo sapiens	33-35
9765662-11	1998	ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin.	Heparin	10-17	serpin family C member 1	Homo sapiens	93-109
10554832-1	1999	Based on heparin"s antithrombin and anti-FXa activity and its in vitro inhibition of activated factor VII (FVIIa) activity, we hypothesized that unfractionated heparin (UFH) may decrease plasma levels of FVIIa in humans.	Heparin	9-16	serpin family C member 1	Homo sapiens	19-31
10215897-15	1999	273, 7478-7487] for the interaction of heparin-derived oligosaccharides with antithrombin, but with a minor extension: in the first step a low-affinity recognition complex between ligand and receptor is formed, accompanied by a conformational change in the tetrasaccharide, possibly creating a complementary three-dimensional structure to fit the protein-binding site.	Heparin	39-46	serpin family C member 1	Homo sapiens	77-89
10326760-0	1999	Evidence that heparin but not hirudin reduces PAI-1 expression in cultured human endothelial cells.	Heparin	14-21	serpin family E member 1	Homo sapiens	46-51
10326760-2	1999	We have analyzed the effect of unfractionated heparin (UFH) and hirudin on PAI-1 gene expression in human umbilical vein endothelial cells (HUVEC).	Heparin	46-53	serpin family E member 1	Homo sapiens	75-80
10326760-8	1999	The addition of UFH (10 or 100 IU/ml) to endotoxin-stimulated HUVEC also reduced the increased PAI-1 mRNA and antigen secretion (45%), whereas no effect could be observed with hirudin.	Heparin	16-19	serpin family E member 1	Homo sapiens	95-100
9765662-11	1998	ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin.	Heparin	48-55	serpin family C member 1	Homo sapiens	93-109
10326760-9	1999	Our results suggest that UFH, but not hirudin, by reducing the endothelial expression of PAI-1 might have a profibrinolytic effect.	Heparin	25-28	serpin family E member 1	Homo sapiens	89-94
65284-12	1977	In three patients with venous thrombosis not treated with heparin, the turnover of labelled antithrombin III was in the normal range.	Heparin	58-65	serpin family C member 1	Homo sapiens	92-108
65284-14	1977	In one of these patients, the labelled antithrombin III had been incubated with an equimolar amount of heparin prior to injection.	Heparin	103-110	serpin family C member 1	Homo sapiens	39-55
65182-0	1977	Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence.	Heparin	11-18	serpin family C member 1	Homo sapiens	28-44
10466208-4	1999	These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide.	Heparin	32-39	serpin family C member 1	Homo sapiens	66-78
9633525-1	1998	The heparin-binding growth-associated molecule HB-GAM (also named pleiotrophin) and the retinoic acid-induced heparin-binding protein RIHB (chicken midkine) are developmentally regulated proteins forming a new family of heparin-binding molecules with putative functions during cell growth and differentiation.	Heparin	4-11	pleiotrophin	Gallus gallus	47-53
9633525-1	1998	The heparin-binding growth-associated molecule HB-GAM (also named pleiotrophin) and the retinoic acid-induced heparin-binding protein RIHB (chicken midkine) are developmentally regulated proteins forming a new family of heparin-binding molecules with putative functions during cell growth and differentiation.	Heparin	4-11	pleiotrophin	Gallus gallus	66-78
9621946-9	1998	The LPL activity was released by heparin, had a pH optimum of approximately 8.5, was activated by serum, and was inhibited by NaCl and protamine.	Heparin	33-40	lipoprotein lipase	Homo sapiens	4-7
65182-4	1977	The binding of heparin to antithrombin III caused a marked fluorescence enhancement by about 30% of the intrinsic protein emission intensity.	Heparin	15-22	serpin family C member 1	Homo sapiens	26-42
10196134-1	1999	Heparan sulfate N-deacetylase/N-sulfotransferase (HSNST) catalyzes the first and obligatory step in the biosynthesis of heparan sulfates and heparin.	Heparin	141-148	N-deacetylase and N-sulfotransferase 1	Homo sapiens	0-48
65182-6	1977	Heparin fractionated by gel filtration seemed to be bound to two sites on antithrombin III with association constants of 0.6-10(6)m-1 and 0.2-10(6)M-1 respectively.	Heparin	0-7	serpin family C member 1	Homo sapiens	74-90
65182-7	1977	Heparin, prepared by affinity chromatography on matrix-bound antithrombin III appeared to be bound to only one site with an association constant of 2.3-10(6)M-1.	Heparin	0-7	serpin family C member 1	Homo sapiens	61-77
9848182-2	1998	Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated.	Heparin	98-105	serpin family C member 1	Homo sapiens	40-56
836042-0	1977	Small-angle x-ray scattering studies on human antithrombin III and its complex with heparin.	Heparin	84-91	serpin family C member 1	Homo sapiens	46-62
9848182-2	1998	Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated.	Heparin	98-105	serpin family C member 1	Homo sapiens	58-64
9848182-2	1998	Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated.	Heparin	252-259	serpin family C member 1	Homo sapiens	40-56
9848182-2	1998	Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated.	Heparin	252-259	serpin family C member 1	Homo sapiens	58-64
9539494-2	1998	The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex.	Heparin	29-36	serpin family C member 1	Homo sapiens	75-91
9539494-2	1998	The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex.	Heparin	29-36	serpin family C member 1	Homo sapiens	225-241
9640420-0	1998	Lipoprotein lipase mass and activity in post-heparin plasma from subjects with intra-abdominal visceral fat accumulation.	Heparin	45-52	lipoprotein lipase	Homo sapiens	0-18
10082128-0	1999	Identification of a heparin binding site and the biological activities of the laminin alpha1 chain carboxy-terminal globular domain.	Heparin	20-27	laminin subunit alpha 1	Rattus norvegicus	78-92
10082128-1	1999	The carboxy-terminal globular domain (G-domain) of the laminin alpha1 chain has been shown to promote heparin binding, cell adhesion, and neurite outgrowth.	Heparin	102-109	laminin subunit alpha 1	Rattus norvegicus	55-69
10082128-8	1999	These results suggest that peptide LG-6 plays a functional role as a heparin binding site in the G-domain of the laminin alpha1 chain, and this sequence was thus concluded to play a crucial role in regulating cell adhesion and spreading and neurite out-growth which is related to integrin alpha2.	Heparin	69-76	laminin subunit alpha 1	Rattus norvegicus	113-127
10235445-2	1999	In in vitro experiments heparin is able to blunt monocyte TF production by inhibiting TF and cytokine gene expression by stimulated cells and after in vivo administration it reduces adverse ischemic outcomes in UA patients.	Heparin	24-31	coagulation factor III, tissue factor	Homo sapiens	58-60
10235445-2	1999	In in vitro experiments heparin is able to blunt monocyte TF production by inhibiting TF and cytokine gene expression by stimulated cells and after in vivo administration it reduces adverse ischemic outcomes in UA patients.	Heparin	24-31	coagulation factor III, tissue factor	Homo sapiens	86-88
10235445-5	1999	Four h after the heparin injection TF furtherly decreased (176.5 pg/ml, 87.5-321 pg/ml; -32.5%.	Heparin	17-24	coagulation factor III, tissue factor	Homo sapiens	35-37
10235445-9	1999	In conclusion, heparin treatment is associated with a decrease of high TF plasma levels and monocyte procoagulant activity in UA patients.	Heparin	15-22	coagulation factor III, tissue factor	Homo sapiens	71-73
10080889-0	1999	Analysis of heparin, alpha-dystroglycan and sulfatide binding to the G domain of the laminin alpha1 chain by site-directed mutagenesis.	Heparin	12-19	laminin subunit alpha 1	Homo sapiens	85-99
10080889-1	1999	The 395-residue proteolytic fragment E3, which comprises the two most C-terminal LG modules of the mouse laminin alpha1 chain, was previously shown to contain major binding sites for heparin, alpha-dystroglycan and sulfatides.	Heparin	183-190	laminin, alpha 1	Mus musculus	105-119
151469-0	1977	Role of heparin in the interaction of serine proteinases with antithrombin III.	Heparin	8-15	serpin family C member 1	Homo sapiens	62-78
10080889-4	1999	Fragment alpha1LG4-5 bound about five- to tenfold better to heparin, alpha-dystroglycan and sulfatides than E3.	Heparin	60-67	adrenoceptor alpha 1D	Homo sapiens	9-18
10080889-6	1999	Side-chain modifications and proteolysis demonstrated that Lys and Arg residues in the C-terminal region of alpha1LG4 are essential for heparin binding.	Heparin	136-143	adrenoceptor alpha 1D	Homo sapiens	108-117
10037709-1	1999	Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively.	Heparin	29-36	serpin family C member 1	Homo sapiens	244-256
10037709-1	1999	Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively.	Heparin	122-129	serpin family C member 1	Homo sapiens	244-256
10037709-5	1999	In contrast, thrombin is protected from inhibition by a covalent antithrombin-heparin complex, suggesting that access of heparin to exosite 2 of thrombin is hampered when ternary complex formation occurs.	Heparin	78-85	serpin family C member 1	Homo sapiens	65-77
10684486-5	1998	Heparin increased PLT CD62 expression, which was significantly more pronounced in group 1 patients with plasma heparin levels less than 0.7 U/mL and ACT of 222 +/- 52 seconds compared with group 2 patients with heparin levels greater than 0.7 U/mL and ACT of 365 +/- 86 seconds (8 +/- 9 v -1 +/- 4% change in resulting PLTs, P =.01, and 11 +/- 12 v 1 +/- 6% increase in adenosine diphosphate (ADP) [5 microM]-stimulated PLTs, P =.02).	Heparin	111-118	selectin P	Homo sapiens	22-26
10684486-5	1998	Heparin increased PLT CD62 expression, which was significantly more pronounced in group 1 patients with plasma heparin levels less than 0.7 U/mL and ACT of 222 +/- 52 seconds compared with group 2 patients with heparin levels greater than 0.7 U/mL and ACT of 365 +/- 86 seconds (8 +/- 9 v -1 +/- 4% change in resulting PLTs, P =.01, and 11 +/- 12 v 1 +/- 6% increase in adenosine diphosphate (ADP) [5 microM]-stimulated PLTs, P =.02).	Heparin	211-218	selectin P	Homo sapiens	22-26
10684486-7	1998	A strong and statistically significant negative correlation between change in platelet CD62 expression and heparin concentration was observed in group 1 patients (r = -.5, P =.05, -ADP; r = -.65, P =.006, +ADP), whereas this relationship was weak and did not reach statistical significance in group 2 patients (r = -0.4, P =.2, -ADP; r =.11, P = 0.9; +ADP).	Heparin	107-114	selectin P	Homo sapiens	87-91
151469-1	1977	To characterize the mode of action of heparin, the kinetics of inhibition of thrombin, factor Xa, and plasmin by antithrombin III was studied without and in the presence of heparin.	Heparin	38-45	serpin family C member 1	Homo sapiens	113-129
151469-5	1977	Thus, heparin acts obviously as an activator of the enzymes and enhances their affinity for antithrombin III.	Heparin	6-13	serpin family C member 1	Homo sapiens	92-108
9559666-0	1998	Loss of a consensus heparin binding site by alternative splicing of latent transforming growth factor-beta binding protein-1.	Heparin	20-27	latent transforming growth factor beta binding protein 1	Homo sapiens	68-124
9559666-5	1998	The loss of the heparin binding site implies that LTBP-1delta53 will bind to the extracellular matrix less efficiently than LTBP-1.	Heparin	16-23	latent transforming growth factor beta binding protein 1	Homo sapiens	50-56
10026234-8	1999	Double antibody techniques also demonstrated that the heparin binding domain of intraepithelial antithrombin was occupied.	Heparin	54-61	serpin family C member 1	Homo sapiens	96-108
10026234-10	1999	These findings suggest that antithrombin, probably in association with heparin or heparan sulfate, is internalized by renal proximal epithelial cells.	Heparin	71-78	serpin family C member 1	Homo sapiens	28-40
10629396-2	1999	Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin.	Heparin	21-29	serpin family C member 1	Homo sapiens	143-155
10629396-2	1999	Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin.	Heparin	21-28	serpin family C member 1	Homo sapiens	143-155
10629396-2	1999	Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin.	Heparin	68-71	serpin family C member 1	Homo sapiens	143-155
9494108-0	1998	Heparin accelerates the inhibition of cathepsin G by mucus proteinase inhibitor: potent effect of O-butyrylated heparin.	Heparin	0-7	cathepsin G	Homo sapiens	38-49
9494108-1	1998	Heparin tightly binds cathepsin G and so protects the enzyme from inhibition by alpha1-antichymotrypsin, alpha1-proteinase inhibitor and eglin c, three proteins which do not bind heparin [Ermolieff J., Boudier C., Laine A., Meyer B. and Bieth J.G.	Heparin	0-7	cathepsin G	Homo sapiens	22-33
9494108-5	1998	Here we show that heparin no longer protects cathepsin G from inhibition when the enzyme is reacted with mucus proteinase inhibitor (MPI), a heparin-binding protein.	Heparin	18-25	cathepsin G	Homo sapiens	45-56
9494108-5	1998	Here we show that heparin no longer protects cathepsin G from inhibition when the enzyme is reacted with mucus proteinase inhibitor (MPI), a heparin-binding protein.	Heparin	18-25	mannose phosphate isomerase	Homo sapiens	133-136
9494108-6	1998	Heparin fragments of Mr=4500 and 8100 and O-butyrylated heparin of Mr=8000 form tight complexes with cathepsin G (Kd=0.5-2.2 nM) and MPI (Kd=0.	Heparin	0-7	cathepsin G	Homo sapiens	101-112
9494108-6	1998	Heparin fragments of Mr=4500 and 8100 and O-butyrylated heparin of Mr=8000 form tight complexes with cathepsin G (Kd=0.5-2.2 nM) and MPI (Kd=0.	Heparin	0-7	mannose phosphate isomerase	Homo sapiens	133-136
9494108-6	1998	Heparin fragments of Mr=4500 and 8100 and O-butyrylated heparin of Mr=8000 form tight complexes with cathepsin G (Kd=0.5-2.2 nM) and MPI (Kd=0.	Heparin	56-63	cathepsin G	Homo sapiens	101-112
10421704-5	1999	Thus, it appears that dextran derivatives can mimic the action of heparin in regard to its interactions with antithrombin and serine proteases involved in blood coagulation.	Heparin	66-73	serpin family C member 1	Homo sapiens	109-121
9494108-6	1998	Heparin fragments of Mr=4500 and 8100 and O-butyrylated heparin of Mr=8000 form tight complexes with cathepsin G (Kd=0.5-2.2 nM) and MPI (Kd=0.	Heparin	56-63	mannose phosphate isomerase	Homo sapiens	133-136
16544-5	1977	Furthermore, the fall in antithrombin III level then its rise can contribute to the "heparine rebound" occurring in certain cases after neutralization of heparinemia with protamine.	Heparin	85-93	serpin family C member 1	Homo sapiens	25-41
9494108-9	1998	The rate acceleration is due to the binding of heparin to MPI.	Heparin	47-54	mannose phosphate isomerase	Homo sapiens	58-61
9494108-10	1998	Butyrylation of heparin slightly decreases its affinity for cathepsin G and MPI but sharply decreases the ionic interactions between the positively charged proteins and the negatively charged polyanion.	Heparin	16-23	cathepsin G	Homo sapiens	60-79
9494108-11	1998	The butyrylated heparin derivative is the best rate accelerator: it increases the rate constant for the MPI-induced inhibition of cathepsin G and elastase by factors of 26 and 23, respectively.	Heparin	16-23	mannose phosphate isomerase	Homo sapiens	104-107
9494108-11	1998	The butyrylated heparin derivative is the best rate accelerator: it increases the rate constant for the MPI-induced inhibition of cathepsin G and elastase by factors of 26 and 23, respectively.	Heparin	16-23	cathepsin G	Homo sapiens	130-141
21341006-0	1999	Characterization of heparin binding variants of antithrombin by crossed immunoelectrophoresis in the presence of heparin.	Heparin	20-27	serpin family C member 1	Homo sapiens	48-60
21341006-0	1999	Characterization of heparin binding variants of antithrombin by crossed immunoelectrophoresis in the presence of heparin.	Heparin	113-120	serpin family C member 1	Homo sapiens	48-60
21341006-4	1999	Thus, the last update of the antithrombin database listed 11 distinct molecular defects causing heparin binding abnormalities and nine defects having pleiotropic effects interfering with both thrombin inhibitory activity and heparin binding.	Heparin	96-103	serpin family C member 1	Homo sapiens	29-41
21341006-4	1999	Thus, the last update of the antithrombin database listed 11 distinct molecular defects causing heparin binding abnormalities and nine defects having pleiotropic effects interfering with both thrombin inhibitory activity and heparin binding.	Heparin	225-232	serpin family C member 1	Homo sapiens	29-41
830556-0	1977	Interaction of heparin with thrombin and antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	41-57
9570257-8	1998	Compared to untreated colitis the MPO activity in heparin-treated animals was of borderline significance.	Heparin	50-57	myeloperoxidase	Rattus norvegicus	34-37
9622211-1	1998	Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins.	Heparin	19-27	serpin family C member 1	Homo sapiens	69-85
9622211-1	1998	Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins.	Heparin	19-27	serpin family C member 1	Homo sapiens	87-92
9886295-5	1999	We also report that short (14-mer) heparin fragments effectively dimerize NK1 in solution, implying that heparan sulfate chains may stabilize the NK1 dimer.	Heparin	35-42	tachykinin receptor 1	Homo sapiens	74-77
65798-3	1976	Heparin facilitated the complex formation between alpha-thrombin and antithrombin-III, whereas beta-thrombin inactivation was only slightly affected.	Heparin	0-7	serpin family C member 1	Homo sapiens	69-85
9886295-5	1999	We also report that short (14-mer) heparin fragments effectively dimerize NK1 in solution, implying that heparan sulfate chains may stabilize the NK1 dimer.	Heparin	35-42	tachykinin receptor 1	Homo sapiens	146-149
10065896-2	1999	Comparisons were made with a surface modified by endpoint attached heparin, which, like the endothelium, is negatively charged and exposes the specific antithrombin binding sequence and also binds FXII and antithrombin.	Heparin	67-74	serpin family C member 1	Homo sapiens	152-164
10065896-2	1999	Comparisons were made with a surface modified by endpoint attached heparin, which, like the endothelium, is negatively charged and exposes the specific antithrombin binding sequence and also binds FXII and antithrombin.	Heparin	67-74	serpin family C member 1	Homo sapiens	206-218
1008906-4	1976	With heparin-Sepharose 4 B affinity chromatography it was possible to partially purify human adipose tissue lipoprotein lipase (LPL) as well as a lipase from human liver.	Heparin	5-12	lipoprotein lipase	Homo sapiens	108-126
10065896-7	1999	It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa.	Heparin	192-199	serpin family C member 1	Homo sapiens	21-33
10065896-7	1999	It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa.	Heparin	192-199	serpin family C member 1	Homo sapiens	56-68
10065896-7	1999	It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa.	Heparin	192-199	serpin family C member 1	Homo sapiens	56-68
10065896-7	1999	It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa.	Heparin	192-199	serpin family C member 1	Homo sapiens	56-68
10348708-9	1999	TF expression induced by the growth factors was inhibited by heparin (IC 50: 10-30 microg/ml), and other sulfated polysaccharides (IC 50: 1-5 microg/ml).	Heparin	61-68	coagulation factor III, tissue factor	Homo sapiens	0-2
10348708-10	1999	SMCs proliferation, late activation of the extracellular signal-regulated kinases (ERK1/2), and PKC activity were inhibited by heparin (IC 50: 30-50 microg/ml) in SMCs stimulated by FCS but not in SMCs treated by PDGF or EGF.	Heparin	127-134	epidermal growth factor	Homo sapiens	221-224
10348708-12	1999	These results indicate that, besides its well known effect on SMC proliferation, heparin displays an inhibitory effect on cell mediated blood clotting processes through regulation of the TF expression.	Heparin	81-88	coagulation factor III, tissue factor	Homo sapiens	187-189
9856996-9	1998	Thus, ATH reacts directly with thrombin through a bridge mechanism and probably catalyzes the reaction of thrombin with antithrombin by a second binding sequence on its heparin chain.	Heparin	169-176	serpin family C member 1	Homo sapiens	120-132
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	matrix metallopeptidase 1	Homo sapiens	118-144
9551864-1	1998	The heparin-binding growth-associated molecule HB-GAM (also named pleiotrophin) is a developmentally-regulated protein that belongs to a new family of heparin-binding molecules with putative functions during cell growth and differentiation.	Heparin	4-11	pleiotrophin	Gallus gallus	47-53
9551864-1	1998	The heparin-binding growth-associated molecule HB-GAM (also named pleiotrophin) is a developmentally-regulated protein that belongs to a new family of heparin-binding molecules with putative functions during cell growth and differentiation.	Heparin	4-11	pleiotrophin	Gallus gallus	66-78
9451022-3	1998	Under identical experimental conditions the binding of3H-heparin to a recombinant soluble form of the cellular receptor for gp120, CD4, is negligible.	Heparin	56-64	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	124-129
9451022-9	1998	Synthetic 33-35 amino acid peptides based on the sequence of the V3 loop of gp120 also bind to heparin with high affinity.	Heparin	95-102	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	76-81
9451022-12	1998	This study confirms that the V3 loop of gp120 is the site at which heparin exerts its anti-HIV-1 activity.	Heparin	67-74	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	40-45
9443912-5	1998	Two of the mutants (HP1 and HP2) showed greatly decreased (more than 50-fold) affinity for heparin and HSPGs but retained full mitogenic and motogenic activities on target cells in culture.	Heparin	91-98	chromobox 5	Homo sapiens	20-23
9443108-7	1998	The gp120 and gp160 specifically recognize the C-terminal heparin-binding domain of Fn (Fn-CTHBD) with a calculated KD of 2.8 x 10(-7) M for gp160.	Heparin	58-65	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	4-9
9827576-1	1998	Here, we describe the influence of heparin(s) on the interleukin-1-beta (IL-1beta)-induced expression of collagenase (matrix metalloproteinase-1, MMP-1), stromelysin-1 (matrix metalloproteinase-3, MMP-3) and tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in human gingival fibroblasts (HGF).	Heparin	35-42	matrix metallopeptidase 1	Homo sapiens	146-151
1008906-4	1976	With heparin-Sepharose 4 B affinity chromatography it was possible to partially purify human adipose tissue lipoprotein lipase (LPL) as well as a lipase from human liver.	Heparin	5-12	lipoprotein lipase	Homo sapiens	128-131
982357-0	1976	Studies on human plasma antithrombin isolated on heparin gel.	Heparin	49-56	serpin family C member 1	Homo sapiens	24-36
19078327-4	1998	This test measures the ability of heparin, as a cofactor of antithrombin III, to inMbit the catalytic function of factor Xa in plasma.	Heparin	34-41	serpin family C member 1	Homo sapiens	60-76
976270-0	1976	Acceleration of the reaction between thrombin and antithrombin III by non-stoichiometric amounts of heparin.	Heparin	100-107	serpin family C member 1	Homo sapiens	50-66
9812994-7	1998	Heparin-Sepharose chromatography demonstrated that HL-LPLC1 and HL-LPLC2 eluted at 0.80 and 1.3 M NaCl, respectively, elution positions that corresponded to native HL and LPL.	Heparin	0-7	lipoprotein lipase	Homo sapiens	54-57
9812994-8	1998	Hence, substitution of LPL sequences into the HL carboxyl-terminal domain resulted in the production of functional lipases, but with distinct heparin binding properties.	Heparin	142-149	lipoprotein lipase	Homo sapiens	23-26
9610759-11	1998	It is concluded that surface-immobilized heparin, unlike heparin in solution, effectively inhibits the initial contact activation enzymes by an antithrombin-mediated mechanism, thereby suppressing the triggering of the intrinsic plasma coagulation pathway.	Heparin	41-48	serpin family C member 1	Homo sapiens	144-156
9426203-1	1997	HB-EGF is a heparin-binding member of the EGF family that was initially identified in the conditioned medium of human macrophages.	Heparin	12-19	heparin binding EGF like growth factor	Homo sapiens	0-6
9813019-3	1998	Second order rate constants for inhibition in the absence of heparin were 1.57 x 10(3) and 0.91 x 10(3) M-1 s-1 for C1-INH and ATIII, respectively.	Heparin	61-68	serpin family C member 1	Homo sapiens	127-132
976270-1	1976	The accelerating effect of heparin on the reaction between purified human antithrombin and thrombin has been investigated by measuring the amount of thrombin inactivated during a short incubation of the enzyme with the inhibitor in the presence and absence of non-stoichiometric amounts of heparin.	Heparin	27-34	serpin family C member 1	Homo sapiens	74-86
9813019-4	1998	Therapeutic heparin concentrations (0.1-1.0 units/ml) enhanced inhibition by ATIII 20-55-fold compared with 0.1-7.0-fold for C1-INH.	Heparin	12-19	serpin family C member 1	Homo sapiens	77-82
9813019-11	1998	Inhibition of FXIa by ATIII in the presence of heparin was decreased 4-fold by alanine substitution at Lys253 (A253), with smaller effects noted for mutants A255 and A252.	Heparin	47-54	serpin family C member 1	Homo sapiens	22-27
956344-2	1976	The activity of the activated form of the enzyme, measured as heparin elutable LPL, was lower in hypothyroid patients (1.54 +/- 0.93; mU/10(6) cells; mean +/- SD) than in controls (3.26 +/- 1.49; P less than .02) and increased (163 +/- 89%; P less than .01) with treatment to levels comparable to the controls.	Heparin	62-69	lipoprotein lipase	Homo sapiens	79-82
9813019-18	1998	The data indicate that FXI/XIa must bind to heparin for optimal inhibition by ATIII and for autoactivation.	Heparin	44-51	serpin family C member 1	Homo sapiens	78-83
9813026-4	1998	A small effect was seen for PN1/heparin inhibition of the exosite-I mutants R35Q, R67Q, R73Q, R75Q, and R77(a)Q, where kon values were decreased 2-4-fold, compared with rIIa.	Heparin	32-39	serpin family E member 2	Homo sapiens	28-31
9813026-4	1998	A small effect was seen for PN1/heparin inhibition of the exosite-I mutants R35Q, R67Q, R73Q, R75Q, and R77(a)Q, where kon values were decreased 2-4-fold, compared with rIIa.	Heparin	32-39	protein kinase cAMP-dependent type I regulatory subunit alpha	Rattus norvegicus	169-173
9813026-9	1998	PN1 bound to heparin uses exosite-I to some extent, possibly by utilizing the positive electrostatic field of exosite-I to enhance orientation and thrombin complex formation.	Heparin	13-20	serpin family E member 2	Homo sapiens	0-3
9811888-4	1998	Mutated hLPL was expressed only in muscle and led to 3,100 and 3,500 ng/ml homodimeric hLPL protein in post-heparin plasma but no hLPL catalytic activity.	Heparin	108-115	lipoprotein lipase	Homo sapiens	8-12
9811888-4	1998	Mutated hLPL was expressed only in muscle and led to 3,100 and 3,500 ng/ml homodimeric hLPL protein in post-heparin plasma but no hLPL catalytic activity.	Heparin	108-115	lipoprotein lipase	Homo sapiens	87-91
9811888-4	1998	Mutated hLPL was expressed only in muscle and led to 3,100 and 3,500 ng/ml homodimeric hLPL protein in post-heparin plasma but no hLPL catalytic activity.	Heparin	108-115	lipoprotein lipase	Homo sapiens	87-91
9435678-6	1997	Because heparin inhibited MC binding of 125I-IGFBP-5, we tested the heparin binding peptide, IGFBP-5-(201-218), for stimulatory activity.	Heparin	8-15	insulin-like growth factor binding protein 5	Rattus norvegicus	45-52
9435678-6	1997	Because heparin inhibited MC binding of 125I-IGFBP-5, we tested the heparin binding peptide, IGFBP-5-(201-218), for stimulatory activity.	Heparin	68-75	insulin-like growth factor binding protein 5	Rattus norvegicus	93-100
9435678-7	1997	IGFBP-5-(201-218) stimulated MC migration, and this effect was inhibited by heparin.	Heparin	76-83	insulin-like growth factor binding protein 5	Rattus norvegicus	0-7
9359845-1	1997	Human lactoferrin (hLF), a protein involved in host defence against infection and excessive inflammation, interacts with heparin, the lipid A moiety of bacterial lipopolysaccharide, human lysozyme (hLZ) and DNA.	Heparin	121-128	HLF transcription factor, PAR bZIP family member	Homo sapiens	19-22
9359845-3	1997	Iron-saturated and natural hLF bound equally well to heparin, lipid A, hLZ and DNA.	Heparin	53-60	HLF transcription factor, PAR bZIP family member	Homo sapiens	27-30
9359845-4	1997	Natural hLF lacking the first two N-terminal amino acids (Gly1-Arg2) showed reactivities of one-half, two-thirds, one-third and one-third towards heparin, lipid A, hLZ and DNA respectively compared with N-terminally intact hLF.	Heparin	146-153	HLF transcription factor, PAR bZIP family member	Homo sapiens	8-11
9359845-8	1997	These results show that the N-terminal stretch of four consecutive arginine residues, Arg2-Arg3-Arg4-Arg5, has a decisive role in the interaction of hLF with heparin, lipid A, hLZ and DNA.	Heparin	158-165	HLF transcription factor, PAR bZIP family member	Homo sapiens	149-152
9359850-5	1997	Among three isoforms of VEGF, the mRNA of a short form (VEGF120) lacking heparin-binding activity was preferentially increased after cold exposure and treatment with the adrenergic agonists.	Heparin	73-80	vascular endothelial growth factor A	Rattus norvegicus	24-28
9792674-3	1998	MCP-1 showed binding to [3H]heparin with a KD of 1.5 microM.	Heparin	28-35	C-C motif chemokine ligand 2	Homo sapiens	0-5
9792674-4	1998	We substituted lysine or histidine residues at the C-terminal end of MCP-1 with alanine residues and tested these mutants for their ability to bind heparin, heparan sulfate, hyaluronic acid, and chondroitin sulfate-C.	Heparin	148-155	C-C motif chemokine ligand 2	Homo sapiens	69-74
956344-5	1976	These increases in PHLA correlated with the increases in the activity of heparin elutable LPL (r = .88, P less than .05).	Heparin	73-80	lipoprotein lipase	Homo sapiens	90-93
9410906-1	1997	Amphiregulin (AR) is a heparin-binding, heparin-inhibited member of the epidermal growth factor (EGF) family and an autocrine growth factor for human keratinocytes.	Heparin	40-47	epidermal growth factor	Homo sapiens	72-95
956344-7	1976	Serial determination of heparin elutable LPL activity, PHLA, and plasma TG during L-thyroxine treatment revealed a correlation between the per cent changes in PHLA and heparin elutable LPL activity (r = .68, P less than .05), an inverse correlation between plasma TG levels and heparin elutable LPL (r = -0.53,P less than .05) and no correlation between plasma TG and PHLA (r = -0.05).	Heparin	24-31	lipoprotein lipase	Homo sapiens	41-44
956344-7	1976	Serial determination of heparin elutable LPL activity, PHLA, and plasma TG during L-thyroxine treatment revealed a correlation between the per cent changes in PHLA and heparin elutable LPL activity (r = .68, P less than .05), an inverse correlation between plasma TG levels and heparin elutable LPL (r = -0.53,P less than .05) and no correlation between plasma TG and PHLA (r = -0.05).	Heparin	168-175	lipoprotein lipase	Homo sapiens	185-188
10101569-4	1998	This phenomenon of heparin resistance was postulated to be due to consumption of circulating antithrombin III as a result of prior heparinisation.	Heparin	19-26	serpin family C member 1	Homo sapiens	93-109
956344-7	1976	Serial determination of heparin elutable LPL activity, PHLA, and plasma TG during L-thyroxine treatment revealed a correlation between the per cent changes in PHLA and heparin elutable LPL activity (r = .68, P less than .05), an inverse correlation between plasma TG levels and heparin elutable LPL (r = -0.53,P less than .05) and no correlation between plasma TG and PHLA (r = -0.05).	Heparin	168-175	lipoprotein lipase	Homo sapiens	185-188
956344-7	1976	Serial determination of heparin elutable LPL activity, PHLA, and plasma TG during L-thyroxine treatment revealed a correlation between the per cent changes in PHLA and heparin elutable LPL activity (r = .68, P less than .05), an inverse correlation between plasma TG levels and heparin elutable LPL (r = -0.53,P less than .05) and no correlation between plasma TG and PHLA (r = -0.05).	Heparin	168-175	lipoprotein lipase	Homo sapiens	185-188
956344-7	1976	Serial determination of heparin elutable LPL activity, PHLA, and plasma TG during L-thyroxine treatment revealed a correlation between the per cent changes in PHLA and heparin elutable LPL activity (r = .68, P less than .05), an inverse correlation between plasma TG levels and heparin elutable LPL (r = -0.53,P less than .05) and no correlation between plasma TG and PHLA (r = -0.05).	Heparin	168-175	lipoprotein lipase	Homo sapiens	185-188
9802760-3	1998	Plasma LPL mass in post-heparin plasma and plasma vWF antigen were quantified by sandwich-enzyme immunoassay and enzyme-linked immunosorbent assay, respectively.	Heparin	24-31	lipoprotein lipase	Homo sapiens	7-10
9391721-2	1997	Binding competition assays of plasminogen and uPA to heparin-sepharose demonstrated that heparin bound to both enzymes.	Heparin	53-60	plasminogen activator, urokinase	Mus musculus	46-49
9391721-2	1997	Binding competition assays of plasminogen and uPA to heparin-sepharose demonstrated that heparin bound to both enzymes.	Heparin	89-96	plasminogen activator, urokinase	Mus musculus	46-49
9802760-5	1998	Heparin-releasable LPL mass was significantly lower in the microalbuminuric than in the normoalbuminuric subjects.	Heparin	0-7	lipoprotein lipase	Homo sapiens	19-22
184224-9	1976	The complete inhibition of triglyceride removal by an antiserum prepared against adipose tissue LPL demonstrates that the NaCl-inhibited, serum-activated lipase prepared by affinity chromatography on heparin-Sepharose and concanavalin A-Sepharose columns is the enzyme responsible in vivo for the catabolism of VLDL triglyceride.	Heparin	200-207	lipoprotein lipase	Oryctolagus cuniculus	96-99
9855818-5	1998	Furthermore, alpha-thrombin-induced DNA synthesis could be inhibited by antithrombin III (2 units/ml) with heparin (2 units/ml) or D-Phe-Pro-ArgCH2Cl (50 micrograms/ml).	Heparin	107-114	serpin family C member 1	Homo sapiens	72-88
9799799-6	1998	The 1.17 Schwann cells demonstrated heparin-releasable lipolytic activity that was inhibited by the lipase inhibitor tetrahydrolipstatin in a dose-dependent manner.	Heparin	36-43	lipase G, endothelial type	Rattus norvegicus	100-106
9988527-3	1998	The peptide containing the sequence Phe-Ser-Trp-Ser-Asp-Trp-Trp-Ser (residues 388-395 in lipoprotein lipase, which include the consensus TSP type I sequence) showed strong binding to heparin.	Heparin	183-190	lipoprotein lipase	Homo sapiens	89-107
9988527-9	1998	The present study confirms the presence of specific heparin-binding sites in LPL.	Heparin	52-59	lipoprotein lipase	Homo sapiens	77-80
9391721-3	1997	Moreover, in the presence of increasing amounts of heparin, plasminogen activation mediated by uPA occurred as a bell-shaped curve, suggesting the formation of a ternary complex.	Heparin	51-58	plasminogen activator, urokinase	Mus musculus	95-98
9391721-4	1997	In contrast, all chemically-modified heparins lacked this cofactor activity, although N-des and heparan sulfate partially retained the uPA binding capacity, and O-des partially bound to both plasminogen and uPA.	Heparin	37-45	plasminogen activator, urokinase	Mus musculus	207-210
9391721-5	1997	Plasmatic euglobulins from mice treated with heparin, as well as with modified heparins with uPA binding capacity, presented a 2-fold enhancement of 47 kDa lytic band, as assessed by zymographic analysis.	Heparin	79-87	plasminogen activator, urokinase	Mus musculus	93-96
9391721-7	1997	These results suggest that the profibrinolytic activity of heparin mediated by uPA could be caused by an increase in uPA protein levels rather than by a cofactor activity mediated by a formation of ternary complexes.	Heparin	59-66	plasminogen activator, urokinase	Mus musculus	79-82
9391721-7	1997	These results suggest that the profibrinolytic activity of heparin mediated by uPA could be caused by an increase in uPA protein levels rather than by a cofactor activity mediated by a formation of ternary complexes.	Heparin	59-66	plasminogen activator, urokinase	Mus musculus	117-120
9429077-3	1997	In this study, the EGF-like growth factor was detected immunohistochemically in a variety of human skin samples by indirect immunofluorescence using a polyclonal rabbit antiserum raised against residues 26-41 of mature heparin-binding EGF.	Heparin	219-226	epidermal growth factor	Homo sapiens	19-22
9429077-7	1997	Immunoreactive heparin-binding EGF was characteristically associated with the surface of cells.	Heparin	15-22	epidermal growth factor	Homo sapiens	31-34
9429077-8	1997	With minor exceptions, the immunoreactive sites are identical to the known EGF receptor distribution in the skin, and suggest that keratinocyte-derived heparin-binding EGF may act in concert with other EGF family members in processes such as skin morphogenesis and wound repair, as well as in the development of skin cancers.	Heparin	152-159	epidermal growth factor	Homo sapiens	75-78
9429077-8	1997	With minor exceptions, the immunoreactive sites are identical to the known EGF receptor distribution in the skin, and suggest that keratinocyte-derived heparin-binding EGF may act in concert with other EGF family members in processes such as skin morphogenesis and wound repair, as well as in the development of skin cancers.	Heparin	152-159	epidermal growth factor	Homo sapiens	168-171
9429077-8	1997	With minor exceptions, the immunoreactive sites are identical to the known EGF receptor distribution in the skin, and suggest that keratinocyte-derived heparin-binding EGF may act in concert with other EGF family members in processes such as skin morphogenesis and wound repair, as well as in the development of skin cancers.	Heparin	152-159	epidermal growth factor	Homo sapiens	168-171
9742130-3	1998	Unlike the other members of the CCN gene family, rCop-1 is not an immediate-early gene, it lacks the conserved C-terminal domain which was shown to confer both growth-stimulating and heparin-binding activities, and its expression is lost in cells transformed by a variety of mechanisms.	Heparin	183-190	COP1, E3 ubiquitin ligase	Rattus norvegicus	49-55
1278547-3	1976	Hovewer, on the 7th--9th day after removal of the spleen, when the ACS function is thoroughly depressed, the 30-min immobilization stress decreases the plasma anticoagulating activity and, to a certain extent, restricts the appearance of the heparin complex compounds.	Heparin	242-249	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	67-70
9784842-0	1998	Purification of heparin-binding protein HBp17 and identification of HBp17 heparin binding site.	Heparin	16-23	fibroblast growth factor binding protein 1	Homo sapiens	40-45
9784842-0	1998	Purification of heparin-binding protein HBp17 and identification of HBp17 heparin binding site.	Heparin	16-23	fibroblast growth factor binding protein 1	Homo sapiens	68-73
9784842-1	1998	HBp17 was purified by Heparin-Copper biaffinity chromatography and HPLC from conditioned medium of A431 cell.	Heparin	22-29	fibroblast growth factor binding protein 1	Homo sapiens	0-5
9350282-9	1997	The glycosaminoglycans heparan sulfate and heparin, which bind SAP, reduced SAPs binding to the virus.	Heparin	43-50	amyloid P component, serum	Homo sapiens	63-66
55783-9	1976	The intra-operative fall in antithrombin-III activity was prevented by a small preoperative dose of subcutaneous heparin.	Heparin	113-120	serpin family C member 1	Homo sapiens	28-44
9329410-8	1997	However, the use of heparin was associated with a lower antithrombin III activity level.	Heparin	20-27	serpin family C member 1	Homo sapiens	56-72
9784842-2	1998	The purified HBp17 was digested by staphylococcus urcus V8 protease or chymotrypsin and the heparin-binding fragments were isolated by Heparin-Sepharose.	Heparin	92-99	fibroblast growth factor binding protein 1	Homo sapiens	13-18
9784842-2	1998	The purified HBp17 was digested by staphylococcus urcus V8 protease or chymotrypsin and the heparin-binding fragments were isolated by Heparin-Sepharose.	Heparin	135-142	fibroblast growth factor binding protein 1	Homo sapiens	13-18
9784842-6	1998	Therefore the residues 110-143 of HBp17 are the principle heparin binding site.	Heparin	58-65	fibroblast growth factor binding protein 1	Homo sapiens	34-39
9784842-7	1998	The basic amino acid cluster in this region may be contribute to the binding of HBp17 to heparin or heparan sulfate proteoglycan on the cell surface and extracellular matrix.	Heparin	89-96	fibroblast growth factor binding protein 1	Homo sapiens	80-85
1253531-8	1976	The effect of changes in nutritional status on the activity of clearing factor lipase in rat post-heparin plasma depends on the heparin dosage used.	Heparin	98-105	lipase G, endothelial type	Rattus norvegicus	79-85
9688635-0	1998	Plasminogen binds the heparin-binding domain of insulin-like growth factor-binding protein-3.	Heparin	22-29	insulin like growth factor binding protein 3	Homo sapiens	48-92
9242619-0	1997	Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity.	Heparin	0-7	serpin family C member 1	Homo sapiens	66-78
9242619-0	1997	Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity.	Heparin	106-113	serpin family C member 1	Homo sapiens	66-78
1253531-8	1976	The effect of changes in nutritional status on the activity of clearing factor lipase in rat post-heparin plasma depends on the heparin dosage used.	Heparin	128-135	lipase G, endothelial type	Rattus norvegicus	79-85
9247347-3	1997	APTT was significantly prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III.	Heparin	82-89	serpin family C member 1	Homo sapiens	93-109
9301108-2	1997	Antithrombin activity appeared in this product was 6.5 times higher than that of standard heparin.	Heparin	90-97	serpin family C member 1	Homo sapiens	0-12
9671710-0	1998	Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin.	Heparin	172-179	peroxiredoxin 5	Homo sapiens	6-27
9712292-7	1998	We found a clear relationship between the antithrombin binding capacity and the antithrombogenic potential of the heparin-coated stents.	Heparin	114-121	serpin family C member 1	Homo sapiens	42-54
9777198-0	1998	[Effect of the synthetic heparin antagonist--quaternary ammonium salt of 25-conidine oligomer on the regeneration of liver injured by CCl4].	Heparin	25-32	C-C motif chemokine ligand 4	Homo sapiens	134-138
942661-2	1976	An acute intravenous injection of heparin produced the following changes in enzyme activities: in serum, phospholipase and lipase were increased, cholesterol esterase unchanged; in tissues phospholipase was increased, lipase was increased in heart and liver but decreased in aorta, cholesterol esterase was increased in heart but decreased in liver and aorta.	Heparin	34-41	carboxyl ester lipase	Homo sapiens	146-166
1194266-5	1975	This activated species is added to purified antithrombin-heparin cofactor and the interaction is studied in the presence and absence of heparin.	Heparin	57-64	serpin family C member 1	Homo sapiens	44-56
9742689-6	1998	The present results warn that the formation of the C-2 epimerized compound has to be circumvented in the structural analysis of heparin/heparan sulfate.	Heparin	128-135	complement C2	Homo sapiens	51-54
9218427-5	1997	TGF-beta2.alpha2-macroglobulin complexes are more refractory to heparin/heparan sulfate, and those involving TGF-beta3 cannot be affected.	Heparin	64-71	alpha-2-macroglobulin	Homo sapiens	10-30
1194266-7	1975	The addition of heparin dramatically accelerates the rate of this interaction with virtually complete inhibition of Factor IXa occurring within 15 s. Sodium dodecyl sulfate gel electrophoresis of reduced and nonreduced proteins indicates that antithrombin-heparin cofactor functions as a potent inhibitor of Factor IXa by forming an undissociable complex with the enzyme which is stable in the presence of denaturing or reducing agents (or both).	Heparin	16-23	serpin family C member 1	Homo sapiens	243-255
9692925-1	1998	We have isolated the collagenase/gelatinase activity of fibronectin from a bovine lens capsule hydrolysate, using heparin-agarose, gelatin-agarose, immunopurification with polyclonal antibodies directed against bovine plasma fibronectin, and immunopurification with a monoclonal antibody directed against the extra-domain A of cellular fibronectin.	Heparin	114-121	fibronectin 1	Bos taurus	56-67
9202242-12	1997	Heparin and heparan sulfate inhibited the IGFBP-5/PAI-1 interaction; however, several other glycosaminoglycans had no effect.	Heparin	0-7	serpin family E member 1	Homo sapiens	50-55
1201144-1	1975	A method for the assay of lipoprotein lipase activity (LPLA) in heparin eluates of needle biopsies of adipose tissue is presented.	Heparin	64-71	lipoprotein lipase	Homo sapiens	26-44
9632653-4	1998	On this basis, the glutathione S-transferase (GST)-TatR49/52/53/55/56/57A mutant, in which six arginine residues within the basic domain of Tat were mutagenized to alanine residues, was compared with GST-Tat for its capacity to bind immobilized heparin.	Heparin	245-252	glutathione S-transferase kappa 1	Homo sapiens	46-49
9632653-5	1998	Dissociation of the GST-TatR49/52/53/55/56/57A.heparin complex occurred at ionic strength significantly lower than that required to dissociate the GST-Tat.heparin complex.	Heparin	47-54	glutathione S-transferase kappa 1	Homo sapiens	20-23
9632653-5	1998	Dissociation of the GST-TatR49/52/53/55/56/57A.heparin complex occurred at ionic strength significantly lower than that required to dissociate the GST-Tat.heparin complex.	Heparin	47-54	glutathione S-transferase kappa 1	Homo sapiens	147-150
9632653-5	1998	Dissociation of the GST-TatR49/52/53/55/56/57A.heparin complex occurred at ionic strength significantly lower than that required to dissociate the GST-Tat.heparin complex.	Heparin	155-162	glutathione S-transferase kappa 1	Homo sapiens	20-23
9632653-5	1998	Dissociation of the GST-TatR49/52/53/55/56/57A.heparin complex occurred at ionic strength significantly lower than that required to dissociate the GST-Tat.heparin complex.	Heparin	155-162	glutathione S-transferase kappa 1	Homo sapiens	147-150
9632653-6	1998	Accordingly, heparin binds immobilized GST-Tat and GST-TatR49/52/53/55/56/57A with a dissociation constant equal to 0.3 and 1.0 microM, respectively.	Heparin	13-20	glutathione S-transferase kappa 1	Homo sapiens	39-42
9254059-7	1997	Co-incubation of HTG-VLDL + LPL with heparin, heparinase, or heparitinase, blocked CE accumulation by 70%, 48%, and 95%, respectively, but had no effect on the increase in cellular TG.	Heparin	37-44	lipoprotein lipase	Homo sapiens	28-31
1201147-1	1975	Rat heart lipoprotein lipase was highly purified by affinity chromatography using heparin-Sepharose 4B.	Heparin	82-89	lipase G, endothelial type	Rattus norvegicus	22-28
9632653-6	1998	Accordingly, heparin binds immobilized GST-Tat and GST-TatR49/52/53/55/56/57A with a dissociation constant equal to 0.3 and 1.0 microM, respectively.	Heparin	13-20	glutathione S-transferase kappa 1	Homo sapiens	51-54
9632653-7	1998	Also, the synthetic basic domain Tat-(41-60) competes with GST-Tat for heparin binding.	Heparin	71-78	glutathione S-transferase kappa 1	Homo sapiens	59-62
1201147-7	1975	In studying the purified enzyme we observed: (i) a cofactor in serum was required for full enzymatic activity; ApoLp-Glu could be substituted for this cofactor; (ii) ApoLp-Ser was inhibitory to lipase activity; (iii) NaCl and protamine sulfate also markedly inhibited the lipase activity; (iv) heparin stimulated the enzymatic activity.	Heparin	294-301	lipase G, endothelial type	Rattus norvegicus	194-200
9223556-4	1997	In contrast to the commonly used nonanticoagulant analog N-desulfated, N-reacetylated heparin, selectively O-desulfated heparin retains potent activity as an inhibitor of the cationic neutrophil proteases human leukocyte elastase and cathepsin G, both in vitro and in vivo.	Heparin	86-93	cathepsin G	Homo sapiens	234-245
9223556-4	1997	In contrast to the commonly used nonanticoagulant analog N-desulfated, N-reacetylated heparin, selectively O-desulfated heparin retains potent activity as an inhibitor of the cationic neutrophil proteases human leukocyte elastase and cathepsin G, both in vitro and in vivo.	Heparin	120-127	cathepsin G	Homo sapiens	234-245
1188792-0	1975	Proceedings: A method for the quantitative determination of the antithrombin III (AT III) activity in plasma and serum using the complex formation with heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	64-80
9168236-8	1997	In the present study we demonstrate that heparin largely reduces Suc-HSA activity on HIV replication in the same concentration in which if affects binding of Suc-HSA to the envelope protein gp120 and in particular its V3 domain.	Heparin	41-48	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	190-195
9636139-5	1998	Using affinity coelectrophoresis, we found heparin to bind as follows: to type I collagen with high affinity (Kd approximately 150 nM); triple-helical peptides (THPs) including the basic N-terminal sequence alpha1(I)87-92, KGHRGF, with intermediate affinities (Kd approximately 2 microM); and THPs including other collagenous sequences, or single-stranded sequences, negligibly (Kd &gt;&gt; 10 microM).	Heparin	43-50	adrenoceptor alpha 1D	Homo sapiens	207-221
9616153-5	1998	With TM containing chondroitin sulfate, heparin did not influence PC activation by thrombin, but with TM lacking chondroitin sulfate, the characteristic high-affinity PC interaction at low Ca2+ (approximately 50 to 100 micromol/L) was largely eliminated by heparin.	Heparin	257-264	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	167-169
9616153-6	1998	In EDTA, heparin enhanced thrombin activation of GDPC by reducing the Km, but it inhibited PC activation by increasing the Km.	Heparin	9-16	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	51-53
9616153-8	1998	These results suggest that, when the Gla-domain of PC is not fully stabilized by Ca2+, it interacts with the anion binding exosite 2 of thrombin and that heparin binding to this site prevents this interaction.	Heparin	154-161	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	51-53
9616153-9	1998	Additional studies indicated that, in the presence of phospholipid vesicles, heparin and dextran sulfate dramatically accelerate PC activation by fXa by also reducing the Km.	Heparin	77-84	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	129-131
9674734-0	1998	Differential effect of unfractionated heparin and low molecular weight heparin on intravascular tissue factor pathway inhibitor: evidence for a difference in antithrombotic action.	Heparin	38-45	coagulation factor III, tissue factor	Homo sapiens	96-109
9674734-0	1998	Differential effect of unfractionated heparin and low molecular weight heparin on intravascular tissue factor pathway inhibitor: evidence for a difference in antithrombotic action.	Heparin	71-78	coagulation factor III, tissue factor	Homo sapiens	96-109
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	150-157	coagulation factor III, tissue factor	Homo sapiens	64-77
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	150-157	coagulation factor III, tissue factor	Homo sapiens	33-35
9674734-1	1998	Tissue factor pathway inhibitor (TFPI) is a potent inhibitor of tissue factor (TF)-induced blood coagulation, which is increased several-fold in post-heparin plasma and thought to contribute significantly to the antithrombotic action of heparin.	Heparin	237-244	coagulation factor III, tissue factor	Homo sapiens	64-77
9645599-9	1998	The heparin-induced inhibition of IL-8 binding and chemotactic responses was reversed in a dose-dependent manner in the presence of alpha2-macroglobulin.	Heparin	4-11	alpha-2-macroglobulin	Homo sapiens	132-152
9169007-0	1997	Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity.	Heparin	72-79	serpin family C member 1	Homo sapiens	56-68
9169007-1	1997	Two major glycoforms of recombinant antithrombin which differ 10-fold in their affinity for the effector glycosaminoglycan, heparin, were previously shown to be expressed in BHK or CHO mammalian cell lines (I. Bjork, et al., 1992, Biochem.	Heparin	124-131	serpin family C member 1	Homo sapiens	36-48
9169007-8	1997	Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form.	Heparin	0-7	serpin family C member 1	Homo sapiens	43-55
9169007-8	1997	Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form.	Heparin	152-159	serpin family C member 1	Homo sapiens	43-55
9169007-10	1997	Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity.	Heparin	12-19	serpin family C member 1	Homo sapiens	226-238
9169007-10	1997	Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity.	Heparin	42-49	serpin family C member 1	Homo sapiens	226-238
9169007-10	1997	Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity.	Heparin	42-49	serpin family C member 1	Homo sapiens	226-238
9169007-10	1997	Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity.	Heparin	42-49	serpin family C member 1	Homo sapiens	226-238
9169007-11	1997	The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin.	Heparin	14-21	serpin family C member 1	Homo sapiens	173-185
9169007-11	1997	The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin.	Heparin	126-133	serpin family C member 1	Homo sapiens	173-185
9169007-13	1997	These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.	Heparin	97-104	serpin family C member 1	Homo sapiens	67-79
9169007-13	1997	These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.	Heparin	97-104	serpin family C member 1	Homo sapiens	221-233
9548562-3	1998	Secreted HB-EGF-AP bound to heparin and exhibited potent growth factor activity.	Heparin	28-35	heparin binding EGF like growth factor	Homo sapiens	9-15
1188792-0	1975	Proceedings: A method for the quantitative determination of the antithrombin III (AT III) activity in plasma and serum using the complex formation with heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	82-88
1188833-0	1975	Proceedings: Effect of heparin on antithrombin III activity during delivery and early puerperium.	Heparin	23-30	serpin family C member 1	Homo sapiens	34-50
21235930-2	1998	PAI-1 also binds to other nonproteinase ligands, including the matrix protein vitronectin, glycosaminoglycans such as heparin, and the endocytic clearance receptor, the low-density-lipoprotein-receptor-related protein (LRP).	Heparin	118-125	serpin family E member 1	Homo sapiens	0-5
9662467-9	1998	Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans.	Heparin	0-7	serpin family C member 1	Homo sapiens	45-57
9662467-9	1998	Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans.	Heparin	114-121	serpin family C member 1	Homo sapiens	45-57
9147040-0	1997	A unique trisaccharide sequence in heparin mediates the early step of antithrombin III activation.	Heparin	35-42	serpin family C member 1	Homo sapiens	70-86
9119887-5	1997	Heparin inhibited FGF2-stimulated epithelial cell growth but also basal myoepithelial cell proliferation and this inhibition could be overcome by the addition of EGF.	Heparin	0-7	epidermal growth factor	Homo sapiens	162-165
9119887-7	1997	This suggests the possibility of an autocrine role for a heparin-binding member of the EGF family in the growth of myoepithelial cells.	Heparin	57-64	epidermal growth factor	Homo sapiens	87-90
9135573-15	1997	Our results with heparin also suggest that the binding sites on IGFBP-3 for IGF-I and IGF-II are not completely identical.	Heparin	17-24	insulin like growth factor 2	Homo sapiens	86-92
1170899-2	1975	Inactivation of Ts-thrombin by antithrombin-III was facilitated with heparin, whereas inactivation of Tp-thrombin was not.	Heparin	69-76	serpin family C member 1	Homo sapiens	31-47
1090031-0	1975	The effect of major surgery, low doses of heparin and thromboembolism on plasma antithrombin.	Heparin	42-49	serpin family C member 1	Homo sapiens	80-92
9149438-0	1997	Exogenous heparin induces fibronectin overexpression parallel to angiogenesis in the extracellular matrix of the chick embryo chorioallantoic membrane.	Heparin	10-17	fibronectin 1	Gallus gallus	26-37
9149438-3	1997	Data to be presented show a close relationship between HE treatment, angiogenic processes, and overexpression of FN, but not of type IV collagen in CAM extracellular matrix.	Heparin	55-57	fibronectin 1	Gallus gallus	113-115
9516447-4	1998	Rapid kinetic studies revealed that elimination of the reducing-end disaccharide marginally affected binding to the native low-heparin-affinity conformational state of antithrombin but greatly affected the conversion of the serpin to the activated high-heparin- affinity state, although the activated conformation was still favored.	Heparin	127-134	serpin family C member 1	Homo sapiens	168-180
9516447-6	1998	These results demonstrate that the nonreducing-end residues of the pentasaccharide function both to recognize the native low-heparin-affinity conformation of antithrombin and to induce and stabilize the activated high-heparin-affinity conformation.	Heparin	125-132	serpin family C member 1	Homo sapiens	158-170
9516447-6	1998	These results demonstrate that the nonreducing-end residues of the pentasaccharide function both to recognize the native low-heparin-affinity conformation of antithrombin and to induce and stabilize the activated high-heparin-affinity conformation.	Heparin	218-225	serpin family C member 1	Homo sapiens	158-170
4151-2	1975	An inactive state of the phospholipase A2 exists : when rats are injected with heparin, their plasma membranes contain a very low phospholipase A2 activity.	Heparin	79-86	phospholipase A2 group IB	Rattus norvegicus	25-41
9497365-6	1998	Finally, mutagenesis of PAI-1 results in loss of LRP binding, confirming that the high affinity binding site is located on PAI-1 and suggesting that the LRP binding site lays within a region of PAI-1 previously shown to contain the heparin binding domain.	Heparin	232-239	serpin family E member 1	Homo sapiens	24-29
9164169-1	1997	Heparin salt ITF 1300 in which low molecular weight heparin is salified with a new counterion, di-[3-(N,N-dibutylamino)]propyl carbonate (ITF 188), was selected for the pharmacological development.	Heparin	52-59	trefoil factor 3	Canis lupus familiaris	13-16
4151-2	1975	An inactive state of the phospholipase A2 exists : when rats are injected with heparin, their plasma membranes contain a very low phospholipase A2 activity.	Heparin	79-86	phospholipase A2 group IB	Rattus norvegicus	130-146
4698271-0	1973	Effects of acidic phospholipids, nucleotides, and heparin on the activity of lipase from rat liver lysosomes.	Heparin	50-57	lipase G, endothelial type	Rattus norvegicus	77-83
9076381-3	1997	The effects of heparin may be partly counteracted by a decrease in antithrombin (III).	Heparin	15-22	serpin family C member 1	Homo sapiens	67-79
9559894-11	1998	Heparin, an inhibitor of betaARK, significantly reduced the magnitude and rate of desensitization, whereas Rp-cyclic AMPS and PKI (14-24)amide, inhibitors of cyclic AMP-dependent protein kinase (PKA), or long-term treatment with phorbol 12-myristate 13-acetate to induce down-regulation of protein kinase C (PKC) had no significant effect.	Heparin	0-7	G protein-coupled receptor kinase 2	Mus musculus	25-32
4693499-0	1973	Reversible binding of lipoprotein lipase from hen adipose tissue to insolubilized heparin.	Heparin	82-89	lipoprotein lipase	Homo sapiens	22-40
9546238-8	1998	RESULTS: Heparin inhibited sustained activity of mitogen-activated protein kinase kinase-1 and mitogen-activated protein kinase and prevented DNA synthesis induced by thrombin, angiotensin II, endothelin-1, and lysophosphatidic acid.	Heparin	9-16	dual specificity mitogen-activated protein kinase kinase 1	Papio anubis	49-90
9546238-8	1998	RESULTS: Heparin inhibited sustained activity of mitogen-activated protein kinase kinase-1 and mitogen-activated protein kinase and prevented DNA synthesis induced by thrombin, angiotensin II, endothelin-1, and lysophosphatidic acid.	Heparin	9-16	endothelin-1	Papio anubis	193-205
5124541-5	1971	Increasing the concentration of heparin in the incubation system caused a gradual decrease in FFA release by postheparin plasma and increases in activity of heart homogenates and adipose tissue lipoprotein lipase.	Heparin	32-39	lipoprotein lipase	Homo sapiens	194-212
9541411-0	1998	The N-terminal segment of antithrombin acts as a steric gate for the binding of heparin.	Heparin	80-87	serpin family C member 1	Homo sapiens	26-38
9541411-1	1998	The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa.	Heparin	15-22	serpin family C member 1	Homo sapiens	57-69
9541411-1	1998	The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa.	Heparin	91-98	serpin family C member 1	Homo sapiens	57-69
9541411-2	1998	The areas of antithrombin involved in binding heparin and stabilizing the interaction in the high-affinity form have been partially resolved through the study of both recombinant and natural variants.	Heparin	46-53	serpin family C member 1	Homo sapiens	13-25
9079763-9	1997	Moreover, an ability of the shorter IE180 variants to bind heparin was also revealed in the study.	Heparin	59-66	transcriptional regulator ICP4	Suid alphaherpesvirus 1	36-41
9131716-0	1997	Effects of heparin coating on the expression of CD11b, CD11c and CD62L by leucocytes in extracorporeal circulation in vitro.	Heparin	11-18	selectin L	Homo sapiens	65-70
9131716-6	1997	Heparin coating reduced the increase in CD11b and CD11c on granulocytes (p &lt; 0.02 at 2 h), but the delayed increase in CD11c on monocytes and the delayed downregulation of CD62L on granulocytes and monocytes did not reach statistical significance.	Heparin	0-7	selectin L	Homo sapiens	175-180
9541411-3	1998	The role of a section of the N-terminal segment of antithrombin, residues 22-46 (segment 22-46), in heparin binding was investigated using rapid kinetic analysis of the protein cleaved at residues 29-30 by limited proteolysis with thermolysin.	Heparin	100-107	serpin family C member 1	Homo sapiens	51-63
9541411-4	1998	The cleaved antithrombin had 5.5-fold lowered affinity for heparin pentasaccharide and 1.8-fold for full-length, high-affinity heparin.	Heparin	59-66	serpin family C member 1	Homo sapiens	12-24
9541411-6	1998	This implies that the segment constituting residues 22-46 in the N terminus of antithrombin hinders access to the binding site for heparin, hence the increased initial binding for the cleaved form, whereas, when heparin is bound, segment 22-46 is involved in the stabilization of the binding interaction, as indicated by the increased dissociation constant.	Heparin	131-138	serpin family C member 1	Homo sapiens	79-91
9541411-6	1998	This implies that the segment constituting residues 22-46 in the N terminus of antithrombin hinders access to the binding site for heparin, hence the increased initial binding for the cleaved form, whereas, when heparin is bound, segment 22-46 is involved in the stabilization of the binding interaction, as indicated by the increased dissociation constant.	Heparin	212-219	serpin family C member 1	Homo sapiens	79-91
9541411-7	1998	When the heparin pentasaccharide is bound to antithrombin prior to incubation with thermolysin, it protects the N-terminal cleavage site, implying that segment 22-46 moves to interact with heparin in the conformational change and thus stabilizes the complex.	Heparin	9-16	serpin family C member 1	Homo sapiens	45-57
9540793-5	1998	Consistent with studies on lipoprotein lipase, the denatured rHL eluted from heparin-Sepharose at a lower salt concentration of 0.42 M NaCl than the native rHL which eluted at 0.72 M NaCl.	Heparin	77-84	hes family bHLH transcription factor 1	Rattus norvegicus	61-64
9038197-4	1997	In addition to binding to alpha2MR/LRP, LpL-(313-448) displayed binding to heparin with an affinity similar to that of the LpL monomer, whereas it bound poorly to lipoprotein particles.	Heparin	75-82	lipoprotein lipase	Homo sapiens	40-43
9038197-6	1997	LpL-(313-448) and LpL-(347-448) showed similar affinities for binding to both purified alpha2MR/LRP and to heparin.	Heparin	107-114	lipoprotein lipase	Homo sapiens	0-3
9038197-6	1997	LpL-(313-448) and LpL-(347-448) showed similar affinities for binding to both purified alpha2MR/LRP and to heparin.	Heparin	107-114	lipoprotein lipase	Homo sapiens	18-21
9038197-9	1997	We conclude that the C-terminal folding domain of human LpL has a site for binding to heparin and to HSPG, presumably involving amino acids within residues 404-430.	Heparin	86-93	lipoprotein lipase	Homo sapiens	56-59
9067613-0	1997	The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site.	Heparin	77-84	serpin family C member 1	Homo sapiens	23-35
9211051-1	1997	Heparin, the most widely used antithrombin, suffers several limitations, including high inter-individual variability of anticoagulant response, a nonlinear dose-response curve, inability to inactivate clot-bound thrombin, a requirement for endogenous cofactors and inactivation by platelet factor 4 and heparinase.	Heparin	0-7	serpin family C member 1	Homo sapiens	30-42
9466983-8	1998	Analysis of defined heparin fragment pools shows a size dependence for interaction, with tetradecasaccharides showing easily detectable binding to L- and P-selectin affinity columns.	Heparin	20-27	selectin P	Homo sapiens	154-164
5549162-0	1971	[Heparin-dependency of lipoprotein lipase in idiopathic hyperlipidemia].	Heparin	1-8	lipoprotein lipase	Homo sapiens	23-41
9466983-12	1998	Notably, P- and L-selectin binding to sialyl-Lewisx and to HL-60 cells (which are known to carry the native ligand PSGL-1) is inhibited by unfractionated pharmaceutical heparin preparations at concentrations 12-50-fold lower than those recommended for effective anticoagulation in vivo.	Heparin	169-176	selectin L	Homo sapiens	16-26
9466983-12	1998	Notably, P- and L-selectin binding to sialyl-Lewisx and to HL-60 cells (which are known to carry the native ligand PSGL-1) is inhibited by unfractionated pharmaceutical heparin preparations at concentrations 12-50-fold lower than those recommended for effective anticoagulation in vivo.	Heparin	169-176	selectin P ligand	Homo sapiens	115-121
9466983-14	1998	Thus, patients undergoing heparin therapy for other reasons may be experiencing clinically significant inhibition of L- and P-selectin function, and the current switchover to low-molecular weight heparins may come at some loss of this effect.	Heparin	26-33	selectin P	Homo sapiens	124-134
9466983-15	1998	Low-dose unfractionated heparin should be investigated as a treatment option for acute and chronic diseases in which P- and L-selectin play pathological roles.	Heparin	24-31	selectin L	Homo sapiens	124-134
9518874-5	1998	Both EGF and transforming growth factor-alpha (TGF-alpha) significantly (P &lt; 0.001) increased DNA synthesis in the presence of heparin.	Heparin	130-137	protransforming growth factor alpha	Ovis aries	13-45
9518874-5	1998	Both EGF and transforming growth factor-alpha (TGF-alpha) significantly (P &lt; 0.001) increased DNA synthesis in the presence of heparin.	Heparin	130-137	protransforming growth factor alpha	Ovis aries	47-56
9518874-6	1998	The effect of TGF-alpha was dose-related, wholly reversing the inhibitory effect of heparin in cell cultures from non-pregnant and 20-week pregnant sheep.	Heparin	84-91	protransforming growth factor alpha	Ovis aries	14-23
9013976-6	1997	Binding of C1q to CSPG was competitively inhibited by free glycosaminoglycans (GAG) in the order dextran sulfate &gt; heparin &gt; heparan sulfate &gt; chondroitin-6-sulfate (CS-C) &gt; dermatan sulfate (CS-B) &gt; chondroitin-4-sulfate (CS-A).	Heparin	118-125	complement C1q A chain	Homo sapiens	11-14
5520720-0	1970	[Lipoprotein lipase activity following heparin infusion.	Heparin	39-46	lipoprotein lipase	Homo sapiens	1-19
9058497-5	1997	In the presence of heparin, AT was bound to the FVIIa/TF complex in a dose-dependent manner with ka of 2 x 10(3) M-1 s-1.	Heparin	19-26	coagulation factor III, tissue factor	Homo sapiens	54-56
9518874-9	1998	In the presence of heparin, TGF-alpha showed synergistic interactions with insulin or IGF-I.	Heparin	19-26	protransforming growth factor alpha	Ovis aries	28-37
9507993-6	1998	Heparin administration released lipoprotein lipase (LPL) and hepatic lipase (HL) activities after 20 min, and significantly reduced apoB-48 concentrations in d &lt; 1.006 g/mL fractions only.	Heparin	0-7	lipoprotein lipase	Homo sapiens	32-50
9507993-6	1998	Heparin administration released lipoprotein lipase (LPL) and hepatic lipase (HL) activities after 20 min, and significantly reduced apoB-48 concentrations in d &lt; 1.006 g/mL fractions only.	Heparin	0-7	lipoprotein lipase	Homo sapiens	52-55
9507993-9	1998	When little LPL was released (LPL activity &lt; 120 mU/mL) by heparin, apoB-48 was preferentially eliminated over apoB-100.	Heparin	62-69	lipoprotein lipase	Homo sapiens	12-15
9507993-9	1998	When little LPL was released (LPL activity &lt; 120 mU/mL) by heparin, apoB-48 was preferentially eliminated over apoB-100.	Heparin	62-69	lipoprotein lipase	Homo sapiens	30-33
4166629-0	1967	Interaction of heparin with the plasma proteins in relation to its antithrombin activity.	Heparin	15-22	serpin family C member 1	Homo sapiens	67-79
9446566-3	1998	The basic carboxyl-terminal region of IGFBP-3 was required for binding to heparin.	Heparin	74-81	insulin like growth factor binding protein 3	Homo sapiens	38-45
9462526-6	1998	UFH in patients with unstable angina increased the percentage of circulating platelets positive to PAC-1 from 2.7+/-1.7% to 4.4+/-3.4% (P&lt;.05) and to CD62 from 1.6+/-0.9% to 2.7+/-1.5% (P&lt;.01).	Heparin	0-3	ADCYAP receptor type I	Homo sapiens	99-104
9018048-7	1997	The cofactor heparin compensated partially for the loss of interactions with Ser195; it increased the affinity of S195A for protease nexin-1 and antithrombin by 140-fold and 1000-fold, respectively.	Heparin	13-20	serpin family C member 1	Homo sapiens	145-157
9291586-2	1997	Experiments using animal and models suggest that heparin-binding epidermal growth factor-like growth factor (HB-EGF) is important for endometrial receptivity, and that it may directly mediate blastocyst implantation We have investigated the expression of HB-EGF mRNA and protein in pregnant and nonpregnant human endometrium and placenta.	Heparin	49-56	heparin binding EGF like growth factor	Homo sapiens	109-115
9291586-2	1997	Experiments using animal and models suggest that heparin-binding epidermal growth factor-like growth factor (HB-EGF) is important for endometrial receptivity, and that it may directly mediate blastocyst implantation We have investigated the expression of HB-EGF mRNA and protein in pregnant and nonpregnant human endometrium and placenta.	Heparin	49-56	heparin binding EGF like growth factor	Homo sapiens	255-261
9868079-4	1997	Low molecular weight heparin (LMWH) prolonged significantly PT and APTT, and this effect ws weakened by an antibody against human AT III.	Heparin	21-28	serpin family C member 1	Homo sapiens	130-136
9462526-6	1998	UFH in patients with unstable angina increased the percentage of circulating platelets positive to PAC-1 from 2.7+/-1.7% to 4.4+/-3.4% (P&lt;.05) and to CD62 from 1.6+/-0.9% to 2.7+/-1.5% (P&lt;.01).	Heparin	0-3	selectin P	Homo sapiens	153-157
9442018-6	1998	The latter has not been reported to date for heparin/heparan sulfate, indicating the substrate specificity of the D-glucuronyl C-5 epimerase.	Heparin	45-52	glucuronic acid epimerase	Homo sapiens	114-140
5984659-0	1966	[Changes in lipoprotein lipase activity in patients with coronary atherosclerosis under the action of therapy with small doses of heparin].	Heparin	130-137	lipoprotein lipase	Homo sapiens	12-30
9839374-4	1998	As a drug AT III is separated from blood preparations by bioselective sorption on sorbents containing heparine as a complementary ligand interacting with AT III molecules.	Heparin	102-110	serpin family C member 1	Homo sapiens	10-16
9839374-4	1998	As a drug AT III is separated from blood preparations by bioselective sorption on sorbents containing heparine as a complementary ligand interacting with AT III molecules.	Heparin	102-110	serpin family C member 1	Homo sapiens	154-160
9574332-2	1997	In a prospective randomised trial, a new automatic pen for subcutaneous injections of low molecular heparin was studied with 489 injections in 51 patients.	Heparin	100-107	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	51-54
9574332-3	1997	The automatic pen with a covered needle allows a safe and standardised subcutaneous administration of low-molecular heparin with good patient comfort and at no additional costs.	Heparin	116-123	proprotein convertase subtilisin/kexin type 1 inhibitor	Homo sapiens	14-17
13135008-0	1953	[Antithrombin action of heparin; role of fibrinogen and of heparin concentration].	Heparin	24-31	serpin family C member 1	Homo sapiens	1-13
9069450-13	1997	ApoB, apoC-III, apoC-III in heparin-manganese precipitate (reflecting apoC-III in VLDL and LDL) and apoE decreased significantly by 21, 18, 26 and 49%, respectively.	Heparin	28-35	apolipoprotein C3	Homo sapiens	16-24
9069450-13	1997	ApoB, apoC-III, apoC-III in heparin-manganese precipitate (reflecting apoC-III in VLDL and LDL) and apoE decreased significantly by 21, 18, 26 and 49%, respectively.	Heparin	28-35	apolipoprotein C3	Homo sapiens	16-24
9422575-12	1998	The KGF-stimulated tumor cell growth was almost completely inhibited by heparin or epidermal growth factor (EGF).	Heparin	72-79	fibroblast growth factor 7	Mus musculus	4-7
34050242-5	2021	Islets were kept intact or dispersed into single cells and cultured in the presence of harmine, glucose, or heparin-binding epidermal growth factor-like growth factor (HB-EGF), and subsequently analyzed by immunohistochemistry or flow cytometry.	Heparin	108-115	heparin binding EGF like growth factor	Homo sapiens	168-174
9459343-13	1998	Unfractionated heparin infused through a mixing device proximal to the perfusion chamber to obtain plasma concentrations of 0.5, 1 and 3 IU/ml, reduced fibrin deposition on TF-coated coverslips in a dose-dependent manner (77% reduction at 3 IU/ml, p &lt;0.01), but had no significant effect on platelet deposition (33% at 3 IU/ml, p &gt;0.05).	Heparin	15-22	coagulation factor III, tissue factor	Homo sapiens	173-175
9489430-11	1997	We observed that incubation of basophils with heparin inhibits histamine release as shown in the table: [table: see text] Preincubation of anti-IgE or MCAF/MCP-I with heparin did not induce any changes in histamine release.	Heparin	46-53	C-C motif chemokine ligand 2	Homo sapiens	151-155
9489430-11	1997	We observed that incubation of basophils with heparin inhibits histamine release as shown in the table: [table: see text] Preincubation of anti-IgE or MCAF/MCP-I with heparin did not induce any changes in histamine release.	Heparin	167-174	C-C motif chemokine ligand 2	Homo sapiens	151-155
9003378-0	1996	Lactoferrin regulates the activity of heparin proteoglycan-bound mast cell chymase: characterization of the binding of heparin to lactoferrin.	Heparin	38-45	lactotransferrin	Rattus norvegicus	0-11
9003378-5	1996	LF proved to decrease the activity of heparin PG-associated RMCP-1, although a portion of the enzyme activity was resistant to regulation.	Heparin	38-45	lactotransferrin	Rattus norvegicus	0-2
34047020-0	2021	Unfractionated heparin reduces hepcidin levels in critically ill patients.	Heparin	15-22	hepcidin antimicrobial peptide	Homo sapiens	31-39
9003378-8	1996	The interaction of LF with heparin was characterized.	Heparin	27-34	lactotransferrin	Rattus norvegicus	19-21
9062695-2	1996	In this work it is shown that heparin, fucose-branched chondroitin sulfate and dextran sulfate 8000 promote a shift of the H(+)-ATPase optimum pH from 6.0 to 7.0.	Heparin	30-37	ATPase	Zea mays	128-134
9398631-6	1997	Heparin and a peptide encompassing the high-affinity heparin-binding site in the C-terminal portion of IGFBP-3 were capable of blocking the multimerization of IGFBP-3.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	103-110
9398631-6	1997	Heparin and a peptide encompassing the high-affinity heparin-binding site in the C-terminal portion of IGFBP-3 were capable of blocking the multimerization of IGFBP-3.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	159-166
9398631-6	1997	Heparin and a peptide encompassing the high-affinity heparin-binding site in the C-terminal portion of IGFBP-3 were capable of blocking the multimerization of IGFBP-3.	Heparin	53-60	insulin like growth factor binding protein 3	Homo sapiens	103-110
9398631-6	1997	Heparin and a peptide encompassing the high-affinity heparin-binding site in the C-terminal portion of IGFBP-3 were capable of blocking the multimerization of IGFBP-3.	Heparin	53-60	insulin like growth factor binding protein 3	Homo sapiens	159-166
9398631-8	1997	The self-association of IGFBP-3 required the high-affinity heparin-binding site in the C-terminal portion of the molecule.	Heparin	59-66	insulin like growth factor binding protein 3	Homo sapiens	24-31
34047020-1	2021	A strong anti-hepcidin activity has been observed in heparins.	Heparin	53-61	hepcidin antimicrobial peptide	Homo sapiens	14-22
9354625-9	1997	The endothelial cell binding sites for IL-8, RANTES, and MCP-1 were deduced to be glycosaminoglycans since competition assays showed the biphasic curves and micromolar IC50 values seen in studies with immobilized heparin, and mRNA for known chemokine receptors was not detected.	Heparin	213-220	C-C motif chemokine ligand 2	Homo sapiens	57-62
34047020-2	2021	Mean hepcidin levels were significantly reduced compared to baseline, following the first day of unfractionated heparin administration in critically patients.	Heparin	112-119	hepcidin antimicrobial peptide	Homo sapiens	5-13
9526947-6	1997	Abciximab, YM 337, and SR 121566A were each found to inhibit platelet microparticle formation and P-selectin expression in whole blood, in response to heparin-induced thrombocytopenia positive serum/heparin.	Heparin	151-158	selectin P	Homo sapiens	98-108
9029353-7	1996	Heparin plus Ca stimulated a greater internalization of Ca2+ than did Ca alone for retentate from bovine follicular fluid, oviductal cell culture, and BSA treatments: glucose consistently and significantly reduced internalization.	Heparin	0-7	albumin	Bos taurus	151-154
8910598-0	1996	Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin.	Heparin	39-46	serpin family C member 1	Homo sapiens	76-88
8910598-1	1996	The binding of heparin to antithrombin greatly accelerates the rate of inhibition of the target proteinases thrombin and factor Xa.	Heparin	15-22	serpin family C member 1	Homo sapiens	26-38
8910598-2	1996	Acceleration of the rate of inhibition of factor Xa involves a conformational change in antithrombin that is translated from the heparin binding site to the reactive center loop.	Heparin	129-136	serpin family C member 1	Homo sapiens	88-100
8910598-3	1996	A mechanism has been proposed for generation and propagation of the conformational change in which the binding of the negatively charged heparin reduces ionic repulsions between positively charged residues on and adjacent to the D-helix in the heparin binding site of antithrombin (van Boeckel, C. A.	Heparin	137-144	serpin family C member 1	Homo sapiens	268-280
8910598-3	1996	A mechanism has been proposed for generation and propagation of the conformational change in which the binding of the negatively charged heparin reduces ionic repulsions between positively charged residues on and adjacent to the D-helix in the heparin binding site of antithrombin (van Boeckel, C. A.	Heparin	244-251	serpin family C member 1	Homo sapiens	268-280
9328841-5	1997	In addition, heparan sulfate drastically inhibited [125I]DCN binding to solid-phase adsorbed TSP (80% inhibition), suggesting that DCN could bind to the N-terminal domain of TSP through interaction with heparin-binding sequences.	Heparin	203-210	decorin	Homo sapiens	57-60
9328841-5	1997	In addition, heparan sulfate drastically inhibited [125I]DCN binding to solid-phase adsorbed TSP (80% inhibition), suggesting that DCN could bind to the N-terminal domain of TSP through interaction with heparin-binding sequences.	Heparin	203-210	decorin	Homo sapiens	131-134
9328841-7	1997	[125I]DCN interacted only with peptides VDAVRTEKGFLLLASLRQMKKTRGT and KKTRGTLLALERKDHS containing the heparin-binding consensus sequence KKTR.	Heparin	102-109	decorin	Homo sapiens	6-9
34047020-3	2021	Heparin displayed a strong independent negative association with hepcidin.	Heparin	0-7	hepcidin antimicrobial peptide	Homo sapiens	65-73
33610598-4	2021	Anti-hepcidin effect of heparin-iron was detected in HepG2 cell and LPS induced acute inflammation mice by qRT-PCR and ELISA.	Heparin	24-31	hepcidin antimicrobial peptide	Homo sapiens	5-13
9296400-0	1997	Antithrombin III during cardiac surgery: effect on response of activated clotting time to heparin and relationship to markers of hemostatic activation.	Heparin	90-97	serpin family C member 1	Homo sapiens	0-16
9296400-1	1997	UNLABELLED: This study was designed to determine if, and to what extent, antithrombin III (AT) levels affect the response of the activated clotting time (ACT) to heparin in concentrations used during cardiac surgery, and to characterize the relationship between AT levels and markers of activation of coagulation during cardiopulmonary bypass (CPB).	Heparin	162-169	serpin family C member 1	Homo sapiens	73-89
8936596-1	1996	A new method of polyethylene glycol precipitation followed by heparin affinity chromatography was established to purify apolioprotein H (Apo H, beta 2-glycoprotein I).	Heparin	62-69	apolipoprotein H	Homo sapiens	120-135
33662819-2	2021	Reinforced hydrogels containing both Vascular Endothelial Growth Factor (VEGF) and Platelet-derived Growth Factor (PDGF) were prepared by crosslinking chemically modified hyaluronic acid and heparin with poly(ethylene glycol)-diacrylate around a reinforcing silk mesh.	Heparin	191-198	vascular endothelial growth factor A	Rattus norvegicus	73-77
8849730-5	1996	Here we show that non-phosphorylated recombinant tau isoforms with three microtubule-binding repeats form paired helical-like filaments under physiological conditions in vitro, when incubated with sulphated glycosaminoglycans such as heparin or heparan sulphate.	Heparin	234-241	microtubule associated protein tau	Homo sapiens	49-52
8849730-6	1996	Furthermore, heparin prevents tau from binding to microtubules and promotes microtubule disassembly.	Heparin	13-20	microtubule associated protein tau	Homo sapiens	30-33
8849730-8	1996	These findings, with previous studies which show that heparin stimulates tau phosphorylation by a number of protein kinases, indicate that sulphated glycosaminoglycans may be a key factor in the formation of the neurofibrillary lesions of Alzheimer"s disease.	Heparin	54-61	microtubule associated protein tau	Homo sapiens	73-76
9288875-8	1997	In other clinical applications, heparin decreases antithrombin activity and causes intracircuit clot formation during extracorporeal circulation when the polymorphonuclear granulocyte elastase level is very high.	Heparin	32-39	serpin family C member 1	Homo sapiens	50-62
9288875-9	1997	The antithrombin activity shows less decrease when argatroban is substituted for heparin.	Heparin	81-88	serpin family C member 1	Homo sapiens	4-16
9305203-2	1997	Specifically, we hypothesized that patients with heterozygous C4A null phenotype (A0BB), who have decreased amounts of C4A, may have increased complement activation because of reduced clearance of heparin-protamine complexes.	Heparin	197-204	complement C4A (Rodgers blood group)	Homo sapiens	62-65
9305203-8	1997	Patients with heterozygous C4A null allele had significantly increased plasma levels of C4a after protamine neutralization of heparin (C4a of 2862 +/- 375 ng/ml; mean +/- standard error of the mean) when compared with patients with normal expression of C4 alleles (AABB) (C4a of 1580 +/- 141 ng/ml) or heterozygous C4B null allele (C4a 1526 +/- 208 ng/ml).	Heparin	126-133	complement C4A (Rodgers blood group)	Homo sapiens	27-30
9305203-8	1997	Patients with heterozygous C4A null allele had significantly increased plasma levels of C4a after protamine neutralization of heparin (C4a of 2862 +/- 375 ng/ml; mean +/- standard error of the mean) when compared with patients with normal expression of C4 alleles (AABB) (C4a of 1580 +/- 141 ng/ml) or heterozygous C4B null allele (C4a 1526 +/- 208 ng/ml).	Heparin	126-133	complement C4A (Rodgers blood group)	Homo sapiens	88-91
32536326-0	2021	Application of goal-directed therapy for the use of concentrated antithrombin for heparin resistance during cardiac surgery.	Heparin	82-89	serpin family C member 1	Homo sapiens	65-77
9305203-10	1997	CONCLUSIONS: Patients with heterozygous C4A null phenotype have increased complement activation by heparin-protamine complexes during cardiac operations, possibly because of their defective clearance.	Heparin	99-106	complement C4A (Rodgers blood group)	Homo sapiens	40-43
8828497-4	1996	Previous studies showed that heparin inhibited IGFBP-3 binding to the cell surface and increased its accumulation in the medium, suggesting that it might act as a competitive inhibitor of IGFBP-3 binding to structurally similar heparan sulfate proteoglycans on the cell surface.	Heparin	29-36	insulin like growth factor binding protein 3	Homo sapiens	47-54
8828497-4	1996	Previous studies showed that heparin inhibited IGFBP-3 binding to the cell surface and increased its accumulation in the medium, suggesting that it might act as a competitive inhibitor of IGFBP-3 binding to structurally similar heparan sulfate proteoglycans on the cell surface.	Heparin	29-36	insulin like growth factor binding protein 3	Homo sapiens	188-195
8828497-5	1996	We evaluated this hypothesis by binding 125I-labeled recombinant glycosylated human IGFBP-3 to human fetal skin fibroblasts (GM-10) and to C6 rat glioma cells at 12 C. Heparin inhibited [125I]IGFBP-3 binding more effectively than chondroitin sulfate and dextran sulfate.	Heparin	168-175	insulin like growth factor binding protein 3	Homo sapiens	84-91
8828497-5	1996	We evaluated this hypothesis by binding 125I-labeled recombinant glycosylated human IGFBP-3 to human fetal skin fibroblasts (GM-10) and to C6 rat glioma cells at 12 C. Heparin inhibited [125I]IGFBP-3 binding more effectively than chondroitin sulfate and dextran sulfate.	Heparin	168-175	insulin like growth factor binding protein 3	Homo sapiens	192-199
8828497-8	1996	These results suggested that IGFBP-3 did not bind to heparan sulfate glycosaminoglycans on the cell surface, and that the inhibition of IGFBP-3 binding by heparin most likely resulted from its direct interaction with the heparin-binding domains of IGFBP-3.	Heparin	155-162	insulin like growth factor binding protein 3	Homo sapiens	29-36
8828497-8	1996	These results suggested that IGFBP-3 did not bind to heparan sulfate glycosaminoglycans on the cell surface, and that the inhibition of IGFBP-3 binding by heparin most likely resulted from its direct interaction with the heparin-binding domains of IGFBP-3.	Heparin	155-162	insulin like growth factor binding protein 3	Homo sapiens	136-143
8828497-8	1996	These results suggested that IGFBP-3 did not bind to heparan sulfate glycosaminoglycans on the cell surface, and that the inhibition of IGFBP-3 binding by heparin most likely resulted from its direct interaction with the heparin-binding domains of IGFBP-3.	Heparin	155-162	insulin like growth factor binding protein 3	Homo sapiens	136-143
8828497-11	1996	These results suggest that direct interaction of heparin or IGF-I with IGFBP-3 inhibits its ability to bind to the surface of GM-10 fibroblasts and C6 glioma cells.	Heparin	49-56	insulin like growth factor binding protein 3	Homo sapiens	71-78
9300039-11	1997	Moreover the enzyme was found to be highly resistant to heparin, a potent inhibitor of casein kinase II (CK II) and also resistant to CK I-7, a synthetic inhibitor of CK I, but very sensitive to a bioflavonoid quercetin.	Heparin	56-63	casein kinase 2 alpha 1	Homo sapiens	87-103
9300039-11	1997	Moreover the enzyme was found to be highly resistant to heparin, a potent inhibitor of casein kinase II (CK II) and also resistant to CK I-7, a synthetic inhibitor of CK I, but very sensitive to a bioflavonoid quercetin.	Heparin	56-63	casein kinase 2 alpha 1	Homo sapiens	105-110
9300039-11	1997	Moreover the enzyme was found to be highly resistant to heparin, a potent inhibitor of casein kinase II (CK II) and also resistant to CK I-7, a synthetic inhibitor of CK I, but very sensitive to a bioflavonoid quercetin.	Heparin	56-63	choline kinase alpha	Homo sapiens	105-109
9300039-11	1997	Moreover the enzyme was found to be highly resistant to heparin, a potent inhibitor of casein kinase II (CK II) and also resistant to CK I-7, a synthetic inhibitor of CK I, but very sensitive to a bioflavonoid quercetin.	Heparin	56-63	choline kinase alpha	Homo sapiens	134-138
9300824-3	1997	Like normal HB-EGF, SF HB-EGF contains the signal peptide, the propeptide, the heparin-binding domain and the first two conservative disulfide loops of the EGF unit.	Heparin	79-86	heparin binding EGF like growth factor	Homo sapiens	23-29
8810923-0	1996	Interaction of lipoprotein lipase with heparin fragments and with heparan sulfate: stoichiometry, stabilization, and kinetics.	Heparin	39-46	lipoprotein lipase	Homo sapiens	15-33
8810923-1	1996	The interaction of lipoprotein lipase (LPL) with heparan sulfate and with size-fractionated fragments of heparin was characterized by several approaches (stabilization, sedimentation, surface plasmon resonance, circular dichroism, fluorescence).	Heparin	105-112	lipoprotein lipase	Homo sapiens	19-37
32536326-3	2021	The purpose of this study was to evaluate a goal-directed approach for the use of antithrombin in patients who were resistant to heparin.	Heparin	129-136	serpin family C member 1	Homo sapiens	82-94
8810923-1	1996	The interaction of lipoprotein lipase (LPL) with heparan sulfate and with size-fractionated fragments of heparin was characterized by several approaches (stabilization, sedimentation, surface plasmon resonance, circular dichroism, fluorescence).	Heparin	105-112	lipoprotein lipase	Homo sapiens	39-42
9258408-6	1997	Heparin, a strong inhibitor of HUASMC proliferation, strongly down-modulated the levels of cyclin D1 mRNA and protein, cdk2 mRNA and cdc2 protein.	Heparin	0-7	cyclin dependent kinase 1	Homo sapiens	133-137
8810923-2	1996	The results show that heparin decasaccharides form a 1:1 complex with dimeric LPL and that decasaccharides are the shortest heparin fragments which can completely satisfy the heparin binding regions in dimeric LPL.	Heparin	22-29	lipoprotein lipase	Homo sapiens	78-81
32536326-5	2021	A goal-directed protocol for antithrombin was established based upon heparin dosing (400 IU kg-1 body weight) and achieving an activated clotting time of >=500 seconds prior to cardiopulmonary bypass.	Heparin	69-76	serpin family C member 1	Homo sapiens	29-41
8810923-2	1996	The results show that heparin decasaccharides form a 1:1 complex with dimeric LPL and that decasaccharides are the shortest heparin fragments which can completely satisfy the heparin binding regions in dimeric LPL.	Heparin	22-29	lipoprotein lipase	Homo sapiens	210-213
32536326-10	2021	Patients in the antithrombin group were on preoperative heparin therapy (80.0% vs. 24.6%, p = 0.001).	Heparin	56-63	serpin family C member 1	Homo sapiens	16-28
8810923-2	1996	The results show that heparin decasaccharides form a 1:1 complex with dimeric LPL and that decasaccharides are the shortest heparin fragments which can completely satisfy the heparin binding regions in dimeric LPL.	Heparin	124-131	lipoprotein lipase	Homo sapiens	210-213
8810923-6	1996	The contribution of electrostatics was estimated to be 44% for the binding of LPL to heparan sulfate, 49% for the binding of LPL to unfractionated heparin, and 60% for the binding of LPL to affinity-purified heparin decasaccharides at 0.15 M NaCl.	Heparin	147-154	lipoprotein lipase	Homo sapiens	125-128
9235938-6	1997	The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII.	Heparin	8-15	serpin family C member 1	Homo sapiens	140-145
9235938-7	1997	Comparisons of binding residue positions in the structure of P14-inserted ATIII and models of native antithrombin, derived from the structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate antithrombin by breaking salt bridges that stabilize its native conformation.	Heparin	205-212	serpin family C member 1	Homo sapiens	74-79
8810923-6	1996	The contribution of electrostatics was estimated to be 44% for the binding of LPL to heparan sulfate, 49% for the binding of LPL to unfractionated heparin, and 60% for the binding of LPL to affinity-purified heparin decasaccharides at 0.15 M NaCl.	Heparin	147-154	lipoprotein lipase	Homo sapiens	125-128
8810923-9	1996	Monomeric LPL had 6000-fold lower affinity for heparin than dimeric LPL had, expressed as a ratio of equilibrium dissociation constants.	Heparin	47-54	lipoprotein lipase	Homo sapiens	10-13
9235938-7	1997	Comparisons of binding residue positions in the structure of P14-inserted ATIII and models of native antithrombin, derived from the structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate antithrombin by breaking salt bridges that stabilize its native conformation.	Heparin	205-212	serpin family C member 1	Homo sapiens	101-113
9235938-7	1997	Comparisons of binding residue positions in the structure of P14-inserted ATIII and models of native antithrombin, derived from the structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate antithrombin by breaking salt bridges that stabilize its native conformation.	Heparin	205-212	serpin family C member 1	Homo sapiens	226-238
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	94-101	serpin family C member 1	Homo sapiens	113-129
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	94-101	serpin family C member 1	Homo sapiens	113-125
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	113-129
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	210-215
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	113-125
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	113-129
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	210-215
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	113-125
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	113-129
8702993-5	1996	Heparin pretreatment and a monoclonal antibody ID7 that blocks LDL receptor-binding domain of apoE both inhibited binding, and apoE2/E2 VLDL from a Type III hyperlipidemic subject did not bind.	Heparin	0-7	low density lipoprotein receptor	Homo sapiens	63-75
8790153-0	1996	Induction of monocyte tissue factor procoagulant activity during coronary artery bypass surgery is reduced with heparin-coated extracorporeal circuit.	Heparin	112-119	coagulation factor III, tissue factor	Homo sapiens	22-35
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	210-215
9235938-9	1997	In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation.	Heparin	172-179	serpin family C member 1	Homo sapiens	113-125
32536326-12	2021	Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003).	Heparin	34-41	serpin family C member 1	Homo sapiens	0-12
8969375-1	1996	BACKGROUND: Recently, heparin-bonded (HBC) cardiopulmonary bypass circuits (CPB) were formed to be associated with improved outcome after coronary artery bypass grafting.	Heparin	22-29	keratin 88, pseudogene	Homo sapiens	38-41
32536326-12	2021	Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003).	Heparin	99-106	serpin family C member 1	Homo sapiens	0-12
8765099-7	1996	The endogenous kinase was identified as casein kinase II (CK II) based on the inhibition of the endogenous phosphorylation 160/150-kDa proteins by heparin, 5.6-dichlorobenzimidazole riboside, polyaspartyl peptide and hemin, and its ability to use [gamma-32P]GTP as the phosphate donor.	Heparin	147-154	casein kinase 2 alpha 1	Homo sapiens	40-56
33579328-0	2021	Baicalein inhibits heparin-induced Tau aggregation by initializing non-toxic Tau oligomer formation.	Heparin	19-26	microtubule associated protein tau	Homo sapiens	35-38
8765099-7	1996	The endogenous kinase was identified as casein kinase II (CK II) based on the inhibition of the endogenous phosphorylation 160/150-kDa proteins by heparin, 5.6-dichlorobenzimidazole riboside, polyaspartyl peptide and hemin, and its ability to use [gamma-32P]GTP as the phosphate donor.	Heparin	147-154	casein kinase 2 alpha 1	Homo sapiens	58-63
8870176-6	1996	In conclusion, plasma thrombomodulin is decreased by heparin, and increased during CPB.	Heparin	53-60	thrombomodulin	Homo sapiens	22-36
8878798-5	1996	PLC isozymes in tissue extracts of the lung were partially purified by successive chromatographic steps on heparin-sepharose CL-6B conventional and TSKgel heparin-5PW HPLC columns and their activities were assayed.	Heparin	107-114	heparan sulfate proteoglycan 2	Homo sapiens	0-3
8840462-5	1996	The increased expression of GMP-140 was paralleled by the enhanced platelet clumping in the samples anticoagulated with either EDTAK2 or heparin, and the raised platelet microparticles in blood withdrawn into citrate.	Heparin	137-144	selectin P	Homo sapiens	28-35
8840467-5	1996	The profile of protein binding to the UFH column was almost the same as that of the DHG column except that ATIII showed affinity for UFH.	Heparin	133-136	serpin family C member 1	Homo sapiens	107-112
9263656-2	1997	The standard antiplatelet and antithrombin agents used today in patients with acute coronary syndromes are aspirin and heparin.	Heparin	119-126	serpin family C member 1	Homo sapiens	30-42
9276686-1	1997	A 74-kDa delta/B" subunit was isolated by heparin-Sepharose column chromatography from human erythrocyte protein phosphatase 2A (PP2A) consisting of a 34-kDa catalytic subunit (alpha/C) and 63- and 74-kDa regulatory subunits (beta/A and delta/B") in a ratio of 1:1:1.	Heparin	42-49	protein phosphatase 2 phosphatase activator	Homo sapiens	129-133
9182528-0	1997	Characterization of the heparin binding properties of annexin II tetramer.	Heparin	24-31	annexin A2	Homo sapiens	54-64
9182528-1	1997	In this report, we have characterized the interaction of heparin with the Ca2+- and phospholipid-binding protein annexin II tetramer (AIIt).	Heparin	57-64	annexin A2	Homo sapiens	113-123
33579328-0	2021	Baicalein inhibits heparin-induced Tau aggregation by initializing non-toxic Tau oligomer formation.	Heparin	19-26	microtubule associated protein tau	Homo sapiens	77-80
33176060-0	2021	Skeletal muscle myosin and cardiac myosin attenuate heparin"s antithrombin-dependent anticoagulant activity.	Heparin	52-59	serpin family C member 1	Homo sapiens	62-74
9184748-8	1997	The alb-hep immobilized surface was able to bind much more thrombin than ATIII, which is probably due to the less specific heparin-thrombin interaction as compared to the heparin-ATIII interaction.	Heparin	123-130	serpin family C member 1	Homo sapiens	73-78
8678329-9	1996	Neointimal proliferation, quantified through the number of cell nuclei peroxidase-stained for PCNA/cyclin antigen, was significantly decreased by 43% and 49% with heparin, respectively, at days 7 and 14 after injury.	Heparin	163-170	proliferating cell nuclear antigen	Oryctolagus cuniculus	94-113
33176060-1	2021	BACKGROUND: Heparin enhances the ability of the plasma protease inhibitor, antithrombin, to neutralize coagulation factor Xa and thrombin.	Heparin	12-19	serpin family C member 1	Homo sapiens	75-87
8813337-2	1996	Antithrombin has two functional domains, a heparin binding site and a reactive centre (that complexes and inactivates the proteinase).	Heparin	43-50	serpin family C member 1	Homo sapiens	0-12
8813337-5	1996	The structure of antithrombin is now considered in terms of the models derived from X-ray crystallography, which have provided explanations for the function of its heparin interaction site and of its reactive loop.	Heparin	164-171	serpin family C member 1	Homo sapiens	17-29
9212075-3	1997	For example, it is well known that the sulfate groups are directly involved in the molecular interaction between heparin and antithrombin III.	Heparin	113-120	serpin family C member 1	Homo sapiens	125-141
33176060-3	2021	OBJECTIVES: The aim of this study was to investigate the influence of myosin binding to heparin on antithrombin"s anticoagulant activity.	Heparin	88-95	myosin heavy chain 14	Homo sapiens	70-76
8813337-6	1996	The structural organization of the antithrombin gene has been defined and numerous mutations have been identified that are responsible for antithrombin deficiency: these may reduce the level of the protein (Type I deficiency), alter the function of the protein (Type II deficiency, altering heparin binding or reactive sites), or even have multiple or "pleiotropic effects" (Type II deficiency, altering both functional domains and the level of protein).	Heparin	291-298	serpin family C member 1	Homo sapiens	35-47
33176060-3	2021	OBJECTIVES: The aim of this study was to investigate the influence of myosin binding to heparin on antithrombin"s anticoagulant activity.	Heparin	88-95	serpin family C member 1	Homo sapiens	99-111
9153200-4	1997	Zinc concentrations as low as 1.25 microM revealed HRG to be a powerful competitor of antithrombin for heparin in the purified component assays.	Heparin	103-110	serpin family C member 1	Homo sapiens	86-98
33176060-4	2021	METHODS: Inhibition of factor Xa and thrombin by antithrombin in the presence of different heparins and skeletal muscle myosin or cardiac myosin was studied by measuring inhibition of each enzyme"s chromogenic substrate hydrolysis.	Heparin	91-99	serpin family C member 1	Homo sapiens	49-61
9153200-7	1997	Investigation of other divalent cations (copper and magnesium) indicated that augmentation of heparin binding by HRG in the presence of antithrombin was restricted to zinc.	Heparin	94-101	serpin family C member 1	Homo sapiens	136-148
33176060-5	2021	RESULTS AND CONCLUSIONS: Skeletal muscle myosin and cardiac myosin neutralized unfractionated heparin"s enhancement of antithrombin"s inhibition of purified factor Xa and thrombin.	Heparin	94-101	serpin family C member 1	Homo sapiens	119-131
9594175-6	1996	The early administration of heparin and aprotinin after the supplement of fibrinogen has shown a great potential benifit to stop the cascade of hypercoagulation and hyperplasminogenemia by enhancing the level of AT-III and fibrinogen in plasma.	Heparin	28-35	serpin family C member 1	Homo sapiens	212-218
9169007-13	1997	These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.	Heparin	197-204	serpin family C member 1	Homo sapiens	67-79
33176060-8	2021	This chain length dependence for skeletal muscle myosin"s ability to reduce heparin"s anticoagulant activity might have potential implications for therapy for patients who experience increases in plasma myosin levels, e.g., acute trauma patients.	Heparin	76-83	myosin heavy chain 14	Homo sapiens	49-55
9169007-13	1997	These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin.	Heparin	197-204	serpin family C member 1	Homo sapiens	221-233
33482195-9	2021	Heparin has previously been reported to interfere with ANGPTL3 binding to LPL, so we questioned if the negatively charged heparin was acting in a similar fashion to the DNA contaminant.	Heparin	0-7	lipoprotein lipase	Homo sapiens	74-77
9187019-1	1997	Previous works suggest the interesting possibility of an effect of heparin on vascular smooth muscle cell (SMC) replication and migration via a selective inhibition of the expression of t-PA and u-PA both of which may play major roles during intimal hyperplasia following endothelial injury.	Heparin	67-74	plasminogen activator, urokinase	Mus musculus	195-199
9187019-4	1997	On control cells, heparin inhibited in a dose-dependent manner the expression of both t-PA and u-PA protein and mRNA.	Heparin	18-25	plasminogen activator, urokinase	Mus musculus	95-99
9187019-5	1997	Heparin however, similarly affected the mitogenic and chemotactic activity of FCS for SMC isolated from control, t-PA or u-PA-deficient mice therefore showing that heparin inhibits FCS-induced SMC proliferation via mechanism(s) other than single inhibition of t-PA or u-PA expression by smooth muscle cells.	Heparin	164-171	plasminogen activator, urokinase	Mus musculus	121-125
9187019-5	1997	Heparin however, similarly affected the mitogenic and chemotactic activity of FCS for SMC isolated from control, t-PA or u-PA-deficient mice therefore showing that heparin inhibits FCS-induced SMC proliferation via mechanism(s) other than single inhibition of t-PA or u-PA expression by smooth muscle cells.	Heparin	164-171	plasminogen activator, urokinase	Mus musculus	268-272
9187023-2	1997	Heparin augments the inhibitory activity of antithrombin (AT) towards thrombin, factor Xa (FXa) and other activated clotting enzymes.	Heparin	0-7	serpin family C member 1	Homo sapiens	44-56
9115268-2	1997	Mutations that decreased the susceptibility of thrombin to inhibition by antithrombin III in the presence and absence of heparin (W50A, E229A, and R233A) also decreased hydrolysis of a small tripeptidyl substrate.	Heparin	121-128	serpin family C member 1	Homo sapiens	73-89
9157959-4	1997	An earlier study showed that growing primary cultures of human umbilical vein endothelial cells (HUVECs) with endothelial cell growth supplement (ECGS) and heparin had impaired the ability of monolayers to express surface membrane TF activity after perturbation.	Heparin	156-163	coagulation factor III, tissue factor	Homo sapiens	231-233
8611699-7	1996	Antithrombin in the presence or absence of heparin prevented this basal activation, whereas TF pathway inhibitor (TFPI/factor Xa complexes had only a limited inhibitory effect.	Heparin	43-50	serpin family C member 1	Homo sapiens	0-12
8636243-24	1996	These data show that the activity of NK1 and NK2 can be modulated by heparin and other related glycosaminoglycans to induce proliferation in cells expressing c-Met.	Heparin	69-76	met proto-oncogene	Mus musculus	158-163
8847350-1	1996	The ability of heparin to interact with plasma proteins, in particular antithrombin III (ATIII) and thrombin, is its primary mechanism as an anticoagulant drug.	Heparin	15-22	serpin family C member 1	Homo sapiens	71-87
8847350-1	1996	The ability of heparin to interact with plasma proteins, in particular antithrombin III (ATIII) and thrombin, is its primary mechanism as an anticoagulant drug.	Heparin	15-22	serpin family C member 1	Homo sapiens	89-94
8847350-4	1996	In this report, insights into binding interaction of direct versus polyethylene oxide space immobilized heparin with ATIII, thrombin, and the generation of the thrombin-antithrombin complex will be presented.	Heparin	104-111	serpin family C member 1	Homo sapiens	117-122
8783184-0	1996	Stimulation of collagenase (matrix metalloproteinase-1) synthesis in histiotypic epithelial cell culture by heparin is enhanced by keratinocyte growth factor.	Heparin	108-115	matrix metallopeptidase 1	Homo sapiens	28-54
8783184-3	1996	Heparin, and, to a lesser extent, heparan sulfate induced release of a 58-kDa, gelatin-degrading enzyme which was subsequently identified as the collagenase, matrix metalloproteinase-1.	Heparin	0-7	matrix metallopeptidase 1	Homo sapiens	158-184
33482195-11	2021	Our data show new similarities and differences in how ANGPTL3 and ANGPTL4 regulate LPL and opens new avenues of investigating the effect of heparin on LPL inhibition by ANGPTL3.	Heparin	140-147	lipoprotein lipase	Homo sapiens	151-154
8630391-2	1996	At near-plasma concentrations of TFPI, ATIII, and factor X, factor X activation that occurs in response to TF:VII is essentially abolished in the presence of heparin (0.5 micromol/L).	Heparin	158-165	serpin family C member 1	Homo sapiens	39-44
8630391-3	1996	This effect requires both inhibitors, acting on different targets: (1) ATIII, which in the presence of heparin blocks the activation of TF:VII, and (2) TFPI, which inhibits the TF:VIIa that is generated.	Heparin	103-110	serpin family C member 1	Homo sapiens	71-76
8630391-6	1996	These results indicated that when the unactivated TF:VII complex is the initiating stimulus, heparin-dependent reduction in the rate and extent of factor X activation requires both ATIII and TFPI.	Heparin	93-100	serpin family C member 1	Homo sapiens	181-186
9079696-8	1997	The T7 RNA polymerase-nuclease is inhibited by T7 lysozyme and heparin, although not completely.	Heparin	63-70	nuclease	Escherichia coli	22-30
33125521-3	2021	METHODS: Capitalising on the IL-2-binding capabilities of heparin, an injectable hydrogel incorporating clinical-grade heparin, collagen and hyaluronan polymers was used to deliver IL-2.	Heparin	119-126	interleukin 2	Mus musculus	181-185
33125521-7	2021	Notably, heparin binding potentiates the activity of IL-2 and enhances IL-2- and TGFbeta-mediated expansion of forkhead box P3-positive regulatory T cells (FOXP3+ Tregs).	Heparin	9-16	interleukin 2	Mus musculus	53-57
9065409-6	1997	This interaction is mediated by the heparan sulfate chains of OCI-5 because it can be inhibited by heparin or by heparitinase.	Heparin	99-106	glypican 3	Rattus norvegicus	62-67
33125521-7	2021	Notably, heparin binding potentiates the activity of IL-2 and enhances IL-2- and TGFbeta-mediated expansion of forkhead box P3-positive regulatory T cells (FOXP3+ Tregs).	Heparin	9-16	interleukin 2	Mus musculus	71-75
8621443-11	1996	The GST-VEGF-exon 7 fusion protein bound to heparin-Sepharose with a similar affinity as VEGF165 and inhibited the binding of 125I-VEGF165 to 231 cells.	Heparin	44-51	glutathione S-transferase kappa 1	Homo sapiens	4-7
33125521-7	2021	Notably, heparin binding potentiates the activity of IL-2 and enhances IL-2- and TGFbeta-mediated expansion of forkhead box P3-positive regulatory T cells (FOXP3+ Tregs).	Heparin	9-16	transforming growth factor alpha	Mus musculus	81-88
9091324-4	1997	An in-gel kinase assay and analysis of phospho-amino acids revealed that the C2 subunit is phosphorylated by a 40-kDa serine/threonine protein kinase, the activity of which is inhibited by heparin, a specific inhibitor of casein kinase II.	Heparin	189-196	Protein kinase superfamily protein	Arabidopsis thaliana	222-238
33125521-7	2021	Notably, heparin binding potentiates the activity of IL-2 and enhances IL-2- and TGFbeta-mediated expansion of forkhead box P3-positive regulatory T cells (FOXP3+ Tregs).	Heparin	9-16	forkhead box P3	Mus musculus	111-126
8906988-4	1996	Monoclonal antibody (MAb) 9284 directed at an epitope overlapping with a putative heparin binding motif in the V3 loop of gp120 almost completely blocked the sCD4-induced binding of virions, while MAbs recognizing other sites of V2 or V3 loops had no effect.	Heparin	82-89	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	122-127
33125521-7	2021	Notably, heparin binding potentiates the activity of IL-2 and enhances IL-2- and TGFbeta-mediated expansion of forkhead box P3-positive regulatory T cells (FOXP3+ Tregs).	Heparin	9-16	forkhead box P3	Mus musculus	156-161
9147313-3	1997	The results obtained strongly suggest that the procoagulant activity of SV-IV/A is due, like SV-IV, to a selective inhibition of the antithrombin III (AT III) activation process induced by heparin, an essential cofactor of AT III.	Heparin	189-196	serpin family C member 1	Homo sapiens	133-149
9147313-3	1997	The results obtained strongly suggest that the procoagulant activity of SV-IV/A is due, like SV-IV, to a selective inhibition of the antithrombin III (AT III) activation process induced by heparin, an essential cofactor of AT III.	Heparin	189-196	serpin family C member 1	Homo sapiens	151-157
9147313-3	1997	The results obtained strongly suggest that the procoagulant activity of SV-IV/A is due, like SV-IV, to a selective inhibition of the antithrombin III (AT III) activation process induced by heparin, an essential cofactor of AT III.	Heparin	189-196	serpin family C member 1	Homo sapiens	223-229
9030826-3	1997	Femoral adipose tissue LPL activity, eluted with serum and heparin or extracted with detergent, showed significant inverse correlations with plasma levels of testosterone, bioavailable testosterone, dihydrotestosterone, and estradiol.	Heparin	59-66	lipoprotein lipase	Homo sapiens	23-26
9119287-0	1996	Anticoagulant effect of unfractionated heparin in antithrombin-depleted plasma in vitro.	Heparin	39-46	serpin family C member 1	Homo sapiens	50-62
9119287-1	1996	The aim of the study was to determine the effect of the antithrombin concentration on the anticoagulant response to heparin in vitro.	Heparin	116-123	serpin family C member 1	Homo sapiens	56-68
9119287-4	1996	Plasma with an antithrombin concentration over 0.27 U/ml shows a similar response to heparin as normal plasma; at lower levels the response is diminished.	Heparin	85-92	serpin family C member 1	Homo sapiens	15-27
9119287-5	1996	Even in plasma fully depleted of antithrombin, the APTT can be prolonged to a therapeutic level, although the amount of heparin needed is twice as high.	Heparin	120-127	serpin family C member 1	Homo sapiens	33-45
9119287-6	1996	At antithrombin concentrations over 0.27 U/ml, heparin is the major determinant of the anticoagulant effect.	Heparin	47-54	serpin family C member 1	Homo sapiens	3-15
33305345-6	2020	We administered antithrombin III concentrate with heparin for 5 days; thereafter, we switched to 60 mg edoxaban.	Heparin	50-57	serpin family C member 1	Homo sapiens	16-32
8830034-1	1996	We have purified 3"-phosphoadenosine-5"-phosphosulfate:GalCer sulfotransferase [EC 2.8.2.11] from a human renal cancer cell line SMKT-R3 through a combination of affinity chromatographies using galactosylsphingosine, 3",5"-bisphosphoadenosine and heparin as ligands.	Heparin	247-254	galactose-3-O-sulfotransferase 1	Homo sapiens	17-78
9021749-9	1997	The intracellular Ca2+ channels/receptors through which the sperm factor-mediated Ca2+ release was investigated by using heparin, a competitive inhibitor of the inositol 1,4,5 trisphosphate receptor (InsP3R), and ryanodine, which binds the ryanodine receptor (RyR).	Heparin	121-128	inositol 1,4,5-trisphosphate receptor 1	Mus musculus	200-206
9021749-10	1997	The sperm factor appeared to stimulate InsP3R, at least in mouse oocytes, because sperm factor-induced oscillations were delayed or blocked in all oocytes by injection of heparin.	Heparin	171-178	inositol 1,4,5-trisphosphate receptor 1	Mus musculus	39-45
9030190-9	1997	Most of LPL protein in control cells showed high affinity for heparin, and there was no difference between the control and CCCP-treated cells.	Heparin	62-69	lipoprotein lipase	Homo sapiens	8-11
32806292-3	2020	Furthermore, the encapsulated heparin can play a role in diminishing inflammation and accelerating wound healing in addition to its well-known function of stabilizing basic fibroblast growth factor.	Heparin	30-37	myotrophin	Rattus norvegicus	184-197
8994426-0	1997	Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate.	Heparin	98-105	serpin family C member 1	Homo sapiens	56-68
8994426-0	1997	Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate.	Heparin	128-135	serpin family C member 1	Homo sapiens	56-68
8994426-6	1997	The addition of a chemically modified heparin with low affinity for antithrombin III to plasma containing UFH increased the anti-IIa activity in a concentration-dependent fashion by displacing UFH from plasma proteins.	Heparin	38-45	serpin family C member 1	Homo sapiens	68-84
8596049-5	1996	HPLC purification with subsequent N-terminal sequencing and mass spectrometric analysis showed that the heparin-binding Eo-chemotactic peak corresponded to the chemokine [Tyr-RANTES]66 that also contained [Ser-RANTES]68 as contaminant, whereas the nonheparin-binding activity was identified as granulocyte-macrophage CSF (GM-CSF) by the use of neutralizing Abs.	Heparin	104-111	colony stimulating factor 2	Homo sapiens	294-320
8596049-5	1996	HPLC purification with subsequent N-terminal sequencing and mass spectrometric analysis showed that the heparin-binding Eo-chemotactic peak corresponded to the chemokine [Tyr-RANTES]66 that also contained [Ser-RANTES]68 as contaminant, whereas the nonheparin-binding activity was identified as granulocyte-macrophage CSF (GM-CSF) by the use of neutralizing Abs.	Heparin	104-111	colony stimulating factor 2	Homo sapiens	322-328
32806292-4	2020	In vitro release test shows the hydrogel network is able to sustainably release basic fibroblast growth factor within 10 days by the regulation of heparin, while released growth factor can significantly promote fibroblast"s proliferation in vitro.	Heparin	147-154	myotrophin	Rattus norvegicus	97-110
8728315-8	1996	Heparin abolished uptake of r-apo[a] by the LDL receptor component only; this indicates that apo[a] must be associated with LDL to be cleared by this receptor.	Heparin	0-7	low density lipoprotein receptor	Homo sapiens	44-56
33128275-7	2021	Compared to plain BCP, expression of endothelial-related genes Flt1 and Vcam1 was higher in BCP-HA and BCP-Hep group at day 30.	Heparin	107-110	vascular cell adhesion molecule 1	Mus musculus	72-77
8641009-4	1996	Thus, we hypothesized that the best concomitant antithrombotic therapy (recombinant [r]-hirudin, heparin, or aspirin) will maximally accelerate thrombolysis by r-tissue-type plasminogen activator (rTPA) and reduce residual thrombus.	Heparin	97-104	plasminogen activator, tissue type	Rattus norvegicus	197-201
9476567-3	1997	Aspirin and heparin have been used as therapeutic mainstays for acute coronary syndromes, acting as antiplatelet and antithrombin agents, respectively.	Heparin	12-19	serpin family C member 1	Homo sapiens	117-129
9034202-7	1997	LDL binding to LPL containing heparin-agarose was also disrupted by the amino-terminal antibodies to apoB.	Heparin	30-37	lipoprotein lipase	Homo sapiens	15-18
33128275-8	2021	Expression of osteogenesis-related genes Sp7 and Bglap after 30 days was the highest in BCP group, followed by BCP-Hep, while the lowest expression was in BCP-HA group which correlates with collagen amount.	Heparin	115-118	bone gamma carboxyglutamate protein	Mus musculus	49-54
8660298-2	1996	In addition, a number of other acidic oligosaccharides (for example heparin or chondroitin sulphate) or glycolipids (for example sulphatides) bind to L-selectin independent of cations.	Heparin	68-75	selectin L	Homo sapiens	150-160
9200337-0	1997	Tissue factor and plasminogen activator inhibitor type 2 expression in human stimulated monocytes is inhibited by heparin.	Heparin	114-121	coagulation factor III, tissue factor	Homo sapiens	0-13
32763614-6	2020	Moreover, the inclusion of IFN-gamma loaded heparin-coated beads prolonged the expression of key regulatory genes upregulated upon licensing, including indoleamine 2,3-dioxygenase 1 (IDO1) and galectin-9 (GAL9).	Heparin	44-51	indoleamine 2,3-dioxygenase 1	Homo sapiens	152-181
9200337-0	1997	Tissue factor and plasminogen activator inhibitor type 2 expression in human stimulated monocytes is inhibited by heparin.	Heparin	114-121	serpin family B member 2	Homo sapiens	18-56
8971549-0	1996	Structure-function relationships in the heparin-binding C-terminal region of insulin-like growth factor binding protein-3.	Heparin	40-47	insulin like growth factor binding protein 3	Homo sapiens	77-121
8971549-1	1996	IGFBP-3 contains a carboxyterminal basic region which, when present as an isolated 18 amino acid peptide (P3), binds heparin, associates with cultured endothelial cells and stimulates glucose uptake.	Heparin	117-124	insulin like growth factor binding protein 3	Homo sapiens	0-7
8977530-10	1996	The release of GM-CSF was not inhibited by catalase but was inhibited by cyclohexamide and by mixing of EPO with heparin, suggesting that the action is due to the cationic property of EPO.	Heparin	113-120	colony stimulating factor 2	Homo sapiens	15-21
8645351-13	1996	However, heparin, which interferes with cell surface proteoglycan interaction, was very effective at blocking HTg-VLDL-mediated increases in cholesterol ester in the presence of LPL (-86% +/- 8% P &lt; 0.0005).	Heparin	9-16	lipoprotein lipase	Homo sapiens	178-181
8567671-7	1996	Heparin increased LPL secretion in the case of the WT hLPL but did not have any stimulatory effect when acting on G142E hLPL-transfected cells.	Heparin	0-7	lipoprotein lipase	Homo sapiens	18-21
8567671-7	1996	Heparin increased LPL secretion in the case of the WT hLPL but did not have any stimulatory effect when acting on G142E hLPL-transfected cells.	Heparin	0-7	lipoprotein lipase	Homo sapiens	54-58
32763614-6	2020	Moreover, the inclusion of IFN-gamma loaded heparin-coated beads prolonged the expression of key regulatory genes upregulated upon licensing, including indoleamine 2,3-dioxygenase 1 (IDO1) and galectin-9 (GAL9).	Heparin	44-51	indoleamine 2,3-dioxygenase 1	Homo sapiens	183-187
8883844-0	1996	A monoclonal antibody against human lipoprotein lipase inhibiting heparin binding without affecting catalytic activity.	Heparin	66-73	lipoprotein lipase	Homo sapiens	36-54
9010384-10	1996	MAIN OUTCOME MEASURES: LPL determination: basal levels and post-heparin levels of LPL activity and mass.	Heparin	64-71	lipoprotein lipase	Homo sapiens	82-85
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	forkhead box P3	Mus musculus	39-61
8910451-10	1996	Heparin, a known inhibitor of MC growth, suppressed serum-induced [3H]thymidine uptake by 39% and egr-1 mRNA expression by 44%.	Heparin	0-7	early growth response 1	Homo sapiens	98-103
8895319-6	1996	In this study we report that IGFBP-2 binds to heparin if IGF-I or IGF-II is also included in the incubation buffer.	Heparin	46-53	insulin like growth factor 2	Homo sapiens	66-72
8820986-2	1996	Heparin-releasable LPL activities were higher in lipomas than those in adjacent normal adipose tissues, and showed good correlation with cellular LPL protein mass.	Heparin	0-7	lipoprotein lipase	Homo sapiens	19-22
8820986-2	1996	Heparin-releasable LPL activities were higher in lipomas than those in adjacent normal adipose tissues, and showed good correlation with cellular LPL protein mass.	Heparin	0-7	lipoprotein lipase	Homo sapiens	146-149
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	forkhead box P3	Mus musculus	63-68
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	interleukin 2	Mus musculus	122-140
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	interleukin 2	Mus musculus	207-211
8830193-4	1996	Receptor binding was partially blocked by preincubation with heparin, indicating a relationship to the heparin-binding subgroup of EGF-like growth factors.	Heparin	61-68	epidermal growth factor	Mus musculus	131-134
8951806-6	1996	Numerous studies indicate that in the case of thinning of the anionic glycosaminoglycan film on the endothelial surface, the lipoprotein-lipase and antithrombin III activity induced by heparin is reduced, as result of which hyperlipoproteinaemia and increased tendency to thrombosis can only by compensated for to an inadequate extent.	Heparin	185-192	lipoprotein lipase	Homo sapiens	125-143
8951806-6	1996	Numerous studies indicate that in the case of thinning of the anionic glycosaminoglycan film on the endothelial surface, the lipoprotein-lipase and antithrombin III activity induced by heparin is reduced, as result of which hyperlipoproteinaemia and increased tendency to thrombosis can only by compensated for to an inadequate extent.	Heparin	185-192	serpin family C member 1	Homo sapiens	148-164
32562271-11	2020	Our results indicate that heparin contributes to Treg -mediated immunosuppression through IL-2 production and suggest that heparin derivatives may be useful for immunopathological control by efficient Treg induction.	Heparin	26-33	interleukin 2	Mus musculus	90-94
8950777-3	1996	The present study was conducted to investigate how repeated (n = 8) and continuous (n = 6) administration of heparin affect plasma TFPI and the inhibition of tissue factor (TF)-induced coagulation ex vivo in humans.	Heparin	109-116	coagulation factor III, tissue factor	Homo sapiens	158-171
8713781-6	1996	K86E in PCI*B causes a charge alteration in helix D which is likely involved in heparin binding in antithrombin III but not likely involved in glycosaminoglycan binding in PCI.	Heparin	80-87	serpin family C member 1	Homo sapiens	99-115
8950777-3	1996	The present study was conducted to investigate how repeated (n = 8) and continuous (n = 6) administration of heparin affect plasma TFPI and the inhibition of tissue factor (TF)-induced coagulation ex vivo in humans.	Heparin	109-116	coagulation factor III, tissue factor	Homo sapiens	131-133
32351125-0	2020	Prophylactic low-molecular-weight heparin administration protected against severe acute pancreatitis partially by VEGF/Flt-1 signaling in a rat model.	Heparin	34-41	vascular endothelial growth factor A	Rattus norvegicus	114-118
8950777-8	1996	The contribution of TFPI to the inhibition of TF-induced coagulation during heparin infusion was estimated to decrease from 60 +/- 15% to 20 +/- 10% (p &lt; 0.0001).	Heparin	76-83	coagulation factor III, tissue factor	Homo sapiens	20-22
8798698-3	1996	In the present study, we demonstrated that heparin binding epidermal growth factor-like growth factor (HB-EGF) induced the expression of c-fms and the scavenger receptor in normal human medial smooth muscle cells to the level observed in the intima.	Heparin	43-50	heparin binding EGF like growth factor	Homo sapiens	103-109
8595089-1	1995	This paper describes the interference of heparin (CAS 9005-49-6) in whole plasma used for free and total levocarnitine (L-carnitine, CAS 541-15-1) analysis.	Heparin	41-48	BCAR1 scaffold protein, Cas family member	Homo sapiens	50-53
8595089-1	1995	This paper describes the interference of heparin (CAS 9005-49-6) in whole plasma used for free and total levocarnitine (L-carnitine, CAS 541-15-1) analysis.	Heparin	41-48	BCAR1 scaffold protein, Cas family member	Homo sapiens	133-136
8580401-10	1995	The free fraction of YH-439 was slightly increased by the addition of heparin (up to 40 U mL-1), sodium azide (NaN3, up to 0.5%), and its metabolites.	Heparin	70-77	L1 cell adhesion molecule	Mus musculus	90-94
8915986-3	1996	The anticoagulant action of heparin is mediated by antithrombin III.	Heparin	28-35	serpin family C member 1	Homo sapiens	51-67
32897051-6	2020	Changes in local flexibility, including a disruption of the N-terminal helix at acidic pH, also accompany heparin binding to GMCSF.	Heparin	106-113	colony stimulating factor 2	Homo sapiens	125-130
8915986-8	1996	The magnitude of the inhibitory action of antithrombin III was equal to that of equimolar concentrations of heparin and that observed with the combination of the two.	Heparin	108-115	serpin family C member 1	Homo sapiens	42-58
8845035-4	1996	Presaturation of solid phase SAP with heparin, which binds SAP with high affinity, did not interfere with the subsequent binding of C4bp or C1q to SAP.	Heparin	38-45	amyloid P component, serum	Homo sapiens	29-32
8845035-4	1996	Presaturation of solid phase SAP with heparin, which binds SAP with high affinity, did not interfere with the subsequent binding of C4bp or C1q to SAP.	Heparin	38-45	amyloid P component, serum	Homo sapiens	59-62
8845035-4	1996	Presaturation of solid phase SAP with heparin, which binds SAP with high affinity, did not interfere with the subsequent binding of C4bp or C1q to SAP.	Heparin	38-45	amyloid P component, serum	Homo sapiens	59-62
8845035-7	1996	Altogether the results indicate that firm binding of C1q and C4bp to SAP requires that SAP is presented on a solid phase, that C1q and C4bp react with sites distinct from the heparin binding site, and that C1q and collagen I share binding sites on SAP.	Heparin	175-182	complement C1q A chain	Homo sapiens	53-56
8845035-7	1996	Altogether the results indicate that firm binding of C1q and C4bp to SAP requires that SAP is presented on a solid phase, that C1q and C4bp react with sites distinct from the heparin binding site, and that C1q and collagen I share binding sites on SAP.	Heparin	175-182	amyloid P component, serum	Homo sapiens	69-72
8798437-4	1996	One, with a higher affinity to heparin, was identified as chondromodulin I (Hiraki, Y., Tanaka, H., Inoue, H. , Kondo, J., Kamizono, A., and Suzuki, F. (1991) Biochem.	Heparin	31-38	chondromodulin	Bos taurus	58-74
8835301-3	1995	Like heparin or heparan sulfates, heparan-like molecules, named carboxymethyl-benzylamide-sulfonated dextrans (CMDBS), are known to potentiate fibroblast growth factor activities by stabilizing them against pH, thermal or proteolytic denaturations, and by enhancing their binding with cell surface receptors.	Heparin	5-12	myotrophin	Rattus norvegicus	154-167
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Heparin	148-155	serpin family D member 1	Rattus norvegicus	104-109
8746633-9	1995	In the presence of glycosaminoglycans, the maximal thrombin inhibition rate (k2 x 10(-3) M-1 min-1) for rHCII was 10.4 +/- 2.5 at 100 micrograms/ml heparin and 16.0 +/- 4.3 at 1000 micrograms/ml dermatan sulfate compared to 9.0 +/- 0.7 at 200 micrograms/ml heparin and 18.5 +/- 5.3 at 1000 micrograms/ml dermatan sulfate for pHCII.	Heparin	257-264	serpin family D member 1	Rattus norvegicus	104-109
8555090-0	1995	Single amino acid mutation of Fc gamma receptor is associated with the development of heparin-induced thrombocytopenia.	Heparin	86-93	Fc gamma receptor Ia	Homo sapiens	30-47
8555090-1	1995	Heparin-induced thrombocytopenia (HIT) is mediated by a heparin-dependent antibody/platelet factor 4/heparin complex binding to platelets via the Fc gamma receptor (type IIA).	Heparin	0-7	Fc gamma receptor Ia	Homo sapiens	146-173
8578545-1	1995	Antithrombin from bony fish (Teleostei), represented by an ancient salmonid, Atlantic salmon (Salmo salar L.), and a more evolved species from the same family, rainbow trout (Oncorhynchus mykiss Walbaum), functions in vitro as does its human counterpart: it inactivates thrombin almost instantaneously in the presence of heparin and only slowly when heparin is absent.	Heparin	321-328	serpin family C member 1	Homo sapiens	0-12
8578545-1	1995	Antithrombin from bony fish (Teleostei), represented by an ancient salmonid, Atlantic salmon (Salmo salar L.), and a more evolved species from the same family, rainbow trout (Oncorhynchus mykiss Walbaum), functions in vitro as does its human counterpart: it inactivates thrombin almost instantaneously in the presence of heparin and only slowly when heparin is absent.	Heparin	350-357	serpin family C member 1	Homo sapiens	0-12
8578545-6	1995	And the thrombin inactivating capacity of purified antithrombin and diluted plasma in the presence of heparin was indeed present at temperatures down to 3 degrees C, a capacity that human antithrombin also has retained.	Heparin	102-109	serpin family C member 1	Homo sapiens	51-63
8578545-6	1995	And the thrombin inactivating capacity of purified antithrombin and diluted plasma in the presence of heparin was indeed present at temperatures down to 3 degrees C, a capacity that human antithrombin also has retained.	Heparin	102-109	serpin family C member 1	Homo sapiens	188-200
32515841-0	2020	Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid.	Heparin	51-58	serpin family C member 1	Homo sapiens	18-30
7578276-0	1995	Oversulfated fucoidan and heparin suppress endotoxin induction of plasminogen activator inhibitor-1 in cultured human endothelial cells: their possible mechanism of action.	Heparin	26-33	serpin family E member 1	Homo sapiens	66-99
7578276-5	1995	The increased PAI-1 level was reduced to control level by the simultaneous addition of 10 micrograms/ml of OSF or heparin.	Heparin	114-121	serpin family E member 1	Homo sapiens	14-19
7578276-13	1995	The suppressive effects of OSF and heparin on LPS-induced PAI-1 release may result from the inhibition of LPS binding to the cell surface HSPG.	Heparin	35-42	serpin family E member 1	Homo sapiens	58-63
8781492-3	1996	It is analogue of the "synthetic pentasaccharide" (SR 90107/ORG 31540), which represents the antithrombin III (AT-III) binding site of heparin.	Heparin	135-142	serpin family C member 1	Homo sapiens	111-117
8896339-1	1996	Antithrombin III was purified to homogeneity from hamster plasma by affinity chromatography on heparin-agrose, ion-exchange chromatography on Mono Q and size-exclusion chromatography on TSK G3000SWG column with 50% yield.	Heparin	95-102	serpin family C member 1	Homo sapiens	0-16
8702896-7	1996	Cleaved PAI-1 did not bind to either PAs or vitronectin but retained the heparin-binding capacity.	Heparin	73-80	serpin family E member 1	Homo sapiens	8-13
32515841-1	2020	Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein.	Heparin	0-7	serpin family C member 1	Homo sapiens	31-43
32515841-3	2020	Indeed, a heparin octasaccharidic sequence obtained by chemoenzymatic synthesis, in which GlcA is replaced by IdoA2S has been found to similarly bind to and activate antithrombin.	Heparin	10-17	serpin family C member 1	Homo sapiens	166-178
8588189-2	1995	Such inhibition causes mast cells to produce heparins with high affinity for antithrombin (AT).	Heparin	45-53	serpin family C member 1	Homo sapiens	77-89
32228213-2	2020	Unfractionated heparin, a glycosaminoglycan that must bind to antithrombin as a cofactor, is currently the standard anticoagulant adopted during extracorporeal membrane oxygenation.	Heparin	15-22	serpin family C member 1	Homo sapiens	62-74
7572800-9	1995	Heparin activates lipoprotein lipase with release of free fatty acids (FFA) from very low density lipoproteins and chylomicrons.	Heparin	0-7	lipoprotein lipase	Homo sapiens	18-36
7547966-6	1995	Heparin increased markedly the kon values for antithrombin III and protease nexin-1 with all thrombin variants tested, but a more dramatic effect was observed with a thrombin mutant (des-ETW) lacking residues Glu146, Thr147, and Trp148 (on the opposite side of the catalytic site relative to the 60-loop insertion).	Heparin	0-7	serpin family C member 1	Homo sapiens	46-62
7547966-7	1995	At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin.	Heparin	30-37	serpin family C member 1	Homo sapiens	78-94
7547966-7	1995	At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin.	Heparin	193-200	serpin family C member 1	Homo sapiens	78-94
8549645-2	1995	Lipoprotein lipase activity was determined in two fractions; lipoprotein lipase released by heparin (10 IU/ml, 1 h) into the medium (heparin-releasable fraction) and lipoprotein lipase activity remaining in cells (extractable fraction).	Heparin	92-99	lipoprotein lipase	Homo sapiens	0-18
8549645-2	1995	Lipoprotein lipase activity was determined in two fractions; lipoprotein lipase released by heparin (10 IU/ml, 1 h) into the medium (heparin-releasable fraction) and lipoprotein lipase activity remaining in cells (extractable fraction).	Heparin	92-99	lipoprotein lipase	Homo sapiens	61-79
8549645-3	1995	Time-course studies showed that endothelin 1 (10(-7) M) progressively decreased both lipoprotein lipase fractions (heparin-releasable, extractable), until nadir at 24 h. Endothelin-1 reduced both lipoprotein lipase activities (heparin-releasable, extractable) in a concentration-dependent manner, whereas endothelin-3 did not produce any significant changes in either of them.	Heparin	115-122	lipoprotein lipase	Homo sapiens	85-103
8756800-3	1996	IgE-independent HRF due to chemokines was removed from mononuclear cell supernatants with heparin-Sepharose.	Heparin	90-97	tumor protein, translationally-controlled 1	Homo sapiens	16-19
8878798-5	1996	PLC isozymes in tissue extracts of the lung were partially purified by successive chromatographic steps on heparin-sepharose CL-6B conventional and TSKgel heparin-5PW HPLC columns and their activities were assayed.	Heparin	155-162	heparan sulfate proteoglycan 2	Homo sapiens	0-3
8663337-4	1996	Furthermore, the human adrenocortical carcinoma cell line, NCI-H295, expresses LPL mRNA and protein, which is localized to the outer cellular membrane as demonstrated by immunofluorescence confocal microscopy and can be released in the medium by heparin addition.	Heparin	246-253	lipoprotein lipase	Homo sapiens	79-82
8663337-7	1996	This decrease after phorbol 12-myristate 13-acetate was associated with diminished heparin-releasable LPL mass and activity in the culture medium.	Heparin	83-90	lipoprotein lipase	Homo sapiens	102-105
8688424-3	1996	We previously found additional heterogeneity in a recombinant N135Q antithrombin variant, evidenced by two isoforms with a 2-fold difference in heparin affinity [Turko, I. V., Fan, B., &amp; Gettins, P. G. W. (1993) FEBS Lett.	Heparin	144-151	serpin family C member 1	Homo sapiens	68-80
8688424-9	1996	We conclude that formation of the two heparin-affinity isoforms of N135Q antithrombin results from the specific difference in fucosylation at residue 155, which may result in different structural properties of the carbohydrate.	Heparin	38-45	serpin family C member 1	Homo sapiens	73-85
8688424-10	1996	Consistent with these findings was the elimination of heparin-affinity heterogeneity in a double N135Q-N155Q variant antithrombin.	Heparin	54-61	serpin family C member 1	Homo sapiens	117-129
32228213-8	2020	Consistently, antithrombin is considered able to achieve better anticoagulation targets in or not in the presence of heparin resistance.	Heparin	117-124	serpin family C member 1	Homo sapiens	14-26
32824376-0	2020	The Non-Fibrillating N-Terminal of alpha-Synuclein Binds and Co-Fibrillates with Heparin.	Heparin	81-88	synuclein alpha	Homo sapiens	35-50
8663282-3	1996	In addition to the sLex carbohydrate, P-selectin binds sulfated proteoglycan, 3-sulfated galactosyl ceramide (sulfatide), and heparin.	Heparin	126-133	selectin P	Homo sapiens	38-48
8663282-5	1996	We report that mutagenic substitution of single amino acid residues in either the P- or E-selectin EGF domain can dramatically alter selectin binding to sLex, heparin, or sulfatide.	Heparin	159-166	selectin E	Homo sapiens	88-98
8663282-8	1996	Additionally, we have determined that conservative substitution of EGF domain residues 124 and 128 can alter E-selectin binding such that it is able to adhere to heparin or sulfatide and can reduce P-selectin adherence to these ligands.	Heparin	162-169	selectin E	Homo sapiens	109-119
8679610-2	1996	A heparin-induced conformational change is required to convert antithrombin from a slow to a fast inhibitor of factor Xa.	Heparin	2-9	serpin family C member 1	Homo sapiens	63-75
7559767-0	1995	Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1).	Heparin	0-7	CD1b molecule	Homo sapiens	64-67
7643627-3	1995	The activity of the co-precipitating kinase is inhibited by heparin and unlabelled GTP suggesting that casein kinase II (CKII) is, at least in part, responsible for the topo II hyperphosphorylation in response to differentiation signals.	Heparin	60-67	casein kinase 2 alpha 1	Homo sapiens	103-119
7643627-3	1995	The activity of the co-precipitating kinase is inhibited by heparin and unlabelled GTP suggesting that casein kinase II (CKII) is, at least in part, responsible for the topo II hyperphosphorylation in response to differentiation signals.	Heparin	60-67	casein kinase 2 alpha 1	Homo sapiens	121-125
32507170-0	2020	Enhanced tendon restoration effects of anti-inflammatory, lactoferrin-immobilized, heparin-polymeric nanoparticles in an Achilles tendinitis rat model.	Heparin	83-90	lactotransferrin	Rattus norvegicus	58-69
17607884-1	1995	Antithrombin, the main inhibitor of thrombosis in blood, is bound and activated by the heparin-like side-chains that line the small vasculature.	Heparin	87-94	serpin family C member 1	Homo sapiens	0-12
17607884-2	1995	We now have good depictions of the heparin-binding site on antithrombin, and of the way in which mutations at this site cause thrombotic disease.	Heparin	35-42	serpin family C member 1	Homo sapiens	59-71
17607884-3	1995	The interaction of heparin with antithrombin is, however, a kinetic one, with binding being followed by formation of a complex with thrombin and then release from the heparin.	Heparin	19-26	serpin family C member 1	Homo sapiens	32-44
8679610-7	1996	1, 423-425] that the reactive center residue P14 is inserted into beta-sheet A in native antithrombin and is displaced from the beta-sheet by heparin binding, thereby altering the conformation of the reactive center and making it a better target for factor Xa binding.	Heparin	142-149	serpin family C member 1	Homo sapiens	89-101
8770923-8	1996	Both the chelator and heparin blocked metformin stimulation of insulin action on whole cells.	Heparin	22-29	insulin S homeolog	Xenopus laevis	63-70
17607884-3	1995	The interaction of heparin with antithrombin is, however, a kinetic one, with binding being followed by formation of a complex with thrombin and then release from the heparin.	Heparin	167-174	serpin family C member 1	Homo sapiens	32-44
31756489-7	2020	Besides, this method also shows good selectivity and sensitivity, and the linear range of heparin is from 0.08 to 8 mug mL-1 with detection limit of 37 ng mL-1.	Heparin	90-97	L1 cell adhesion molecule	Mus musculus	120-124
8585002-8	1995	From the linear correlation between these two parameters it was found that 5 out of the 6 tested aprotinin analogues, rTAP and r-hirudin completely inhibited thrombus formation at a therapeutical (2- to 3-fold) aPTT prolongation while 4C2, heparin and enoxaparin only inhibited thrombus formation for 40 to 50 percent at a 2-fold aPTT prolongation.	Heparin	240-247	pancreatic trypsin inhibitor	Bos taurus	97-106
7557658-6	1995	In addition, AT III was characterized by crossed immunoelectrophoresis in the presence of heparin and by gel filtration.	Heparin	90-97	serpin family C member 1	Homo sapiens	13-19
7540614-5	1995	We also show that ARIA can be released from freshly dissociated cells from embryonic chick spinal cord and cerebellum by either heparin, high salt or limited proteolysis with subtilisin, suggesting that ARIA is bound to the extracellular matrix through charged interactions.	Heparin	128-135	prion protein	Gallus gallus	18-22
7540614-5	1995	We also show that ARIA can be released from freshly dissociated cells from embryonic chick spinal cord and cerebellum by either heparin, high salt or limited proteolysis with subtilisin, suggesting that ARIA is bound to the extracellular matrix through charged interactions.	Heparin	128-135	prion protein	Gallus gallus	203-207
8698481-5	1996	The inhibitory action depended on the fimbrial interaction with heparin-binding and cell attachment domains in the fibronectin structure.	Heparin	64-71	fibronectin 1	Mus musculus	115-126
8661426-0	1996	Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase.	Heparin	24-31	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	55-58
8661426-1	1996	Heparin can substitute for double-stranded (ds) RNA in the autophosphorylation and activation of the interferon-inducible, RNA-dependent elF-2 alpha protein kinase (PKR).	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	165-168
8661426-3	1996	Heparin oligosaccharide with 8 sugar residues was nearly as efficient as 16-residue heparin (Hep-16) in mediating the activation of PKR autophosphorylation, whereas 6-residue heparin was a poor activator.	Heparin	84-91	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	132-135
8661426-6	1996	When the catalytically inactive, histidine-tagged mutant PKR protein [His-PKR(K296R)] was examined as a substrate for purified wild-type PKR, the intermolecular phosphorylation of His-PKR(K296R) was efficiently catalyzed by dsRNA-activated PKR but not by heparin-activated PKR.	Heparin	255-262	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	57-60
8661426-6	1996	When the catalytically inactive, histidine-tagged mutant PKR protein [His-PKR(K296R)] was examined as a substrate for purified wild-type PKR, the intermolecular phosphorylation of His-PKR(K296R) was efficiently catalyzed by dsRNA-activated PKR but not by heparin-activated PKR.	Heparin	255-262	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	74-77
8661426-6	1996	When the catalytically inactive, histidine-tagged mutant PKR protein [His-PKR(K296R)] was examined as a substrate for purified wild-type PKR, the intermolecular phosphorylation of His-PKR(K296R) was efficiently catalyzed by dsRNA-activated PKR but not by heparin-activated PKR.	Heparin	255-262	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	74-77
8661426-6	1996	When the catalytically inactive, histidine-tagged mutant PKR protein [His-PKR(K296R)] was examined as a substrate for purified wild-type PKR, the intermolecular phosphorylation of His-PKR(K296R) was efficiently catalyzed by dsRNA-activated PKR but not by heparin-activated PKR.	Heparin	255-262	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	74-77
8661426-6	1996	When the catalytically inactive, histidine-tagged mutant PKR protein [His-PKR(K296R)] was examined as a substrate for purified wild-type PKR, the intermolecular phosphorylation of His-PKR(K296R) was efficiently catalyzed by dsRNA-activated PKR but not by heparin-activated PKR.	Heparin	255-262	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	74-77
8661426-6	1996	When the catalytically inactive, histidine-tagged mutant PKR protein [His-PKR(K296R)] was examined as a substrate for purified wild-type PKR, the intermolecular phosphorylation of His-PKR(K296R) was efficiently catalyzed by dsRNA-activated PKR but not by heparin-activated PKR.	Heparin	255-262	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	74-77
8661426-10	1996	These results suggest that, while both dsRNA and heparin are capable of activating PKR autophosphorylation, the structural and functional basis of PKR activation differs for these two classes of polyanionic biomolecules.	Heparin	49-56	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	83-86
7794926-9	1995	Heparin, which binds to CKII alpha, inhibited the binding of CKII to HSP90-Sepharose.	Heparin	0-7	casein kinase 2 alpha 1	Homo sapiens	24-28
7794926-9	1995	Heparin, which binds to CKII alpha, inhibited the binding of CKII to HSP90-Sepharose.	Heparin	0-7	heat shock protein 90 alpha family class A member 1	Homo sapiens	69-74
31756489-7	2020	Besides, this method also shows good selectivity and sensitivity, and the linear range of heparin is from 0.08 to 8 mug mL-1 with detection limit of 37 ng mL-1.	Heparin	90-97	L1 cell adhesion molecule	Mus musculus	155-159
8663298-6	1996	IGFBP-3 peptides containing one of the two heparin-binding consensus sequences bound heparin in a solid phase binding assay in a dose-dependent and saturable manner.	Heparin	85-92	insulin like growth factor binding protein 3	Homo sapiens	0-7
7797516-6	1995	(ii) Phosphorylation of residue Ser488 influences the affinity of RK for heparin-Sepharose only moderately, whereas Thr489 and Lys491 are important for this interaction.	Heparin	73-80	G protein-coupled receptor kinase 1	Homo sapiens	66-68
8663298-7	1996	However, the IGFBP-3 peptide containing the heparin-binding consensus sequence 149KKGHA153 bound heparin with approximately 4-fold less affinity than the IGFBP-3 peptide containing the longer heparin-binding consensus sequence 219YKKKQCRP226.	Heparin	44-51	insulin like growth factor binding protein 3	Homo sapiens	13-20
32709152-2	2020	In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase.	Heparin	81-88	tryptase alpha/beta 1	Mus musculus	27-35
8663298-7	1996	However, the IGFBP-3 peptide containing the heparin-binding consensus sequence 149KKGHA153 bound heparin with approximately 4-fold less affinity than the IGFBP-3 peptide containing the longer heparin-binding consensus sequence 219YKKKQCRP226.	Heparin	97-104	insulin like growth factor binding protein 3	Homo sapiens	13-20
8663298-7	1996	However, the IGFBP-3 peptide containing the heparin-binding consensus sequence 149KKGHA153 bound heparin with approximately 4-fold less affinity than the IGFBP-3 peptide containing the longer heparin-binding consensus sequence 219YKKKQCRP226.	Heparin	97-104	insulin like growth factor binding protein 3	Homo sapiens	13-20
8663298-8	1996	Examination of several well characterized glycosaminoglycans to inhibit the binding of heparin to both heparin-binding IGFBP-3 peptides revealed that the most potent inhibitors were heparin, heparan sulfate, and dermatan sulfate; chondroitin sulfate A and hyaluronic acid were intermediate in their inhibitory activities; and chondroitin sulfate C caused no inhibition.	Heparin	87-94	insulin like growth factor binding protein 3	Homo sapiens	119-126
8663298-8	1996	Examination of several well characterized glycosaminoglycans to inhibit the binding of heparin to both heparin-binding IGFBP-3 peptides revealed that the most potent inhibitors were heparin, heparan sulfate, and dermatan sulfate; chondroitin sulfate A and hyaluronic acid were intermediate in their inhibitory activities; and chondroitin sulfate C caused no inhibition.	Heparin	103-110	insulin like growth factor binding protein 3	Homo sapiens	119-126
8663298-8	1996	Examination of several well characterized glycosaminoglycans to inhibit the binding of heparin to both heparin-binding IGFBP-3 peptides revealed that the most potent inhibitors were heparin, heparan sulfate, and dermatan sulfate; chondroitin sulfate A and hyaluronic acid were intermediate in their inhibitory activities; and chondroitin sulfate C caused no inhibition.	Heparin	103-110	insulin like growth factor binding protein 3	Homo sapiens	119-126
8767305-11	1996	After coronary angioplasty and heparin treatment all patients had once more an elevation of TnT and TnI 8 and 27 hours after the invasive therapy.	Heparin	31-38	troponin T1, slow skeletal type	Homo sapiens	92-95
8732755-11	1996	In order to investigate PSA"s heparin interaction sites, electrostatic computations were carried out on PSA, hK2, protein C, ACT, and PCI.	Heparin	30-37	kallikrein related peptidase 3	Homo sapiens	24-27
8732755-12	1996	Two heparin binding sites are suggested on the PSA surface and could explain the enhanced complex formation between PSA and PCI, while inhibiting the formation of the ACT-PSA complex, PSA, hK2, and their preliminary complexes with ACT should facilitate the understanding and prediction of structural and functional properties for these important proteins also with respect to prostate diseases.	Heparin	4-11	kallikrein related peptidase 3	Homo sapiens	47-50
7539022-9	1995	PAF induced a dose-dependent angiogenic response, which at pharmacologic concentrations (1-5 microM) did not require heparin, but at physiologic concentrations (5-50 nM) required the presence of heparin at doses that were not angiogenic per se.	Heparin	195-202	PCNA clamp associated factor	Homo sapiens	0-3
7647223-1	1995	It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs).	Heparin	202-210	serpin family C member 1	Homo sapiens	45-50
7706383-2	1995	Both AR and HB-EGF share with EGF the ability to interact with the type-1 EGF receptor; however, AR and HB-EGF differ from EGF in that both of these mitogens bind to heparin while EGF does not.	Heparin	166-173	heparin-binding EGF-like growth factor	Mus musculus	12-18
7706383-2	1995	Both AR and HB-EGF share with EGF the ability to interact with the type-1 EGF receptor; however, AR and HB-EGF differ from EGF in that both of these mitogens bind to heparin while EGF does not.	Heparin	166-173	heparin-binding EGF-like growth factor	Mus musculus	104-110
7706383-8	1995	Chlorate treatment did not significantly alter the ability of HB-EGF to compete with 125I-EGF for cell surface binding sites, however, heparin and hexadimethrine reduced the ability of HB-EGF to compete for 125I-EGF binding.	Heparin	135-142	heparin-binding EGF-like growth factor	Mus musculus	185-191
7706383-9	1995	These results suggest that, in AKR-2B cells, HB-EGF may mediate its mitogenic response at least in part through a receptor which appears to be selective for HB-EGF and permits HB-EGF-mediated mitogenic responses in the presence of hexadimethrine or heparin.	Heparin	249-256	heparin-binding EGF-like growth factor	Mus musculus	45-51
7721864-0	1995	Mapping of network-forming, heparin-binding, and alpha 1 beta 1 integrin-recognition sites within the alpha-chain short arm of laminin-1.	Heparin	28-35	laminin subunit alpha 1	Rattus norvegicus	127-136
8732755-12	1996	Two heparin binding sites are suggested on the PSA surface and could explain the enhanced complex formation between PSA and PCI, while inhibiting the formation of the ACT-PSA complex, PSA, hK2, and their preliminary complexes with ACT should facilitate the understanding and prediction of structural and functional properties for these important proteins also with respect to prostate diseases.	Heparin	4-11	kallikrein related peptidase 3	Homo sapiens	116-119
8732755-12	1996	Two heparin binding sites are suggested on the PSA surface and could explain the enhanced complex formation between PSA and PCI, while inhibiting the formation of the ACT-PSA complex, PSA, hK2, and their preliminary complexes with ACT should facilitate the understanding and prediction of structural and functional properties for these important proteins also with respect to prostate diseases.	Heparin	4-11	kallikrein related peptidase 3	Homo sapiens	116-119
8732755-12	1996	Two heparin binding sites are suggested on the PSA surface and could explain the enhanced complex formation between PSA and PCI, while inhibiting the formation of the ACT-PSA complex, PSA, hK2, and their preliminary complexes with ACT should facilitate the understanding and prediction of structural and functional properties for these important proteins also with respect to prostate diseases.	Heparin	4-11	kallikrein related peptidase 3	Homo sapiens	116-119
32709152-2	2020	In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase.	Heparin	124-131	tryptase alpha/beta 1	Mus musculus	27-35
8704054-2	1996	Extrahepatic lipoprotein lipase, which is well known to be liberated by heparin from the capillar binding sites, may cleave triacylglycerols as well as diacylglycerols.	Heparin	72-79	lipoprotein lipase	Homo sapiens	13-31
8704054-3	1996	When a heparin bolus injection is given to a patient, the released lipoprotein lipase renders high lipase activities in blood misleading for a pancreatic disorder.	Heparin	7-14	lipoprotein lipase	Homo sapiens	67-85
7605368-4	1995	LPL metabolism in HepG2 cells was characterized by a high capacity to degrade the enzyme, an extremely high sensitivity to heparin and was inhibited by 60%-70% after treatment of the cells with sodium chlorate and heparinase (but not chondroitinase).	Heparin	123-130	lipoprotein lipase	Homo sapiens	0-3
8857192-0	1996	Binding of antithrombin III and thrombin to immobilized heparin under flow conditions.	Heparin	56-63	serpin family C member 1	Homo sapiens	11-27
32709152-2	2020	In the secretory granules, tryptase is stored in complex with negatively charged heparin proteoglycans and it is known that heparin is essential for stabilizing the enzymatic activity of tryptase.	Heparin	124-131	tryptase alpha/beta 1	Mus musculus	187-195
8857192-3	1996	However, few studies have been performed to investigate the binding kinetics of spacer-immobilized heparin under flow (shear stress) with antithrombin III (ATIII) and thrombin.	Heparin	99-106	serpin family C member 1	Homo sapiens	138-154
32709152-4	2020	Here we hypothesized that tryptase, as well as being stabilized by heparin, can be stabilized by DNA, the rationale being that the anionic charge of DNA could potentially substitute for that of heparin to execute this function.	Heparin	67-74	tryptase alpha/beta 1	Mus musculus	26-34
8857192-3	1996	However, few studies have been performed to investigate the binding kinetics of spacer-immobilized heparin under flow (shear stress) with antithrombin III (ATIII) and thrombin.	Heparin	99-106	serpin family C member 1	Homo sapiens	156-161
8857192-5	1996	Heparinized tubing was prepared by chemically immobilizing a high-ATIII-affinity fraction of heparin onto the surface of poly(ethylene)-oxide grafted, poly(styrene-co-p-aminostyrene)-coated polyethylene tubing.	Heparin	93-100	serpin family C member 1	Homo sapiens	66-71
7893664-10	1995	Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively.	Heparin	0-7	acrosin	Homo sapiens	47-54
7893664-10	1995	Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively.	Heparin	0-7	serpin family C member 1	Homo sapiens	58-70
7893664-10	1995	Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively.	Heparin	0-7	serpin family C member 1	Homo sapiens	207-219
7893664-10	1995	Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively.	Heparin	137-144	acrosin	Homo sapiens	47-54
7893664-10	1995	Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively.	Heparin	137-144	serpin family C member 1	Homo sapiens	58-70
7893664-10	1995	Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively.	Heparin	137-144	serpin family C member 1	Homo sapiens	207-219
7890669-4	1995	The p53 kinase activity co-purifies with UV-activated c-Jun kinase activity on heparin-Sepharose and on a c-Jun (but not a v-Jun-) affinity column.	Heparin	79-86	transformation related protein 53, pseudogene	Mus musculus	4-7
8857192-6	1996	ATIII was first bound onto the immobilized heparin, followed by the introduction of thrombin to interact with ATIII.	Heparin	43-50	serpin family C member 1	Homo sapiens	0-5
8728326-7	1996	Despite an absolute deficiency of LPL mass and activity demonstrated by analysis of patient post-heparin plasma, in vitro expression of both LPL mutants was normal, suggesting that the absence of LPL in patient post-heparin plasma was a result of altered in vivo processing.	Heparin	97-104	lipoprotein lipase	Homo sapiens	34-37
8728326-8	1996	Analysis of the heparin binding properties of the mutant enzymes by heparin-Sepharose affinity chromatography indicated that most of the LPL-262 mass was present in an inactive peak, which like the normal LPL monomer, eluted at 0.8 M NaCl.	Heparin	16-23	lipoprotein lipase	Homo sapiens	137-140
8728326-9	1996	Thus, the Tyr262 --> His mutation may alter the stability of the LPL dimer, leading to the formation of inactive LPL-262 monomer which exhibits reduced heparin affinity.	Heparin	152-159	lipoprotein lipase	Homo sapiens	65-68
8728326-9	1996	Thus, the Tyr262 --> His mutation may alter the stability of the LPL dimer, leading to the formation of inactive LPL-262 monomer which exhibits reduced heparin affinity.	Heparin	152-159	lipoprotein lipase	Homo sapiens	113-116
8907299-4	1996	Heparins exert their anticoagulant effect by enhancing ATIII inhibitory action on factor Xa and thrombin, which results in decreased factor X activation, prothrombinase formation, prothrombin activation and thrombin generation.	Heparin	0-8	serpin family C member 1	Homo sapiens	55-60
8907301-4	1996	Although it is well established that the in vitro and in vivo anticoagulant activities of heparin is mediated via the potentiation of the major coagulation inhibitor, antithrombin III (ATIII), some in vivo antithrombotic mechanisms are not fully understood.	Heparin	90-97	serpin family C member 1	Homo sapiens	167-183
8907301-4	1996	Although it is well established that the in vitro and in vivo anticoagulant activities of heparin is mediated via the potentiation of the major coagulation inhibitor, antithrombin III (ATIII), some in vivo antithrombotic mechanisms are not fully understood.	Heparin	90-97	serpin family C member 1	Homo sapiens	185-190
7734360-0	1995	Antithrombins Southport (Leu 99 to Val) and Vienna (Gln 118 to Pro): two novel antithrombin variants with abnormal heparin binding.	Heparin	115-122	serpin family C member 1	Homo sapiens	79-91
7538367-3	1995	Of the 6 IGFBPs, IGFBP-3 and IGFBP-5 had the greatest heparin affinity.	Heparin	54-61	insulin like growth factor binding protein 3	Homo sapiens	9-15
32709152-4	2020	Here we hypothesized that tryptase, as well as being stabilized by heparin, can be stabilized by DNA, the rationale being that the anionic charge of DNA could potentially substitute for that of heparin to execute this function.	Heparin	194-201	tryptase alpha/beta 1	Mus musculus	26-34
7538367-3	1995	Of the 6 IGFBPs, IGFBP-3 and IGFBP-5 had the greatest heparin affinity.	Heparin	54-61	insulin like growth factor binding protein 3	Homo sapiens	17-24
8601723-4	1996	At 37 degree C and pH 7.2, radioactively labeled MIP-1 beta, RANTES, and heparanase bound to confluent layers of resting keratinocytes in a saturable and an heparan sulfate- or heparin-dependent manner, and thereby induced the adhesion of resting CD4+ T cells to keratinocytes.	Heparin	177-184	C-C motif chemokine ligand 4	Homo sapiens	49-59
32709152-8	2020	Further, we showed that DNA-stabilized tryptase was more efficient in degrading nuclear core histones than heparin-stabilized enzyme.	Heparin	107-114	tryptase alpha/beta 1	Mus musculus	39-47
7538367-4	1995	Peptides of 18 amino acids were synthesized, corresponding to a common basic region of IGFBP-3 (P3), IGFBP-5 and IGFBP-6 (P6) which contained a heparin binding sequence.	Heparin	144-151	insulin like growth factor binding protein 3	Homo sapiens	87-94
32272450-2	2020	Heparin-binding epidermal growth factor-like growth factor (HB-EGF), an EGF family member, stimulates differentiation and invasive capacity of extravillous trophoblasts in vitro.	Heparin	0-7	heparin binding EGF like growth factor	Homo sapiens	60-66
10155375-2	1995	However, the anticoagulation activity of heparin is based on its binding to antithrombin, and if the specific structure involved in this interaction is compromised by the coating procedure, then the activity is lost.	Heparin	41-48	serpin family C member 1	Homo sapiens	76-88
8815578-5	1996	Heparinase digestion of Desmin 370 eliminated 90% of the in vitro anti-Xa activity without significantly interfering with its ability to potentiate inactivation of thrombin by HCII, suggesting that the anti-Xa activity is not due to dermatan sulphate and is probably heparin.	Heparin	267-274	desmin	Homo sapiens	24-30
8815578-9	1996	We conclude that Desmin 370 contains detectable quantities of biologically active low molecular weight heparin, which is responsible for persistent anti-Xa activity following intravenous administration.	Heparin	103-110	desmin	Homo sapiens	17-23
32503118-3	2020	Here, we showed that a conjugate of 2,5-dihydroxybenzoic acid with gelatin (2,5-DHBA-gelatin), a synthetic polymer with heparin-like properties, suppressed the basal (unstimulated) migration and invasion of human glioblastoma A-172 and fibrosarcoma HT1080 cells, which was accompanied by the detachment of a fraction of Hsp90 from cell surface HSPGs.	Heparin	120-127	heat shock protein 90 alpha family class A member 1	Homo sapiens	320-325
8734279-6	1996	Immediately postoperatively the patient received therapeutic doses of heparin with AT-III concentrates to increase AT-III levels; no recurrent thrombotic episode was observed.	Heparin	70-77	serpin family C member 1	Homo sapiens	115-121
8766399-6	1996	AT III is of special importance for the treatment of DIC, where as different opinions exist regarding the application of heparin.	Heparin	121-128	serpin family C member 1	Homo sapiens	0-6
8565823-7	1996	Epidermal growth factor (EGF) and fibroblast growth factor-4 (FGF-4) inhibited apoptosis in the dental mesenchyme when applied locally using agarose or heparin-coated acrylic beads, suggesting involvement of these or related growth factors in the prevention of apoptosis in dental tissues in vivo.	Heparin	152-159	epidermal growth factor	Mus musculus	0-23
8565823-7	1996	Epidermal growth factor (EGF) and fibroblast growth factor-4 (FGF-4) inhibited apoptosis in the dental mesenchyme when applied locally using agarose or heparin-coated acrylic beads, suggesting involvement of these or related growth factors in the prevention of apoptosis in dental tissues in vivo.	Heparin	152-159	epidermal growth factor	Mus musculus	25-28
16727665-3	1995	In the presence of heparin (1, 10 and 100 microg/ml), nearly all the oocytes were fertilized with and without BSA.	Heparin	19-26	albumin	Bos taurus	110-113
7786411-0	1995	Tau protein kinase I/GSK-3 beta/kinase FA in heparin phosphorylates tau on Ser199, Thr231, Ser235, Ser262, Ser369, and Ser400 sites phosphorylated in Alzheimer disease brain.	Heparin	45-52	microtubule associated protein tau	Homo sapiens	0-3
7786411-0	1995	Tau protein kinase I/GSK-3 beta/kinase FA in heparin phosphorylates tau on Ser199, Thr231, Ser235, Ser262, Ser369, and Ser400 sites phosphorylated in Alzheimer disease brain.	Heparin	45-52	microtubule associated protein tau	Homo sapiens	68-71
7786411-2	1995	In this report, we find that the TPKI/GSK-3 beta/FA can be stimulated to phosphorylate brain tau up to 8.5 mol of phosphates per mol of protein by heparin, a polyanion compound.	Heparin	147-154	microtubule associated protein tau	Homo sapiens	93-96
7786411-4	1995	Phosphoamino acid analysis together with sequential manual Edman degradation and peptide sequence analysis further reveals that TPKI/GSK-3 beta/FA after heparin potentiation phosphorylates tau on sites of Ser199, Thr231, Ser235, Ser262, Ser396, and Ser400, which are potential sites abnormally phosphorylated in Alzheimer tau and potent sites responsible for reducing microtubule binding possibly involved in neuronal degeneration.	Heparin	153-160	microtubule associated protein tau	Homo sapiens	189-192
7786411-4	1995	Phosphoamino acid analysis together with sequential manual Edman degradation and peptide sequence analysis further reveals that TPKI/GSK-3 beta/FA after heparin potentiation phosphorylates tau on sites of Ser199, Thr231, Ser235, Ser262, Ser396, and Ser400, which are potential sites abnormally phosphorylated in Alzheimer tau and potent sites responsible for reducing microtubule binding possibly involved in neuronal degeneration.	Heparin	153-160	microtubule associated protein tau	Homo sapiens	322-325
7786411-5	1995	The results provide initial evidence that TPKI/GSK-3 beta/FA after heparin potentiation may represent one of the most potent systems possibly involved in the abnormal phosphorylation of PHF-tau and neuronal degeneration in Alzheimer disease brains.	Heparin	67-74	microtubule associated protein tau	Homo sapiens	186-193
7832187-0	1995	Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin.	Heparin	109-116	serpin family C member 1	Homo sapiens	0-12
7832187-0	1995	Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin.	Heparin	109-116	serpin family C member 1	Homo sapiens	88-104
7832187-6	1995	Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin.	Heparin	98-105	serpin family C member 1	Homo sapiens	188-194
7832187-6	1995	Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin.	Heparin	140-147	serpin family C member 1	Homo sapiens	188-194
8664906-1	1996	Human antithrombin is the major plasma inhibitor of thrombin both in the presence and absence of heparin.	Heparin	97-104	serpin family C member 1	Homo sapiens	6-18
8788110-0	1996	Effect of fibronectin on the binding of antithrombin III to immobilized heparin.	Heparin	72-79	serpin family C member 1	Homo sapiens	40-56
8788110-2	1996	The competition and binding interaction between immobilized heparin and antithrombin III (ATIII)/thrombin have been described in vitro.	Heparin	60-67	serpin family C member 1	Homo sapiens	72-88
8788110-2	1996	The competition and binding interaction between immobilized heparin and antithrombin III (ATIII)/thrombin have been described in vitro.	Heparin	60-67	serpin family C member 1	Homo sapiens	90-95
7832187-6	1995	Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin.	Heparin	140-147	serpin family C member 1	Homo sapiens	188-194
7832187-10	1995	Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin.	Heparin	0-7	serpin family C member 1	Homo sapiens	38-44
8788110-6	1996	The binding interaction of immobilized heparin with ATIII was then determined in the presence of different fibronectin concentrations.	Heparin	39-46	serpin family C member 1	Homo sapiens	52-57
31943091-3	2020	This non-signal producing Met-HGF interaction can also be eliminated by addition of a heparin mimetic sucrose octasulphate (SOS).	Heparin	86-93	SAFB like transcription modulator	Homo sapiens	26-29
8858487-0	1996	The interactions between antithrombin III, thrombin and surface immobilized heparin.	Heparin	76-83	serpin family C member 1	Homo sapiens	25-41
8858487-2	1996	Carboxylated polystyrene modified with covalently immobilized albumin-heparin conjugate contain sites which can bind ATIII from buffer and plasma solutions.	Heparin	70-77	serpin family C member 1	Homo sapiens	117-122
8858487-7	1996	It was observed that heparin binding proteins were able to compete with ATIII for binding to the immobilized heparin.	Heparin	21-28	serpin family C member 1	Homo sapiens	72-77
8858487-15	1996	In general it was concluded that only the surface immobilized heparin molecules that can bind ATIII in a reversible way determine the anticoagulant properties of the surface.	Heparin	62-69	serpin family C member 1	Homo sapiens	94-99
7832187-10	1995	Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin.	Heparin	0-7	serpin family C member 1	Homo sapiens	249-265
8858487-16	1996	The mechanism of inactivation of a protease on a heparinized surface depends either on the catalytic effect of heparin on the inactivation rate of proteases by ATIII or on an increased uncatalytic inactivation due to increased concentrations of ATIII near the surface as compared to the concentration of ATIII in the bulk phase.	Heparin	49-56	serpin family C member 1	Homo sapiens	160-165
32483116-2	2020	Here we construct heparin-coated 3D-printed hydrogel scaffolds seeded with hypoxia inducible factor-1alpha (HIF-1alpha)-mutated muscle-derived stem cells (MDSCs) to develop bioengineered vascularized corpora.	Heparin	18-25	hypoxia-inducible factor 1-alpha	Oryctolagus cuniculus	75-106
8858487-16	1996	The mechanism of inactivation of a protease on a heparinized surface depends either on the catalytic effect of heparin on the inactivation rate of proteases by ATIII or on an increased uncatalytic inactivation due to increased concentrations of ATIII near the surface as compared to the concentration of ATIII in the bulk phase.	Heparin	49-56	serpin family C member 1	Homo sapiens	245-250
8858487-16	1996	The mechanism of inactivation of a protease on a heparinized surface depends either on the catalytic effect of heparin on the inactivation rate of proteases by ATIII or on an increased uncatalytic inactivation due to increased concentrations of ATIII near the surface as compared to the concentration of ATIII in the bulk phase.	Heparin	49-56	serpin family C member 1	Homo sapiens	245-250
8592081-4	1996	A second growth factor was identified as heparin-binding epidermal growth factor-like growth factor (HB-EGF) based on its heparin affinity, competition with 125I-labeled epidermal growth factor (EGF) for EGF receptor binding, and recognition in biological assays and Western blots by two HB-EGF antisera.	Heparin	41-48	heparin binding EGF like growth factor	Homo sapiens	101-107
8592081-4	1996	A second growth factor was identified as heparin-binding epidermal growth factor-like growth factor (HB-EGF) based on its heparin affinity, competition with 125I-labeled epidermal growth factor (EGF) for EGF receptor binding, and recognition in biological assays and Western blots by two HB-EGF antisera.	Heparin	41-48	heparin binding EGF like growth factor	Homo sapiens	288-294
8592081-4	1996	A second growth factor was identified as heparin-binding epidermal growth factor-like growth factor (HB-EGF) based on its heparin affinity, competition with 125I-labeled epidermal growth factor (EGF) for EGF receptor binding, and recognition in biological assays and Western blots by two HB-EGF antisera.	Heparin	122-129	heparin binding EGF like growth factor	Homo sapiens	101-107
8726866-1	1996	UNLABELLED: This study examined the effects of the anticoagulant heparin on plasma follistatin (FS) concentrations used during blood sampling in Corriedale ewes.	Heparin	65-72	follistatin	Ovis aries	83-94
32483116-2	2020	Here we construct heparin-coated 3D-printed hydrogel scaffolds seeded with hypoxia inducible factor-1alpha (HIF-1alpha)-mutated muscle-derived stem cells (MDSCs) to develop bioengineered vascularized corpora.	Heparin	18-25	hypoxia-inducible factor 1-alpha	Oryctolagus cuniculus	108-118
32466274-5	2020	Moreover, multilayers containing either HA or Hep dampened the inflammatory response visible by reduced adhesion, formation of multinucleated giant cells (MNGCs) and IL-1beta release, which was studied using THP-1 derived macrophages.	Heparin	46-49	interleukin 1 alpha	Homo sapiens	166-174
8547175-7	1995	The behaviour of 3 beta-HSD on a column of Heparin-Sepharose is modified by the presence of cyt.	Heparin	43-50	3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase	Bos taurus	17-27
32332168-7	2020	Heparin binding stabilizes LPL helices, and the presence of substrate triggers helix disassembly.	Heparin	0-7	lipoprotein lipase	Homo sapiens	27-30
7488169-2	1995	By these purification steps, DNA polymerase and proliferating cell nuclear antigen (PCNA) were completely separated at the step of heparin-Sepharose CL-6B column chromatography.	Heparin	131-138	proliferating cell nuclear antigen	Homo sapiens	48-82
32088260-4	2020	Commercial heparins were shown to be strong inhibitors of hepcidin expression, by interfering with BMP6/SMAD pathway.	Heparin	11-19	hepcidin antimicrobial peptide	Homo sapiens	58-66
7488169-2	1995	By these purification steps, DNA polymerase and proliferating cell nuclear antigen (PCNA) were completely separated at the step of heparin-Sepharose CL-6B column chromatography.	Heparin	131-138	proliferating cell nuclear antigen	Homo sapiens	84-88
8573397-2	1995	The major anticoagulant activity of heparin results from binding to the plasma protein antithrombin (AT).	Heparin	36-43	serpin family C member 1	Homo sapiens	87-99
32088260-6	2020	To perform its anti-hepcidin activity heparin needs 2O- and 6O-sulfation and an average molecular weight (MW) up to 4000-8000 Dalton, depending on the sulfation level.	Heparin	38-45	hepcidin antimicrobial peptide	Homo sapiens	20-28
31750755-1	2020	BACKGROUND: Antithrombin III deficiency can occur with heparin anticoagulation during extracorporeal membrane oxygenation leading to heparin resistance.	Heparin	55-62	serpin family C member 1	Homo sapiens	12-28
8582900-0	1995	Interaction of antithrombin III with surface-immobilized albumin-heparin conjugates.	Heparin	65-72	serpin family C member 1	Homo sapiens	15-31
8582900-4	1995	The binding of ATIII to surface binding sites with a high affinity for ATIII was correlated with the presence of specific ATIII binding sites in the immobilized heparin.	Heparin	161-168	serpin family C member 1	Homo sapiens	15-20
8582900-4	1995	The binding of ATIII to surface binding sites with a high affinity for ATIII was correlated with the presence of specific ATIII binding sites in the immobilized heparin.	Heparin	161-168	serpin family C member 1	Homo sapiens	71-76
8582900-4	1995	The binding of ATIII to surface binding sites with a high affinity for ATIII was correlated with the presence of specific ATIII binding sites in the immobilized heparin.	Heparin	161-168	serpin family C member 1	Homo sapiens	71-76
8582900-5	1995	Binding of ATIII from albumin solutions to binding sites with a low affinity for ATIII was dominated by nonspecific binding of ATIII to the immobilized heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	11-16
8582900-5	1995	Binding of ATIII from albumin solutions to binding sites with a low affinity for ATIII was dominated by nonspecific binding of ATIII to the immobilized heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	81-86
31750755-1	2020	BACKGROUND: Antithrombin III deficiency can occur with heparin anticoagulation during extracorporeal membrane oxygenation leading to heparin resistance.	Heparin	133-140	serpin family C member 1	Homo sapiens	12-28
8582900-5	1995	Binding of ATIII from albumin solutions to binding sites with a low affinity for ATIII was dominated by nonspecific binding of ATIII to the immobilized heparin.	Heparin	152-159	serpin family C member 1	Homo sapiens	81-86
8582900-7	1995	ATIII is probably adsorbed to sites on the surface not covered with heparin.	Heparin	68-75	serpin family C member 1	Homo sapiens	0-5
31750755-4	2020	METHODS: We conducted a retrospective cohort study using electronic medical records of patients who received >=1 dose of antithrombin III during extracorporeal membrane oxygenation while on continuous heparin.	Heparin	201-208	serpin family C member 1	Homo sapiens	121-137
8582900-11	1995	The amount of ATIII bound to immobilized heparin via specific ATIII binding sites was 30% lower in plasma solutions as compared to the specific binding of ATIII using albumin solutions.	Heparin	41-48	serpin family C member 1	Homo sapiens	14-19
31750755-9	2020	Mean (standard deviation) heparin rates at 6 versus 12 h after antithrombin III for pediatrics were 23.6 (6) versus 23.5 (6.5) units/kg/h (p-value: 0.728), and 15.3 (6.6) versus 13.5 (8) units/kg/h (p-value: 0.188) for adults.	Heparin	26-33	serpin family C member 1	Homo sapiens	63-79
8582900-11	1995	The amount of ATIII bound to immobilized heparin via specific ATIII binding sites was 30% lower in plasma solutions as compared to the specific binding of ATIII using albumin solutions.	Heparin	41-48	serpin family C member 1	Homo sapiens	62-67
8582900-11	1995	The amount of ATIII bound to immobilized heparin via specific ATIII binding sites was 30% lower in plasma solutions as compared to the specific binding of ATIII using albumin solutions.	Heparin	41-48	serpin family C member 1	Homo sapiens	62-67
31750755-11	2020	Our findings suggest that the use of antithrombin III restores heparin responsiveness in patients with low antithrombin III activity and low anti-Xa activity.	Heparin	63-70	serpin family C member 1	Homo sapiens	37-53
8582900-12	1995	It is concluded that the accessibility of immobilized heparin for ATIII in plasma decreases by binding of heparin-binding proteins onto the immobilized heparin and/or adsorption of other plasma proteins on the heparinized surface.	Heparin	54-61	serpin family C member 1	Homo sapiens	66-71
8582900-12	1995	It is concluded that the accessibility of immobilized heparin for ATIII in plasma decreases by binding of heparin-binding proteins onto the immobilized heparin and/or adsorption of other plasma proteins on the heparinized surface.	Heparin	106-113	serpin family C member 1	Homo sapiens	66-71
8582900-12	1995	It is concluded that the accessibility of immobilized heparin for ATIII in plasma decreases by binding of heparin-binding proteins onto the immobilized heparin and/or adsorption of other plasma proteins on the heparinized surface.	Heparin	106-113	serpin family C member 1	Homo sapiens	66-71
8562839-0	1995	Thrombocytopenia, antithrombin deficiency and extensive thromboembolism in pregnancy: treatment with low-molecular-weight heparin.	Heparin	122-129	serpin family C member 1	Homo sapiens	18-30
8562839-2	1995	We describe a case of extensive thromboembolism associated with antithrombin (AT) deficiency complicated by thrombocytopenia which resolved when low-molecular-weight heparin was instituted.	Heparin	166-173	serpin family C member 1	Homo sapiens	64-76
31750755-11	2020	Our findings suggest that the use of antithrombin III restores heparin responsiveness in patients with low antithrombin III activity and low anti-Xa activity.	Heparin	63-70	serpin family C member 1	Homo sapiens	107-123
8557728-0	1995	Antithrombin activity of surface-bound heparin studied under flow conditions.	Heparin	39-46	serpin family C member 1	Homo sapiens	0-12
8557728-5	1995	It is demonstrated that the rate of thrombin inactivation at the antithrombin-heparin surface equals the maximal rate of transport of thrombin toward the surface when the surface coverage of antithrombin exceeds 10 pmol/cm2.	Heparin	78-85	serpin family C member 1	Homo sapiens	65-77
32402428-1	2020	The recognized therapeutic effect of heparins is an anticoagulant activity (anti-Xa and anti-IIa) acting in an indirect manner (cofactor of antithrombin) but which is carried by only 20% at best of the glycan chains composing any commercial preparation of heparin, whether unfractionated or low molecular weight.	Heparin	37-45	serpin family C member 1	Homo sapiens	140-152
8557728-5	1995	It is demonstrated that the rate of thrombin inactivation at the antithrombin-heparin surface equals the maximal rate of transport of thrombin toward the surface when the surface coverage of antithrombin exceeds 10 pmol/cm2.	Heparin	78-85	serpin family C member 1	Homo sapiens	191-203
8557728-8	1995	The uptake of antithrombin increased with the heparin content of the surface, but the stoichiometry decreased from 2 to 0.5 pmol antithrombin/micrograms heparin.	Heparin	46-53	serpin family C member 1	Homo sapiens	14-26
32402428-1	2020	The recognized therapeutic effect of heparins is an anticoagulant activity (anti-Xa and anti-IIa) acting in an indirect manner (cofactor of antithrombin) but which is carried by only 20% at best of the glycan chains composing any commercial preparation of heparin, whether unfractionated or low molecular weight.	Heparin	37-44	serpin family C member 1	Homo sapiens	140-152
8557728-8	1995	The uptake of antithrombin increased with the heparin content of the surface, but the stoichiometry decreased from 2 to 0.5 pmol antithrombin/micrograms heparin.	Heparin	153-160	serpin family C member 1	Homo sapiens	14-26
7548166-5	1995	We also show that protamine was able to displace AChE bound to heparin-agarose.	Heparin	63-70	acetylcholinesterase	Rattus norvegicus	49-53
32410995-3	2020	Here, kaempferol was shown to bind with vascular endothelial growth factor (VEGF), probably in the heparin binding domain of VEGF: this binding potentiated the angiogenic functions of VEGF in various culture models.	Heparin	99-106	vascular endothelial growth factor A	Rattus norvegicus	125-129
7548166-7	1995	Finally, we propose that two heparin-binding consensus sequences (-B-B-X-B-) are present in the tail of AChE.	Heparin	29-36	acetylcholinesterase	Rattus norvegicus	104-108
32410995-3	2020	Here, kaempferol was shown to bind with vascular endothelial growth factor (VEGF), probably in the heparin binding domain of VEGF: this binding potentiated the angiogenic functions of VEGF in various culture models.	Heparin	99-106	vascular endothelial growth factor A	Rattus norvegicus	125-129
32048330-2	2020	Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions.	Heparin	0-22	serpin family C member 1	Homo sapiens	83-99
7668220-2	1995	Recombinant hirudin is potentially effective as an antithrombotic treatment in the management of heparin-induced thrombocytopenia, given its potent antithrombin effects without known interaction with platelets.	Heparin	97-104	serpin family C member 1	Homo sapiens	148-160
32048330-2	2020	Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions.	Heparin	0-22	serpin family C member 1	Homo sapiens	101-107
32048330-2	2020	Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions.	Heparin	24-27	serpin family C member 1	Homo sapiens	83-99
7582773-0	1995	[Significance of heparin elimination from plasma in the assessment of coagulogram and antithrombin III activity].	Heparin	17-24	serpin family C member 1	Homo sapiens	86-102
32048330-2	2020	Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions.	Heparin	24-27	serpin family C member 1	Homo sapiens	101-107
31903737-10	2020	In vitro coadministration of heparin normalized the procoagulant effect and required dose escalation based on TF expression.	Heparin	29-36	coagulation factor III, tissue factor	Homo sapiens	110-112
7642636-4	1995	to understand the interaction of mMCP-7 with heparin inside and outside the mast cell, this trytase was first studied by comparative protein modeling.	Heparin	45-52	tryptase alpha/beta 1	Mus musculus	33-39
7642636-6	1995	Although mMCP-7 lacks known linear sequences of amino acis that interact with heparin, the three-dimensional model of mMCP-7 revealed an area on the surface of the folded protein away from the substrate-binding site that exhibits a strong positive electrostatic potential at the acidic pH of the granule.	Heparin	78-85	tryptase alpha/beta 1	Mus musculus	9-15
7642636-7	1995	In agreement with this calculation, recombinant pro-mMCP-7 bound to a heparin-affinity column at pH 5.5 and readily dissociated from the column at pH &gt; 6.5.	Heparin	70-77	tryptase alpha/beta 1	Mus musculus	52-58
31903737-14	2020	The TF procoagulant effect is reversible with heparin.	Heparin	46-53	coagulation factor III, tissue factor	Homo sapiens	4-6
31895135-14	2020	The AT-III mRNA levels increased from groups A to C and was positively associated with heparin sensitivity; the factor X mRNA levels changed in the opposite direction; a significant difference was observed between groups A and C (P < 0.05).	Heparin	87-94	serpin family C member 1	Homo sapiens	4-10
7561632-9	1995	Charge interaction between IGF-I and heparin could also protect IGF-I in the stomach but not in duodenum flushings.	Heparin	37-44	insulin-like growth factor 1	Rattus norvegicus	64-69
31895135-18	2020	Individual variation in heparin sensitivity is related to the mRNA and plasma levels of AT-III and factor X.	Heparin	24-31	serpin family C member 1	Homo sapiens	88-94
31778962-8	2020	The new CP-ELISA displayed a wide working range (0.10-6.78 mg CP/L) and low sample requirement (2 muL of serum, EDTA-, heparin- or citrate-plasma).	Heparin	119-126	ceruloplasmin	Homo sapiens	8-10
7676404-0	1995	Antithrombin binding by human umbilical vein endothelial cells: effects of exogenous heparin.	Heparin	85-92	serpin family C member 1	Homo sapiens	0-12
7599134-0	1995	Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity.	Heparin	230-237	serpin family C member 1	Homo sapiens	25-41
7599134-0	1995	Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity.	Heparin	230-237	serpin family C member 1	Homo sapiens	191-207
7599134-3	1995	The beta-ATIII isoform lacks carbohydrate on asparagine-135 (N135), which is near the heparin binding site, and binds heparin with higher affinity than does alpha-ATIII.	Heparin	86-93	serpin family C member 1	Homo sapiens	9-14
7599134-3	1995	The beta-ATIII isoform lacks carbohydrate on asparagine-135 (N135), which is near the heparin binding site, and binds heparin with higher affinity than does alpha-ATIII.	Heparin	118-125	serpin family C member 1	Homo sapiens	9-14
7599134-4	1995	Two isoforms are also produced when the normal human ATIII cDNA sequence is expressed in baculovirus-infected insect cells, and the recombinant beta" isoform similarly binds heparin with higher affinity than the recombinant alpha" isoform.	Heparin	174-181	serpin family C member 1	Homo sapiens	53-58
7788881-2	1995	Within FN, a number of functional domains have been identified, including the 33/66-kD carboxyl-terminal heparin-binding fragments, which support the adhesion of vascular endothelial cells.	Heparin	105-112	fibronectin 1	Rattus norvegicus	7-9
31894660-2	2020	Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays).	Heparin	359-366	serpin family C member 1	Homo sapiens	44-56
7788881-11	1995	These findings suggest that peptide FN-C/H-V is unique among this group of peptides derived from the 33/66-kD heparin-binding fragments of FN in its ability to promote the adhesion, spreading, and migration of vascular endothelial cells and further suggest that the sequence defined by this peptide plays an important role in vascular endothelial cell interactions with the 33/66-kD fragments of FN.	Heparin	110-117	fibronectin 1	Rattus norvegicus	36-38
7788881-11	1995	These findings suggest that peptide FN-C/H-V is unique among this group of peptides derived from the 33/66-kD heparin-binding fragments of FN in its ability to promote the adhesion, spreading, and migration of vascular endothelial cells and further suggest that the sequence defined by this peptide plays an important role in vascular endothelial cell interactions with the 33/66-kD fragments of FN.	Heparin	110-117	fibronectin 1	Rattus norvegicus	139-141
7613763-1	1995	By aligning nucleotide and amino acid sequences of lipoprotein lipase in eight species (man, pig, cow, sheep, mouse, rat, guinea-pig and chicken), we found that the main domains (catalytic, N-glycosylation and putative heparin binding sites) are well conserved.	Heparin	219-226	lipoprotein lipase	Homo sapiens	51-69
32009036-8	2020	The heparin-binding domain corresponding to the pre-S1(30-42) region has a strong affinity to heparin as compared to that of known heparin-binding peptides, such as vitronectin and gp120 in human immunodeficiency virus-1.	Heparin	4-11	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	181-186
7796887-5	1995	The binding can also be almost completely inhibited by preincubation of the 125I-labeled RIHB with heparin or with a monoclonal antibody which recognizes the heparin binding site of both RIHB and HBNF.	Heparin	158-165	pleiotrophin	Gallus gallus	196-200
31771729-1	2019	OBJECTIVE: To investigate the effects of heparin on the secretion of monocyte chemotactic protein-1 (MCP-1) in human umbilical vein endothelial cells (HUVEC) and the adhesion of monocytes to endothelial cells stimulated by lipopolysaccharide (LPS).	Heparin	41-48	C-C motif chemokine ligand 2	Homo sapiens	69-99
7609317-2	1995	Twenty six type IV hyperlipoproteinemic and 28 normolipidemic males underwent measurement of the immunoreactive LPL mass in postheparin plasma (30 unit of heparin/kg of body weight) and were interviewed as to their alcohol consumption.	Heparin	128-135	lipoprotein lipase	Homo sapiens	112-115
7657726-12	1995	Taken together, these data suggest that human bone cells, unlike bovine corneal epithelial cells, have an attachment mechanism for the heparin-binding region of fibronectin.	Heparin	135-142	fibronectin 1	Bos taurus	161-172
7721817-0	1995	Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin.	Heparin	79-86	serpin family C member 1	Homo sapiens	29-41
7721817-1	1995	Role of the antithrombin binding pentasaccharide in heparin rate enhancement.	Heparin	52-59	serpin family C member 1	Homo sapiens	12-24
31771729-1	2019	OBJECTIVE: To investigate the effects of heparin on the secretion of monocyte chemotactic protein-1 (MCP-1) in human umbilical vein endothelial cells (HUVEC) and the adhesion of monocytes to endothelial cells stimulated by lipopolysaccharide (LPS).	Heparin	41-48	C-C motif chemokine ligand 2	Homo sapiens	101-106
7721817-2	1995	The role of the sequence-specific pentasaccharide region of high affinity heparin (HAH) in heparin acceleration of antithrombin-proteinase reactions was elucidated by determining the accelerating mechanism of low affinity heparin (LAH) lacking this sequence.	Heparin	74-81	serpin family C member 1	Homo sapiens	115-127
7721817-2	1995	The role of the sequence-specific pentasaccharide region of high affinity heparin (HAH) in heparin acceleration of antithrombin-proteinase reactions was elucidated by determining the accelerating mechanism of low affinity heparin (LAH) lacking this sequence.	Heparin	91-98	serpin family C member 1	Homo sapiens	115-127
31771729-8	2019	Heparin preconditioning significantly reduced LPS-induced MCP-1 mRNA expression [2-DeltaDeltaCt: 2.06 (1.72, 2.46) vs. 16.41 (15.03, 18.00) at 6 hours, 2.46 (2.19, 4.56) vs. 9.27 (8.11, 9.85) at 12 hours, both P < 0.05].	Heparin	0-7	C-C motif chemokine ligand 2	Homo sapiens	58-63
7721817-7	1995	By contrast, LAH and HAH both accelerated the antithrombin-factor Xa reaction with a simple saturable dependence on heparin or inhibitor concentrations which paralleled the formation of an antithrombin-heparin binary complex.	Heparin	116-123	serpin family C member 1	Homo sapiens	46-58
7721817-8	1995	The maximal accelerations of the two heparins in this case correlated with the inhibitor fluorescence enhancements induced by the polysaccharides, consistent with the accelerations arising from conformational activation of antithrombin.	Heparin	37-45	serpin family C member 1	Homo sapiens	223-235
31771729-11	2019	CONCLUSIONS: Heparin preconditioning could inhibit the MCP-1 mRNA expression , thereby reduce the adhesion of THP-1 to HUVEC, thus play a protective role in sepsis.	Heparin	13-20	C-C motif chemokine ligand 2	Homo sapiens	55-60
31660084-3	2019	Methods: Characterization of Laponite, Laponite/Heparin (Lap/Hep) and Laponite/Heparin loaded with FGF4 (Lap/Hep@FGF4) hydrogels were measured by rheometer.	Heparin	79-86	fibroblast growth factor 4	Rattus norvegicus	99-103
7779998-3	1995	The results demonstrated that 1) in these blastocysts, contact of EPC cells with fibronectin-coated glass substratum in the presence of FBS triggered an outburst of cell proliferation with the eventual differentiation of the EPC cells into secondary giant trophoblast cells and 2) frequencies of blastocysts that exhibited EPC cell proliferation significantly increased if FO medium (modified Eagle"s minimum essential medium) was supplemented with FBS depleted of heparin-binding substances (H-FBS).	Heparin	465-472	fibronectin 1	Mus musculus	81-92
7721431-3	1995	To test this hypothesis, in two separate protocols 10% Intralipid was infused into a dorsal hand vein with heparin to activate lipoprotein lipase and raise fatty acid levels locally.	Heparin	107-114	lipoprotein lipase	Homo sapiens	127-145
7887917-0	1995	The heparin binding site of follistatin is involved in its interaction with activin.	Heparin	4-11	inhibin subunit beta E	Homo sapiens	76-83
7887917-1	1995	Whether the heparin-binding site of follistatin would interact with activin has been examined.	Heparin	12-19	inhibin subunit beta E	Homo sapiens	68-75
7887917-7	1995	These results indicated that mutation at the heparin binding site alters the activin binding affinity.	Heparin	45-52	inhibin subunit beta E	Homo sapiens	77-84
7887917-9	1995	These findings suggest that the heparin binding site of follistatin also contributes to its binding for activin, and heparin may play an important role in the bioactivity of follistatin.	Heparin	32-39	inhibin subunit beta E	Homo sapiens	104-111
31388039-4	2019	Characterization of ACE-083 in vitro revealed its high affinity for heparin and extracellular matrix while surface plasmon resonance and cell-based assays confirmed that ACE-083 binds and potently neutralizes myostatin, activin A, activin B and growth differentiation factor 11 (GDF11).	Heparin	68-75	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	20-23
7538797-4	1995	Uterine extracts also contained an EGF-R-binding factor that was eluted from heparin by 1.0 M NaCl and was antagonized by HB-EGF antiserum.	Heparin	77-84	epidermal growth factor	Sus scrofa	35-38
7883853-3	1995	Addition of GH (50 micrograms/L) to the cortisol-containing medium during the last 24 h (day 6) caused a decrease by 84 +/- 4% (P &lt; 0.01) in heparin-releasable LPL activity and by 65 +/- 4% (P &lt; 0.01) in total LPL activity.	Heparin	144-151	lipoprotein lipase	Homo sapiens	163-166
7883853-3	1995	Addition of GH (50 micrograms/L) to the cortisol-containing medium during the last 24 h (day 6) caused a decrease by 84 +/- 4% (P &lt; 0.01) in heparin-releasable LPL activity and by 65 +/- 4% (P &lt; 0.01) in total LPL activity.	Heparin	144-151	lipoprotein lipase	Homo sapiens	216-219
7883853-4	1995	Moreover, the heparin-releasable fraction was reduced from 42% of the total LPL activity with cortisol alone to 17% when both GH and cortisol were present in the incubation medium during the last 24 h (P &lt; 0.01).	Heparin	14-21	lipoprotein lipase	Homo sapiens	76-79
7531705-0	1995	A single heparin binding region within the fibrinogen-like domain is functional in chick tenascin-C.	Heparin	9-16	tenascin C	Gallus gallus	89-99
7531705-1	1995	Tenascin-C binds to cell surface and matrix proteoglycans and to heparin.	Heparin	65-72	tenascin C	Gallus gallus	0-10
30540616-4	2019	When heparin resistance was encountered, 54.2% of respondents (95% CI, 50.0%-58.4%) administered antithrombin concentrates as a first-line therapy.	Heparin	5-12	serpin family C member 1	Homo sapiens	97-109
7531705-2	1995	Two heparin binding regions have recently been localized per tenascin-C monomer, one in the C-terminal fibrinogen-like domain and the other in fibronectin type III repeats 3-5.	Heparin	4-11	tenascin C	Gallus gallus	61-71
7531705-2	1995	Two heparin binding regions have recently been localized per tenascin-C monomer, one in the C-terminal fibrinogen-like domain and the other in fibronectin type III repeats 3-5.	Heparin	4-11	fibronectin 1	Gallus gallus	143-154
7531705-3	1995	Here we show that a single region in each subunit is necessary and sufficient for heparin binding by whole tenascin-C at physiological ionic strength.	Heparin	82-89	tenascin C	Gallus gallus	107-117
7531705-4	1995	First, native tenascin-C was bound to heparin-agarose and digested with Pronase.	Heparin	38-45	tenascin C	Gallus gallus	14-24
7531705-11	1995	Thus, whole chick tenascin-C contains one essential heparin binding region per subunit, located in the fibrinogen-like domain within 10 kDa from the C terminus.	Heparin	52-59	tenascin C	Gallus gallus	18-28
7803789-4	1995	AT III alone and AT III/heparin to a greater extent reduced factor VIIa bound to cell surface TF.	Heparin	24-31	coagulation factor III, tissue factor	Homo sapiens	94-96
31212795-9	2019	The unique ascidian HS is a potent inhibitor of the binding of human colon adenocarcinoma cells to immobilized P-selectin, being 11-fold more potent than mammalian heparin, but almost ineffective as an anticoagulant.	Heparin	164-171	selectin P	Homo sapiens	111-121
7588997-3	1995	During the 30 s interaction, OSXS and SP-54 enhanced both AT-III-thrombin and HC-II-thrombin interaction while heparin was more selective and enhanced only the AT-III-thrombin interaction.	Heparin	111-118	serpin family C member 1	Homo sapiens	160-166
7588997-6	1995	The Western blotting method of detecting thrombin showed that during the 10 s interaction, heparin enhanced the thrombin-AT-III complex formation while OSXS enhanced the thrombin-HC-II complex formation.	Heparin	91-98	serpin family C member 1	Homo sapiens	121-127
7864824-2	1995	This phospholipase A2 was purified by sequential cation, hydrophobic, heparin and gel-filtration chromatography.	Heparin	70-77	phospholipase A2 group IB	Rattus norvegicus	5-21
7789600-0	1995	Administration of heparin inhalations for correction of blood antithrombin activity in pregnant women with IDDM.	Heparin	18-25	serpin family C member 1	Homo sapiens	62-74
31186035-1	2019	BACKGROUND: Normal levels of plasma antithrombin (AT) activity might decrease heparin requirements to achieve an adequate level of anticoagulation during treatment with extracorporeal membrane oxygenation (ECMO).	Heparin	78-85	serpin family C member 1	Homo sapiens	36-48
7532176-4	1995	b-FGF and HB-EGF binding to HS-modified CD44 was eliminated by pretreating the protein with heparitinase or by blocking with free heparin.	Heparin	130-137	heparin binding EGF like growth factor	Homo sapiens	10-16
8817695-6	1995	In addition, exogeneously added soluble heparin or heparan sulfate inhibited the binding of IGFBP-3 to the cell surface in a dose-dependent manner.	Heparin	40-47	insulin like growth factor binding protein 3	Homo sapiens	92-99
8817695-7	1995	However, when heparin and heparan sulfate linkages of glycosaminoglycans on the cell surface were enzymatically remove, IGFBP-3 binding was only minimally affected.	Heparin	14-21	insulin like growth factor binding protein 3	Homo sapiens	120-127
8817695-8	1995	These data suggest that soluble heparin or heparan sulfate forms a complex with IGFBP-3, thereby inhibiting receptor binding of IGFBP-3, rather than competing with cell-surface glycosaminoglycans for binding of IGFBP-3.	Heparin	32-39	insulin like growth factor binding protein 3	Homo sapiens	80-87
8817695-8	1995	These data suggest that soluble heparin or heparan sulfate forms a complex with IGFBP-3, thereby inhibiting receptor binding of IGFBP-3, rather than competing with cell-surface glycosaminoglycans for binding of IGFBP-3.	Heparin	32-39	insulin like growth factor binding protein 3	Homo sapiens	128-135
8817695-8	1995	These data suggest that soluble heparin or heparan sulfate forms a complex with IGFBP-3, thereby inhibiting receptor binding of IGFBP-3, rather than competing with cell-surface glycosaminoglycans for binding of IGFBP-3.	Heparin	32-39	insulin like growth factor binding protein 3	Homo sapiens	128-135
7660142-0	1995	Antithrombin III affinity dependence on the anticoagulant, antiprotease, and tissue factor pathway inhibitor actions of heparins.	Heparin	120-128	serpin family C member 1	Homo sapiens	0-16
7660142-1	1995	To investigate AT-III affinity dependence on heparin"s actions, heparin (UH) was fractionated on an AT-III-Sepharose column into a high (HAH) and a low affinity (LAH) fraction.	Heparin	45-52	serpin family C member 1	Homo sapiens	15-21
7660143-3	1995	The fractionated heparin retains many of its biological properties such as AT III affinity and sulfate content gamma-irradiation (60Co) has been used to depolymerize GAGs (De Ambrosi et al.	Heparin	17-24	serpin family C member 1	Homo sapiens	75-81
7660143-8	1995	In standard clotting and amidolytic antiprotease assays (PT, APTT, AXa, Alla), gamma-irradiated depolymerized heparin produced equal or stronger activity when compared to a LMWH produced by nitrous acid depolymerization and retained the ability to active AT III and HCHII.	Heparin	110-117	serpin family C member 1	Homo sapiens	255-261
7534486-6	1994	alpha 2-Macroglobulin inhibits fibrin-bound miniplasmin and PMN-elastase with a second-order rate constant of 1.8 x 10(4) M-1 s-1 and heparin (300 nM) increases the rate insignificantly for miniplasmin and by a factor of two for PMN-elastase.	Heparin	134-141	alpha-2-macroglobulin	Homo sapiens	0-21
7807964-0	1994	Heparin selectively inhibits synthesis of tissue type plasminogen activator and matrix deposition of plasminogen activator inhibitor 1 by human mesangial cells.	Heparin	0-7	serpin family E member 1	Homo sapiens	101-134
7807964-5	1994	The effect of heparin on the mesangial plasminogen activating system (tissue type plasminogen activator, t-PA, and plasminogen activator inhibitor type 1, PAI-1), which is thought to be involved in matrix remodelling, has not been previously reported.	Heparin	14-21	serpin family E member 1	Homo sapiens	155-160
7807964-12	1994	Heparin decreased PAI-1 matrix accumulation.	Heparin	0-7	serpin family E member 1	Homo sapiens	18-23
7807964-14	1994	Heparin decreased PAI-1 matrix accumulation.	Heparin	0-7	serpin family E member 1	Homo sapiens	18-23
7811743-3	1995	Nearly all the LPL in post-heparin plasma of controls bound to heparin-Sepharose and this LPL bound was mainly eluted with 1.5 M NaCl in parallel with the activity.	Heparin	27-34	lipoprotein lipase	Homo sapiens	15-18
7811743-3	1995	Nearly all the LPL in post-heparin plasma of controls bound to heparin-Sepharose and this LPL bound was mainly eluted with 1.5 M NaCl in parallel with the activity.	Heparin	27-34	lipoprotein lipase	Homo sapiens	90-93
7811743-3	1995	Nearly all the LPL in post-heparin plasma of controls bound to heparin-Sepharose and this LPL bound was mainly eluted with 1.5 M NaCl in parallel with the activity.	Heparin	63-70	lipoprotein lipase	Homo sapiens	15-18
7811743-3	1995	Nearly all the LPL in post-heparin plasma of controls bound to heparin-Sepharose and this LPL bound was mainly eluted with 1.5 M NaCl in parallel with the activity.	Heparin	63-70	lipoprotein lipase	Homo sapiens	90-93
7811743-4	1995	In post-heparin plasma of the patient, 58% of the LPL subunits did not bind to heparin-Sepharose and 23% was eluted with 0.6 M NaCl.	Heparin	8-15	lipoprotein lipase	Homo sapiens	50-53
7811743-5	1995	Studies by sucrose density gradient centrifugation showed that almost all the LPL in post-heparin plasma of controls was recovered in the peak with a sedimentation coefficient of 6.8 S, corresponding to the position of a dimeric form of LPL, in parallel with the activity; little LPL was recovered in the peak with a sedimentation coefficient of 4.0 S, corresponding to the position of a monomeric form of LPL.	Heparin	90-97	lipoprotein lipase	Homo sapiens	78-81
7811743-6	1995	In post-heparin plasma of the patient, 35% of the LPL subunits was recovered in fractions with larger sedimentation coefficients at the bottom of the centrifuge tube, indicating the presence of an aggregated form(s) of LPL; the amount of the monomeric form of LPL was increased, while that of the dimeric form was decreased.	Heparin	8-15	lipoprotein lipase	Homo sapiens	219-222
7811743-6	1995	In post-heparin plasma of the patient, 35% of the LPL subunits was recovered in fractions with larger sedimentation coefficients at the bottom of the centrifuge tube, indicating the presence of an aggregated form(s) of LPL; the amount of the monomeric form of LPL was increased, while that of the dimeric form was decreased.	Heparin	8-15	lipoprotein lipase	Homo sapiens	219-222
7811743-7	1995	Thus, defect of LPL activity in post-heparin plasma of the patient with hyperchylomicronemia could result from reduced dimerization of LPL subunits.	Heparin	37-44	lipoprotein lipase	Homo sapiens	16-19
7811743-7	1995	Thus, defect of LPL activity in post-heparin plasma of the patient with hyperchylomicronemia could result from reduced dimerization of LPL subunits.	Heparin	37-44	lipoprotein lipase	Homo sapiens	135-138
7811745-3	1995	LPL in normal cells was active, dimeric, and showed high affinity for heparin.	Heparin	70-77	lipoprotein lipase	Homo sapiens	0-3
7811745-5	1995	LPL proteins were found as an aggregate, and had low affinity for heparin.	Heparin	66-73	lipoprotein lipase	Homo sapiens	0-3
7811745-7	1995	Most of LPL proteins were totally endo H-sensitive, present as an aggregate, and had low affinity for heparin.	Heparin	102-109	lipoprotein lipase	Homo sapiens	8-11
7811745-8	1995	LPL in cells treated with deoxymannojirimycin, an inhibitor of Golgi mannosidase I, was active, dimeric, and had high affinity for heparin as in normal cells.	Heparin	131-138	lipoprotein lipase	Homo sapiens	0-3
7807964-16	1994	CONCLUSIONS: In human mesangial cells, anticoagulant and nonanticoagulant heparin exert an antiproliferative effect and may prevent mesangial matrix changes by decreasing FCS-stimulated t-PA synthesis and PAI-1 deposition in the matrix.	Heparin	74-81	serpin family E member 1	Homo sapiens	205-210
7526102-6	1994	In 7 control patients, PTCA caused a rise in platelet surface expression of P-selectin and glycoprotein IIb/IIIa, which was maximal 5 minutes after PTCA, indicating increased platelet activation despite treatment with aspirin, glyceryl trinitrate, and heparin.	Heparin	252-259	selectin P	Homo sapiens	76-86
30840313-7	2019	Moreover, E4 neurons released increased amounts of phosphorylated tau extracellularly in an isoform-dependent manner by a heparin sulfate proteoglycan-dependent mechanism.	Heparin	122-129	microtubule associated protein tau	Homo sapiens	66-69
7947827-2	1994	Lysine residues in two different regions of antithrombin have been proposed to be involved in heparin binding and heparin-mediated acceleration of proteinase inhibition.	Heparin	94-101	serpin family C member 1	Homo sapiens	44-56
7947827-2	1994	Lysine residues in two different regions of antithrombin have been proposed to be involved in heparin binding and heparin-mediated acceleration of proteinase inhibition.	Heparin	114-121	serpin family C member 1	Homo sapiens	44-56
7947827-10	1994	The K290M,K294M,K297M variant had properties very similar to those of wild-type recombinant antithrombin in affinity for heparin, and in rates of inhibition of thrombin and factor Xa.	Heparin	121-128	serpin family C member 1	Homo sapiens	92-104
7947827-11	1994	In contrast, K125M antithrombin had reduced affinity for both heparin pentasaccharide and full-length heparin, corresponding to delta delta Gs of 3.1 and 2.0 kcal mol-1, respectively.	Heparin	62-69	serpin family C member 1	Homo sapiens	19-31
7767440-1	1995	This work deals with the synthesis and blood compatibility studies of Heparin immobilized chitosan--polyethyleneglycol (Chit-PEG) hydrogels for various biomedical applications.	Heparin	70-77	chitinase 1	Homo sapiens	120-124
7767440-3	1995	An optimum gel combination was selected from the IPN of Chit-PEG and used for bonding heparin.	Heparin	86-93	chitinase 1	Homo sapiens	56-60
7767440-6	1995	Recalcification times of plasma exposed to heparin immobilized Chit-PEG hydrogel were markedly increased as compared to heparin free gels.	Heparin	43-50	chitinase 1	Homo sapiens	63-67
7767440-6	1995	Recalcification times of plasma exposed to heparin immobilized Chit-PEG hydrogel were markedly increased as compared to heparin free gels.	Heparin	120-127	chitinase 1	Homo sapiens	63-67
7806495-12	1994	Antithrombin employs a template mechanism that requires heparin to interact with thrombin exosite II, whereas HCII employs an allosteric mechanism that requires thrombin exosite I but is largely independent of exosite II.	Heparin	56-63	serpin family C member 1	Homo sapiens	0-12
7983076-4	1994	Two isoforms of transmembrane HB-EGF (HB-EGFTM) were purified from membrane fractions of infected insect cells by a combination of heparin affinity chromatography and reversed-phase high performance liquid chromatography.	Heparin	131-138	heparin binding EGF like growth factor	Homo sapiens	30-36
7983076-4	1994	Two isoforms of transmembrane HB-EGF (HB-EGFTM) were purified from membrane fractions of infected insect cells by a combination of heparin affinity chromatography and reversed-phase high performance liquid chromatography.	Heparin	131-138	heparin binding EGF like growth factor	Homo sapiens	38-46
7961924-1	1994	We have used a monoclonal antibody-based binding procedure to determine the dissociation constants of the interactions between the essential antithrombin-binding pentasaccharide and a series of 13 distinct N- and C-terminal antithrombin substitution mutation variants with defective binding interaction with heparin.	Heparin	308-315	serpin family C member 1	Homo sapiens	141-153
7524669-7	1994	HRG also binds to extracellular matrices (ECM), originating from bovine corneal endothelial cells, in a heparin-inhibitable manner.	Heparin	104-111	histidine rich glycoprotein	Bos taurus	0-3
7947925-0	1994	Binding of serum amyloid P component to heparin in human serum.	Heparin	40-47	amyloid P component, serum	Homo sapiens	11-36
7947925-2	1994	We employed a quantitative immunoelectrophoresis (QIE) method and a native polyacrylamide gel electrophoresis (PAGE) method to characterize the SAP-heparin binding in soluble state.	Heparin	148-155	amyloid P component, serum	Homo sapiens	144-147
7947925-4	1994	The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06 x 10(-7) M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91 x 10(-7) M at 2 mM CaCl2, when estimated by the QIE method.	Heparin	24-31	amyloid P component, serum	Homo sapiens	51-54
7947925-4	1994	The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06 x 10(-7) M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91 x 10(-7) M at 2 mM CaCl2, when estimated by the QIE method.	Heparin	24-31	amyloid P component, serum	Homo sapiens	114-117
7947925-4	1994	The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06 x 10(-7) M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91 x 10(-7) M at 2 mM CaCl2, when estimated by the QIE method.	Heparin	24-31	amyloid P component, serum	Homo sapiens	114-117
7947925-4	1994	The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06 x 10(-7) M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91 x 10(-7) M at 2 mM CaCl2, when estimated by the QIE method.	Heparin	118-125	amyloid P component, serum	Homo sapiens	51-54
7947925-4	1994	The apparent numbers of heparin molecules bound to SAP varied with the calcium concentration with a ratio of 1:1 (SAP/heparin), a Kd of 2.06 x 10(-7) M at 0.1 mM CaCl2 and a ratio of 1:1.6 (SAP/heparin), a Kd of 3.91 x 10(-7) M at 2 mM CaCl2, when estimated by the QIE method.	Heparin	118-125	amyloid P component, serum	Homo sapiens	51-54
7979371-4	1994	Heparin fractions differing in size and in antithrombin III affinity were prepared.	Heparin	0-7	serpin family C member 1	Homo sapiens	43-59
7840818-9	1994	Post-heparin plasma (PHP) LPL activity and mass increased significantly (P &lt; 0.01) after the alcohol ingestion (controls remained unchanged) without changing LPL specific activity.	Heparin	5-12	lipoprotein lipase	Homo sapiens	26-29
7955182-2	1994	BACKGROUND: Heparin needs the plasma protein antithrombin III to function as an inhibitor of thrombin, and local antithrombin III deficiency might therefore limit the antithrombotic effectiveness of heparin during percutaneous transluminal coronary angioplasty.	Heparin	12-19	serpin family C member 1	Homo sapiens	45-61
30842157-0	2019	ROBO1 Expression in Metastasizing Breast and Ovarian Cancer: SLIT2-induced Chemotaxis Requires Heparan Sulfates (Heparin).	Heparin	113-120	slit guidance ligand 2	Homo sapiens	61-66
7955182-2	1994	BACKGROUND: Heparin needs the plasma protein antithrombin III to function as an inhibitor of thrombin, and local antithrombin III deficiency might therefore limit the antithrombotic effectiveness of heparin during percutaneous transluminal coronary angioplasty.	Heparin	199-206	serpin family C member 1	Homo sapiens	45-61
7868983-8	1994	These data demonstrate that charged residues at positions 279-282 and 292-304 of LPL are important for heparin binding affinity whereas the residues 390-393 and 439-448 in the C-terminal domain are not involved in heparin binding.	Heparin	103-110	lipoprotein lipase	Homo sapiens	81-84
7829396-4	1994	This enhanced DNA synthesis was blocked by exposing the cells to AIGF antisense oligonucleotides, heparin, or suramin, indicating that enforced AIGF expression is responsible for the increase in DNA synthesis.	Heparin	98-105	fibroblast growth factor 8	Homo sapiens	144-148
30842157-9	2019	CONCLUSION: SLIT2 can induce BC cell motility and chemotaxis, but the latter requires the presence of heparin.	Heparin	102-109	slit guidance ligand 2	Homo sapiens	12-17
7863481-3	1994	In both cases, the expression of the mutation is pleiotropic, i.e. results in a reduction in the circulating concentration of antithrombin and impairs both its anti-thrombin activity and its ability to bind heparin.	Heparin	207-214	serpin family C member 1	Homo sapiens	126-138
7929416-4	1994	The inhibition constant of heparin with low affinity for antithrombin was indistinguishable from heparin with high affinity for antithrombin (Ki = 20 nM).	Heparin	27-34	serpin family C member 1	Homo sapiens	57-69
30660948-0	2019	Monitoring of heparins in antithrombin-deficient patients.	Heparin	14-22	serpin family C member 1	Homo sapiens	26-38
7929416-4	1994	The inhibition constant of heparin with low affinity for antithrombin was indistinguishable from heparin with high affinity for antithrombin (Ki = 20 nM).	Heparin	97-104	serpin family C member 1	Homo sapiens	128-140
7929416-9	1994	We propose that part of the antithrombotic action of heparin and low molecular weight heparin is due to anti-thrombin-independent inhibition of intrinsic fXase and that heparin with low affinity for antithrombin may be useful as an antithrombotic agent.	Heparin	53-60	serpin family C member 1	Homo sapiens	199-211
7532447-4	1994	Antithrombin, which does not inhibit APC but which does bind to heparin/heparan sulphate with higher affinity than PCI, caused only a small decrease in the inhibition rate of PCI-APC in the presence of unfractionated heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	0-12
7532447-4	1994	Antithrombin, which does not inhibit APC but which does bind to heparin/heparan sulphate with higher affinity than PCI, caused only a small decrease in the inhibition rate of PCI-APC in the presence of unfractionated heparin.	Heparin	217-224	serpin family C member 1	Homo sapiens	0-12
7522051-5	1994	The mutant K128Q-K138Q required a 10-fold higher concentration of heparin to promote binding to heparan sulfate proteoglycan (HSPG)-deficient CHO cells transfected with fibroblast growth factor receptor-1 (FGFR1) or to induce DNA synthesis in HSPG-deficient myeloid cells transfected with FGFR1.	Heparin	66-73	fibroblast growth factor receptor 1	Cricetulus griseus	169-204
7522051-5	1994	The mutant K128Q-K138Q required a 10-fold higher concentration of heparin to promote binding to heparan sulfate proteoglycan (HSPG)-deficient CHO cells transfected with fibroblast growth factor receptor-1 (FGFR1) or to induce DNA synthesis in HSPG-deficient myeloid cells transfected with FGFR1.	Heparin	66-73	fibroblast growth factor receptor 1	Cricetulus griseus	206-211
7522051-5	1994	The mutant K128Q-K138Q required a 10-fold higher concentration of heparin to promote binding to heparan sulfate proteoglycan (HSPG)-deficient CHO cells transfected with fibroblast growth factor receptor-1 (FGFR1) or to induce DNA synthesis in HSPG-deficient myeloid cells transfected with FGFR1.	Heparin	66-73	fibroblast growth factor receptor 1	Cricetulus griseus	289-294
7553356-1	1994	Previously we have shown that the measurable soluble sialyltransferase (STase) activity released into the medium during the incubation of rat jejunal slices was dependent upon the presence of a heparin-binding fraction (HBF) from heat-inactivated serum or a trypsin-binding protein (TBP) isolated from HBF.	Heparin	194-201	TATA box binding protein	Rattus norvegicus	258-281
7553356-1	1994	Previously we have shown that the measurable soluble sialyltransferase (STase) activity released into the medium during the incubation of rat jejunal slices was dependent upon the presence of a heparin-binding fraction (HBF) from heat-inactivated serum or a trypsin-binding protein (TBP) isolated from HBF.	Heparin	194-201	TATA box binding protein	Rattus norvegicus	283-286
7931292-6	1994	As Ser235, Ser262, Ser324, Ser356, and Ser404 (particularly the site of Ser262) have been identified as five of the most potent sites in tau responsible for reducing microtubule binding possibly involved in neuronal degeneration, and Thr231, Ser235, Ser262, and Ser404 are four of the most well documented sites abnormally phosphorylated in Alzheimer-tau, the results provide initial evidence that protein kinase FA/GSK-3 alpha after heparin potentiation may represent one of the most potent systems possibly involved in the abnormal phosphorylation of PHF-tau in Alzheimer"s disease brains.	Heparin	434-441	microtubule associated protein tau	Homo sapiens	553-560
7878636-1	1994	beta 2 glycoprotein-I (beta 2GPI), a cofactor for antiphospholipid antibody (aPA) binding, binds to many anionic macromolecules including heparin.	Heparin	138-145	apolipoprotein H	Homo sapiens	0-21
7878636-1	1994	beta 2 glycoprotein-I (beta 2GPI), a cofactor for antiphospholipid antibody (aPA) binding, binds to many anionic macromolecules including heparin.	Heparin	138-145	apolipoprotein H	Homo sapiens	23-32
7878636-3	1994	We have examined the interactions of dermatan sulphate (DS) and different pharmaceutical preparations of heparin with beta 2GPI by crossed immunoelectrophoresis (CIE) and investigated the effect of these agents on plasma levels of beta 2GPI antigen (beta 2GPI:Ag) by a standardised enzyme linked immunosorbent assay (ELISA).	Heparin	105-112	apolipoprotein H	Homo sapiens	118-127
7878636-5	1994	CIE results confirmed a heparin-beta 2GPI interaction with unfractionated (UF) heparin.	Heparin	24-31	apolipoprotein H	Homo sapiens	32-41
7944706-1	1994	The anticoagulant effect of heparin in the milieu of altered antithrombin III levels was investigated in adult (n = 7) and pediatric (n = 14) patients undergoing open heart operations.	Heparin	28-35	serpin family C member 1	Homo sapiens	61-77
7944706-7	1994	This result may be related to the different actions of heparin when antithrombin III levels are reduced.	Heparin	55-62	serpin family C member 1	Homo sapiens	68-84
7522446-5	1994	Heparin and N-desulfated heparin efficiently inhibited the binding of 125I-VEGF165 to alpha 2-macroglobulin, but surprisingly, O-desulfated heparin was an ineffective inhibitor.	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	86-107
30660948-1	2019	INTRODUCTION: Heparins exert their anticoagulant effect through activation of antithrombin.	Heparin	14-22	serpin family C member 1	Homo sapiens	78-90
7522446-5	1994	Heparin and N-desulfated heparin efficiently inhibited the binding of 125I-VEGF165 to alpha 2-macroglobulin, but surprisingly, O-desulfated heparin was an ineffective inhibitor.	Heparin	25-32	alpha-2-macroglobulin	Homo sapiens	86-107
7806969-2	1994	Previous studies have localized the catalytic domain of LPL, responsible for the hydrolytic function of the enzyme, to the N-terminus whereas the C-terminal end may play a role in lipid and heparin binding.	Heparin	190-197	lipoprotein lipase	Homo sapiens	56-59
7806969-4	1994	In this manuscript we describe the defect in the LPL gene of a patient with triglycerides ranging from normal to 12,000 mg/dl, low LPL mass, and no LPL activity in post-heparin plasma.	Heparin	169-176	lipoprotein lipase	Homo sapiens	49-52
30660948-2	2019	Whether antithrombin deficiency leads to clinically relevantly reduced anti-Xa activity of heparins is unknown.	Heparin	91-99	serpin family C member 1	Homo sapiens	8-20
30660948-9	2019	Antithrombin activity correlated with anti-Xa activity of UFH (R = 0.77) and LMWH (R = 0.66).	Heparin	58-61	serpin family C member 1	Homo sapiens	0-12
8049432-0	1994	Low-affinity heparin stimulates the inactivation of plasminogen activator inhibitor-1 by thrombin.	Heparin	13-20	serpin family E member 1	Homo sapiens	52-85
8049432-1	1994	The influence of heparin on the reaction between thrombin and plasminogen activator inhibitor-1 (PAI-1) has been examined.	Heparin	17-24	serpin family E member 1	Homo sapiens	62-95
30660948-12	2019	Standard LWMH- or UFH-doses are likely to lead to under treatment in antithrombin-deficient individuals.	Heparin	18-21	serpin family C member 1	Homo sapiens	69-81
8049432-1	1994	The influence of heparin on the reaction between thrombin and plasminogen activator inhibitor-1 (PAI-1) has been examined.	Heparin	17-24	serpin family E member 1	Homo sapiens	97-102
7848824-6	1994	Odontoblast-like cells obtained in the presence of IGF-1 combined with heparin did not express TGF beta 1 transcripts and expressed weakly TGF beta 3 transcripts.	Heparin	71-78	transforming growth factor, beta 3	Mus musculus	139-149
8049432-2	1994	With a 50-fold excess of PAI-1, the rate constant for the inhibition of thrombin was 458 mol/L-1s-1, which increased to 5,000 mol/L-1s-1 in the presence of 25 micrograms/mL unfractionated heparin or heparin with low affinity for antithrombin.	Heparin	188-195	serpin family E member 1	Homo sapiens	25-30
30168023-6	2019	TSP-2/FGF2 binding was inhibited by calcium and heparin.	Heparin	48-55	thrombospondin 2	Homo sapiens	0-5
8049432-2	1994	With a 50-fold excess of PAI-1, the rate constant for the inhibition of thrombin was 458 mol/L-1s-1, which increased to 5,000 mol/L-1s-1 in the presence of 25 micrograms/mL unfractionated heparin or heparin with low affinity for antithrombin.	Heparin	199-206	serpin family E member 1	Homo sapiens	25-30
8049432-4	1994	Thrombin and PAI-1 formed a stable stoichiometric complex in the absence of heparin, which did not dissociate after the addition of 25 micrograms/mL low-affinity heparin.	Heparin	76-83	serpin family E member 1	Homo sapiens	13-18
8049432-4	1994	Thrombin and PAI-1 formed a stable stoichiometric complex in the absence of heparin, which did not dissociate after the addition of 25 micrograms/mL low-affinity heparin.	Heparin	162-169	serpin family E member 1	Homo sapiens	13-18
8049432-5	1994	In contrast, when low-affinity heparin was added at the beginning of the reaction, there was an initial increase in PAI-1-thrombin complex formation, but this was rapidly followed by substantial proteolytic cleavage of unreacted PAI-1 and of the thrombin-PAI-1 complex.	Heparin	31-38	serpin family E member 1	Homo sapiens	116-121
7528019-1	1994	Interactions between the IGF-binding proteins (IGFBPs) and glycosaminoglycans (GAGs) such as heparin may be involved in the regulatory control of IGF exerted by the IGFBPs at the level of the extracellular matrix and capillary endothelium, although the precise mechanisms of this remain uncertain.	Heparin	93-100	insulin like growth factor binding protein 1	Homo sapiens	47-53
7528019-1	1994	Interactions between the IGF-binding proteins (IGFBPs) and glycosaminoglycans (GAGs) such as heparin may be involved in the regulatory control of IGF exerted by the IGFBPs at the level of the extracellular matrix and capillary endothelium, although the precise mechanisms of this remain uncertain.	Heparin	93-100	insulin like growth factor binding protein 1	Homo sapiens	165-171
7528019-5	1994	Affinity of the IGFBP preparations for heparin was examined experimentally by affinity chromatography using pooled fractions of fetal and adult ovine plasma obtained by size exclusion chromatography.	Heparin	39-46	insulin like growth factor binding protein 1	Homo sapiens	16-21
8034581-4	1994	Nuclear granzyme B had an apparent molecular mass of approximately 32 kDa in human cells and approximately 30 kDa in RNK-16 and was eluted from immobilized heparin at the same NaCl concentration as granzyme B from cytoplasmic granules.	Heparin	156-163	granzyme B	Homo sapiens	8-18
8025278-1	1994	The ability of heparin to dramatically enhance the inactivation of thrombin (IIa) by antithrombin III (ATIII) in buffer is negated through formation of a IIa-fibrin-heparin ternary complex (Hogg and Jackson, Proc Natl Acad Sci USA 86:3619, 1989; Hogg and Jackson, J Biol Chem 265:241, 1990).	Heparin	15-22	serpin family C member 1	Homo sapiens	85-101
8025278-1	1994	The ability of heparin to dramatically enhance the inactivation of thrombin (IIa) by antithrombin III (ATIII) in buffer is negated through formation of a IIa-fibrin-heparin ternary complex (Hogg and Jackson, Proc Natl Acad Sci USA 86:3619, 1989; Hogg and Jackson, J Biol Chem 265:241, 1990).	Heparin	15-22	serpin family C member 1	Homo sapiens	103-108
8025278-7	1994	Fibrin was found to inhibit the heparin-catalyzed inactivation of IIa by ATIII with half-maximal effect at 97 +/- 19 nmol/L fibrin.	Heparin	32-39	serpin family C member 1	Homo sapiens	73-78
8025278-9	1994	These findings imply that fibrin is a potent modulator of heparin activity in vivo by inhibiting heparin-catalyzed IIa-ATIII complex formation through formation of ternary IIa-fibrin-heparin complexes.	Heparin	58-65	serpin family C member 1	Homo sapiens	119-124
7516869-6	1994	Soluble heparin, at a half-maximal concentration of approximately 5 microgram/ml, inhibited the decrease in IGFBP-3 in the medium.	Heparin	8-15	insulin-like growth factor binding protein 3	Rattus norvegicus	108-115
7516869-7	1994	In addition, soluble heparin decreased the amount of IGFBP-3 detectable on the cell surface, as determined by performing ligand blots on plasma membrane preparations.	Heparin	21-28	insulin-like growth factor binding protein 3	Rattus norvegicus	53-60
7965660-4	1994	Substituents introduced at this position had a minimal effect on the antithrombin III binding sites found in heparin"s interior.	Heparin	109-116	serpin family C member 1	Homo sapiens	69-85
7974394-1	1994	Congenital deficiency of antithrombin (AT) is associated with thrombotic events and AT consumption occurs in some severe disorders and after treatment with heparin.	Heparin	156-163	serpin family C member 1	Homo sapiens	25-37
30168023-11	2019	Binding of TSP-2 to FGF2 impaired the growth factor ability to interact with its cellular receptors, since TSP-2-derived fragments prevented the binding of FGF2 to both heparin (used as a structural analog of heparan sulfate proteoglycans) and FGFR-1.	Heparin	169-176	thrombospondin 2	Homo sapiens	11-16
7987496-2	1994	Heparin immobilized in this way proved to be useful as an affinity carrier for the isolation of antithrombin III and heparin-binding proteins from boar seminal plasma.	Heparin	0-7	serpin family C member 1	Homo sapiens	96-112
8086857-3	1994	Osteogenin was extracted from bovine bone with 6 M urea and purified by chromatography on hydroxyapatite, heparin-Sepharose and Sephacryl S-200 gel filtration.	Heparin	106-113	bone morphogenetic protein 3	Bos taurus	0-10
30168023-11	2019	Binding of TSP-2 to FGF2 impaired the growth factor ability to interact with its cellular receptors, since TSP-2-derived fragments prevented the binding of FGF2 to both heparin (used as a structural analog of heparan sulfate proteoglycans) and FGFR-1.	Heparin	169-176	thrombospondin 2	Homo sapiens	107-112
30535446-0	2019	The AIB1siRNA-loaded hyaluronic acid-assembled PEI/heparin/Ca2+ nanocomplex as a novel therapeutic strategy in lung cancer treatment.	Heparin	51-58	nuclear receptor coactivator 3	Homo sapiens	4-8
7515052-3	1994	125I-RAP binding to the low affinity site was abolished by heparin or Suramin.	Heparin	59-66	LDL receptor related protein associated protein 1	Homo sapiens	5-8
8206972-6	1994	Heparin, which displaces LPL from binding sites on cell surface proteoglycans, increased [3H]retinoid uptake by an additional 2-fold.	Heparin	0-7	lipoprotein lipase	Oryctolagus cuniculus	25-28
7911328-5	1994	Our studies reveal that for chemically modified heparins and heparin-derived fragments there is a striking correlation between anti-HIV-1 activity in vitro and binding to the V3 loop of gp120 in solid phase ELISA.	Heparin	48-56	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	186-191
7911328-5	1994	Our studies reveal that for chemically modified heparins and heparin-derived fragments there is a striking correlation between anti-HIV-1 activity in vitro and binding to the V3 loop of gp120 in solid phase ELISA.	Heparin	48-55	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	186-191
7911328-6	1994	This strongly suggests that the heparin exerts its anti-HIV-1 activity by binding to the V3 loop of gp120.	Heparin	32-39	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	100-105
8172858-8	1994	PAI-1 stimulatory activity in SMC CM was completely abolished by boiling or incubation with protamine sulfate and was reduced by transient acidification or heparin-Sepharose pretreatment by 33% or 48%, respectively.	Heparin	156-163	serpin family E member 1	Homo sapiens	0-5
30535446-1	2019	In the present study, AIB1siRNA-loaded polyethyleneimine (PEI)/heparin/Ca2+ nanoparticles (NPs) were successfully prepared and evaluated for their efficacy in lung cancer cells.	Heparin	63-70	nuclear receptor coactivator 3	Homo sapiens	22-26
8202520-5	1994	Heparin affinity was assessed by NaCl gradient elution from heparin-agarose, and second-order rate constants for inhibition by antithrombin III were determined in the absence and presence of heparin.	Heparin	191-198	serpin family C member 1	Homo sapiens	127-143
30535446-9	2019	Together, these results indicated that HA-PEI/heparin/Ca2+ NPs may be a promising carrier for the anticancer activity of AIB1siRNA in lung cancer cells.	Heparin	46-53	nuclear receptor coactivator 3	Homo sapiens	121-125
8202520-8	1994	However, affinity for heparin-agarose correlated directly with the rate of inhibition by antithrombin III with heparin.	Heparin	22-29	serpin family C member 1	Homo sapiens	89-105
8202520-8	1994	However, affinity for heparin-agarose correlated directly with the rate of inhibition by antithrombin III with heparin.	Heparin	111-118	serpin family C member 1	Homo sapiens	89-105
8068301-0	1994	Calcium-enhanced aggregation of serum amyloid P component and its inhibition by the ligands heparin and heparan sulphate.	Heparin	92-99	amyloid P component, serum	Homo sapiens	32-57
8157673-3	1994	Abundant hLPL transcripts were detected in RNA from different tissues of transgenic mice which resulted in an increase in post-heparin plasma LPL activity of approximately 154%.	Heparin	127-134	lipoprotein lipase	Homo sapiens	9-13
8155721-1	1994	The role of processing of the oligosaccharide chains in the affinity of lipoprotein lipase (LPL) for heparin was examined in 3T3-L1 adipocytes.	Heparin	101-108	lipoprotein lipase	Homo sapiens	72-90
8155721-1	1994	The role of processing of the oligosaccharide chains in the affinity of lipoprotein lipase (LPL) for heparin was examined in 3T3-L1 adipocytes.	Heparin	101-108	lipoprotein lipase	Homo sapiens	92-95
8155721-5	1994	Thus, core glycosylation and subsequent removal of the distal glucose residue from oligosaccharide chains of LPL in the endoplasmic reticulum (ER) is required for acquisition of a higher affinity for heparin.	Heparin	200-207	lipoprotein lipase	Homo sapiens	109-112
29910226-11	2019	The levels of the plasma post-heparin LPL and HL activities in the proband (57 and 177 mU/mL) were reduced to 24% and 75%, respectively, compared with those assayed in the control subject with normal plasma triglycerides.	Heparin	30-37	lipoprotein lipase	Homo sapiens	38-41
8138582-6	1994	However, beta-xyloside treatment which reduces the abundance of membrane-associated CS-PG, as evidenced by molecular sieve chromatography, produced a major and specific decrease in HPC adhesion to the heparin-promoting binding fragment of fibronectin.	Heparin	201-208	fibronectin 1	Mus musculus	239-250
8138588-3	1994	This IP3-induced internal Ca2+ release can be inhibited by heparin (an IP3 receptor antagonist).	Heparin	59-66	inositol 1,4,5-trisphosphate receptor type 3	Bos taurus	71-83
8068301-13	1994	Binding of the ligands heparin and heparan sulphate to SAP completely abolished the calcium-enhanced aggregation, but the distribution of the SAP molecules was affected, resulting in strands or groups of adjacent molecules.	Heparin	23-30	amyloid P component, serum	Homo sapiens	55-58
8068301-17	1994	SAP"s tendency to self-aggregation is abolished after its binding to heparin or heparin sulphate.	Heparin	69-76	amyloid P component, serum	Homo sapiens	0-3
8205697-7	1994	Our major finding was that coronary artery reocclusion occurred in 72 +/- 11 minutes after treatment with TPA (80 micrograms/kg + 8 micrograms.kg-1.min-1) and heparin (200 U/kg) (n = 7); in 142 +/- 24 minutes after TPA, heparin, and VCL (4 mg/kg + 2 mg.kg-1.h-1) (n = 7) (compared with TPA and heparin, P &lt; .05); in 74 +/- 13 minutes after TPA, heparin, and aspirin (5 mg/kg) (n = 8); and in 173 +/- 8 minutes after TPA, heparin, VCL, and aspirin (n = 8) (compared with TPA and heparin, P &lt; .001).	Heparin	159-166	vinculin	Canis lupus familiaris	233-236
8205697-7	1994	Our major finding was that coronary artery reocclusion occurred in 72 +/- 11 minutes after treatment with TPA (80 micrograms/kg + 8 micrograms.kg-1.min-1) and heparin (200 U/kg) (n = 7); in 142 +/- 24 minutes after TPA, heparin, and VCL (4 mg/kg + 2 mg.kg-1.h-1) (n = 7) (compared with TPA and heparin, P &lt; .05); in 74 +/- 13 minutes after TPA, heparin, and aspirin (5 mg/kg) (n = 8); and in 173 +/- 8 minutes after TPA, heparin, VCL, and aspirin (n = 8) (compared with TPA and heparin, P &lt; .001).	Heparin	159-166	vinculin	Canis lupus familiaris	433-436
7910971-2	1994	A dose-dependent t-PA release from the isolated perfused vascular preparations may be induced by mediators (platelet-activating factor, bradykinin, histamine) adrenergic and cholinergic transmitters (isoprenaline, acetylcholine), thrombin, heparin and analogues, and 1-desamino-8-D-arginine-vasopression (DDAVP).	Heparin	240-247	plasminogen activator, tissue type	Rattus norvegicus	17-21
7910971-5	1994	Presently, this could only be achieved by unfractionated and low molecular weight heparins which have been shown to release t-PA.	Heparin	82-90	plasminogen activator, tissue type	Rattus norvegicus	124-128
8167338-0	1994	Autoantibodies to heparin from patients with antiphospholipid antibody syndrome inhibit formation of antithrombin III-thrombin complexes.	Heparin	18-25	serpin family C member 1	Homo sapiens	101-117
30072263-1	2019	OBJECTIVES: To determine whether precardiopulmonary bypass (CPB) normalization of antithrombin levels in infants to 100% improves heparin sensitivity and anticoagulation during CPB and has beneficial effects into the postoperative period.	Heparin	130-137	serpin family C member 1	Homo sapiens	82-94
8167338-7	1994	Furthermore, APS IgG antiheparin antibodies inhibited heparin-accelerated formation of antithrombin III-thrombin complexes.	Heparin	25-32	serpin family C member 1	Homo sapiens	87-103
8091393-6	1994	Heparin and sera from patients with HAT stimulated GT platelets in the same manner as determined by 14C-serotonin release and the changes in phosphorylation of p20 and p47.	Heparin	0-7	pleckstrin	Homo sapiens	168-171
8087553-1	1994	BACKGROUND: Antithrombin, a member of the serpin family of inhibitors, controls coagulation in human plasma by forming complexes with thrombin and other coagulation proteases in a process greatly accelerated by heparin.	Heparin	211-218	serpin family C member 1	Homo sapiens	12-24
8087553-3	1994	We have determined the structure of intact antithrombin in order to study its mechanism of activation, particularly with respect to heparin, and the dysfunctions of this mechanism that predispose individuals to thrombotic disease.	Heparin	132-139	serpin family C member 1	Homo sapiens	43-55
8052962-2	1994	In the present work, we investigated the effects of decreased plasma antithrombin III (ATIII) levels on anticoagulant effects of rhs-TM, as compared to findings with heparin, of which effect is lowered by the decreased plasma ATIII levels in patients with DIC.	Heparin	166-173	serpin family C member 1	Homo sapiens	226-231
8133054-11	1994	Heparin, which is known to inhibit the interaction between SAP and C4BP, was also found to counteract the inhibitory effect of SAP on C4BP binding to C4(H2O).	Heparin	0-7	amyloid P component, serum	Homo sapiens	59-62
8133054-11	1994	Heparin, which is known to inhibit the interaction between SAP and C4BP, was also found to counteract the inhibitory effect of SAP on C4BP binding to C4(H2O).	Heparin	0-7	amyloid P component, serum	Homo sapiens	127-130
8016817-6	1994	The addition of AT-III to the system did not influence the action of DuP 714 or rH, but it strongly increased the inhibitory effects of unfractionated heparin (PMH) as well as of a low molecular weight heparin (LMWH) on both thrombin and factor Xa generation.	Heparin	151-158	serpin family C member 1	Homo sapiens	16-22
8016817-6	1994	The addition of AT-III to the system did not influence the action of DuP 714 or rH, but it strongly increased the inhibitory effects of unfractionated heparin (PMH) as well as of a low molecular weight heparin (LMWH) on both thrombin and factor Xa generation.	Heparin	202-209	serpin family C member 1	Homo sapiens	16-22
8029789-0	1994	Thrombin-based antithrombin assays show overestimation of antithrombin III activity in patients on heparin therapy due to heparin cofactor II influence.	Heparin	99-106	serpin family C member 1	Homo sapiens	15-27
8029789-0	1994	Thrombin-based antithrombin assays show overestimation of antithrombin III activity in patients on heparin therapy due to heparin cofactor II influence.	Heparin	99-106	serpin family C member 1	Homo sapiens	58-74
8029789-6	1994	The results thus suggest that the Factor Xa-based antithrombin III activity method provides more valid results in patients on heparin therapy.	Heparin	126-133	serpin family C member 1	Homo sapiens	50-66
7509746-8	1994	Less than 10% of the initial PSA activity remained after 3 h incubation with a sevenfold molar excess of PCI and in the presence of heparin.	Heparin	132-139	kallikrein related peptidase 3	Homo sapiens	29-32
8307953-2	1994	The purified extracellular domain of FGFR-1 formed complexes with 125I-bFGF both in the presence or absence of heparin.	Heparin	111-118	fibroblast growth factor receptor 1	Cricetulus griseus	37-43
8307953-7	1994	When FGFR-1 or FGFR-2 were expressed in mutant CHO cells deficient in heparan sulfate synthesis, the cells also bound 125I-bFGF in the absence of heparin, and the addition of heparin increased the affinity of bFGF for its receptors 2-3-fold.	Heparin	175-182	fibroblast growth factor receptor 1	Cricetulus griseus	5-11
8307953-10	1994	Expression of c-fos mRNA was induced by bFGF in 32D cells expressing FGFR-1 to the same extent in the presence or absence of heparin.	Heparin	125-132	FBJ osteosarcoma oncogene	Mus musculus	14-19
8087553-9	1994	The conformation of the two forms of antithrombin demonstrates the extraordinary mobility of the reactive loop in the serpins and provides insights into the folding of the loop required for inhibitory activity together with the potential modification of this by heparin.	Heparin	262-269	serpin family C member 1	Homo sapiens	37-49
7511146-3	1994	Our previous work indicated that 1) TGF-beta 1 has strong heparin-binding properties that were not previously recognized because of neutralization by iodination, and 2) heparin, and certain other polyanions, could block the binding of TGF-beta 1 to alpha 2-macroglobulin (alpha 2-M).	Heparin	169-176	alpha-2-macroglobulin	Homo sapiens	249-270
7511146-3	1994	Our previous work indicated that 1) TGF-beta 1 has strong heparin-binding properties that were not previously recognized because of neutralization by iodination, and 2) heparin, and certain other polyanions, could block the binding of TGF-beta 1 to alpha 2-macroglobulin (alpha 2-M).	Heparin	169-176	alpha-2-macroglobulin	Homo sapiens	272-281
7511146-5	1994	The results indicate that heparin and fucoidan, a naturally occurring sulfated L-fucose polymer, suppress the formation of an initial non-covalent interaction between 125I-TGF-beta 1 and activated alpha 2-M.	Heparin	26-33	alpha-2-macroglobulin	Homo sapiens	197-206
8205009-3	1994	Two functional domains in antithrombin are recognised, the reactive site domain which interacts with the active site serine residue of the protease and the heparin binding domain.	Heparin	156-163	serpin family C member 1	Homo sapiens	26-38
8043225-7	1994	Pre-incubation of gp120 with excess sCD4 increases the potency of heparin in blocking the binding of V3 loop monoclonals severalfold.	Heparin	66-73	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	18-23
8305414-7	1994	Furthermore, we found that binding at 4 degrees C of VLDL and LDL to CHO-LPL was greater than to CHO-anti-LPL, and this binding difference was abolished by washing the cells with heparin.	Heparin	179-186	lipoprotein lipase	Homo sapiens	73-76
8305417-6	1994	The inhibitory activity of antithrombin III was enhanced in the presence of heparin, which on its own had no inhibitory effect on thrombin-induced DNA synthesis.	Heparin	76-83	serpin family C member 1	Homo sapiens	27-43
8308035-4	1994	These models allow us to propose a few hypotheses on the structural determinants of lipoprotein lipase which are responsible for heparin binding, dimer formation, and phospholipase activity.	Heparin	129-136	lipoprotein lipase	Homo sapiens	84-102
8305417-8	1994	This inhibition was dependent on the presence of antithrombin III in serum, since heparin lacked effect if antithrombin III was depleted from serum by immunoaffinity chromatography.	Heparin	82-89	serpin family C member 1	Homo sapiens	49-65
30072263-7	2019	Higher first post-heparin activated clotting times (sec) were observed in the antithrombin group despite similar initial heparin dosing.	Heparin	18-25	serpin family C member 1	Homo sapiens	78-90
8043225-1	1994	OBJECTIVE: To investigate the binding of the sulphated polysaccharides, dextran sulphate and heparin, to CD4 and gp120 in order to examine the anti-HIV mechanisms of these compounds.	Heparin	93-100	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	113-118
8288594-0	1994	Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III.	Heparin	70-77	serpin family C member 1	Homo sapiens	104-120
30072263-8	2019	There was an increase in heparin sensitivity in the antithrombin group.	Heparin	25-32	serpin family C member 1	Homo sapiens	52-64
8288594-1	1994	The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin.	Heparin	44-51	serpin family C member 1	Homo sapiens	90-106
8288594-1	1994	The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin.	Heparin	44-51	serpin family C member 1	Homo sapiens	90-102
8169523-6	1994	Mouse apoJ contains six potential N-glycosylation sites, a potential Arg-Ser cleavage site to generate alpha and beta subunits, a cluster of five cysteine residues in each subunit, three putative amphipathic helices, and four potential heparin-binding domains.	Heparin	236-243	clusterin	Mus musculus	6-10
30798810-3	2019	Heparin was found to inhibit hepcidin expression and BMP6 activity in hepatic cell lines and in mice, suggesting that endogenous heparan sulfates are involved in the pathway of hepcidin expression.	Heparin	0-7	bone morphogenetic protein 6	Mus musculus	53-57
7524276-3	1994	Heparin reduces the exposure of the media to platelet derived growth factor, a mitogen from aggregating platelets responsible for the migration and proliferation of the myofibroblasts.	Heparin	0-7	myotrophin	Rattus norvegicus	62-75
8288594-1	1994	The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin.	Heparin	44-51	serpin family C member 1	Homo sapiens	165-177
8288594-2	1994	Point mutations at Arg-180, Arg-245, Lys-248, and Lys-252 in thrombin markedly reduced the efficiency of heparin catalysis by decreasing the stability of the ternary intermediate, whereas the inactivation of thrombin by antithrombin alone was not affected by these mutations.	Heparin	105-112	serpin family C member 1	Homo sapiens	220-232
8280781-1	1994	Small amounts of a variant antithrombin (AT) bearing an Arg-129 to Gln mutation were purified from plasma by means of affinity chromatography on insolubilized heparin at very low ionic strength.	Heparin	159-166	serpin family C member 1	Homo sapiens	27-39
8186357-2	1994	In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans.	Heparin	91-98	serpin family C member 1	Homo sapiens	40-52
30442128-10	2018	Both in vivo and in vitro studies showed that UFH pretreatment blocked the LPS-induced increase in guanine nucleotide exchange factor (GEF-H1) expression and myosin phosphatase target subunit 1 (MYPT1) phosphorylation, and microtubule (MT) disassembly in LPS-induced ALI mouse model and human pulmonary microvascular endothelial cells (HPMECs).	Heparin	46-49	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	135-141
7959639-4	1994	These cells also release an HB-EGF-like activity that (i) stimulates smooth muscle cell and BALB/c 3T3 cell but not endothelial cell proliferation; (ii) binds to TSK heparin affinity columns and is eluted with 0.9-1.2 M NaCl, and (iii) triggers phosphorylation of a protein with the same molecular weight as the 170-kD EGF receptor.	Heparin	166-173	heparin binding EGF like growth factor	Homo sapiens	28-34
7959639-4	1994	These cells also release an HB-EGF-like activity that (i) stimulates smooth muscle cell and BALB/c 3T3 cell but not endothelial cell proliferation; (ii) binds to TSK heparin affinity columns and is eluted with 0.9-1.2 M NaCl, and (iii) triggers phosphorylation of a protein with the same molecular weight as the 170-kD EGF receptor.	Heparin	166-173	tsukushi, small leucine rich proteoglycan	Mus musculus	162-165
7947469-0	1994	Heparin surface immobilization through hydrophilic spacers: thrombin and antithrombin III binding kinetics.	Heparin	0-7	serpin family C member 1	Homo sapiens	73-89
7947469-2	1994	In this study, the effect of hydrophilic spacers (PEO) on the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin was investigated.	Heparin	94-101	serpin family C member 1	Homo sapiens	107-123
7947469-2	1994	In this study, the effect of hydrophilic spacers (PEO) on the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin was investigated.	Heparin	94-101	serpin family C member 1	Homo sapiens	125-130
7947469-3	1994	Monodispersed, low molecular weight heparin was fractionated on an ATIII affinity column to isolate high-ATIII affinity heparin.	Heparin	36-43	serpin family C member 1	Homo sapiens	67-72
7947469-3	1994	Monodispersed, low molecular weight heparin was fractionated on an ATIII affinity column to isolate high-ATIII affinity heparin.	Heparin	120-127	serpin family C member 1	Homo sapiens	105-110
7947469-9	1994	Soluble heparin bound both thrombin and ATIII, while heparin immobilized directly onto the surface bound only thrombin.	Heparin	8-15	serpin family C member 1	Homo sapiens	40-45
7947469-10	1994	Spacer-immobilized heparin bound both ATIII and thrombin, although to a lesser extent than soluble heparin.	Heparin	19-26	serpin family C member 1	Homo sapiens	38-43
7947469-11	1994	Thus, the enhanced bioactivity of spacer-immobilized heparin, compared to direct-immobilization, may be attributed to the retention of ATIII binding.	Heparin	53-60	serpin family C member 1	Homo sapiens	135-140
7819594-4	1994	As a result, our understanding of structural domains involved in catalysis, heparin, lipid binding, and enzyme-cofactor interaction as well as the mechanism of action of LPL as an acylglycerol hydrolase has been greatly enhanced.	Heparin	76-83	lipoprotein lipase	Homo sapiens	170-173
22823116-1	1994	A retrospective analysis of the results of cataract surgery using heparin surface modified intraocular lenses (HSM-IOL) performed on patients with uveitis between August 1989 and July 1993 was undertaken.	Heparin	66-73	leucine rich repeat containing 4B	Homo sapiens	111-114
7824964-0	1994	Detection of the low molecular weight heparin component of ITF 1300 in urines after intranasal administration to dogs.	Heparin	38-45	trefoil factor 3	Canis lupus familiaris	59-62
7535497-5	1994	ITI was purified from the prothrombin complex concentrate (PCC) by diethylaminoethyl-Sepharose fast-flow chromatography followed by a chromatographic step on immobilized heparin designed to remove C4, factor X and protein C.	Heparin	170-177	complement C4A (Rodgers blood group)	Homo sapiens	197-223
8182587-3	1994	Purified proacrosin was allowed to autoactivate at pH 8.0 in the presence of different concentrations of homologous zona glycoproteins, sulfated polymers (fucoidan, chondroitin sulfates A, B and C, dextran sulfate, polyvinylsulfate and heparin) and non-sulfated polymers (dextran, polyvinylphosphate and hyaluronic acid).	Heparin	236-243	acrosin	Homo sapiens	9-19
30442128-10	2018	Both in vivo and in vitro studies showed that UFH pretreatment blocked the LPS-induced increase in guanine nucleotide exchange factor (GEF-H1) expression and myosin phosphatase target subunit 1 (MYPT1) phosphorylation, and microtubule (MT) disassembly in LPS-induced ALI mouse model and human pulmonary microvascular endothelial cells (HPMECs).	Heparin	46-49	protein phosphatase 1, regulatory subunit 12A	Mus musculus	158-193
7801599-1	1994	We describe an improved method for large-scale purification of antithrombin III (AT-III) from human plasma involving heparin affinity chromatography of redissolved fraction IV-1 paste, viral inactivation by heating, followed by a second heparin affinity column.	Heparin	117-124	serpin family C member 1	Homo sapiens	63-79
7801599-1	1994	We describe an improved method for large-scale purification of antithrombin III (AT-III) from human plasma involving heparin affinity chromatography of redissolved fraction IV-1 paste, viral inactivation by heating, followed by a second heparin affinity column.	Heparin	117-124	serpin family C member 1	Homo sapiens	81-87
30442128-10	2018	Both in vivo and in vitro studies showed that UFH pretreatment blocked the LPS-induced increase in guanine nucleotide exchange factor (GEF-H1) expression and myosin phosphatase target subunit 1 (MYPT1) phosphorylation, and microtubule (MT) disassembly in LPS-induced ALI mouse model and human pulmonary microvascular endothelial cells (HPMECs).	Heparin	46-49	protein phosphatase 1, regulatory subunit 12A	Mus musculus	195-200
7863705-8	1994	An anticoagulation with heparin seems to improve the efficacy of the more fibrin-specific thrombolytics t-PA, r-PA, and pro-urokinase.	Heparin	24-31	replication protein A1	Homo sapiens	110-114
30389911-6	2018	The inhibitory effects of syndecan ectodomains, heparan sulfate, and N-desulfated heparin derivatives on osteoclast differentiation were attributed to their direct binding to the macrophage-colony stimulating factor (M-CSF), resulting in the blocking of M-CSF-mediated downstream signals such as extracellular signal-regulated kinase (ERK), c-JUN N-terminal kinase (JNK), p38, and Akt.	Heparin	82-89	colony stimulating factor 1	Homo sapiens	179-215
8165617-2	1993	In molar terms, antithrombin III was the most abundant protein bound to therapeutic doses of unfractionated heparin (M(r) = 12,000), whereas heparin cofactor II constituted &lt; 1% of the protein bound.	Heparin	108-115	serpin family C member 1	Homo sapiens	16-32
8165617-5	1993	Binding of both antithrombin III and histidine-rich glycoprotein varied with the ratio of heparin to plasma.	Heparin	90-97	serpin family C member 1	Homo sapiens	16-32
8262929-10	1993	The enhancing effect of heparin on the inhibitory process is concentration dependent and exhibits an optimum, reminiscent of the "template" model for heparin"s acceleration of thrombin and factor IXa inhibition by antithrombin III.	Heparin	24-31	serpin family C member 1	Homo sapiens	214-230
30389911-6	2018	The inhibitory effects of syndecan ectodomains, heparan sulfate, and N-desulfated heparin derivatives on osteoclast differentiation were attributed to their direct binding to the macrophage-colony stimulating factor (M-CSF), resulting in the blocking of M-CSF-mediated downstream signals such as extracellular signal-regulated kinase (ERK), c-JUN N-terminal kinase (JNK), p38, and Akt.	Heparin	82-89	colony stimulating factor 1	Homo sapiens	217-222
8262139-5	1993	Growth factor activity in a C6 cell lysate was characterized by heparin affinity chromatography and Western blot analysis using an anti-bFGF antibody.	Heparin	64-71	myotrophin	Rattus norvegicus	0-13
30149230-6	2018	Disruption of the interaction between the Dystrophin-Associated-Protein-Complex (DAPC) and laminin by heparin or anti-alpha-dystroglycan antibody IIH6 disenables myotubes to align perpendicular to nanogrooves, suggesting that this phenotype is controlled by the DAPC-mediated cytoskeleton-extracellular matrix linkage.	Heparin	102-109	dystrophin	Homo sapiens	42-52
8128425-3	1993	As an alternative we define a unit of heparin in terms of anti-factor Xa- and antithrombin-activity that is independent of the heparin standard and of the assay method, but that is based upon a quantitative description of the catalytic effect of heparin on AT III mediated thrombin- and factor Xa breakdown.	Heparin	38-45	serpin family C member 1	Homo sapiens	78-90
8128425-3	1993	As an alternative we define a unit of heparin in terms of anti-factor Xa- and antithrombin-activity that is independent of the heparin standard and of the assay method, but that is based upon a quantitative description of the catalytic effect of heparin on AT III mediated thrombin- and factor Xa breakdown.	Heparin	38-45	serpin family C member 1	Homo sapiens	257-263
8128425-4	1993	Expression of the results of existing anti-factor Xa- and antithrombin tests in terms of these units will allow to express heparin levels in plasma in terms of concentrations of active anticoagulant material.	Heparin	123-130	serpin family C member 1	Homo sapiens	58-70
8115989-1	1993	The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis.	Heparin	48-55	serpin family C member 1	Homo sapiens	90-106
8115989-1	1993	The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis.	Heparin	48-55	serpin family C member 1	Homo sapiens	90-102
8172566-5	1993	At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.).	Heparin	396-403	complement C1q A chain	Homo sapiens	29-32
8172566-5	1993	At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.).	Heparin	396-403	complement C1q A chain	Homo sapiens	94-97
8172566-5	1993	At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.).	Heparin	396-403	complement C1q A chain	Homo sapiens	94-97
8172566-5	1993	At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.).	Heparin	396-403	complement C1q A chain	Homo sapiens	94-97
8137606-3	1993	All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin.	Heparin	8-15	serpin family C member 1	Homo sapiens	29-45
7692967-0	1993	High molecular weight kininogen potentiates the heparin-accelerated inhibition of plasma kallikrein by antithrombin: role for antithrombin in the regulation of kallikrein.	Heparin	48-55	serpin family C member 1	Homo sapiens	103-115
7692967-2	1993	H-kininogen, at levels sufficient to fully complex kallikrein, greatly potentiated the acceleration of antithrombin inhibition of kallikrein produced by heparin with high affinity for antithrombin.	Heparin	153-160	serpin family C member 1	Homo sapiens	103-115
7692967-2	1993	H-kininogen, at levels sufficient to fully complex kallikrein, greatly potentiated the acceleration of antithrombin inhibition of kallikrein produced by heparin with high affinity for antithrombin.	Heparin	153-160	serpin family C member 1	Homo sapiens	184-196
8409405-1	1993	Macrophage inflammatory protein-1 alpha (MIP-1 alpha) is a member of the intercrine/chemokine family which consists of basic, heparin-binding, small molecular weight proteins.	Heparin	126-133	chemokine (C-C motif) ligand 3	Mus musculus	0-39
8409405-1	1993	Macrophage inflammatory protein-1 alpha (MIP-1 alpha) is a member of the intercrine/chemokine family which consists of basic, heparin-binding, small molecular weight proteins.	Heparin	126-133	chemokine (C-C motif) ligand 3	Mus musculus	41-52
7692967-3	1993	At I = 0.15, pH 7.4, 25 degrees C, kininogen thus maximally increased the heparin enhancement of the second-order rate constant for the antithrombin-kallikrein reaction from 13-fold (1.6 x 10(2) M-1 s-1 to 2.1 x 10(3) M-1 s-1) to 1200-fold (1.9 x 10(5) M-1 s-1).	Heparin	74-81	serpin family C member 1	Homo sapiens	136-148
30081240-8	2018	Intriguingly, the heparin-induced in vitro aggregation propensity of the protein attenuated at both acidic and alkaline pH, illustrating the significance of altered conformations in pathological functions of tau.	Heparin	18-25	microtubule associated protein tau	Homo sapiens	208-211
8240409-2	1993	Heparin (Hep) as well as N-oleoyl-heparins behaved as tight-binding, hyperbolic noncompetitive inhibitors of HLE (KiHep = 75 pM) and CatG (KiHep &lt; 25 pM).	Heparin	0-7	cathepsin G	Homo sapiens	133-137
8240409-2	1993	Heparin (Hep) as well as N-oleoyl-heparins behaved as tight-binding, hyperbolic noncompetitive inhibitors of HLE (KiHep = 75 pM) and CatG (KiHep &lt; 25 pM).	Heparin	0-3	cathepsin G	Homo sapiens	133-137
8240409-8	1993	The residual activities of N-oleoyl-Hep complexes with CatG were much lower than the corresponding activities in the presence of Hep.	Heparin	36-39	cathepsin G	Homo sapiens	55-59
8408655-2	1993	We have explored the effect of shear stress on the expression of the heparin-binding growth factors platelet-derived growth factor B chain (PDGF-B) and basic fibroblast growth factor (bFGF) in bovine aortic endothelial cells using a purpose-built cone-plate viscometer.	Heparin	69-76	platelet derived growth factor subunit B	Bos taurus	100-138
8408655-2	1993	We have explored the effect of shear stress on the expression of the heparin-binding growth factors platelet-derived growth factor B chain (PDGF-B) and basic fibroblast growth factor (bFGF) in bovine aortic endothelial cells using a purpose-built cone-plate viscometer.	Heparin	69-76	platelet derived growth factor subunit B	Bos taurus	140-146
8122184-0	1993	Antithrombin-III plasma activity during and after prolonged use of heparin in unstable angina.	Heparin	67-74	serpin family C member 1	Homo sapiens	0-16
8122184-4	1993	Plasma antithrombin-III activity decreased rapidly from 1.05 +/- 0.03 to 1.0 +/- 0.03 U/ml (p &lt; 0.03) following heparin initiation with no further significant subsequent decrease.	Heparin	115-122	serpin family C member 1	Homo sapiens	7-23
8246447-0	1993	Ultrastructural localization of heparin to human mast cells of the MCTC and MCT types by labeling with antithrombin III-gold.	Heparin	32-39	serpin family C member 1	Homo sapiens	103-119
8246447-9	1993	CONCLUSIONS: The data with rodent mast cells indicate that antithrombin III-gold labels cells that contain heparin, but not those that contain only over-sulfated chondroitin sulfates.	Heparin	107-114	serpin family C member 1	Homo sapiens	59-75
8408007-7	1993	The cytoplasmic antithrombin activity was purified to apparent homogeneity from the cytosol of BSC-1 cells previously pulsed with [35S]methionine by a combination of heparin-agarose chromatography, Mono Q fast protein liquid chromatography, and anhydrotrypsin-Affi-Gel 10 affinity chromatography.	Heparin	166-173	serpin family C member 1	Homo sapiens	16-28
8216224-11	1993	for protease nexin I, protein C inhibitor and antithrombin III showed a bell-shaped dependence on heparin concentration.	Heparin	98-105	serpin family E member 2	Homo sapiens	4-20
8228638-3	1993	Fifteen min after heparin injection, LPL mass had increased to 536 +/- 60 ng.ml-1 and LPL activity to 261 +/- 34 mU.ml-1 and a highly significant correlation between the increments in mass and activity was observed.	Heparin	18-25	lipoprotein lipase	Homo sapiens	37-40
8228638-3	1993	Fifteen min after heparin injection, LPL mass had increased to 536 +/- 60 ng.ml-1 and LPL activity to 261 +/- 34 mU.ml-1 and a highly significant correlation between the increments in mass and activity was observed.	Heparin	18-25	lipoprotein lipase	Homo sapiens	86-89
8228638-5	1993	The LPL mass in preheparin plasma eluted early from heparin-Sepharose, in the position expected for inactive LPL monomers.	Heparin	19-26	lipoprotein lipase	Homo sapiens	4-7
8228638-7	1993	The increment of mass and activity after heparin eluted later from heparin-Sepharose, in the position expected for active LPL dimers.	Heparin	41-48	lipoprotein lipase	Homo sapiens	122-125
8216224-11	1993	for protease nexin I, protein C inhibitor and antithrombin III showed a bell-shaped dependence on heparin concentration.	Heparin	98-105	serpin family C member 1	Homo sapiens	46-62
8216224-12	1993	At optimal concentrations, heparin accelerated the rate of inhibition by protease nexin I, protein C inhibitor and antithrombin III by 44-, 18- and 13-fold respectively.	Heparin	27-34	serpin family E member 2	Homo sapiens	73-89
8228638-7	1993	The increment of mass and activity after heparin eluted later from heparin-Sepharose, in the position expected for active LPL dimers.	Heparin	67-74	lipoprotein lipase	Homo sapiens	122-125
32254968-5	2018	With the introduction of heparin, the antithrombin III (AT-III) binding ability was significantly enhanced with prolonged APTT time.	Heparin	25-32	serpin family C member 1	Homo sapiens	38-54
8246925-2	1993	These proteins, corresponding to human Oct-1 and Oct-2A nuclear factors, were purified by ion exchange and heparin-agarose chromatography.	Heparin	107-114	POU class 2 homeobox 1	Homo sapiens	39-44
8216224-12	1993	At optimal concentrations, heparin accelerated the rate of inhibition by protease nexin I, protein C inhibitor and antithrombin III by 44-, 18- and 13-fold respectively.	Heparin	27-34	serpin family C member 1	Homo sapiens	115-131
7505345-9	1993	3) Inflammatory reactants such as fibrinogen, alpha 2-PI,alpha 2-macroglobulin and alpha 1-antitrypsin decreased more significantly during this heparin-urokinase-pulse combined therapy than during our previous combined therapy consisting of only heparin and urokinase.	Heparin	144-151	alpha-2-macroglobulin	Homo sapiens	57-78
32254968-5	2018	With the introduction of heparin, the antithrombin III (AT-III) binding ability was significantly enhanced with prolonged APTT time.	Heparin	25-32	serpin family C member 1	Homo sapiens	56-62
8122184-5	1993	Antithrombin-III activity returned to the control values 4 hours after the discontinuation of heparin.	Heparin	94-101	serpin family C member 1	Homo sapiens	0-16
30172259-0	2018	Sulfated non-anticoagulant heparin blocks Th2-induced asthma by modulating the IL-4/signal transducer and activator of transcription 6/Janus kinase 1 pathway.	Heparin	27-34	heart and neural crest derivatives expressed 2	Mus musculus	42-45
8122184-6	1993	Thus, heparin treatment is associated with small, non-cumulative and rapidly reversible decrease in antithrombin-III activity.	Heparin	6-13	serpin family C member 1	Homo sapiens	100-116
8222262-3	1993	The plasma LPL mass increased by heparin injection (30 USP units/kg) and was found to positively correlate with LPL activity.	Heparin	33-40	lipoprotein lipase	Homo sapiens	11-14
30172259-0	2018	Sulfated non-anticoagulant heparin blocks Th2-induced asthma by modulating the IL-4/signal transducer and activator of transcription 6/Janus kinase 1 pathway.	Heparin	27-34	interleukin 4	Mus musculus	79-83
29734651-5	2018	Our data show that the hyperacetylation of Tau by p300 histone acetyltransferase (HAT) disfavors LLPS, inhibits heparin-induced aggregation, and impedes access to LLPS-initiated microtubule assembly.	Heparin	112-119	microtubule associated protein tau	Homo sapiens	43-46
8343518-2	1993	We have determined the dissociation constants, Kd, of 48.8 nM for the heparin-AT III interaction, of 175 nM for the specific pentasaccharide-AT III interaction, and of 13 microM for the low-affinity heparin-AT III interaction, using a binding assay based on a monoclonal antibody (MAb) that recognizes an epitope at or close to the heparin binding site of AT III.	Heparin	70-77	serpin family C member 1	Homo sapiens	78-84
8343518-0	1993	Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	60-76
8343518-0	1993	Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	145-161
8343518-0	1993	Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III.	Heparin	121-128	serpin family C member 1	Homo sapiens	60-76
8343518-0	1993	Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III.	Heparin	121-128	serpin family C member 1	Homo sapiens	145-161
8343518-1	1993	The inhibitory activity of the plasma serine proteinase inhibitor antithrombin III (AT III) is enhanced about 1000-fold upon binding to heparin.	Heparin	136-143	serpin family C member 1	Homo sapiens	66-82
8343518-1	1993	The inhibitory activity of the plasma serine proteinase inhibitor antithrombin III (AT III) is enhanced about 1000-fold upon binding to heparin.	Heparin	136-143	serpin family C member 1	Homo sapiens	84-90
8360197-4	1993	Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina.	Heparin	84-91	acetylcholinesterase	Rattus norvegicus	203-207
8360197-4	1993	Analysis of extracted AChE oligomeric forms showed that low salt buffers containing heparin and high salt buffers were capable of solubilizing substantial amounts of catalytically active collagen-tailed AChE, whereas none of these buffers were capable of detaching AChE from synaptic basal lamina.	Heparin	84-91	acetylcholinesterase	Rattus norvegicus	203-207
8354695-3	1993	Sequence analysis of the cDNA encoding murine clusterin revealed 92 and 75% sequence identity with the rat and human cDNAs, respectively, and conservation of the predicted structural features which include alpha-helical regions and heparin-binding domains.	Heparin	232-239	clusterin	Mus musculus	46-55
8349603-3	1993	HGF/NK1 was expressed in Escherichia coli and purified to homogeneity using heparin-affinity and fast protein liquid cation-exchange chromatography.	Heparin	76-83	tachykinin receptor 1	Homo sapiens	4-7
8236137-2	1993	The present report describes the antithrombin mediated inhibition of thrombin and factor Xa by surfaces modified with end point immobilized heparin.	Heparin	140-147	serpin family C member 1	Homo sapiens	33-45
8236137-4	1993	Both enzymes were rapidly inactivated by heparin surfaces after selective presaturation with antithrombin on the immobilized high affinity heparin molecules.	Heparin	41-48	serpin family C member 1	Homo sapiens	93-105
8236137-4	1993	Both enzymes were rapidly inactivated by heparin surfaces after selective presaturation with antithrombin on the immobilized high affinity heparin molecules.	Heparin	139-146	serpin family C member 1	Homo sapiens	93-105
7686910-13	1993	Heparin, but not alpha 2MRAP, inhibited cellular binding of 125I-LPL or 125I-beta-VLDL supplemented with LPL.	Heparin	0-7	lipoprotein lipase	Oryctolagus cuniculus	65-68
8331659-6	1993	The most significant difference between ATIII and alpha 1-antitrypsin lies in the 45 residue N-terminal extension in ATIII which contribute to the definition of the heparin binding site.	Heparin	165-172	serpin family C member 1	Homo sapiens	40-45
8331659-6	1993	The most significant difference between ATIII and alpha 1-antitrypsin lies in the 45 residue N-terminal extension in ATIII which contribute to the definition of the heparin binding site.	Heparin	165-172	serpin family C member 1	Homo sapiens	117-122
8331659-9	1993	Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein.	Heparin	77-84	serpin family C member 1	Homo sapiens	101-106
8331659-9	1993	Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein.	Heparin	171-178	serpin family C member 1	Homo sapiens	101-106
7686910-13	1993	Heparin, but not alpha 2MRAP, inhibited cellular binding of 125I-LPL or 125I-beta-VLDL supplemented with LPL.	Heparin	0-7	lipoprotein lipase	Oryctolagus cuniculus	105-108
29597024-11	2018	Moreover, the heparin mimetic hydrogel surface can augment endogenous BMP activity by sequestering and localizing the cell-produced BMPs.	Heparin	14-21	bone morphogenetic protein 1	Homo sapiens	70-73
8331144-5	1993	The second approach consisted of using heparin, a mucopolysaccharide with a strong affinity towards ATIII, coupled to amine-modified or epoxy-activated membranes by reductive amination, for the purification of rATIII.	Heparin	39-46	serpin family C member 1	Homo sapiens	100-105
29561141-0	2018	Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin.	Heparin	42-49	serpin family C member 1	Homo sapiens	109-121
8490170-2	1993	However, in the present study, we present evidence that factor VIIa bound to tissue factor, unlike free factor VIIa, is readily inactivated by AT III in the presence of heparin.	Heparin	169-176	serpin family C member 1	Homo sapiens	143-149
8490170-4	1993	AT III/heparin was also shown to inhibit the catalytic activity towards factor X of factor VIIa/tissue factor complexes formed on monolayers of an ovarian carcinoma cell line (OC-2008) that constitutively expresses surface membrane tissue factor.	Heparin	7-14	serpin family C member 1	Homo sapiens	0-6
8371063-7	1993	Heparin displacement of PG binding suggested a greater binding strength for DSPG-LpL-LDL with 0.25 micrograms heparin required to displace 50% of DSPG compared to 0.01 micrograms to displace 50% of CSPG.	Heparin	0-7	lipoprotein lipase	Homo sapiens	81-84
8371063-7	1993	Heparin displacement of PG binding suggested a greater binding strength for DSPG-LpL-LDL with 0.25 micrograms heparin required to displace 50% of DSPG compared to 0.01 micrograms to displace 50% of CSPG.	Heparin	110-117	lipoprotein lipase	Homo sapiens	81-84
8501120-8	1993	Immunoreactive PDGF A and B could be partially released by incubation of matrix material with heparin but not with other glycosaminoglycans.	Heparin	94-101	platelet-derived growth factor subunit A	Cricetulus griseus	15-27
29561141-0	2018	Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	109-121
29561141-1	2018	Heparin allosterically activates the anticoagulant serpin, antithrombin, by binding through a sequence-specific pentasaccharide and inducing activating conformational changes in the protein.	Heparin	0-7	serpin family C member 1	Homo sapiens	59-71
7506041-5	1993	The U138 PAI-2-like protein was adherent to an anti-PAI-2 immunoaffinity column and was demonstrated to be nonadherent to concanavalin A-agarose, heparin-Sepharose, and the anti-PAI-1 immunoaffinity column.	Heparin	146-153	serpin family E member 1	Homo sapiens	9-12
29784539-8	2018	These assays are not equivalent in terms of diagnosing protein abnormalities, associated with increased thrombotic incidence, and they have variable performance for reflecting impaired antithrombin binding capacity for heparin, reduced progressive inhibition of serine proteases, or accelerated switch rates to the latent and less active forms.	Heparin	219-226	serpin family C member 1	Homo sapiens	185-197
7506041-5	1993	The U138 PAI-2-like protein was adherent to an anti-PAI-2 immunoaffinity column and was demonstrated to be nonadherent to concanavalin A-agarose, heparin-Sepharose, and the anti-PAI-1 immunoaffinity column.	Heparin	146-153	serpin family B member 2	Homo sapiens	9-14
7506041-9	1993	This 50-kDa PAI was adherent to heparin-Sepharose and thrombin-agarose columns, and was not reactive with any antibodies for either PAI-1 or PAI-2.	Heparin	32-39	serpin family E member 1	Homo sapiens	12-15
8485868-4	1993	Nevertheless, very low PLA1 activities (&lt; or = 5 U/L, most likely due to heparin perfusion therapy) could also be detected by palmitic and stearic acid release from the sn-1 position, leading to small changes in fatty acid release patterns of sera with low PLA activities.	Heparin	76-83	POU class 2 homeobox 3	Homo sapiens	23-27
8485868-4	1993	Nevertheless, very low PLA1 activities (&lt; or = 5 U/L, most likely due to heparin perfusion therapy) could also be detected by palmitic and stearic acid release from the sn-1 position, leading to small changes in fatty acid release patterns of sera with low PLA activities.	Heparin	76-83	phospholipase A and acyltransferase 1	Homo sapiens	23-26
8485868-5	1993	Measurements with sera from heparin-treated volunteers demonstrated that heparin therapy may initially contribute as much as 22 U/L to increased PLA1 activities but is not important under prolonged therapy.	Heparin	28-35	POU class 2 homeobox 3	Homo sapiens	145-149
8485868-5	1993	Measurements with sera from heparin-treated volunteers demonstrated that heparin therapy may initially contribute as much as 22 U/L to increased PLA1 activities but is not important under prolonged therapy.	Heparin	73-80	POU class 2 homeobox 3	Homo sapiens	145-149
8364981-2	1993	Adding heparin to the NPC cultured medium stimulated the growth-factor secretion from NPC.	Heparin	7-14	myotrophin	Rattus norvegicus	57-70
29440901-7	2018	P28 release from mSIS-heparin-P28 and its effects on the proliferation, viability, and osteogenic differentiation of bone marrow stromal stem cells from ovariectomized rats (rBMSCs-OVX) were investigated in vitro.	Heparin	22-29	golgi SNAP receptor complex member 1	Rattus norvegicus	0-3
8364981-4	1993	The partially purified growth factor from the NPC appeared to be related to the HGF isolated from platelets according to three criteria: (a) binding to Heparin-Sepharose and eluting at about 0.65 M NaCl, (b) having a Mr of about 70 kDa, (c) having an immunoreactivity to antibody against rat platelet-derived HGF.	Heparin	152-159	myotrophin	Rattus norvegicus	23-36
8364981-5	1993	Adding heparin to the NPC cultured medium also resulted in protection of the growth factor from heat- and acid-inactivation, but the direct interaction of heparin with the partially purified growth factor did not lead to such protection.	Heparin	7-14	myotrophin	Rattus norvegicus	77-90
8443391-0	1993	Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis.	Heparin	78-85	serpin family C member 1	Homo sapiens	0-16
8443391-1	1993	A novel variant of antithrombin III (AT III) that lacks affinity for heparin was found in a 33-year-old man who suffered from recurrent cerebral infarction.	Heparin	69-76	serpin family C member 1	Homo sapiens	19-35
8443391-1	1993	A novel variant of antithrombin III (AT III) that lacks affinity for heparin was found in a 33-year-old man who suffered from recurrent cerebral infarction.	Heparin	69-76	serpin family C member 1	Homo sapiens	37-43
8443391-7	1993	Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally.	Heparin	100-107	serpin family C member 1	Homo sapiens	152-158
8443391-7	1993	Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally.	Heparin	100-107	serpin family C member 1	Homo sapiens	152-158
8443391-7	1993	Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally.	Heparin	100-107	serpin family C member 1	Homo sapiens	152-158
8389334-5	1993	Abdominal as well as femoral AT-LPL activities were significantly reduced after the exercise training programme (P &lt; 0.05) whereas plasma post-heparin (PH) LPL activity was significantly increased by training (P &lt; 0.05).	Heparin	146-153	lipoprotein lipase	Homo sapiens	159-162
8515556-3	1993	Although antithrombin-III activity was not measured in this case, the heparin resistance might have been caused by the decrease in the activity of antithrombin-III which might have resulted from the preoperative malnutrition, infection of urinary tract and/or institution of intraaortic balloon pumping (IABP).	Heparin	70-77	serpin family C member 1	Homo sapiens	147-163
8386317-7	1993	The phospho-CREB (P-CREB) phosphatase activity present in nuclear extracts coelutes with protein Ser/Thr phosphatase type 2A (PP2A) on Mono Q, amino-hexyl Sepharose, and heparin agarose columns and was chromatographically resolved from nuclear protein Ser/Thr-phosphatase type 1 (PP1).	Heparin	170-177	protein phosphatase 2 phosphatase activator	Homo sapiens	126-130
8487783-6	1993	Of the 22 complement proteins examined, 13 bound heparin (C1q, C2, C4, C4bp, C1INH, B, D, H, P, C6, C8, C9, and vitronectin) while 9 did not bind heparin (C1r, C1s, C3, Factor I, C5, C7, C3b, Ba and Bb).	Heparin	49-56	complement C1q A chain	Homo sapiens	58-61
8487654-5	1993	In studying lipoprotein lipase (LPL) activity and mass as one of the elements of lipid metabolism, heparin administration is necessary.	Heparin	99-106	lipoprotein lipase	Homo sapiens	12-30
8487654-5	1993	In studying lipoprotein lipase (LPL) activity and mass as one of the elements of lipid metabolism, heparin administration is necessary.	Heparin	99-106	lipoprotein lipase	Homo sapiens	32-35
29440901-11	2018	In vivo experiments revealed that mSIS-heparin-P28 dramatically stimulated osteoporotic bone regeneration.	Heparin	39-46	golgi SNAP receptor complex member 1	Rattus norvegicus	47-50
29215785-0	2018	Expression and functional characterization of two natural heparin-binding site variants of antithrombin.	Heparin	58-65	serpin family C member 1	Homo sapiens	91-103
8431448-6	1993	Heparin, at concentrations between 0.1 and 1 microgram/mL, significantly promoted thrombin inhibition by PAI-1 as well as SDS-stable complex formation.	Heparin	0-7	serpin family E member 1	Homo sapiens	105-110
8350512-8	1993	The authors developed an antithrombin III assay method to be able to estimate real activity without the influence of heparin cofactor II activity11), and to apply the low molecular weight heparin to prevent relapse of thrombosis, and finally to find an anticoagulant substance in an interesting case of hepatocellular carcinoma (Edmondson type 1) producing normal antithrombin III30).	Heparin	117-124	serpin family C member 1	Homo sapiens	25-41
8392227-5	1993	In the presence of heparin the potency of t-PA on fresh clots was considerably increased whilst the effect on old clots was not affected, a fresh clot selectivity for t-PA (64% lysis of fresh clots, 24% lysis of old clots) was thus effected.	Heparin	19-26	tissue-type plasminogen activator	Oryctolagus cuniculus	42-46
8392227-5	1993	In the presence of heparin the potency of t-PA on fresh clots was considerably increased whilst the effect on old clots was not affected, a fresh clot selectivity for t-PA (64% lysis of fresh clots, 24% lysis of old clots) was thus effected.	Heparin	19-26	tissue-type plasminogen activator	Oryctolagus cuniculus	167-171
7680324-4	1993	For heparin-binding sites, HSP90 was digested completely with trypsin, and the digests were applied to a heparin-Sepharose column and eluted with 1.0 M NaCl, followed by 8.0 M urea.	Heparin	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	27-32
29215785-1	2018	Essentials Heparin-binding site (HBS) variants of antithrombin (AT) are associated with thrombosis risk.	Heparin	11-18	serpin family C member 1	Homo sapiens	50-62
7680324-25	1993	The heparin-binding sites are present from the middle region of the HSP90 molecule, and the antigen sites are at the N-terminal domain.	Heparin	4-11	heat shock protein 90 alpha family class A member 1	Homo sapiens	68-73
8473288-0	1993	Binding of lipoprotein lipase to heparin.	Heparin	33-40	lipoprotein lipase	Homo sapiens	11-29
29215785-5	2018	SUMMARY: Background Several heparin-binding site (HBS) variants of antithrombin (AT) have been identified that predispose carriers to a higher incidence of thrombosis.	Heparin	28-35	serpin family C member 1	Homo sapiens	67-79
30271699-4	2018	The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated.	Heparin	44-51	serpin family C member 1	Homo sapiens	102-118
7682054-10	1993	In the presence of heparin aprotinin prolongs the activated clotting time and the in vitro activated partial thromboplastin time.	Heparin	19-26	pancreatic trypsin inhibitor	Bos taurus	27-36
8441232-7	1993	Furthermore, heparin treatment markedly inhibited the mesangial matrix expansion for a variety of ECM proteins, including laminin, type I and IV collagen, fibronectin and entactin.	Heparin	13-20	fibronectin 1	Rattus norvegicus	155-166
8419351-4	1993	Our data show that the activity of recombinant human factor VIIa is inhibited by antithrombin III in the presence of heparin at a rate of 1.7 x 10(2) M-1 s-1.	Heparin	117-124	serpin family C member 1	Homo sapiens	81-97
30271699-4	2018	The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated.	Heparin	44-51	serpin family C member 1	Homo sapiens	120-126
7678446-7	1993	MIP-1 beta was immobilized by binding to proteoglycan: a conjugate of heparin with bovine serum albumin and cellular proteoglycan CD44 were both effective.	Heparin	70-77	C-C motif chemokine ligand 4	Homo sapiens	0-10
8121125-4	1993	By day 3 activity of PAI increased from 13.5 +/- 2.0 to 18.2 +/- 1.93 U/ml, p = 0.018, and from 17.8 +/- 1.83 to 20.2 +/- 2.44 U/ml, ns, in heparin- and aspirin-treated patients, respectively.	Heparin	140-147	serpin family E member 1	Homo sapiens	21-24
8121125-7	1993	A decrease in antithrombin III observed in heparin group (from 115 +/- 3.2% to 98 +/- 3.4%, p &lt; 0.001) reflected specific action of the drug.	Heparin	43-50	serpin family C member 1	Homo sapiens	14-30
8394172-10	1993	Heparin was found to be the most potent inhibitor for both kinases with IC50s of 1.4 and 1.1 microM for beta ARK1 and beta ARK2, respectively.	Heparin	0-7	G protein-coupled receptor kinase 3	Bos taurus	118-127
8495867-6	1993	The development of ATIII-reactive capillaries was associated with a survival advantage, and such reactivity seemed to be promoted by heparin.	Heparin	133-140	serpin family C member 1	Homo sapiens	19-24
30271699-6	2018	In the two state binding process between AT III and heparin, temperature played a negligible role on ATIII binding to heparin (1st state reaction), but demonstrated a role in the conformational change process (2nd state reaction).	Heparin	118-125	serpin family C member 1	Homo sapiens	41-47
8439557-4	1993	Rabbit CEase (RCEase) retains the active-site serine (gxsxg), the active-site histidine and the tentative heparin binding site (KKRCLQ) at similar positions in comparison to pancreatic CEases of other species.	Heparin	106-113	carboxyl ester lipase	Homo sapiens	7-12
8412815-0	1993	Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin.	Heparin	28-35	serpin family C member 1	Homo sapiens	109-121
28301908-1	2018	Thrombate III is a human plasma-derived antithrombin III (AT-III) often utilized in patients on extracorporeal membrane oxygenation (ECMO) with suspected AT-III-mediated heparin resistance.	Heparin	170-177	serpin family C member 1	Homo sapiens	154-160
8362268-4	1993	In the AT III supplemented systems, heparin was able to inhibit strongly both Factor Xa and thrombin, while pentasaccharide could only inhibit Factor Xa.	Heparin	36-43	serpin family C member 1	Homo sapiens	7-13
8429040-6	1993	The second order rate constant (k2) for inhibition by antithrombin III without heparin was 3.7 x 10(5) M-1 min-1 for wild-type thrombin; rates for the mutant thrombins varied less than 2-fold.	Heparin	79-86	serpin family C member 1	Homo sapiens	54-70
8429040-7	1993	For inhibition by antithrombin III with heparin, the rate constant was 4.5 x 10(8) M-1 min-1 for wild-type thrombin with no significant differences between any of the recombinant thrombins.	Heparin	40-47	serpin family C member 1	Homo sapiens	18-34
8431448-4	1993	Inhibition of thrombin by PAI-1 was quantitatively analyzed in the presence of a wide range of concentrations of heparin, heparan sulfate, dermatan sulfate, chondroitin 4-sulfate, chondroitin 6-sulfate, keratan sulfate, and hyaluronic acid by measuring residual amidolytic activity.	Heparin	113-120	serpin family E member 1	Homo sapiens	26-31
29399079-1	2018	The anticoagulation effect of heparin requires adequate serum antithrombin (AT)-III levels.	Heparin	30-37	serpin family C member 1	Homo sapiens	62-83
8470059-5	1993	Small amounts of heparin were consistently detected in AT-III concentrates and post-infusion plasma samples.	Heparin	17-24	serpin family C member 1	Homo sapiens	55-61
8470059-6	1993	The short-lived quenching of thrombin generation after AT-III concentrate could be partially explained by the infusion of heparin, rather than by supranormal AT-III levels.	Heparin	122-129	serpin family C member 1	Homo sapiens	55-61
8465268-11	1993	On the other hand, antithrombin III makes little use of the recognition exosite; instead, its interactions are tightened with the help of heparin, which binds to a second basic site (the heparin binding site).	Heparin	138-145	serpin family C member 1	Homo sapiens	19-35
8465268-11	1993	On the other hand, antithrombin III makes little use of the recognition exosite; instead, its interactions are tightened with the help of heparin, which binds to a second basic site (the heparin binding site).	Heparin	187-194	serpin family C member 1	Homo sapiens	19-35
1366018-6	1992	Full activation requires longer heparin chains in order to stabilize the ternary complex between antithrombin and thrombin.	Heparin	32-39	serpin family C member 1	Homo sapiens	97-109
8154338-6	1993	Impairment by fibrin of thrombin inhibition by antithrombin III may account in part for the inability of unfractionated heparin to prevent post-operative deep vein thrombosis in up to 20% of patients who undergo major elective orthopaedic surgery, and may also explain the need for oral anticoagulants after unfractionated and low molecular weight heparins are used to initiate the treatment of established deep vein thrombi.	Heparin	348-356	serpin family C member 1	Homo sapiens	47-63
30037590-7	2018	LPL activity was measured in cell culture medium after heparin addition using human VLDL-TG as substrate.	Heparin	55-62	lipoprotein lipase	Homo sapiens	0-3
8274299-5	1993	It could also be partially blocked by incubation with heparin, suggesting that at least a component of the activity might be due to a member of the heparin-binding subgroup of the EGF family of growth factors.	Heparin	54-61	epidermal growth factor	Homo sapiens	180-183
8274299-5	1993	It could also be partially blocked by incubation with heparin, suggesting that at least a component of the activity might be due to a member of the heparin-binding subgroup of the EGF family of growth factors.	Heparin	148-155	epidermal growth factor	Homo sapiens	180-183
1280262-10	1992	Heparin or HS glycosaminoglycans are a prerequisite for the FGF receptor encoded by flg gene to bind basic FGF (Yayon, A., Klagsbrun, M., Esko, J. D., Leder, P., and Ornitz, D. M. (1991) Cell 64, 841-848).	Heparin	0-7	filaggrin	Homo sapiens	84-87
29031112-0	2017	Quantitative analysis of antithrombin III binding site in low molecular weight heparins by exhausetive heparinases digestion and capillary electrophoresis.	Heparin	79-87	serpin family C member 1	Homo sapiens	25-41
1448834-7	1992	CONCLUSIONS: We conclude that abnormal antithrombin III with defective heparin binding, even though heterozygous, may cause ischemic stroke in young adults.	Heparin	71-78	serpin family C member 1	Homo sapiens	39-55
8318251-3	1993	Partial purification of the immunoreactive 18 kDa BMP-2 from Xenopus embryo extract by gel filtration, heparin-Sepharose affinity chromatography and preparative SDS-PAGE resulted in co-purification and identification of higher molecular forms of BMP-2 of 110 kDa and 36 kDa.	Heparin	103-110	bone morphogenetic protein 2 S homeolog	Xenopus laevis	50-55
28664670-12	2017	CONCLUSIONS: Antithrombin pharmacokinetics are significantly influenced by the concurrent use of unfractionated heparin and baseline antithrombin activity.	Heparin	112-119	serpin family C member 1	Homo sapiens	13-25
1472067-7	1992	Heparin inhibited phosphorylation of the D4 peptide or phosvitin by CKI alpha.	Heparin	0-7	casein kinase I isoform alpha	Oryctolagus cuniculus	68-77
1426886-2	1992	The heparin-sensitive binding of 125I-low-density lipoprotein (LDL) to liver homogenates (reflecting the expression of the LDL receptor) was determined, together with the activities of the rate-limiting enzymes in cholesterol synthesis [3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase], bile acid production (cholesterol 7 alpha-hydroxylase), and cholesterol esterification (acyl CoA:cholesterol acyl transferase).	Heparin	4-11	low density lipoprotein receptor	Homo sapiens	123-135
1426886-2	1992	The heparin-sensitive binding of 125I-low-density lipoprotein (LDL) to liver homogenates (reflecting the expression of the LDL receptor) was determined, together with the activities of the rate-limiting enzymes in cholesterol synthesis [3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase], bile acid production (cholesterol 7 alpha-hydroxylase), and cholesterol esterification (acyl CoA:cholesterol acyl transferase).	Heparin	4-11	3-hydroxy-3-methylglutaryl-CoA reductase	Homo sapiens	239-294
1331763-10	1992	When permeabilized neurons were loaded with heparin, an inhibitor of the beta-adrenergic receptor kinase (beta ARK), 5-HT4 receptor desensitization was reduced by 30-40%.	Heparin	44-51	G protein-coupled receptor kinase 2	Mus musculus	73-104
1331763-10	1992	When permeabilized neurons were loaded with heparin, an inhibitor of the beta-adrenergic receptor kinase (beta ARK), 5-HT4 receptor desensitization was reduced by 30-40%.	Heparin	44-51	G protein-coupled receptor kinase 2	Mus musculus	106-114
1465181-3	1992	Heparan sulphate, heparinase lyase type I and to a lesser degree, heparin and chondroitin sulphate were effective in solubilizing a large part of the cholinesterase activity.	Heparin	18-25	butyrylcholinesterase	Homo sapiens	150-164
1333637-4	1992	The plasma level of lipoprotein lipase (LPL) was increased on the first post-operative day both in the heparin/dihydroergotamine (preoperative 217 +/- 79 microU ml-1 vs. 1289 +/- 318, n = 6, p &lt; 0.05) and the Fragmin-groups (136 +/- 16 vs. 668 +/- 123, n = 6, p &lt; 0.05).	Heparin	103-110	lipoprotein lipase	Homo sapiens	20-38
1333637-4	1992	The plasma level of lipoprotein lipase (LPL) was increased on the first post-operative day both in the heparin/dihydroergotamine (preoperative 217 +/- 79 microU ml-1 vs. 1289 +/- 318, n = 6, p &lt; 0.05) and the Fragmin-groups (136 +/- 16 vs. 668 +/- 123, n = 6, p &lt; 0.05).	Heparin	103-110	lipoprotein lipase	Homo sapiens	40-43
1333637-5	1992	This increase in plasma LPL was significantly higher in the heparin/dihydroergotamine-group compared to the Fragmin-group (p &lt; 0.05).	Heparin	60-67	lipoprotein lipase	Homo sapiens	24-27
1469094-2	1992	In all seven families, variant antithrombins with heparin-binding abnormalities were detected by crossed immunoelectrophoresis, and in six of the kindreds there was a reduced antigen concentration of plasma antithrombin.	Heparin	50-57	serpin family C member 1	Homo sapiens	31-43
1469094-5	1992	In contrast, s1C is spatially distant to the positively charged surface which forms the heparin binding site of antithrombin; altered heparin binding properties of s1C variants may therefore reflect conformational linkage between the reactive site and heparin binding regions of the molecule.	Heparin	88-95	serpin family C member 1	Homo sapiens	112-124
1469094-5	1992	In contrast, s1C is spatially distant to the positively charged surface which forms the heparin binding site of antithrombin; altered heparin binding properties of s1C variants may therefore reflect conformational linkage between the reactive site and heparin binding regions of the molecule.	Heparin	134-141	serpin family C member 1	Homo sapiens	112-124
1469094-5	1992	In contrast, s1C is spatially distant to the positively charged surface which forms the heparin binding site of antithrombin; altered heparin binding properties of s1C variants may therefore reflect conformational linkage between the reactive site and heparin binding regions of the molecule.	Heparin	134-141	serpin family C member 1	Homo sapiens	112-124
1385448-8	1992	This inhibition by heparin was also observed with laminin and fibronectin and, in the case of perlecan, was found to be independent of heparin binding to substrate.	Heparin	19-26	fibronectin 1	Mus musculus	62-73
29202212-11	2017	In alveolar macrophages, nebulized heparin reduced expression of procoagulant genes and the effectors of transforming growth factor beta (Smad 2, Smad 3) and nuclear factor kappa B (p-selectin, CCL-2).	Heparin	35-42	SMAD family member 2	Rattus norvegicus	138-144
1404598-8	1992	G10BP has stronger affinity for heparin and GC boxes than does Sp1, suggesting that G10BP may repress FN gene transcription by displacing Sp1.	Heparin	32-39	fibronectin 1	Rattus norvegicus	102-104
1390919-0	1992	Thermodynamic analysis of heparin binding to human antithrombin.	Heparin	26-33	serpin family C member 1	Homo sapiens	51-63
1390919-1	1992	The binding of heparin to human antithrombin III (ATIII) was investigated by titration calorimetry (TC) and differential scanning calorimetry (DSC).	Heparin	15-22	serpin family C member 1	Homo sapiens	32-48
1390919-1	1992	The binding of heparin to human antithrombin III (ATIII) was investigated by titration calorimetry (TC) and differential scanning calorimetry (DSC).	Heparin	15-22	serpin family C member 1	Homo sapiens	50-55
1390919-8	1992	This supports a two domain model of ATIII folding in which the lower stability domain (329 K) binds and is stabilized by heparin.	Heparin	121-128	serpin family C member 1	Homo sapiens	36-41
1400461-9	1992	Specifically, both HL and the LPL/HL chimera were eluted from immobilized heparin by 0.75 M NaCl, whereas 1.1 M NaCl was required to elute LPL and the HL/LPL chimera.	Heparin	74-81	lipoprotein lipase	Homo sapiens	30-33
29202212-11	2017	In alveolar macrophages, nebulized heparin reduced expression of procoagulant genes and the effectors of transforming growth factor beta (Smad 2, Smad 3) and nuclear factor kappa B (p-selectin, CCL-2).	Heparin	35-42	C-C motif chemokine ligand 2	Rattus norvegicus	194-199
28892658-1	2017	We report four children from different families with homozygous antithrombin (AT) deficiency type II affecting the heparin binding site (p.Leu131Phe mutation).	Heparin	115-122	serpin family C member 1	Homo sapiens	64-76
1480152-2	1992	This surface-bound LPL could be released into the medium when cardiac myocytes were incubated with heparin.	Heparin	99-106	lipoprotein lipase	Homo sapiens	19-22
1480152-4	1992	However, incubation of cardiac myocytes with either VLDL or oleic acid for &gt; 60 min did reduce heparin-releasable LPL activity.	Heparin	98-105	lipoprotein lipase	Homo sapiens	117-120
1327146-6	1992	From heparin-Agarose column, two PLC activity peaks exhibiting different substrate specificities were eluted.	Heparin	5-12	heparan sulfate proteoglycan 2	Homo sapiens	33-36
28820035-10	2017	CONCLUSION: It can be hypothesized that the wide discrepancy in HDR slope versus heparin sensitivity may be explained by an inaccurate prediction of the plasma heparin level and/or the change in HDR of individual patients, depending on in vivo factors such as extravascular sequestration of heparin, decreased intrinsic antithrombin activity level and platelet count and/or activity.	Heparin	160-167	serpin family C member 1	Homo sapiens	320-332
1326533-3	1992	The membrane-associated cytochrome b558 was solubilized with a detergent, n-heptyl beta-thioglucoside, and purified by DEAE-Sepharose, heparin-Sepharose, and Mono Q column chromatography.	Heparin	135-142	cytochrome b	Oryctolagus cuniculus	24-36
1326533-6	1992	However, the system showed high O2(-)-generating activity of 31.8 mol/s/mol of cytochrome b558 (52.5% of the original O2(-)-generating activity of the solubilized membranes) in the presence of a nitro blue tetrazolium (NBT) reductase fraction that was separated from the cytochrome b fraction by heparin-Sepharose chromatography.	Heparin	296-303	cytochrome b	Oryctolagus cuniculus	79-91
1428206-2	1992	Heparin-assisted dialysis resulted in a significant rise of VIII:C and AT III; with defibrotide, instead, there was evidence of thrombin activation (increased FPA and TAT).	Heparin	0-7	serpin family C member 1	Homo sapiens	71-77
1383494-11	1992	The present data demonstrate that, in the presence of heparin, [125I]aFGF binds with high affinity to the cloned FGF-flg receptor on NFlg26 cell membranes.	Heparin	54-61	filaggrin	Homo sapiens	117-120
1520875-8	1992	Several results suggested that heparin increased the binding of rt-PA to "cell-associated" PAI-1.	Heparin	31-38	serpin family E member 1	Homo sapiens	91-96
1520875-10	1992	Second, extracts from HUVEC preincubated with heparin contained increased amounts of rt-PA-PAI-1 complexes as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Heparin	46-53	serpin family E member 1	Homo sapiens	91-96
1520875-14	1992	Therefore, heparin, at therapeutic concentrations, may enhance or stabilize the association of PAs with endothelial cell-associated PAI-1.	Heparin	11-18	serpin family E member 1	Homo sapiens	132-137
1527025-2	1992	We have developed a significantly improved method for isolation of RK based on the specific interactions of phosphorylated forms of the enzyme with heparin-Sepharose.	Heparin	148-155	G protein-coupled receptor kinase 1	Homo sapiens	67-69
1425951-0	1992	O-acylated heparin derivatives with low anticoagulant activity decrease proliferation and increase alpha-smooth muscle actin expression in cultured arterial smooth muscle cells.	Heparin	11-18	actin gamma 2, smooth muscle	Rattus norvegicus	99-124
1425951-4	1992	The O-acylated derivatives of heparin fragments were also very active in reversing the de-differentiation of smooth muscle cell in culture, as estimated by the increase in the expression of alpha-smooth muscle actin and alpha-smooth muscle actin mRNA.	Heparin	30-37	actin gamma 2, smooth muscle	Rattus norvegicus	190-215
1425951-4	1992	The O-acylated derivatives of heparin fragments were also very active in reversing the de-differentiation of smooth muscle cell in culture, as estimated by the increase in the expression of alpha-smooth muscle actin and alpha-smooth muscle actin mRNA.	Heparin	30-37	actin gamma 2, smooth muscle	Rattus norvegicus	220-245
1477349-6	1992	Similar changes in pHi were observed after modification of additional recognition binding site by heparin.	Heparin	98-105	glucose-6-phosphate isomerase	Rattus norvegicus	19-22
28820035-10	2017	CONCLUSION: It can be hypothesized that the wide discrepancy in HDR slope versus heparin sensitivity may be explained by an inaccurate prediction of the plasma heparin level and/or the change in HDR of individual patients, depending on in vivo factors such as extravascular sequestration of heparin, decreased intrinsic antithrombin activity level and platelet count and/or activity.	Heparin	160-167	serpin family C member 1	Homo sapiens	320-332
28817384-5	2017	LMW elastic polymer improved the elasticity of the scaffolds, and significantly increased the amount of heparin conjugated to the micro/nanofibrous scaffolds, which in turn increased the loading capacity of vascular endothelial growth factor (VEGF) and prolonged the release of VEGF.	Heparin	104-111	vascular endothelial growth factor A	Rattus norvegicus	207-241
1412223-4	1992	The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III.	Heparin	97-104	serpin family C member 1	Homo sapiens	13-29
1377216-3	1992	SAP neutralized the catalytic effect of heparin on the thrombin-antithrombin III reaction more effectively than vitronectin, histidine-rich glycoprotein, fibronectin, and high-molecular-weight kininogen and almost as effectively as platelet factor 4.	Heparin	40-47	amyloid P component, serum	Homo sapiens	0-3
1377216-3	1992	SAP neutralized the catalytic effect of heparin on the thrombin-antithrombin III reaction more effectively than vitronectin, histidine-rich glycoprotein, fibronectin, and high-molecular-weight kininogen and almost as effectively as platelet factor 4.	Heparin	40-47	serpin family C member 1	Homo sapiens	64-80
1412223-4	1992	The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III.	Heparin	62-69	serpin family C member 1	Homo sapiens	13-29
1385458-1	1992	A panel of monoclonal antibodies (mAbs) to bovine fibronectin (FN) is described which modulates either heparin binding or cell adhesion to FN, or both.	Heparin	103-110	fibronectin 1	Bos taurus	50-61
28817384-5	2017	LMW elastic polymer improved the elasticity of the scaffolds, and significantly increased the amount of heparin conjugated to the micro/nanofibrous scaffolds, which in turn increased the loading capacity of vascular endothelial growth factor (VEGF) and prolonged the release of VEGF.	Heparin	104-111	vascular endothelial growth factor A	Rattus norvegicus	243-247
1639873-2	1992	Heparin appeared to bind directly to TGF-beta 1 and to prevent the association of TGF-beta 1 with alpha 2-macroglobulin (alpha 2-M).	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	98-119
1639873-2	1992	Heparin appeared to bind directly to TGF-beta 1 and to prevent the association of TGF-beta 1 with alpha 2-macroglobulin (alpha 2-M).	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	121-130
28817384-5	2017	LMW elastic polymer improved the elasticity of the scaffolds, and significantly increased the amount of heparin conjugated to the micro/nanofibrous scaffolds, which in turn increased the loading capacity of vascular endothelial growth factor (VEGF) and prolonged the release of VEGF.	Heparin	104-111	vascular endothelial growth factor A	Rattus norvegicus	278-282
1457941-0	1992	Binding kinetics of thrombin and antithrombin III with immobilized heparin using a spacer.	Heparin	67-74	serpin family C member 1	Homo sapiens	33-49
28442532-7	2017	Our data showed that compared with saline and heparin controls, monotherapy of simvastatin and the adjunctive therapy with simvastatin and heparin significantly improved the thrombus resolution and reduced inflammatory cells migration into the venous wall, the release of the inflammatory cell adhesion molecule (P-selectin), inflammatory chemokine (MCP-1) and pleiotropic proinflammatory cytokines (IL-6) into the blood, and the local expression of P-selectin and MCP-1 in the venous wall.	Heparin	139-146	P-selectin	Oryctolagus cuniculus	313-323
1457941-2	1992	In this study, the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin were investigated.	Heparin	51-58	serpin family C member 1	Homo sapiens	64-80
1457941-2	1992	In this study, the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin were investigated.	Heparin	51-58	serpin family C member 1	Homo sapiens	82-87
1457941-3	1992	Low molecular weight heparin (molecular weight, 6,000 daltons) was fractionated on an ATIII affinity column, and it was immobilized onto a styrene/p-amino styrene random co-polymer surface via hydrophilic spacer groups.	Heparin	21-28	serpin family C member 1	Homo sapiens	86-91
1457941-7	1992	The binding constants of immobilized heparin and ATIII, and immobilized heparin and thrombin, were 0.958 x 10(7) M-1 and 1.76 x 10(8) M-1, respectively.	Heparin	37-44	serpin family C member 1	Homo sapiens	49-54
1457941-8	1992	The immobilized heparin bound with both ATIII and thrombin, and the binding mechanism was similar to that of free heparin.	Heparin	16-23	serpin family C member 1	Homo sapiens	40-45
1378017-6	1992	The binding of GMP-140 to primed T cells is not influenced by preactivation with phorbol 12-myristate 13-acetate, is almost completely abolished by pretreatment of T cells with neuraminidase or trypsin, and is also strongly inhibited by EDTA, the soluble sulfated glycans dextran sulfate, fucoidan, and heparin, but not by chondroitin sulfates.	Heparin	303-310	selectin P	Homo sapiens	15-22
1613550-1	1992	FN-C/H II is a heparin binding synthetic peptide from the C-terminal cell and heparin binding domain of fibronectin (FN) that mediates neuronal cell adhesion, spreading, and neurite outgrowth.	Heparin	15-22	fibronectin 1	Rattus norvegicus	104-115
1613550-1	1992	FN-C/H II is a heparin binding synthetic peptide from the C-terminal cell and heparin binding domain of fibronectin (FN) that mediates neuronal cell adhesion, spreading, and neurite outgrowth.	Heparin	15-22	fibronectin 1	Rattus norvegicus	0-2
1613550-1	1992	FN-C/H II is a heparin binding synthetic peptide from the C-terminal cell and heparin binding domain of fibronectin (FN) that mediates neuronal cell adhesion, spreading, and neurite outgrowth.	Heparin	78-85	fibronectin 1	Rattus norvegicus	104-115
1613550-1	1992	FN-C/H II is a heparin binding synthetic peptide from the C-terminal cell and heparin binding domain of fibronectin (FN) that mediates neuronal cell adhesion, spreading, and neurite outgrowth.	Heparin	78-85	fibronectin 1	Rattus norvegicus	0-2
1613550-5	1992	Additionally, heparitinase treatment decreased the spreading of cells on the 33/66 kDa fragments containing the C-terminal heparin binding domain of FN.	Heparin	123-130	fibronectin 1	Rattus norvegicus	149-151
1618758-1	1992	Resolution of the antithrombin conformational change contribution to heparin rate enhancement.	Heparin	69-76	serpin family C member 1	Homo sapiens	18-30
1425930-0	1992	Inhibition by heparin of platelet activation induced by neutrophil-derived cathepsin G.	Heparin	14-21	cathepsin G	Homo sapiens	75-86
1425930-3	1992	The present study shows that different heparin preparations (50 nM) completely prevent human platelet aggregation, serotonin release and thromboxane B2 production induced by purified neutrophil-derived cathepsin G (E.C.	Heparin	39-46	cathepsin G	Homo sapiens	202-213
1377216-4	1992	SAP also blocked the effects of heparin and dermatan sulfate on the inhibition of thrombin by heparin cofactor II.	Heparin	32-39	amyloid P component, serum	Homo sapiens	0-3
1377216-5	1992	We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP.	Heparin	83-90	amyloid P component, serum	Homo sapiens	75-78
1377216-5	1992	We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP.	Heparin	162-169	amyloid P component, serum	Homo sapiens	75-78
1377216-5	1992	We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP.	Heparin	162-169	serpin family C member 1	Homo sapiens	142-158
1377216-5	1992	We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP.	Heparin	162-169	amyloid P component, serum	Homo sapiens	183-186
1377216-6	1992	We conclude that SAP may account for much of the heparin-neutralizing capacity of plasma under some conditions and that basement-membrane-bound SAP may modulate extravascular coagulation by blocking the anticoagulant effects of basement membrane glycosaminoglycans.	Heparin	49-56	amyloid P component, serum	Homo sapiens	17-20
1322691-0	1992	Ratios of anti-factor Xa to antithrombin activities of heparins as determined in recalcified human plasma.	Heparin	55-63	serpin family C member 1	Homo sapiens	28-40
1322691-8	1992	Calcium reduced the anti-thrombin activities of all the heparin preparations studied about 1.5 times when purified ATIII was used, although in plasma this effect was less clear.	Heparin	56-63	serpin family C member 1	Homo sapiens	115-120
1643206-1	1992	Commercial partial thromboplastin reagents markedly differ in their sensitivity to factor deficiency, heparin, or the lupus anticoagulant.	Heparin	102-109	coagulation factor III, tissue factor	Bos taurus	19-33
1425930-6	1992	This inhibitory effect was not related to the anticoagulant property of the compounds, since a heparin preparation with an inactivated active for antithrombin III was also effective.	Heparin	95-102	serpin family C member 1	Homo sapiens	146-162
1425930-9	1992	Heparins were also shown to reduce platelet activation induced by cathepsin G released from activated polymorphonuclear leucocytes in mixed cell suspensions.	Heparin	0-8	cathepsin G	Homo sapiens	66-77
1425930-10	1992	As polymorphonuclear leucocytes might contribute to both arterial and venous thrombosis through platelet activation induced by the release of cathepsin G, this novel property of heparin could be used to optimize its antithrombotic efficacy.	Heparin	178-185	cathepsin G	Homo sapiens	142-153
1376317-4	1992	Utilizing synthetic peptides encompassing overlapping sequences of the heparin-binding domain of VN, adjacent heparin and PAI-1-binding sites were localized within the sequence 348-370 of VN.	Heparin	71-78	serpin family E member 1	Homo sapiens	122-127
28442532-7	2017	Our data showed that compared with saline and heparin controls, monotherapy of simvastatin and the adjunctive therapy with simvastatin and heparin significantly improved the thrombus resolution and reduced inflammatory cells migration into the venous wall, the release of the inflammatory cell adhesion molecule (P-selectin), inflammatory chemokine (MCP-1) and pleiotropic proinflammatory cytokines (IL-6) into the blood, and the local expression of P-selectin and MCP-1 in the venous wall.	Heparin	139-146	P-selectin	Oryctolagus cuniculus	450-460
1643210-9	1992	Mutations causing amino acid substitutions solely affecting the heparin binding site have thus far been located primarily at the N-terminal region of the molecule, residues 7-129; this region has been postulated to align as a positive groove in the molecule that forms the primary contact region for the essential antithrombin binding pentasaccharide of heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	314-326
27852920-4	2017	The purpose of this study was to assess the effect of heparin, including nonanticoagulant (desulfated) heparins, on basal and Thr-induced expression of TF and inflammatory cytokines in DCs.	Heparin	54-61	coagulation factor III, tissue factor	Homo sapiens	152-154
1374298-9	1992	These results in the injured rat carotid artery agree with our earlier observations that heparin inhibits t-PA gene expression in cultured baboon aortic SMCs.	Heparin	89-96	plasminogen activator, tissue type	Rattus norvegicus	106-110
1505142-5	1992	Heparin produces its antithrombotic effect by binding to antithrombin III and this complex then binds to thrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	57-73
1374012-10	1992	However, the inhibition of collagen synthesis by heparin and bFGF appears to involve divergent pathways since exogenous IGF-1 could overcome the effect of heparin but not bFGF on collagen synthesis.	Heparin	49-56	insulin-like growth factor 1	Rattus norvegicus	120-125
1374012-10	1992	However, the inhibition of collagen synthesis by heparin and bFGF appears to involve divergent pathways since exogenous IGF-1 could overcome the effect of heparin but not bFGF on collagen synthesis.	Heparin	155-162	insulin-like growth factor 1	Rattus norvegicus	120-125
27852920-4	2017	The purpose of this study was to assess the effect of heparin, including nonanticoagulant (desulfated) heparins, on basal and Thr-induced expression of TF and inflammatory cytokines in DCs.	Heparin	103-111	coagulation factor III, tissue factor	Homo sapiens	152-154
1567914-11	1992	The effects of emulsion were quite different from those of heparin, which caused an immediate release of the lipase to plasma, decreased uptake of LPL in most extrahepatic tissues by 60-95%, and increased the fraction taken up in the liver.	Heparin	59-66	lipase G, endothelial type	Rattus norvegicus	109-115
1551875-6	1992	Unlabeled heparin, dextran sulfate, and the CD4-derived peptides were able to compete with the binding of soluble gp120 to immobilized antibodies against fragments of the V3 from isolate IIIB, but they had no effect on the binding of gp120 to anti-peptide antibodies targeted against another unrelated region of gp120.	Heparin	10-17	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	114-119
1551875-6	1992	Unlabeled heparin, dextran sulfate, and the CD4-derived peptides were able to compete with the binding of soluble gp120 to immobilized antibodies against fragments of the V3 from isolate IIIB, but they had no effect on the binding of gp120 to anti-peptide antibodies targeted against another unrelated region of gp120.	Heparin	10-17	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	234-239
1551875-6	1992	Unlabeled heparin, dextran sulfate, and the CD4-derived peptides were able to compete with the binding of soluble gp120 to immobilized antibodies against fragments of the V3 from isolate IIIB, but they had no effect on the binding of gp120 to anti-peptide antibodies targeted against another unrelated region of gp120.	Heparin	10-17	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	234-239
1556128-3	1992	HB-EGF was purified from the conditioned medium of U-937 cells using cation exchange, copper affinity, heparin affinity, and two rounds of C4 reversed phase liquid chromatography.	Heparin	103-110	heparin binding EGF like growth factor	Homo sapiens	0-6
1595109-1	1992	BACKGROUND AND PURPOSE: The aims of this study were to verify that tissue-type plasminogen activator given either 1 or 2 hours after experimental embolic stroke in rabbits diminishes the volume of resulting ischemic brain and to ascertain the effect of the simultaneous administration of heparin.	Heparin	288-295	tissue-type plasminogen activator	Oryctolagus cuniculus	67-100
1329257-0	1992	Study of low molecular weight heparin effect on the relation between anticoagulant activity and antithrombin III affinity.	Heparin	30-37	serpin family C member 1	Homo sapiens	96-112
1374012-6	1992	A high concentration of insulin-like growth factor-1 (IGF-1, 3 x 10(-8) M) reversed the inhibitory effect of heparin on DNA synthesis and CDP labeling.	Heparin	109-116	insulin-like growth factor 1	Rattus norvegicus	24-52
1374012-6	1992	A high concentration of insulin-like growth factor-1 (IGF-1, 3 x 10(-8) M) reversed the inhibitory effect of heparin on DNA synthesis and CDP labeling.	Heparin	109-116	insulin-like growth factor 1	Rattus norvegicus	54-59
1551911-3	1992	The protein kinase was separable from HSP90 by adsorption to heparin-Sepharose or phosphocellulose.	Heparin	61-68	heat shock protein 90 alpha family class A member 1	Homo sapiens	38-43
1311318-7	1992	We found that heparin, a beta ARK inhibitor, ablated short term agonist-induced desensitization of alpha 2AAR, while such desensitization was unaffected by inhibition of protein kinase A.	Heparin	14-21	AXL receptor tyrosine kinase	Homo sapiens	30-33
1311598-0	1992	1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.	Heparin	120-127	serpin family C member 1	Homo sapiens	70-86
27975162-7	2017	Heparin-induced c-Met activation increased migration and invasion through ERK1/2, early growth response factor 1 (EGR1) and Matrix Metalloproteinases (MMP) axis.	Heparin	0-7	early growth response 1	Homo sapiens	82-112
1311598-4	1992	Perturbations to the 1H resonances in the NMR spectrum of antithrombin upon binding of the two series of heparin fragments are compared to those generated by intact heparin binding, as well as to the effects of binding of a synthetic high-affinity pentasaccharide.	Heparin	105-112	serpin family C member 1	Homo sapiens	58-70
1547341-0	1992	Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity.	Heparin	74-81	serpin family C member 1	Homo sapiens	0-16
27975162-7	2017	Heparin-induced c-Met activation increased migration and invasion through ERK1/2, early growth response factor 1 (EGR1) and Matrix Metalloproteinases (MMP) axis.	Heparin	0-7	early growth response 1	Homo sapiens	114-118
1547341-1	1992	Antithrombin-III-Stockholm is a new structural variant of antithrombin-III (AT-III) with normal heparin affinity but defective serine protease inhibitory activity.	Heparin	96-103	serpin family C member 1	Homo sapiens	0-16
1311598-5	1992	All of the heparin fragments examined appear to bind to antithrombin at the same site.	Heparin	11-18	serpin family C member 1	Homo sapiens	56-68
1547341-1	1992	Antithrombin-III-Stockholm is a new structural variant of antithrombin-III (AT-III) with normal heparin affinity but defective serine protease inhibitory activity.	Heparin	96-103	serpin family C member 1	Homo sapiens	58-74
1311598-6	1992	Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49.	Heparin	13-20	serpin family C member 1	Homo sapiens	136-148
28229161-8	2017	Antithrombin deficiency in these cases should be classified as pleiotropic based on the impaired reactivity and low heparin affinity of the variant.	Heparin	116-123	serpin family C member 1	Homo sapiens	0-12
1582175-7	1992	Both heparin-releasable and non-releasable lipoprotein lipase fractions had similar Km values for Intralipid and a similar pattern of inhibition by high density lipoprotein but different responses to heparin.	Heparin	200-207	lipoprotein lipase	Homo sapiens	43-61
1547341-1	1992	Antithrombin-III-Stockholm is a new structural variant of antithrombin-III (AT-III) with normal heparin affinity but defective serine protease inhibitory activity.	Heparin	96-103	serpin family C member 1	Homo sapiens	76-82
1547341-11	1992	The minimal thrombin-complexing ability of the mutant AT-III protein that was observed was accelerated by heparin, but to subnormal levels.	Heparin	106-113	serpin family C member 1	Homo sapiens	54-60
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	44-51	serpin family C member 1	Homo sapiens	149-155
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	94-101	serpin family C member 1	Homo sapiens	149-155
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	94-101	serpin family C member 1	Homo sapiens	149-155
1321995-4	1992	On the other hand, UF-heparin bound to F.Xa, thrombin and AT III with the strongest affinity to AT III followed by thrombin and F.Xa.	Heparin	22-29	serpin family C member 1	Homo sapiens	58-64
1321995-4	1992	On the other hand, UF-heparin bound to F.Xa, thrombin and AT III with the strongest affinity to AT III followed by thrombin and F.Xa.	Heparin	22-29	serpin family C member 1	Homo sapiens	96-102
1321995-5	1992	AT III mediated the binding between F.Xa and FR-860 and accelerated the reaction between F.Xa and UF-heparin.	Heparin	101-108	serpin family C member 1	Homo sapiens	0-6
1541298-5	1992	This reaction can be inhibited by heparin and the ATP analogue 5,6-dichloro-1-(beta-D-ribofuranosyl)benzimidazole (DRB), both known to be potent inhibitors of CKII.	Heparin	34-41	casein kinase 2 alpha 1	Homo sapiens	159-163
1315572-13	1992	It is possible that heparin could interact with endothelium and bind ATIII to maintain a state of thromboresistance.	Heparin	20-27	serpin family C member 1	Homo sapiens	69-74
1541873-0	1992	Heparin inhibits neutrophil-induced platelet activation via cathepsin G.	Heparin	0-7	cathepsin G	Homo sapiens	60-71
1733939-1	1992	The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity.	Heparin	17-24	serpin family C member 1	Homo sapiens	128-144
1733939-1	1992	The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity.	Heparin	17-24	serpin family C member 1	Homo sapiens	146-151
1733939-1	1992	The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity.	Heparin	179-186	serpin family C member 1	Homo sapiens	128-144
1733939-1	1992	The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity.	Heparin	179-186	serpin family C member 1	Homo sapiens	146-151
1733939-2	1992	The isolation of a significant fraction of heparin chains without antithrombin III-binding sites and having low affinity for ATIII suggests the presence of a precursor site, lacking the 3-O-sulfate group.	Heparin	43-50	serpin family C member 1	Homo sapiens	125-130
1733939-8	1992	This oligosaccharide was only slightly enriched in heparin having a low affinity for ATIII and only slightly disenriched in high affinity heparin.	Heparin	51-58	serpin family C member 1	Homo sapiens	85-90
1733939-9	1992	The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis.	Heparin	98-106	serpin family C member 1	Homo sapiens	26-31
1733939-9	1992	The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis.	Heparin	98-105	serpin family C member 1	Homo sapiens	26-31
1733939-9	1992	The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis.	Heparin	155-162	serpin family C member 1	Homo sapiens	26-31
1560580-4	1992	There was a distinct negative correlation between the reduction in protein binding ratio of lidocaine and the increase of non-esterified fatty acid (NEFA) based on the activated lipoprotein lipase after heparin administration.	Heparin	203-210	lipoprotein lipase	Homo sapiens	178-196
27761978-5	2017	The association of the previously published heparin plasma MMP-7 threshold of 12.1 ng/mL with all-cause mortality or transplant-free survival (TFS) was determined, either as an independent biomarker or as part of the modified personal clinical and molecular mortality index (m-PCMI).	Heparin	44-51	matrix metallopeptidase 7	Homo sapiens	59-64
1346414-2	1992	While heparin functions as an anticoagulant primarily by its ability to accelerate the action of the plasma protein inhibitor antithrombin III, dermatan sulphate acts selectively through a structurally related inhibitor, heparin co-factor II, to inhibit thrombin.	Heparin	6-13	serpin family C member 1	Homo sapiens	126-142
1730729-0	1992	Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor.	Heparin	85-92	serpin family C member 1	Homo sapiens	14-26
1730729-6	1992	The antithrombin-peptide complex had a conformation similar to that of reactive bond-cleaved antithrombin and, like the cleaved inhibitor, also had a higher conformational stability and lower heparin affinity than intact antithrombin.	Heparin	192-199	serpin family C member 1	Homo sapiens	4-16
1733939-9	1992	The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis.	Heparin	155-162	serpin family C member 1	Homo sapiens	140-145
1733939-10	1992	Rather these data suggest that some earlier step, involved in the formation of placement of these precursor sites, may be primarily responsible for high and low ATIII affinity heparins.	Heparin	176-184	serpin family C member 1	Homo sapiens	161-166
1319616-7	1992	The specific antithrombin activity of all heparins, when expressed in terms of material with high affinity to antithrombin III (HAM) with a MW greater than 5,400 is 13.0 min-1/(microgram/ml) (range 10.5-15.9).	Heparin	42-50	serpin family C member 1	Homo sapiens	110-126
1346095-9	1992	These results suggest that LACI serves as a cofactor for heparin and thus greatly enhances the inhibition of TF-induced coagulation.	Heparin	57-64	coagulation factor III, tissue factor	Homo sapiens	109-111
1346095-14	1992	Based on the above results, it is concluded that LACI is a cofactor for heparin in the inhibition of TF-induced clotting and that LACI and sulfated polysaccharides act synergistically in whole plasma.	Heparin	72-79	coagulation factor III, tissue factor	Homo sapiens	101-103
1730729-8	1992	The extent of complex formation was reduced in the presence of heparin with high affinity for antithrombin, which is consistent with heparin binding and peptide incorporation being linked.	Heparin	63-70	serpin family C member 1	Homo sapiens	94-106
1730729-8	1992	The extent of complex formation was reduced in the presence of heparin with high affinity for antithrombin, which is consistent with heparin binding and peptide incorporation being linked.	Heparin	133-140	serpin family C member 1	Homo sapiens	94-106
28297651-4	2017	Here, we used surface plasmon resonance (SPR) and NMR spectroscopy to characterize the interaction between two tau fragments, K18 and K19, and several polysaccharides, including heparin, heparin oligosaccharides, chemically modified heparin, and related glycans.	Heparin	187-194	keratin 18	Homo sapiens	126-129
1730217-4	1992	The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III.	Heparin	25-32	serpin family C member 1	Homo sapiens	73-89
1730217-4	1992	The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III.	Heparin	25-32	serpin family C member 1	Homo sapiens	138-154
28297651-5	2017	Using a heparin-immobilized chip, SPR revealed that tau K18 and K19 bind heparin with a KD of 0.2 and 70 muM, respectively.	Heparin	8-15	keratin 18	Homo sapiens	56-59
1579895-8	1992	Based on the good results in these two patients, and a review of previously reported cases, we propose that heparin alone, in a dose to maintain the APTT in a therapeutic range, provides adequate prophylaxis and treatment for VTE during pregnancy and delivery in many AT III deficient subjects.	Heparin	108-115	serpin family C member 1	Homo sapiens	268-274
1579900-2	1992	Nevertheless functional assays can be biased by the antithrombin III (AT III)-heparin complex activity; in fact trace amounts of heparin generally contaminate dermatan sulfate (DS) commercial preparations used as HC II reaction activators.	Heparin	78-85	serpin family C member 1	Homo sapiens	52-68
1579900-2	1992	Nevertheless functional assays can be biased by the antithrombin III (AT III)-heparin complex activity; in fact trace amounts of heparin generally contaminate dermatan sulfate (DS) commercial preparations used as HC II reaction activators.	Heparin	78-85	serpin family C member 1	Homo sapiens	70-76
1332442-10	1992	Further studies show that the GlcA residue in the antithrombin III binding pentasaccharide is oxidized much more rapidly than the bulk of the GlcA residues in heparin.	Heparin	159-166	serpin family C member 1	Homo sapiens	50-66
1552236-5	1992	Improved diabetes control resulted in a significant increase in LPL activity in both the heparin-releasable (HR) and extractable (EXT) fractions of adipose tissue, as well as in LPL immunoreactive mass.	Heparin	89-96	lipoprotein lipase	Homo sapiens	64-67
1579900-5	1992	The absence of any interference due to AT III-heparin complexes was verified in a kinetic HC II assay of some human plasma pools.	Heparin	46-53	serpin family C member 1	Homo sapiens	39-45
1579900-7	1992	Progressive increase of heparin concentration in the assay was effective only starting from 30 U/ml (the assay was carried out in the presence of polybrene to prevent any AT III activation).	Heparin	24-31	serpin family C member 1	Homo sapiens	171-177
1456017-2	1992	The bone inductive activity, termed osteogenin, can be dissociatively extracted, and it was isolated by heparin affinity, hydroxyapatite and molecular sieve chromatography.	Heparin	104-111	bone morphogenetic protein 3	Bos taurus	36-46
1364970-5	1992	The in vivo acceleration of lipoprotein metabolism by heparin resulted in: 1) the reduction of VLDL-TAG and HDL2-TAG, and in the increase of HDL3-TAG, 2) the appearance of positive relation of HDL2-C to the LPL activity and of opposite relation to the HL activity, 3) the lack of HL correlation to the TAG of HDL and HDL3.	Heparin	54-61	lipoprotein lipase	Homo sapiens	207-210
28297651-5	2017	Using a heparin-immobilized chip, SPR revealed that tau K18 and K19 bind heparin with a KD of 0.2 and 70 muM, respectively.	Heparin	73-80	keratin 18	Homo sapiens	56-59
1309590-4	1992	By using a cytokine-dependent lymphoid cell line engineered to express mFR1, we also showed that FGF-induced mitogenic activity is heparin dependent.	Heparin	131-138	aldo-keto reductase family 1, member B8	Mus musculus	71-75
1576105-0	1992	In vivo inactivation of antithrombin III is promoted by heparin during cardiopulmonary bypass.	Heparin	56-63	serpin family C member 1	Homo sapiens	24-40
1576105-1	1992	To study the in vivo effect of heparin on antithrombin III (AT3) when elastase is elevated, the blood of 20 patients undergoing cardiopulmonary bypass (CPB) was assayed for elastase and AT3.	Heparin	31-38	serpin family C member 1	Homo sapiens	42-58
28297651-9	2017	NMR showed the largest chemical-shift perturbation (CSP) in R2 in tau K18, which was absent in K19, revealing differential binding sites in K18 and K19 to heparin.	Heparin	155-162	keratin 18	Homo sapiens	70-73
1576105-1	1992	To study the in vivo effect of heparin on antithrombin III (AT3) when elastase is elevated, the blood of 20 patients undergoing cardiopulmonary bypass (CPB) was assayed for elastase and AT3.	Heparin	31-38	serpin family C member 1	Homo sapiens	60-63
28297651-9	2017	NMR showed the largest chemical-shift perturbation (CSP) in R2 in tau K18, which was absent in K19, revealing differential binding sites in K18 and K19 to heparin.	Heparin	155-162	keratin 18	Homo sapiens	140-143
1576105-7	1992	These data indicate that (1) CPB is associated with an increase in plasma elastase, (2) elevated plasma elastase is associated with a reduction in AT3, and (3) heparin promotes the inactivation of AT3 when serum elastase is increased.	Heparin	160-167	serpin family C member 1	Homo sapiens	197-200
28297651-11	2017	2-O-desulfated heparin induced much larger CSP in K18 than 6-O-desulfated heparin.	Heparin	15-22	keratin 18	Homo sapiens	50-53
1576105-8	1992	These data confirm the in vitro observation that heparin accelerates the inactivation of AT3 in the presence of elastase.	Heparin	49-56	serpin family C member 1	Homo sapiens	89-92
28104757-0	2017	Analysis and identification of the Grem2 heparin/heparan sulfate-binding motif.	Heparin	41-48	gremlin 2, DAN family BMP antagonist	Homo sapiens	35-40
28104757-2	2017	Similar to the BMP ligands, certain DAN family members have been shown to interact with heparin and heparan sulfate (HS).	Heparin	88-95	bone morphogenetic protein 1	Homo sapiens	15-18
1946443-4	1991	The stimulated protein kinase activity, which was blocked by a selective antagonist of N-methyl-D-aspartate receptors, exhibited specific properties of CK-II, including phosphorylation of the specific substrates of CK-II, marked inhibition by a low heparin concentration, and the use of GTP as a phosphate donor.	Heparin	249-256	casein kinase 2 alpha 1	Homo sapiens	152-157
1946443-4	1991	The stimulated protein kinase activity, which was blocked by a selective antagonist of N-methyl-D-aspartate receptors, exhibited specific properties of CK-II, including phosphorylation of the specific substrates of CK-II, marked inhibition by a low heparin concentration, and the use of GTP as a phosphate donor.	Heparin	249-256	casein kinase 2 alpha 1	Homo sapiens	215-220
1746447-7	1991	Although antiplatelet and antithrombin agents such as aspirin and heparin help to decrease rethrombosis, these agents are far from ideal.	Heparin	66-73	serpin family C member 1	Homo sapiens	26-38
28104757-4	2017	In the present study, we used mutagenesis, heparin-binding measurements, and cell surface-binding analysis to identify lysine residues that are important for heparin/HS binding in Grem2.	Heparin	158-165	gremlin 2, DAN family BMP antagonist	Homo sapiens	180-185
28104757-7	2017	Overall, the present study shows that the Grem2 heparin/HS and BMP-binding epitopes are unique and independent, where, interestingly, the Grem2-BMP2 complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope.	Heparin	48-55	gremlin 2, DAN family BMP antagonist	Homo sapiens	42-47
28104757-7	2017	Overall, the present study shows that the Grem2 heparin/HS and BMP-binding epitopes are unique and independent, where, interestingly, the Grem2-BMP2 complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope.	Heparin	48-55	gremlin 2, DAN family BMP antagonist	Homo sapiens	138-143
28104757-7	2017	Overall, the present study shows that the Grem2 heparin/HS and BMP-binding epitopes are unique and independent, where, interestingly, the Grem2-BMP2 complex exhibits a significant increase in binding affinity toward heparin moieties that appear to be partially independent of the Grem2 heparin/HS-binding epitope.	Heparin	48-55	gremlin 2, DAN family BMP antagonist	Homo sapiens	138-143
1722112-5	1991	Culturing NFS-5.3 with heparin similarly decreases the membrane-form mu; however, it increases the surface level of a pentameric mu molecule containing secreted-form mu (microS) heavy chains, disulfide-linked omega (lambda 5) chains, and noncovalently associated proteins.	Heparin	23-30	immunoglobulin lambda like polypeptide 1	Homo sapiens	192-224
28225998-2	2017	Heparin and insulin activate lipoprotein lipase (LPL), thereby reducing plasma triglyceride levels.	Heparin	0-7	lipoprotein lipase	Homo sapiens	49-52
1922367-3	1991	We show here that the reactive centre of the serpins can adopt varying conformations and that mobility of the reactive centre is necessary for the function of antithrombin and its binding and activation by heparin; the identification of a new locked conformation explains the latent inactive state of PAI-1.	Heparin	206-213	serpin family C member 1	Homo sapiens	159-171
1917988-2	1991	We have found that heparin and other polyanions compete with photoactivated, phosphorylated rhodopsin to bind arrestin (48-kDa protein, S-antigen).	Heparin	19-26	S-antigen visual arrestin	Bos taurus	120-134
1917988-4	1991	When bound to arrestin, heparin also mimics phosphorylated rhodopsin by similarly exposing arrestin to limited proteolysis.	Heparin	24-31	rhodopsin	Bos taurus	59-68
1833592-7	1991	Despite this increased heparin consumption, the patients who had received heparin before operation demonstrated increased activation of coagulation at the end of cardiopulmonary bypass (thrombin-antithrombin III complex, 19 +/- 4.1 ng/ml in group M and 61 +/- 7 ng/ml in group Hsc, p less than 0.05; cross-linked fibrin fragments, 257 +/- 92 ng/ml in group M and 875 +/- 152 ng/ml in group Hiv, p less than 0.05).	Heparin	74-81	serpin family C member 1	Homo sapiens	195-211
1833592-7	1991	Despite this increased heparin consumption, the patients who had received heparin before operation demonstrated increased activation of coagulation at the end of cardiopulmonary bypass (thrombin-antithrombin III complex, 19 +/- 4.1 ng/ml in group M and 61 +/- 7 ng/ml in group Hsc, p less than 0.05; cross-linked fibrin fragments, 257 +/- 92 ng/ml in group M and 875 +/- 152 ng/ml in group Hiv, p less than 0.05).	Heparin	74-81	fucosyltransferase 1 (H blood group)	Homo sapiens	277-280
1833592-8	1991	Increased platelet activation was also found in patients with preoperative heparin therapy (beta-thromboglobulin at the end of cardiopulmonary bypass was 585 +/- 88 ng/ml in group M versus 1341 +/- 190 ng/ml in group Hsc, p less than 0.05).	Heparin	75-82	fucosyltransferase 1 (H blood group)	Homo sapiens	217-220
1763970-0	1991	Binding of antithrombin to immobilized heparin under varying flow conditions.	Heparin	39-46	serpin family C member 1	Homo sapiens	11-23
1763970-2	1991	In this study, the effects of flow-velocity/wall shear stress on the interaction of antithrombin (AT) with surface-immobilized heparin were investigated.	Heparin	127-134	serpin family C member 1	Homo sapiens	84-96
1763970-2	1991	In this study, the effects of flow-velocity/wall shear stress on the interaction of antithrombin (AT) with surface-immobilized heparin were investigated.	Heparin	127-134	serpin family C member 1	Homo sapiens	98-100
1763970-3	1991	The binding of AT to low-affinity and high-affinity heparin could be discriminated by measurements at physiological of elevated ionic strength.	Heparin	52-59	serpin family C member 1	Homo sapiens	15-17
1763970-4	1991	Under low shear stress conditions, substantial binding of AT to both high- and low-affinity heparin was observed, in relative quantities largely reflecting the proportion of these polysaccharide populations on the surface.	Heparin	92-99	serpin family C member 1	Homo sapiens	58-60
1763970-6	1991	Furthermore, under the highest shear stress (greater than 1,000 N/m2), the binding of AT to low-affinity heparin completely disappeared while binding to the high-affinity fraction persisted.	Heparin	105-112	serpin family C member 1	Homo sapiens	86-88
1800965-2	1991	The hypertriglyceridaemia was attributed to impaired clearance of triglyceride-rich lipoprotein particles secondary to heparin-induced reduction in the activity of the lipolytic enzyme, lipoprotein lipase.	Heparin	119-126	lipoprotein lipase	Homo sapiens	186-204
1935790-3	1991	Upon refeeding, the activity returned to control values in 48 h. In isolated livers from fed male rats, a sharp peak of hepatic endothelial lipase activity appeared in the perfusate upon heparin addition.	Heparin	187-194	lipase G, endothelial type	Rattus norvegicus	128-146
1955379-0	1991	Recombinant fusion polypeptide with cell- and heparin-binding domains of fibronectin inhibits liver metastasis of L5178Y-ML25 lymphoma cells.	Heparin	46-53	fibronectin 1	Mus musculus	73-84
27918140-3	2017	Binding to the polysaccharide heparin was found to induce the unfolding of preformed structural elements in OPN.	Heparin	30-37	secreted phosphoprotein 1	Homo sapiens	108-111
1780805-6	1991	Inhibition by heparin was restored by addition of increasing amounts of antithrombin (AT) to samples containing constant amounts of heparin, thrombin and 125I-r.hirudin and was not neutralized by protamine sulfate.	Heparin	14-21	serpin family C member 1	Homo sapiens	72-84
1780805-6	1991	Inhibition by heparin was restored by addition of increasing amounts of antithrombin (AT) to samples containing constant amounts of heparin, thrombin and 125I-r.hirudin and was not neutralized by protamine sulfate.	Heparin	132-139	serpin family C member 1	Homo sapiens	72-84
1723816-0	1991	Experimental evaluation of heparin-coated cardiopulmonary bypass equipment with low systemic heparinization and high-dose aprotinin.	Heparin	27-34	pancreatic trypsin inhibitor	Bos taurus	122-131
1665594-0	1991	Low molecular weight heparin-catalyzed inactivation of factor Xa and thrombin by antithrombin III--effect of platelet factor 4.	Heparin	21-28	serpin family C member 1	Homo sapiens	81-97
1665594-3	1991	Pseudo-first order rate constants of inactivation of factor Xa and thrombin by antithrombin III were determined as function of heparin concentration, in the presence of 4.0 mM CaCl2.	Heparin	127-134	serpin family C member 1	Homo sapiens	79-95
1885605-2	1991	This protein, designated HBp17, was found to bind the heparin-binding peptide growth factors HBGF-1 and HBGF-2 in a noncovalent, reversible manner.	Heparin	54-61	fibroblast growth factor binding protein 1	Homo sapiens	25-30
1885605-4	1991	Both the binding and inactivation of HBGF-1 and HBGF-2 by HBp17 were abolished by heparin.	Heparin	82-89	fibroblast growth factor binding protein 1	Homo sapiens	58-63
28168066-3	2017	We present a case of a woman with antithrombin (AT) deficiency who presented with a VTE despite therapeutic low molecular weight heparin (LMWH).	Heparin	129-136	serpin family C member 1	Homo sapiens	34-46
1897511-7	1991	Purified GAC possessed only 2% (W/W) of the antithrombin III cofactor activity of porcine heparin.	Heparin	90-97	serpin family C member 1	Homo sapiens	44-60
1958050-11	1991	Simultaneously drawn serum and heparin-plasma samples gave comparable myoglobin results.	Heparin	31-38	myoglobin	Homo sapiens	70-79
1875058-6	1991	Supernatants from melanocyte cultures stimulated with either IL-1 alpha or TNF alpha and separated on a heparin-Sepharose column became positive for neutrophil and monocyte chemotactic activity in a dose- and time-dependent fashion.	Heparin	104-111	interleukin 1 alpha	Homo sapiens	61-71
1747261-3	1991	Plasma Antithrombin III (ATIII) is one of the most important coagulation inhibitors and the fundamental enzyme for the therapeutical action of heparin.	Heparin	143-150	serpin family C member 1	Homo sapiens	7-23
27765766-0	2016	TULA-2 (T-Cell Ubiquitin Ligand-2) Inhibits the Platelet Fc Receptor for IgG IIA (FcgammaRIIA) Signaling Pathway and Heparin-Induced Thrombocytopenia in Mice.	Heparin	117-124	ubiquitin associated and SH3 domain containing, B	Mus musculus	0-6
1747261-3	1991	Plasma Antithrombin III (ATIII) is one of the most important coagulation inhibitors and the fundamental enzyme for the therapeutical action of heparin.	Heparin	143-150	serpin family C member 1	Homo sapiens	25-30
1747261-4	1991	In the last years it was well established that ATIII deficiency accounts for a thrombotic state and inefficiency of heparin therapy.	Heparin	116-123	serpin family C member 1	Homo sapiens	47-52
1715220-5	1991	Our results show that: (1) Heparin exclusively increases the rate of inhibition of thrombin by PAI-1, whereas in the presence of heparin the rate of inhibition of the other proteases is not altered; (2) Vitronectin is an obligatory cofactor for the inhibition of thrombin by PAI-1.	Heparin	27-34	serpin family E member 1	Homo sapiens	95-100
1840095-2	1991	Since adequate thromboembolism protection requires a cofactor AT III for heparin to provide full antithrombotic coverage, the preoperative AT III and protein C levels in the plasma of 105 patients treated with marcumar are measured.	Heparin	73-80	serpin family C member 1	Homo sapiens	62-68
1661447-0	1991	Standard heparin but not LMW heparin induces a concomitant increase of t-PA and PAI-1 without modification of global fibrinolysis: study after 60 days treatment.	Heparin	9-16	serpin family E member 1	Homo sapiens	80-85
1860682-0	1991	Antithrombin III supplementation reduces heparin requirement and platelet loss during hemodialysis of patients with fulminant hepatic failure.	Heparin	41-48	serpin family C member 1	Homo sapiens	0-16
1860682-2	1991	In this study, we have performed a controlled, randomized trial of antithrombin III supplementation on heparin activity, occurrence of bleeding and the platelet count and activation during hemodialysis in 24 patients with fulminant hepatic failure.	Heparin	103-110	serpin family C member 1	Homo sapiens	67-83
1860682-6	1991	Total heparin usage was significantly decreased by antithrombin III supplementation (median 5,200 U; range = 2,000 to 13,000) as compared with the control group (median 10,200 U; range = 5,000 to 16,500; p less than 0.005).	Heparin	6-13	serpin family C member 1	Homo sapiens	51-67
1860682-7	1991	Blood heparin level (antifactor Xa activity) after the initial bolus was significantly greater in the antithrombin III-supplemented subjects (0.40 +/- 0.07 U/ml compared with 0.22 +/- 0.05 U/ml in the control group; p less than 0.05).	Heparin	6-13	serpin family C member 1	Homo sapiens	102-118
27765766-0	2016	TULA-2 (T-Cell Ubiquitin Ligand-2) Inhibits the Platelet Fc Receptor for IgG IIA (FcgammaRIIA) Signaling Pathway and Heparin-Induced Thrombocytopenia in Mice.	Heparin	117-124	ubiquitin associated and SH3 domain containing, B	Mus musculus	8-33
1940520-8	1991	In patients with familial ATIII deficiency, 50% of normal ATIII activity can be expected because they are heterozygotes, so the cardio-pulmonary bypass should be run with special caution to the heparin dosage.	Heparin	194-201	serpin family C member 1	Homo sapiens	26-31
1875911-8	1991	Furthermore, the Ca2+ signals elicited by both bradykinin and epidermal growth factor were blocked in cells microinjected with the inositol 1,4,5-trisphosphate receptor antagonist heparin, whereas the intracellular Ca(2+)-ATPase inhibitor thapsigargin still mobilized Ca2+.	Heparin	180-187	epidermal growth factor	Homo sapiens	62-85
27765766-1	2016	OBJECTIVE: The objective of this study is to investigate the role of T-cell ubiquitin ligand-2 (TULA-2) in the platelet Fc receptor for IgG IIA (FcgammaRIIA) pathway and in the pathogenesis of heparin-induced thrombocytopenia (HIT).	Heparin	193-200	ubiquitin associated and SH3 domain containing, B	Mus musculus	69-94
27765766-1	2016	OBJECTIVE: The objective of this study is to investigate the role of T-cell ubiquitin ligand-2 (TULA-2) in the platelet Fc receptor for IgG IIA (FcgammaRIIA) pathway and in the pathogenesis of heparin-induced thrombocytopenia (HIT).	Heparin	193-200	ubiquitin associated and SH3 domain containing, B	Mus musculus	96-102
2070046-9	1991	Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly.	Heparin	15-22	serpin family C member 1	Homo sapiens	99-104
1712476-4	1991	We show that the phosphorylation of threonine residues in GST-TK8 by extracts of A431 cells is stimulated by heparin but not by EGF.	Heparin	109-116	glutathione S-transferase kappa 1	Homo sapiens	58-61
27765766-1	2016	OBJECTIVE: The objective of this study is to investigate the role of T-cell ubiquitin ligand-2 (TULA-2) in the platelet Fc receptor for IgG IIA (FcgammaRIIA) pathway and in the pathogenesis of heparin-induced thrombocytopenia (HIT).	Heparin	193-200	Fc receptor	Mus musculus	120-131
2070046-9	1991	Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly.	Heparin	57-64	serpin family C member 1	Homo sapiens	99-104
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	275-282	serpin family C member 1	Homo sapiens	81-93
1920862-6	1991	Management of high TAT began with the use of an anticoagulant such as heparin under the condition of sufficient ATIII level.	Heparin	70-77	serpin family C member 1	Homo sapiens	112-117
1712491-0	1991	Induction of mast cell proliferation, maturation, and heparin synthesis by the rat c-kit ligand, stem cell factor.	Heparin	54-61	KIT ligand	Rattus norvegicus	83-95
1712491-0	1991	Induction of mast cell proliferation, maturation, and heparin synthesis by the rat c-kit ligand, stem cell factor.	Heparin	54-61	KIT ligand	Rattus norvegicus	97-113
27681598-2	2016	The detailed mechanisms on how angiotensin is carried by l-ANT and how heparin binds l-ANT and mediates thrombin inhibition are unclear.	Heparin	71-78	solute carrier family 25 member 6	Homo sapiens	87-90
1711036-3	1991	CEase-LDL, in comparison to native LDL, was smaller in size, possessed fewer free lysine amino groups (by 14%), and demonstrated reduced binding to heparin (by 83%) and reduced immunoreactivity against monoclonal antibodies directed toward epitopes along the LDL apoB-100.	Heparin	148-155	carboxyl ester lipase	Homo sapiens	0-5
1892484-9	1991	LPL activities in the post-heparin plasma were decreased significantly from 2.53 +/- 0.71 mumol free fatty acids (FFA)/ml/h to 1.71 +/- 0.71 mumol FFA/ml/h by probucol while HTGL activities remained unchanged.	Heparin	27-34	lipoprotein lipase	Homo sapiens	0-3
2066426-2	1991	The heparin concentration and the incubation time in the assay were optimised specifically to permit the detection of heparin binding defects of antithrombin.	Heparin	4-11	serpin family C member 1	Homo sapiens	145-157
27681598-3	2016	Here we have solved the crystal structure of cleaved l-ANT at 2.7 A resolution and characterized its properties in heparin binding and protease inhibition.	Heparin	115-122	solute carrier family 25 member 6	Homo sapiens	55-58
2066426-2	1991	The heparin concentration and the incubation time in the assay were optimised specifically to permit the detection of heparin binding defects of antithrombin.	Heparin	118-125	serpin family C member 1	Homo sapiens	145-157
2066426-4	1991	Several commercially available assays recommend a longer incubation time than 30 seconds and therefore some patients with heparin binding defects of antithrombin may not be identified.	Heparin	122-129	serpin family C member 1	Homo sapiens	149-161
2066426-5	1991	The assay described here allows heparin binding variants of antithrombin to be identified and distinguished from other types of antithrombin deficiency in a simple two stage procedure.	Heparin	32-39	serpin family C member 1	Homo sapiens	60-72
27681598-5	2016	Heparin binds l-ANT tightly with a dissociation constant of ~10 nm involving ~8 monosaccharides and ~6 ionic interactions.	Heparin	0-7	solute carrier family 25 member 6	Homo sapiens	16-19
2029579-8	1991	Approximately 50% of the AT-III from the propositus isolated by heparin-Sepharose chromatography, when incubated with either human alpha-thrombin or factor Xa, did not form complex but was cleaved, presumably at the reactive center Arg393-Ser394.	Heparin	64-71	serpin family C member 1	Homo sapiens	25-31
2019790-1	1991	Three recent studies have reported that fibrin in solution significantly inhibits the ability of heparin to catalyze the inhibition of thrombin by antithrombin III.	Heparin	97-104	serpin family C member 1	Homo sapiens	147-163
2019790-4	1991	Because the results of these studies suggest that fibrin inhibits the reactivity of thrombin with antithrombin III-heparin but not with heparin cofactor II-dermatan sulfate, we compared the relative catalytic effects of heparin and dermatan sulfate on thrombin inhibition in plasma, both in the presence and absence of fibrin.	Heparin	115-122	serpin family C member 1	Homo sapiens	98-114
2033259-1	1991	Heparin, a polyion, exerts its main activity to inhibit coagulation through a serine protease inhibitor, antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	105-121
2026595-5	1991	One component, a fragment with a molecular mass of 110-150 kDa, was estimated to contain the central cell-binding domain and the carboxyl-terminal heparin-binding domain of the intact FN molecule.	Heparin	147-154	fibronectin 1	Rattus norvegicus	184-186
1708387-10	1991	In addition, these experiments indicate that Lp(a) may regulate fibrinolysis by competing with PAI-1 and plasminogen for fibrinogen- and heparin-bound t-PA.	Heparin	137-144	serpin family E member 1	Homo sapiens	95-100
27681598-7	2016	Although l-ANT by itself is a poor thrombin inhibitor with a second order rate constant of 500 m-1 s-1, its interaction with thrombin is accelerated 90-fold by high molecular weight heparin following a bell-shaped dose-dependent curve.	Heparin	182-189	solute carrier family 25 member 6	Homo sapiens	11-14
27681598-9	2016	Furthermore, an l-ANT mutant with the P1 Ile mutated to Arg inhibits thrombin nearly 1500-fold faster than the wild type, which is further accelerated by high molecular weight heparin.	Heparin	176-183	solute carrier family 25 member 6	Homo sapiens	18-21
2027669-2	1991	Only AT-III molecules with a low heparin affinity were detected in her plasma and these pathological AT-III molecules could not increase the rate of the thrombin-inactivation at all.	Heparin	33-40	serpin family C member 1	Homo sapiens	5-11
2031941-1	1991	A phospholipase A2 was purified from rabbit platelet cytosolic fraction to near homogeneity by sequential column chromatographies on heparin-Sepharose, DEAE-Sephacel, butyl-Toyopearl, DEAE-5PW ion-exchange HPLC, and TSK gel G3000SW gel-filtration HPLC.	Heparin	133-140	phospholipase A2	Oryctolagus cuniculus	2-18
27681598-10	2016	Taken together, these results suggest that heparin binds l-ANT at a conserved heparin binding site around helix D and promotes the interaction between l-ANT and thrombin through a template mechanism conserved in vertebrates.	Heparin	43-50	solute carrier family 25 member 6	Homo sapiens	59-62
27681598-10	2016	Taken together, these results suggest that heparin binds l-ANT at a conserved heparin binding site around helix D and promotes the interaction between l-ANT and thrombin through a template mechanism conserved in vertebrates.	Heparin	43-50	solute carrier family 25 member 6	Homo sapiens	153-156
2025651-3	1991	The reduction in LPL activity was most prominent in the heparin releasable pool; IL-1 treatment resulted in a 7.2-8.3-fold decrease in the functional compartment and a 2.5-2.8-fold decrease in residual cellular activity.	Heparin	56-63	lipoprotein lipase	Homo sapiens	17-20
2025651-3	1991	The reduction in LPL activity was most prominent in the heparin releasable pool; IL-1 treatment resulted in a 7.2-8.3-fold decrease in the functional compartment and a 2.5-2.8-fold decrease in residual cellular activity.	Heparin	56-63	interleukin 1 alpha	Homo sapiens	81-85
27681598-10	2016	Taken together, these results suggest that heparin binds l-ANT at a conserved heparin binding site around helix D and promotes the interaction between l-ANT and thrombin through a template mechanism conserved in vertebrates.	Heparin	78-85	solute carrier family 25 member 6	Homo sapiens	59-62
27322714-1	2016	BACKGROUND: Heparin fulfills its anticoagulant action through activation of antithrombin (AT), and thus thrombosis secondary to AT deficiency can be associated with heparin resistance.	Heparin	12-19	serpin family C member 1	Homo sapiens	76-88
2061622-7	1991	In adherent cell-depleted murine and human marrow cultures, the addition of B-FGF possessed synergistic activity in combination with the optimal concentration of GM-CSF for CFU-gm at a dose of 10 ng/ml which was inhibited in the presence of protamine sulfate (LD50 dose, 100 mu gm/ml), an inhibitor of B-FGF mitogenic activity, or in the presence of heparin (LD50 dose, 100 U/ml), an effective B-FGF binding agent.	Heparin	350-357	colony stimulating factor 2	Homo sapiens	162-168
1706335-6	1991	Both neutrophil and HL60 GMP-140 binding and platelet rosetting were strongly inhibited by heparin, fucoidin, and dextran sulfate 500,000, were partially inhibited by dextran sulfate 5,000 and lambda- and kappa-carrageenan, but were not inhibited by chondroitins 4- and 6-sulfate.	Heparin	91-98	selectin P	Homo sapiens	25-32
2057915-1	1991	Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose.	Heparin	311-318	serpin family C member 1	Homo sapiens	48-64
1893059-5	1991	If the XaI activity was corrected for the ATIII concentration, the heparin activities no longer differed significantly from zero.	Heparin	67-74	serpin family C member 1	Homo sapiens	42-47
1705837-5	1991	Cells growth with HBGF-1/heparin had both decreased surface and total TF activity as compared with HUVEC from the same endothelial cell pool grown without HBGF-1/heparin.	Heparin	25-32	coagulation factor III, tissue factor	Homo sapiens	70-72
27322714-1	2016	BACKGROUND: Heparin fulfills its anticoagulant action through activation of antithrombin (AT), and thus thrombosis secondary to AT deficiency can be associated with heparin resistance.	Heparin	165-172	serpin family C member 1	Homo sapiens	76-88
2013315-2	1991	The heparin affinity of normal and two P1 variants of antithrombin-III (AT) was studied by gradient elution with NaCl in Tris buffer on heparin-Sepharose.	Heparin	4-11	serpin family C member 1	Homo sapiens	54-70
27739168-3	2016	In this work, the protein transduction ability of a novel CPP (termed HBP) derived from the heparin-binding domain of HB-EGF was evaluated.	Heparin	92-99	heparin binding EGF like growth factor	Homo sapiens	118-124
1998643-1	1991	Heparin inhibits arterial smooth muscle cell (SMC) proliferation in vivo and in vitro; moreover, it reinduces the expression of alpha-smooth muscle (SM) actin (an accepted marker of SMC differentiation) in SMCs of the intimal thickening that develops after experimentally induced endothelial lesions.	Heparin	0-7	actin gamma 2, smooth muscle	Rattus norvegicus	128-158
1872461-1	1991	The identification of a specific required carbohydrate structure for the antithrombin III binding site on heparin suggests that there may be specific structures in glycosaminoglycan chains which are necessary for other vascular functions of these carbohydrates.	Heparin	106-113	serpin family C member 1	Homo sapiens	73-89
1706595-1	1991	This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis.	Heparin	116-123	serpin family C member 1	Homo sapiens	203-219
1706595-1	1991	This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis.	Heparin	146-153	serpin family C member 1	Homo sapiens	203-219
1988041-13	1991	These chemical studies established that the active site of human milk BAL is located at serine-194, the N-glycosylation site is present at asparagine-187, the O-glycosylation region is in the 16 repeating units near the C-terminus, and the heparin binding domain is in the N-terminal region.	Heparin	240-247	carboxyl ester lipase	Homo sapiens	70-73
1851740-7	1991	Dextran sulfate, dextran, and heparin inhibited the increase in MPO activity.	Heparin	30-37	myeloperoxidase	Cavia porcellus	64-67
1995647-7	1991	This recombinant ATIII protein was immunologically reactive with antisera raised against native human ATIII, formed stable complexes with thrombin, and was heparin-accelerated at the same concentration as native human ATIII.	Heparin	156-163	serpin family C member 1	Homo sapiens	17-22
1995647-8	1991	In addition, the recombinant ATIII retained specificity for the same molecular species of heparin that activates authentic human ATIII.	Heparin	90-97	serpin family C member 1	Homo sapiens	29-34
1995647-8	1991	In addition, the recombinant ATIII retained specificity for the same molecular species of heparin that activates authentic human ATIII.	Heparin	90-97	serpin family C member 1	Homo sapiens	129-134
27780200-2	2016	NHBA binds heparin through a conserved Arg-rich region that is the target of two proteases, the meningococcal NalP and human lactoferrin (hLf).	Heparin	11-18	HLF transcription factor, PAR bZIP family member	Homo sapiens	138-141
1998743-6	1991	Measured in post-heparin plasma, the activity of lipoprotein lipase was decreased in WHHL rabbits, but this was not associated with clear evidence of defective lipolysis of emulsion triolein.	Heparin	17-24	lipoprotein lipase	Oryctolagus cuniculus	49-67
1989599-1	1991	An intracellular form of phospholipase A2 was purified about 47,500-fold to near homogeneity from bovine platelets 100,000 x g supernatant by sequential use of column chromatographies on Heparin-Sepharose, DEAE-Sephacel, Butyl-Toyopearl, Sephacryl S-300, DEAE-5PW HPLC, TSK G 3000 SW HPLC and Mono Q FPLC.	Heparin	187-194	LOC104974671	Bos taurus	25-41
2064235-0	1991	Eglin C and heparin inhibition of platelet activation induced by cathepsin G or human neutrophils.	Heparin	12-19	cathepsin G	Homo sapiens	65-76
27602496-0	2016	Heparins that block VEGF-A-mediated von Willebrand factor fiber generation are potent inhibitors of hematogenous but not lymphatic metastasis.	Heparin	0-8	Von Willebrand factor	Mus musculus	36-57
1789731-5	1991	Detachability of membrane-bound acrosin inhibitors was increased with significance, following in-vitro capacitation of bull sperma under heparin action.	Heparin	137-144	acrosin	Homo sapiens	32-39
2035830-4	1991	The application of these new QAC developments is illustrated by the determination of binding constants for the interactions of high-affinity heparin (Mr 20,300) with antithrombin III at three temperatures.	Heparin	141-148	serpin family C member 1	Homo sapiens	166-182
1848441-8	1991	The anti Xa activity peak seen after adding AT III to plasma was much higher with heparin than with enoxaparin.	Heparin	82-89	serpin family C member 1	Homo sapiens	44-50
27602496-5	2016	Unlike the anticoagulant Fondaparinux, an inhibitor of thrombin generation, the low-molecular-weight heparin (LMWH) Tinzaparin inhibited VWF fiber formation and vessel occlusion in tumor vessels by blocking thrombin-induced EC activation and vascular endothelial growth factor-A (VEGF-A)-mediated VWF release.	Heparin	101-108	Von Willebrand factor	Mus musculus	137-140
1848441-9	1991	In urine, biological activities, measured with AT III supplementation, were higher with enoxaparin than with heparin.	Heparin	109-116	serpin family C member 1	Homo sapiens	47-53
27602496-5	2016	Unlike the anticoagulant Fondaparinux, an inhibitor of thrombin generation, the low-molecular-weight heparin (LMWH) Tinzaparin inhibited VWF fiber formation and vessel occlusion in tumor vessels by blocking thrombin-induced EC activation and vascular endothelial growth factor-A (VEGF-A)-mediated VWF release.	Heparin	101-108	Von Willebrand factor	Mus musculus	297-300
1703436-0	1991	Functional interaction of plasminogen activator inhibitor type 1 (PAI-1) and heparin.	Heparin	77-84	serpin family E member 1	Homo sapiens	26-64
1703436-3	1991	Recently, it has been demonstrated that the PAI-1-binding site on vitronectin is adjacent to a heparin-binding site (Preissner et al., 1990).	Heparin	95-102	serpin family E member 1	Homo sapiens	44-49
2019613-1	1991	Poly(sodium vinyl sulfonate) (PVS) was found to be 1/14 times as active as heparin in inducing the conformational change and activation of antithrombin III.	Heparin	75-82	serpin family C member 1	Homo sapiens	139-155
2019613-3	1991	It was evident in the experiment using 2,4,6-trinitrobenzene sulfonate that PVS elicited the activity of antithrombin III by interacting with amino groups of the protein as does heparin.	Heparin	178-185	serpin family C member 1	Homo sapiens	105-121
1703436-4	1991	Furthermore, it can be deduced that the amino acid residues, proposed to mediate heparin binding in the serpins antithrombin III and heparin cofactor II, are conserved in PAI-1.	Heparin	81-88	serpin family C member 1	Homo sapiens	112-128
1846019-5	1991	Heparin"s inhibition of growth of HepG2 cells correlated with changes in the mRNA synthesis and abundance of insulinlike growth factor II (IGF II) and transforming growth factor beta (TGF beta).	Heparin	0-7	insulin like growth factor 2	Homo sapiens	109-137
27342999-7	2016	Furthermore, majority of the LPL in the pre-heparin plasma was found in the RLP as inactive form, with broadly diffused lipoprotein profiles in the presence and absence of THL.	Heparin	44-51	lipoprotein lipase	Homo sapiens	29-32
1846019-5	1991	Heparin"s inhibition of growth of HepG2 cells correlated with changes in the mRNA synthesis and abundance of insulinlike growth factor II (IGF II) and transforming growth factor beta (TGF beta).	Heparin	0-7	insulin like growth factor 2	Homo sapiens	139-145
1846019-8	1991	Transcriptionally, IGF II was regulated by the additive effects of insulin, glucagon, and growth hormone in combination with heparin; TGF beta was regulated primarily by the synergistic effects of insulin and growth hormone in combination with heparin.	Heparin	125-132	insulin like growth factor 2	Homo sapiens	19-25
1846019-10	1991	Heparin induction of all IGF II transcripts was also dependent on triiodotyronine and prolactin, but it is unknown whether their induction by heparin was via transcriptional or posttranscriptional mechanisms.	Heparin	0-7	insulin like growth factor 2	Homo sapiens	25-31
1703436-4	1991	Furthermore, it can be deduced that the amino acid residues, proposed to mediate heparin binding in the serpins antithrombin III and heparin cofactor II, are conserved in PAI-1.	Heparin	81-88	serpin family E member 1	Homo sapiens	171-176
1703436-6	1991	At pH 7.4, PAI-1 quantitatively binds to heparin-Sepharose and can be eluted with increasing [NaCl].	Heparin	41-48	serpin family E member 1	Homo sapiens	11-16
1703436-7	1991	Binding of PAI-1 to heparin-Sepharose can be efficiently competed with heparin in solution (IC50, 7 microM).	Heparin	20-27	serpin family E member 1	Homo sapiens	11-16
1703436-7	1991	Binding of PAI-1 to heparin-Sepharose can be efficiently competed with heparin in solution (IC50, 7 microM).	Heparin	71-78	serpin family E member 1	Homo sapiens	11-16
1703436-8	1991	In the presence of heparin, the protease specificity of PAI-1 toward thrombin is substantially increased.	Heparin	19-26	serpin family E member 1	Homo sapiens	56-61
1703436-9	1991	This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin.	Heparin	80-87	serpin family E member 1	Homo sapiens	55-60
1703436-9	1991	This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin.	Heparin	80-87	serpin family E member 1	Homo sapiens	169-174
1703436-9	1991	This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin.	Heparin	178-185	serpin family E member 1	Homo sapiens	55-60
1794751-0	1991	Heparin requires both antithrombin and extrinsic pathway inhibitor for its anticoagulant effect in human blood.	Heparin	0-7	serpin family C member 1	Homo sapiens	22-34
1650391-3	1991	The interest raised by low molecular weight heparins (LMWH), prepared as early as 1970, was based on a concept that is currently called into question: their anti-Xa activity, accounting for the antithrombotic activity, is high, while the anti-IIa (antithrombin) activity, producing the hemorrhagic risks, is lower.	Heparin	44-52	serpin family C member 1	Homo sapiens	248-260
2049431-6	1991	We conclude that the intraperitoneal administration of heparin at these doses is effective in preventing fibrin precipitation when intraperitoneal AT-III levels are expected to be relatively increased such as at the start of CAPD or in the presence of peritonitis.	Heparin	55-62	serpin family C member 1	Homo sapiens	147-153
2229057-0	1990	Important role of arginine 129 in heparin-binding site of antithrombin III.	Heparin	34-41	serpin family C member 1	Homo sapiens	58-74
2229057-4	1990	This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding.	Heparin	209-216	serpin family C member 1	Homo sapiens	31-36
2229057-6	1990	High affinity (for ATIII) heparin had only a minimal effect on thrombin and activated factor X inhibition by the purified abnormal ATIII.	Heparin	26-33	serpin family C member 1	Homo sapiens	19-24
2229057-7	1990	Taken together, these results demonstrate an important role for Arg-129 in the binding and interaction of ATIII with heparin of high affinity.	Heparin	117-124	serpin family C member 1	Homo sapiens	106-111
27412396-1	2016	In the absence of specific antidote to fondaparinux, two modified forms of antithrombin (AT), one recombinant inactive (ri-AT) and the other chemically inactivated (chi-AT), were designed to antagonise AT-mediated anticoagulants, e. g. heparins or fondaparinux.	Heparin	236-244	serpin family C member 1	Homo sapiens	75-87
2241151-9	1990	The brain HSP90 was separable from glucocorticoid receptor by heparin-agarose and DNA-cellulose columns.	Heparin	62-69	heat shock protein 90 alpha family class A member 1	Homo sapiens	10-15
1829853-5	1991	The inhibitory activity of the normal hemostatic process produced by heparin and its products could be reversed either by ATP or myosin.	Heparin	69-76	myosin heavy chain 14	Homo sapiens	129-135
2089037-5	1990	When this soluble fraction was subjected to heparin-Sepharose column chromatography, phospholipase A2 activity was detected in both heparin-binding and heparin-non-binding fractions.	Heparin	44-51	phospholipase A2	Oryctolagus cuniculus	85-101
2089037-5	1990	When this soluble fraction was subjected to heparin-Sepharose column chromatography, phospholipase A2 activity was detected in both heparin-binding and heparin-non-binding fractions.	Heparin	132-139	phospholipase A2	Oryctolagus cuniculus	85-101
2089037-5	1990	When this soluble fraction was subjected to heparin-Sepharose column chromatography, phospholipase A2 activity was detected in both heparin-binding and heparin-non-binding fractions.	Heparin	132-139	phospholipase A2	Oryctolagus cuniculus	85-101
2089037-9	1990	The heparin-non-binding phospholipase A2 hydrolyzed a phospholipid bearing an arachidonoyl residue at the sn-2 position more effectively than one with a linoleoyl residue.	Heparin	4-11	phospholipase A2	Oryctolagus cuniculus	24-40
33465876-2	2016	Heparin mimetic peptide nanofibers can bind to and enhance production and activity of major angiogenic growth factors, including VEGF.	Heparin	0-7	vascular endothelial growth factor A	Rattus norvegicus	129-133
2128972-5	1990	Heparin and pentosan polysulfate did not stimulate PAI-1 production by HOMC, while phorbol 12-myristate 13-acetate (100 nM) increased the concentration of PAI-1 in the conditioned medium by 2.6-fold over 24 h. The interaction of heparin with HOMC was studied by direct binding experiments.	Heparin	229-236	serpin family E member 1	Homo sapiens	155-160
2226466-4	1990	We determined the concentrations of each of heparin, dermatan sulfate and a pentasaccharide with high affinity for antithrombin III, to delay intrinsic prothrombin activation for at least 15s.	Heparin	44-51	serpin family C member 1	Homo sapiens	115-131
2248954-3	1990	The 10,000-fold rate enhancement elicited by the addition of heparin to the antithrombin III inhibition reaction, however, is the same.	Heparin	61-68	serpin family C member 1	Homo sapiens	76-92
27322195-0	2016	Heparanase Activates Antithrombin through the Binding to Its Heparin Binding Site.	Heparin	61-68	serpin family C member 1	Homo sapiens	21-33
1698787-12	1990	Ligand binding of rPAI-1 to nitrocellulose replicas from sodium dodecyl sulfate-polyacrylamide gels containing electrophoretically separated peptides from VN digests documented the association of PAI-1 with Mr = 10,000-20,000 fragments originating from the heparin-binding domain of VN.	Heparin	257-264	serpin family E member 1	Homo sapiens	19-24
1964634-2	1990	Heparin is only effective as an anticoagulant in the presence of a plasma protein termed antithrombin III, with which it forms a complex.	Heparin	0-7	serpin family C member 1	Homo sapiens	89-105
1699533-0	1990	Effect of heparin on the binding affinity of acidic FGF for the cloned human FGF receptors, flg and bek.	Heparin	10-17	filaggrin	Homo sapiens	92-95
27322195-4	2016	Trying to check the effect of heparanase on heparin, a highly sulphated glycosaminoglycan, when it activates antithrombin, our results demonstrated that heparanase, but not proheparanase, interacted directly with antithrombin in a non-covalent manner.	Heparin	44-51	serpin family C member 1	Homo sapiens	109-121
1699533-2	1990	We report that heparin increases the binding affinity of aFGF for the two cloned and overexpressed human FGF receptors, flg and bek, by 2-3 fold.	Heparin	15-22	filaggrin	Homo sapiens	120-123
1964634-3	1990	High- and low-affinity heparin are 2 types that readily bind or do not bind, respectively, to antithrombin III.	Heparin	23-30	serpin family C member 1	Homo sapiens	94-110
27322195-7	2016	Heparanase bound to the heparin binding site of antithrombin as the activation of Pro41Leu, Arg47Cys, Lys114Ala and Lys125Alaantithrombin mutants was impaired when it was compared to wild type antithrombin.	Heparin	24-31	serpin family C member 1	Homo sapiens	48-60
27322195-7	2016	Heparanase bound to the heparin binding site of antithrombin as the activation of Pro41Leu, Arg47Cys, Lys114Ala and Lys125Alaantithrombin mutants was impaired when it was compared to wild type antithrombin.	Heparin	24-31	serpin family C member 1	Homo sapiens	125-137
27322195-8	2016	Intrinsic fluorescence analysis showed that heparanase induced an activating conformational change in antithrombin similar to that induced by heparin and with a KD of 18.81 pM.	Heparin	142-149	serpin family C member 1	Homo sapiens	102-114
2145148-5	1990	p53 (serine 389) kinase activity was detected on lysates of SV3T3 cells; this activity co-purified with casein kinase II on phosphocellulose and Mono Q columns and was inhibited by heparin.	Heparin	181-188	transformation related protein 53, pseudogene	Mus musculus	0-3
2228024-9	1990	Heparin with a high affinity for antithrombin III (anti-coagulant heparin; HAH) inhibited IL-1 generation, whereas low-affinity heparin (non-anticoagulant; LAH) had no effect.	Heparin	0-7	antithrombin-III	Cavia porcellus	33-49
2228024-9	1990	Heparin with a high affinity for antithrombin III (anti-coagulant heparin; HAH) inhibited IL-1 generation, whereas low-affinity heparin (non-anticoagulant; LAH) had no effect.	Heparin	66-73	antithrombin-III	Cavia porcellus	33-49
2207328-6	1990	Heparin-Sepharose chromatography resulted in the elution of cell-free derived AT-III as a broad peak between 0.2 and 0.7 mol/L NaCl.	Heparin	0-7	serpin family C member 1	Homo sapiens	78-84
2282507-4	1990	Sulfated glycosaminoglycans as heparan sulfate and heparin extracted the asymmetric AChE from the synaptic basal lamina.	Heparin	51-58	acetylcholinesterase	Rattus norvegicus	84-88
2282507-5	1990	Here we show that dermatan sulfate as well as de-sulfated heparin, are also able to extract collagen-tailed AChE.	Heparin	58-65	acetylcholinesterase	Rattus norvegicus	108-112
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	20-27	serpin family C member 1	Homo sapiens	231-237
27148674-3	2016	Heparin activates antithrombin and promotes the inactivation of thrombin and other target proteinases.	Heparin	0-7	serpin family C member 1	Homo sapiens	18-30
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	103-110	serpin family C member 1	Homo sapiens	231-237
1962909-0	1990	Comparative studies of heparin cofactor activity toward antithrombin III and heparin cofactor II, and antithrombin III affinity between low molecular weight heparin and unfractionated heparin.	Heparin	23-30	serpin family C member 1	Homo sapiens	56-68
1962909-0	1990	Comparative studies of heparin cofactor activity toward antithrombin III and heparin cofactor II, and antithrombin III affinity between low molecular weight heparin and unfractionated heparin.	Heparin	23-30	serpin family C member 1	Homo sapiens	56-72
1962909-1	1990	The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system.	Heparin	61-69	serpin family C member 1	Homo sapiens	96-102
2175954-2	1990	ATIII-dependent production of PGI2 was abolished by addition of heparin, but pretreatment of HUVEC with polyclonal antibody against thrombomodulin could not prevent the PGI2 productions by ATIII and thrombin.	Heparin	64-71	serpin family C member 1	Homo sapiens	0-5
2246830-4	1990	In recent reports, pregnant women with hereditary AT-III deficiency had been treated with heparin or warfarin except for during abortion and delivery, in which time AT-III concentrate was widely utilized.	Heparin	90-97	serpin family C member 1	Homo sapiens	50-56
27252904-12	2016	CONCLUSIONS: Low-dose heparin infusion compared to subcutaneous heparin can decrease the plasma PAI-1 and urinary NGAL levels more rapidly.	Heparin	22-29	serpin family E member 1	Homo sapiens	96-101
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Heparin	191-198	serpin family C member 1	Homo sapiens	6-22
2390061-1	1990	Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor.	Heparin	191-198	serpin family C member 1	Homo sapiens	24-30
2387848-0	1990	Modulation of haptotactic migration of metastatic melanoma cells by the interaction between heparin and heparin-binding domain of fibronectin.	Heparin	92-99	fibronectin 1	Mus musculus	130-141
2387848-0	1990	Modulation of haptotactic migration of metastatic melanoma cells by the interaction between heparin and heparin-binding domain of fibronectin.	Heparin	104-111	fibronectin 1	Mus musculus	130-141
2387848-4	1990	At the same time, heparin or two monoclonal antibodies against the heparin-binding domain were able to inhibit the haptotactic migration to CH-271 or fibronectin, though not to C-274 or a mixture of C-274 and H-271.	Heparin	18-25	fibronectin 1	Mus musculus	150-161
2387848-6	1990	It seems likely that the regulatory mechanism may depend on interaction between heparin-like molecules on the cell surface and the heparin-binding domain in fibronectin, rather than on simple steric hindrance or on the masking of the cell-binding domain caused by the binding of heparin to heparin-binding domain.	Heparin	80-87	fibronectin 1	Mus musculus	157-168
2237824-0	1990	Ability of high-affinity heparin fractions with decreasing affinity for antithrombin III to activate ATIII isoforms.	Heparin	25-32	serpin family C member 1	Homo sapiens	72-88
2237824-0	1990	Ability of high-affinity heparin fractions with decreasing affinity for antithrombin III to activate ATIII isoforms.	Heparin	25-32	serpin family C member 1	Homo sapiens	101-106
27252904-12	2016	CONCLUSIONS: Low-dose heparin infusion compared to subcutaneous heparin can decrease the plasma PAI-1 and urinary NGAL levels more rapidly.	Heparin	64-71	serpin family E member 1	Homo sapiens	96-101
2237824-1	1990	Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin.	Heparin	44-51	serpin family C member 1	Homo sapiens	121-137
2237824-1	1990	Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin.	Heparin	44-51	serpin family C member 1	Homo sapiens	139-144
2387848-6	1990	It seems likely that the regulatory mechanism may depend on interaction between heparin-like molecules on the cell surface and the heparin-binding domain in fibronectin, rather than on simple steric hindrance or on the masking of the cell-binding domain caused by the binding of heparin to heparin-binding domain.	Heparin	131-138	fibronectin 1	Mus musculus	157-168
2387848-6	1990	It seems likely that the regulatory mechanism may depend on interaction between heparin-like molecules on the cell surface and the heparin-binding domain in fibronectin, rather than on simple steric hindrance or on the masking of the cell-binding domain caused by the binding of heparin to heparin-binding domain.	Heparin	131-138	fibronectin 1	Mus musculus	157-168
2387848-6	1990	It seems likely that the regulatory mechanism may depend on interaction between heparin-like molecules on the cell surface and the heparin-binding domain in fibronectin, rather than on simple steric hindrance or on the masking of the cell-binding domain caused by the binding of heparin to heparin-binding domain.	Heparin	131-138	fibronectin 1	Mus musculus	157-168
2237824-1	1990	Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin.	Heparin	181-188	serpin family C member 1	Homo sapiens	121-137
2237824-1	1990	Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin.	Heparin	181-188	serpin family C member 1	Homo sapiens	139-144
2237824-2	1990	Heparin with low-affinity for ATIII increased the rate of thrombin inhibition by the higher affinity isoform about 10-fold more effectively than by the other isoform.	Heparin	0-7	serpin family C member 1	Homo sapiens	30-35
2397213-4	1990	18, 135-147] was used to characterize high-affinity heparin binding fragments of the laminin "A" chain.	Heparin	52-59	laminin, alpha 1	Mus musculus	85-102
2165828-9	1990	The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL).	Heparin	30-37	serpin family C member 1	Homo sapiens	85-101
2165828-9	1990	The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL).	Heparin	52-59	serpin family C member 1	Homo sapiens	85-101
27018672-2	2016	Decellularized adipose tissues were heparin crosslinked and loaded with basic fibroblast growth factor (bFGF).	Heparin	36-43	WD and tetratricopeptide repeats 1	Mus musculus	15-22
2280186-4	1990	Unmasking of LPL activity occurred upon dilution: the higher the concentration of LPL, the higher were the dilution factor and the concentration of heparin required to reach a plateau of activity.	Heparin	148-155	lipoprotein lipase	Homo sapiens	13-16
2280186-4	1990	Unmasking of LPL activity occurred upon dilution: the higher the concentration of LPL, the higher were the dilution factor and the concentration of heparin required to reach a plateau of activity.	Heparin	148-155	lipoprotein lipase	Homo sapiens	82-85
2394942-0	1990	The importance of anti-factor Xa and antithrombin activities of low molecular weight heparins.	Heparin	85-93	serpin family C member 1	Homo sapiens	37-49
2237157-4	1990	However, pregnancy may be envisaged without risk since there has been an improvement in knowledge concerning the physiology of the AT III molecule, its exact role in coagulation, the application of accurate laboratory tests which measure the deficiency, and especially the programming of pregnancy under cover of preventive treatment consisting of the perfusion of AT III concentrate in association with heparin.	Heparin	404-411	serpin family C member 1	Homo sapiens	131-137
2112878-0	1990	Intravenous nitroglycerin-induced heparin resistance: a qualitative antithrombin III abnormality.	Heparin	34-41	serpin family C member 1	Homo sapiens	68-84
1700488-2	1990	Heparin enhanced the reaction of antithrombin III (AT) with plasmin (up to 40-fold with 20 units/ml).	Heparin	0-7	serpin family C member 1	Homo sapiens	33-49
26769965-9	2016	Knockdown of transmembrane protein 184A (TMEM184A) confirmed its involvement in heparin-induced signaling as seen in VSMCs.	Heparin	80-87	transmembrane protein 184A	Homo sapiens	13-39
1700488-6	1990	Heparin did not affect the rank-order of miniplasmin-inhibitory activity; it remained alpha 2M greater than alpha 2AP greater than AT.	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	86-94
26769965-9	2016	Knockdown of transmembrane protein 184A (TMEM184A) confirmed its involvement in heparin-induced signaling as seen in VSMCs.	Heparin	80-87	transmembrane protein 184A	Homo sapiens	41-49
2176902-3	1990	The mechanism by which such high affinity heparin acts when antithrombin III is the inhibitor is promotion of the formation of an intermediate proteinase-heparin-antithrombin complex.	Heparin	42-49	serpin family C member 1	Homo sapiens	60-76
1966669-2	1990	10 IU/ml heparin (90 micrograms/ml) brought about a significant (20-fold) increase in intracellular tPA levels over the 6-day culture period; intracellular PAI-1 levels were significantly decreased (by 60-70%) and culture growth rate promoted.	Heparin	9-16	serpin family E member 1	Homo sapiens	156-161
2176902-6	1990	Binding of heparin to both thrombin and antithrombin III interferes with thrombin inactivation.	Heparin	11-18	serpin family C member 1	Homo sapiens	40-56
26769966-0	2016	Transmembrane Protein 184A Is a Receptor Required for Vascular Smooth Muscle Cell Responses to Heparin.	Heparin	95-102	transmembrane protein 184A	Homo sapiens	0-26
2176902-8	1990	Low ionic strength in in vitro reactions also results in cleavage of antithrombin III by thrombin in the presence of heparin and effectively converts antithrombin III from an inhibitor to a substrate.	Heparin	117-124	serpin family C member 1	Homo sapiens	69-85
26769966-7	2016	A GFP-TMEM184A construct was employed to determine colocalization with heparin after endocytosis.	Heparin	71-78	transmembrane protein 184A	Homo sapiens	6-14
26769966-8	2016	Knockdown of TMEM184A eliminated the physiological responses to heparin, including effects on ERK pathway activity and BrdU incorporation.	Heparin	64-71	transmembrane protein 184A	Homo sapiens	13-21
26769966-9	2016	Isolated GFP-TMEM184A binds heparin, and overexpression results in additional heparin uptake.	Heparin	28-35	transmembrane protein 184A	Homo sapiens	13-21
2191783-14	1990	In a randomized, placebo-controlled double-blinded study, we will determine whether simultaneous administration of warfarin with heparin initiation provides more time to increase antithrombin III levels and prevent coronary reocclusion upon heparin discontinuance, compared to heparin without warfarin therapy.	Heparin	129-136	serpin family C member 1	Homo sapiens	179-195
26769966-9	2016	Isolated GFP-TMEM184A binds heparin, and overexpression results in additional heparin uptake.	Heparin	78-85	transmembrane protein 184A	Homo sapiens	13-21
2115815-3	1990	Two of the nine urticaria subjects had only a minimal rise in plasma DAO activity after heparin, three had a response which was at the lower end of the normal range, and four were normal.	Heparin	88-95	D-amino acid oxidase	Homo sapiens	69-72
27192836-5	2016	sulfates by heparinase I/III as well as treatment of cells with heparin lead to an abrupt reduction in the expression level of Hsp90 isoforms.	Heparin	12-19	heat shock protein 90 alpha family class A member 1	Homo sapiens	127-132
2115815-4	1990	In four out of five cases in which jejunal biopsy activity was obtained, there was concordance between mucosal DAO activity and the post-heparin plasma DAO response.	Heparin	137-144	D-amino acid oxidase	Homo sapiens	152-155
2169656-0	1990	Protein C inhibitor and other components of the protein C pathway in patients with acute deep vein thrombosis during heparin treatment.	Heparin	117-124	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	48-57
2169656-3	1990	In contrast, antithrombin III decreased progressively 25% during 5 days of heparin treatment.	Heparin	75-82	serpin family C member 1	Homo sapiens	13-29
2347543-4	1990	The activity of LpL in post-heparin plasma was positively correlated with changes in plasma HDL-C (r = 0.668, P less than 0.001) and HDL2b (r = 0.457, P less than 0.001), and negatively with plasma triglycerides (r = -0.546, P less than 0.001).	Heparin	28-35	lipoprotein lipase	Homo sapiens	16-19
2320065-6	1990	After weight loss, the level of heparin-releasable lipoprotein lipase activity increased in all patients, from 3.8 +/- 1.1 to 7.1 +/- 1.6 neq of free fatty acid released per minute per 10(6) cells (P less than 0.05).	Heparin	32-39	lipoprotein lipase	Homo sapiens	51-69
26758598-8	2016	The utility of this approach is demonstrated for tetrasaccharide SEC fractions of the low molecular weight heparin drug enoxaparin facilitating the isolation and characterization of an unsaturated 3-O-sulfated tetrasaccharide containing a portion of the antithrombin-III binding sequence.	Heparin	107-114	serpin family C member 1	Homo sapiens	254-270
2363123-4	1990	The abnormal AT III was characterized in plasma by the discrepancy between a normal progressive activity and a reduced heparin cofactor activity.	Heparin	119-126	serpin family C member 1	Homo sapiens	13-19
2363123-5	1990	This variant AT III was purified, separated from the normal protein by heparin-Sepharose chromatography and was eluted with increased NaCl concentrations.	Heparin	71-78	serpin family C member 1	Homo sapiens	13-19
2363123-6	1990	At pH 7.4, the variant AT III eluted at lower (0.3 to 0.5 M) NaCl concentrations than normal (1 to 1.5 M) AT III, thus demonstrating a decreased affinity for heparin.	Heparin	158-165	serpin family C member 1	Homo sapiens	23-29
2363123-7	1990	At pH 6.0, however, the abnormal molecule bound more avidly to heparin-Sepharose and was eluted like normal AT III at pH 7.4.	Heparin	63-70	serpin family C member 1	Homo sapiens	108-114
2363123-8	1990	Similarly, the heparin enhancement of intrinsic fluorescence of the variant AT III, markedly reduced at pH 7.4, was normalized at pH 6.0.	Heparin	15-22	serpin family C member 1	Homo sapiens	76-82
2110364-3	1990	Analysis of the patient"s post-heparin plasma by heparin-Sepharose affinity chromatography demonstrated that the mutant LPL had an altered affinity for heparin.	Heparin	31-38	lipoprotein lipase	Homo sapiens	120-123
2110364-3	1990	Analysis of the patient"s post-heparin plasma by heparin-Sepharose affinity chromatography demonstrated that the mutant LPL had an altered affinity for heparin.	Heparin	49-56	lipoprotein lipase	Homo sapiens	120-123
2110364-3	1990	Analysis of the patient"s post-heparin plasma by heparin-Sepharose affinity chromatography demonstrated that the mutant LPL had an altered affinity for heparin.	Heparin	49-56	lipoprotein lipase	Homo sapiens	120-123
2110364-9	1990	The identification of this mutation in the LPL gene defines a region of the LPL enzyme, at Ala-176, that is essential for normal heparin-binding and catalytic activity.	Heparin	129-136	lipoprotein lipase	Homo sapiens	43-46
2110364-9	1990	The identification of this mutation in the LPL gene defines a region of the LPL enzyme, at Ala-176, that is essential for normal heparin-binding and catalytic activity.	Heparin	129-136	lipoprotein lipase	Homo sapiens	76-79
2106684-6	1990	Both fractions of heparin effectively accelerate inactivation of thrombin by antithrombin III.	Heparin	18-25	serpin family C member 1	Homo sapiens	77-93
2339364-0	1990	Phosphotungstate as a useful eluent for antithrombin III purification by heparin-agarose affinity chromatography.	Heparin	73-80	serpin family C member 1	Homo sapiens	40-56
2339364-2	1990	In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography.	Heparin	99-106	serpin family C member 1	Homo sapiens	71-87
2138609-5	1990	The rHCII was expressed in Escherichia coli and partially purified by heparin-Sepharose chromatography.	Heparin	70-77	serpin family D member 1	Rattus norvegicus	4-9
2138609-9	1990	Heparin was less effective than dermatan sulfate in stimulating both forms of rHCII.	Heparin	0-7	serpin family D member 1	Rattus norvegicus	78-83
26553458-6	2016	Lower baseline antithrombin activity was associated with lower postheparin anti-Xa activity (EST [SE]: +0.47 (0.19) U/mL per 100 U/kg heparin; P = .01) and higher heparin doses during surgery (EST [SE]: +51 (17) U/kg per hour; P = .003).	Heparin	67-74	serpin family C member 1	Homo sapiens	15-27
2191809-2	1990	The anticoagulant agent heparin inhibits thrombosis by interacting with antithrombin III.	Heparin	24-31	serpin family C member 1	Homo sapiens	72-88
2339364-2	1990	In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography.	Heparin	99-106	serpin family C member 1	Homo sapiens	89-94
2339364-3	1990	Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M.	Heparin	28-35	serpin family C member 1	Homo sapiens	6-11
2339367-3	1990	The AT-III deficient plasma is prepared by passage of plasma through a heparin-agarose column.	Heparin	71-78	serpin family C member 1	Homo sapiens	4-10
2339367-4	1990	In the presence of heparin, AT-III in the sample shows concentration dependent anticoagulant activity and calibration curve is linear on semi-logarithmic graph paper.	Heparin	19-26	serpin family C member 1	Homo sapiens	28-34
26553458-6	2016	Lower baseline antithrombin activity was associated with lower postheparin anti-Xa activity (EST [SE]: +0.47 (0.19) U/mL per 100 U/kg heparin; P = .01) and higher heparin doses during surgery (EST [SE]: +51 (17) U/kg per hour; P = .003).	Heparin	134-141	serpin family C member 1	Homo sapiens	15-27
26553458-9	2016	CONCLUSIONS: Low circulating antithrombin activity is associated with lower heparin efficacy, which ultimately leads to a lower ability to suppress thrombin generation during CPB.	Heparin	76-83	serpin family C member 1	Homo sapiens	29-41
2106346-0	1990	Sex- and age-related variations in the in vitro heparin-releasable lipoprotein lipase from mononuclear leukocytes in blood.	Heparin	48-55	lipoprotein lipase	Homo sapiens	67-85
2197226-7	1990	In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin dose required might cause an unacceptable bleeding risk, e.g. in simultaneous thrombocytopenia.	Heparin	122-129	serpin family C member 1	Homo sapiens	46-62
2197226-7	1990	In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin dose required might cause an unacceptable bleeding risk, e.g. in simultaneous thrombocytopenia.	Heparin	191-198	serpin family C member 1	Homo sapiens	21-33
2106346-2	1990	The in vitro heparin-releasable LPL activity from blood correlated well with the LPL activity of postheparin plasma obtained from both normolipidemic and hyperlipidemic rabbits.	Heparin	13-20	lipoprotein lipase	Oryctolagus cuniculus	32-35
2197226-7	1990	In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin dose required might cause an unacceptable bleeding risk, e.g. in simultaneous thrombocytopenia.	Heparin	191-198	serpin family C member 1	Homo sapiens	46-62
26581031-1	2016	UNLABELLED: ESSENTIALS: Antithrombin III (AT)beta binds heparin with higher affinity than ATalpha.	Heparin	56-63	serpin family C member 1	Homo sapiens	24-40
2106346-2	1990	The in vitro heparin-releasable LPL activity from blood correlated well with the LPL activity of postheparin plasma obtained from both normolipidemic and hyperlipidemic rabbits.	Heparin	13-20	lipoprotein lipase	Oryctolagus cuniculus	81-84
2106346-3	1990	Studies in humans revealed sex- and age-related variations in the in vitro heparin-releasable LPL from monocytes in the blood of 134 normal subjects and 24 hypertriglyceridemic subjects: The mean LPL activity was significantly higher in normal females over the age of 30, than in the corresponding males.	Heparin	75-82	lipoprotein lipase	Homo sapiens	94-97
2106346-3	1990	Studies in humans revealed sex- and age-related variations in the in vitro heparin-releasable LPL from monocytes in the blood of 134 normal subjects and 24 hypertriglyceridemic subjects: The mean LPL activity was significantly higher in normal females over the age of 30, than in the corresponding males.	Heparin	75-82	lipoprotein lipase	Homo sapiens	196-199
2106346-5	1990	The in vitro heparin-releasable LPL activity from monocytes in blood was comparable to the LPL activity derived from adipose tissue and postheparin plasma, and thus it reflects lipoprotein metabolism.	Heparin	13-20	lipoprotein lipase	Homo sapiens	32-35
2303528-3	1990	In the presence of heparin, aFGF was as potent as EGF.	Heparin	19-26	epidermal growth factor	Mus musculus	50-53
2156859-4	1990	Likewise, a heparin- and dermatan sulfate-binding peptide which represents a portion of the glycosaminoglycan-binding domain of vitronectin (VN) selectively inhibited activities b and c, indicating the presence of clustered acidic domain(s) in TM responsible for these activities.	Heparin	12-19	vitronectin	Oryctolagus cuniculus	128-139
2156859-4	1990	Likewise, a heparin- and dermatan sulfate-binding peptide which represents a portion of the glycosaminoglycan-binding domain of vitronectin (VN) selectively inhibited activities b and c, indicating the presence of clustered acidic domain(s) in TM responsible for these activities.	Heparin	12-19	vitronectin	Oryctolagus cuniculus	141-143
2196192-0	1990	Low molecular weight heparin restores antithrombin III activity from hyperglycemia induced alterations.	Heparin	21-28	serpin family C member 1	Homo sapiens	38-54
2196192-2	1990	In this study the ability of a low molecular weight heparin (LMWH) (Fluxum, Alfa-Wassermann S.p.A., Bologna, Italy), as well as unfractioned heparin, to preserve ATIII activity from glucose-induced alterations, both in vitro and in vivo, is reported.	Heparin	52-59	serpin family C member 1	Homo sapiens	162-167
2315891-1	1990	According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin.	Heparin	358-365	serpin family C member 1	Homo sapiens	95-111
2315891-5	1990	A recovery of heparin cofactor activity towards coagulation factor Xa was observed upon prolonged storage of low affinity forms at -70 degrees C. It is considered that the loss of high affinity for heparin upon modification of antithrombin III arises from change or stabilization of conformation associated with tryptophan modification and is not a singular property of modification of Trp 49.	Heparin	14-21	serpin family C member 1	Homo sapiens	227-243
2196192-2	1990	In this study the ability of a low molecular weight heparin (LMWH) (Fluxum, Alfa-Wassermann S.p.A., Bologna, Italy), as well as unfractioned heparin, to preserve ATIII activity from glucose-induced alterations, both in vitro and in vivo, is reported.	Heparin	141-148	serpin family C member 1	Homo sapiens	162-167
2315894-1	1990	Heparin with low affinity for antithrombin III (ATIII) and devoid of anticoagulant activity was chemically oversulfated and fractionated by affinity for ATIII.	Heparin	0-7	serpin family C member 1	Homo sapiens	30-46
2196192-3	1990	The subcutaneous and intravenous LMWH and heparin administration increases basal depressed ATIII activity in diabetic patients.	Heparin	42-49	serpin family C member 1	Homo sapiens	91-96
26431853-5	2016	Multivariable linear regression analyses were used to explore the relationship between AT activity and heparin response measured by HSI.	Heparin	103-110	serpin family C member 1	Homo sapiens	87-89
2196192-4	1990	Heparin shows an equivalent effect on both anti-IIa and anti-Xa activity of ATIII, while LMWH is more effective in preserving the anti-Xa activity.	Heparin	0-7	serpin family C member 1	Homo sapiens	76-81
2315894-1	1990	Heparin with low affinity for antithrombin III (ATIII) and devoid of anticoagulant activity was chemically oversulfated and fractionated by affinity for ATIII.	Heparin	0-7	serpin family C member 1	Homo sapiens	48-53
2315894-1	1990	Heparin with low affinity for antithrombin III (ATIII) and devoid of anticoagulant activity was chemically oversulfated and fractionated by affinity for ATIII.	Heparin	0-7	serpin family C member 1	Homo sapiens	153-158
2315894-3	1990	The fluorescence increase was comparable to that of the AT III high affinity fraction of native heparin.	Heparin	96-103	serpin family C member 1	Homo sapiens	56-62
2315894-5	1990	The high affinity fractions of native heparin and the sulfated material were almost equally effective in enhancing the rate of thrombin neutralization by ATIII.	Heparin	38-45	serpin family C member 1	Homo sapiens	154-159
26431853-7	2016	After adjusting for low-molecular-weight heparin, unfractionated heparin, and platelet count, there was a significant relationship between AT activity and HSI (r = 0.44; P = 0.009).	Heparin	41-48	serpin family C member 1	Homo sapiens	139-141
2111292-12	1990	This was also seen in the LPL activity when measured in post-heparin plasma.	Heparin	61-68	lipoprotein lipase	Homo sapiens	26-29
26431853-7	2016	After adjusting for low-molecular-weight heparin, unfractionated heparin, and platelet count, there was a significant relationship between AT activity and HSI (r = 0.44; P = 0.009).	Heparin	65-72	serpin family C member 1	Homo sapiens	139-141
1964669-4	1990	The interaction of heparin with monocytes reversibly decreases the expression of tissue factor on the cellular surface, so hampering the cellular procoagulant potential.	Heparin	19-26	coagulation factor III, tissue factor	Homo sapiens	81-94
26431853-9	2016	CONCLUSIONS: There was a moderate relationship between AT activity and heparin response measured by HSI.	Heparin	71-78	serpin family C member 1	Homo sapiens	55-57
2104849-13	1990	Chromatography studies with heparin-Sepharose indicated that at least some of the lipoprotein lipase in cld/cld cells was dimerized.	Heparin	28-35	lipase maturation factor 1	Mus musculus	104-107
26411319-7	2016	In this minireview paper, we are to summarize the structural features of antithrombin, as well as its heparin binding modes and anti-coagulation mechanisms, in hopes that the discussion and analysis presented in this paper can stimulate new strategies to find more effective approaches or compounds to modulate the antithrombin.	Heparin	102-109	serpin family C member 1	Homo sapiens	73-85
2331700-1	1990	The conformation in solution of the pentasaccharide methyl glycoside (As-G-A*-Is-AM; 1), which represents the binding site of heparin for Antithrombin III, has been investigated using molecular mechanics and 1H-n.m.r.	Heparin	126-133	serpin family C member 1	Homo sapiens	138-154
2294104-9	1990	This effect of heparin is also independent of whether it has high or low affinity for antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	86-102
2313202-5	1990	A 56 kD protein increased after heparin injection, and likely represented active LPL.	Heparin	32-39	lipoprotein lipase	Homo sapiens	81-84
1710698-0	1990	[A method of determining heparin in blood plasma based on its antithrombin activity].	Heparin	25-32	serpin family C member 1	Homo sapiens	62-74
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	48-55	serpin family C member 1	Homo sapiens	95-107
26892137-2	2016	The proband"s LPL level after injection of heparin was measured at 184 U/L, considerably lower than the normal controls (382 U/L).	Heparin	43-50	lipoprotein lipase	Homo sapiens	14-17
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	48-55	serpin family C member 1	Homo sapiens	120-136
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	48-55	serpin family C member 1	Homo sapiens	138-144
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	68-75	serpin family C member 1	Homo sapiens	95-107
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	68-75	serpin family C member 1	Homo sapiens	120-136
1710698-1	1990	The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor.	Heparin	68-75	serpin family C member 1	Homo sapiens	138-144
1710698-2	1990	The method consists in measurement of blood plasma AT-III activity in the presence and absence of protamine sulfate that destroys the heparin--AT-III complex.	Heparin	134-141	serpin family C member 1	Homo sapiens	51-57
1710698-2	1990	The method consists in measurement of blood plasma AT-III activity in the presence and absence of protamine sulfate that destroys the heparin--AT-III complex.	Heparin	134-141	serpin family C member 1	Homo sapiens	143-149
1710698-3	1990	Heparin content in U/ml is determined from the difference in the activities of heparin--AT-III complex and AT-III proper activity represented on the calibration curve.	Heparin	0-7	serpin family C member 1	Homo sapiens	88-94
1710698-3	1990	Heparin content in U/ml is determined from the difference in the activities of heparin--AT-III complex and AT-III proper activity represented on the calibration curve.	Heparin	0-7	serpin family C member 1	Homo sapiens	107-113
2749591-0	1989	The effect of trace amounts of tissue factor on thrombin generation in platelet rich plasma, its inhibition by heparin.	Heparin	111-118	coagulation factor III, tissue factor	Homo sapiens	31-44
15681940-0	2005	A phase III, double-blind, placebo-controlled, multicenter study on the efficacy of recombinant human antithrombin in heparin-resistant patients scheduled to undergo cardiac surgery necessitating cardiopulmonary bypass.	Heparin	118-125	serpin family C member 1	Homo sapiens	102-114
2142645-3	1990	A recombinant hst-1 protein was synthesized in silkworm cells and found to be a potent heparin-binding mitogen for murine fibroblasts and human vascular endothelial cells.	Heparin	87-94	hybrid sterility 1	Mus musculus	14-19
26516227-1	2015	Fc receptor for IgG IIA (FcgammaRIIA)-mediated platelet activation is essential in heparin-induced thrombocytopenia (HIT) and other immune-mediated thrombocytopenia and thrombosis disorders.	Heparin	83-90	Fc receptor	Mus musculus	0-11
15681940-1	2005	BACKGROUND: The study evaluated the efficacy of recombinant human antithrombin (rhAT) for restoring heparin responsiveness in heparin resistant patients undergoing cardiac surgery.	Heparin	100-107	serpin family C member 1	Homo sapiens	66-78
15681940-1	2005	BACKGROUND: The study evaluated the efficacy of recombinant human antithrombin (rhAT) for restoring heparin responsiveness in heparin resistant patients undergoing cardiac surgery.	Heparin	126-133	serpin family C member 1	Homo sapiens	66-78
26834284-4	2015	Factor V Leiden patients can be safely anti-coagulated using heparin for CPB procedures when monitored with ACT, heparin protamine titration, and thrombelastography.	Heparin	61-68	coagulation factor V	Homo sapiens	0-15
34610468-5	2022	LpL is detected only in the heparin-bound fraction.	Heparin	28-35	lipoprotein lipase	Homo sapiens	0-3
34610468-6	2022	Transient binding to heparin activates this VLDL-associated LpL, which hydrolyses TG, leading to gradual VLDL remodeling into IDL/LDL and HDL-size particles.	Heparin	21-28	lipoprotein lipase	Homo sapiens	60-63
34895060-11	2021	HBP is critical for pancreatic necrosis response in acute pancreatitis by increasing the infiltration of M1 macrophages and promoting the secretion of inflammatory factors, such as TNF-alpha, IL-6, IL-1beta, which can be reduced by heparin.	Heparin	232-239	interleukin 1 alpha	Mus musculus	198-206
26834284-4	2015	Factor V Leiden patients can be safely anti-coagulated using heparin for CPB procedures when monitored with ACT, heparin protamine titration, and thrombelastography.	Heparin	113-120	coagulation factor V	Homo sapiens	0-15
25361738-0	2015	Prothrombotic SERPINC1 gene polymorphism may affect heparin sensitivity among different ethnicities of Chinese patients receiving heart surgery.	Heparin	52-59	serpin family C member 1	Homo sapiens	14-22
34718129-3	2021	The discovery of heparin as an effective inducer of Tau aggregation in vitro was instrumental to enabling different lines of research into the role of Tau aggregation in the pathogenesis of Tauopathies.	Heparin	17-24	microtubule associated protein tau	Homo sapiens	52-55
34718129-4	2021	However, recent proteomics and cryogenic electron microscopy (cryo-EM) studies have revealed that heparin-induced Tau fibrils generated in vitro do not reproduce the biochemical and ultrastructural properties of disease-associated brain-derived Tau fibrils.	Heparin	98-105	microtubule associated protein tau	Homo sapiens	114-117
34718129-6	2021	In this review article, we present an up-to-date analysis of 1) how our understanding of the Tau-heparin interactions has evolved over the years, 2) the various structural and mechanistic models of the heparin-induced Tau aggregation, 3) the similarities and differences between pathological and heparin-induced Tau fibrils; and 4) emerging concepts on the biochemical and structural determinants underpinning Tau pathological heterogeneity in Tauopathies.	Heparin	97-104	microtubule associated protein tau	Homo sapiens	93-96
34718129-6	2021	In this review article, we present an up-to-date analysis of 1) how our understanding of the Tau-heparin interactions has evolved over the years, 2) the various structural and mechanistic models of the heparin-induced Tau aggregation, 3) the similarities and differences between pathological and heparin-induced Tau fibrils; and 4) emerging concepts on the biochemical and structural determinants underpinning Tau pathological heterogeneity in Tauopathies.	Heparin	202-209	microtubule associated protein tau	Homo sapiens	218-221
25361738-1	2015	The purpose of this study was to investigate a possible correlation between single-nucleotide polymorphisms (SNPs) of the antithrombin (gene, SERPINC1, and perioperative sensitivity to heparin in patients receiving heart surgery.	Heparin	185-192	serpin family C member 1	Homo sapiens	122-134
34795305-5	2021	eGFs were even more potent in combination, and the "triple therapy" of vascular endothelial growth factor-A (VEGF-PlGF-2123-144), platelet-derived growth factor-BB (PDGF-BB-PlGF-2123-144), and heparin-binding epidermal growth factor (HB-EGF-PlGF-2123-144) both improved wound healing and remained at the site of administration for significantly longer than wild-type growth factors.	Heparin	193-200	heparin-binding EGF-like growth factor	Mus musculus	234-240
25361738-1	2015	The purpose of this study was to investigate a possible correlation between single-nucleotide polymorphisms (SNPs) of the antithrombin (gene, SERPINC1, and perioperative sensitivity to heparin in patients receiving heart surgery.	Heparin	185-192	serpin family C member 1	Homo sapiens	142-150
25361738-6	2015	The increased SERPINC1 SNP frequency among Han patients receiving heart surgery might contribute to the differences in their perioperative sensitivity to heparin.	Heparin	154-161	serpin family C member 1	Homo sapiens	14-22
34768285-1	2022	Plasmodium falciparum (Pf)-derived histidine-rich protein II (HRPII) has been shown to inhibit heparin-dependent anticoagulant activity of antithrombin (AT) and induce inflammation in vitro and in vivo.	Heparin	95-102	serpin family C member 1	Homo sapiens	139-151
26497525-6	2015	Finally, we present some new data investigating whether levels of the extracellular ligand-binding region of platelet glycoprotein VI which is rapidly shed upon engagement of platelet FcgammaRIIa by autoantibodies, can report on the presence of pathological anti-heparin/platelet factor 4 immune complexes and thus identify patients with pathological autoantibodies who are at the greatest risk of developing life-threatening thrombosis in the setting of heparin-induced thrombocytopenia.	Heparin	263-270	glycoprotein VI platelet	Homo sapiens	109-133
34851773-0	2021	Management of heparin resistance due to antithrombin deficiency in a Chinese pregnant woman: a case report.	Heparin	14-21	serpin family C member 1	Homo sapiens	40-52
26370484-0	2015	Acute coronary syndromes: Bivalirudin versus heparin for ACS.	Heparin	45-52	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	57-60
34691438-2	2021	Multiple treatment modalities have been suggested for patients with HTG-AP, such as permanent removal of TG by plasmapheresis, the use of insulin and heparin to enhance lipoprotein lipase activity and fibrate therapy, but the data remains limited.	Heparin	150-157	lipoprotein lipase	Homo sapiens	169-187
34659892-8	2021	Moreover, TNIIIA2-induced senescent fibroblasts secreted heparin-binding epidermal growth factor-like growth factor (HB-EGF), which caused preneoplastic epithelial HaCaT cells to acquire malignant properties, including colony-forming and focus-forming abilities.	Heparin	57-64	heparin binding EGF like growth factor	Homo sapiens	117-123
34153666-0	2021	The ERK/CREB/PTN/syndecan-3 pathway involves in heparin-mediated neuro-protection and neuro-regeneration against cerebral ischemia-reperfusion injury following cardiac arrest.	Heparin	48-55	cAMP responsive element binding protein 1	Rattus norvegicus	8-12
26115461-2	2015	Heparin has been used as a therapeutic anticoagulant drug for several decades through its interaction with ATIII, a serine protease inhibitor that plays a central role in the blood coagulation cascade.	Heparin	0-7	serpin family C member 1	Homo sapiens	107-112
34153666-5	2021	CREB antagonist (KG-501), ERK antagonist (PD98059) and si-PTN were used respectively to inhibit the expression of CREB, ERK and PTN in cells, so as to explore the role of heparin in regulating neuronal regeneration.	Heparin	171-178	cAMP responsive element binding protein 1	Rattus norvegicus	114-118
34153666-9	2021	In terms of the mechanism, heparin upregulated the expression of ERK, CREB, NF200, BDNF, NGF, PTN and syndecan-3 in the rat brains.	Heparin	27-34	cAMP responsive element binding protein 1	Rattus norvegicus	70-74
34293069-9	2021	A recombinant LDLR protein could block heparin-mediated apoE pulldown, suggesting that LDLR may act as an HBV cell attachment receptor via binding to the HBV-associated apoE.	Heparin	39-46	low density lipoprotein receptor	Homo sapiens	87-91
26115461-4	2015	Arixtra is the smallest synthetic Hp containing the specific pentasaccharide sequence required to bind with ATIII.	Heparin	34-36	serpin family C member 1	Homo sapiens	108-113
26522454-8	2015	The latter function is modulated by two distinct heparin-binding domains of IGFBP-2 which are lacking in IGFBP-1.	Heparin	49-56	insulin like growth factor binding protein 1	Homo sapiens	105-112
34230127-2	2021	MATERIALS AND METHODS: We examined the influence of small interfering RNA (siRNA) and short heparin RNA (shRNA) mediated knockdown of FosL1 on cell migration, invasion, and proliferation in vitro as well as on regional metastasis in vivo.	Heparin	92-99	FOS like 1, AP-1 transcription factor subunit	Homo sapiens	134-139
26308736-5	2015	The normalized ADAMTS13 activity guided the clinicians in the diagnosis of a concurrent heparin-induced thrombocytopenia due to the heparin lock, used for the indwelling catheter.	Heparin	88-95	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	15-23
34188079-11	2021	The growth-related oncogene/keratinocyte chemoattractant (GRO/KC) serum levels in rats treated with rBbCI-His(6) (1.40 mg/kg) or heparin (200 IU/kg) were reduced.	Heparin	129-136	C-X-C motif chemokine ligand 1	Rattus norvegicus	58-61
25969127-11	2015	Procoagulant TF activity of therapeutic MSCs is associated with reductions in myocardial perfusion when delivered IC may be successfully managed by heparin coadministration.	Heparin	148-155	coagulation factor III, tissue factor	Homo sapiens	13-15
34780727-5	2021	For LPL purification, we used heparin-Sepharose affinity chromatography, which disrupted LPL-GPIHBP1 complexes causing GPIHBP1 to elute with the flow-through of the conditioned media.	Heparin	30-37	lipoprotein lipase	Homo sapiens	89-92
26126828-6	2015	Antibody-independent Tau uptake into BV2 cells was blocked by heparin, consistent with a previously described role for heparan sulfate proteoglycans.	Heparin	62-69	microtubule associated protein tau	Homo sapiens	21-24
35605639-0	2022	Mixing study to diagnose heparin-resistance caused by functional antithrombin deficiency.	Heparin	25-32	serpin family C member 1	Homo sapiens	65-77
32262660-0	2015	Surface modification of poly(dimethylsiloxane) with a covalent antithrombin-heparin complex for the prevention of thrombosis: use of polydopamine as bonding agent.	Heparin	76-83	serpin family C member 1	Homo sapiens	63-75
35577786-4	2022	Functionally, compared with the unmodified aggregates, which require heparin induction to assemble, these self-assembled hyperphosphorylated tau aggregates more efficiently disrupt membrane bilayers and induce Toll-like receptor 4-dependent responses in human macrophages.	Heparin	69-76	microtubule associated protein tau	Homo sapiens	141-144
32262660-2	2015	To prevent thrombosis triggered by blood-material contact, an antithrombin-heparin (ATH) covalent complex was coated on PDMS surface using polydopamine (PDA) as a "bioglue".	Heparin	75-82	serpin family C member 1	Homo sapiens	62-74
25855705-8	2015	The STA liquid heparin method was the most sensitive to presence of rivaroxaban.	Heparin	15-22	GCY	Homo sapiens	4-7
35446751-0	2022	Physico-mechanical and Biological Evaluation of Heparin/VEGF-loaded Electrospun Polycaprolactone/ Decellularized Rat Aorta Extracellular Matrix for Small-Diameter Vascular Grafts.	Heparin	48-55	vascular endothelial growth factor A	Rattus norvegicus	56-60
25855705-11	2015	The STA liquid heparin, being exquisitely sensitive to rivaroxaban, may be suitable for ruling out presence of the drug.	Heparin	15-22	GCY	Homo sapiens	4-7
35457009-6	2022	In vitro recombinant tau can be aggregated by the action of polyanions, such as heparin, arachidonic acid, and more recently, the action of polyphosphates.	Heparin	80-87	microtubule associated protein tau	Homo sapiens	21-24
26130925-4	2015	METHODS: The Pax6 transcription factor was purified by heparin agarose affinity chromatography and DEAE cellulose chromatography techniques from the developing zebrafish embryos.	Heparin	55-62	paired box 6a	Danio rerio	13-17
26032846-2	2015	In pursuit of a regenerative wound therapy, we developed a heparin-based coacervate delivery system that provides controlled release of heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) within the wound bed.	Heparin	59-66	heparin-binding EGF-like growth factor	Mus musculus	136-200
35051745-1	2022	Glypican-3 (GPC3), a heparin sulfate proteoglycan, is a potential diagnostic and therapeutic target for hepatocellular carcinoma.	Heparin	21-28	glypican 3	Homo sapiens	0-10
35051745-1	2022	Glypican-3 (GPC3), a heparin sulfate proteoglycan, is a potential diagnostic and therapeutic target for hepatocellular carcinoma.	Heparin	21-28	glypican 3	Homo sapiens	12-16
35142393-9	2022	Furthermore, exosomes overexpressing SOD3 significantly enhanced angiogenesis in ECs by increasing local H2 O2  levels in a heparin-binding domain-dependent manner as well as restored defective wound healing and angiogenesis in T2DM or SOD3-/- mice.	Heparin	124-131	superoxide dismutase 3, extracellular	Mus musculus	37-41
35204047-3	2022	The gene mdka, a member of a small family of heparin binding growth factors, was previously shown to be involved in regeneration in the zebrafish retina, heart, and fin.	Heparin	45-52	midkine a	Danio rerio	9-13
26032846-2	2015	In pursuit of a regenerative wound therapy, we developed a heparin-based coacervate delivery system that provides controlled release of heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) within the wound bed.	Heparin	59-66	heparin-binding EGF-like growth factor	Mus musculus	202-208
25873395-7	2015	Heparin dissociated LPL from the N-terminal domain, and partially from wild type GPIHBP1, but was unable to elute the enzyme from the Ly6 domain.	Heparin	0-7	lipoprotein lipase	Homo sapiens	20-23
1697824-7	1990	Moreover, heparin administration was connected with significantly higher levels of AT III and protein C along with a lower concentration of factor X and FDP on the seventh day of the disease.	Heparin	10-17	serpin family C member 1	Homo sapiens	83-89
25988257-7	2015	UF/heparin-purified EVs from cell culture displayed the EV marker Alix, contained a diverse RNA profile, had lower levels of protein contamination, and were functional at binding to and uptake into cells.	Heparin	3-10	programmed cell death 6 interacting protein	Homo sapiens	66-70
25813285-9	2015	Unfractionated heparin and LMWHs attenuated the TNF-alpha-mediated induction of CXCL8 and enhanced CXCL5, CCL2, and CCL5.	Heparin	15-22	C-C motif chemokine ligand 2	Homo sapiens	106-110
24663337-7	2015	CXCL4-induced up-regulation of both MMP7 and S100A8 was curbed in the presence of heparin, which binds to CXCL4 and glycosaminoglycans, most likely representing the macrophage receptor for CXCL4.	Heparin	82-89	matrix metallopeptidase 7	Homo sapiens	36-40
25632836-9	2015	The normal range of LPL in pre-heparin serum was 50-77ng/ml and in post-heparin plasma 354-410ng/ml, respectively.	Heparin	31-38	lipoprotein lipase	Homo sapiens	20-23
2161390-0	1990	Heparin, a potent releasing agent of extracellular superoxide dismutase (EC-SOD C), suppresses ischaemic paw oedema in mice.	Heparin	0-7	superoxide dismutase 3, extracellular	Mus musculus	37-71
1710698-3	1990	Heparin content in U/ml is determined from the difference in the activities of heparin--AT-III complex and AT-III proper activity represented on the calibration curve.	Heparin	79-86	serpin family C member 1	Homo sapiens	88-94
25632836-9	2015	The normal range of LPL in pre-heparin serum was 50-77ng/ml and in post-heparin plasma 354-410ng/ml, respectively.	Heparin	72-79	lipoprotein lipase	Homo sapiens	20-23
25632836-10	2015	CONCLUSION: The LTIA assay is applicable in quantitating the concentration of LPL in both pre-heparin serum and post-heparin plasma.	Heparin	94-101	lipoprotein lipase	Homo sapiens	78-81
2079997-6	1990	The inhibition of fibrin formation of intraperitoneal heparin was increased by addition of AT III without a systemic inhibitory effect on fibrin formation.	Heparin	54-61	serpin family C member 1	Homo sapiens	91-97
2079997-7	1990	These data suggest that intraperitoneal administration of heparin without AT III would be sufficient for the purpose of preventing fibrin formation in CAPD patients without any trouble, and additional AT III might increase inhibitory effect of heparin.	Heparin	244-251	serpin family C member 1	Homo sapiens	201-207
25632836-10	2015	CONCLUSION: The LTIA assay is applicable in quantitating the concentration of LPL in both pre-heparin serum and post-heparin plasma.	Heparin	117-124	lipoprotein lipase	Homo sapiens	78-81
26390679-8	2015	Data were collected on 15 patients undergoing CPB who received antithrombin III (AT) replacement therapy for diminished heparin response.	Heparin	120-127	serpin family C member 1	Homo sapiens	63-79
2343430-3	1990	Though lipidic parameters were not modified after treatment, gemfibrozil increased the LPL and HL plasmatic activities measured 10 minutes after heparin injection.	Heparin	145-152	lipoprotein lipase	Homo sapiens	87-90
25181538-0	2015	Low molecular weight heparin improves proteinuria in rats with L-NAME induced preeclampsia by decreasing the expression of nephrin, but not podocin.	Heparin	21-28	NPHS1 adhesion molecule, nephrin	Rattus norvegicus	123-130
33822598-0	2021	Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin.	Heparin	56-63	serpin family C member 1	Homo sapiens	89-101
33822598-1	2021	Antithrombin is unique among serpin family protein protease inhibitors with respect to the major reactive center loop (RCL) and core conformational changes that mediate allosteric activation of its anticoagulant function by heparin.	Heparin	224-231	serpin family C member 1	Homo sapiens	0-12
25665603-1	2015	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of granulocyte colony-stimulating factor (G-CSF), and the role of Toll-like receptor 4 (TLR4) signaling pathway in this process.	Heparin	53-60	colony stimulating factor 3	Homo sapiens	117-154
25665603-1	2015	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of granulocyte colony-stimulating factor (G-CSF), and the role of Toll-like receptor 4 (TLR4) signaling pathway in this process.	Heparin	53-60	colony stimulating factor 3	Homo sapiens	156-161
33805059-7	2021	Consequently, a simultaneous blockade of thrombin and P-selectin binding seems to be a powerful approach, as mediated by heparin to crucially reduce the hypercoagulable state of pancreatic cancer patients.	Heparin	121-128	selectin P	Homo sapiens	54-64
25665603-1	2015	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of granulocyte colony-stimulating factor (G-CSF), and the role of Toll-like receptor 4 (TLR4) signaling pathway in this process.	Heparin	62-65	colony stimulating factor 3	Homo sapiens	117-154
25665603-1	2015	OBJECTIVE: To determine the effect of unfractionated heparin (UFH) on lipopolysaccharide (LPS)-induced expression of granulocyte colony-stimulating factor (G-CSF), and the role of Toll-like receptor 4 (TLR4) signaling pathway in this process.	Heparin	62-65	colony stimulating factor 3	Homo sapiens	156-161
25665603-17	2015	UFH with 0.1 U/mL and 1 U/mL lowered TLR-4 protein expression induced by LPS (0.68+-0.18, 0.62+-0.26 vs. 0.87+-0.23, both P &lt; 0.05).	Heparin	0-3	toll like receptor 4	Homo sapiens	37-42
25665603-19	2015	UFH might take its therapeutic effect through TLR4-dependent pathway.	Heparin	0-3	toll like receptor 4	Homo sapiens	46-50
34601007-4	2022	Moreover, we found that the heparin-binding motif-containing regions of Cfl1, i.e., Cfl19-25, Cfl134-51 and Cfl1108-125, like rCfl1, were also able to bind to LPS and LTA and to inhibit the bacterial growth.	Heparin	28-35	cofilin 1	Danio rerio	72-76
25687119-5	2015	Biacore experiments revealed that the binding affinity of Bothrops jararaca snake antithrombin to heparin was ~30 times higher than that of human antithrombin.	Heparin	98-105	serpin family C member 1	Homo sapiens	82-94
34939461-9	2021	Patients receiving continuous AT-III infusions spent a significantly higher percentage of ECMO time within the therapeutic range, measured using anti-Factor Xa levels (64.9+-4.2% vs. 29.1+-8.57%, p = 0.008), and required fewer changes to the heparin infusion rate (6.48+-0.88 vs 2.38+-0.36 changes/day changes/day, p = 0.005).	Heparin	242-249	serpin family C member 1	Homo sapiens	30-36
34939461-11	2021	CONCLUSION: AT-III as a continuous infusion in CDH neonates on ECMO provides a decreased need to modify heparin infusion and more consistent therapeutic anticoagulation without increasing the risk of life-threatening bleeding.	Heparin	104-111	serpin family C member 1	Homo sapiens	12-18
34927362-9	2022	Ki for the inhibition by full-length TFPI of these FXa variants was increased by 7- to 1150-fold, while ATIII inhibition in the presence of the heparin-analogue Fondaparinux was modestly increased by 2- to 15-fold compared to wild type.	Heparin	144-151	serpin family C member 1	Homo sapiens	104-109
25331949-0	2014	Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.	Heparin	45-52	serpin family C member 1	Homo sapiens	29-41
34507094-5	2021	It shows dynamic linear concentration of heparin in the ranges of 0.1-40 U mL-1 and 0.01-20 U mL-1 for the absorptive and fluorescent measurements, respectively, which both cover the clinically relevant levels of heparin.	Heparin	41-48	L1 cell adhesion molecule	Mus musculus	75-79
34507094-5	2021	It shows dynamic linear concentration of heparin in the ranges of 0.1-40 U mL-1 and 0.01-20 U mL-1 for the absorptive and fluorescent measurements, respectively, which both cover the clinically relevant levels of heparin.	Heparin	41-48	L1 cell adhesion molecule	Mus musculus	94-98
25331949-1	2014	Heparin allosterically activates antithrombin as an inhibitor of factors Xa and IXa by enhancing the initial Michaelis complex interaction of inhibitor with protease through exosites.	Heparin	0-7	serpin family C member 1	Homo sapiens	33-45
25331949-6	2014	These results demonstrate that the exosite is a key determinant of antithrombin reactivity with factors Xa and IXa in the native as well as the heparin-activated state and support a new model of allosteric activation we recently proposed in which a balance between attractive and repulsive exosite interactions in the native state is shifted to favor the attractive interactions in the activated state through core conformational changes induced by heparin binding.	Heparin	144-151	serpin family C member 1	Homo sapiens	67-79
34775044-4	2021	The crosslinked particles, XDSCS NPs, are stable in NaCl solutions up to 3 M. XDSCS NPs were able to incorporate heparin-binding proteins (VEGF and SDF-1alpha) rapidly and efficiently, and maintain the full biological activity of the proteins.	Heparin	113-120	vascular endothelial growth factor A	Rattus norvegicus	139-143
25331949-6	2014	These results demonstrate that the exosite is a key determinant of antithrombin reactivity with factors Xa and IXa in the native as well as the heparin-activated state and support a new model of allosteric activation we recently proposed in which a balance between attractive and repulsive exosite interactions in the native state is shifted to favor the attractive interactions in the activated state through core conformational changes induced by heparin binding.	Heparin	449-456	serpin family C member 1	Homo sapiens	67-79
25364825-18	2014	CONCLUSIONS: From this balb/c mice study, the analyses of mRNA and cytokines revealed that both intranasal heparin and lmw heparin treatment decreased the expression of Th1, Th2, and Th17 in spleen.	Heparin	107-114	heart and neural crest derivatives expressed 2	Mus musculus	174-177
34931195-3	2021	N released by SARS-CoV-2 infected cells or N-expressing transfected cells binds to neighboring cells by electrostatic high-affinity binding to heparan sulfate and heparin, but not other sulfated glycosaminoglycans.	Heparin	163-170	nucleocapsid phosphoprotein	Severe acute respiratory syndrome coronavirus 2	0-1
34931195-3	2021	N released by SARS-CoV-2 infected cells or N-expressing transfected cells binds to neighboring cells by electrostatic high-affinity binding to heparan sulfate and heparin, but not other sulfated glycosaminoglycans.	Heparin	163-170	nucleocapsid phosphoprotein	Severe acute respiratory syndrome coronavirus 2	43-44
25364825-18	2014	CONCLUSIONS: From this balb/c mice study, the analyses of mRNA and cytokines revealed that both intranasal heparin and lmw heparin treatment decreased the expression of Th1, Th2, and Th17 in spleen.	Heparin	123-130	heart and neural crest derivatives expressed 2	Mus musculus	174-177
34931184-3	2021	N released by SARS-CoV-2 infected cells or N-expressing transfected cells binds to neighboring cells by electrostatic high-affinity binding to heparan sulfate and heparin, but not other sulfated glycosaminoglycans.	Heparin	163-170	nucleocapsid phosphoprotein	Severe acute respiratory syndrome coronavirus 2	0-1
24711209-2	2014	This study evaluates how the mode of covalent heparin bonding affects the hemocompatibility and uptake of antithrombin on surfaces in whole blood.	Heparin	46-53	serpin family C member 1	Homo sapiens	106-118
34931184-3	2021	N released by SARS-CoV-2 infected cells or N-expressing transfected cells binds to neighboring cells by electrostatic high-affinity binding to heparan sulfate and heparin, but not other sulfated glycosaminoglycans.	Heparin	163-170	nucleocapsid phosphoprotein	Severe acute respiratory syndrome coronavirus 2	43-44
34944495-4	2021	Annexin A2 is a Ca2+-binding protein that binds F-actin, phospholipid, RNA, and specific polysaccharides such as heparin.	Heparin	113-120	annexin A2	Homo sapiens	0-10
24711209-8	2014	In addition, antithrombin constituted ~40% of the total adsorbed plasma protein concentration on the EPA-heparin surfaces.	Heparin	105-112	serpin family C member 1	Homo sapiens	13-25
24793094-0	2014	A "turn-off" SERS assay of heparin with high selectivity based on heparin-peptide complex and Raman labelled gold nanoparticles.	Heparin	27-34	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	13-17
34783530-6	2021	In contrast, Fe2+ neither enhanced tau droplet formation nor increased the heparin-induced aggregation of tau.	Heparin	75-82	microtubule associated protein tau	Homo sapiens	106-109
34718129-6	2021	In this review article, we present an up-to-date analysis of 1) how our understanding of the Tau-heparin interactions has evolved over the years, 2) the various structural and mechanistic models of the heparin-induced Tau aggregation, 3) the similarities and differences between pathological and heparin-induced Tau fibrils; and 4) emerging concepts on the biochemical and structural determinants underpinning Tau pathological heterogeneity in Tauopathies.	Heparin	296-303	microtubule associated protein tau	Homo sapiens	312-315
24793094-1	2014	Stable SERS response originating from gold nanoparticles (Au NPs) is demonstrated for the first time to be suitable for detection of heparin with high selectivity.	Heparin	133-140	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	7-11
24793094-2	2014	Herein we report a novel "turn-off" SERS assay for heparin based on Raman labelled Au NPs and competitive bonding between heparin and two specialized peptides, such as RKGSGRRLVKC (11-peptide) and CALNN (5-peptide).	Heparin	51-58	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	36-40
34389520-5	2021	The culture supernatants of rat peritoneal mast cells and RBL-2H3 mast cells contained 20-30 mug/ml of heparin, effectively activated PPAR-responsive luciferase activity, promoted mRNA and protein expressions of key adipogenic genes, and hence increased adipogenic differentiation of fascia- or epididymal adipose-derived stromal cells.	Heparin	103-110	peroxisome proliferator activated receptor alpha	Rattus norvegicus	134-138
24793094-2	2014	Herein we report a novel "turn-off" SERS assay for heparin based on Raman labelled Au NPs and competitive bonding between heparin and two specialized peptides, such as RKGSGRRLVKC (11-peptide) and CALNN (5-peptide).	Heparin	122-129	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	36-40
34778381-6	2021	In the presence of the poly-anion heparin, Tau35 increases thioflavin T fluorescence significantly faster and to a greater extent than full-length tau, demonstrating a higher propensity to aggregate.	Heparin	34-41	microtubule associated protein tau	Homo sapiens	147-150
34754684-2	2021	Antithrombin III (ATIII) is the most potent endogenous anticoagulant and is required for the clinical efficacy of heparin.	Heparin	114-121	serpin family C member 1	Homo sapiens	0-16
34754684-2	2021	Antithrombin III (ATIII) is the most potent endogenous anticoagulant and is required for the clinical efficacy of heparin.	Heparin	114-121	serpin family C member 1	Homo sapiens	18-23
24793094-3	2014	By means of coordination interactions and other non-electrostatic forces, these 5-peptide capped Au NPs are induced to undergo controllable aggregation upon the additive of 11-peptide and heparin with a concentration range (0-2.4 U/mL), which correspondingly cause quantitative changes of SERS intensity of 4-MBA conjugated on Au NPs.	Heparin	188-195	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	289-293
34596979-3	2021	In this study, we compared the binding of four inflammatory cytokines (CCL8, IL-1beta, IL-2 and IL-6) to immobilized heparin by an SPR analysis.	Heparin	117-124	interleukin 1 alpha	Homo sapiens	77-85
25419511-0	2014	Low-molecular-weight heparin modulates vein wall fibrotic response in a plasminogen activator inhibitor 1-dependent manner.	Heparin	21-28	serine (or cysteine) peptidase inhibitor, clade E, member 1	Mus musculus	72-105
34494046-3	2021	Heparin has been often used to trigger Tau aggregation in in vitro studies.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	39-42
34494046-4	2021	However, the conformational changes induced by heparin and the underlying mechanism of promotion of Tau aggregation by heparin are not well understood.	Heparin	47-54	microtubule associated protein tau	Homo sapiens	100-103
24901804-15	2014	In cohort 2, unfractionated heparin doses to achieve a target anti-factor Xa activity pre-post antithrombin concentrate were 28 and 19 U/kg/hr, respectively, for children 12 months old or younger and 25 and 19 U/kg/hr, respectively, for children older than 12 months.	Heparin	28-35	serpin family C member 1	Homo sapiens	95-107
34494046-4	2021	However, the conformational changes induced by heparin and the underlying mechanism of promotion of Tau aggregation by heparin are not well understood.	Heparin	119-126	microtubule associated protein tau	Homo sapiens	100-103
34494046-11	2021	Our results suggest that heparin remodels the conformations of R3 towards fibril-prone structures by increasing chain dimension and intermolecular contact regions, which may shed light on the atomic mechanism of heparin-induced amyloid fibrillization of Tau protein.	Heparin	25-32	microtubule associated protein tau	Homo sapiens	254-257
34494046-11	2021	Our results suggest that heparin remodels the conformations of R3 towards fibril-prone structures by increasing chain dimension and intermolecular contact regions, which may shed light on the atomic mechanism of heparin-induced amyloid fibrillization of Tau protein.	Heparin	212-219	microtubule associated protein tau	Homo sapiens	254-257
25153692-3	2014	Utilizing heparin as a cofactor and employing repetitive cycles of shearing and growth, synthetic Tau fibrils and Tau fibrils in AD brain extract are progressively amplified.	Heparin	10-17	microtubule associated protein tau	Homo sapiens	98-101
34529926-1	2021	Objective: Heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF), which binds to the EGF receptor, plays an important role in the occurrence and development of inflammation in various diseases.	Heparin	11-18	heparin binding EGF like growth factor	Homo sapiens	77-83
25153692-3	2014	Utilizing heparin as a cofactor and employing repetitive cycles of shearing and growth, synthetic Tau fibrils and Tau fibrils in AD brain extract are progressively amplified.	Heparin	10-17	microtubule associated protein tau	Homo sapiens	114-117
24945939-5	2014	Then, recombinant human VEGF-165 (rhVEGF) was immobilized by affinity binding to heparin.	Heparin	81-88	vascular endothelial growth factor A	Rattus norvegicus	24-28
34513101-0	2021	Treatment of Homozygous Type II Antithrombin Heparin-Binding Site Deficiency in Pregnancy.	Heparin	45-52	serpin family C member 1	Homo sapiens	32-44
34184429-0	2021	In vitro and in vivo safety studies indicate that R15, a synthetic poly-arginine peptide, could safely reverse the effects of unfractionated heparin.	Heparin	141-148	ribonuclease A family member 2	Rattus norvegicus	50-53
34184429-5	2021	We previously described R15, a linear peptide composed of 15 arginine molecules, as a potential UFH antagonist.	Heparin	96-99	ribonuclease A family member 2	Rattus norvegicus	24-27
34184429-10	2021	However, those influences weakened in whole blood or in live animals, and were avoided when R15 was in a complex with UFH.	Heparin	118-121	ribonuclease A family member 2	Rattus norvegicus	92-95
24705477-3	2014	One key target of heparin, among others, is antithrombin, a serine protease inhibitor that, upon activation, mainly targets anticoagulation factors IIa and Xa.	Heparin	18-25	serpin family C member 1	Homo sapiens	44-56
34184429-15	2021	In conclusion, R15 is non-immunogenic and potentially safe at a therapeutic dose to reverse the effects of UFH.	Heparin	107-110	ribonuclease A family member 2	Rattus norvegicus	15-18
34153666-10	2021	Inhibition of ERK, CREB and interference with PTN expression notably weakened the heparin-mediated neuroprotective effects and restrained the expression of ERK/CREB and PTN/syndecan-3 pathway.	Heparin	82-89	cAMP responsive element binding protein 1	Rattus norvegicus	19-23
34153666-11	2021	CONCLUSION: Heparin attenuates the secondary brain injury induced by CA-CPR through regulating the ERK/CREB-mediated PTN/syndecan-3 pathway.	Heparin	12-19	cAMP responsive element binding protein 1	Rattus norvegicus	103-107
24824609-11	2014	In contrast, variant 2, with similar electrophoretic mobility and heparin affinity to wild-type antithrombin, had impaired inhibitory activity that was partially compensated for by activation with heparin.	Heparin	197-204	serpin family C member 1	Homo sapiens	96-108
34318803-3	2021	Inspiringly, this facile nanoplatform with low cytotoxicity favors the ultrasensitive fluorescence assay for heparin and protamine with a detection limit (LOD, S/N = 3) as low as 1.2 ng mL-1 and 0.5 ng mL-1, respectively, involving heparin-induced aggregation of OFPNPs through electrostatic interaction or competitive rebinding of protamine to heparin.	Heparin	109-116	L1 cell adhesion molecule	Mus musculus	186-190
34318803-3	2021	Inspiringly, this facile nanoplatform with low cytotoxicity favors the ultrasensitive fluorescence assay for heparin and protamine with a detection limit (LOD, S/N = 3) as low as 1.2 ng mL-1 and 0.5 ng mL-1, respectively, involving heparin-induced aggregation of OFPNPs through electrostatic interaction or competitive rebinding of protamine to heparin.	Heparin	109-116	L1 cell adhesion molecule	Mus musculus	202-206
34318803-3	2021	Inspiringly, this facile nanoplatform with low cytotoxicity favors the ultrasensitive fluorescence assay for heparin and protamine with a detection limit (LOD, S/N = 3) as low as 1.2 ng mL-1 and 0.5 ng mL-1, respectively, involving heparin-induced aggregation of OFPNPs through electrostatic interaction or competitive rebinding of protamine to heparin.	Heparin	232-239	L1 cell adhesion molecule	Mus musculus	186-190
24748467-0	2014	Probing the impact of GFP tagging on Robo1-heparin interaction.	Heparin	43-50	roundabout guidance receptor 1	Homo sapiens	37-42
34318803-3	2021	Inspiringly, this facile nanoplatform with low cytotoxicity favors the ultrasensitive fluorescence assay for heparin and protamine with a detection limit (LOD, S/N = 3) as low as 1.2 ng mL-1 and 0.5 ng mL-1, respectively, involving heparin-induced aggregation of OFPNPs through electrostatic interaction or competitive rebinding of protamine to heparin.	Heparin	232-239	L1 cell adhesion molecule	Mus musculus	202-206
34489931-13	2021	Addition of 2-O-desulfated heparin significantly reduced FHR1- and FHR5-mediated C3b deposition on ciGEnCs.	Heparin	27-34	complement factor H related 1	Homo sapiens	57-61
34126147-0	2021	Induced forms of alpha2-macroglobulin neutralize heparin and direct oral anticoagulant effects.	Heparin	49-56	alpha-2-macroglobulin	Homo sapiens	17-37
34126147-12	2021	Induced forms of alpha2M have the potential to neutralize direct oral anticoagulants and heparins, and might be developed as a universal antidote in case of major bleeding or urgent surgery.	Heparin	89-97	alpha-2-macroglobulin	Homo sapiens	17-24
24748467-6	2014	In this report, we use surface plasmon resonance (SPR) spectroscopy to study the impact of the GFP tagging on the binding interaction between heparin and a heparin-binding protein, the Roundabout homolog 1 (Robo1).	Heparin	142-149	roundabout guidance receptor 1	Homo sapiens	185-205
34451811-3	2021	Surface plasmon resonance-based data indicate that BoSG can bind both HIV-1 proteins at nM concentrations with preference for Tat (7.5 x 10-8 M) over gp120 (3.2 x 10-7 M) as compared to UFH, which bound gp120 (8.7 x 10-7 M) over Tat (5.7 x 10-6 M).	Heparin	186-189	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	203-208
24748467-6	2014	In this report, we use surface plasmon resonance (SPR) spectroscopy to study the impact of the GFP tagging on the binding interaction between heparin and a heparin-binding protein, the Roundabout homolog 1 (Robo1).	Heparin	142-149	roundabout guidance receptor 1	Homo sapiens	207-212
24748467-7	2014	SPR reveals that heparin binds with higher affinity to Robo1 than GFP-tagged Robo1 and through a different kinetic mechanism.	Heparin	17-24	roundabout guidance receptor 1	Homo sapiens	55-60
24748467-7	2014	SPR reveals that heparin binds with higher affinity to Robo1 than GFP-tagged Robo1 and through a different kinetic mechanism.	Heparin	17-24	roundabout guidance receptor 1	Homo sapiens	77-82
24748467-10	2014	These data demonstrate that GFP tagging can reduce the binding affinity of Robo1 to heparin and hinder heparin binding-induced Robo1 conformation change.	Heparin	84-91	roundabout guidance receptor 1	Homo sapiens	75-80
34218546-6	2021	The matrices" suitability for delivery of relevant growth factors, like heparin-binding epidermal growth factor like growth factor (HB-EGF), further highlights their potential as bioinspired, functional microenvironments for enhancing skin regeneration.	Heparin	72-79	heparin binding EGF like growth factor	Homo sapiens	132-138
24024568-2	2014	MATERIALS &amp; METHODS: Chitosan/heparin nanoparticle-encapsulated CdtB was prepared and the delivery efficiency was monitored by confocal laser scanning microscopy.	Heparin	34-41	corneal dystrophy of Bowman's layer type II (Thiel-Behnke)	Homo sapiens	68-72
34019003-1	2021	OBJECTIVE: Novel antibodies to trisulfated heparin disaccharide (TS-HDS) and fibroblast growth factor receptor 3 (FGFR-3) have been recently described in otherwise cryptogenic small fiber neuropathy (SFN) cases.	Heparin	43-50	RNA exonuclease 2	Homo sapiens	200-203
24024568-5	2014	RESULTS: Chitosan/heparin nanoparticle-encapsulated CdtB preferentially inhibited the proliferation of cells derived from gastric cancer, but not in primary gastric epithelial cells.	Heparin	18-25	corneal dystrophy of Bowman's layer type II (Thiel-Behnke)	Homo sapiens	52-56
24024568-8	2014	CONCLUSION: These findings indicate that chitosan/heparin nanoparticle-encapsulated CdtB could represent a new CdtB delivery strategy for the treatment of gastric cancer.	Heparin	50-57	corneal dystrophy of Bowman's layer type II (Thiel-Behnke)	Homo sapiens	84-88
24024568-8	2014	CONCLUSION: These findings indicate that chitosan/heparin nanoparticle-encapsulated CdtB could represent a new CdtB delivery strategy for the treatment of gastric cancer.	Heparin	50-57	corneal dystrophy of Bowman's layer type II (Thiel-Behnke)	Homo sapiens	111-115
24276985-3	2014	METHODS: From January 2010 to December 2012 all consecutive patients undergoing CEA under general anesthesia at our institution received 5,000 U of heparin prior to carotid clamping, which was partially (half-dose) reversed with PS 25 mg immediately after declamping (group I).	Heparin	148-155	protein S	Homo sapiens	229-234
34070790-4	2021	Structural constraint of OPN, by immobilization or by addition of heparin, is required for its strong ligation of CD44.	Heparin	66-73	secreted phosphoprotein 1	Homo sapiens	25-28
34070790-5	2021	Prior literature provides evidence that heparin binding to OPN prompts the unfolding of a core element in the protein.	Heparin	40-47	secreted phosphoprotein 1	Homo sapiens	59-62
24444746-4	2014	Here we show that O-GlcNAc modification of full-length human tau impairs the rate and extent of its heparin-induced aggregation without perturbing its activity toward microtubule polymerization.	Heparin	100-107	microtubule associated protein tau	Homo sapiens	61-64
34072393-0	2021	Heparin-Binding Protein 17/Fibroblast Growth Factor-Binding Protein-1 Knockout Inhibits Proliferation and Induces Differentiation of Squamous Cell Carcinoma Cells.	Heparin	0-7	fibroblast growth factor binding protein 1	Homo sapiens	27-69
34072393-1	2021	Heparin-binding protein 17/fibroblast growth factor-binding protein-1 (HBp17/FGFBP-1) has been observed to induce the tumorigenic potential of epithelial cells and is highly expressed in oral cancer cell lines and tissues.	Heparin	0-7	fibroblast growth factor binding protein 1	Homo sapiens	27-69
34072393-1	2021	Heparin-binding protein 17/fibroblast growth factor-binding protein-1 (HBp17/FGFBP-1) has been observed to induce the tumorigenic potential of epithelial cells and is highly expressed in oral cancer cell lines and tissues.	Heparin	0-7	fibroblast growth factor binding protein 1	Homo sapiens	71-76
34072393-1	2021	Heparin-binding protein 17/fibroblast growth factor-binding protein-1 (HBp17/FGFBP-1) has been observed to induce the tumorigenic potential of epithelial cells and is highly expressed in oral cancer cell lines and tissues.	Heparin	0-7	fibroblast growth factor binding protein 1	Homo sapiens	77-84
24439425-9	2014	Finally, GPC3"s inhibitory effects on cell viability and Hh target gene expression are partially abrogated by heparin, a competitor for GPC3 binding.	Heparin	110-117	glypican 3	Homo sapiens	9-13
34067120-2	2021	Antithrombin has different conformations: native, heparin-activated, prelatent, latent, and cleaved.	Heparin	50-57	serpin family C member 1	Homo sapiens	0-12
24439425-9	2014	Finally, GPC3"s inhibitory effects on cell viability and Hh target gene expression are partially abrogated by heparin, a competitor for GPC3 binding.	Heparin	110-117	glypican 3	Homo sapiens	136-140
24627550-1	2014	In this issue of Blood, Poli et al demonstrate that heparin analogs engineered to minimize their anticoagulant properties can potently downregulate hepcidin production in vitro and in vivo, and may potentially be used to treat the anemia of inflammation.	Heparin	52-59	hepcidin antimicrobial peptide	Homo sapiens	148-156
34634786-1	2021	INTRODUCTION: Laparoscopic sleeve gastrectomy (LSG) significantly increases high-density lipoprotein cholesterol (HDL-C) and lipoprotein lipase (LPL) in pre-heparin serum (pre-heparin LPL levels).	Heparin	157-164	lipoprotein lipase	Homo sapiens	184-187
24438318-4	2014	Our study aimed to monitor AT-III levels in the early post-LT period to assess the need for the administration of AT-III concentrate to ensure the effectiveness of heparin.	Heparin	164-171	serpin family C member 1	Homo sapiens	27-33
34634786-1	2021	INTRODUCTION: Laparoscopic sleeve gastrectomy (LSG) significantly increases high-density lipoprotein cholesterol (HDL-C) and lipoprotein lipase (LPL) in pre-heparin serum (pre-heparin LPL levels).	Heparin	176-183	lipoprotein lipase	Homo sapiens	184-187
34634786-7	2021	Conversely, HDL-C levels and pre-heparin LPL levels were significantly increased after LSG.	Heparin	33-40	lipoprotein lipase	Homo sapiens	41-44
34634786-8	2021	Simple linear regression showed that changes in HDL-C levels were significantly correlated with total weight loss percentage, change in TG levels, abdominal fat areas, and pre-heparin LPL levels.	Heparin	176-183	lipoprotein lipase	Homo sapiens	184-187
34634786-9	2021	Additionally, the multiple regression model revealed that a decrease in TG levels and an increase in pre-heparin LPL levels were correlated with increased HDL-C levels after LSG.	Heparin	105-112	lipoprotein lipase	Homo sapiens	113-116
35102496-12	2022	Activated partial thromboplastin time was not prolonged (> 35 sec) until a concentration of 0.1 U mL-1 heparin was added.	Heparin	103-110	L1 cell adhesion molecule	Mus musculus	98-102
35196163-8	2022	Comparative quantitative tandem-mass-tag proteomics and functional assays on the heparin-binding secretomes of WT-MEF and Pdia3-/- MEF identified multiple ECM and growth factor proteins to be down-regulated in the CM of Pdia3-/- MEF.	Heparin	81-88	protein disulfide isomerase associated 3	Mus musculus	122-127
35242277-7	2022	Here, we used pharmacological inhibitors and transfection with siRNA to evaluate whether matrix metalloprotease (MMP)2/9, heparin-binding- (HB-) epidermal growth factor (EGF), EGF receptor (EGFR), PI3K/Akt, MAPKs, and transcription factor AP-1 participated in the S1P-induced COX-2/PGE2 system determined by Western blotting, real-time polymerase chain reaction (RT-PCR), chromatin immunoprecipitation (ChIP), and promoter-reporter assays in HCFs.	Heparin	122-129	epidermal growth factor	Homo sapiens	170-173
24438318-4	2014	Our study aimed to monitor AT-III levels in the early post-LT period to assess the need for the administration of AT-III concentrate to ensure the effectiveness of heparin.	Heparin	164-171	serpin family C member 1	Homo sapiens	114-120
24438318-14	2014	AT-III levels were low in 70% of pediatric patients following LT, thereby risking heparin ineffectiveness.	Heparin	82-89	serpin family C member 1	Homo sapiens	0-6
34626387-3	2022	Heparin polymers carrying rare 3-O-sulfated glucosamine units have been proven to be critical for binding to antithrombin and elicit an anticoagulant response.	Heparin	0-7	serpin family C member 1	Homo sapiens	109-121
24647152-4	2014	Fondaparinux, a chemically synthesized ULMWH of pentasaccharide, has the same antithrombin III (AT-III)-binding sequence as found in UFH and LMWH.	Heparin	133-136	serpin family C member 1	Homo sapiens	96-102
35024539-1	2022	Introduction: Studies using lipid infusions to raise fatty acid levels require heparin to release lipoprotein lipase (LPL), thus calling into question the appropriate control infusion for this type of study: saline alone or saline plus heparin.	Heparin	79-86	lipoprotein lipase	Homo sapiens	98-116
35024539-1	2022	Introduction: Studies using lipid infusions to raise fatty acid levels require heparin to release lipoprotein lipase (LPL), thus calling into question the appropriate control infusion for this type of study: saline alone or saline plus heparin.	Heparin	79-86	lipoprotein lipase	Homo sapiens	118-121
35024539-2	2022	We aimed to evaluate whether the addition of heparin alone, in doses needed to release LPL, would alter circulating free fatty acids (FFAs) and/or affect gonadotropins.	Heparin	45-52	lipoprotein lipase	Homo sapiens	87-90
24645228-3	2014	METHODS: In this retrospective case-control study we performed a chart review for the years 2004-2010 of homozygous and heterozygous FVL carriers who were treated with low molecular weight heparin (LMWH) at a dose of 0.6 mg/kg/day during pregnancy.	Heparin	189-196	coagulation factor V	Homo sapiens	133-136
24247245-0	2014	Hyaluronic acid receptor for endocytosis (HARE)-mediated endocytosis of hyaluronan, heparin, dermatan sulfate, and acetylated low density lipoprotein (AcLDL), but not chondroitin sulfate types A, C, D, or E, activates NF-kappaB-regulated gene expression.	Heparin	84-91	stabilin 2	Homo sapiens	0-40
24247245-0	2014	Hyaluronic acid receptor for endocytosis (HARE)-mediated endocytosis of hyaluronan, heparin, dermatan sulfate, and acetylated low density lipoprotein (AcLDL), but not chondroitin sulfate types A, C, D, or E, activates NF-kappaB-regulated gene expression.	Heparin	84-91	stabilin 2	Homo sapiens	42-46
24247245-1	2014	The hyaluronan (HA) receptor for endocytosis (HARE; Stab2) clears 14 systemic ligands, including HA and heparin.	Heparin	104-111	stabilin 2	Homo sapiens	46-50
24247245-1	2014	The hyaluronan (HA) receptor for endocytosis (HARE; Stab2) clears 14 systemic ligands, including HA and heparin.	Heparin	104-111	stabilin 2	Homo sapiens	52-57
24247245-3	2014	Unique intermediate size Select-HA(TM), heparin, dermatan sulfate, and acetylated LDL stimulated dose-dependent HARE-mediated NF-kappaB activation of luciferase expression, with half-maximal values of 10-25 nM.	Heparin	40-47	stabilin 2	Homo sapiens	112-116
24354321-1	2014	Heparin is best known for its anticoagulant activity, which is mediated by the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin-III (AT-III).	Heparin	0-7	serpin family C member 1	Homo sapiens	152-168
24354321-1	2014	Heparin is best known for its anticoagulant activity, which is mediated by the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin-III (AT-III).	Heparin	0-7	serpin family C member 1	Homo sapiens	170-176
25036482-0	2014	Effects of heparin and cholesterol sulfate on the activity and stability of human matrix metalloproteinase 7.	Heparin	11-18	matrix metallopeptidase 7	Homo sapiens	82-108
25036482-2	2014	In this study, the effects of heparin and cholesterol sulfate (CS) on the activity and stability of MMP-7 in the hydrolysis of a synthetic substrate, (7-methoxycoumarin-4-yl)acetyl-l-Pro-l-Leu-Gly-l-Leu-[N(3)-(2,4-dinitrophenyl)-l-2,3-diaminopropionyl]-l-Ala-l-Arg-NH2, were examined.	Heparin	30-37	matrix metallopeptidase 7	Homo sapiens	100-105
25036482-5	2014	In thermal incubation at 50-70  C, heparin increased relative activity (the ratio of kcat/Km of MMP-7 with incubation to that without it), while CS decreased relative activity.	Heparin	35-42	matrix metallopeptidase 7	Homo sapiens	96-101
24985584-10	2014	Heparin markedly decreased both IL-1alpha and IL-1beta expression in the spleens and serum of burned mice.	Heparin	0-7	interleukin 1 alpha	Mus musculus	32-41
24478399-9	2014	Furthermore, while insulin infusion during clamp decreased miR-222 (-62%; P = 0.002), the intralipid/heparin mixture increased circulating miR-222 (163%; P = 0.015) and miR-140-5p (67.5%; P = 0.05).	Heparin	101-108	microRNA 222	Homo sapiens	139-146
24201825-6	2014	Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes.	Heparin	14-21	serpin family C member 1	Homo sapiens	126-138
24201825-6	2014	Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes.	Heparin	107-114	serpin family C member 1	Homo sapiens	126-138
24735089-1	2014	To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer.	Heparin	108-115	serpin family C member 1	Homo sapiens	95-107
24735089-6	2014	It was shown that surfaces modified with ATH bound antithrombin selectively from plasma through the pentasaccharide sequence on the heparin moiety of ATH, indicating the ability of the ATH-modified surfaces to inhibit coagulation.	Heparin	132-139	serpin family C member 1	Homo sapiens	51-63
24473387-8	2014	The level of plasma PAI-1 in the heparin group was significant reduced compared with the group of CBP without anticoagulation (P&lt;0.05).	Heparin	33-40	serpin family E member 1	Homo sapiens	20-25
24473387-9	2014	There was negative correlation between the level of PAI-1 and the dosage of heparin used during a CBP session in the heparin group (r=-0.746, P&lt;0.001).	Heparin	76-83	serpin family E member 1	Homo sapiens	52-57
24473387-9	2014	There was negative correlation between the level of PAI-1 and the dosage of heparin used during a CBP session in the heparin group (r=-0.746, P&lt;0.001).	Heparin	117-124	serpin family E member 1	Homo sapiens	52-57
24473387-12	2014	Heparin used during CBP can reduce PAI-1 which intensifies its function of anticoagulation.	Heparin	0-7	serpin family E member 1	Homo sapiens	35-40
24247246-4	2013	As part of an effort to bioengineer CHO cells to produce heparin, we previously showed that the introduction of both HS3st1 and NDST2 (N-deacetylase/N-sulfotransferase isoform-2) afforded HS with a very low level of anticoagulant activity.	Heparin	57-64	bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2	Cricetulus griseus	128-133
24127555-6	2013	Accordingly, exogenous HS/heparin can regulate cytokine production by KIR2DL4-expressing NK cells and HEK293T cells (HEK293T-2DL4), and induces differential localization of KIR2DL4 to rab5(+) and rab7(+) endosomes, thus leading to downregulation of cytokine production and degradation of the receptor.	Heparin	26-33	RAB5A, member RAS oncogene family	Homo sapiens	184-188
23990470-1	2013	The nonspecific binding of heparin to plasma proteins compromises its anticoagulant activity by reducing the amount of heparin available to bind antithrombin.	Heparin	27-34	serpin family C member 1	Homo sapiens	145-157
23990470-1	2013	The nonspecific binding of heparin to plasma proteins compromises its anticoagulant activity by reducing the amount of heparin available to bind antithrombin.	Heparin	119-126	serpin family C member 1	Homo sapiens	145-157
23990470-2	2013	In addition, interaction of heparin with fibrin promotes formation of a ternary heparin-thrombin-fibrin complex that protects fibrin-bound thrombin from inhibition by the heparin-antithrombin complex.	Heparin	28-35	serpin family C member 1	Homo sapiens	179-191
23990470-9	2013	As a consequence, heparin-catalyzed inhibition of factor Xa by antithrombin is compromised by fibrinogen to a greater extent when Zn(2+) is present.	Heparin	18-25	serpin family C member 1	Homo sapiens	63-75
23811002-5	2013	Heparin and heparin derivatives might have a direct beneficial effect in APS via binding to beta2GPI and interfering with prothrombotic properties of beta2GPI/antibody complexes.	Heparin	0-7	apolipoprotein H	Homo sapiens	92-100
23811002-5	2013	Heparin and heparin derivatives might have a direct beneficial effect in APS via binding to beta2GPI and interfering with prothrombotic properties of beta2GPI/antibody complexes.	Heparin	0-7	apolipoprotein H	Homo sapiens	150-158
23811002-5	2013	Heparin and heparin derivatives might have a direct beneficial effect in APS via binding to beta2GPI and interfering with prothrombotic properties of beta2GPI/antibody complexes.	Heparin	12-19	apolipoprotein H	Homo sapiens	92-100
23811002-5	2013	Heparin and heparin derivatives might have a direct beneficial effect in APS via binding to beta2GPI and interfering with prothrombotic properties of beta2GPI/antibody complexes.	Heparin	12-19	apolipoprotein H	Homo sapiens	150-158
23811002-6	2013	We compared fondaparinux to heparin regarding its ability to bind beta2GPI and inhibit the binding of beta2GPI/antibody complexes to negatively charged phospholipids and endothelial cells.	Heparin	28-35	apolipoprotein H	Homo sapiens	66-74
23811002-6	2013	We compared fondaparinux to heparin regarding its ability to bind beta2GPI and inhibit the binding of beta2GPI/antibody complexes to negatively charged phospholipids and endothelial cells.	Heparin	28-35	apolipoprotein H	Homo sapiens	102-110
23845186-5	2013	RESULTS: At least 0.61 IU/mL UFH or 0.024 mg/mL LMWH was necessary for reliable prevention of coagulation of hPL pools used in this study.	Heparin	29-32	galectin 1	Homo sapiens	109-112
23845186-9	2013	CONCLUSIONS: Heparin concentration is critical for culture of MSCs in hPL media; this is of particular relevance for cellular therapy where cell culture procedures need to be optimized and standardized.	Heparin	13-20	galectin 1	Homo sapiens	70-73
23559035-1	2013	(hbd) PRELP is a peptide corresponding to the N-terminal heparin binding domain of the matrix protein proline/arginine-rich end leucine-rich repeat protein (PRELP).	Heparin	57-64	proline arginine-rich end leucine-rich repeat	Mus musculus	6-11
23559035-1	2013	(hbd) PRELP is a peptide corresponding to the N-terminal heparin binding domain of the matrix protein proline/arginine-rich end leucine-rich repeat protein (PRELP).	Heparin	57-64	proline arginine-rich end leucine-rich repeat	Mus musculus	102-155
23559035-1	2013	(hbd) PRELP is a peptide corresponding to the N-terminal heparin binding domain of the matrix protein proline/arginine-rich end leucine-rich repeat protein (PRELP).	Heparin	57-64	proline arginine-rich end leucine-rich repeat	Mus musculus	157-162
23850456-7	2013	We also determined that PRDC binds heparin with high affinity and that heparin binding to PRDC interferes with BMP antagonism.	Heparin	35-42	gremlin 2, DAN family BMP antagonist	Homo sapiens	24-28
23850456-7	2013	We also determined that PRDC binds heparin with high affinity and that heparin binding to PRDC interferes with BMP antagonism.	Heparin	71-78	gremlin 2, DAN family BMP antagonist	Homo sapiens	90-94
23850456-7	2013	We also determined that PRDC binds heparin with high affinity and that heparin binding to PRDC interferes with BMP antagonism.	Heparin	71-78	bone morphogenetic protein 1	Homo sapiens	111-114
23867845-3	2013	To stimulate this process, heparin, a glycosaminoglycan involved in growth factor binding, was covalently bound to porous collagenous scaffolds (14%), with or without vascular endothelial growth factor (VEGF; 0.4 microg/mg scaffold), hepatocyte growth factor (HGF; 0.5 microg/mg scaffold) or a combination of VEGF + HGF (0.2 + 0.5 microg/mg scaffold).	Heparin	27-34	vascular endothelial growth factor A	Rattus norvegicus	203-207
23867845-3	2013	To stimulate this process, heparin, a glycosaminoglycan involved in growth factor binding, was covalently bound to porous collagenous scaffolds (14%), with or without vascular endothelial growth factor (VEGF; 0.4 microg/mg scaffold), hepatocyte growth factor (HGF; 0.5 microg/mg scaffold) or a combination of VEGF + HGF (0.2 + 0.5 microg/mg scaffold).	Heparin	27-34	vascular endothelial growth factor A	Rattus norvegicus	309-313
23408671-3	2013	Although antithrombin deficiency has generally been thought to be the primary mechanism of heparin resistance, the reasons for heparin resistance are both complex and multifactorial.	Heparin	91-98	serpin family C member 1	Homo sapiens	9-21
2558424-0	1989	Influence of a low molecular weight heparin on the inhibition of factor Xa and thrombin in hip surgery.	Heparin	36-43	coagulation factor X	Homo sapiens	65-74
23408671-7	2013	Treatments for heparin resistance/alterations in heparin responsiveness include additional heparin or antithrombin supplementation.	Heparin	15-22	serpin family C member 1	Homo sapiens	102-114
2677012-3	1989	Soluble HDGF was purified essentially to homogeneity in a single step by heparin affinity chromatography.	Heparin	73-80	heparin binding growth factor	Bos taurus	8-12
23408671-7	2013	Treatments for heparin resistance/alterations in heparin responsiveness include additional heparin or antithrombin supplementation.	Heparin	49-56	serpin family C member 1	Homo sapiens	102-114
2677012-4	1989	The purified HDGF was identified to be acidic fibroblast growth factor based on the following properties: molecular weight of 18,000, isoelectric point of 5.2, amino acid composition and sequence, its dissociation from a heparin affinity column at 0.9 M NaCl, potentiation of activity in the presence of heparin, and antigenicity.	Heparin	221-228	heparin binding growth factor	Bos taurus	13-17
2677012-4	1989	The purified HDGF was identified to be acidic fibroblast growth factor based on the following properties: molecular weight of 18,000, isoelectric point of 5.2, amino acid composition and sequence, its dissociation from a heparin affinity column at 0.9 M NaCl, potentiation of activity in the presence of heparin, and antigenicity.	Heparin	304-311	heparin binding growth factor	Bos taurus	13-17
2482065-3	1989	In the presence of heparin, recognition of vitronectin by 8E6 was increased 64- or 52-fold by interaction with the complex of alpha-thrombin and heparin cofactor II or the Pittsburgh mutant (Met358----Arg) of alpha 1-protease inhibitor, respectively.	Heparin	19-26	vitronectin	Homo sapiens	43-54
2482065-8	1989	gamma-Thrombin caused 7- and 34-fold increases in recognition of vitronectin by MaVN 8E6 in the absence and presence of heparin, respectively.	Heparin	120-127	vitronectin	Homo sapiens	65-76
2529852-4	1989	Differences were also observed in the maximal acceleration of the antithrombin III-Factor Xa interaction: 1.2 x 10(9) M-1.min-1 at 0.2 microM-heparin sulphate compared with 2.2 x 10(9) M-1.min-1 at 0.04 microM-heparin.	Heparin	142-149	coagulation factor X	Homo sapiens	83-92
2529852-11	1989	The rate constant for transformation of the antithrombin III-Factor Xa complex into irreversible product differed between heparan sulphate (96 min-1) and heparin (429 min-1).	Heparin	154-161	coagulation factor X	Homo sapiens	61-70
23408671-7	2013	Treatments for heparin resistance/alterations in heparin responsiveness include additional heparin or antithrombin supplementation.	Heparin	49-56	serpin family C member 1	Homo sapiens	102-114
2476115-15	1989	Among several derivatives of pentosan polysulphate or of heparin which were tested, those having the higher degree of sulphation and/or molecular mass were the most efficient in enhancing the rate of activation of protein C by factor Xa in the presence of phospholipids.	Heparin	57-64	coagulation factor X	Homo sapiens	227-236
23408673-0	2013	The influence of antithrombin substitution on heparin sensitivity and activation of hemostasis during coronary artery bypass graft surgery: a dose-finding study.	Heparin	46-53	serpin family C member 1	Homo sapiens	17-29
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	12-19	coagulation factor X	Homo sapiens	180-189
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	12-19	coagulation factor X	Homo sapiens	230-244
23408673-2	2013	Supplementation of antithrombin (AT) may attenuate this activation and increase a patient"s susceptibility to heparin.	Heparin	110-117	serpin family C member 1	Homo sapiens	19-31
2722856-10	1989	243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin.	Heparin	21-29	coagulation factor X	Homo sapiens	75-84
2722856-10	1989	243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin.	Heparin	21-29	coagulation factor X	Homo sapiens	191-200
23408673-2	2013	Supplementation of antithrombin (AT) may attenuate this activation and increase a patient"s susceptibility to heparin.	Heparin	110-117	serpin family C member 1	Homo sapiens	33-35
2722856-10	1989	243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin.	Heparin	21-28	coagulation factor X	Homo sapiens	75-84
23408673-14	2013	DISCUSSION: High dosages of AT were required to preserve physiologic AT activity during coronary artery bypass graft surgery and to significantly enhance heparin sensitivity, respectively.	Heparin	154-161	serpin family C member 1	Homo sapiens	28-30
2722856-10	1989	243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin.	Heparin	21-28	coagulation factor X	Homo sapiens	191-200
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	130-138	coagulation factor X	Homo sapiens	187-196
23481656-9	2013	The latter events required interactions of these receptors with both the RGD-like sequence and the heparin-binding domain of Thy-1.	Heparin	99-106	Thy-1 cell surface antigen	Homo sapiens	125-130
2722856-11	1989	Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way.	Heparin	206-214	coagulation factor X	Homo sapiens	187-196
2520655-5	1989	Protamine reversal of heparin further increased the plasma levels of C3a and TCC.	Heparin	22-29	complement C3	Homo sapiens	69-72
23418741-4	2013	In the present study, we determined the structure of full-length zebrafish midkine and show that it interacts with fondaparinux (a synthetic highly sulfated pentasaccharide) and natural heparin through a previously uncharacterized, but highly conserved, hinge region.	Heparin	186-193	midkine a	Danio rerio	75-82
2713492-1	1989	Platelets secrete a low-molecular-weight protein, platelet factor four (PF-4), which binds to and neutralizes heparin and related sulfated glycosaminoglycans (GAGs).	Heparin	110-117	platelet factor 4	Bos taurus	72-76
2785004-2	1989	In this study we evaluated complement activation (C3a and C4a) by the heparin-protamine complex in 46 consecutive patients (40 received protamine sulfate to reverse heparin, and six did not) during and after coronary angiography.	Heparin	70-77	complement C3	Homo sapiens	50-53
23418741-7	2013	Instead, we have demonstrated that the N-terminal half domain is needed to enhance heparin binding and mediate midkine embryogenic activity surprisingly in both heparin-dependent and -independent manners.	Heparin	161-168	midkine a	Danio rerio	111-118
23016581-8	2013	Low affinity relaxed conformation with reduced heparin binding like cleaved and latent are antiangiogenic but native high affinity heparin binding stressed conformation is not, indicating the critical importance of heparin affinity in antithrombin antiangiogenic function.	Heparin	47-54	serpin family C member 1	Homo sapiens	235-247
2500671-4	1989	An oxidant scavenging mechanism is also inferred from the fact that heparin is capable of inhibiting luminol-dependent chemiluminescence resulting from the reduction of 15-HPETE by methemoglobin.	Heparin	68-75	hemoglobin subunit gamma 2	Homo sapiens	181-194
2465025-2	1989	Vitronectin was found to exist in fresh human plasma as a heterogeneous mixture consisting of 2% heparin-binding form and the remainder as a non-binding species.	Heparin	97-104	vitronectin	Homo sapiens	0-11
2465025-3	1989	Heparin-binding vitronectin consisted of 6.5 S aggregates with a Stokes radius of 5.6 nm, which was enriched in the 65 kDa polypeptide, with a high content of molecules and a putative unfolded conformation.	Heparin	0-7	vitronectin	Homo sapiens	16-27
2465025-4	1989	In contrast, non-heparin-binding vitronectin was a 4.2 S monomer with a Stokes radius of 3.9 nm, which appeared to be in a folded conformation with an immunologically cryptic site.	Heparin	17-24	vitronectin	Homo sapiens	33-44
2465025-6	1989	During blood coagulation, 5% more of the non-heparin-binding vitronectin was converted into the heparin-binding form, producing a greater than 3.5-fold increase in this species.	Heparin	45-52	vitronectin	Homo sapiens	61-72
2783543-7	1989	Both gel filtration and heparin-Sepharose affinity chromatography separate the cytosolic androgen receptor from MEB.	Heparin	24-31	androgen receptor	Rattus norvegicus	89-106
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	167-174	serpin family C member 1	Homo sapiens	234-246
2920007-1	1989	We have proposed previously that the steps in coagulation most sensitive to inhibition by heparin are the thrombin-dependent amplification reactions, and that prothrombinase is formed in heparinized plasma only after Factor Xa activates Factor VIII and Factor V. These propositions were based on the demonstration that both heparin and Phe-Pro-Arg-CH2Cl completely inhibited 125I-prothrombin activation for up to 60 s when contact-activated plasma (CAP) was replenished with Ca2+.	Heparin	187-194	coagulation factor X	Homo sapiens	159-173
23016581-9	2013	Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation.	Heparin	314-321	serpin family C member 1	Homo sapiens	234-246
2920007-3	1989	Additional support for the above hypotheses is provided in this study by demonstrating that, when the activity of thrombin is suppressed by heparin (indirectly) or by Phe-Pro-Arg-CH2Cl (directly), exogenous Factor Xa reverses the ability of these two agents to inhibit prothrombin activation.	Heparin	140-147	coagulation factor X	Homo sapiens	207-216
23016581-10	2013	It is also possible that cleaved and latent conformations with reduced affinity for heparins can also induce conformational change in the antithrombin which can open an epitope on the antithrombin surface for appropriate interactions on the endothelial surface for better antiangiogenic activity.	Heparin	84-92	serpin family C member 1	Homo sapiens	138-150
3238649-3	1988	In contact-activated plasma prothrombinase generation is inhibited by heparin, because heparin lowers the ambient concentrations of thrombin so that the feedback activation of factor VIII by thrombin is diminished.	Heparin	70-77	coagulation factor X	Homo sapiens	28-42
3238649-3	1988	In contact-activated plasma prothrombinase generation is inhibited by heparin, because heparin lowers the ambient concentrations of thrombin so that the feedback activation of factor VIII by thrombin is diminished.	Heparin	87-94	coagulation factor X	Homo sapiens	28-42
23016581-10	2013	It is also possible that cleaved and latent conformations with reduced affinity for heparins can also induce conformational change in the antithrombin which can open an epitope on the antithrombin surface for appropriate interactions on the endothelial surface for better antiangiogenic activity.	Heparin	84-92	serpin family C member 1	Homo sapiens	184-196
2851191-7	1988	This concentration of the three LMW heparins increased, by approximately 70-fold, the rate of factor Xa inhibition by purified antithrombin III compared to the 50-fold increase seen with the two unfractionated heparins.	Heparin	36-44	coagulation factor X	Homo sapiens	94-103
23223449-5	2013	The activities of tryptase and carboxypeptidase-A were decreased in HS6ST-2(-/-)-FSMCs in which 6-O-sulfation of heparin was decreased at 50% of WT-FSMCs and almost lost in HS6ST-1(-/-)/HS6ST-2(-/-)-FSMCs, which lacked the 6-O-sulfation in heparin nearly completely.	Heparin	113-120	tryptase alpha/beta 1	Mus musculus	18-26
2458767-0	1988	Heparin-, dextran sulfate- and protamine-induced release of extracellular-superoxide dismutase to plasma in pigs.	Heparin	0-7	superoxide dismutase 3	Sus scrofa	60-94
23223449-5	2013	The activities of tryptase and carboxypeptidase-A were decreased in HS6ST-2(-/-)-FSMCs in which 6-O-sulfation of heparin was decreased at 50% of WT-FSMCs and almost lost in HS6ST-1(-/-)/HS6ST-2(-/-)-FSMCs, which lacked the 6-O-sulfation in heparin nearly completely.	Heparin	113-120	heparan sulfate 6-O-sulfotransferase 2	Mus musculus	68-75
23223449-5	2013	The activities of tryptase and carboxypeptidase-A were decreased in HS6ST-2(-/-)-FSMCs in which 6-O-sulfation of heparin was decreased at 50% of WT-FSMCs and almost lost in HS6ST-1(-/-)/HS6ST-2(-/-)-FSMCs, which lacked the 6-O-sulfation in heparin nearly completely.	Heparin	240-247	tryptase alpha/beta 1	Mus musculus	18-26
3140769-1	1988	Tissue plasminogen activator"s thrombolytic action is relatively specific for fibrin; however, systemic bleeding can occur in patients, especially when heparin is simultaneously administered.	Heparin	152-159	chromosome 20 open reading frame 181	Homo sapiens	0-28
23223449-5	2013	The activities of tryptase and carboxypeptidase-A were decreased in HS6ST-2(-/-)-FSMCs in which 6-O-sulfation of heparin was decreased at 50% of WT-FSMCs and almost lost in HS6ST-1(-/-)/HS6ST-2(-/-)-FSMCs, which lacked the 6-O-sulfation in heparin nearly completely.	Heparin	240-247	heparan sulfate 6-O-sulfotransferase 2	Mus musculus	68-75
23223449-9	2013	These observations suggest that both HS6ST-1 and HS6ST-2 are involved in 6-O-sulfation of heparin and that the proper packaging and storage of tryptase, carboxypeptidase-A, and chymase may be regulated differently by the 6-O-sulfate residues in heparin.	Heparin	90-97	heparan sulfate 6-O-sulfotransferase 2	Mus musculus	49-56
23223449-9	2013	These observations suggest that both HS6ST-1 and HS6ST-2 are involved in 6-O-sulfation of heparin and that the proper packaging and storage of tryptase, carboxypeptidase-A, and chymase may be regulated differently by the 6-O-sulfate residues in heparin.	Heparin	245-252	heparan sulfate 6-O-sulfotransferase 2	Mus musculus	49-56
23083208-1	2013	The 3-O-sulfation of N-sulfated glucosamine is the last event in the biosynthesis of heparin/heparan sulfate, giving rise to the antithrombin-binding pentasaccharide sequence AGA*IA, which is largely associated with the antithrombotic activity of these molecules.	Heparin	85-92	serpin family C member 1	Homo sapiens	129-141
2459497-6	1988	HNT potentiated this antiangiogenic activity in a dose-dependent manner when the concentration of heparin was suboptimal.	Heparin	98-105	neurotrimin	Gallus gallus	0-3
2459497-7	1988	Potentiation of the antiangiogenic activity of steroids by HNT correlated inversely with the concentration of exogenous heparin.	Heparin	120-127	neurotrimin	Gallus gallus	59-62
2459497-13	1988	These results suggest that HNT (a) potentiates the anticoagulant function of heparin, (b) prevents the inactivation of antiangiogenic activity of heparin by an endogenous arylsulfatase in the chorioallantoic membrane and by a commercial arylsulfatase, and (c) in the presence of angiostatic steroids can inhibit angiogenesis in the chick embryo without the addition of exogenous heparin.	Heparin	77-84	neurotrimin	Gallus gallus	27-30
2459497-13	1988	These results suggest that HNT (a) potentiates the anticoagulant function of heparin, (b) prevents the inactivation of antiangiogenic activity of heparin by an endogenous arylsulfatase in the chorioallantoic membrane and by a commercial arylsulfatase, and (c) in the presence of angiostatic steroids can inhibit angiogenesis in the chick embryo without the addition of exogenous heparin.	Heparin	146-153	neurotrimin	Gallus gallus	27-30
2459497-13	1988	These results suggest that HNT (a) potentiates the anticoagulant function of heparin, (b) prevents the inactivation of antiangiogenic activity of heparin by an endogenous arylsulfatase in the chorioallantoic membrane and by a commercial arylsulfatase, and (c) in the presence of angiostatic steroids can inhibit angiogenesis in the chick embryo without the addition of exogenous heparin.	Heparin	146-153	neurotrimin	Gallus gallus	27-30
2455567-1	1988	Vitronectin, also known as serum-spreading factor or S-protein, mediates cell adhesion and inhibits formation of the membrane-lytic complex of complement and the rapid inactivation of thrombin by antithrombin III in the presence of heparin.	Heparin	232-239	vitronectin	Homo sapiens	0-11
2455567-1	1988	Vitronectin, also known as serum-spreading factor or S-protein, mediates cell adhesion and inhibits formation of the membrane-lytic complex of complement and the rapid inactivation of thrombin by antithrombin III in the presence of heparin.	Heparin	232-239	vitronectin	Homo sapiens	27-49
2455567-1	1988	Vitronectin, also known as serum-spreading factor or S-protein, mediates cell adhesion and inhibits formation of the membrane-lytic complex of complement and the rapid inactivation of thrombin by antithrombin III in the presence of heparin.	Heparin	232-239	vitronectin	Homo sapiens	53-62
3396757-3	1988	MGSA has been purified to homogeneity from conditioned medium of Hs294T human malignant melanoma cells using acetic acid extraction of the crude conditioned medium followed by three chromatographic processes, including gel-filtration, heparin-Sepharose, and reverse-phase HPLC.	Heparin	235-242	C-X-C motif chemokine ligand 1	Homo sapiens	0-4
23103358-5	2013	The assay revealed that murine pre-heparin plasma does not contain measurable EL activity, indicating that the hydrolysis of HDL phospholipids by EL in vivo likely occurs on the cell surface.	Heparin	35-42	lipase, endothelial	Mus musculus	146-148
3334902-4	1988	Of the subendothelium-bound 125I-antithrombin III, more than 80% was efficiently removed by excess thrombin or by excess heparin.	Heparin	121-128	prothrombin	Oryctolagus cuniculus	37-45
23105116-8	2012	To further evaluate the functional role of Trx-1, we used a heparin-binding EGF shedding cell model and observed that the overexpression of Trx-1 in HEK293 cells could decrease the activity of ADAM17, activated by either phorbol 12-myristate 13-acetate or EGF.	Heparin	60-67	thioredoxin	Homo sapiens	140-145
3068010-5	1988	Studies with primary rat osteoblast-like cells exposed either to mixed BDGFs, pure TGF-beta, or heparin-purified PDGF, aFGF, or bFGF from bovine bone have shown a general dose-dependent mitogenic effect.	Heparin	96-103	fibroblast growth factor 1	Rattus norvegicus	119-123
22923734-0	2012	Stable complex formation between serine protease inhibitor and zymogen: coagulation factor X cleaves the Arg393-Ser394 bond in a reactive centre loop of antithrombin in the presence of heparin.	Heparin	185-192	serpin family C member 1	Homo sapiens	153-165
2906331-9	1988	The mitogenic activities of aFGF and bFGF were potentiated similarly by heparan sulfate and by heparin, with a maximum stimulation of about 100% at 100 micrograms/ml heparin.	Heparin	95-102	fibroblast growth factor 1	Rattus norvegicus	28-32
2906331-9	1988	The mitogenic activities of aFGF and bFGF were potentiated similarly by heparan sulfate and by heparin, with a maximum stimulation of about 100% at 100 micrograms/ml heparin.	Heparin	166-173	fibroblast growth factor 1	Rattus norvegicus	28-32
2445746-0	1987	Structural requirements for the neutralization of heparin-like saccharides by complement S protein/vitronectin.	Heparin	50-57	vitronectin	Homo sapiens	89-98
2445746-0	1987	Structural requirements for the neutralization of heparin-like saccharides by complement S protein/vitronectin.	Heparin	50-57	vitronectin	Homo sapiens	99-110
2445746-3	1987	We have studied the structural requirements for the heparin neutralizing properties of S protein/vitronectin using heparin, heparan sulfate, and heparin oligosaccharides with well defined anticoagulant specificities.	Heparin	52-59	vitronectin	Homo sapiens	87-96
22978548-0	2012	By increasing the affinity of heparin for fibrin, Zn(2+) promotes the formation of a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin.	Heparin	30-37	serpin family C member 1	Homo sapiens	167-179
2445746-3	1987	We have studied the structural requirements for the heparin neutralizing properties of S protein/vitronectin using heparin, heparan sulfate, and heparin oligosaccharides with well defined anticoagulant specificities.	Heparin	52-59	vitronectin	Homo sapiens	97-108
22978548-8	2012	Therefore, by enhancing the binding of heparin to fibrin, physiological concentrations of Zn(2+) render fibrin-bound thrombin more protected from inhibition by antithrombin.	Heparin	39-46	serpin family C member 1	Homo sapiens	160-172
22905983-8	2012	UFH (62-fold) and fondaparinux (42-fold) demonstrated markedly increased EC(50) values in antithrombin-depleted plasma, whereas LMWH (9.4-fold) and ssLMWH (two-fold) were less affected, with an EC(50) within the therapeutic range for LMWH.	Heparin	0-3	serpin family C member 1	Homo sapiens	90-102
3481140-1	1987	Heparin therapy was monitored with the activated partial thromboplastin time (APTT) and with chromogenic substrate assays (factor Xa and factor IIa inhibition) in 100 plasma samples from 47 patients.	Heparin	0-7	coagulation factor X	Homo sapiens	123-147
3653103-6	1987	Heparin activation of the p68 kinase is reversible since it can be prevented by addition of antithrombin III, heparin-binding protein.	Heparin	0-7	azurocidin 1	Homo sapiens	110-133
22641771-7	2012	Functional studies observed that HSCF inhibited antithrombin binding to heparin and neutralized the antifactor IIa and Xa activities of heparin and the antifactor IIa activity of low-molecular-weight heparin (LMWH).	Heparin	72-79	serpin family C member 1	Homo sapiens	48-60
3675305-3	1987	Specifically, we examined: 1) the role of different substrates (plastic, fibronectin, monomeric, and fibrillar collagens I and III, and EC-derived matrices) on the growth rate and population density of SMC; 2) the heparin-sensitivity of SMC on these diverse substrates; and 3) the effect of these same substrates on EC ability to secrete heparin-like and polypeptide inhibitors of SMC growth.	Heparin	214-221	structural maintenance of chromosomes 2	Homo sapiens	202-208
22492552-0	2012	Heparin-modified dendrimer crosslinked collagen matrices for the delivery of heparin-binding epidermal growth factor.	Heparin	0-7	heparin binding EGF like growth factor	Homo sapiens	77-116
3499389-4	1987	LPS suppressed in a dose- and time-dependent manner the heparin-induced secretion of LPL from the macrophage-like tumor cell line J774.1 and from bone marrow derived mononuclear phagocytes (BMM).	Heparin	56-63	lipoprotein lipase	Mus musculus	85-88
3499435-5	1987	The activity was strongly inhibited by micromolar concentrations of heavy metal ions, such as Zn2+ and Fe2+, and glycylarginine-methylcoumarinamide (Gly-Arg-MCA) in the presence of 100 ng/ml heparin.	Heparin	191-198	serine hydroxymethyltransferase 2	Homo sapiens	113-160
3585139-4	1987	Heparin, and low-affinity heparin, reduced the anti-Xa activity of HTGL, suggesting that heparin and factor Xa compete for the same binding sites on the lipase molecule.	Heparin	0-7	coagulation factor X	Homo sapiens	101-110
3585139-4	1987	Heparin, and low-affinity heparin, reduced the anti-Xa activity of HTGL, suggesting that heparin and factor Xa compete for the same binding sites on the lipase molecule.	Heparin	26-33	coagulation factor X	Homo sapiens	101-110
3553192-7	1987	Binding of heparin did not detectably affect catalysis of peptide substrates, but may reduce accessibility of proteinase to protein substrates.	Heparin	11-18	endogenous retrovirus group K member 9	Homo sapiens	110-120
22492552-9	2012	Heparinized dendrimer crosslinked collagen (CHG) gels were capable of HB-EGF uptake, which was influenced by heparin concentration within the gel, growth factor concentration and exposure time to the growth factor.	Heparin	109-116	heparin binding EGF like growth factor	Homo sapiens	70-76
3468112-1	1987	Casein kinase II of yeast has been purified to near homogeneity by a procedure which includes affinity chromatography on heparin-agarose.	Heparin	121-128	casein kinase IIalpha	Drosophila melanogaster	0-16
22534410-2	2012	Therefore, the authors determined the relationship between AT and other coagulation-related factors that affect the ACT measurement and heparin sensitivity index before the establishment of cardiopulmonary bypass.	Heparin	136-143	serpin family C member 1	Homo sapiens	59-61
3481165-2	1987	The heparin surface was highly thromboresistant in contact with blood, as manifested by minimal cell adhesion and a pronounced capacity to inactivate coagulation enzymes such as thrombin and factor Xa.	Heparin	4-11	coagulation factor X	Homo sapiens	191-200
3028582-6	1987	It is proposed that the polyanionic component of thrombomodulin blocks a site on thrombin required for heparin binding, thus rendering the antithrombin-heparin complex ineffective.	Heparin	103-110	prothrombin	Oryctolagus cuniculus	81-89
3028582-6	1987	It is proposed that the polyanionic component of thrombomodulin blocks a site on thrombin required for heparin binding, thus rendering the antithrombin-heparin complex ineffective.	Heparin	152-159	prothrombin	Oryctolagus cuniculus	81-89
22453684-0	2012	Limitations of conventional anticoagulant therapy and the promises of non-heparin based conformational activators of antithrombin.	Heparin	74-81	serpin family C member 1	Homo sapiens	117-129
2430628-2	1986	Using a Ca2+-selective electrode and Quin 2 and chlortetracycline fluorescence, a Ca2+ release from terminal cysterns of skeletal muscle sarcoplasmic reticulum under effects of heparin, caffeine and Ca2+ has been studied.	Heparin	177-184	carbonic anhydrase 2	Homo sapiens	82-85
2430628-2	1986	Using a Ca2+-selective electrode and Quin 2 and chlortetracycline fluorescence, a Ca2+ release from terminal cysterns of skeletal muscle sarcoplasmic reticulum under effects of heparin, caffeine and Ca2+ has been studied.	Heparin	177-184	carbonic anhydrase 2	Homo sapiens	82-85
2430628-3	1986	It was shown that Ca2+ release induced by heparin is insensitive to the blockers of Mg2+-dependent system of Ca2+-induced Ca2+ release, i.e., Mg2+, tetracaine and dimethylsulfoxide.	Heparin	42-49	carbonic anhydrase 2	Homo sapiens	18-21
22453684-4	2012	The conformational activation of antithrombin by heparin is a critical step in the inhibition of factor Xa by antithrombin.	Heparin	49-56	serpin family C member 1	Homo sapiens	33-45
2430628-6	1986	It has been shown that the heparin-induced release of Ca2+ diminishes with a decrease in a decrease in Ca2+ concentration.	Heparin	27-34	carbonic anhydrase 2	Homo sapiens	54-57
22453684-4	2012	The conformational activation of antithrombin by heparin is a critical step in the inhibition of factor Xa by antithrombin.	Heparin	49-56	serpin family C member 1	Homo sapiens	110-122
2430628-6	1986	It has been shown that the heparin-induced release of Ca2+ diminishes with a decrease in a decrease in Ca2+ concentration.	Heparin	27-34	carbonic anhydrase 2	Homo sapiens	103-106
22453684-5	2012	Despite heparin being the most potent physiological activator which enhances the otherwise very lethargic antithrombin inhibition of factor Xa by approximately 1,000-fold, the conventional heparin therapy poses serious complications because of heparin"s polyanionic nature and its cross-reactivity.	Heparin	8-15	serpin family C member 1	Homo sapiens	106-118
2430628-8	1986	The data obtained suggest that sarcoplasmic reticulum terminal cysterns contain two systems of Ca2+-induced release of Ca2+, i.e., a Mg2+-dependent, caffeine-sensitive and a Mg2+-independent heparin-sensitive ones.	Heparin	191-198	carbonic anhydrase 2	Homo sapiens	95-98
22453684-6	2012	A number of attempts have been carried out in designing alternative non-heparin based conformational activators of antithrombin for factor Xa inhibition.	Heparin	72-79	serpin family C member 1	Homo sapiens	115-127
2430628-8	1986	The data obtained suggest that sarcoplasmic reticulum terminal cysterns contain two systems of Ca2+-induced release of Ca2+, i.e., a Mg2+-dependent, caffeine-sensitive and a Mg2+-independent heparin-sensitive ones.	Heparin	191-198	carbonic anhydrase 2	Homo sapiens	119-122
2430628-9	1986	The mechanism of activation of both systems by caffeine and heparin consists, in all probability, in their increased affinity for Ca2+.	Heparin	60-67	carbonic anhydrase 2	Homo sapiens	130-133
22453684-8	2012	It is assumed that these activators of antithrombin perform their function by binding to heparin binding site.	Heparin	89-96	serpin family C member 1	Homo sapiens	39-51
22453684-9	2012	A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin.	Heparin	45-52	serpin family C member 1	Homo sapiens	87-99
3015922-10	1986	Addition of heparin to hepatic cytosols from mice or rats shifted sedimentation of Ah receptor from approximately equal to 9.5 S to approximately equal to 5.5 S. Molybdate, again, provided stabilization in the approximately equal to 9.5 S form, but only for about one-half the total Ah receptor content in both rat and mouse hepatic cytosols.	Heparin	12-19	aryl hydrocarbon receptor	Rattus norvegicus	83-94
22453684-9	2012	A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin.	Heparin	45-52	serpin family C member 1	Homo sapiens	178-190
3015922-10	1986	Addition of heparin to hepatic cytosols from mice or rats shifted sedimentation of Ah receptor from approximately equal to 9.5 S to approximately equal to 5.5 S. Molybdate, again, provided stabilization in the approximately equal to 9.5 S form, but only for about one-half the total Ah receptor content in both rat and mouse hepatic cytosols.	Heparin	12-19	aryl hydrocarbon receptor	Rattus norvegicus	283-294
22453684-9	2012	A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin.	Heparin	154-161	serpin family C member 1	Homo sapiens	87-99
22453684-9	2012	A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin.	Heparin	154-161	serpin family C member 1	Homo sapiens	178-190
2940243-2	1986	This HS-PG was poorly extracted from cultures by solutions containing 1% Triton X-100 in low salt buffer or by solutions containing 1 M KCl, 4 M urea plus dithiothreitol, 1 mM Tris-HCl, 5 mM EDTA, or 100 micrograms/ml of heparin.	Heparin	221-228	CD44 molecule (Indian blood group)	Homo sapiens	5-10
3754869-10	1986	Thus, S-protein may mediate its effect by scavenging heparin required for ATIII activation.	Heparin	53-60	vitronectin	Homo sapiens	6-15
3740376-5	1986	At the latest eight hours after the beginning of heparin-infusion the steady state of plasma heparin concentration was reached in 100%, but only in 56.67% it equalled the therapeutical factor Xa inhibition-level of 0.10 IE/ml to 0.20 IE/ml (= 0.077 USP-E/ml to 0.154 USP-E/ml).	Heparin	49-56	coagulation factor X	Homo sapiens	185-194
22453684-11	2012	This review summarizes the current literature on the mainstay anticoagulants and non-heparin based antithrombin conformation modulators.	Heparin	85-92	serpin family C member 1	Homo sapiens	99-111
3698718-5	1986	Low-dose heparin acts through its effect of factor Xa and activation of antithrombin III; DHE selectively increases venous smooth muscle tone to accelerate venous blood flow velocity and minimize venous pooling.	Heparin	9-16	coagulation factor X	Homo sapiens	44-53
22742452-0	2012	In silico discovery of a compound with nanomolar affinity to antithrombin causing partial activation and increased heparin affinity.	Heparin	115-122	serpin family C member 1	Homo sapiens	61-73
3458170-2	1986	Radioimmunoassay, using monoclonal antibodies, of fractions from the heparin-Sepharose chromatography showed one peak of EDN activity and two peaks of ECP activity (termed ECP-1 and ECP-2).	Heparin	69-76	ribonuclease A family member 3	Homo sapiens	151-154
3458170-2	1986	Radioimmunoassay, using monoclonal antibodies, of fractions from the heparin-Sepharose chromatography showed one peak of EDN activity and two peaks of ECP activity (termed ECP-1 and ECP-2).	Heparin	69-76	ribonuclease A family member 3	Homo sapiens	172-175
3458170-2	1986	Radioimmunoassay, using monoclonal antibodies, of fractions from the heparin-Sepharose chromatography showed one peak of EDN activity and two peaks of ECP activity (termed ECP-1 and ECP-2).	Heparin	69-76	ribonuclease A family member 3	Homo sapiens	172-175
22742452-2	2012	Heparin is widely used as activator of antithrombin but incurs side effects.	Heparin	0-7	serpin family C member 1	Homo sapiens	39-51
3955063-9	1986	Heparin injected intraperitoneally increased plasma lipoprotein lipase activity to 152 mU/ml, but had no effect on plasma hepatic lipase activity, in unaffected mice.	Heparin	0-7	lipoprotein lipase	Mus musculus	52-70
3955063-12	1986	Heparin injection increased plasma lipoprotein lipase activity in cld/cld mice, but the increment was less than 10% of that in unaffected mice.	Heparin	0-7	lipoprotein lipase	Mus musculus	35-53
22742452-5	2012	Functional studies, fluorescence analysis, and citrullination experiments revealed that TMI induced a partial activation of antithrombin that facilitated the interaction with heparin and low affinity heparins.	Heparin	175-182	serpin family C member 1	Homo sapiens	124-136
22742452-5	2012	Functional studies, fluorescence analysis, and citrullination experiments revealed that TMI induced a partial activation of antithrombin that facilitated the interaction with heparin and low affinity heparins.	Heparin	200-208	serpin family C member 1	Homo sapiens	124-136
22742452-6	2012	TMI improved antithrombin inhibitory function of plasma from homozygous patients with antithrombin deficiency with a heparin binding defect and also in a model with endothelial cells.	Heparin	117-124	serpin family C member 1	Homo sapiens	86-98
3087006-4	1986	Differences between citrate-PRP and heparin-PRP are probably due to citrate inhibition of platelet aggregation, since addition of citrate to heparin-PRP decreased aggregation, while addition of heparin to citrate-PRP did not alter aggregation.	Heparin	36-43	proline rich protein 2-like 1	Rattus norvegicus	44-47
22742452-7	2012	Our in silico screen identified a new, non-polysaccharide scaffold able to interact with the heparin binding domain of antithrombin.	Heparin	93-100	serpin family C member 1	Homo sapiens	119-131
3087006-4	1986	Differences between citrate-PRP and heparin-PRP are probably due to citrate inhibition of platelet aggregation, since addition of citrate to heparin-PRP decreased aggregation, while addition of heparin to citrate-PRP did not alter aggregation.	Heparin	36-43	proline rich protein 2-like 1	Rattus norvegicus	44-47
3087006-4	1986	Differences between citrate-PRP and heparin-PRP are probably due to citrate inhibition of platelet aggregation, since addition of citrate to heparin-PRP decreased aggregation, while addition of heparin to citrate-PRP did not alter aggregation.	Heparin	36-43	proline rich protein 2-like 1	Rattus norvegicus	44-47
22547069-3	2012	It is believed that Stabilin-2 is the primary receptor for the clearance of unfractionated and low molecular weight heparins in the liver.	Heparin	116-124	stabilin 2	Homo sapiens	20-30
3744134-3	1986	Comparison of a low molecular weight heparin, Kabi 2165, revealed that it can inhibit fibrin formation in the extracorporeal circulation, that this property is largely reflected in its anti-factor Xa activity in plasma, and that a useful and effective dose of Kabi 2165 for haemodialysis may be 4,000 anti-factor Xa U intravenous bolus + 750 anti-factor Xa U/h intravenous maintenance infusion.	Heparin	37-44	coagulation factor X	Homo sapiens	190-199
3744134-3	1986	Comparison of a low molecular weight heparin, Kabi 2165, revealed that it can inhibit fibrin formation in the extracorporeal circulation, that this property is largely reflected in its anti-factor Xa activity in plasma, and that a useful and effective dose of Kabi 2165 for haemodialysis may be 4,000 anti-factor Xa U intravenous bolus + 750 anti-factor Xa U/h intravenous maintenance infusion.	Heparin	37-44	coagulation factor X	Homo sapiens	306-315
3744134-3	1986	Comparison of a low molecular weight heparin, Kabi 2165, revealed that it can inhibit fibrin formation in the extracorporeal circulation, that this property is largely reflected in its anti-factor Xa activity in plasma, and that a useful and effective dose of Kabi 2165 for haemodialysis may be 4,000 anti-factor Xa U intravenous bolus + 750 anti-factor Xa U/h intravenous maintenance infusion.	Heparin	37-44	coagulation factor X	Homo sapiens	306-315
22547069-4	2012	Here, we identify the modifications and length of the heparin polymer that are required for binding and endocytosis by both human Stabilin receptors: Stabilin-2 and its homolog Stabilin-1 (also found in liver endothelium).	Heparin	54-61	stabilin 2	Homo sapiens	150-160
22646534-1	2012	BACKGROUND: Membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields soluble HB-EGF, which is an epidermal growth factor receptor (EGFR) ligand, and a carboxy-terminal fragment of HB-EGF (HB-EGF-CTF) after ectodomain shedding.	Heparin	30-37	heparin binding EGF like growth factor	Homo sapiens	93-99
4092689-5	1985	These enzymes could, however, be separated from SF2 by chromatography on heparin-Sepharose.	Heparin	73-80	serine and arginine rich splicing factor 1	Homo sapiens	48-51
22646534-1	2012	BACKGROUND: Membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields soluble HB-EGF, which is an epidermal growth factor receptor (EGFR) ligand, and a carboxy-terminal fragment of HB-EGF (HB-EGF-CTF) after ectodomain shedding.	Heparin	30-37	heparin binding EGF like growth factor	Homo sapiens	116-122
2935971-1	1985	Plasmin and kallikrein but not thrombin cleave purified histidine-rich glycoprotein (HRG), and heparin binding inhibits the proteolysis of HRG.	Heparin	95-102	histidine rich glycoprotein	Homo sapiens	139-142
4086476-9	1985	(1985) Biochemistry 24, 1496-1501) imply that HRG is composed of at least two domains with distinct functional properties; i.e. an amino-terminal domain with heparin-binding ability and a carboxy-terminal domain with heme- and divalent metal-binding abilities.	Heparin	158-165	histidine rich glycoprotein	Homo sapiens	46-49
4069976-3	1985	During the first two hours of exercise the heparin releasable form of LPL was progressively increasing, whereas the heparin unreleasable form of the enzyme was decreasing.	Heparin	43-50	lipoprotein lipase	Canis lupus familiaris	70-73
4069976-5	1985	In the final period of exercise, activity of the heparin releasable form of LPL tended to stabilize on the enhanced level, and activity of the heparin unreleasable form increased.	Heparin	49-56	lipoprotein lipase	Canis lupus familiaris	76-79
4069976-6	1985	In the further series of experiments a relationship between exercise intensity and activity of the heparin releasable form of LPL was studied during 1 h exercise bouts.	Heparin	99-106	lipoprotein lipase	Canis lupus familiaris	126-129
4069976-10	1985	The latter suggestion is based on the reciprocal changes of the heparin releasable and unreleasable (probably intracellular) forms of LPL.	Heparin	64-71	lipoprotein lipase	Canis lupus familiaris	134-137
22646534-1	2012	BACKGROUND: Membrane-anchored heparin-binding epidermal growth factor-like growth factor (proHB-EGF) yields soluble HB-EGF, which is an epidermal growth factor receptor (EGFR) ligand, and a carboxy-terminal fragment of HB-EGF (HB-EGF-CTF) after ectodomain shedding.	Heparin	30-37	heparin binding EGF like growth factor	Homo sapiens	116-122
22008945-8	2012	A bolus of intravenously administered heparin caused a rapid increase in circulating LPL and decreased plasma triglyceride levels in control individuals but not in two GPIHBP1-deficient patients.	Heparin	38-45	lipoprotein lipase	Homo sapiens	85-88
4082106-3	1985	injection of 100 USP units/kg body weight lipoprotein lipase (LPL) activity, and inhibition of factor Xa decreased with a half life twice as long after LMW heparin compared to normal heparin (p less than 0.05).	Heparin	156-163	coagulation factor X	Homo sapiens	95-104
4082106-5	1985	The area under the activity time curve (AUC) of LPL and factor Xa was double with LMW heparin (p less than 0.05).	Heparin	86-93	coagulation factor X	Homo sapiens	56-65
3898072-0	1985	Heparin-treated, v-myc-transformed chicken heart mesenchymal cells assume a normal morphology but are hypersensitive to epidermal growth factor (EGF) and brain fibroblast growth factor (bFGF); cells transformed by the v-Ha-ras oncogene are refractory to EGF and bFGF but are hypersensitive to insulin-like growth factors.	Heparin	0-7	epidermal growth factor	Gallus gallus	120-143
22134617-5	2012	His antithrombin (AT) activity was decreased and DNA sequence analysis revealed heterozygosity for AT Basel (p.Pro41Leu), a variant with impaired heparin binding.	Heparin	146-153	serpin family C member 1	Homo sapiens	4-16
2410295-0	1985	Heparin induces Ca2+ release from the terminal cisterns of skeletal muscle sarcoplasmic reticulum.	Heparin	0-7	carbonic anhydrase 2	Homo sapiens	16-19
22134617-5	2012	His antithrombin (AT) activity was decreased and DNA sequence analysis revealed heterozygosity for AT Basel (p.Pro41Leu), a variant with impaired heparin binding.	Heparin	146-153	serpin family C member 1	Homo sapiens	99-101
2410295-2	1985	It was shown that heparin (0.5-10 micrograms/ml) causes a rapid release of 40-50 nmol Ca2+/mg protein from the terminal cistern SR vesicles bound to 130-150 nmol/mg protein of Ca2+ in the presence of ATP.	Heparin	18-25	carbonic anhydrase 2	Homo sapiens	86-89
2410295-2	1985	It was shown that heparin (0.5-10 micrograms/ml) causes a rapid release of 40-50 nmol Ca2+/mg protein from the terminal cistern SR vesicles bound to 130-150 nmol/mg protein of Ca2+ in the presence of ATP.	Heparin	18-25	carbonic anhydrase 2	Homo sapiens	176-179
22083130-0	2012	Cooperative folding of tau peptide by coordination of group IIB metal cations during heparin-induced aggregation.	Heparin	85-92	microtubule associated protein tau	Homo sapiens	23-26
2410295-6	1985	When the Ca2+ release is induced by heparin, no Ca2+-induced release of Ca2+ takes place.	Heparin	36-43	carbonic anhydrase 2	Homo sapiens	9-12
22268819-11	2012	In addition, heparin, heparinoid, serpins and alpha(2)-macroglobulin, which all bind to HNPs, blocked HNP-1-induced platelet activation in contrast to direct thrombin inhibitors such as hirudin.	Heparin	13-20	HNP1	Homo sapiens	102-107
3884609-3	1985	These adipose cells were previously shown to secrete lipoprotein lipase during exposure to heparin.	Heparin	91-98	lipoprotein lipase	Mus musculus	53-71
4002198-9	1985	The incomplete inhibitory effect of protamine chloride on LPL, HTGL and factor Xa activities of LMW heparin indicate that protamine chloride requires more than 14 saccharide units in the heparin molecule for interaction.	Heparin	100-107	coagulation factor X	Homo sapiens	72-81
22334695-10	2012	EMILIN-3 was found to bind heparin with high affinity, a property mediated by the EMI domain, thus revealing a new function for this domain that may contribute to the interaction of EMILIN-3 with other extracellular matrix and/or cell surface molecules.	Heparin	27-34	elastin microfibril interfacer 3	Mus musculus	0-8
3926759-2	1985	They were named RNase K1 and RNase K2 in order of elution from the heparin-Sepharose column.	Heparin	67-74	ribonuclease A family member k6	Bos taurus	29-37
22334695-10	2012	EMILIN-3 was found to bind heparin with high affinity, a property mediated by the EMI domain, thus revealing a new function for this domain that may contribute to the interaction of EMILIN-3 with other extracellular matrix and/or cell surface molecules.	Heparin	27-34	elastin microfibril interfacer 3	Mus musculus	182-190
22194593-6	2012	Mechanistic studies revealed that heparin inhibits L- and P-selectin, as well as the chemokine CXCL12, leading to leukocytosis.	Heparin	34-41	selectin P	Homo sapiens	58-68
2982601-2	1985	Human plasma fibronectin is composed of at least five distinct domains which we refer to as Hep-1/Fib-1, Gel, Cell, Hep-2 and Fib-2 depending on their affinity for heparin (Hep), gelatin (Gel), the cell surface (Cell) or fibrin (Fib).	Heparin	164-171	DNL-type zinc finger	Homo sapiens	92-97
2982601-2	1985	Human plasma fibronectin is composed of at least five distinct domains which we refer to as Hep-1/Fib-1, Gel, Cell, Hep-2 and Fib-2 depending on their affinity for heparin (Hep), gelatin (Gel), the cell surface (Cell) or fibrin (Fib).	Heparin	164-171	dachsous cadherin-related 1	Homo sapiens	98-103
22194593-8	2012	We conclude that heparin-induced leukocytosis requires glucosamine 6-O-sulfation and is caused by blockade of L-selectin-, P-selectin-, and CXCL12-mediated leukocyte trafficking.	Heparin	17-24	selectin L	Homo sapiens	110-120
22194593-8	2012	We conclude that heparin-induced leukocytosis requires glucosamine 6-O-sulfation and is caused by blockade of L-selectin-, P-selectin-, and CXCL12-mediated leukocyte trafficking.	Heparin	17-24	selectin P	Homo sapiens	123-133
3965047-10	1985	These results indicate that the antithrombotic effect achieved by inhibiting factor Xa is limited and that better antithrombotic effects are achieved by heparin or heparin-like substances capable of influencing the inactivation and/or the generation of thrombin.	Heparin	164-171	prothrombin	Oryctolagus cuniculus	253-261
22149666-2	2012	An antithrombin-heparin (ATH) covalent complex was subsequently attached to the free PEO chain ends, which had been functionalized with N-hydroxysuccinimide (NHS) groups.	Heparin	16-23	serpin family C member 1	Homo sapiens	3-15
3158644-4	1985	The inhibitory substances from the supernatant of the thrombin-induced aggregates were separated into two major fractions, a low affinity fraction and a high affinity fraction, on a heparin-Sepharose column.	Heparin	182-189	coagulation factor II, thrombin	Bos taurus	54-62
6210287-6	1984	The order of these fragments within the vitronectin polypeptides was determined by comparison of the NH2-terminal sequences of the polypeptides and their fragments, by further cleavage of the largest fragments with BrCN or 70% formic acid, and by assaying for heparin-binding and cell-attachment activities.	Heparin	260-267	vitronectin	Homo sapiens	40-51
6498233-0	1984	Resolution of the molecular forms of rat liver glucocorticoid receptor by affinity chromatography on immobilized heparin.	Heparin	113-120	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	47-70
6498233-1	1984	Rat liver cytosolic glucocorticoid receptor labelled with [3H] dexamethasone and stabilized with molybdate was bound to heparin-ultrogel and eluted with NaCl or heparin as a single peak of radioactivity.	Heparin	120-127	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	20-43
6498233-4	1984	The results presented here suggest that the two forms eluted from heparin-agarose correspond to the untransformed and transformed states of the glucocorticoid receptor complex.	Heparin	66-73	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	144-167
2556813-0	1989	The relationship between anti-factor Xa level and clinical outcome in patients receiving enoxaparine low molecular weight heparin to prevent deep vein thrombosis after hip replacement.	Heparin	122-129	coagulation factor X	Homo sapiens	30-39
2481855-5	1989	This study establishes: (1) the cynomolgus monkey as a model for PAPP-A studies, (2) that haemochorially implanted placentae produce PAPP-A, a heparin-binding inhibitor of HGE, (3) that administration of progesterone receptor antagonist suppressed placental PAPP-A synthesis, and (4) disrupted protease-protease inhibitor equilibrium at the feto-maternal interface.	Heparin	143-150	pappalysin-1	Macaca fascicularis	133-139
2481855-5	1989	This study establishes: (1) the cynomolgus monkey as a model for PAPP-A studies, (2) that haemochorially implanted placentae produce PAPP-A, a heparin-binding inhibitor of HGE, (3) that administration of progesterone receptor antagonist suppressed placental PAPP-A synthesis, and (4) disrupted protease-protease inhibitor equilibrium at the feto-maternal interface.	Heparin	143-150	pappalysin-1	Macaca fascicularis	133-139
2791981-4	1989	However, in the Ob cultures, bFGF was intrinsically 10-fold more stimulatory than aFGF, whereas heparin enhanced the mitotic response only to aFGF.	Heparin	96-103	fibroblast growth factor 1	Rattus norvegicus	142-146
21930168-7	2012	In vivo studies on jugular vein rat thrombosis model showed that the clot lysis of the heparin-triggered camouflaged tPA group was equivalent to the tPA+heparin group without prolongation of activated partial thromboplastin time (aPTT) before and after the treatment.	Heparin	87-94	plasminogen activator, tissue type	Rattus norvegicus	117-120
2552660-6	1989	The 31-kDa D12L protein copurified with the virus capping enzyme through chromatography on heparin-agarose and phosphocellulose and also cosedimented with the capping enzyme through a glycerol density gradient.	Heparin	91-98	small subunit of mRNA capping enzyme	Vaccinia virus	11-15
2475499-1	1989	Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces.	Heparin	121-128	vitronectin	Homo sapiens	0-20
6425408-6	1984	The ability of heparin to block the activation function of chymase without inhibition of esterase activity reveals a possible physiologic regulatory mechanism for limiting the potential action of secreted chymase.	Heparin	15-22	chymase 1	Rattus norvegicus	59-66
6425408-6	1984	The ability of heparin to block the activation function of chymase without inhibition of esterase activity reveals a possible physiologic regulatory mechanism for limiting the potential action of secreted chymase.	Heparin	15-22	chymase 1	Rattus norvegicus	205-212
2475499-1	1989	Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces.	Heparin	121-128	vitronectin	Homo sapiens	24-35
21930168-7	2012	In vivo studies on jugular vein rat thrombosis model showed that the clot lysis of the heparin-triggered camouflaged tPA group was equivalent to the tPA+heparin group without prolongation of activated partial thromboplastin time (aPTT) before and after the treatment.	Heparin	87-94	plasminogen activator, tissue type	Rattus norvegicus	149-152
22566218-4	2012	In 1976, it was found that only one third of heparin chains bound with high affinity to antithrombin, and subsequent studies identified a unique pentasaccharide sequence, which was essential for antithrombin binding and anticoagulant activity - this pentasaccharide was synthesised in 1983.	Heparin	45-52	serpin family C member 1	Homo sapiens	88-100
6331390-6	1984	Cytochrome b-245 was chromatographed on a column of heparin-agarose and eluted with NaCl to give a peak specific content of 11-16 nmol of cytochrome b-245/mg of protein, representing a 140-200-fold purification with a recovery of 15%.	Heparin	52-59	mitochondrially encoded cytochrome b	Homo sapiens	0-12
22509483-0	2012	Structural basis of heparin binding to camel peptidoglycan recognition protein-S. Short peptidoglycan recognition protein (PGRP-S) is a member of the innate immunity system in mammals.	Heparin	20-27	LOW QUALITY PROTEIN: peptidoglycan recognition protein 1	Camelus dromedarius	123-129
6422851-6	1984	In the presence of heparin the inhibition of thrombin as well as factor Xa was enhanced.	Heparin	19-26	coagulation factor X	Homo sapiens	65-74
2547648-9	1989	Heparins with high and low affinity for antithrombin III both inhibited Ins 1,4,5-P3 binding.	Heparin	0-8	serpin family C member 1	Rattus norvegicus	40-56
21984036-0	2012	Regulation of PMA-induced MUC5AC expression by heparin in human bronchial epithelial cells.	Heparin	47-54	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	26-32
2738078-5	1989	Bioactivity of the immobilized conjugate (heparin activity) was measured in terms of increased clotting times (thrombin time assay) and for the inactivation of Factor Xa.	Heparin	42-49	coagulation factor X	Homo sapiens	160-169
6382161-8	1984	The two most probable sites of action of heparin are: inhibition of thrombin and frustration of the feedback loops and/or inhibition of factor Xa.	Heparin	41-48	coagulation factor X	Homo sapiens	136-145
21984036-4	2012	Here, we hypothesized that heparin has some influence on the expression of mucin 5AC (MUC5AC) induced by phorbol myristate acetate (PMA) in a bronchial epithelial cell line (HBE16), also we have investigated the potential mechanism involved in the process.	Heparin	27-34	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	75-84
21984036-4	2012	Here, we hypothesized that heparin has some influence on the expression of mucin 5AC (MUC5AC) induced by phorbol myristate acetate (PMA) in a bronchial epithelial cell line (HBE16), also we have investigated the potential mechanism involved in the process.	Heparin	27-34	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	86-92
6710943-1	1984	Content of antithrombin III in blood was decreased by 30-40% as compared with the initial level after eight intravenous injections of heparin (40 IU/200 g of body mass) into healthy rats and into animals with experimental atherosclerosis.	Heparin	134-141	serpin family C member 1	Rattus norvegicus	11-27
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	118-124
6710943-2	1984	The maximal decrease of antithrombin III content was found within 30 min after the last administration of heparin in circulation.	Heparin	106-113	serpin family C member 1	Rattus norvegicus	24-40
6710943-3	1984	Normalization of the antithrombin III occurred within 1.5-4 hrs after the heparin administration.	Heparin	74-81	serpin family C member 1	Rattus norvegicus	21-37
6710943-4	1984	Decrease in the content of antithrombin III after the heparin administration was accompanied by elevation in total fibrinolytic activity and in nonenzymatic fibrinolysis, thus indicating apparently the transient formation of heparin-blood proteins complexes including antithrombin III.	Heparin	54-61	serpin family C member 1	Rattus norvegicus	27-43
6710943-4	1984	Decrease in the content of antithrombin III after the heparin administration was accompanied by elevation in total fibrinolytic activity and in nonenzymatic fibrinolysis, thus indicating apparently the transient formation of heparin-blood proteins complexes including antithrombin III.	Heparin	54-61	serpin family C member 1	Rattus norvegicus	268-284
6607710-4	1983	The purified vertebrate inhibitors all show the following physical and functional homologies to human antithrombin: (i) heparin-enhanced inhibition of both bovine thrombin and human Factor Xa, (ii) molecular masses of approximately 60,000, and (iii) heparin-induced increases in ultraviolet fluorescence.	Heparin	120-127	coagulation factor II, thrombin	Bos taurus	106-114
6607710-4	1983	The purified vertebrate inhibitors all show the following physical and functional homologies to human antithrombin: (i) heparin-enhanced inhibition of both bovine thrombin and human Factor Xa, (ii) molecular masses of approximately 60,000, and (iii) heparin-induced increases in ultraviolet fluorescence.	Heparin	120-127	coagulation factor X	Homo sapiens	182-191
6630199-1	1983	Serum spreading factor (SF) was isolated from human serum by a four-step procedure employing affinity chromatography on glass beads, concanavalin A-Sepharose, DEAE-agarose, and heparin-agarose.	Heparin	177-184	vitronectin	Homo sapiens	0-27
2785417-5	1989	However, when heparin was less than saturating, we observed that various heparin preparations affected the AT III-induced inactivation of factor XIa to different degrees even though they exhibited the same inhibitory activity (1 U/mL) against thrombin.	Heparin	73-80	coagulation factor II, thrombin	Bos taurus	243-251
2713384-3	1989	It was observed that lipoprotein lipase accounted for most of the triglyceride hydrolase activity in the heparin-treated plasma, and that the heparin-releasable activities caused an increase in HDL density but no measurable change in particle size when LCAT was inhibited.	Heparin	142-149	lecithin cholesterol acyltransferase	Rattus norvegicus	253-257
2713384-6	1989	Subsequent incubation for 18 h at 37 degrees C produced marked increases in the apoE content of HDL from heparin-treated plasma even when LCAT was inhibited.	Heparin	105-112	lecithin cholesterol acyltransferase	Rattus norvegicus	138-142
2713384-7	1989	Time-course studies showed that in the presence of an LCAT inhibitor there was considerable conversion of phosphatidylcholine to lysophosphatidylcholine in heparin-treated plasma, and that this activity was diminished by 1 M NaCl, but that no phospholipolysis was observed in control plasma.	Heparin	156-163	lecithin cholesterol acyltransferase	Rattus norvegicus	54-58
2725510-8	1989	These differences should significantly affect the secondary structure and heparin-binding properties of the protein based on considerations of the bovine PF4 crystal structure.	Heparin	74-81	platelet factor 4	Bos taurus	154-157
2543098-0	1989	Effect of rabbit thrombomodulin on thrombin inhibition by antithrombin in the presence of heparin.	Heparin	90-97	prothrombin	Oryctolagus cuniculus	35-43
2543098-4	1989	The acidic form (retarded on ion-exchange chromatography) of thrombomodulin is now shown to prevent the rapid inactivation of thrombin by antithrombin in the presence of heparin, presumably by preventing the formation of the ternary thrombin-AT-heparin complex.	Heparin	170-177	prothrombin	Oryctolagus cuniculus	126-134
2543098-4	1989	The acidic form (retarded on ion-exchange chromatography) of thrombomodulin is now shown to prevent the rapid inactivation of thrombin by antithrombin in the presence of heparin, presumably by preventing the formation of the ternary thrombin-AT-heparin complex.	Heparin	170-177	prothrombin	Oryctolagus cuniculus	142-150
2543098-8	1989	It is concluded that the acidic domain of rabbit thrombomodulin, a chondroitin (dermatan) sulfate glycosaminoglycan, interacts with a site of the thrombin molecule that is not involved in the protein C activation cofactor function, but is essential to the cleavage of fibrinogen or binding of heparin.	Heparin	293-300	prothrombin	Oryctolagus cuniculus	146-154
6631307-6	1983	Androgen-receptor complexes obtained from nuclease-sensitive or nuclease-resistant regions by extraction with KCl or heparin were indistinguishable by routine sedimentation analysis.	Heparin	117-124	androgen receptor	Rattus norvegicus	0-17
21984036-6	2012	After pretreatment with heparin however, there was a significant decrease in ROS levels, the mRNA of Duox1, EGFR, and MUC5AC, and the protein levels of Duox1, p-EGFR, EGFR, and MUC5AC, when compared with the PMA group (all P &lt; 0.01).	Heparin	24-31	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	177-183
21984036-7	2012	MUC5AC protein in the supernatant was inhibited in a dose-dependent manner by heparin.	Heparin	78-85	mucin 5AC, oligomeric mucus/gel-forming	Homo sapiens	0-6
22026648-3	2012	We found that MEK-ERK signaling is necessary for their cell-cycle entry, and signaling pathways whose activities can be modulated by heparin, such as Wnt-, Shh-, and thrombin-mediated pathways, are capable of regulating the cell-cycle entry.	Heparin	133-140	sonic hedgehog signaling molecule	Homo sapiens	156-159
6554235-1	1983	Neutralization of the negative charges of heparin by polycations in the fluid phase suppressed the inhibitory effect of heparin on the generation of the C3b-dependent amplification convertase of complement C3b,Bb.	Heparin	42-49	complement C3	Homo sapiens	153-156
6554235-1	1983	Neutralization of the negative charges of heparin by polycations in the fluid phase suppressed the inhibitory effect of heparin on the generation of the C3b-dependent amplification convertase of complement C3b,Bb.	Heparin	42-49	complement C3	Homo sapiens	206-209
6554235-1	1983	Neutralization of the negative charges of heparin by polycations in the fluid phase suppressed the inhibitory effect of heparin on the generation of the C3b-dependent amplification convertase of complement C3b,Bb.	Heparin	120-127	complement C3	Homo sapiens	153-156
6554235-1	1983	Neutralization of the negative charges of heparin by polycations in the fluid phase suppressed the inhibitory effect of heparin on the generation of the C3b-dependent amplification convertase of complement C3b,Bb.	Heparin	120-127	complement C3	Homo sapiens	206-209
6222069-7	1983	On this basis, we suggest that high in vivo rates of thrombin generation may lead to the sequestration of Factor Xa on the platelet surface and hence allow this serine protease to resist the action of heparin until the complex is cleared from the circulation.	Heparin	201-208	coagulation factor X	Homo sapiens	106-115
2465300-1	1989	The mechanism(s) by which heparin influences the biological activities of acidic and basic fibroblast growth factors (aFGF and bFGF) is not completely understood.	Heparin	26-33	fibroblast growth factor 1	Rattus norvegicus	118-122
2465300-2	1989	One mechanism by which heparin could alter the biological activities of aFGF and bFGF is by altering their biological half-lives.	Heparin	23-30	fibroblast growth factor 1	Rattus norvegicus	72-76
2465300-3	1989	We investigated the possibility that heparin potentiates aFGF-induced neurite outgrowth from PC12 cells by prolonging its biological half-life.	Heparin	37-44	fibroblast growth factor 1	Rattus norvegicus	57-61
2465300-4	1989	Under conditions where heparin potentiated aFGF-induced neurite outgrowth, we observed that heparin increased the biological half-life of aFGF from 7 to 39 hr.	Heparin	23-30	fibroblast growth factor 1	Rattus norvegicus	43-47
2465300-4	1989	Under conditions where heparin potentiated aFGF-induced neurite outgrowth, we observed that heparin increased the biological half-life of aFGF from 7 to 39 hr.	Heparin	23-30	fibroblast growth factor 1	Rattus norvegicus	138-142
2465300-4	1989	Under conditions where heparin potentiated aFGF-induced neurite outgrowth, we observed that heparin increased the biological half-life of aFGF from 7 to 39 hr.	Heparin	92-99	fibroblast growth factor 1	Rattus norvegicus	43-47
2713873-10	1989	This is particularly significant as regards the mechanism of action of heparin, because the synthetic pentasaccharide activates ATIII towards Factor Xa, but not towards thrombin.	Heparin	71-78	coagulation factor X	Homo sapiens	142-151
2912214-2	1989	This FGF-like activity in the cerebrospinal fluid was bioassayed in two systems: depression of the feeding response of Hydra and DNA synthesis-stimulating activity in BALB/c 3T3 cells after fractionation on a heparin affinity column.	Heparin	209-216	fibroblast growth factor 1	Rattus norvegicus	5-8
2463827-2	1989	Twelve known heparin-binding sequences in vitronectin, apolipoproteins E and B-100, and platelet factor 4 were used to formulate two search strings for identifying potential heparin-binding regions in other proteins.	Heparin	13-20	vitronectin	Homo sapiens	42-53
6339618-8	1983	In the presence of heparin, another component of the mast cell secretory granule, the rate of appearance and the distribution of C3 cleavage fragments as assessed in SDS polyacrylamide gels are not appreciably changed with the exception that no C3a material can be detected in the SDS polyacrylamide gels or by radioimmunoassay and bioassay of the unresolved reaction mixture.	Heparin	19-26	complement C3	Homo sapiens	245-248
6339618-9	1983	Enhanced catabolism of authentic C3a by tryptase occurs in the presence of heparin and by analogy when C3a is generated from C3 by tryptase in the presence of heparin.	Heparin	75-82	complement C3	Homo sapiens	33-36
6339618-9	1983	Enhanced catabolism of authentic C3a by tryptase occurs in the presence of heparin and by analogy when C3a is generated from C3 by tryptase in the presence of heparin.	Heparin	159-166	complement C3	Homo sapiens	33-36
6339618-9	1983	Enhanced catabolism of authentic C3a by tryptase occurs in the presence of heparin and by analogy when C3a is generated from C3 by tryptase in the presence of heparin.	Heparin	159-166	complement C3	Homo sapiens	103-106
6822493-5	1983	Differences between thrombin and Factor Xa at low (nanomolar) concentrations of heparin were evident in this rate constant and the relative affinities for the heparin-antithrombin complex (Km for Factor Xa = 100 nM; Km for thrombin less than or equal to 2 nM).	Heparin	80-87	coagulation factor X	Homo sapiens	196-205
6822493-7	1983	At high heparin concentrations (micromolar), the kinetic parameters for Factor Xa were unchanged but the Km for thrombin increased dramatically to 100 nM.	Heparin	8-15	coagulation factor X	Homo sapiens	72-81
2463827-2	1989	Twelve known heparin-binding sequences in vitronectin, apolipoproteins E and B-100, and platelet factor 4 were used to formulate two search strings for identifying potential heparin-binding regions in other proteins.	Heparin	174-181	vitronectin	Homo sapiens	42-53
2562205-2	1989	More recently, assays have been developed which measure the inhibitory action of heparin on isolated coagulation enzymes, notably Factor Xa and thrombin, using specific amidolytic peptide substrates.	Heparin	81-88	coagulation factor X	Homo sapiens	130-139
22912725-11	2012	Our results suggest that Egr1 activates HGF-induced cell invasion through the regulation of MMPs in HCC cells and heparin inhibits HGF-induced cellular invasion via the downregulation of Egr1.	Heparin	114-121	early growth response 1	Homo sapiens	187-191
2530427-6	1989	Antithrombin III inhibition of activated Hageman factor is augmented by heparin which is also an activator of Hageman factor.	Heparin	72-79	coagulation factor XII	Homo sapiens	41-55
2530427-6	1989	Antithrombin III inhibition of activated Hageman factor is augmented by heparin which is also an activator of Hageman factor.	Heparin	72-79	coagulation factor XII	Homo sapiens	110-124
6845275-6	1983	The catalytic activity of thrombin is inhibited by heparin.	Heparin	51-58	coagulation factor II, thrombin	Bos taurus	26-34
21895488-2	2012	We have employed a freely interconnecting porous scaffold developed by us to determine the utility of a covalently bound heparin surface coating for the delivery of vascular endothelial growth factor (VEGF) and platelet-derived growth factor BB (PDGF-BB) in vivo.	Heparin	121-128	vascular endothelial growth factor A	Rattus norvegicus	165-199
6184096-4	1983	Antithrombin-heparin cofactor, which eluted from heparin-agarose with buffer containing 0.4 M NaCl and did not cross-react with antibody specific for antithrombin III and did not inhibit factor Xa at an appreciable rate in the presence of heparin, was designated heparin cofactor A.	Heparin	13-20	tubulin folding cofactor A	Homo sapiens	271-281
6373139-12	1983	Employing human and bovine thrombin; bovine and human Xa with their respective substrates, the absolute quantitation of heparin is satisfactorily carried out, however, these assays only measure heparin concentrations and do not reflect the overall anticoagulant effect of heparin.	Heparin	120-127	coagulation factor II, thrombin	Bos taurus	27-35
6923655-4	1982	A significant reduction of kallikrein and antiplasmin in per- and post-operative periods was observed in the control patients compared with the heparin-treated patients, while there was a significant reduction of anti-thrombin III in the control patients compared with the treated patients only in the per-operative period.	Heparin	144-151	kallikrein related peptidase 4	Homo sapiens	27-37
2976993-3	1988	S protein significantly counteracted the anticoagulant activity of heparin and pentosan polysulfate but not of dermatan sulfate.	Heparin	67-74	vitronectin	Homo sapiens	0-9
2976993-4	1988	In the presence of 0.3 micrograms/ml heparin, 0.5 micrograms/ml pentosan polysulfate, or 2 micrograms/ml dermatan sulfate, S protein induced a concentration-dependent reduction of the inhibition rate of thrombin by heparin cofactor II.	Heparin	37-44	vitronectin	Homo sapiens	123-132
2976993-4	1988	In the presence of 0.3 micrograms/ml heparin, 0.5 micrograms/ml pentosan polysulfate, or 2 micrograms/ml dermatan sulfate, S protein induced a concentration-dependent reduction of the inhibition rate of thrombin by heparin cofactor II.	Heparin	215-222	vitronectin	Homo sapiens	123-132
2976993-6	1988	Exposure of the glycosaminoglycan-binding region of S protein by reduction and carboxymethylation of the protein increased the neutralizing activity of S protein towards heparin and pentosan polysulfate.	Heparin	170-177	vitronectin	Homo sapiens	52-61
2976993-6	1988	Exposure of the glycosaminoglycan-binding region of S protein by reduction and carboxymethylation of the protein increased the neutralizing activity of S protein towards heparin and pentosan polysulfate.	Heparin	170-177	vitronectin	Homo sapiens	152-161
21895488-2	2012	We have employed a freely interconnecting porous scaffold developed by us to determine the utility of a covalently bound heparin surface coating for the delivery of vascular endothelial growth factor (VEGF) and platelet-derived growth factor BB (PDGF-BB) in vivo.	Heparin	121-128	vascular endothelial growth factor A	Rattus norvegicus	201-205
7112518-0	1982	Demonstration of a direct anti-factor Xa activity in certain heparin-related glycosaminoglycans.	Heparin	61-68	coagulation factor X	Homo sapiens	31-40
7115310-2	1982	Intravenous injection of heparin into the trout resulted in the appearance in the plasma of a lipase with the properties of lipoprotein lipase.	Heparin	25-32	lipoprotein lipase	Oncorhynchus mykiss	124-142
6279617-8	1982	The enzyme phosphorylated phosvitin, casein, and glycogen synthase but not histone or phosphorylase and was inhibited by heparin.	Heparin	121-128	casein kinase II subunit beta	Oryctolagus cuniculus	26-35
3209587-5	1988	The factor from NT2/D1 EC cells, bovine FGFb and FGFb produced by the human hepatoma cell line SK-HEP-1 elute from heparin at similar salt concentrations.	Heparin	115-122	DNL-type zinc finger	Homo sapiens	98-103
2851882-3	1988	The neutralizing effect of protamine chloride on the inhibition of factor Xa (clot test) was 95% for conventional heparin and 55% for low molecular weight heparin, whereas the effect of both heparin preparations on the thrombin inhibition could be completely neutralized.	Heparin	114-121	coagulation factor X	Homo sapiens	67-76
2851882-3	1988	The neutralizing effect of protamine chloride on the inhibition of factor Xa (clot test) was 95% for conventional heparin and 55% for low molecular weight heparin, whereas the effect of both heparin preparations on the thrombin inhibition could be completely neutralized.	Heparin	155-162	coagulation factor X	Homo sapiens	67-76
7101245-4	1982	Heparin also inhibited platelet aggregation, release of (14C) 5-HT and production of malondialdehyde in response to collagen and thrombin.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	129-137
2851882-3	1988	The neutralizing effect of protamine chloride on the inhibition of factor Xa (clot test) was 95% for conventional heparin and 55% for low molecular weight heparin, whereas the effect of both heparin preparations on the thrombin inhibition could be completely neutralized.	Heparin	155-162	coagulation factor X	Homo sapiens	67-76
21895488-3	2012	The heparin surface was shown to release VEGF far more rapidly than PDGF-BB in vitro (VEGF: 75 ng/h for 24 h; PDGF-BB: 86 pg/h for &gt;7 days).	Heparin	4-11	vascular endothelial growth factor A	Rattus norvegicus	41-45
7060276-3	1982	The effect of intravenous administration of 100 U/kg of heparin on LCAT activity was examined in 21 haemodialysis patients and 19 normal subjects.	Heparin	56-63	lecithin-cholesterol acyltransferase	Homo sapiens	67-71
21895488-3	2012	The heparin surface was shown to release VEGF far more rapidly than PDGF-BB in vitro (VEGF: 75 ng/h for 24 h; PDGF-BB: 86 pg/h for &gt;7 days).	Heparin	4-11	vascular endothelial growth factor A	Rattus norvegicus	86-90
21895488-9	2012	Thus, the covalent modification of a porous scaffold with heparin allows for the differential release of VEGF and PDGF-BB that results in both a rapid and sustained increase in scaffold vascularization.	Heparin	58-65	vascular endothelial growth factor A	Rattus norvegicus	105-109
7060276-4	1982	Heparin inhibited LCAT activity by increasing plasma free fatty acid concentrations.	Heparin	0-7	lecithin-cholesterol acyltransferase	Homo sapiens	18-22
2848523-0	1988	Influence of heparin fragments on the biological activities of elastase(s) and alpha 1 proteinase inhibitor.	Heparin	13-20	serpin family A member 1	Rattus norvegicus	79-107
22328880-3	2011	RESULTS: Heparin caused a high PAPP-A increase in ACS-STE patients, in all patients with heparin without ACS and angiographic signs of significant atherosclerosis.	Heparin	9-16	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	50-53
3262615-3	1988	In the absence of heparin, the second-order rate constant of inhibition of factor Xa generated by factor IXa was 2.5-fold lower than the rate constant of inhibition of exogenous factor Xa.	Heparin	18-25	coagulation factor X	Homo sapiens	75-84
7336661-1	1981	A procedure is described for isolation of prethrombin I using biospecific chromatography of the thrombin hydrolysate of prothrombin complex on heparin-Sepharose.	Heparin	143-150	prothrombin	Oryctolagus cuniculus	45-53
7336661-1	1981	A procedure is described for isolation of prethrombin I using biospecific chromatography of the thrombin hydrolysate of prothrombin complex on heparin-Sepharose.	Heparin	143-150	prothrombin	Oryctolagus cuniculus	120-131
3262615-7	1988	With unfractionated heparin above 40 ng/ml and antithrombin III at 200 nM, the apparent second-order rate constant of inhibition of exogenous and generated factor Xa were the same.	Heparin	20-27	coagulation factor X	Homo sapiens	156-165
21946214-0	2011	Low molecular weight heparin downregulates tissue factor expression and activity by modulating growth factor receptor-mediated induction of nuclear factor-kappaB.	Heparin	21-28	coagulation factor III, tissue factor	Homo sapiens	43-56
2852498-8	1988	PCI also blocks the amidolytic activities of urokinase plasminogen activator (u-PA), thrombin and factor Xa on their chromogenic substrates in a heparin-dependent manner.	Heparin	145-152	coagulation factor X	Homo sapiens	98-107
7302926-0	1981	The sensitivity of human and bovine thrombin to heparin in plasma.	Heparin	48-55	coagulation factor II, thrombin	Bos taurus	36-44
7292448-0	1981	Influence of variations in the chemical structure of heparin on its anticoagulant and anti-factor Xa activities.	Heparin	53-60	coagulation factor X	Homo sapiens	91-100
21946214-2	2011	In this study, the influence of low molecular weight heparin (LMWH) on tissue factor (TF) expression and activity in five cell lines from various tissues was analysed and explored.	Heparin	53-60	coagulation factor III, tissue factor	Homo sapiens	71-84
21946214-2	2011	In this study, the influence of low molecular weight heparin (LMWH) on tissue factor (TF) expression and activity in five cell lines from various tissues was analysed and explored.	Heparin	53-60	coagulation factor III, tissue factor	Homo sapiens	86-88
3045234-5	1988	Platelet factor 4 inhibited activation of Hageman factor by ellagic acid, as measured by amidolysis of a synthetic substrate of activated Hageman factor, an effect inhibited by heparin or by an anti-platelet factor 4 antiserum.	Heparin	177-184	coagulation factor XII	Homo sapiens	42-56
3045234-5	1988	Platelet factor 4 inhibited activation of Hageman factor by ellagic acid, as measured by amidolysis of a synthetic substrate of activated Hageman factor, an effect inhibited by heparin or by an anti-platelet factor 4 antiserum.	Heparin	177-184	coagulation factor XII	Homo sapiens	138-152
7005084-1	1980	Interactions of glucocorticoids and heparin on the humoral immune response of mice to SRBC have been studied.	Heparin	36-43	caveolae associated 3	Mus musculus	86-90
21978664-0	2011	Heparin activates PKR by inducing dimerization.	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	18-21
7005084-3	1980	Cortisone (ip) and heparin (sc) per se injected at about the time of immunization with suboptimal doses of SRBC resulted only in a slight stimulating or no effect on spleen PFC count and serum antibody level.	Heparin	19-26	caveolae associated 3	Mus musculus	107-111
7005084-4	1980	Cortisone and heparin applied in combination, however, exerted a stimulatory effect on the humoral immune response to SRBC.	Heparin	14-21	caveolae associated 3	Mus musculus	118-122
2460263-0	1988	Novel purification of vitronectin from human plasma by heparin affinity chromatography.	Heparin	55-62	vitronectin	Homo sapiens	22-33
21978664-4	2011	PKR is also activated by heparin, a highly sulfated glycosaminoglycan.	Heparin	25-32	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	0-3
2460263-2	1988	We developed a strikingly simple method to purify vitronectin from human plasma by heparin affinity chromatography.	Heparin	83-90	vitronectin	Homo sapiens	50-61
21978664-5	2011	We have used biophysical methods to define the mechanism of PKR activation by heparin.	Heparin	78-85	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	60-63
2460263-4	1988	The heparin-binding activity of vitronectin in human serum was activated with 8 M urea.	Heparin	4-11	vitronectin	Homo sapiens	32-43
2460263-5	1988	The activated vitronectin specifically bound to heparin-Sepharose in 8 M urea and was eluted with 0.5 M NaCl containing 8 M urea.	Heparin	48-55	vitronectin	Homo sapiens	14-25
3415672-1	1988	Leucocyte proteinases, e.g. leucocyte elastase and cathepsin G, are inhibited by heparin.	Heparin	81-88	cathepsin G	Sus scrofa	51-62
7210056-0	1980	Inhibition of nucleic acid and chromatin binding of the rat prostate androgen receptor by pyridoxal phosphate, heparin and Cibacron blue.	Heparin	111-118	androgen receptor	Rattus norvegicus	69-86
7349668-5	1980	Thrombin and Factor Xa were instantaneously inhibited by AT III in the presence of soluble heparin.	Heparin	91-98	coagulation factor X	Homo sapiens	13-22
6771334-5	1980	Inhibition of chymase by serotonin stored in its active site and of chymase and acid hydrolases by their interaction with heparin probably occurs.	Heparin	122-129	chymase 1	Rattus norvegicus	14-21
21978664-6	2011	Heparins as short as hexasaccharide bind strongly to PKR and activate autophosphorylation.	Heparin	0-8	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	53-56
6771334-5	1980	Inhibition of chymase by serotonin stored in its active site and of chymase and acid hydrolases by their interaction with heparin probably occurs.	Heparin	122-129	chymase 1	Rattus norvegicus	68-75
21978664-7	2011	In contrast to double-stranded RNA, heparin activates PKR by binding to the kinase domain.	Heparin	36-43	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	54-57
22110207-5	2011	RESULTS: Mouse 4T1 cells expressed ADAMTS1 and its substrates amphiregulin and heparin-binding EGF.	Heparin	79-86	epidermal growth factor	Mus musculus	95-98
7371948-0	1980	Lipoprotein lipase activity in the post-heparin plasma and adipose tissue of the rainbow trout (Salmo gairdnerii) [proceedings].	Heparin	40-47	lipoprotein lipase	Oncorhynchus mykiss	0-18
7368180-0	1980	A differential effect of low-affinity heparin on the inhibition of thrombin and factor Xa by antithrombin.	Heparin	38-45	coagulation factor X	Homo sapiens	80-89
7417594-3	1980	Heparin stimulates the inactivation of Factor Xa and thrombin by AT III.	Heparin	0-7	coagulation factor X	Homo sapiens	39-48
7417594-10	1980	Hep, like soluble AT III and heparin, instantaneously neutralized both thrombin and Factor Xa.	Heparin	29-36	DNL-type zinc finger	Homo sapiens	0-3
7417594-10	1980	Hep, like soluble AT III and heparin, instantaneously neutralized both thrombin and Factor Xa.	Heparin	29-36	coagulation factor X	Homo sapiens	84-93
3129047-8	1988	Plasma concentrations of alpha-2-antiplasmin after exposure of blood to t-PA were less depressed with increasing concentrations of heparin.	Heparin	131-138	serpin family F member 2	Homo sapiens	25-44
2967302-2	1988	Recent studies have shown that heparin, a GAG found in mast cells, potentiates the ability of acidic fibroblast growth factor (aFGF) to induce neurite outgrowth in pheochromocytoma (PC12) cells.	Heparin	31-38	fibroblast growth factor 1	Rattus norvegicus	94-125
2967302-2	1988	Recent studies have shown that heparin, a GAG found in mast cells, potentiates the ability of acidic fibroblast growth factor (aFGF) to induce neurite outgrowth in pheochromocytoma (PC12) cells.	Heparin	31-38	fibroblast growth factor 1	Rattus norvegicus	127-131
2967302-5	1988	Heparin potentiated aFGF-induced neurite outgrowth in a concentration-dependent fashion; potentiation increased with increasing heparin concentrations of 0.01-100 micrograms/ml.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	20-24
2967302-5	1988	Heparin potentiated aFGF-induced neurite outgrowth in a concentration-dependent fashion; potentiation increased with increasing heparin concentrations of 0.01-100 micrograms/ml.	Heparin	128-135	fibroblast growth factor 1	Rattus norvegicus	20-24
2967302-7	1988	The maximally active concentration of heparin (100 micrograms/ml) increased the potency of aFGF 102-fold.	Heparin	38-45	fibroblast growth factor 1	Rattus norvegicus	91-95
465719-3	1979	Heparin inhibits thrombin-induced eczocytosis.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	17-25
21325262-0	2011	A heparin binding site Arg79Cys missense mutation in the SERPINC1 gene in a Korean patient with hereditary antithrombin deficiency.	Heparin	2-9	serpin family C member 1	Homo sapiens	57-65
486155-1	1979	The inactivation of thrombin and factor Xa by antithrombin was determined in the presence of heparin fractions of different molecular weights and with high affinity for antithrombin.	Heparin	93-100	coagulation factor X	Homo sapiens	33-42
573262-4	1979	The yields of disulfated disaccharide (b-2) and monosulfated disaccharides (e-2-1 and e-2-3) indicated that 2-O-sulfates in L-iduronic acid residues of heparin were more libile than 6-O-sulfates in glucosamine residues to the dilute acid treatment, whereas the opposite was the case for the solvolysis.	Heparin	152-159	immunoglobulin kappa variable 5-2	Homo sapiens	39-42
573262-4	1979	The yields of disulfated disaccharide (b-2) and monosulfated disaccharides (e-2-1 and e-2-3) indicated that 2-O-sulfates in L-iduronic acid residues of heparin were more libile than 6-O-sulfates in glucosamine residues to the dilute acid treatment, whereas the opposite was the case for the solvolysis.	Heparin	152-159	small nucleolar RNA, H/ACA box 62	Homo sapiens	76-81
573262-4	1979	The yields of disulfated disaccharide (b-2) and monosulfated disaccharides (e-2-1 and e-2-3) indicated that 2-O-sulfates in L-iduronic acid residues of heparin were more libile than 6-O-sulfates in glucosamine residues to the dilute acid treatment, whereas the opposite was the case for the solvolysis.	Heparin	152-159	cystatin 12, pseudogene	Homo sapiens	86-91
389756-8	1979	Heparin reversed the effect of thrombin.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	31-39
303667-5	1977	Evidence is presented which supports previous findings that C1-INH, alpha1-AT, and antithrombin (in the presence of heparin) contribute to factor XIIa and XI a inactivation in ellagic acid-activated plasma and that plasma albumin may compete with factor XII for ellagic acid binding.	Heparin	116-123	serpin family G member 1	Homo sapiens	60-66
146278-0	1977	Role of heparin in the inactivation of thrombin, factor Xa, and plasmin by antithrombin III.	Heparin	8-15	coagulation factor X	Homo sapiens	49-58
336834-7	1977	The chymase complexed with native macromolecular rat mast cell heparin in molar ratios of 12:1 and 16:1, and complete heparin uptake occurred at a 40:1 ratio of chymase to heparin.	Heparin	63-70	chymase 1	Rattus norvegicus	4-11
336834-7	1977	The chymase complexed with native macromolecular rat mast cell heparin in molar ratios of 12:1 and 16:1, and complete heparin uptake occurred at a 40:1 ratio of chymase to heparin.	Heparin	118-125	chymase 1	Rattus norvegicus	4-11
336834-7	1977	The chymase complexed with native macromolecular rat mast cell heparin in molar ratios of 12:1 and 16:1, and complete heparin uptake occurred at a 40:1 ratio of chymase to heparin.	Heparin	118-125	chymase 1	Rattus norvegicus	161-168
336834-7	1977	The chymase complexed with native macromolecular rat mast cell heparin in molar ratios of 12:1 and 16:1, and complete heparin uptake occurred at a 40:1 ratio of chymase to heparin.	Heparin	118-125	chymase 1	Rattus norvegicus	4-11
336834-7	1977	The chymase complexed with native macromolecular rat mast cell heparin in molar ratios of 12:1 and 16:1, and complete heparin uptake occurred at a 40:1 ratio of chymase to heparin.	Heparin	118-125	chymase 1	Rattus norvegicus	161-168
336834-8	1977	Chymase activity was partially masked by combination with heparin in the isolated granule or experimental chymase-heparin complex, and soluble purified chymase was inhibited by concentrations of 5-HT comparable to those present in mast cells.	Heparin	58-65	chymase 1	Rattus norvegicus	0-7
336834-8	1977	Chymase activity was partially masked by combination with heparin in the isolated granule or experimental chymase-heparin complex, and soluble purified chymase was inhibited by concentrations of 5-HT comparable to those present in mast cells.	Heparin	114-121	chymase 1	Rattus norvegicus	0-7
336834-8	1977	Chymase activity was partially masked by combination with heparin in the isolated granule or experimental chymase-heparin complex, and soluble purified chymase was inhibited by concentrations of 5-HT comparable to those present in mast cells.	Heparin	114-121	chymase 1	Rattus norvegicus	106-113
336834-9	1977	It is therefore possible that the active site of chymase in the mast cell granule is largely masked by the combined effects of macromolecular heparin and 5-HT.	Heparin	142-149	chymase 1	Rattus norvegicus	49-56
268650-4	1977	The heparin-induced inhibition of thrombosis decreased in the order, activated Factor IX &gt; activated Factor X &gt; thrombin at each heparin concentration.	Heparin	4-11	prothrombin	Oryctolagus cuniculus	118-126
268650-4	1977	The heparin-induced inhibition of thrombosis decreased in the order, activated Factor IX &gt; activated Factor X &gt; thrombin at each heparin concentration.	Heparin	135-142	prothrombin	Oryctolagus cuniculus	118-126
193851-0	1977	Interaction of canine and swine lipoproteins with the low density lipoprotein receptor of fibroblasts as correlated with heparin/manganese precipitability.	Heparin	121-128	low density lipoprotein receptor	Sus scrofa	54-86
594303-3	1977	By this method they have been able to demonstrate that TRA is more sensitive than PTT during the haemorrhagic manifestations in thrombocytopenic patients and in monitoring heparin therapy, while it shows a behaviour similar to PTT in detecting coagulation defects.	Heparin	172-179	T cell receptor alpha locus	Homo sapiens	55-58
576747-2	1977	Five hours after a limited, nonhypotensive trauma without gross interference with coagulopathy, lungs of dogs were found to be completely deficient of heparin-releasable, metabolically active lipoprotein lipase.	Heparin	151-158	lipoprotein lipase	Canis lupus familiaris	192-210
836345-6	1977	A possible mechanism for this elevation resides in the known effect of heparin to increase plasma free fatty acid concentrations by its activation of lipoprotein lipase.	Heparin	71-78	lipoprotein lipase	Canis lupus familiaris	150-168
1005888-0	1976	Action of heparin on lecithin:cholesterol acyltransferase activity in normal subjects.	Heparin	10-17	lecithin-cholesterol acyltransferase	Homo sapiens	21-57
1031823-1	1976	Five hours after a limited, nonhypotensive trauma without gross interference with coagulopathy the lung of dogs was found to be completely deficient of heparin-releasable, metabolically active lipoprotein lipase.	Heparin	152-159	lipoprotein lipase	Canis lupus familiaris	193-211
1123560-2	1975	Factor Xa is prepared in a concentration adjusted to produce a clotting time of 18 to 20 seconds when heparin-free plasma is tested in the system.	Heparin	102-109	coagulation factor X	Homo sapiens	0-9
47195-0	1975	Effect of heparin on the neutralization of factor Xa and thrombin by the plasma alpha-2-globulin inhibitor.	Heparin	10-17	coagulation factor X	Homo sapiens	43-52
1115795-1	1975	Thrombin partially purified from bovine plasma can be inactivated at 60 degress C. In the presence of 10 units of heparin the extent of inactivation decreases.	Heparin	114-121	coagulation factor II, thrombin	Bos taurus	0-8
4281540-6	1974	The preventive administration of heparin reduces or abolishes the biological and histological disorders induced by thrombin; its beneficial effect is considerably reduced when thrombin is combined with fibrinolytic inhibitors.	Heparin	33-40	prothrombin	Oryctolagus cuniculus	115-123
4281540-6	1974	The preventive administration of heparin reduces or abolishes the biological and histological disorders induced by thrombin; its beneficial effect is considerably reduced when thrombin is combined with fibrinolytic inhibitors.	Heparin	33-40	prothrombin	Oryctolagus cuniculus	176-184
4405992-0	1974	Effect of heparin on insulin secretion induced by glucose in dogs.	Heparin	10-17	insulin	Canis lupus familiaris	21-28
16742805-9	1973	This discovery of relatively high proportions of chondroitin 4-sulphate in these mastocytoma-derived cells is noteworthy, since mast cells have generally been considered to produce heparin as their major glycosaminoglycan.	Heparin	181-188	carbohydrate sulfotransferase 11	Mus musculus	49-62
5900021-0	1964	Effect of heparin on glucose-6-phosphate dehydrogenase from normal erythrocytes and leucocytes.	Heparin	10-17	glucose-6-phosphate dehydrogenase	Homo sapiens	21-54
14208251-8	1964	The platelet injury induced by thrombin can be inhibited by small quantities of heparin.	Heparin	80-87	prothrombin	Oryctolagus cuniculus	31-39
13311031-0	1955	[Heparin treated bovine plasma, reagent for opacimetric determination of thrombin].	Heparin	1-8	coagulation factor II, thrombin	Bos taurus	73-81
34050225-6	2021	Docking simulation identified one positively selected site in APLP1 that alters the heparin-binding site, which could affect its function, and dimerization rate.	Heparin	84-91	amyloid beta precursor like protein 1	Homo sapiens	62-67
33860518-4	2021	Thus, by activating antithrombin, heparin mainly inhibits factor Xa and thrombin, whereas VKAs lower the levels of the vitamin K-dependent clotting factors.	Heparin	34-41	coagulation factor X	Homo sapiens	58-67
33683394-4	2021	Here, we found that protein A (SpA) of S. aureus was a heparin-binding protein, contributing to the interaction between S. aureus and heparin.	Heparin	134-141	SAOUHSC_00069	Staphylococcus aureus subsp. aureus NCTC 8325	20-29
33225455-6	2021	The structural modelling and molecular docking predictions indicated that bovine OPN binds to heparin disaccharide, hyaluronic acid and hyaluronan.	Heparin	94-101	secreted phosphoprotein 1	Bos taurus	81-84
32892505-12	2021	tPA, TFPI and VEGF were increased in critical patients, which are hypothesized to reflect endothelial dysfunction and/or contribution of heparin (which may cause endothelial TFPI/tPA release).	Heparin	137-144	chromosome 20 open reading frame 181	Homo sapiens	179-182
33512867-0	2021	Enoxaparin Dose Requirements to Achieve Therapeutic Low-molecular-weight Heparin Anti-factor Xa Levels in Infants and Young Children.	Heparin	73-80	coagulation factor X	Homo sapiens	86-95
33454168-8	2021	HBP levels increased immediately after heparin administration, further increased during CPB, but decreased rapidly after protamine administration.	Heparin	39-46	azurocidin 1	Homo sapiens	0-3
33454168-11	2021	CONCLUSIONS: HBP levels are elevated by the administration of heparin and the use of CPB but reduced by protamine administration.	Heparin	62-69	azurocidin 1	Homo sapiens	13-16
33309971-3	2021	The co-immobilization of these two key molecules with distinct therapeutic effects is achieved by simultaneous conjugation of heparin (HT) and copper nanoparticles (Cu NPs), an NO-generating catalyst, via a simple tyrosinase (Tyr)-mediated reaction.	Heparin	126-133	tyrosinase	Homo sapiens	214-224
33362545-5	2020	For example, single-nucleotide polymorphisms (SNPs) in FGG, FGA, and F5 mediate increases in D-dimer and SNPs in ABO, CBS, CPS1 and MTHFR mediate differences in homocysteine levels, and SNPs in TDAG8 associate with Heparin-induced Thrombocytopenia.	Heparin	215-222	methylenetetrahydrofolate reductase	Homo sapiens	132-137
32135222-2	2020	At the same time, the anti-microbial activity of the heparin-binding region of human Vn has been documented.	Heparin	53-60	vitronectin	Homo sapiens	85-87
33214666-4	2020	In myeloid precursors, the granulocyte-macrophage progenitors (GMPs), loss of NSP4 results in the decrease of cellular levels of histamine, serotonin and heparin/heparan sulfate.	Heparin	154-161	protease, serine 57	Mus musculus	78-82
32441664-12	2020	Conclusions Our study demonstrates that the choice of the anti-FXa method is particularly important for UFH and LMWH measurement.	Heparin	104-107	coagulation factor X	Homo sapiens	63-66
32568405-6	2020	NGF and BDNF were bound by electrostatic interaction to heparin, and the release profile evaluated by ELISA assay, which showed that ca.	Heparin	56-63	brain derived neurotrophic factor	Homo sapiens	8-12
32433187-0	2020	Perils of Antithrombotic Transitions: Effect of Oral Factor Xa Inhibitors on the Heparin Antifactor Xa Assay.	Heparin	81-88	coagulation factor X	Homo sapiens	53-62
32849563-11	2020	In solid-phase binding assays, properdin binding to C3b could be dose-dependently inhibited by recombinant Salp20> heparin(oid) > C3b.	Heparin	115-122	complement C3	Homo sapiens	52-55
32849563-15	2020	Binding of properdin to C3b could also be blocked by heparin(oids) and recombinant Salp20.	Heparin	53-60	complement C3	Homo sapiens	24-27
32849614-13	2020	Immobilized heparin was used as a model polyanion and SPR confirmed the presence of heparin binding sites in CCP 6-8 (K d 1.2 muM) and in CCP 19-20 (4.9 muM) and suggested the existence of a weak third polyanion binding site in the center of Factor H (CCP 11-13).	Heparin	12-19	AGBL carboxypeptidase 4	Homo sapiens	109-116
32849614-13	2020	Immobilized heparin was used as a model polyanion and SPR confirmed the presence of heparin binding sites in CCP 6-8 (K d 1.2 muM) and in CCP 19-20 (4.9 muM) and suggested the existence of a weak third polyanion binding site in the center of Factor H (CCP 11-13).	Heparin	84-91	AGBL carboxypeptidase 4	Homo sapiens	109-116
32849614-13	2020	Immobilized heparin was used as a model polyanion and SPR confirmed the presence of heparin binding sites in CCP 6-8 (K d 1.2 muM) and in CCP 19-20 (4.9 muM) and suggested the existence of a weak third polyanion binding site in the center of Factor H (CCP 11-13).	Heparin	84-91	complement factor H	Homo sapiens	242-250
32422680-5	2020	Results demonstrate the inhibitory activity of AT-T90S toward thrombin and factor Xa has been impaired three- to fivefold in both the absence and presence of heparin.	Heparin	158-165	coagulation factor X	Homo sapiens	75-84
32422680-7	2020	Kinetic analysis revealed the stoichiometry of AT-T90S inhibition of both thrombin and factor Xa has been elevated by three- to fourfold in both the absence and presence of heparin, suggesting that the reactivity of coagulation proteases with AT-T90S has been elevated in the substrate pathway.	Heparin	173-180	coagulation factor X	Homo sapiens	87-96
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	49-56	complement C3	Homo sapiens	210-213
32469940-4	2020	In the present study carried out in whole blood, heparin and selectively desulfated heparin reduced histone induced inflammatory markers such as interleukin 6 (IL 6), interleukin 8 (IL 8) and tissue factor and C3a, a complement component.	Heparin	84-91	complement C3	Homo sapiens	210-213
2900022-7	1988	These results suggest that heparin may modulate the oxidation and thus the insolubilization of extracellular collagen fibers, possibly under conditions where elastin fiber synthesis is not affected, and that the tight binding of lysyl oxidase to collagen is not completely related to the expression of enzyme activity toward this substrate.	Heparin	27-34	elastin	Homo sapiens	158-165
3291184-7	1988	Platelet aggregation induced by thrombin or thrombocytin could be inhibited by heparin with antithrombin III while that by acutin or batroxobin could not.	Heparin	79-86	prothrombin	Oryctolagus cuniculus	32-40
3291828-3	1988	However, heparin has been reported to inhibit in vitro insulin secretion by rat islets and to suppress in vivo insulin secretion in dogs.	Heparin	9-16	insulin	Canis lupus familiaris	55-62
3291828-4	1988	Therefore, the following evaluation was made on the effect of different heparin preparations on insulin secretion.	Heparin	72-79	insulin	Canis lupus familiaris	96-103
2448300-7	1988	The sequence of the peptide, Ser-Arg-Arg-Pro-[32PO4]Ser-Arg-Ala-Thr, corresponds to residues 374-381 which are located in the heparin-binding fragment of vitronectin identified by Suzuki et al.	Heparin	126-133	vitronectin	Homo sapiens	154-165
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	17-24	coagulation factor X	Homo sapiens	180-189
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	17-24	vitronectin	Homo sapiens	234-243
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	17-24	vitronectin	Homo sapiens	244-255
2445746-4	1987	The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin.	Heparin	115-122	coagulation factor X	Homo sapiens	180-189
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	30-37	vitronectin	Homo sapiens	41-50
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	30-37	vitronectin	Homo sapiens	51-62
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	30-37	vitronectin	Homo sapiens	140-149
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	30-37	vitronectin	Homo sapiens	150-161
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	41-50
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	51-62
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	140-149
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	150-161
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	41-50
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	51-62
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	140-149
2445746-5	1987	Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site.	Heparin	80-87	vitronectin	Homo sapiens	150-161
2445746-7	1987	Furthermore, S protein/vitronectin neutralized the anti-Factor Xa activity of a synthetic pentasaccharide comprising the antithrombin-binding sequence of heparin.	Heparin	154-161	vitronectin	Homo sapiens	13-22
2445746-7	1987	Furthermore, S protein/vitronectin neutralized the anti-Factor Xa activity of a synthetic pentasaccharide comprising the antithrombin-binding sequence of heparin.	Heparin	154-161	vitronectin	Homo sapiens	23-34
2445746-7	1987	Furthermore, S protein/vitronectin neutralized the anti-Factor Xa activity of a synthetic pentasaccharide comprising the antithrombin-binding sequence of heparin.	Heparin	154-161	coagulation factor X	Homo sapiens	56-65
2445746-8	1987	High molar excess of a synthetic tridecapeptide corresponding to part (amino acids 374-359) of the proposed glycosaminoglycan binding domain of S protein/vitronectin neutralized high affinity heparin and some oligosaccharides, but failed to neutralize the synthetic antithrombin-binding pentasaccharide.	Heparin	192-199	vitronectin	Homo sapiens	144-153
2445746-8	1987	High molar excess of a synthetic tridecapeptide corresponding to part (amino acids 374-359) of the proposed glycosaminoglycan binding domain of S protein/vitronectin neutralized high affinity heparin and some oligosaccharides, but failed to neutralize the synthetic antithrombin-binding pentasaccharide.	Heparin	192-199	vitronectin	Homo sapiens	154-165
2445746-10	1987	These findings suggest that S protein/vitronectin may interact through its glycosaminoglycan binding domain(s) with various functional domains of the heparin (heparan sulfate) molecule, including the antithrombin-binding pentasaccharide sequence.	Heparin	150-157	vitronectin	Homo sapiens	28-37
2445746-10	1987	These findings suggest that S protein/vitronectin may interact through its glycosaminoglycan binding domain(s) with various functional domains of the heparin (heparan sulfate) molecule, including the antithrombin-binding pentasaccharide sequence.	Heparin	150-157	vitronectin	Homo sapiens	38-49
3319692-1	1987	A hepatocyte growth factor (HGF) that stimulates DNA synthesis of adult rat hepatocytes in primary culture was purified as a homogeneous material from platelets of 1000 rats by a four-step procedure: stimulation of its release from platelets by thrombin, cation-exchanger fast protein liquid chromatography (FPLC) on a Mono S column, heparin-Sepharose CL-6B chromatography, and reverse-phase HPLC on a C4 column.	Heparin	334-341	hepatocyte growth factor	Rattus norvegicus	2-26
3319692-1	1987	A hepatocyte growth factor (HGF) that stimulates DNA synthesis of adult rat hepatocytes in primary culture was purified as a homogeneous material from platelets of 1000 rats by a four-step procedure: stimulation of its release from platelets by thrombin, cation-exchanger fast protein liquid chromatography (FPLC) on a Mono S column, heparin-Sepharose CL-6B chromatography, and reverse-phase HPLC on a C4 column.	Heparin	334-341	hepatocyte growth factor	Rattus norvegicus	28-31
2822410-14	1987	Both thrombin and chymotrypsin produced small fragments (35 kDa and 27 kDa respectively) which bound to heparin with high affinity, and large fragments (160 kDa for thrombin and 140 kDa for chymotrypsin) which had low affinity.	Heparin	104-111	coagulation factor II, thrombin	Bos taurus	5-13
2821539-9	1987	The rEC-SOD produced is type C, since its affinity for heparin-Sepharose was identical to that of nEC-SOD type C. Both enzymes bound to concanavalin A, lentil lectin, and wheat germ lectin and are thus glycoproteins.	Heparin	55-62	superoxide dismutase 3	Rattus norvegicus	4-11
3621562-1	1987	We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III).	Heparin	62-69	coagulation factor X	Homo sapiens	131-140
3621562-1	1987	We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III).	Heparin	99-106	coagulation factor X	Homo sapiens	131-140
3621562-2	1987	Residual Factor Xa is determined kinetically by the Du Pont aca discrete clinical analyzer with a chromogenic substrate and is inversely related to heparin activity.	Heparin	148-155	coagulation factor X	Homo sapiens	9-18
2956835-6	1987	Heparin has additional antithrombotic actions, largely mediated through the formation of the same complex, but involving precursor elements such as factor Xa.	Heparin	0-7	coagulation factor X	Homo sapiens	148-157
2823841-3	1987	The course of the activated partial thromboplastin time showed no difference between the medications given, whereas the inhibition of factor Xa was significantly stronger after application of all dosages of LMWH than after unfractionated heparin injections.	Heparin	238-245	coagulation factor X	Homo sapiens	134-143
3584128-3	1987	The strong interaction between heparin and HRG was demonstrated to be competitive with the binding of both antithrombin and thrombin to the heparin chain.	Heparin	31-38	prothrombin	Oryctolagus cuniculus	111-119
3584128-3	1987	The strong interaction between heparin and HRG was demonstrated to be competitive with the binding of both antithrombin and thrombin to the heparin chain.	Heparin	140-147	prothrombin	Oryctolagus cuniculus	111-119
3584128-4	1987	HRG was further tested as a modulator of the anticoagulant activity of heparin by comparing rates of the heparin-catalyzed reaction between antithrombin and thrombin in the presence and absence of added HRG.	Heparin	71-78	prothrombin	Oryctolagus cuniculus	144-152
3584128-4	1987	HRG was further tested as a modulator of the anticoagulant activity of heparin by comparing rates of the heparin-catalyzed reaction between antithrombin and thrombin in the presence and absence of added HRG.	Heparin	105-112	prothrombin	Oryctolagus cuniculus	144-152
3584128-5	1987	The heparin-antithrombin-thrombin reaction was modeled using the formalism of a two-substrate enzyme-catalyzed reaction with heparin as the enzyme and HRG analyzed as an enzyme inhibitor.	Heparin	4-11	prothrombin	Oryctolagus cuniculus	16-24
3584128-9	1987	Since little change in the rate of the heparin-catalyzed inhibition of thrombin by antithrombin occurs in this pH region, the dramatic change in HRG inhibition seen upon pH titration may reflect increasing ionic interaction between heparin and HRG due to the protonation of histidine residues which occurs in this pH region.	Heparin	39-46	prothrombin	Oryctolagus cuniculus	71-79
3603420-1	1987	A synthetic pentasaccharide, representing the critical sequence required in heparin for binding to antithrombin III (AT III), produces strong anti-factor Xa activity in vitro in the presence of AT III and is devoid of any activity directed towards thrombin.	Heparin	76-83	prothrombin	Oryctolagus cuniculus	103-111
3030755-4	1987	This ribosomal protein S6 kinase activity was substantially purified by a combination of phosphocellulose, DEAE-cellulose, Mono Q and heparin-Sepharose chromatography, and some of its characteristics were examined.	Heparin	134-141	40S ribosomal protein S6	Mesocricetus auratus	5-25
3032991-4	1987	While the neurotropic activities of aFGF and NGF are potentiated by heparin, that of bFGF is both partially inhibited or stimulated, depending upon the concentration of bFGF.	Heparin	68-75	fibroblast growth factor 1	Rattus norvegicus	36-40
3032991-8	1987	Heparin blocked the binding of bFGF to the receptor but had only a small inhibitory effect on the binding of aFGF to the receptor.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	109-113
3032991-10	1987	The stimulatory effects of heparin on the neurotropic activity of aFGF, bFGF, and NGF may occur through a site not associated with the respective cellular receptor for the growth factors.	Heparin	27-34	fibroblast growth factor 1	Rattus norvegicus	66-70
3556575-2	1987	Here we report studies showing that heparin, besides releasing asymmetric AChE from the skeletal muscle extracellular matrix (ECM), specifically solubilizes a dermatan sulfate proteoglycan (DSPG) which accounts for more than 95% of the 35S-released material.	Heparin	36-43	decorin	Rattus norvegicus	159-188
3556575-2	1987	Here we report studies showing that heparin, besides releasing asymmetric AChE from the skeletal muscle extracellular matrix (ECM), specifically solubilizes a dermatan sulfate proteoglycan (DSPG) which accounts for more than 95% of the 35S-released material.	Heparin	36-43	decorin	Rattus norvegicus	190-194
3821895-3	1987	In this paper we report that pure basic fibroblast growth factor (bFGF), at very low concentrations and with high specificity, closely mimics the effect of the ventrovegetal (VV) signal and that the transmission of the natural VV signal can be blocked by heparin, suggesting that it may be a heparin-binding factor such as bFGF.	Heparin	255-262	fibroblast growth factor 2 L homeolog	Xenopus laevis	34-64
3821895-3	1987	In this paper we report that pure basic fibroblast growth factor (bFGF), at very low concentrations and with high specificity, closely mimics the effect of the ventrovegetal (VV) signal and that the transmission of the natural VV signal can be blocked by heparin, suggesting that it may be a heparin-binding factor such as bFGF.	Heparin	255-262	fibroblast growth factor 2 L homeolog	Xenopus laevis	66-70
3821895-3	1987	In this paper we report that pure basic fibroblast growth factor (bFGF), at very low concentrations and with high specificity, closely mimics the effect of the ventrovegetal (VV) signal and that the transmission of the natural VV signal can be blocked by heparin, suggesting that it may be a heparin-binding factor such as bFGF.	Heparin	255-262	fibroblast growth factor 2 L homeolog	Xenopus laevis	323-327
3819648-0	1987	Histidine-rich glycoprotein inhibits the antiproliferative effect of heparin on smooth muscle cells.	Heparin	69-76	histidine rich glycoprotein	Homo sapiens	0-27
3819648-1	1987	Histidine-rich glycoprotein (HRGP), an alpha-glycoprotein in human plasma that is also present in platelets and macrophages, binds heparin with high affinity and neutralizes its anticoagulant activity.	Heparin	131-138	histidine rich glycoprotein	Homo sapiens	0-27
3819648-1	1987	Histidine-rich glycoprotein (HRGP), an alpha-glycoprotein in human plasma that is also present in platelets and macrophages, binds heparin with high affinity and neutralizes its anticoagulant activity.	Heparin	131-138	histidine rich glycoprotein	Homo sapiens	29-33
3819648-2	1987	We now report that HRGP specifically inhibits the antiproliferative effect of heparin on arterial smooth muscle cells while other heparinoid-binding proteins do not influence mitogenesis.	Heparin	78-85	histidine rich glycoprotein	Homo sapiens	19-23
3790599-0	1987	Comparison of the kinetic behavior of human and bovine proteins in the heparin-catalyzed antithrombin III/thrombin reaction.	Heparin	71-78	coagulation factor II, thrombin	Bos taurus	93-101
3028582-4	1987	The present study showed that thrombin bound to acidic thrombomodulin was inactivated at a lower rate by antithrombin in the presence of exogenous heparin than was free thrombin or thrombin bound to the non-acidic form of thrombomodulin.	Heparin	147-154	prothrombin	Oryctolagus cuniculus	30-38
3028582-4	1987	The present study showed that thrombin bound to acidic thrombomodulin was inactivated at a lower rate by antithrombin in the presence of exogenous heparin than was free thrombin or thrombin bound to the non-acidic form of thrombomodulin.	Heparin	147-154	prothrombin	Oryctolagus cuniculus	109-117
3028582-4	1987	The present study showed that thrombin bound to acidic thrombomodulin was inactivated at a lower rate by antithrombin in the presence of exogenous heparin than was free thrombin or thrombin bound to the non-acidic form of thrombomodulin.	Heparin	147-154	prothrombin	Oryctolagus cuniculus	109-117
3028582-5	1987	The data suggest that the acidic component of thrombomodulin is primarily responsible for the retardation of thrombin-antithrombin complex formation in the presence of exogenous heparin.	Heparin	178-185	prothrombin	Oryctolagus cuniculus	109-117
3801610-0	1986	[Effect of heparin on the activation of the anticoagulation system by alpha-thrombin].	Heparin	11-18	prothrombin	Oryctolagus cuniculus	76-84
3801610-4	1986	DIP-alpha-thrombin-heparin perfusates contained no endogenic heparin, unlike DIP-alpha-thrombin perfusates.	Heparin	19-26	prothrombin	Oryctolagus cuniculus	10-18
3782075-0	1986	Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.	Heparin	36-43	coagulation factor X	Homo sapiens	158-167
3782075-2	1986	Moreover, all high-affinity oligosaccharides and heparins enhanced, to a similar extent, the amount of free proteolytically modified antithrombin cleaved at the reactive bond by Factor Xa.	Heparin	49-57	coagulation factor X	Homo sapiens	178-187
2434472-3	1986	Two states of vitronectin were previously reported; the open state binds to heparin, but the cryptic state does not (Hayashi et al.	Heparin	76-83	vitronectin	Homo sapiens	14-25
3810553-2	1986	Using canine AT III purified by heparin-Sepharose affinity chromatography, antiserum against canine AT III was raised in rabbit.	Heparin	32-39	serpin family C member 1	Canis lupus familiaris	13-19
3810553-2	1986	Using canine AT III purified by heparin-Sepharose affinity chromatography, antiserum against canine AT III was raised in rabbit.	Heparin	32-39	serpin family C member 1	Canis lupus familiaris	100-106
3790498-8	1986	It is our conclusion that factor Xa when acting in prothrombinase on prothrombin is profoundly protected from inhibition by antithrombin III in the absence as well as in the presence of heparin.	Heparin	186-193	coagulation factor X	Homo sapiens	26-35
3756204-4	1986	Activities of both lipoprotein lipase and hepatic triacylglycerol lipase in the plasma after heparin injection were markedly lower in the W/WV mice than in the congenic normal mice, although activities of both lipoprotein lipase in the heart and adipose tissue and hepatic triacylglycerol lipase in the liver were not decreased.	Heparin	93-100	lipoprotein lipase	Mus musculus	19-37
3800942-0	1986	The relative molecular mass dependence of the anti-factor Xa properties of heparin.	Heparin	75-82	coagulation factor X	Homo sapiens	51-60
3800942-1	1986	The effect of heparin fractions of various Mr, with high affinity for antithrombin III, on the kinetics of the reaction between factor Xa and antithrombin III have been studied using purified human proteins.	Heparin	14-21	coagulation factor X	Homo sapiens	128-137
3800942-5	1986	The disparity in these rates of inhibition was shown to be due to a change in the Km for factor Xa when a two-substrate model of heparin catalysis was used.	Heparin	129-136	coagulation factor X	Homo sapiens	89-98
3800942-7	1986	These data suggest that the increased rates of inhibition observed with heparins of higher Mr may be due to an involvement of heparin binding to factor Xa as well as to antithrombin III.	Heparin	72-80	coagulation factor X	Homo sapiens	145-154
3800942-7	1986	These data suggest that the increased rates of inhibition observed with heparins of higher Mr may be due to an involvement of heparin binding to factor Xa as well as to antithrombin III.	Heparin	72-79	coagulation factor X	Homo sapiens	145-154
3529086-2	1986	HGF was purified from rat platelets to homogeneity by a three-step procedure: stimulation of its release from platelets by thrombin, cation-exchanger fast protein liquid chromatography on a Mono S column, and heparin-Sepharose chromatography.	Heparin	209-216	hepatocyte growth factor	Rattus norvegicus	0-3
3762321-3	1986	During liver perfusion with heparin, perfusate peaks of TGL and CEH did not consistently coincide, and TGL activity was considerably higher and less heat-stable than that of CEH.	Heparin	28-35	epoxide hydrolase 2	Rattus norvegicus	64-67
3762321-3	1986	During liver perfusion with heparin, perfusate peaks of TGL and CEH did not consistently coincide, and TGL activity was considerably higher and less heat-stable than that of CEH.	Heparin	28-35	epoxide hydrolase 2	Rattus norvegicus	174-177
2943315-1	1986	The amidolytic plasmin activity of a mixture of tissue plasminogen activator (tPA) and plasminogen is enhanced by heparin at therapeutic concentrations.	Heparin	114-121	chromosome 20 open reading frame 181	Homo sapiens	48-76
3510667-13	1986	Despite this lack of activation, the lipoprotein lipase molecule was able to migrate intracellularily and to undergo secretion after heparin stimulation of the tunicamycin-treated cells.	Heparin	133-140	lipoprotein lipase	Mus musculus	37-55
2422780-0	1986	Effect of NaC1 on inactivation of bovine thrombin by antithrombin III in the presence of low affinity-heparin or dextran sulfate.	Heparin	102-109	coagulation factor II, thrombin	Bos taurus	41-49
2422780-1	1986	Heparin with low affinity (LA-heparin) to antithrombin III (AT III) enhanced the rate of inactivation of thrombin by AT III.	Heparin	0-7	coagulation factor II, thrombin	Bos taurus	46-54
4089812-5	1985	Heparin prevented the appearance of thrombin activity completely only if given just before the trauma.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	36-44
3902118-8	1985	Vessel contraction and thrombin generation can be minimized, respectively, by the use of a smooth muscle relaxant and heparin administered prior to killing of the animals.	Heparin	118-125	prothrombin	Oryctolagus cuniculus	23-31
3936965-9	1985	A LMW-heparin dose was used that produced plasma anti-FXa-activity of 0.5 to 0.9 U/ml (initial dose: 30 to 40; dose/hr: 8 to 15 anti-FXa-units/kg body wt).	Heparin	6-13	coagulation factor X	Homo sapiens	54-57
4041471-10	1985	Thus, avian adipose lipoprotein lipase has been purified by a one-step immunoaffinity followed by a concentrating step on heparin-Sepharose 4B.	Heparin	122-129	lipoprotein lipase	Mus musculus	20-38
2416739-0	1985	Activation of vitronectin (serum spreading factor) binding of heparin by denaturing agents.	Heparin	62-69	vitronectin	Homo sapiens	14-25
2416739-0	1985	Activation of vitronectin (serum spreading factor) binding of heparin by denaturing agents.	Heparin	62-69	vitronectin	Homo sapiens	27-49
2416739-1	1985	Vitronectin (serum spreading factor), a cell-adhesive glycoprotein present in mammalian serum, has previously been the subject of conflicting reports concerning its binding to heparin.	Heparin	176-183	vitronectin	Homo sapiens	0-11
2416739-1	1985	Vitronectin (serum spreading factor), a cell-adhesive glycoprotein present in mammalian serum, has previously been the subject of conflicting reports concerning its binding to heparin.	Heparin	176-183	vitronectin	Homo sapiens	13-35
2416739-3	1985	These treatments seem to expose a heparin-binding site in vitronectin; this finding thus resolves the conflicts concerning this function.	Heparin	34-41	vitronectin	Homo sapiens	58-69
2410408-0	1985	Heparin-binding properties of human serum spreading factor.	Heparin	0-7	vitronectin	Homo sapiens	36-58
2411283-4	1985	Standard heparin was the only sulphated polysaccharide that could equally inhibit thrombin generation and enhance the inactivation of factor Xa and thrombin by plasma.	Heparin	9-16	coagulation factor X	Homo sapiens	134-143
4024529-0	1985	[Antithrombin III activity in relation to multiple administration of various doses of heparin to normal animals].	Heparin	86-93	serpin family C member 1	Rattus norvegicus	1-17
4024529-1	1985	Heparin affected the content of antithrombin III and the thrombin time of blood plasma coagulation depending on the dose of the anticoagulant administered (eight intravenous administrations at single doses of 225, 150, 75, 37 or 18 IU/kg of body mass of healthy rats).	Heparin	0-7	serpin family C member 1	Rattus norvegicus	32-48
4024529-2	1985	High doses of heparin decreased more distinctly the content of antithrombin III as compared with low doses.	Heparin	14-21	serpin family C member 1	Rattus norvegicus	63-79
4024529-3	1985	8 intravenous infusions of small doses of heparin (37 IU/kg) as well as intramuscular administration of the anticoagulant (10 injections) at a dose of 225 IU/kg caused a compensatory increase in content of antithrombin III.	Heparin	42-49	serpin family C member 1	Rattus norvegicus	206-222
3155697-3	1985	Studies of the binding parameters and kinetic characteristics of the heparin-antithrombin-hemostatic enzyme interactions have revealed that binding of heparin to antithrombin is responsible for a approximately 1000-fold acceleration of the thrombin-antithrombin or factor IXa-antithrombin and factor Xa-antithrombin interactions (allosteric effect).	Heparin	69-76	coagulation factor II, thrombin	Bos taurus	81-89
6523442-9	1984	Thus, the heparin-sensitized inactivation of thrombin by antithrombin III is affected by the modification of one tryptophan residue.	Heparin	10-17	coagulation factor II, thrombin	Bos taurus	45-53
6523442-12	1984	It appears that the one tryptophan residue of thrombin is situated at or close to the binding site of heparin.	Heparin	102-109	coagulation factor II, thrombin	Bos taurus	46-54
6509026-0	1984	Interaction of rat liver glucocorticoid receptor with heparin.	Heparin	54-61	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	25-48
6509026-1	1984	When rat liver cytosol containing [3H]dexamethasone-glucocorticoid receptor complex is exposed to immobilized heparin (Sepharose-heparin; Seph-hep) the steroid receptor complex binds to the substituted Sepharose avidly [Kd = 3.5 (+/- 1.7) X 10(-10) M], and 80-90% of the receptor present is adsorbed to the solid phase after 40 min at 0 degree C. The binding is enhanced by Mn2+ (10 mM) and Mg2+, whereas Ca2+ and Sr2+ are ineffective.	Heparin	110-117	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	52-75
6509026-1	1984	When rat liver cytosol containing [3H]dexamethasone-glucocorticoid receptor complex is exposed to immobilized heparin (Sepharose-heparin; Seph-hep) the steroid receptor complex binds to the substituted Sepharose avidly [Kd = 3.5 (+/- 1.7) X 10(-10) M], and 80-90% of the receptor present is adsorbed to the solid phase after 40 min at 0 degree C. The binding is enhanced by Mn2+ (10 mM) and Mg2+, whereas Ca2+ and Sr2+ are ineffective.	Heparin	129-136	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	52-75
6509026-5	1984	Both "native" and temperature "transformed" forms of the glucocorticoid receptor interact with immobilized heparin.	Heparin	107-114	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	57-80
6509026-7	1984	An immediate application of this newly found ability of the glucocorticoid receptor to interact with heparin is the use of Seph-hep for affinity chromatography purification of the glucocorticoid receptor.	Heparin	101-108	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	60-83
6509026-7	1984	An immediate application of this newly found ability of the glucocorticoid receptor to interact with heparin is the use of Seph-hep for affinity chromatography purification of the glucocorticoid receptor.	Heparin	101-108	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	180-203
6734448-3	1984	Low-molecular heparin caused a ten-fold stronger inhibition of factor Xa.	Heparin	14-21	coagulation factor X	Homo sapiens	63-72
6734448-5	1984	Half-life of heparin measured in terms of the inhibition of factor Xa was 5.5 hours for the low-molecular and 3.5 hours for the commercial preparation.	Heparin	13-20	coagulation factor X	Homo sapiens	60-69
6734448-6	1984	These results indicate that low-molecular heparin has a high specificity in the inhibition of factor Xa.	Heparin	42-49	coagulation factor X	Homo sapiens	94-103
6474448-1	1984	Acid and neutral cholesterol esterase activities in rat arterial wall were released from the lysosomal fraction and microsomal fraction respectively into the 105,000 X g supernatant fraction by treatment with Triton X-100, heparin and dextran sulfate.	Heparin	223-230	carboxyl ester lipase	Rattus norvegicus	17-37
6474448-2	1984	The percentage releases of acid cholesterol esterase by Triton X-100 (0.1%), heparin (50 micrograms/ml) and dextran sulfate (1 mg/ml) were 21%, 18% and 4%, respectively, while those of neutral cholesterol esterase were 66%, 56% and 39%, respectively.	Heparin	77-84	carboxyl ester lipase	Rattus norvegicus	32-52
6715365-4	1984	The bimolecular rate constant k2/Ki for intact heparin is 3 X 10(8) M-1 S-1 and the corresponding second order rate constant k1 is 6.7 X 10(8) M-1 S-1, a value greater than that expected for a diffusion-controlled bimolecular reaction.	Heparin	47-54	RBPJ pseudogene 3	Homo sapiens	30-35
31857208-14	2020	Antimicrobial agents plus low-dose heparin (500-2500 U/mL), TSC and low-dose heparin locks had lower risk of bleeding events than heparin 5000 U/mL.	Heparin	35-42	thrombopoietin	Mus musculus	55-57
31857208-18	2020	CONCLUSIONS: Taking into account both efficacy and safety, antibiotics plus low-dose heparin (500-2500 U/mL) may be the preferred lock solution.	Heparin	85-92	thrombopoietin	Mus musculus	105-107
32425936-0	2020	MASP-2 Is a Heparin-Binding Protease; Identification of Blocking Oligosaccharides.	Heparin	12-19	MBL associated serine protease 2	Homo sapiens	0-6
32425936-4	2020	Interaction of human MASP-2 with heparan sulfate/heparin was evaluated by surface plasmon resonance, ELISA and in renal tissue.	Heparin	49-56	MBL associated serine protease 2	Homo sapiens	21-27
32425936-9	2020	Surface plasmon resonance showed MASP-2 binding with heparin and heparan sulfate, revealing high Kon and Koff rates resulted in a Kd of ~2 muM and confirmed inhibition by heparin-derived tetrasaccharide.	Heparin	53-60	MBL associated serine protease 2	Homo sapiens	33-39
32425936-9	2020	Surface plasmon resonance showed MASP-2 binding with heparin and heparan sulfate, revealing high Kon and Koff rates resulted in a Kd of ~2 muM and confirmed inhibition by heparin-derived tetrasaccharide.	Heparin	171-178	MBL associated serine protease 2	Homo sapiens	33-39
32425936-11	2020	Our data show that highly sulfated GAGs mediated inhibition of all three complement pathways, whereas short heparin- and heparan sulfate-derived oligosaccharides selectively blocked the lectin pathway via MASP-2 inhibition.	Heparin	108-115	MBL associated serine protease 2	Homo sapiens	205-211
32425936-12	2020	Binding of MASP-2 to immobilized heparan sulfate/heparin and partial co-localization of agrin/heparan sulfate with MASP, but not C3b, might suggest that in vivo heparan sulfate proteoglycans act as a docking platform for MASP-2 and possibly prevent the lectin pathway from activation.	Heparin	49-56	MBL associated serine protease 2	Homo sapiens	11-17
32271162-8	2020	The p.G1675S mutation in the LG2 domain attenuated anchoring of agrin to the sarcolemma by compromising its binding to heparin.	Heparin	119-126	agrin	Homo sapiens	64-69
31629123-1	2020	BACKGROUND: The purpose of this study was to compare cryopreserved arterial allograft (CAA) to heparin-bonded prosthesis (HBP) in infragenicular bypasses for patients with chronic limb-threatening ischemia (CLTI).	Heparin	95-102	azurocidin 1	Homo sapiens	122-125
31843715-4	2020	An injectable, self-assembling peptide/heparin (SAP/Hep) hydrogel was used to co-deliver TNF-alpha neutralizing antibody (anti-TNF-alpha) and hepatocyte growth factor (HGF).	Heparin	39-46	hepatocyte growth factor	Mus musculus	142-166
31774689-1	2020	A disintegrin and metalloproteinase (ADAM)12 is considered to promote cardiac dysfunction based on the finding that a small-molecule ADAM12 inhibitor, KB-R7785, ameliorated cardiac function in a transverse aortic constriction (TAC) model by inhibiting the proteolytic activation of heparin-binding-EGF signaling.	Heparin	282-289	a disintegrin and metallopeptidase domain 12 (meltrin alpha)	Mus musculus	133-139
31574241-8	2020	Nur77 and 6-MP may provide a basis to develop a new treatment for patients who suffer from embryo adhesion dysfunction.Abbreviations: HB-EGF: heparin-binding epidermal growth factor-like growth factor; HOXA10: homeobox A10; NGFI-B: nerve growth factor-induced gene B; RIF: recurrent implantation failure; RPL: recurrent pregnancy loss; 6-MP: 6-mercaptopurine; IGFBP-1: insulin-like growth factor binding protein-1; LIF: leukemia inhibitory factor; IL-1beta: Interleukin - 1beta; CRISPR/Cas9: Clustered Regularly Interspaced Short Palindromic Repeats; AF-1: activation function-1 domain; HIF-1alpha: hypoxia-inducible factor 1alpha; CREB: cAMP response element binding.	Heparin	142-149	cAMP responsive element binding protein 1	Homo sapiens	632-636
33214783-0	2020	Evaluation of Heparin Anti-Factor Xa Levels Following Antithrombin Supplementation in Pediatric Patients Supported With Extracorporeal Membrane Oxygenation.	Heparin	14-21	coagulation factor X	Homo sapiens	27-36
31797980-1	2019	Heparin is a widely used anticoagulant which inhibits factor Xa and thrombin through potentiation of antithrombin.	Heparin	0-7	coagulation factor X	Homo sapiens	54-63
31810297-0	2019	Heparanase as an Additional Tool for Detecting Structural Peculiarities of Heparin Oligosaccharides.	Heparin	75-82	heparanase	Bos taurus	0-10
31810297-3	2019	Hereby, we apply an efficient heparanase-based strategy to assert the structure of two major isomeric octasaccharides of dalteparin and investigate the tetrasaccharides arising from antithrombin binding region (ATBR) of bovine mucosal heparin.	Heparin	235-242	heparanase	Bos taurus	30-40
31810297-4	2019	Heparanase, especially when combined with other sample preparation methods (e.g., size exclusion, affinity chromatography, heparinase depolymerization), was shown to be a powerful tool providing relevant information about heparin structural peculiarities.	Heparin	123-130	heparanase	Bos taurus	0-10
31810297-6	2019	When extended to ATBR-related tetramers of bovine heparin, the heparanase-based approach allowed for elucidation of the structure of minor sequences that have not been reported yet.	Heparin	50-57	heparanase	Bos taurus	63-73
32063701-10	2019	Heparin inhibits collagen crosslinking while stimulating elastin repair and might therefore be the ideal companion of copper for emphysema patients.	Heparin	0-7	elastin	Homo sapiens	57-64
31530752-2	2019	In this study, a simple approach was developed to immobilize bioactive heparin to the surface of e-polycaprolactone (PCL) grafts through a two-step strategy combining covalent grafting and layer by layer (LBL) assembly of polyelectrolytes.	Heparin	71-78	PHD finger protein 1	Homo sapiens	117-120
31530752-3	2019	The performance of heparinized PCL was evaluated in vitro, including the release behavior of heparin, anticoagulation and different types of cells adhesion characteristic.	Heparin	19-26	PHD finger protein 1	Homo sapiens	31-34
31530752-5	2019	Surface remaining heparin was up to 1.10 mug cm-2 on the modified PCL after release in vitro for 30 days.	Heparin	18-25	PHD finger protein 1	Homo sapiens	66-69
31530752-7	2019	The two-step strategy provides a simple and general route to incorporate heparin on PCL graft surface.	Heparin	73-80	PHD finger protein 1	Homo sapiens	84-87
31324409-1	2019	INTRODUCTION: Administering intravenous IV tissue plasminogen activator (tPA) is the recommended standard of care in acute ischemic stroke (AIS), although it is not recommended to administer intravenous thrombolysis with tPA following heparin reversal with protamine sulfate in patients with AIS.	Heparin	235-242	chromosome 20 open reading frame 181	Homo sapiens	43-71
31243789-0	2019	Clinical outcomes with unfractionated heparin monitored by anti-factor Xa vs. activated partial Thromboplastin time.	Heparin	38-45	coagulation factor X	Homo sapiens	64-73
21325262-1	2011	We describe a case of heparin binding site Arg79Cys mutation in the gene encoding antithrombin, SERPINC1, in a Korean patient with hereditary antithrombin (AT) deficiency.	Heparin	22-29	serpin family C member 1	Homo sapiens	82-94
21325262-1	2011	We describe a case of heparin binding site Arg79Cys mutation in the gene encoding antithrombin, SERPINC1, in a Korean patient with hereditary antithrombin (AT) deficiency.	Heparin	22-29	serpin family C member 1	Homo sapiens	96-104
21325262-1	2011	We describe a case of heparin binding site Arg79Cys mutation in the gene encoding antithrombin, SERPINC1, in a Korean patient with hereditary antithrombin (AT) deficiency.	Heparin	22-29	serpin family C member 1	Homo sapiens	142-154
21799398-0	2011	Peroperative effects of fresh frozen plasma and antithrombin III on heparin sensitivity and coagulation during nitroglycerine infusion in coronary artery bypass surgery.	Heparin	68-75	serpin family C member 1	Homo sapiens	48-64
21799398-2	2011	Fresh frozen plasma (FFP) and antithrombin III (ATIII) may be used for the treatment of heparin resistance.	Heparin	88-95	serpin family C member 1	Homo sapiens	30-46
21799398-2	2011	Fresh frozen plasma (FFP) and antithrombin III (ATIII) may be used for the treatment of heparin resistance.	Heparin	88-95	serpin family C member 1	Homo sapiens	48-53
21995826-9	2011	Heparin, a known binding partner of AnxA2, inhibited Delta4 RNA-protein complex formation.	Heparin	0-7	annexin A2	Mus musculus	36-41
21733881-0	2011	Role of vimentin in the inhibitory effects of low-molecular-weight heparin on PC-3M cell adhesion to, and migration through, endothelium.	Heparin	67-74	vimentin	Homo sapiens	8-16
21496885-4	2011	Here we report heparin reversal by the most effective of these virus-like particles (VLP) in samples from patients who were administered heparin during cardiac procedures or therapeutically for treatment of various thrombotic conditions.	Heparin	15-22	VHL like	Homo sapiens	85-88
21496885-4	2011	Here we report heparin reversal by the most effective of these virus-like particles (VLP) in samples from patients who were administered heparin during cardiac procedures or therapeutically for treatment of various thrombotic conditions.	Heparin	137-144	VHL like	Homo sapiens	85-88
21496885-5	2011	The VLP consistently reversed heparin in these samples, including those from patients that received high doses of heparin, with greater efficiency than a negative control VLP and with significantly less variability than protamine sulfate.	Heparin	30-37	VHL like	Homo sapiens	4-7
21496885-5	2011	The VLP consistently reversed heparin in these samples, including those from patients that received high doses of heparin, with greater efficiency than a negative control VLP and with significantly less variability than protamine sulfate.	Heparin	114-121	VHL like	Homo sapiens	4-7
21640648-8	2011	In summary, after PH pretreatment, transplantation of fetal hepatocyte-embedded, heparin-immobilized, collagen-gel-filled PUF scaffold into a VEGF-induced prevascularized cavity appears to be a promising strategy for future liver tissue engineering.	Heparin	81-88	vascular endothelial growth factor A	Rattus norvegicus	142-146
21648090-3	2011	In a previous study, it was demonstrated that dPGS, a fully synthetic heparin analogue, works as an efficient inhibitor towards L- and P-selectin in vitro as well as in vivo.	Heparin	70-77	selectin P	Homo sapiens	135-145
21788507-5	2011	Inhibition of HB-EGF by antibody neutralization or heparin treatment efficiently counteracted PAR-2-mediated activation of hypoxic ECs.	Heparin	51-58	heparin binding EGF like growth factor	Homo sapiens	14-20
20530051-10	2011	Heparin-induced thrombocytopenia and thrombotic thrombocytopenic purpura is rare but they must be ruled out in thrombocytopenia with nontypical clinical course, and the assays for HIT antibody and ADAMTS13 activity are useful tools.	Heparin	0-7	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	197-205
21720642-7	2011	hMSC phenotype is maintained over multiple population doublings on heparin-sequestering substrates in growth medium, while hMSC osteogenic differentiation is enhanced in a bone morphogenetic protein-dependent manner on the same substrates during culture in osteogenic induction medium.	Heparin	67-74	musculin	Homo sapiens	0-4
21720642-10	2011	Importantly, the use of chemically well-defined SAMs in this study eliminated the confounding factor of random, non-specific biomolecule adsorption, and identified serum-borne heparin as a key mediator of hMSC response to endogenous growth factors.	Heparin	176-183	musculin	Homo sapiens	205-209
20211924-6	2011	Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined.	Heparin	218-225	serpin family C member 1	Homo sapiens	0-12
21454702-4	2011	We have previously reported that in mouse lung epithelial cells, the pro-EGF ligands TGFalpha, neuregulin 1beta (NRG), and heparin-binding EGF are differentially cleaved depending on the cleavage stimulus (Herrlich, A., Klinman, E., Fu, J., Sadegh, C., and Lodish, H. (2008) FASEB J.).	Heparin	123-130	epidermal growth factor	Mus musculus	73-76
21454702-4	2011	We have previously reported that in mouse lung epithelial cells, the pro-EGF ligands TGFalpha, neuregulin 1beta (NRG), and heparin-binding EGF are differentially cleaved depending on the cleavage stimulus (Herrlich, A., Klinman, E., Fu, J., Sadegh, C., and Lodish, H. (2008) FASEB J.).	Heparin	123-130	epidermal growth factor	Mus musculus	139-142
21398697-4	2011	Here, we show that ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment in culture and in vivo.	Heparin	108-115	angiopoietin like 4	Homo sapiens	19-26
20926921-5	2011	RESULTS: The diabetic obese subjects had significantly lower fasting and post-prandial AT heparin-releasable LPL activity than only obese and control subjects (p&lt;0.05) as well as lower mRNA LPL levels.	Heparin	90-97	lipoprotein lipase	Homo sapiens	109-112
31251821-1	2019	The authors describe a case of unfractionated heparin (UFH) unresponsiveness in the operating room secondary to reversal of rivaroxaban with coagulation factor Xa (recombinant) inactivated-zhzo (andexanet alfa).	Heparin	46-53	coagulation factor X	Homo sapiens	153-162
21439895-1	2011	Cysteine-rich protein 61 (Cyr61) selectively binds heparin and insulin-like growth factors and mediates a variety of biological actions, including cell adhesion, differentiation, proliferation, migration, angiogenesis, and tumorigenesis.	Heparin	51-58	cellular communication network factor 1	Homo sapiens	0-24
31251821-1	2019	The authors describe a case of unfractionated heparin (UFH) unresponsiveness in the operating room secondary to reversal of rivaroxaban with coagulation factor Xa (recombinant) inactivated-zhzo (andexanet alfa).	Heparin	55-58	coagulation factor X	Homo sapiens	153-162
31357538-2	2019	Domain III (ED3) of the viral envelope protein contains the two dominant putative epitopes and part of the heparin sulfate receptor binding region that drives the dengue virus (DENV)"s fusion with the host cell.	Heparin	107-114	ectodysplasin A receptor	Homo sapiens	12-15
33405584-2	2019	In this study, multilayers of heparin and collagen (HEP/COL) were used as a bioactive surface coating to enhance human MSC (hMSC) response to soluble interferon-gamma (IFN-gamma).	Heparin	30-37	DNL-type zinc finger	Homo sapiens	52-55
21439895-1	2011	Cysteine-rich protein 61 (Cyr61) selectively binds heparin and insulin-like growth factors and mediates a variety of biological actions, including cell adhesion, differentiation, proliferation, migration, angiogenesis, and tumorigenesis.	Heparin	51-58	cellular communication network factor 1	Homo sapiens	26-31
6562157-11	1984	Experiments designed to determine the cause of this difference revealed that treatment of blood with some anticoagulants, in particular heparin and EDTA, resulted in a marked reduction in the amount of measurable tissue kallikrein.	Heparin	136-143	kallikrein related peptidase 4	Homo sapiens	220-230
21845882-0	2011	[Effects of ambroxol combined with low-dose heparin on TNF-alpha and IL-1beta in rabbits with acute lung injury].	Heparin	44-51	tumor necrosis factor	Oryctolagus cuniculus	55-64
6420398-7	1984	Similar studies with O-sulfated heparin intermediates showed that O-sulfate groups either at C-2 of the L-iduronosyl moieties or at C-6 of vicinal D-glucosaminyl moieties prevent 5-epimerization.	Heparin	32-39	complement component 2 (within H-2S)	Mus musculus	93-96
6735276-1	1984	Spectrophotometric heparin assays which are based on the catalytic effect of heparin on either the inactivation of thrombin or that of factor Xa by antithrombin III, were adapted for use in a laboratory batch analyzer.	Heparin	19-26	coagulation factor X	Homo sapiens	135-144
6710943-0	1984	[Effect of multiple intravenous injections of heparin on the content of antithrombin III in healthy animals and experimental atherosclerosis].	Heparin	46-53	serpin family C member 1	Rattus norvegicus	72-88
30972039-6	2019	Moreover, cell culture infection analyses with primary endothelial cells characterized VWF as bridging molecule that mediates bacterial adherence to endothelial cells in a heparin-sensitive manner.	Heparin	172-179	von Willebrand factor	Danio rerio	87-90
21845882-1	2011	OBJECTIVE: To investigate the intervention and mechanism of ambroxol combined with low-dose heparin on oxidative stress, TNF-alpha and IL-1beta in rabbits with acute lung injury (ALI).	Heparin	92-99	tumor necrosis factor	Oryctolagus cuniculus	121-130
30698048-4	2019	In fed mice, some LPL colocalized with the endothelial markers CD31 and GPIHBP1 and could be removed by perfusion with heparin, indicating a vascular location.	Heparin	119-126	lipoprotein lipase	Mus musculus	18-21
6558419-0	1983	Heparin prevents formation of the human C3 amplification convertase by inhibiting the binding site for B on C3b.	Heparin	0-7	complement C3	Homo sapiens	108-111
21845882-16	2011	Ambroxol combined with low-dose heparin can reduce lung cells oxidative stress to inhibit the release of IL-1beta and TNF-alpha, which play a role in the treatment of ALI.	Heparin	32-39	tumor necrosis factor	Oryctolagus cuniculus	118-127
6558419-1	1983	Fluid-phase heparin prevents generation of the C3 amplification convertase of human complement, C3b, Bb most likely by inhibiting the formation of the bimolecular complex between cell-bound C3b and B.	Heparin	12-19	complement C3	Homo sapiens	96-99
6558419-1	1983	Fluid-phase heparin prevents generation of the C3 amplification convertase of human complement, C3b, Bb most likely by inhibiting the formation of the bimolecular complex between cell-bound C3b and B.	Heparin	12-19	complement C3	Homo sapiens	190-199
20558775-5	2011	We found that: (1) hypoxia increased ROCK expression in mice and PASMCs; (2) overexpression of RhoA diminished the inhibitory effect of heparin on PASMC proliferation and down-regulated p27 expression; and (3) overexpression of GEF-H1 negated heparin inhibition of PASMC proliferation, which was accompanied by increased GTP-RhoA and decreased p27.	Heparin	136-143	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	228-234
6558419-2	1983	The effect of heparin on the binding of B to C3b was examined using 125I-labelled B and C3b-bearing sheep erythrocytes (EsC3b).	Heparin	14-21	complement C3	Homo sapiens	45-48
6558419-4	1983	Incremental amounts of heparin (100-700 micrograms/10(7) EsC3b) inhibited the binding of 125I-B to C3b in a dose-dependent manner.	Heparin	23-30	complement C3	Homo sapiens	59-62
6558419-5	1983	Scatchard analysis of the binding data in the presence of four inhibitory concns of heparin revealed that heparin did not affect the binding affinity of B for C3b but decreased the number of C3b sites recognized by B on the cells.	Heparin	106-113	complement C3	Homo sapiens	191-194
30653275-9	2019	Hpse knockdown using siRNA delayed epithelial growth in the first postnatal week ex vivo, which was similar to treating with the lower concentration of heparin.	Heparin	152-159	heparanase	Rattus norvegicus	0-4
6558419-7	1983	These results demonstrate that heparin prevents generation of the C3 amplification convertase by binding to cell-bound C3b and masking the binding site for B on C3b.	Heparin	31-38	complement C3	Homo sapiens	119-122
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	183-189
6558419-7	1983	These results demonstrate that heparin prevents generation of the C3 amplification convertase by binding to cell-bound C3b and masking the binding site for B on C3b.	Heparin	31-38	complement C3	Homo sapiens	161-164
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	rho/rac guanine nucleotide exchange factor (GEF) 2	Mus musculus	242-248
6577437-4	1983	The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and antithrombin III/factor Xa reactions differed in terms of apparent maximum velocity (Vmax) and apparent heparin-protease dissociation constant values.	Heparin	31-38	coagulation factor X	Homo sapiens	96-105
21216953-6	2011	Western blot analysis revealed that both tetrameric and dimeric alpha2M interacted with SDS-denatured beta2-m. At a physiologically relevant acidic pH and in the presence of heparin, alpha2M was also dissociated into dimers, and both tetrameric and dimeric alpha2M interacted with beta2-m, resulting in the inhibition of fibril growth reaction.	Heparin	174-181	alpha-2-macroglobulin	Homo sapiens	64-71
6310817-6	1983	This conclusion was further supported by the ability of heparin to reverse the inhibitory effect of altered factor Xa when the anticoagulant was added simultaneously to platelets.	Heparin	56-63	coagulation factor X	Homo sapiens	108-117
7085627-3	1982	Both clotting and amidolytic chromogenic assays were used to measure heparin-potentiated inhibition of both thrombin and Factor Xa.	Heparin	69-76	coagulation factor X	Homo sapiens	121-130
29974515-8	2019	We examined whether heparin could be cytoprotective: although it could not suppress LPC-triggered Ca2+ signal, p38 activation and mitochondrial membrane potential drop, it did suppress LPC-induced caspase 3 activation and alleviate LPC-inflicted cytotoxicity.	Heparin	20-27	caspase 3	Mus musculus	197-206
29974515-10	2019	Heparin is protective against LPC cytotoxicity and might intervene steps between mitochondrial membrane potential drop/p38 activation and caspase 3 activation.	Heparin	0-7	caspase 3	Mus musculus	138-147
30616835-2	2019	This polymorphism occurs in short consensus repeat (SCR) 7 of FH and results in decreased binding affinity of SCR6-8 for heparin.	Heparin	121-128	complement factor H	Homo sapiens	62-64
30616835-3	2019	As FH is responsible for regulating the complement system, decreased affinity for heparin results in decreased regulation on surfaces of self.	Heparin	82-89	complement factor H	Homo sapiens	3-5
21216953-6	2011	Western blot analysis revealed that both tetrameric and dimeric alpha2M interacted with SDS-denatured beta2-m. At a physiologically relevant acidic pH and in the presence of heparin, alpha2M was also dissociated into dimers, and both tetrameric and dimeric alpha2M interacted with beta2-m, resulting in the inhibition of fibril growth reaction.	Heparin	174-181	alpha-2-macroglobulin	Homo sapiens	183-190
7051949-3	1982	On activating surfaces of the alternative pathway, C3b, Bb is relatively resistant to regulation by H. In contrast, non-activating surfaces exhibit surface characteristics such as high content in membrane-associated sialic acid or heparin-related material which increase the interaction of H with cell-bound C3b.	Heparin	231-238	complement C3	Homo sapiens	51-54
30543092-3	2018	Additionally, we evaluated the roles  of  heparin-binding  epidermal-like  growth  factor  (HB-EGF)  and  matrix  metalloproteinases  (MMPs)  in  Ang  II-induced  EGFR  transactivation.	Heparin	42-49	epidermal growth factor receptor	Rattus norvegicus	163-167
21216953-6	2011	Western blot analysis revealed that both tetrameric and dimeric alpha2M interacted with SDS-denatured beta2-m. At a physiologically relevant acidic pH and in the presence of heparin, alpha2M was also dissociated into dimers, and both tetrameric and dimeric alpha2M interacted with beta2-m, resulting in the inhibition of fibril growth reaction.	Heparin	174-181	alpha-2-macroglobulin	Homo sapiens	183-190
21365655-10	2011	Therefore, we conclude that the interaction between beta2gpI and heparin is dependent on electrostatic interactions and on the conformation of beta2gpI.	Heparin	65-72	apolipoprotein H	Homo sapiens	143-151
7061710-5	1982	Platelet factor 4, protamine sulfate and diisopropylphosphoryl thrombin, all antagonists of the antithrombin III cofactor activity of heparin, significantly reduced the capacity of the preparation to inhibit thrombin.	Heparin	134-141	serpin family C member 1	Rattus norvegicus	96-112
21159364-4	2011	It is the aim of this study to investigate i) the effect of immunomodulatory treatment on endothelial cell tissue factor (TF) expression and function, ii) the regulation of the observed TF activity, and iii) the modulating effect of low molecular weight heparin and aspirin on TF activity in vitro.	Heparin	254-261	coagulation factor III, tissue factor	Homo sapiens	186-188
6175043-4	1982	In these respects it resembles "heparin cofactor A", which is, however, characterized by a substantially larger molecular weight.	Heparin	32-39	tubulin folding cofactor A	Homo sapiens	40-50
6918183-1	1981	Heparin in the fluid phase inhibits generation of the C3 amplification convertase of complement C3b,Bb.	Heparin	0-7	complement C3	Homo sapiens	96-99
6918183-5	1981	As for heparin, the major site of the inhibitory action of polycations is on the binding capacity of C3b for B.	Heparin	7-14	complement C3	Homo sapiens	101-104
21159364-4	2011	It is the aim of this study to investigate i) the effect of immunomodulatory treatment on endothelial cell tissue factor (TF) expression and function, ii) the regulation of the observed TF activity, and iii) the modulating effect of low molecular weight heparin and aspirin on TF activity in vitro.	Heparin	254-261	coagulation factor III, tissue factor	Homo sapiens	186-188
21289173-9	2011	Importantly, treatment with heparin or heparinase blocked LRP1-mediated cellular uptake of Abeta.	Heparin	28-35	prolow-density lipoprotein receptor-related protein 1	Cricetulus griseus	58-62
7280114-1	1981	Amounts of thromboxane A2 (TXA2) synthesized during the collagen-induced aggregation was much higher in citrated PRP than in heaprinized PRP implying that heparin might inhibit the synthesis of endoperoxide metabolites besides its anticoagulant action.	Heparin	155-162	proline rich protein 2-like 1	Rattus norvegicus	113-116
7280114-1	1981	Amounts of thromboxane A2 (TXA2) synthesized during the collagen-induced aggregation was much higher in citrated PRP than in heaprinized PRP implying that heparin might inhibit the synthesis of endoperoxide metabolites besides its anticoagulant action.	Heparin	155-162	proline rich protein 2-like 1	Rattus norvegicus	137-140
7280114-2	1981	Preincubation of citrated PRP with heparin resulted in dose dependent inhibition of the formation of TXA2 and PGE2.	Heparin	35-42	proline rich protein 2-like 1	Rattus norvegicus	26-29
7470199-0	1981	Effect of intrapulmonary heparin on lipoprotein lipase activity in mice.	Heparin	25-32	lipoprotein lipase	Mus musculus	36-54
7470199-1	1981	The lipoprotein lipase (LPL) activity obtained from the intrapulmonary administration of 2-10 mg of heparin in mice was compared with the same parameter measured for intravenously administered heparin.	Heparin	100-107	lipoprotein lipase	Mus musculus	4-22
7470199-1	1981	The lipoprotein lipase (LPL) activity obtained from the intrapulmonary administration of 2-10 mg of heparin in mice was compared with the same parameter measured for intravenously administered heparin.	Heparin	100-107	lipoprotein lipase	Mus musculus	24-27
21289173-12	2011	We also showed that heparin and a neutralizing antibody to LRP1 suppressed Abeta uptake in primary neurons.	Heparin	20-27	prolow-density lipoprotein receptor-related protein 1	Cricetulus griseus	59-63
7470199-3	1981	A relatively large dose of intrapulmonary heparin produced a peak LPL activity which was a third of the maximum response obtained from a small dose of i.v.	Heparin	42-49	lipoprotein lipase	Mus musculus	66-69
7470199-7	1981	administration of heparin produced dose-dependent increases in plasma LPL activity (correlation coefficient r = 0.9).	Heparin	18-25	lipoprotein lipase	Mus musculus	70-73
21104785-1	2011	The heparin-degrading endosulfatases sulfatase 1 (SULF1) and sulfatase 2 (SULF2) have opposing effects in hepatocarcinogenesis despite structural similarity.	Heparin	4-11	sulfatase 2	Homo sapiens	61-72
7222474-11	1981	5) Finally there is also an inhibitory effect of heparin on the activated Stuart-Prower factor.	Heparin	49-56	coagulation factor X	Homo sapiens	74-94
7419968-0	1980	Heparin inhibits thrombin binding to rabbit thoracic aorta endothelium.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	17-25
7419968-5	1980	However, incubation of the aorta in a thrombin solution containing 1 to 10 USP U/ml heparin did reduce enzyme binding to the endothelium by up to 60%.	Heparin	84-91	prothrombin	Oryctolagus cuniculus	38-46
7419968-6	1980	Similarly, the presence of heparin inhibited thrombin binding to the thoracic aorta of exsanguinated rabbits in situ.	Heparin	27-34	prothrombin	Oryctolagus cuniculus	45-53
7419968-7	1980	Endothelium, to which 125I-labeled thrombin was bound, lost 50% to 70% of the bound enzyme when suspended in a solution containing heparin (10 USP U/ml) and compared to the control incubated without heparin.	Heparin	131-138	prothrombin	Oryctolagus cuniculus	35-43
7419968-7	1980	Endothelium, to which 125I-labeled thrombin was bound, lost 50% to 70% of the bound enzyme when suspended in a solution containing heparin (10 USP U/ml) and compared to the control incubated without heparin.	Heparin	199-206	prothrombin	Oryctolagus cuniculus	35-43
7419968-8	1980	These observations are consistent with the proposal that a major portion of endothelium-bound thrombin may be associated with pericellular heparan sulfate; heparin competes for thrombin with the heparan sulfate sites, and because of its higher affinity for thrombin, heparin displaces bound thrombin from, or inhibits binding of free thrombin by, the endothelium.	Heparin	267-274	prothrombin	Oryctolagus cuniculus	94-102
7417517-1	1980	The heparin-accelerated neutralisation of bovine alpha and beta thrombins has been examined using a peptide substrate H-D-phenylalanyl-pipecolyl-arginine-paranitroanilide-HCl to measure thrombin amidase activity.	Heparin	4-11	coagulation factor II, thrombin	Bos taurus	64-72
7417517-3	1980	Low and high molecular weight heparin and heparins fractionated by their affinity for antithrombin III were all able to accelerate the neutralisation of alpha and beta thrombin.	Heparin	30-37	coagulation factor II, thrombin	Bos taurus	90-98
7417517-3	1980	Low and high molecular weight heparin and heparins fractionated by their affinity for antithrombin III were all able to accelerate the neutralisation of alpha and beta thrombin.	Heparin	42-50	coagulation factor II, thrombin	Bos taurus	90-98
7349668-1	1980	The reactions of covalently immobilized heparin, abbreviated as I-Hep, with thrombin or Factor Xa were investigated both in the presence and absence of antithrombin III, AT III.	Heparin	40-47	coagulation factor X	Homo sapiens	88-97
21104785-1	2011	The heparin-degrading endosulfatases sulfatase 1 (SULF1) and sulfatase 2 (SULF2) have opposing effects in hepatocarcinogenesis despite structural similarity.	Heparin	4-11	sulfatase 2	Homo sapiens	74-79
7374009-0	1980	[Antithrombin III level on the intravenous injection of tissue thromboplastin and heparin to rats with depressed blood anticoagulating system function due to an atherogenic diet].	Heparin	82-89	serpin family C member 1	Rattus norvegicus	1-17
7374009-3	1980	Preliminary intravenous injection of small doses of heparin into animals with depressed function of the anticoagulation system and low level of heparin in blood stimulates and promotes the binding of thrombin by antithrombin III under conditions of increased thrombinogenesis following intravenous injection of tissue thromboplastin.	Heparin	52-59	serpin family C member 1	Rattus norvegicus	212-228
7374009-3	1980	Preliminary intravenous injection of small doses of heparin into animals with depressed function of the anticoagulation system and low level of heparin in blood stimulates and promotes the binding of thrombin by antithrombin III under conditions of increased thrombinogenesis following intravenous injection of tissue thromboplastin.	Heparin	144-151	serpin family C member 1	Rattus norvegicus	212-228
21345279-2	2011	There is, however, increasing evidence questioning its safety, particularly in the critically ill. Heparin mainly confers its anticoagulant effect by binding to antithrombin.	Heparin	99-106	serpin family C member 1	Homo sapiens	161-173
7189413-4	1980	LDL inhibited the high molecular weight (but not low molecular weight) heparin accelerated neutralisation of factor Xa by antithrombin III.	Heparin	71-78	coagulation factor X	Homo sapiens	109-118
21345279-4	2011	Owing to antithrombin consumption and degradation, and to the binding of heparin to acute phase proteins, and to apoptotic and necrotic cells, critical illness confers heparin resistance.	Heparin	168-175	serpin family C member 1	Homo sapiens	9-21
7189413-6	1980	These observations suggest that certain plasma lipoproteins may selectively modulate the inhibitory action of heparin against factor Xa.	Heparin	110-117	coagulation factor X	Homo sapiens	126-135
21076043-0	2011	Heparin: a potent inhibitor of hepcidin expression in vitro and in vivo.	Heparin	0-7	hepcidin antimicrobial peptide	Homo sapiens	31-39
7362830-1	1980	Antithrombin III was purified from rat plasma in 70% yield by salting out with (NH4)2SO4, affinity chromatography on heparin-Sepharose 4B, and ion-exchange chromatography on DE-52.	Heparin	117-124	serpin family C member 1	Rattus norvegicus	0-16
21076043-2	2011	Here we show that exogenous heparin strongly inhibited hepcidin expression in hepatic HepG2 cells at pharmacologic concentrations, with a mechanism that probably involves bone morphogenetic protein 6 sequestering and the blocking of SMAD signaling.	Heparin	28-35	hepcidin antimicrobial peptide	Homo sapiens	55-63
21076043-4	2011	Moreover, we observed a strong reduction of serum hepcidin in 5 patients treated with heparin to prevent deep vein thrombosis, which was accompanied by an increase of serum iron and a reduction of C-reactive protein levels.	Heparin	86-93	hepcidin antimicrobial peptide	Homo sapiens	50-58
6445726-0	1980	[State of the thrombin-plasmin system in nephrotoxic nephritis treated with heparin, urokinase, and uroplasmin].	Heparin	76-83	prothrombin	Oryctolagus cuniculus	14-22
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	C-C motif chemokine ligand 2	Homo sapiens	180-214
6445726-3	1980	Heparin inoculated prophylactically prevented the development of nephritis and typical changes in the thrombin-plasmin system.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	102-110
6445726-4	1980	Treatment with heparin, urokinase or uroplasmin produced regression of nephritis, elimination of fibrin-positive substances from the kidneys and gradual complete normalization of the functional status of the thrombin-plasmin system.	Heparin	15-22	prothrombin	Oryctolagus cuniculus	208-216
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	C-C motif chemokine ligand 2	Homo sapiens	216-221
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	C-C motif chemokine ligand 2	Homo sapiens	222-226
7409614-1	1980	The heparin-antagonizing effect of human alpha 1-acid glycoprotein (alpha 1-acid GP) was studied by activated partial thromboplastin time (APTT) and by a factor Xa assay for heparin using a chromogenic substrate for factor Xa.	Heparin	4-11	coagulation factor X	Homo sapiens	154-163
20827464-6	2011	These heparin-immobilized microspheres exhibited broad dynamic ranges for binding to the four cytokines (aFGF, 1.0-1,000 ng/mL; VEGF, 0.5-1,000 ng/mL; CCL2, 1.95-1,000 ng/mL; CCL5, 1.95-500 ng/mL).	Heparin	6-13	C-C motif chemokine ligand 2	Homo sapiens	151-155
7409614-1	1980	The heparin-antagonizing effect of human alpha 1-acid glycoprotein (alpha 1-acid GP) was studied by activated partial thromboplastin time (APTT) and by a factor Xa assay for heparin using a chromogenic substrate for factor Xa.	Heparin	4-11	coagulation factor X	Homo sapiens	216-225
30781910-6	1979	Also thrombin infusion in rabbits induces an increase of both VHMWFC and HMWFC; pretreatment with heparin prevents these changes.	Heparin	98-105	prothrombin	Oryctolagus cuniculus	5-13
658785-4	1978	Heparin accelerates the saturation of antithrombin with factor Xa.	Heparin	0-7	coagulation factor X	Homo sapiens	56-65
21467632-2	2011	We prepared recombinant glutathione S-transferase-fused extracellular lectin-like domains (AA 94-231) of natural killer group 2A (NKG2A) (rGST-NKG2A) and NKG2C (rGST-NKG2C) and determined the binding of these receptors to plates coated with heparin-conjugated bovine serum albumin (heparin-BSA) and glycoproteins.	Heparin	241-248	killer cell lectin like receptor C1	Homo sapiens	105-128
720957-2	1978	When factor Xa was added to a system containing antithrombin III in excess and heparin in low concentration, the amount of factor Xa immediately inactivated was found to be a function of the concentration of heparin.	Heparin	79-86	coagulation factor X	Homo sapiens	5-14
21467632-3	2011	rGST-NKG2A and rGST-NKG2C directly bound to heparin-BSA with K(d) values of 20 and 40 nM, respectively.	Heparin	44-51	killer cell lectin like receptor C1	Homo sapiens	5-10
21467632-4	2011	Binding of rGST-NKG2A and rGST-NKG2C to heparin-BSA was suppressed in the presence of soluble heparin, heparan sulfate, fucoidan, lambda-carrageenan, and dextran sulfate.	Heparin	40-47	killer cell lectin like receptor C1	Homo sapiens	16-21
21467632-4	2011	Binding of rGST-NKG2A and rGST-NKG2C to heparin-BSA was suppressed in the presence of soluble heparin, heparan sulfate, fucoidan, lambda-carrageenan, and dextran sulfate.	Heparin	94-101	killer cell lectin like receptor C1	Homo sapiens	16-21
193712-1	1977	Human serum beta-lipoproteins, isolated by percipitation with heparin-calcium mixture, showed cholinesterase activity.	Heparin	62-69	butyrylcholinesterase	Rattus norvegicus	94-108
21467632-5	2011	2-O-Sulfate residues in heparin were essential for the binding of rGST-NKG2A and rGST-NKG2C.	Heparin	24-31	killer cell lectin like receptor C1	Homo sapiens	71-76
21467632-7	2011	This is the first report showing that NKG2A and NKG2C bind to heparin and alpha2,3-NeuAc-containing glycoproteins.	Heparin	62-69	killer cell lectin like receptor C1	Homo sapiens	38-43
20946474-5	2011	However, we recently demonstrated that co-expression of MT1-MMP and HB-EGF in gastric carcinoma cells leads to cleavage of HB-EGF within its N-terminal heparin-binding region, converting it into a potent heparin-independent growth factor.	Heparin	152-159	heparin binding EGF like growth factor	Homo sapiens	68-74
611046-2	1977	As expected, the sensitivity to heparin depended on the concentrations of AT-III and thrombin, whereas the fibrinogen level was less decisive.	Heparin	32-39	coagulation factor II, thrombin	Bos taurus	85-93
611046-4	1977	Thus, the sensitivity to heparin was greater with crude bovine thrombin than with highly purified thrombin from the same species.	Heparin	25-32	coagulation factor II, thrombin	Bos taurus	63-71
611046-7	1977	Smaller amounts of heparin were required to give a prolonged thrombin clotting time than in whole plasma, indicating that components of normal platelet-poor plasma (besides AT-III and fibrinogen) interfere with the anticoagulant effect of heparin.	Heparin	19-26	coagulation factor II, thrombin	Bos taurus	61-69
611046-7	1977	Smaller amounts of heparin were required to give a prolonged thrombin clotting time than in whole plasma, indicating that components of normal platelet-poor plasma (besides AT-III and fibrinogen) interfere with the anticoagulant effect of heparin.	Heparin	239-246	coagulation factor II, thrombin	Bos taurus	61-69
20946474-5	2011	However, we recently demonstrated that co-expression of MT1-MMP and HB-EGF in gastric carcinoma cells leads to cleavage of HB-EGF within its N-terminal heparin-binding region, converting it into a potent heparin-independent growth factor.	Heparin	152-159	heparin binding EGF like growth factor	Homo sapiens	123-129
22615650-2	2011	Thus, the aim of this study was to enhance the thermal stability and bio activity of a therapeutic FGF20 by addition of sucrose or heparin as additives and also at different temperatures.	Heparin	131-138	fibroblast growth factor 20	Homo sapiens	99-104
790496-0	1976	Effect of heparin on insulin secretion in vivo and in vitro.	Heparin	10-17	insulin	Canis lupus familiaris	21-28
22615650-6	2011	From 10  C to 60  C, no significant changes were observed in far-UV CD spectrum compared to the control, but significant changes were observed by adding sucrose when these temperatures are above 45  C. Upon addition of heparin and sucrose, the mitogenic activity increased significantly at all tested temperatures, and these changes may be related to the roles of heparin and sucrose on the structure and conformation of FGF20.	Heparin	219-226	fibroblast growth factor 20	Homo sapiens	421-426
22615650-7	2011	CONCLUSION: Results of this study suggest that heparin and sucrose as additives seems to benjm sufficient to prevent thermal inactivation of FGF20 and also maintain its conformation stability and bio activity.	Heparin	47-54	fibroblast growth factor 20	Homo sapiens	141-146
1244924-7	1976	The heparin requirements in the GSR rabbits were found to be in excess of those needed to neutralize a defibrinating dose of thrombin.	Heparin	4-11	prothrombin	Oryctolagus cuniculus	125-133
21829057-4	2011	Low-molecular-weight heparin decreases the concentrations of prothrombin fragments, D-dimers; orally administered anticoagulants reduce the concentrations of interleukin 6, von Willebrand factor, intercellular adhesion molecules, fibrinogen 1+2 and increases the concentration of plasminogen activator inhibitor-1.	Heparin	21-28	serpin family E member 1	Homo sapiens	280-313
1262050-8	1976	It seems to be limited by the ability of free heparin to potentiate the activity of C1-INH, and perhaps also by its direct effect upon the early acting C components.	Heparin	46-53	serpin family G member 1	Homo sapiens	84-90
955331-0	1976	Effect of heparin on lecithin: cholesterol acyltransferase and lipids in cholestasis.	Heparin	10-17	lecithin-cholesterol acyltransferase	Homo sapiens	21-58
22180365-6	2011	Although heparin decreased the phosphorylation of Smad1/5/8 after 0.5 h of culture, prolonged periods of culture with heparin enhanced the Smad phosphorylation.	Heparin	9-16	SMAD family member 1	Mus musculus	50-57
22180365-6	2011	Although heparin decreased the phosphorylation of Smad1/5/8 after 0.5 h of culture, prolonged periods of culture with heparin enhanced the Smad phosphorylation.	Heparin	9-16	SMAD family member 1	Mus musculus	50-54
1133068-6	1975	In 2 dogs, intravenous (IV) administration of heparin caused shifing of the lipoprotein electrophoretic pattern, indicating activated lipoprotein lipase.	Heparin	46-53	lipoprotein lipase	Canis lupus familiaris	134-152
22180365-7	2011	In addition, 72 h of treatment with heparin enhanced the mRNA expression of runx2 and osterix in BMP-2-stimulated MC3T3-E1 cells.	Heparin	36-43	runt related transcription factor 2	Mus musculus	76-81
21829577-7	2011	Heparin also decreased the level of beta-secretase (BACE1) and alpha-secretase (ADAM10).	Heparin	0-7	beta-site APP cleaving enzyme 1	Mus musculus	52-57
5822597-5	1969	In contrast to the effects of oleate infusion, elevation of plasma FFA to correspondingly high levels by triolein ingestion and intravenous heparin produced only small increases in plasma insulin, which did not correlate well with the FFA level reached, and small increases in plasma glucose.The results indicate that under certain conditions elevated FFA levels may be a potent stimulus of insulin secretion.	Heparin	140-147	insulin	Canis lupus familiaris	188-195
5794247-0	1969	Effect of heparin on the inactivation of serum lipoprotein lipase by the liver in unanesthetized dogs.	Heparin	10-17	lipoprotein lipase	Canis lupus familiaris	47-65
5794247-1	1969	The injection of heparin into the circulation produces a rapid increase in circulating serum lipoprotein lipase.	Heparin	17-24	lipoprotein lipase	Canis lupus familiaris	93-111
13253360-0	1955	[Heparin therapy of transfusional hemolytic reaction caused by blood group (ABO) incompatibility].	Heparin	1-8	ABO, alpha 1-3-N-acetylgalactosaminyltransferase and alpha 1-3-galactosyltransferase	Homo sapiens	76-79
32876926-1	2021	BACKGROUND: Binding of thyroglobulin (Tg) to heparin is involved in Tg transcytosis via megalin.	Heparin	45-52	LDL receptor related protein 2	Rattus norvegicus	88-95
33984481-2	2022	Postoperative unfractionated heparin dosing can be monitored by activated partial thromboplastin time (APTT) or by anti-factor Xa activity (anti-Xa).	Heparin	29-36	coagulation factor X	Homo sapiens	120-129
30622668-6	2018	Kallistatin via its heparin-binding site antagonizes TNF-alpha-induced senescence and superoxide formation, while kallistatin"s active site is essential for inhibiting miR-34a synthesis, thus elevating sirtuin 1 (SIRT1)/eNOS synthesis in EPCs.	Heparin	20-27	serpin family A member 4	Homo sapiens	0-11
21829577-7	2011	Heparin also decreased the level of beta-secretase (BACE1) and alpha-secretase (ADAM10).	Heparin	0-7	a disintegrin and metallopeptidase domain 10	Mus musculus	80-86
21129229-2	2010	Studies in animals have shown that LMW-heparins release lipoprotein lipase (LPL) as efficiently as unfractionated (UF) heparin, but are less able to retard hepatic uptake of the lipase.	Heparin	39-46	lipoprotein lipase	Homo sapiens	56-74
30259961-6	2018	For FXa inhibitors, a standard heparin-calibrated anti-Xa level of &lt; 0.1 IU.ml-1 should be measured, indicating sufficient reduction in the anticoagulant effect.	Heparin	31-38	coagulation factor X	Homo sapiens	4-7
30253213-1	2018	Self-assembling aliphatic heparin derivatives were shown to inhibit the immune system by antagonizing Toll-like receptor 4/myeloid differentiation protein 2 (TLR4/MD2).	Heparin	26-33	lymphocyte antigen 96	Homo sapiens	163-166
32885997-0	2021	A Systemwide Approach for Navigating the Dilemma of Oral Factor Xa Inhibitor Interference With Unfractionated Heparin Anti-Factor Xa Concentrations.	Heparin	110-117	coagulation factor X	Homo sapiens	57-66
32885997-0	2021	A Systemwide Approach for Navigating the Dilemma of Oral Factor Xa Inhibitor Interference With Unfractionated Heparin Anti-Factor Xa Concentrations.	Heparin	110-117	coagulation factor X	Homo sapiens	123-132
21129229-2	2010	Studies in animals have shown that LMW-heparins release lipoprotein lipase (LPL) as efficiently as unfractionated (UF) heparin, but are less able to retard hepatic uptake of the lipase.	Heparin	39-46	lipoprotein lipase	Homo sapiens	76-79
32885997-1	2021	BACKGROUND: Oral factor Xa inhibitors are known to significantly increase heparin anti-Xa concentrations, which leads to inaccuracies when monitoring intravenous unfractionated heparin (IV UFH).	Heparin	74-81	coagulation factor X	Homo sapiens	17-26
30539834-5	2018	Results: Significant difference was noted in the messenger RNA expression of VEGF, VEGFR, and HIF-1alpha after treating with heparin with a concentration of 15, 50, or 150 IU/ml in the A549 cell line at 24 and 48 h, respectively.	Heparin	125-132	kinase insert domain receptor	Homo sapiens	83-88
32885997-1	2021	BACKGROUND: Oral factor Xa inhibitors are known to significantly increase heparin anti-Xa concentrations, which leads to inaccuracies when monitoring intravenous unfractionated heparin (IV UFH).	Heparin	177-184	coagulation factor X	Homo sapiens	17-26
29730503-5	2018	In vitro analysis revealed that Fbln7 bound heparin at the N-terminal coiled-coil domain.	Heparin	44-51	fibulin 7	Mus musculus	32-37
20864536-8	2010	Furthermore, the heparan sulfate/heparin population was less sulfated in serglycin-deficient than in wild type mice indicative for the absence of heparin, which supports that heparin production is dependent on the serglycin core protein.	Heparin	33-40	serglycin	Mus musculus	73-82
30118980-5	2018	As proof of principle, we generated alkyne-modified heparin, immobilized it onto azide-incorporated acellular lungs, and demonstrated its bioactivity by Antithrombin III immobilization and Factor Xa inhibition.	Heparin	52-59	coagulation factor X	Homo sapiens	189-198
32959678-3	2021	Clinically, UFH is monitored through activated clotting time (ACT), activated partial thromboplastin time (aPTT), and anti-factor Xa assay.	Heparin	12-15	coagulation factor X	Homo sapiens	123-132
32959678-12	2021	CONCLUSION AND RELEVANCE: The adaption of a multifaceted anticoagulation protocol using anti-factor Xa assay may provide a better prediction of heparin dosing in adults ECMO patients compared with the conventional ACT-based protocol.	Heparin	144-151	coagulation factor X	Homo sapiens	93-102
30064820-10	2018	QCM-D analysis also showed binding of Stx2a to heparin and an impaired binding of AT to Stx2a-bound heparin.	Heparin	47-54	syntaxin 2	Homo sapiens	38-43
20864536-8	2010	Furthermore, the heparan sulfate/heparin population was less sulfated in serglycin-deficient than in wild type mice indicative for the absence of heparin, which supports that heparin production is dependent on the serglycin core protein.	Heparin	33-40	serglycin	Mus musculus	214-223
30064820-10	2018	QCM-D analysis also showed binding of Stx2a to heparin and an impaired binding of AT to Stx2a-bound heparin.	Heparin	100-107	syntaxin 2	Homo sapiens	88-93
20970300-0	2010	Study on anti-metastasis of heparin derivatives as ligand antagonist of p-selectin.	Heparin	28-35	selectin P	Homo sapiens	72-82
30064820-15	2018	The well-known non-beneficial administration of heparin in eHUS patients could be explained by the interaction of Stx2a with heparin.	Heparin	48-55	syntaxin 2	Homo sapiens	114-119
30064820-15	2018	The well-known non-beneficial administration of heparin in eHUS patients could be explained by the interaction of Stx2a with heparin.	Heparin	125-132	syntaxin 2	Homo sapiens	114-119
29999301-1	2018	Factor Xa (fXa) inhibition by antithrombin (AT) enabled by heparin or heparan sulfate is critical for controlling blood coagulation.	Heparin	59-66	coagulation factor X	Homo sapiens	0-9
29999301-1	2018	Factor Xa (fXa) inhibition by antithrombin (AT) enabled by heparin or heparan sulfate is critical for controlling blood coagulation.	Heparin	59-66	coagulation factor X	Homo sapiens	11-14
33026569-3	2021	We aimed to characterize the burden of CRRT filter clotting in COVID-19 infection and to describe a CRRT anticoagulation protocol that used anti-factor Xa levels for systemic heparin dosing.	Heparin	175-182	coagulation factor X	Homo sapiens	145-154
33026569-10	2021	An anticoagulation protocol using systemic unfractionated heparin, dosed by anti-factor Xa levels is reasonable approach to anticoagulation in this population.	Heparin	58-65	coagulation factor X	Homo sapiens	81-90
20970300-1	2010	Heparin has a potential value as therapeutic agents that block P-selectin-mediated cell adhesion and prevent tumor metastasis.	Heparin	0-7	selectin P	Homo sapiens	63-73
20970300-3	2010	Carboxyl and sulfate groups of heparin are closely related to its anticoagulant activity, so seven kinds of heparin derivatives related to carboxyl and sulfate groups were prepared, and their effects on anti-metastasis as ligand antagonist of p-selectin were studied.	Heparin	31-38	selectin P	Homo sapiens	243-253
33925501-2	2021	As a result, a number of nonvitamin K antagonist oral anticoagulants (NOAC) that directly target the enzymatic activity of factor II and factor Xa have been successfully licensed providing a more predictable effect and better safety profile compared to conventional anticoagulants (heparins and vitamin K antagonists (VKAs)).	Heparin	282-290	coagulation factor X	Homo sapiens	137-146
33610598-8	2021	Heparin-iron was also found to cause a reduction on hepcidin expression through BMP/SMAD and JAK/STAT3 pathways in LPS induced acute inflammation model in mice.	Heparin	0-7	hepcidin antimicrobial peptide	Mus musculus	52-60
33610598-9	2021	In ACD mice, heparin-iron could lower elevated serum hepcidin and improve anemia.	Heparin	13-20	hepcidin antimicrobial peptide	Mus musculus	53-61
33610598-10	2021	These findings demonstrated low anticoagulant heparin-iron has potential applications for the treatment of ACD with high hepcidin levels.	Heparin	46-53	hepcidin antimicrobial peptide	Mus musculus	121-129
32882780-3	2021	Methods: We evaluated the practical use of heparin-conjugated PLGA nanoparticles (molecular weight ~15,000) in conjugation with VEGF-A/C, embryoid body (EB) formation, and LEC differentiation using immunofluorescence staining followed by quantification and quantitative real-time polymerase chain reaction (qPCR) analysis.	Heparin	43-50	vascular endothelial growth factor A	Mus musculus	128-134
29874597-2	2018	In this regard, we designed a novel multifunctional nano-sized drug delivery system based on LyP-1 peptide-modified low-molecular-weight heparin-quercetin conjugate (PLQ).	Heparin	137-144	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	93-98
29874597-9	2018	STATEMENT OF SIGNIFICANCE: Herein, we successfully developed a novel amphiphilic nanomaterial, LyP-1-LMWH-Qu (PLQ) conjugate, consisting of a tumor-targeting moiety LyP-1, a hydrophobic quercetin (a multidrug resistance [MDR]-reversing drug) inner core, and a hydrophilic low-molecular-weight heparin (an antiangiogenic agent) outer shell for encapsulating and delivering a hydrophobic chemotherapeutic agent (gambogic acid).	Heparin	293-300	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	95-100
29812912-8	2018	We found that FGF1 binds CD44 through its heparin-binding moiety.	Heparin	42-49	CD44 molecule (Indian blood group)	Homo sapiens	25-29
20970300-3	2010	Carboxyl and sulfate groups of heparin are closely related to its anticoagulant activity, so seven kinds of heparin derivatives related to carboxyl and sulfate groups were prepared, and their effects on anti-metastasis as ligand antagonist of p-selectin were studied.	Heparin	108-115	selectin P	Homo sapiens	243-253
20685328-3	2010	The serpin, antithrombin, together with its cofactors, heparin and heparan sulfate, perform a critical anticoagulant function by preventing the activation of blood clotting proteinases except when needed at the site of a vascular injury.	Heparin	55-62	serpin family C member 1	Homo sapiens	12-24
29783776-3	2018	After the first heparin layer was coated on human umbilical vein endothelial cells (HUVECs) by means of the HBP-polyethylene glycol-phospholipid conjugate, HBP-HSA and heparin were then applied to the cell surface sequentially to form multiple layers.	Heparin	16-23	azurocidin 1	Homo sapiens	108-111
29783776-3	2018	After the first heparin layer was coated on human umbilical vein endothelial cells (HUVECs) by means of the HBP-polyethylene glycol-phospholipid conjugate, HBP-HSA and heparin were then applied to the cell surface sequentially to form multiple layers.	Heparin	16-23	azurocidin 1	Homo sapiens	156-159
33513400-7	2021	Additionally, OXT can promote gamma-interferon expression to inhibit cathepsin L and increases superoxide dismutase expression to reduce heparin and heparan sulphate fragmentation.	Heparin	137-144	oxytocin/neurophysin I prepropeptide	Homo sapiens	14-17
33336117-0	2021	Myocardial protection by heparin-based coacervate of FGF10.	Heparin	25-32	fibroblast growth factor 10	Mus musculus	53-58
20685328-7	2010	Binding of a specific heparin or heparan sulfate pentasaccharide to antithrombin induces allosteric activating changes that mitigate the unfavorable interactions and promote template bridging of the serpin and proteinase.	Heparin	22-29	serpin family C member 1	Homo sapiens	68-80
33336117-10	2021	The downstream signaling of the FGF10 was also investigated, with the western blot results showing that FGF10 coacervate activated the p-FGFR, PI3K/Akt and ERK1/2 pathways to a more proper level than free FGF10 or heparin+FGF10.	Heparin	214-221	fibroblast growth factor 10	Mus musculus	32-37
29462487-2	2018	Ovalbumin-related protein X (OVAX), a chicken egg white protein, has 77% sequence similarity to OVA and binds to heparin.	Heparin	113-120	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	0-27
33336117-10	2021	The downstream signaling of the FGF10 was also investigated, with the western blot results showing that FGF10 coacervate activated the p-FGFR, PI3K/Akt and ERK1/2 pathways to a more proper level than free FGF10 or heparin+FGF10.	Heparin	214-221	fibroblast growth factor 10	Mus musculus	104-109
29462487-2	2018	Ovalbumin-related protein X (OVAX), a chicken egg white protein, has 77% sequence similarity to OVA and binds to heparin.	Heparin	113-120	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	29-33
20682766-4	2010	Pikachurin-dystroglycan binding is calcium-dependent and relatively less sensitive to inhibition by heparin and high NaCl concentration, as compared with other dystroglycan ligand proteins.	Heparin	100-107	EGF-like, fibronectin type III and laminin G domains	Mus musculus	0-10
29462487-3	2018	In this study, structure characteristics and heparin-binding affinity of alkali-treated OVAX were investigated.	Heparin	45-52	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	88-92
29462487-10	2018	Consequently, it is suggested that alkali treatment causes the collapse of the OVAX heparin binding site, which might participate in regulating the functions of heparin.	Heparin	84-91	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	79-83
29462487-10	2018	Consequently, it is suggested that alkali treatment causes the collapse of the OVAX heparin binding site, which might participate in regulating the functions of heparin.	Heparin	161-168	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	79-83
33336117-10	2021	The downstream signaling of the FGF10 was also investigated, with the western blot results showing that FGF10 coacervate activated the p-FGFR, PI3K/Akt and ERK1/2 pathways to a more proper level than free FGF10 or heparin+FGF10.	Heparin	214-221	fibroblast growth factor 10	Mus musculus	104-109
33336117-10	2021	The downstream signaling of the FGF10 was also investigated, with the western blot results showing that FGF10 coacervate activated the p-FGFR, PI3K/Akt and ERK1/2 pathways to a more proper level than free FGF10 or heparin+FGF10.	Heparin	214-221	fibroblast growth factor 10	Mus musculus	104-109
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	caspase 3	Mus musculus	459-468
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	caspase 3	Mus musculus	469-478
33344474-8	2020	Mice in the heparin intervention group showed decreased levels of EH4, neutrophil gelatinase-associated lipocalin (NAGL), kidney injury molecule-1 (KIM-1), tumor necrosis factor-alpha (TNF-alpha), and interleukin (IL)-6 in the blood serum, longer average 72-h survival rate, significantly decreased kidney tissue edema, and a clearer glomerular structure coupled with decreased protein and mRNA expression levels of kidney apoptosis-related proteins (cleaved Caspase-3/Caspase-3 and Bax/Bcl-2) compared with those in the sepsis group at 6 h after CLP (P < 0.05).	Heparin	12-19	BCL2-associated X protein	Mus musculus	483-486
33257607-2	2020	Current guidelines suggest recombinant tissue plasminogen activator (not to exceed 100 mg) with unfractionated heparin.	Heparin	111-118	chromosome 20 open reading frame 181	Homo sapiens	39-67
28862013-0	2018	Influence of Direct Oral Anticoagulants on Anti-Factor Xa Measurements Utilized for Monitoring Heparin.	Heparin	95-102	coagulation factor X	Homo sapiens	48-57
28862013-1	2018	BACKGROUND: Unanticipated drug-laboratory interactions may occur between direct oral anticoagulants (DOACs) and anti-factor Xa (AXA) levels used to monitor parenteral heparin infusions.	Heparin	167-174	coagulation factor X	Homo sapiens	117-126
20142342-1	2010	BACKGROUND: Unfractionated heparin"s primary mechanism of action is to enhance the enzymatic activity of antithrombin (AT).	Heparin	27-34	serpin family C member 1	Homo sapiens	105-117
29346400-8	2018	In defibrinated, recalcified plasma, on the contrary, heparin is able to reduce CXCL5 and CXCL7 release from platelets by thrombin inhibition.	Heparin	54-61	C-X-C motif chemokine ligand 5	Homo sapiens	80-85
29024003-10	2017	In both cases, critical functional domains of FGF5, including one heparin binding site, are lost.	Heparin	66-73	fibroblast growth factor 5	Homo sapiens	46-50
32986858-8	2021	Here, we find by heparin affinity chromatography and NMR that an engineered XCL1 variant called CC5 can trigger a dose-dependent shift in XCL1"s metamorphic equilibrium such that the receptor binding structure is depleted, and the antimicrobial structure is more heavily populated.	Heparin	17-24	X-C motif chemokine ligand 1	Homo sapiens	76-80
32986858-8	2021	Here, we find by heparin affinity chromatography and NMR that an engineered XCL1 variant called CC5 can trigger a dose-dependent shift in XCL1"s metamorphic equilibrium such that the receptor binding structure is depleted, and the antimicrobial structure is more heavily populated.	Heparin	17-24	X-C motif chemokine ligand 1	Homo sapiens	138-142
33005203-5	2020	We, furthermore, investigated the influence of heparin on the expressions of TNF-alpha, IL-1beta, CD40, NF-kappaB, and HIF-1alpha after asphyxial CA.	Heparin	47-54	hypoxia inducible factor 1 subunit alpha	Rattus norvegicus	119-129
33005203-7	2020	Treatment with heparin significantly inhibited the upregulation of CD40, NF-kappaB, and HIF-1alpha induced by asphyxial CA.	Heparin	15-22	hypoxia inducible factor 1 subunit alpha	Rattus norvegicus	88-98
21433364-0	2010	High Throughput Screening for Small Molecule Inhibitors of Heparin-induced Tau Fibril Formation The microtubule-associated protein tau contributes directly or indirectly to key structural and regulatory cellular functions.	Heparin	59-66	microtubule associated protein tau	Homo sapiens	100-134
32677060-0	2020	The relationship between the initial anti-factor Xa measurement and the duration of direct oral anticoagulant influence in patients transitioning to heparin.	Heparin	149-156	coagulation factor X	Homo sapiens	42-51
32677060-2	2020	Factor-Xa inhibitors influence the heparin calibrated anti-factor Xa assay.	Heparin	35-42	coagulation factor X	Homo sapiens	0-9
32677060-2	2020	Factor-Xa inhibitors influence the heparin calibrated anti-factor Xa assay.	Heparin	35-42	coagulation factor X	Homo sapiens	59-68
32677060-3	2020	The University of Virginia (UVA) Medical Center utilized a corrected anti-factor Xa assay (c-AXA) during this transition period, which removes DOAC-mediated anti-factor Xa activity (d-AXA) and reflects heparin-specific activity.	Heparin	202-209	coagulation factor X	Homo sapiens	74-83
28987880-0	2017	Heparin-functionalized polymer graft surface eluting MK2 inhibitory peptide to improve hemocompatibility and anti-neointimal activity.	Heparin	0-7	MAPK activated protein kinase 2	Homo sapiens	53-56
20197127-0	2010	Surface modification with an antithrombin-heparin complex for anticoagulation: studies on a model surface with gold as substrate.	Heparin	42-49	serpin family C member 1	Homo sapiens	29-41
28742513-4	2017	Kallistatin via its heparin-binding site inhibits angiogenesis by blocking vascular endothelial growth factor (VEGF)-induced growth, migration and adhesion of endothelial cells.	Heparin	20-27	vascular endothelial growth factor A	Mus musculus	75-109
28742513-4	2017	Kallistatin via its heparin-binding site inhibits angiogenesis by blocking vascular endothelial growth factor (VEGF)-induced growth, migration and adhesion of endothelial cells.	Heparin	20-27	vascular endothelial growth factor A	Mus musculus	111-115
32703545-9	2020	The UFH group had a lower nadir PFL than the LMWH group (P = .03).	Heparin	4-7	profilin 2	Homo sapiens	32-35
20466649-1	2010	The hyaluronic acid receptor for endocytosis (HARE)/Stabilin-2 is the primary systemic scavenger receptor for 13 ligands including hyaluronan (HA), heparin and chondroitin sulfates.	Heparin	148-155	stabilin 2	Homo sapiens	4-44
32216028-0	2020	Anti-Factor IIa (FIIa) Heparin Assay for Patients on Direct Factor Xa (FXa) Inhibitors.	Heparin	23-30	coagulation factor X	Homo sapiens	60-69
32216028-0	2020	Anti-Factor IIa (FIIa) Heparin Assay for Patients on Direct Factor Xa (FXa) Inhibitors.	Heparin	23-30	coagulation factor X	Homo sapiens	71-74
32216028-1	2020	BACKGROUND: Direct factor Xa (FXa) inhibitors are increasingly prescribed for outpatients, and those transitioning to unfractionated heparin (UFH) for hospital admission are monitored via an anti-FXa assay.	Heparin	142-145	coagulation factor X	Homo sapiens	196-199
29091276-3	2017	Based on the structural knowledge available from the FGF1-heparin interaction studies, we have designed a novel heparin-binding peptide (HBP) affinity tag that can be used for the simple, efficient, and cost-effective purification of recombinant proteins of interest.	Heparin	58-65	azurocidin 1	Homo sapiens	112-135
29091276-3	2017	Based on the structural knowledge available from the FGF1-heparin interaction studies, we have designed a novel heparin-binding peptide (HBP) affinity tag that can be used for the simple, efficient, and cost-effective purification of recombinant proteins of interest.	Heparin	58-65	azurocidin 1	Homo sapiens	137-140
29091276-4	2017	HBP-tagged fusion proteins can be purified by heparin Sepharose affinity chromatography using a simple sodium chloride gradient to elute the bound fusion protein.	Heparin	46-53	azurocidin 1	Homo sapiens	0-3
20466649-1	2010	The hyaluronic acid receptor for endocytosis (HARE)/Stabilin-2 is the primary systemic scavenger receptor for 13 ligands including hyaluronan (HA), heparin and chondroitin sulfates.	Heparin	148-155	stabilin 2	Homo sapiens	46-50
20466649-1	2010	The hyaluronic acid receptor for endocytosis (HARE)/Stabilin-2 is the primary systemic scavenger receptor for 13 ligands including hyaluronan (HA), heparin and chondroitin sulfates.	Heparin	148-155	stabilin 2	Homo sapiens	52-62
32187355-5	2020	Induction of FXa activity by ICs containing IgG antibodies to platelet factor 4 (PF4) involved in heparin-induced thrombocytopenia (HIT), beta-2-glycoprotein-1 implicated in antiphospholipid syndrome, or red blood cells coated with anti-(alpha)-Rh(D) antibodies that mediate hemolysis in vivo was inhibited by a humanized monoclonal antibody (mAb) that blocks IgG binding to human FcRn.	Heparin	98-105	coagulation factor X	Homo sapiens	13-16
33043139-2	2020	Fibroblast Growth Factor-2 (FGF-2) and Vascular Endothelial Growth Factor-A (VEGF-A) induce hemorrhage in murine models with heparin exposure.	Heparin	125-132	vascular endothelial growth factor A	Mus musculus	39-75
33043139-2	2020	Fibroblast Growth Factor-2 (FGF-2) and Vascular Endothelial Growth Factor-A (VEGF-A) induce hemorrhage in murine models with heparin exposure.	Heparin	125-132	vascular endothelial growth factor A	Mus musculus	77-83
32302701-7	2020	RESULTS: Low-dose heparin posttreatment improved neurobehavioral function, brain edema, blood-brain barrier disruption and death in the cortex, associated with an increase in SphK1 and phosphorylated Akt, and a decrease in cleaved caspase-3.	Heparin	18-25	caspase 3	Mus musculus	231-240
20659659-5	2010	This review proposes that alternative anticoagulants (danaparoid, fondaparinux) that share certain properties of heparin-namely its irreversible antithrombin-mediated inhibition of factor Xa-and that have relatively long half-lives, have several advantages in the therapy for HIT over short-acting agents that inhibit thrombin directly (recombinant hirudin, argatroban, and bivalirudin).	Heparin	113-120	serpin family C member 1	Homo sapiens	145-157
31364287-7	2020	Bioinformatics analyses showed that these altered proteins were involved in various functions, including the kallikrein-related proteolytic cascade, immune response, and heparin binding.	Heparin	170-177	kallikrein related peptidase 4	Homo sapiens	109-119
20587521-3	2010	Processing of HB-EGF by proprotein convertases, and successively, by ADAM family proteases, generates a soluble growth factor that requires heparin as a cofactor.	Heparin	140-147	heparin binding EGF like growth factor	Homo sapiens	14-20
20587521-4	2010	Although heparin potentiates HB-EGF activity in vitro, it is not clear how the heparin-binding activity of HB-EGF is regulated.	Heparin	9-16	heparin binding EGF like growth factor	Homo sapiens	29-35
31517745-12	2019	CONCLUSION: Molecular-weight heparin and intraoperative intermittent pneumatic compression controls the hypercoagulation effect more efficiently when it is administered 1 hour before surgery: it causes significant reduction of F1+2, TAT, and MP-TF indexes and significant increases of fTFPI levels during and after laparoscopic fundoplication.	Heparin	29-36	coagulation factor XII	Homo sapiens	227-231
20711880-0	2010	Effect of the C-terminal domain peptide fragment (65-76) of monocytic chemotactic protein-1 (MCP-1) on the interaction between MCP-1 and heparin.	Heparin	137-144	C-C motif chemokine ligand 2	Homo sapiens	60-91
31222360-0	2019	Migration of chicken egg-white protein ovalbumin-related protein X and its alteration in heparin-binding affinity during embryogenesis of fertilized egg.	Heparin	89-96	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	39-66
31222360-1	2019	Ovalbumin-related protein X (OVAX) is a 50 kDa egg-white protein which has heparin-binding affinity.	Heparin	75-82	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	0-27
31222360-1	2019	Ovalbumin-related protein X (OVAX) is a 50 kDa egg-white protein which has heparin-binding affinity.	Heparin	75-82	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	29-33
31222360-6	2019	Heparin-sepharose chromatography, isothermal titrating calorimetry using fondaparinux as a ligand, and zeta potential measurement indicated that OVAX retained the heparin-binding affinity (Kd = 0.185 +- 0.037) even after 10 D incubation of fertilized egg, although the affinity was slightly decreased during egg incubation because of acidification of molecular surface charge.	Heparin	0-7	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	145-149
20711880-0	2010	Effect of the C-terminal domain peptide fragment (65-76) of monocytic chemotactic protein-1 (MCP-1) on the interaction between MCP-1 and heparin.	Heparin	137-144	C-C motif chemokine ligand 2	Homo sapiens	93-98
31222360-6	2019	Heparin-sepharose chromatography, isothermal titrating calorimetry using fondaparinux as a ligand, and zeta potential measurement indicated that OVAX retained the heparin-binding affinity (Kd = 0.185 +- 0.037) even after 10 D incubation of fertilized egg, although the affinity was slightly decreased during egg incubation because of acidification of molecular surface charge.	Heparin	163-170	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	145-149
31222360-7	2019	In conclusion, although heparin-binding ability of egg-white OVAX slightly decreases during embryogenesis, OVAX incorporated into embryo can retain heparin-binding affinity.	Heparin	24-31	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	61-65
20711880-0	2010	Effect of the C-terminal domain peptide fragment (65-76) of monocytic chemotactic protein-1 (MCP-1) on the interaction between MCP-1 and heparin.	Heparin	137-144	C-C motif chemokine ligand 2	Homo sapiens	127-132
31222360-7	2019	In conclusion, although heparin-binding ability of egg-white OVAX slightly decreases during embryogenesis, OVAX incorporated into embryo can retain heparin-binding affinity.	Heparin	148-155	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	107-111
20503388-6	2010	Gene expression of wnt7A increased dramatically beginning on day 3 and was enhanced even further on days 7 and 9 by heparin, whereas protein expression appeared at days 7 and 9.	Heparin	116-123	Wnt family member 7A	Homo sapiens	19-24
31222360-8	2019	Our findings provide a new insight that OVAX participates in the functions of heparin during embryogenesis.	Heparin	78-85	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	40-44
20561432-0	2010	[Preparation of recombinant polypeptide of N-terminal heparin-binding domain of fibronectin and its effect on disseminated intravascular coagulation in rats].	Heparin	54-61	fibronectin 1	Rattus norvegicus	80-91
32104478-4	2019	In the present study, we prepared sulfated chitooligosaccharides (SCOS), which have heparin-like properties, to improve the bioactivity of aFGF.	Heparin	84-91	fibroblast growth factor 1	Rattus norvegicus	139-143
20561432-1	2010	This study was aimed to prepare the polypeptide of N-terminal heparin-binding domain of fibronectin(rhFNHN-29 polypeptide) with pichia expression system, to detect biological activity of recombinant polypeptide and investigate its effect on disseminated intravascular coagulation (DIC) in rats.	Heparin	62-69	fibronectin 1	Rattus norvegicus	88-99
20561432-2	2010	The sequence of N-terminal heparin-binding domain of fibronectin was amplified from FNcDNA by PCR.	Heparin	27-34	fibronectin 1	Rattus norvegicus	53-64
20131286-9	2010	Heparin inhibited aPL binding and restored HB-EGF expression in a dose-dependent manner.	Heparin	0-7	heparin binding EGF like growth factor	Homo sapiens	43-49
31444404-0	2019	Low-molecular-weight-heparin increases Th1- and Th17-associated chemokine levels during pregnancy in women with unexplained recurrent pregnancy loss: a randomised controlled trial.	Heparin	21-28	negative elongation factor complex member C/D	Homo sapiens	39-42
31251821-6	2019	This case highlights the potential complications of using UFH anticoagulation following reversal of factor Xa inhibitors with andexanet alfa and underscores the importance of peri-procedural anticoagulation planning.	Heparin	58-61	coagulation factor X	Homo sapiens	100-109
20514621-0	2010	Conventional chromogenic heparin assays are influenced by patient"s endogenous plasma Antithrombin levels.	Heparin	25-32	serpin family C member 1	Homo sapiens	86-98
30947118-5	2019	The resulting surface combines the anti-coagulant (anti-FXa) function provided by the heparin and the anti-platelet activity of the catalytically produced NO.	Heparin	86-93	coagulation factor X	Homo sapiens	56-59
30727756-0	2019	Selective Inhibition of PAR4 (Protease-Activated Receptor 4)-Mediated Platelet Activation by a Synthetic Nonanticoagulant Heparin Analog.	Heparin	122-129	F2R like thrombin or trypsin receptor 3	Homo sapiens	24-28
30727756-0	2019	Selective Inhibition of PAR4 (Protease-Activated Receptor 4)-Mediated Platelet Activation by a Synthetic Nonanticoagulant Heparin Analog.	Heparin	122-129	F2R like thrombin or trypsin receptor 3	Homo sapiens	30-59
30727756-2	2019	Previous studies implied that thrombin exosite II, known as a binding site for heparin, may be involved in thrombin-induced PAR4 activation.	Heparin	79-86	F2R like thrombin or trypsin receptor 3	Homo sapiens	124-128
20422004-2	2010	Extracellular superoxide dismutase (ecSOD) is a major secreted extracellular enzyme that catalyzes the dismutation of superoxide to H(2)O(2), and anchors to EC surface through heparin-binding domain (HBD).	Heparin	176-183	superoxide dismutase 3, extracellular	Mus musculus	0-34
30935029-3	2019	MMP-9 expression was assessed in response to ethylenediaminetetraacetic acid, citrate, and high-/low-molecular-weight heparin (HMWH, LMWH) in co-culture experiments using THP-1, Jurkat, and HT cells (representing monocytes, T, and B cells).	Heparin	118-125	matrix metallopeptidase 9	Homo sapiens	0-5
20422004-2	2010	Extracellular superoxide dismutase (ecSOD) is a major secreted extracellular enzyme that catalyzes the dismutation of superoxide to H(2)O(2), and anchors to EC surface through heparin-binding domain (HBD).	Heparin	176-183	superoxide dismutase 3, extracellular	Mus musculus	36-41
20124439-7	2010	When the GPIHBP1-Q115P homozygote was given a 6-hour infusion of heparin, a significant amount of LPL appeared in the plasma, resulting in a fall in the plasma triglyceride levels from 1780 to 120 mg/dL.	Heparin	65-72	lipoprotein lipase	Homo sapiens	98-101
30590020-3	2019	We determined, however, that the most commonly used commercial assays in published literature were not specific or sensitive enough to detect levels of IL-21 in heparin plasma or serum from healthy human individuals.	Heparin	161-168	interleukin 21	Homo sapiens	152-157
30590020-10	2019	These ultrasensitive assays, for the first time, allow for the accurate quantitation of human IL-21 in heparin plasma and serum.	Heparin	103-110	interleukin 21	Homo sapiens	94-99
19517216-1	2010	Owing to its beneficial pharmacological profile, the low-molecular-weight heparin (LMWH) enoxaparin is increasingly being taken as an alternative to UFH in the treatment of ACS with an early invasive strategy and in elective percutaneous coronary interventions (PCI).	Heparin	74-81	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	173-176
30414409-4	2019	In in vitro assays with cells stably expressing human Sulfs, heparin, a structural analog of HS S-domains, promoted aggregation of transthyretin in an HS S-domain-dependent manner.	Heparin	61-68	transthyretin	Homo sapiens	131-144
20298971-4	2010	METHODS: Atomic force microscopy and transmission electron microscopy methodologies were used to determine the structure of tau assemblies that formed when soluble tau was incubated with heparin for increasing lengths of time.	Heparin	187-194	microtubule associated protein tau	Homo sapiens	124-127
31030744-6	2019	The anticoagulant activity of heparin is attributable to a 3-O-sulfate and 6-O-sulfate containing pentasaccharide sequence or a minimum eight-repeating disaccharide units containing the pentasaccharide sequence that catalyzes the suicidal inactivation of factor Xa or thrombin by a serpin or serine protease inhibitor named antithrombin III, respectively.	Heparin	30-37	coagulation factor II, thrombin	Bos taurus	268-276
31030744-7	2019	Thus, heparin is responsible for the simultaneous inhibition of both thrombin generation and thrombin activity in the blood circulation.	Heparin	6-13	coagulation factor II, thrombin	Bos taurus	69-77
20298971-4	2010	METHODS: Atomic force microscopy and transmission electron microscopy methodologies were used to determine the structure of tau assemblies that formed when soluble tau was incubated with heparin for increasing lengths of time.	Heparin	187-194	microtubule associated protein tau	Homo sapiens	164-167
30469334-2	2018	Density functional theory (DFT) has provided detailed information on the molecular structure and spin-spin coupling constants of heparin tetrasaccharide (GlcNS,6S-IdoA2S-GlcNS,6S-IdoA2S-OMe) representing the predominant heparin repeating-sequence.	Heparin	129-136	spindlin 1	Homo sapiens	97-101
20135058-3	2010	The main depolymerisation mechanism involves Hep radical intermediates that cleave the glycosidic linkage at unsulphated uronic acids followed by a 6-O-nonsulphated glucosamine, thus largely preserving the pentasaccharide sequence responsible for the binding to antithrombin III (AT).	Heparin	45-48	serpin family C member 1	Homo sapiens	262-278
30469334-2	2018	Density functional theory (DFT) has provided detailed information on the molecular structure and spin-spin coupling constants of heparin tetrasaccharide (GlcNS,6S-IdoA2S-GlcNS,6S-IdoA2S-OMe) representing the predominant heparin repeating-sequence.	Heparin	129-136	spindlin 1	Homo sapiens	102-106
19822709-3	2010	We have previously cloned and characterized two human extracellular endoglucosamine 6-sulfatases, HSulf-1 and HSulf-2, which selectively liberate the 6-O sulfate groups on glucosamines present in N, 6-O, and 2-O trisulfated disaccharides of intact HS and heparins.	Heparin	255-263	sulfatase 2	Homo sapiens	110-117
29956017-4	2018	Compared to the absence of heparin, treatment with heparin decreased the vascular endothelial growth factor (VEGF)-mediated activation of VEGFR2 and mitogenic effect on human lung microvascular endothelial cells in vitro.	Heparin	51-58	kinase insert domain receptor	Homo sapiens	138-144
29173042-1	2018	Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate.	Heparin	126-133	coagulation factor X	Homo sapiens	64-67
19822709-8	2010	We then developed an ELISA and confirmed that the RB4CD12 epitope in immobilized heparin was degraded by purified recombinant HSulf-1 and HSulf-2, and conditioned medium (CM) of MCF-7 breast carcinoma cells, which contain a native form of HSulf-2.	Heparin	81-88	sulfatase 2	Homo sapiens	138-145
19822709-8	2010	We then developed an ELISA and confirmed that the RB4CD12 epitope in immobilized heparin was degraded by purified recombinant HSulf-1 and HSulf-2, and conditioned medium (CM) of MCF-7 breast carcinoma cells, which contain a native form of HSulf-2.	Heparin	81-88	sulfatase 2	Homo sapiens	239-246
29638199-10	2018	CONCLUSION: This study investigates CD11b levels in response to an air stimulus in blood that was anticoagulated with citrate or heparin.	Heparin	129-136	integrin subunit alpha M	Homo sapiens	36-41
20075597-1	2010	AIM: Enhancement of lipoprotein lipase (LPL) activity through drug administration has been shown to increase pre-heparin serum LPL concentrations; however, pre-heparin serum LPL responses to exercise training have not been determined.	Heparin	113-120	lipoprotein lipase	Homo sapiens	20-38
29638199-12	2018	Activation of CD11b was less when using heparin as an anticoagulant compared to citrate.	Heparin	40-47	integrin subunit alpha M	Homo sapiens	14-19
29953858-6	2018	Moreover, ephrin-B3 binding affinities to heparin and CD44 in solution was strong.	Heparin	42-49	ephrin B3	Homo sapiens	10-19
20075597-1	2010	AIM: Enhancement of lipoprotein lipase (LPL) activity through drug administration has been shown to increase pre-heparin serum LPL concentrations; however, pre-heparin serum LPL responses to exercise training have not been determined.	Heparin	113-120	lipoprotein lipase	Homo sapiens	40-43
29717364-3	2018	The heparin effect on EC adhesion molecule (ICAM-1, VCAM-1, E-selectin) expression was also assessed.	Heparin	4-11	intercellular adhesion molecule 1	Homo sapiens	44-50
29999301-2	2018	AT activation by heparin has been investigated extensively, while interaction of heparin with trapped AT/fXa intermediates has received relatively little attention.	Heparin	81-88	coagulation factor X	Homo sapiens	105-108
29999301-6	2018	These species are also observed when the trapped intermediate is initially prepared in the presence of a short oligoheparin (dp6), followed by addition of a longer heparin chain (dp20), indicating that binding of heparin to AT/fXa complexes takes place after the inhibition event.	Heparin	116-123	coagulation factor X	Homo sapiens	227-230
29999301-9	2018	The observed post-inhibition binding of heparin to the trapped AT/fXa intermediates hints at the likely role played by heparan sulfate in their catabolism.	Heparin	40-47	coagulation factor X	Homo sapiens	66-69
20075597-1	2010	AIM: Enhancement of lipoprotein lipase (LPL) activity through drug administration has been shown to increase pre-heparin serum LPL concentrations; however, pre-heparin serum LPL responses to exercise training have not been determined.	Heparin	160-167	lipoprotein lipase	Homo sapiens	40-43
20075597-7	2010	RESULTS: Pre-heparin serum LPL concentrations were increased in the jogging group after 12 weeks compared with the baseline values (mean+/-SEM: 37.6+/-4.7 vs. 51.0+/-6.6 ng/mL, respectively, p= 0.033).	Heparin	13-20	lipoprotein lipase	Homo sapiens	27-30
20075597-9	2010	CONCLUSIONS: This study demonstrates that 12 weeks of jogging training increases pre-heparin serum LPL concentrations in overweight/obese middle-aged men.	Heparin	85-92	lipoprotein lipase	Homo sapiens	99-102
20024502-0	2010	Contribution of exosite occupancy by heparin to the regulation of coagulation proteases by antithrombin.	Heparin	37-44	serpin family C member 1	Homo sapiens	91-103
30061484-0	2018	Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures.	Heparin	112-119	advanced glycosylation end-product specific receptor	Homo sapiens	64-108
30061484-0	2018	Inhibition of Homophilic Interactions and Ligand Binding of the Receptor for Advanced Glycation End Products by Heparin and Heparin-Related Carbohydrate Structures.	Heparin	124-131	advanced glycosylation end-product specific receptor	Homo sapiens	64-108
30061484-1	2018	Background: Heparin and heparin-related sulphated carbohydrates inhibit ligand binding of the receptor for advanced glycation end products (RAGE).	Heparin	12-19	advanced glycosylation end-product specific receptor	Homo sapiens	94-138
30061484-1	2018	Background: Heparin and heparin-related sulphated carbohydrates inhibit ligand binding of the receptor for advanced glycation end products (RAGE).	Heparin	12-19	advanced glycosylation end-product specific receptor	Homo sapiens	140-144
30061484-1	2018	Background: Heparin and heparin-related sulphated carbohydrates inhibit ligand binding of the receptor for advanced glycation end products (RAGE).	Heparin	24-31	advanced glycosylation end-product specific receptor	Homo sapiens	94-138
30061484-1	2018	Background: Heparin and heparin-related sulphated carbohydrates inhibit ligand binding of the receptor for advanced glycation end products (RAGE).	Heparin	24-31	advanced glycosylation end-product specific receptor	Homo sapiens	140-144
20024502-1	2010	Heparin promotes the antithrombin (AT) inactivation of factors IXa (fIXa) and Xa (fXa) through a conformational activation of the serpin and also by a template mechanism in the presence of physiological levels of Ca2+.	Heparin	0-7	serpin family C member 1	Homo sapiens	21-33
30061484-2	2018	Here, we have studied the ability of heparin to inhibit homophilic interactions of RAGE in living cells and studied how heparin related structures interfere with RAGE-ligand interactions.	Heparin	37-44	advanced glycosylation end-product specific receptor	Homo sapiens	83-87
30061484-7	2018	Dimerisation of RAGE on the living cell surface was inhibited by heparin.	Heparin	65-72	advanced glycosylation end-product specific receptor	Homo sapiens	16-20
20807651-4	2010	The non-anticoagulant activity of heparin on metastasis includes the ability to inhibit cell-cell-interaction through blocking of P- and L-selectin, to inhibit extracellular matrix protease heparanase, and to inhibit angiogenesis.	Heparin	34-41	selectin L	Homo sapiens	137-147
30016181-11	2018	UFH inhibited LPS-induced phosphorylation of IkappaB-alpha, c-Jun, ERK1/2, JNK, and p38 MAPK but not c-fos.	Heparin	0-3	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	60-65
19966216-4	2009	In this study we demonstrate that PDGF-AA binds directly to fibronectin and that this association is greatly enhanced by heparin.	Heparin	121-128	platelet derived growth factor subunit A L homeolog	Xenopus laevis	34-38
19843180-8	2009	We confirmed that citrullination of antithrombin abolished its activity; this abolition of activity was accelerated by heparin, which facilitated the early citrullination of Arg393 (P1 residue).	Heparin	119-126	serpin family C member 1	Homo sapiens	36-48
30091727-7	2018	Ejection fraction, fractional shortening and levels of VEGF significantly improved in MSCsand MSCs + heparin group (P&lt;0.05).	Heparin	101-108	vascular endothelial growth factor A	Oryctolagus cuniculus	55-59
19689925-1	2009	BACKGROUND &amp; AIMS: Heparin-binding epidermal growth factor-like growth factor (HB-EGF) is produced as a type-I, single-pass transmembrane protein that can be cleaved to release a diffusible peptide.	Heparin	23-30	heparin binding EGF like growth factor	Homo sapiens	83-89
29988697-5	2018	We administered recombinant tissue plasminogen activator for suspected pulmonary embolism to successfully resuscitate the patient experiencing refractory cardiac arrest despite heparin infusion.	Heparin	177-184	chromosome 20 open reading frame 181	Homo sapiens	28-56
19996706-2	2009	In order to apply this technology to tissue engineering, we have developed nanoscaled 3D scaffolds consisting of growth factor-loaded heparin/poly(l-lysine) nanoparticles (NPs) attached to the surface of polymeric microspheres via polyionic complex methods.	Heparin	134-141	myotrophin	Rattus norvegicus	113-126
29106676-1	2018	Background: Taurolidine citrate with heparin (Taurolock/Hep) is a promising central venous catheter lock solution.	Heparin	37-44	DNL-type zinc finger	Homo sapiens	56-59
19888512-1	2009	The elucidation of the structure of the antithrombin binding sequence in heparin has given a large impulse to the rational design of heparin related drugs.	Heparin	73-80	serpin family C member 1	Homo sapiens	40-52
29371243-9	2018	Arterial macrophage numbers decreased after heparin-mediated LpL cell dissociation and by genetic knockout of arterial LpL.	Heparin	44-51	lipoprotein lipase	Mus musculus	61-64
19769346-7	2009	In contrast, the pseudophosphorylation mimic of tau efficiently interacts with the polyanion heparin.	Heparin	93-100	microtubule associated protein tau	Homo sapiens	48-51
29212374-0	2018	Performance of Anti-Factor Xa Versus Activated Partial Thromboplastin Time for Heparin Monitoring Using Multiple Nomograms.	Heparin	79-86	coagulation factor X	Homo sapiens	20-29
28735423-8	2017	In contrast, D-dimer and prothrombin fragment F1+2 plasma levels indicated a higher activation of the coagulation cascade in apixaban/heparin than in rivaroxaban/heparin patients.	Heparin	134-141	coagulation factor XII	Homo sapiens	46-50
19723805-3	2009	Indeed, heparin, heparitinase treatment and mutation of the Thy-1 heparin-binding site each inhibited Thy-1-induced RhoA activation, as well as formation of focal adhesions and stress fibers in DI TNC(1) astrocytes.	Heparin	8-15	Thy-1 cell surface antigen	Homo sapiens	102-107
28575981-5	2017	We have developed an ultrathin nanofilm of starPEG with incorporated heparin (Hep-PEG) that binds covalently to the amine groups of islet surface membrane via its N-hydroxysuccinimide groups.	Heparin	69-76	DNL-type zinc finger	Homo sapiens	78-81
28871223-0	2017	Effects of Enzymatically Depolymerized Low Molecular Weight Heparins on CCl4-Induced Liver Fibrosis.	Heparin	60-68	chemokine (C-C motif) ligand 4	Mus musculus	72-76
28671597-6	2017	For all heparins, potentiation of thrombin inhibition by antithrombin and heparin cofactor II was preferentially neutralized over antithrombin-mediated inhibition of factor Xa or plasma clotting time.	Heparin	8-16	coagulation factor II, thrombin	Bos taurus	34-42
29701427-0	2017	Heparin Resistance During Surgical Resection of Inferior Vena Cava and Right Atrial Tumor Thrombus: A Case Report.	Heparin	0-7	carbonic anhydrase 5A	Homo sapiens	62-66
29289480-3	2018	Here we focused on the Delta-unsaturated 2-sulfouronic acid-N-sulfoglucosamine (D2S0), which is a sulfated disaccharide derived from heparin, as a candidate compound for a pharmacological chaperone for MPS II, and analyzed the chaperone effect of the saccharide on IDS by using recombinant protein and cells expressing mutated enzyme.	Heparin	133-140	iduronate 2-sulfatase	Homo sapiens	265-268
28986203-16	2018	Pre-clinical studies demonstrated that the basic proteins lactoferrin, platelet factor-4 (PF-4), IL-8 and polyarginine, as a model of the eosinophil cationic protein (ECP), found in COPD sputum neutralise the anticoagulant activity of heparin.	Heparin	235-242	ribonuclease A family member 3	Homo sapiens	138-165
28986203-16	2018	Pre-clinical studies demonstrated that the basic proteins lactoferrin, platelet factor-4 (PF-4), IL-8 and polyarginine, as a model of the eosinophil cationic protein (ECP), found in COPD sputum neutralise the anticoagulant activity of heparin.	Heparin	235-242	ribonuclease A family member 3	Homo sapiens	167-170
19723805-3	2009	Indeed, heparin, heparitinase treatment and mutation of the Thy-1 heparin-binding site each inhibited Thy-1-induced RhoA activation, as well as formation of focal adhesions and stress fibers in DI TNC(1) astrocytes.	Heparin	66-73	Thy-1 cell surface antigen	Homo sapiens	60-65
28377232-11	2017	More patients received GPIIb/IIIa antagonist in the UFH group (30% vs. 3%; p &lt;0.001).	Heparin	52-55	integrin subunit alpha 2b	Homo sapiens	23-28
19723805-3	2009	Indeed, heparin, heparitinase treatment and mutation of the Thy-1 heparin-binding site each inhibited Thy-1-induced RhoA activation, as well as formation of focal adhesions and stress fibers in DI TNC(1) astrocytes.	Heparin	66-73	Thy-1 cell surface antigen	Homo sapiens	102-107
19608732-6	2009	HB-EGF binds to and activates two receptors, epidermal growth factor receptor (EGFR) and ErbB4, as well as heparin moieties and CD9/DRAP27.	Heparin	107-114	heparin binding EGF like growth factor	Homo sapiens	0-6
28574291-0	2017	Temperature-sensitive heparin-modified poloxamer hydrogel with affinity to KGF facilitate the morphologic and functional recovery of the injured rat uterus.	Heparin	22-29	fibroblast growth factor 7	Rattus norvegicus	75-78
28574291-4	2017	Here, a temperature-sensitive heparin-modified poloxamer (HP) hydrogel with affinity to KGF (KGF-HP) was used as a support matrix to prevent IUA and deliver KGF.	Heparin	30-37	fibroblast growth factor 7	Rattus norvegicus	88-91
28574291-4	2017	Here, a temperature-sensitive heparin-modified poloxamer (HP) hydrogel with affinity to KGF (KGF-HP) was used as a support matrix to prevent IUA and deliver KGF.	Heparin	30-37	fibroblast growth factor 7	Rattus norvegicus	93-99
28574291-4	2017	Here, a temperature-sensitive heparin-modified poloxamer (HP) hydrogel with affinity to KGF (KGF-HP) was used as a support matrix to prevent IUA and deliver KGF.	Heparin	30-37	fibroblast growth factor 7	Rattus norvegicus	93-96
28427524-4	2017	Kallistatin"s heparin-binding site is crucial for antagonizing the signaling pathways of vascular endothelial growth factor, tumor necrosis factor-alpha, Wnt, transforming growth factor-beta and epidermal growth factor.	Heparin	14-21	serpin family A member 4	Homo sapiens	0-11
28650000-2	2017	Parenteral anticoagulants with an indirect inhibitory action on FXa (low-molecular-weight heparins) have a well-established clinical efficacy in the prophylaxis and therapy of thromboembolic conditions.	Heparin	90-98	coagulation factor X	Homo sapiens	64-67
19614626-9	2009	Heparin, which acts as a pro-survival factor in human trophoblast, attenuated the anti-beta(2)GPI antibody-mediated cell death, and also the pro-inflammatory response, but only at high concentrations.	Heparin	0-7	apolipoprotein H	Homo sapiens	87-97
28087378-6	2017	The scaffolds were prepared from poly(lactic-co-glycolic acid), and BMP-7/TGF-beta3 were loaded as nanocomplexes with heparin and Tetronic 1107.	Heparin	118-125	bone morphogenetic protein 7	Homo sapiens	68-73
29089529-6	2017	Surprisingly, we found that heparin at physiological concentration can enhance HBV infection in a PreS1-peptide sensitive, NTCP-dependent manner in both HepaRG and HepG2-NTCP-AS cells.	Heparin	28-35	large envelope protein;middle envelope protein;small envelope protein	Hepatitis B virus	98-103
28118750-5	2017	Moreover, it was found that lower concentrations of the tested ovine-derived mucosal heparin are required to form the large PF4/heparin complexes as compared to mucosal porcine and bovine heparin.	Heparin	128-135	platelet factor 4	Bos taurus	124-127
19468011-3	2009	Thrombin-inducible cleavage of PAR-1 was inhibited by heparin, but not affected by bivalirudin (P = 0.0001).	Heparin	54-61	Prader Willi/Angelman region RNA 1	Homo sapiens	31-36
29093604-10	2017	A significant decrease in CCL5 expression was only detected in KLE cells following treatment with heparin and paclitaxel, and an increase in the expression of CCL5 in RL 95-2 cells.	Heparin	98-105	C-C motif chemokine ligand 5	Homo sapiens	26-30
28405641-3	2017	Herein, we develop an aggregation-induced emission (AIE) probe HPQ-TBP-I for light up detection of heparin based on the electrostatic interaction-triggered formation of the HPQ-TBP/heparin complex and simultaneous displacement of the fluorescence quencher iodide ion.	Heparin	99-106	TATA-box binding protein	Homo sapiens	67-70
28405641-3	2017	Herein, we develop an aggregation-induced emission (AIE) probe HPQ-TBP-I for light up detection of heparin based on the electrostatic interaction-triggered formation of the HPQ-TBP/heparin complex and simultaneous displacement of the fluorescence quencher iodide ion.	Heparin	99-106	TATA-box binding protein	Homo sapiens	177-180
28405641-3	2017	Herein, we develop an aggregation-induced emission (AIE) probe HPQ-TBP-I for light up detection of heparin based on the electrostatic interaction-triggered formation of the HPQ-TBP/heparin complex and simultaneous displacement of the fluorescence quencher iodide ion.	Heparin	181-188	TATA-box binding protein	Homo sapiens	67-70
19468011-4	2009	Further, PAR-1 internalization was more effectively inhibited by heparin than bivalirudin (P = 0.002).	Heparin	65-72	Prader Willi/Angelman region RNA 1	Homo sapiens	9-14
28405641-3	2017	Herein, we develop an aggregation-induced emission (AIE) probe HPQ-TBP-I for light up detection of heparin based on the electrostatic interaction-triggered formation of the HPQ-TBP/heparin complex and simultaneous displacement of the fluorescence quencher iodide ion.	Heparin	181-188	TATA-box binding protein	Homo sapiens	177-180
28397746-0	2017	Non-Anticoagulant Heparins Are Hepcidin Antagonists for the Treatment of Anemia.	Heparin	18-26	hepcidin antimicrobial peptide	Mus musculus	31-39
28979172-4	2017	Andexanet alfa is a FXa decoy designed to reverse all anticoagulants that act through this part of the coagulation cascade including anti-FXa DOACs, such as apixaban, edoxaban and rivaroxaban, and indirect FXa inhibitors such as low-molecular-weight heparins.	Heparin	250-258	coagulation factor X	Homo sapiens	20-23
28877477-0	2017	Heparin Increases Food Intake through AgRP Neurons.	Heparin	0-7	agouti related neuropeptide	Homo sapiens	38-42
28877477-3	2017	By using electrophysiological, pharmacological, molecular biological, and chemogenetic approaches, we provide evidence that heparin increases food intake by stimulating AgRP neurons and increasing AgRP release.	Heparin	124-131	agouti related neuropeptide	Homo sapiens	169-173
28877477-3	2017	By using electrophysiological, pharmacological, molecular biological, and chemogenetic approaches, we provide evidence that heparin increases food intake by stimulating AgRP neurons and increasing AgRP release.	Heparin	124-131	agouti related neuropeptide	Homo sapiens	197-201
28877477-4	2017	Our results support a model whereby heparin competes with insulin for insulin receptor binding on AgRP neurons, and by doing so it inhibits FoxO1 activity to promote AgRP release and feeding.	Heparin	36-43	agouti related neuropeptide	Homo sapiens	98-102
28877477-4	2017	Our results support a model whereby heparin competes with insulin for insulin receptor binding on AgRP neurons, and by doing so it inhibits FoxO1 activity to promote AgRP release and feeding.	Heparin	36-43	agouti related neuropeptide	Homo sapiens	166-170
28397746-2	2017	In fact, heparins are strong suppressors of hepcidin expression in hepatic cell lines that act by inhibiting the phosphorylation of SMAD1/5/8 proteins elicited by the BMPs.	Heparin	9-17	hepcidin antimicrobial peptide	Mus musculus	44-52
28397746-3	2017	The inhibitory effect of heparins has been demonstrated in cells and in mice, where subcutaneous injections of non-anticoagulant heparins inhibited liver hepcidin expression and increased iron bioavailability.	Heparin	25-33	hepcidin antimicrobial peptide	Mus musculus	154-162
28397746-3	2017	The inhibitory effect of heparins has been demonstrated in cells and in mice, where subcutaneous injections of non-anticoagulant heparins inhibited liver hepcidin expression and increased iron bioavailability.	Heparin	129-137	hepcidin antimicrobial peptide	Mus musculus	154-162
28397746-5	2017	The most potent heparins have been found to be the super-sulfated ones, active in hepcidin suppression with a molecular weight as low as 4 kDa.	Heparin	16-24	hepcidin antimicrobial peptide	Mus musculus	82-90
28397746-6	2017	Moreover, the alteration of endogenous heparan sulfates has been found to cause a reduction in hepcidin expression in vitro and in vivo, indicating that heparins act by interfering with the interaction between BMPs and components of the complex involved in the activation of the BMP/SMAD1/5/8 pathway.	Heparin	153-161	hepcidin antimicrobial peptide	Mus musculus	95-103
28397746-7	2017	This review summarizes recent findings on the anti-hepcidin activity of heparins and their possible use for the treatment of anemia caused by hepcidin excess, including the anemia of chronic diseases.	Heparin	72-80	hepcidin antimicrobial peptide	Mus musculus	51-59
28238530-6	2017	Heparin capacitated samples had a significant decrease in LDH and CK activities, while in hyaluronic acid capacitated samples LDH and CK activities both increased compared to control samples, in heparin and hyaluronic acid capacitation conditions, respectively.	Heparin	0-7	LDH	Bos taurus	58-61
19468011-5	2009	Conclusion Heparin has stronger inhibitory effects on thrombin-dependent PAR-1 cleavage and internalization, thus providing a biological explanation for lower clinical bleeding rates with bivalirudin.	Heparin	11-18	Prader Willi/Angelman region RNA 1	Homo sapiens	73-78
19564340-10	2009	Also, MASP-1"s multifunctional behavior as both a complement and a coagulation enzyme is in accordance with our observation that antithrombin in the presence of heparin is a more potent inhibitor of MASP-1 than C1 inhibitor.	Heparin	161-168	MBL associated serine protease 1	Homo sapiens	6-12
28299286-6	2017	By expressing R. conorii Adr1 on the surface of non-pathogenic E. coli, we demonstrate that the interaction between Adr1 and vitronectin is salt-sensitive and cannot be interrupted by addition of heparin.	Heparin	196-203	vitronectin	Homo sapiens	125-136
28478442-6	2017	However, the F1 + 2 increase in women exposed to heparin prophylaxis was significantly lower than that in normal pregnant women in all 3 measurements carried out during gestation (p &lt; 0.05); a statistically significant inverse correlation between F1 + 2 levels and anti-Xa activity (R = -0.8575, p &lt; 0.05) was observed in treated women during pregnancy.	Heparin	49-56	coagulation factor XII	Homo sapiens	13-19
28478442-6	2017	However, the F1 + 2 increase in women exposed to heparin prophylaxis was significantly lower than that in normal pregnant women in all 3 measurements carried out during gestation (p &lt; 0.05); a statistically significant inverse correlation between F1 + 2 levels and anti-Xa activity (R = -0.8575, p &lt; 0.05) was observed in treated women during pregnancy.	Heparin	49-56	coagulation factor XII	Homo sapiens	250-256
19564340-10	2009	Also, MASP-1"s multifunctional behavior as both a complement and a coagulation enzyme is in accordance with our observation that antithrombin in the presence of heparin is a more potent inhibitor of MASP-1 than C1 inhibitor.	Heparin	161-168	serpin family C member 1	Homo sapiens	129-141
19564340-10	2009	Also, MASP-1"s multifunctional behavior as both a complement and a coagulation enzyme is in accordance with our observation that antithrombin in the presence of heparin is a more potent inhibitor of MASP-1 than C1 inhibitor.	Heparin	161-168	MBL associated serine protease 1	Homo sapiens	199-205
19185514-0	2009	Differentiation of 3-O-sulfated heparin disaccharide isomers: identification of structural aspects of the heparin CCL2 binding motif.	Heparin	32-39	C-C motif chemokine ligand 2	Homo sapiens	114-118
27917715-4	2017	The direct oral anticoagulants (DOACs) inhibiting factor Xa or thrombin activity represent an alternative for heparins and VKAs.	Heparin	110-118	coagulation factor X	Homo sapiens	50-59
27736032-15	2017	However, anti-FXa levels were relatively increased over anti-FIIa levels in infants and after high-dose UFH bolus administration.	Heparin	104-107	coagulation factor X	Homo sapiens	14-17
27862941-6	2016	It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin).	Heparin	37-44	coagulation factor X	Homo sapiens	173-182
19185514-1	2009	The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection.	Heparin	53-60	serpin family C member 1	Homo sapiens	107-123
19452598-0	2009	The critical role of hinge-region expulsion in the induced-fit heparin binding mechanism of antithrombin.	Heparin	63-70	serpin family C member 1	Homo sapiens	92-104
28133197-6	2016	Owing to elevated D-dimer and CA125 levels as well as multiple liver metastases, the patient was diagnosed with Trousseau"s syndrome and treated using heparin-based anticoagulant therapy.	Heparin	151-158	mucin 16, cell surface associated	Homo sapiens	30-35
17895513-0	2009	Unfractionated heparin but not enoxaparin causes delayed plasma PAI-1 depletion in hemodialysis patients: a prospective study.	Heparin	15-22	serpin family E member 1	Homo sapiens	64-69
27783665-6	2016	Given the known potentiating effect of heparin on C1-INH, sulfated glycans (SG) may be such candidates.	Heparin	39-46	serpin family G member 1	Homo sapiens	50-56
27301751-0	2016	Blocking inhibition of prothrombinase by tissue factor pathway inhibitor alpha: a procoagulant property of heparins.	Heparin	107-115	coagulation factor X	Homo sapiens	23-37
27301751-2	2016	UFH prevents tissue factor pathway inhibitor alpha (TFPIalpha) from inhibiting the procoagulant enzyme complex, prothrombinase, providing a possible mechanism for its procoagulant activity.	Heparin	0-3	coagulation factor X	Homo sapiens	112-126
27583038-10	2016	There may be reinforcement in the sole utilization of heparin confining GP IIb/IIIa inhibitors and other intravenous antithrombotics to bailout therapy for periprocedural PCI complications in AMI patients".	Heparin	54-61	integrin subunit alpha 2b	Homo sapiens	72-78
17895513-5	2009	RESULTS: The switch from LMWH to UFH resulted in decreased pre-HD levels of PAI-1 and TM and increased PF 1+2 concentrations.	Heparin	33-36	serpin family E member 1	Homo sapiens	76-81
26920026-6	2016	Cell attachment to PRELP was inhibited by addition of soluble heparin or heparan sulfate (HS), by blocking sulfation of the fibroblasts or by treating the cells with a combination of chondroitinase and heparinase.	Heparin	62-69	proline and arginine rich end leucine rich repeat protein	Rattus norvegicus	19-24
19101225-9	2009	The impact of concomitant heparin administration on the clearance of PAPP-A from the circulation was also explored in mice.	Heparin	26-33	pregnancy-associated plasma protein A	Mus musculus	69-75
19580651-3	2009	We hypothesized that subcutaneous injections of unfractionated heparin and enoxaparin would decrease neutrophil infiltration, lung edema, and plasminogen-activator inhibitor-1 (PAI-1) production in mice exposed to high-tidal-volume ventilation.	Heparin	63-70	serine (or cysteine) peptidase inhibitor, clade E, member 1	Mus musculus	142-175
26876877-10	2016	Factor Xa analysis indicated that the heparin conjugate was still active on the cell surface at 24h post-coating.	Heparin	38-45	coagulation factor X	Homo sapiens	0-9
26979432-0	2016	Sialylation of vitronectin regulates stress fiber formation and cell spreading of dermal fibroblasts via a heparin-binding site.	Heparin	107-114	vitronectin	Mus musculus	15-26
19580651-3	2009	We hypothesized that subcutaneous injections of unfractionated heparin and enoxaparin would decrease neutrophil infiltration, lung edema, and plasminogen-activator inhibitor-1 (PAI-1) production in mice exposed to high-tidal-volume ventilation.	Heparin	63-70	serine (or cysteine) peptidase inhibitor, clade E, member 1	Mus musculus	177-182
26979432-10	2016	Furthermore, de-sialylation increased the binding activity of VN to heparin, as detected by surface plasmon resonance (SPR).	Heparin	68-75	vitronectin	Mus musculus	62-64
19580651-12	2009	Understanding the protective mechanism of unfractionated heparin and enoxaparin related to the reduction of PAI-1 may afford further knowledge of the effects of mechanical forces in the lung and development of possible therapeutic strategies involved in acute lung injury.	Heparin	57-64	serine (or cysteine) peptidase inhibitor, clade E, member 1	Mus musculus	108-113
26979432-11	2016	These results demonstrate that sialylation of VN glycans regulates stress fiber formation and cell spreading of dermal fibroblast cells via a heparin binding site.	Heparin	142-149	vitronectin	Mus musculus	46-48
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	24-31	serpin family C member 1	Homo sapiens	47-52
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	24-31	serpin family C member 1	Homo sapiens	107-112
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	24-31	serpin family C member 1	Homo sapiens	107-112
26836755-3	2016	Basic residues within a conformationally selective dimeric variant of XCL1 (W55D) were mutated and analyzed for their effects on heparin binding.	Heparin	129-136	X-C motif chemokine ligand 1	Homo sapiens	70-74
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	33-36	serpin family C member 1	Homo sapiens	47-52
26607136-2	2016	Both TFPI and FXa interact with several plasma proteins (e. g. prothrombin, FV/FVa, protein S) and non-proteinaceous compounds (e. g. phospholipids, heparin).	Heparin	149-156	coagulation factor X	Homo sapiens	14-17
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	33-36	serpin family C member 1	Homo sapiens	107-112
26607136-6	2016	Unfractionated heparin at concentrations (0.2-1 U/ml) enhanced FXa inhibition by TFPI ~8-fold, but impaired inhibition at concentrations &gt; 1 U/ml.	Heparin	15-22	coagulation factor X	Homo sapiens	63-66
19689280-3	2009	In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin.	Heparin	33-36	serpin family C member 1	Homo sapiens	107-112
19514602-11	2009	Prophylactic treatment with heparin should be recommended from the very beginning of the following pregnancy in women with antithrombin, protein C or protein S deficiency.	Heparin	28-35	serpin family C member 1	Homo sapiens	123-135
26821679-3	2016	Proteins that bind to heparin heparin-binding protein (HBPs) play important roles in health and disease and interact with each other via networks known as "heparin interactomes".	Heparin	22-29	azurocidin 1	Homo sapiens	30-53
19035835-1	2008	A specific pentasaccharide sequence of heparin binds with high affinity to native antithrombin and induces a conformational change in the inhibitor by a previously described two-step interaction mechanism.	Heparin	39-46	serpin family C member 1	Homo sapiens	82-94
26808444-3	2016	By using truncated vitronectin fragments we found that all analyzed microbial pathogens (n = 13) bound human vitronectin via the same C-terminal heparin-binding domain (amino acids 352-374).	Heparin	145-152	vitronectin	Homo sapiens	109-120
19035835-2	2008	In this work, the interactions of heparin with the antiangiogenic latent and cleaved antithrombin forms were studied.	Heparin	34-41	serpin family C member 1	Homo sapiens	85-97
19035835-3	2008	Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin.	Heparin	11-18	serpin family C member 1	Homo sapiens	28-40
19035835-3	2008	Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin.	Heparin	11-18	serpin family C member 1	Homo sapiens	108-120
19040574-4	2008	Treatment of clones with heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) neutralizing antibodies as well as an EGFR inhibitor allowed the dissection of mechanisms regulating cell proliferation and apoptosis.	Heparin	25-32	epidermal growth factor	Homo sapiens	66-69
26519056-8	2015	However, heparin anticoagulation increased TWEAK levels in patient"s plasma whereas citrate did not, favouring the latter as anticoagulant in CVVH for AKI.	Heparin	9-16	TNF superfamily member 12	Homo sapiens	43-48
26156753-1	2015	Kallistatin, an endogenous protein, consists of two structural elements: active site and heparin-binding domain.	Heparin	89-96	serpin family A member 4	Homo sapiens	0-11
26156753-9	2015	Kallistatin via its heparin-binding site blocked TGF-beta-induced miR-21, Snail1 expression, and ROS formation, as wild-type kallistatin, but not heparin-binding site mutant kallistatin, exerted the effect.	Heparin	20-27	serpin family A member 4	Homo sapiens	0-11
26156753-11	2015	This is the first study to demonstrate that kallistatin"s heparin-binding site is crucial for preventing TGF-beta-induced miR-21 and oxidative stress, while its active site is key for stimulating the expression of antioxidant genes via interaction with an endothelial surface tyrosine kinase.	Heparin	58-65	serpin family A member 4	Homo sapiens	44-55
26157071-6	2015	In contrast to ovalbumin and OVAY, OVAX interacts with heparin, a negatively charged glycosaminoglycan, via a positively charged domain exposed at the surface of the molecule.	Heparin	55-62	ovalbumin-related protein X (SERPINB14C)	Gallus gallus	35-39
19040574-4	2008	Treatment of clones with heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) neutralizing antibodies as well as an EGFR inhibitor allowed the dissection of mechanisms regulating cell proliferation and apoptosis.	Heparin	25-32	heparin binding EGF like growth factor	Homo sapiens	91-97
26524358-0	2015	[Heparin-treated dendritic cells promote Th0 to Th1 differentiation via the Toll-like receptor 3 in peripheral blood monocytes of patients with chronic hepatitis B].	Heparin	1-8	negative elongation factor complex member C/D	Homo sapiens	48-51
18674534-11	2008	As well, heparin counteracted the known inhibitory effect of fibronectin on adipogenesis and decreased basal focal adhesion kinase and paxillin phosphorylation.	Heparin	9-16	fibronectin 1	Mus musculus	61-72
26266343-6	2015	Meta-regression analyses demonstrated that additional administration of GP IIb/IIIa receptor inhibitors (P = 0.01), especially eptifibatide (P = 0.001) and tirofiban (P = 0.002), was likely to increase the major bleeding risk associated with bivalirudin.Bivalirudin, in comparison to heparin, is associated with a markedly lower risk of major bleeding, and the additional use of GP IIb/IIIa inhibitors may weaken this benefit.	Heparin	284-291	integrin subunit alpha 2b	Homo sapiens	72-78
18667434-4	2008	The ionomycin-induced Pyk2 phosphorylation was partially sensitive to AG1478, heparin, or the matrix-metalloproteinase inhibitor BB2116, and the ionomycin-induced EGF receptor phosphorylation was almost completely blocked by these inhibitors of extracellular transactivation.	Heparin	78-85	protein tyrosine kinase 2 beta	Homo sapiens	22-26
25775976-5	2015	The SRA also provides useful information on whether a HIT serum produces strong platelet activation even in the absence of heparin: such heparin-"independent" platelet activation is a marker of unusually severe HIT, including delayed-onset HIT and severe HIT complicated by consumptive coagulopathy with risk for microvascular thrombosis.	Heparin	137-144	steroid receptor RNA activator 1	Homo sapiens	4-7
18783251-8	2008	The aggregation of the Tau repeat domain (that forms the core of PHFs) in the presence of nucleating polyanionic cofactors (heparin) is efficient in a range of buffers and pH values between approximately 5 and 10 but breaks down beyond that range, presumably because the pattern of charged interactions disappears.	Heparin	124-131	microtubule associated protein tau	Homo sapiens	23-26
25886769-9	2015	Having an increased cTnI reported on the Architect assay that would not have been reported as such on the Dimension assay (0.03-0.06 mug/L) correlated with increased inpatient mortality, length of stay, non-ST elevation myocardial infarction diagnosis, therapeutic heparin use, and percutaneous coronary intervention, relative to individuals with cTnI &lt;0.03 mug/L.	Heparin	265-272	troponin I3, cardiac type	Homo sapiens	20-24
18558097-8	2008	This mechanism resembles the action of heparin with low affinity for antithrombin, as opposed to heparin with high affinity for serpin.	Heparin	39-46	serpin family C member 1	Homo sapiens	69-81
26102015-10	2015	There may be reinforcement in the sole utilization of heparin confining GP IIb/IIIa inhibitors and other intravenous antithrombotics to bailout therapy for periprocedural PCI complications in acute coronary syndrome patients."	Heparin	54-61	integrin subunit alpha 2b	Homo sapiens	72-78
18685429-2	2008	Heparin-induced thrombocytopenia caused by heparin-platelet factor 4 antibodies (HPF4-As), however, remains a serious concern.	Heparin	0-7	zinc finger protein 85	Homo sapiens	81-85
26056484-11	2015	Heparin and angiogenesis stimulators such as VEGFbeta negatively regulate its expression.	Heparin	0-7	vascular endothelial growth factor B	Homo sapiens	45-53
18685429-3	2008	While up to 50% of cardiovascular surgical patients develop HPF4-As while receiving heparin, the rate of seroconversion is lower in medical patients, suggesting an impact of the patient population on the underlying immune response.	Heparin	84-91	zinc finger protein 85	Homo sapiens	60-64
18657648-1	2008	BACKGROUND: Unfractionated heparin (UFH) is a mainstay of treatment for patients with non-ST-segment elevation acute coronary syndromes (NSTE ACS), but the practice of weight-adjusted bolus and infusion dosing has not been carefully evaluated.	Heparin	27-34	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	142-145
25969653-0	2015	Identification of core active disaccharides in heparin for HGF-inducing activity.	Heparin	47-54	hepatocyte growth factor	Mus musculus	59-62
18657648-1	2008	BACKGROUND: Unfractionated heparin (UFH) is a mainstay of treatment for patients with non-ST-segment elevation acute coronary syndromes (NSTE ACS), but the practice of weight-adjusted bolus and infusion dosing has not been carefully evaluated.	Heparin	36-39	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	142-145
18463113-0	2008	Characterization and secondary structure analysis of endostatin covalently modified by polyethylene glycol and low molecular weight heparin.	Heparin	132-139	collagen type XVIII alpha 1 chain	Homo sapiens	53-63
25791723-6	2015	Mutant constructs of RANTES restricted either in binding to heparin, or in forming dimers or tetramers, appeared either in a granular, non-filamentous pattern or were not detectable on the cell surface.	Heparin	60-67	C-C motif chemokine ligand 5	Homo sapiens	21-27
28717459-3	2015	In the presence of heparin, NK1 can self-associate into a "head to tail" dimer which is considered as the minimal structural module able to trigger MET dimerization and activation whereas isolated K1 and N domains showed a weak or a complete lack of agonistic activity respectively.	Heparin	19-26	hepatocyte growth factor	Mus musculus	28-31
18574264-2	2008	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors.	Heparin	0-3	serpin family C member 1	Homo sapiens	66-78
18308722-5	2008	In oocytes, ENaC currents were also inhibited by TBB and by the structurally unrelated inhibitors heparin and poly(E:Y).	Heparin	98-105	sodium channel, nonvoltage-gated 1 alpha	Mus musculus	12-16
25545620-4	2015	These techniques consisted of cross-linking heparin to graft surfaces to immobilize vascular endothelial growth factor (VEGF) or antibodies against CD34 (anti-CD34Ab).	Heparin	44-51	vascular endothelial growth factor A	Mus musculus	84-118
25545620-4	2015	These techniques consisted of cross-linking heparin to graft surfaces to immobilize vascular endothelial growth factor (VEGF) or antibodies against CD34 (anti-CD34Ab).	Heparin	44-51	vascular endothelial growth factor A	Mus musculus	120-124
25174443-0	2015	Heparin-coated cardiopulmonary bypass circuits selectively deplete the pattern recognition molecule ficolin-2 of the lectin complement pathway in vivo.	Heparin	0-7	ficolin 2	Homo sapiens	100-109
25174443-12	2015	Ficolin-2 was depleted from plasma during cardiac surgery when using heparin-coated bypass circuits and did not reach baseline level 24 h postoperation.	Heparin	69-76	ficolin 2	Homo sapiens	0-9
18288776-5	2008	The results showed that 2,3-O-sulfate groups are more important than N-sulfate groups in heparin-G-CSF interaction.	Heparin	89-96	colony stimulating factor 3	Homo sapiens	97-102
26309784-10	2015	The addition of supplemental growth factors VEGF, fibroblastic growth factor-2, EGF, hydrocortisone, insulin growth factor-1, ascorbic acid, and heparin to MSC cocultures promoted stable EOC network formation over 2 weeks in vitro, without affecting CD45 expression, as evidenced by a lack of significant differences in total segment length (p=0.96).	Heparin	145-152	protein tyrosine phosphatase receptor type C	Homo sapiens	250-254
18645924-10	2008	As heparins are strong inhibitors of heparanase, in view of the effect of heparanase on TF/TFPI pathway, the role of heparins" anticoagulant activity may potentially be expanded.	Heparin	3-11	coagulation factor III, tissue factor	Homo sapiens	88-90
25618841-2	2015	Tissue plasminogen activator (tPA) is a thrombolytic agent which dissolves the thrombus more rapidly than conventional heparin therapy and reduces the mortality and morbidity rates associated with PE.	Heparin	119-126	chromosome 20 open reading frame 181	Homo sapiens	0-28
17961072-7	2008	We found that ROS-induced heparin and heparan sulfate fragments induced neutrophil chemotaxis across a modified Boyden chamber, which was inhibited by the presence of EC-SOD by scavenging oxygen radicals.	Heparin	26-33	superoxide dismutase 3, extracellular	Mus musculus	167-173
26819958-0	2015	Heparin Interaction with the Primed Polymorphonuclear Leukocyte CD11b Induces Apoptosis and Prevents Cell Activation.	Heparin	0-7	integrin subunit alpha M	Homo sapiens	64-69
26819958-7	2015	Blocking antibodies to CD11b inhibited heparin binding and abolished the apoptotic response.	Heparin	39-46	integrin subunit alpha M	Homo sapiens	23-28
26819958-8	2015	Moreover, heparin caused a significant dose-dependent decrease in the rate of superoxide release from PMNLs, which was blunted by blocking antibodies to CD11b.	Heparin	10-17	integrin subunit alpha M	Homo sapiens	153-158
26819958-9	2015	Altogether, this study shows that the interaction of heparin with the PMNL CD11b results in cell apoptosis and explains heparin"s anti-inflammatory effects.	Heparin	53-60	integrin subunit alpha M	Homo sapiens	75-80
26819958-9	2015	Altogether, this study shows that the interaction of heparin with the PMNL CD11b results in cell apoptosis and explains heparin"s anti-inflammatory effects.	Heparin	120-127	integrin subunit alpha M	Homo sapiens	75-80
18006516-1	2008	We have studied the effect of heparin, a glycosaminoglycan widely used in releasing tags from fusion proteins, on isoform 8 of Arabidopsis thaliana PM Ca(2+)-ATPase (ACA8) expressed in Saccharomyces cerevisiae strain K616.	Heparin	30-37	autoinhibited Ca2+-ATPase 1	Arabidopsis thaliana	151-164
25521480-2	2014	Heparin, a soluble heparin sulfate (HS), can inhibit TCA HIV and FIV entry mediated by HSPG interaction in vitro.	Heparin	0-7	syndecan 2	Homo sapiens	87-91
28572686-8	2017	Heparin, which binds ligands including PDGF and SCF, and imatininib which blocks downstream tyrosine kinase receptors, both inhibited lung fibroblast migration individually but showed synergy in SSc cells.	Heparin	0-7	KIT ligand	Homo sapiens	48-51
18055456-6	2008	Previous studies demonstrated that heparin heightens the affinity of thrombin for fibrin by simultaneously binding to fibrin and exosite 2 on thrombin to generate a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin and heparin cofactor II.	Heparin	35-42	serpin family C member 1	Homo sapiens	247-259
28558026-4	2017	Using this system, we demonstrate that heparin, an analog of heparan sulfate, induced the dimerization of RPTPsigma, whereas chondroitin sulfate increased RPTPsigma activity by inhibiting RPTPsigma dimerization.	Heparin	39-46	protein tyrosine phosphatase receptor type S	Homo sapiens	106-115
25521480-6	2014	Peptides representing either the N- or C-terminal side of the V3 loop and containing HSPG binding sites were able to compete away the heparin block of TCA SU binding to CXCR4.	Heparin	134-141	syndecan 2	Homo sapiens	85-89
25521480-6	2014	Peptides representing either the N- or C-terminal side of the V3 loop and containing HSPG binding sites were able to compete away the heparin block of TCA SU binding to CXCR4.	Heparin	134-141	C-X-C motif chemokine receptor 4	Homo sapiens	169-174
25521480-8	2014	Our data show that heparin blocks TCA FIV infection or entry not only through its competition of HSPG on the cell surface interaction with SU, but also by its interference with CXCR4 binding to SU.	Heparin	19-26	syndecan 2	Homo sapiens	97-101
25521480-8	2014	Our data show that heparin blocks TCA FIV infection or entry not only through its competition of HSPG on the cell surface interaction with SU, but also by its interference with CXCR4 binding to SU.	Heparin	19-26	C-X-C motif chemokine receptor 4	Homo sapiens	177-182
17766169-3	2008	Attachment of endothelial cells in vitro to heparin-binding domain of fibronectin was inhibited by heparin.	Heparin	44-51	fibronectin 1	Gallus gallus	70-81
25241290-0	2014	Oversulfated heparins with low anticoagulant activity are strong and fast inhibitors of hepcidin expression in vitro and in vivo.	Heparin	13-21	hepcidin antimicrobial peptide	Mus musculus	88-96
18585473-3	2008	PHEX was eluted from a heparin-Sepharose chromatography column at 0.8 M NaCl showing a strong interaction with heparin.	Heparin	23-30	phosphate regulating endopeptidase homolog X-linked	Homo sapiens	0-4
25241290-2	2014	Heparins have been shown to be efficient hepcidin inhibitors both in vitro and in vivo, even when their anticoagulant activity has been abolished by chemical reactions of oxidation/reduction (glycol-split).	Heparin	0-8	hepcidin antimicrobial peptide	Mus musculus	41-49
25241290-9	2014	This modified heparin has potential applications for the treatment of diseases with high hepcidin levels.	Heparin	14-21	hepcidin antimicrobial peptide	Mus musculus	89-97
25385546-5	2014	Accordingly, heparan sulphate and heparin oligomers compete with TrkC for RPTPsigma binding in vitro and disrupt TrkC-dependent synaptic differentiation in neuronal co-culture assays.	Heparin	34-41	neurotrophic receptor tyrosine kinase 3	Homo sapiens	65-69
25385546-5	2014	Accordingly, heparan sulphate and heparin oligomers compete with TrkC for RPTPsigma binding in vitro and disrupt TrkC-dependent synaptic differentiation in neuronal co-culture assays.	Heparin	34-41	protein tyrosine phosphatase receptor type S	Homo sapiens	74-83
18585473-3	2008	PHEX was eluted from a heparin-Sepharose chromatography column at 0.8 M NaCl showing a strong interaction with heparin.	Heparin	111-118	phosphate regulating endopeptidase homolog X-linked	Homo sapiens	0-4
25385546-5	2014	Accordingly, heparan sulphate and heparin oligomers compete with TrkC for RPTPsigma binding in vitro and disrupt TrkC-dependent synaptic differentiation in neuronal co-culture assays.	Heparin	34-41	neurotrophic receptor tyrosine kinase 3	Homo sapiens	113-117
18585473-5	2008	Heparin, heparan sulfate and chondroitin sulfate inhibited PHEX catalytic activity, however among them, heparin presented the highest inhibitory activity (Ki=2.5+/-0.2 nM).	Heparin	0-7	phosphate regulating endopeptidase homolog X-linked	Homo sapiens	59-63
25289044-0	2014	Azurocidin-induced inhibition of oxygen metabolism in mitochondria is antagonized by heparin.	Heparin	85-92	azurocidin 1	Homo sapiens	0-10
25289044-3	2014	Azurocidin (AZU), a protein with strong heparin-binding potential that induces inflammatory responses and apoptosis, has been shown to increase the permeability of endothelial cells and induce the prognosis of sepsis.	Heparin	40-47	azurocidin 1	Homo sapiens	0-10
25289044-3	2014	Azurocidin (AZU), a protein with strong heparin-binding potential that induces inflammatory responses and apoptosis, has been shown to increase the permeability of endothelial cells and induce the prognosis of sepsis.	Heparin	40-47	azurocidin 1	Homo sapiens	12-15
25289044-5	2014	The aim of the present study was to investigate whether heparin exhibits an antagonistic effect on AZU-induced mitochondrial dysfunction in human umbilical vein endothelial cells (HUVECs) and to further investigate the possible underlying mechanisms.	Heparin	56-63	azurocidin 1	Homo sapiens	99-102
25289044-11	2014	Heparin exhibited an antagonistic function on these processes and inhibited the endocytosis of AZU by HUVECs.	Heparin	0-7	azurocidin 1	Homo sapiens	95-98
25289044-12	2014	In conclusion, the results indicated that AZU inhibited the oxygen metabolic function in mitochondria, and this function was effectively antagonized by heparin via the inhibition of AZU endocytosis by HUVECs.	Heparin	152-159	azurocidin 1	Homo sapiens	42-45
25289044-12	2014	In conclusion, the results indicated that AZU inhibited the oxygen metabolic function in mitochondria, and this function was effectively antagonized by heparin via the inhibition of AZU endocytosis by HUVECs.	Heparin	152-159	azurocidin 1	Homo sapiens	182-185
18585473-5	2008	Heparin, heparan sulfate and chondroitin sulfate inhibited PHEX catalytic activity, however among them, heparin presented the highest inhibitory activity (Ki=2.5+/-0.2 nM).	Heparin	104-111	phosphate regulating endopeptidase homolog X-linked	Homo sapiens	59-63
17899320-5	2008	We analyse the interaction of IGFBP-5 (and IGFBP-3) with heparin and other biomolecules and describe experiments, which were designed to monitor multi-protein complex formation in this molecular axis.	Heparin	57-64	insulin like growth factor binding protein 3	Homo sapiens	43-50
25526009-1	2014	Enoxaparin sodium is a heparin of low molecular weight with antithrombotic properties that acts by inhibiting factor Xa.	Heparin	23-30	coagulation factor X	Homo sapiens	110-119
24879919-2	2014	FKBP25 isolated from natural sources, its recombinant murine homologue (mFKBP25) and their complexes with rapamycin bind to diverse DNAs, RNAs and heparin affinity beads.	Heparin	147-154	FK506 binding protein 3	Mus musculus	0-6
17878401-1	2007	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin.	Heparin	104-111	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	0-19
24879919-2	2014	FKBP25 isolated from natural sources, its recombinant murine homologue (mFKBP25) and their complexes with rapamycin bind to diverse DNAs, RNAs and heparin affinity beads.	Heparin	147-154	FK506 binding protein 3	Mus musculus	72-79
17878401-1	2007	Heparin cofactor II (HCII) is a plasma protein that inhibits thrombin when bound to dermatan sulfate or heparin.	Heparin	104-111	serine (or cysteine) peptidase inhibitor, clade D, member 1	Mus musculus	21-25
18085394-10	2007	There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis.	Heparin	74-81	serpin family C member 1	Homo sapiens	33-49
24573541-3	2014	To address this, we compared the capacity of dabigatran and/or heparin to inhibit catheter-induced thrombin generation in vitro and to attenuate catheter occlusion in rabbits.	Heparin	63-70	prothrombin	Oryctolagus cuniculus	99-107
18085394-10	2007	There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis.	Heparin	74-81	serpin family C member 1	Homo sapiens	51-56
24924394-3	2014	We describe modifications to a previously reported heparin-based affinity chromatography procedure that improve yield and achieve efficient removal of endotoxin from washed and urea-solubilized human VTN inclusion bodies following standard autoinduction of expression in Escherichia coli.	Heparin	51-58	vitronectin	Homo sapiens	200-203
18085394-10	2007	There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis.	Heparin	133-140	serpin family C member 1	Homo sapiens	33-49
18085394-10	2007	There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis.	Heparin	133-140	serpin family C member 1	Homo sapiens	51-56
18220975-7	2007	Chemical modification of the natural or synthetic heparin increased factor activation of AT III Xa affinity.	Heparin	50-57	serpin family C member 1	Homo sapiens	89-95
24718936-8	2014	Inhibition of candidate signaling pathways that may link GPER activation to proliferation revealed a dependence on Src, epidermal growth factor receptor transactivation by heparin-bound EGF and subsequent ERK phosphorylation.	Heparin	172-179	G protein-coupled estrogen receptor 1	Homo sapiens	57-61
17875649-8	2007	Together these results show that exosites generated by heparin activation of antithrombin function both to promote the formation of an initial antithrombin-protease Michaelis complex and to favor the subsequent acylation of this complex.	Heparin	55-62	serpin family C member 1	Homo sapiens	77-89
17875649-8	2007	Together these results show that exosites generated by heparin activation of antithrombin function both to promote the formation of an initial antithrombin-protease Michaelis complex and to favor the subsequent acylation of this complex.	Heparin	55-62	serpin family C member 1	Homo sapiens	143-155
24561026-6	2014	Here we present the isolation and identification of an octadecasaccharide with very high anti-factor Xa activity (~3 times higher than USP [U.S. Pharmacopeia] heparin).	Heparin	159-166	coagulation factor X	Homo sapiens	94-103
18307901-5	2007	RESULTS: In the culture systems with heparin and normal serum, normal serum, heparin and serum with positive autoantibody, serum with positive autoantibody, the mean fluorescence gray scale values of PCNA were 34.8 +/- 3.1, 33.8 +/- 1.8, 33.4 +/- 2.2 and 25.1 +/- 2.3, the 490 nm A values were 0.0560 +/- 0.0033, 0.0535 +/- 0.0024, 0.0524 +/- 0.0027 and 0.0350 +/- 0.0040, respectively.	Heparin	37-44	proliferating cell nuclear antigen	Homo sapiens	200-204
25126416-2	2014	We have used a multilayer technology to graft a range of 5 mug/mL - 5 mg/mL heparin onto the surface of MSC aggregates.	Heparin	76-83	kinocilin	Mus musculus	63-69
18307901-5	2007	RESULTS: In the culture systems with heparin and normal serum, normal serum, heparin and serum with positive autoantibody, serum with positive autoantibody, the mean fluorescence gray scale values of PCNA were 34.8 +/- 3.1, 33.8 +/- 1.8, 33.4 +/- 2.2 and 25.1 +/- 2.3, the 490 nm A values were 0.0560 +/- 0.0033, 0.0535 +/- 0.0024, 0.0524 +/- 0.0027 and 0.0350 +/- 0.0040, respectively.	Heparin	77-84	proliferating cell nuclear antigen	Homo sapiens	200-204
23104956-11	2014	CONCLUSIONS: Impact of heparin on endothelial cells and simultaneously on OPG/RANK/RANKL axis reinforces the presumption of the pathophysiological linkage between bone mineralization and endothelial dysfunction in end-stage renal disease.	Heparin	23-30	TNF superfamily member 11	Homo sapiens	83-88
24616065-1	2014	The anticoagulant properties of heparin stem in part from high-affinity binding to antithrombin-III (AT-III) inducing a 300-fold increase in its inhibitory activity against the coagulation protease factor Xa.	Heparin	32-39	coagulation factor X	Homo sapiens	198-207
17912162-8	2007	The antithrombin agents, unfractionated heparin, low molecular weight (LMW) heparin, Xa inhibitors, and direct thrombin antagonists, act specifically to target thrombin generation, thrombin activity, or both.	Heparin	76-83	serpin family C member 1	Homo sapiens	4-16
24627466-2	2014	The objective of this study was to explore the use of an engineered follistatin therapeutic created by fusing FST315 lacking heparin binding activity to the N terminus of a murine IgG1 Fc (FST315-DeltaHBS-Fc) as a systemic therapeutic agent in models of muscle injury.	Heparin	125-132	follistatin	Mus musculus	68-79
17492649-6	2007	We further studied the heparin cofactor activity and the binding to heparin of each recombinant AT molecule.	Heparin	23-30	serpin family C member 1	Homo sapiens	96-98
24758297-7	2014	DNA binding ability of recombinant GATA3 was evaluated using electrophoretic mobility shift assay and heparin chromatography.	Heparin	102-109	GATA binding protein 3	Homo sapiens	35-40
17492649-8	2007	In contrast, we found that Ala59Val mutant AT unexpectedly showed a normal affinity to heparin, but severely impaired the heparin cofactor activity.	Heparin	87-94	serpin family C member 1	Homo sapiens	43-45
17560185-10	2007	A (125)I-OPG binding assay showed that OPG binds to osteoblasts and that this binding is inhibited by the addition of heparin, suggesting that OPG binds to RANKL on the osteoblast membrane and that heparin blocks this interaction.	Heparin	118-125	tumor necrosis factor (ligand) superfamily, member 11	Mus musculus	156-161
24744754-10	2014	In common with other CFH interactions with its physiological and pathophysiological ligands, the CFH-heparin and CFH-C3b interactions have moderate micromolar dissociation constants K D, meaning that these complexes do not fully form in vivo.	Heparin	101-108	complement factor H	Homo sapiens	21-24
24744754-10	2014	In common with other CFH interactions with its physiological and pathophysiological ligands, the CFH-heparin and CFH-C3b interactions have moderate micromolar dissociation constants K D, meaning that these complexes do not fully form in vivo.	Heparin	101-108	complement factor H	Homo sapiens	97-100
24744754-10	2014	In common with other CFH interactions with its physiological and pathophysiological ligands, the CFH-heparin and CFH-C3b interactions have moderate micromolar dissociation constants K D, meaning that these complexes do not fully form in vivo.	Heparin	101-108	complement factor H	Homo sapiens	97-100
24744754-11	2014	The combination of the solution structures and binding studies indicated a two-site interaction model of CFH with heparin at cell surfaces.	Heparin	114-121	complement factor H	Homo sapiens	105-108
24744754-13	2014	Defective interactions at either of the two independent CFH-heparin sites reduce the CFH interaction with surface-bound C3b and lead to immune disorders.	Heparin	60-67	complement factor H	Homo sapiens	56-59
24744754-13	2014	Defective interactions at either of the two independent CFH-heparin sites reduce the CFH interaction with surface-bound C3b and lead to immune disorders.	Heparin	60-67	complement factor H	Homo sapiens	85-88
24744754-13	2014	Defective interactions at either of the two independent CFH-heparin sites reduce the CFH interaction with surface-bound C3b and lead to immune disorders.	Heparin	60-67	complement C3	Homo sapiens	120-123
17544586-7	2007	The expression of HB-EGF as well as of transforming growth factor-alpha (TGF-alpha), two of the EGFR ligands, in the cells was confirmed by reverse transcription polymerase chain reaction, and the only partial inhibition by heparin suggests that both of these EGFR agonists are involved.	Heparin	224-231	heparin-binding EGF-like growth factor	Mus musculus	18-24
24641672-0	2014	Heparin binding VEGF isoforms attenuate hyperoxic embryonic lung growth retardation via a FLK1-neuropilin-1-PKC dependent pathway.	Heparin	0-7	kinase insert domain receptor	Homo sapiens	90-94
17560876-8	2007	In contrast, among patients randomized to receive unfractionated heparin and planned glycoprotein IIb/IIIa, pretreatment with antithrombin therapy was associated with increased protocol-defined composite major or minor bleeding and increased need for transfusion.	Heparin	65-72	serpin family C member 1	Homo sapiens	126-138
24398330-9	2014	A single dose of heparin reduced the already low level of hepcidin of these mice and prevented its induction by LPS.	Heparin	17-24	hepcidin antimicrobial peptide	Mus musculus	58-66
24388571-9	2014	Anti-FXa activity reduced on the start of CPB compared to the level after heparinization, to almost the baseline value following protamine reversal of heparin.	Heparin	74-81	coagulation factor X	Homo sapiens	5-8
17385667-1	2007	We evaluated the role of nonspecific electrostatic binding in the interaction of antithrombin (AT) with heparin (Hp), a paradigmatic protein-glycosaminoglycan (GAG) system.	Heparin	104-111	serpin family C member 1	Homo sapiens	81-93
24148803-7	2014	In parallel experiments heparin was shown to have minor inhibitory effects on fibulin-5 interactions with tropoelastin and LTBP-2.	Heparin	24-31	elastin	Homo sapiens	106-118
24148803-8	2014	However, LTBP-2 was shown to significantly inhibit the binding of heparin to tropoelastin with 50% inhibition achieved with 10 fold molar excess of LTBP-2.	Heparin	66-73	elastin	Homo sapiens	77-89
24678194-0	2014	Elucidating the specificity of non-heparin-based conformational activators of antithrombin for factor Xa inhibition.	Heparin	35-42	coagulation factor X	Homo sapiens	95-104
17473571-8	2007	There was a statistically significant rise in the concentrations of von Willebrand factor (P &lt; 0.0001) and soluble thrombomodulin (P = 0.004) when patients with heparin-induced thrombocytopenia type II were compared with healthy laboratory controls and patients having had cardiopulmonary bypass surgery (von Willebrand factor 324 versus 103 versus 108 U/dl and soluble thrombomodulin 9.5 versus 2.3 versus 1.2 ng/ml, respectively).	Heparin	164-171	thrombomodulin	Homo sapiens	118-132
24577046-8	2014	Furthermore, the BDNF levels detected in plasma stored in heparin tubes at 4 C and those for samples stored in EDTA tubes at 25 C were much higher than those of the other samples.	Heparin	58-65	brain derived neurotrophic factor	Homo sapiens	17-21
17473571-8	2007	There was a statistically significant rise in the concentrations of von Willebrand factor (P &lt; 0.0001) and soluble thrombomodulin (P = 0.004) when patients with heparin-induced thrombocytopenia type II were compared with healthy laboratory controls and patients having had cardiopulmonary bypass surgery (von Willebrand factor 324 versus 103 versus 108 U/dl and soluble thrombomodulin 9.5 versus 2.3 versus 1.2 ng/ml, respectively).	Heparin	164-171	thrombomodulin	Homo sapiens	373-387
17498058-5	2007	MC-like cells that contain tryptase-heparin complexes in their secretory granules have been identified in the Ciona intestinalis and Styela plicata urochordates that appeared approximately 500 million years ago.	Heparin	36-43	tryptase alpha/beta 1	Mus musculus	27-35
22511397-2	2013	To accelerate angiogenesis, we delivered vascular endothelial growth factor (VEGF) using PCL scaffolds with surface crosslinked heparin.	Heparin	128-135	vascular endothelial growth factor A	Mus musculus	41-75
22511397-2	2013	To accelerate angiogenesis, we delivered vascular endothelial growth factor (VEGF) using PCL scaffolds with surface crosslinked heparin.	Heparin	128-135	vascular endothelial growth factor A	Mus musculus	77-81
22511397-6	2013	At day 7, the heparin-modified PCL scaffolds with VEGF exhibited significantly increased angiogenesis and engraftment of enteric cells, with a simultaneous reduction in hypoxia.	Heparin	14-21	vascular endothelial growth factor A	Mus musculus	50-54
24124146-9	2013	CONCLUSIONS: Anti-FXa antithrombin assay is recommended as a first-line test to detect type II heparin-binding site antithrombin deficiency.	Heparin	95-102	coagulation factor X	Homo sapiens	18-21
24095600-2	2013	The anticoagulation process is mainly caused by the interaction of heparin with antithrombin followed by inhibition of anticoagulant factor IIa and factor Xa.	Heparin	67-74	coagulation factor X	Homo sapiens	148-157
23627997-7	2013	MEASUREMENTS AND MAIN RESULTS: Plasma heparin expressed as anti-FXa activity was detected in 180 (88%) samples.	Heparin	38-45	coagulation factor X	Homo sapiens	64-67
27809364-11	2017	Multivariable analysis showed that the risks for PPB were as follows: heparin bridging therapy (OR 6.34, P = 0.0002); low-dose aspirin (LDA) continuation (OR 5.30, P = 0.0079); and lesion size (OR 1.06, P &lt; 0.0001).	Heparin	70-77	histatin 1	Homo sapiens	49-52
28169396-10	2017	Finally, we demonstrate that the conformational change in FGF9 resulting from the S99N mutation disrupts FGF9/FGFR/heparin interaction, which impedes FGF signaling in developmental joints.	Heparin	115-122	fibroblast growth factor 9	Homo sapiens	58-62
28169396-10	2017	Finally, we demonstrate that the conformational change in FGF9 resulting from the S99N mutation disrupts FGF9/FGFR/heparin interaction, which impedes FGF signaling in developmental joints.	Heparin	115-122	fibroblast growth factor 9	Homo sapiens	105-109
28169396-10	2017	Finally, we demonstrate that the conformational change in FGF9 resulting from the S99N mutation disrupts FGF9/FGFR/heparin interaction, which impedes FGF signaling in developmental joints.	Heparin	115-122	fibroblast growth factor 9	Homo sapiens	58-61
28153312-8	2017	Additionally, the inhibition of T4 PNKP activity by the inhibitor heparin is demonstrated.	Heparin	66-73	polynucleotide kinase 3'-phosphatase	Homo sapiens	35-39
17458940-0	2007	Kinetic analysis of heparin and glucan sulfates binding to P-selectin and its impact on the general understanding of selectin inhibition.	Heparin	20-27	selectin P	Homo sapiens	59-69
27527263-5	2017	RESULTS: Stimulation with anti-IgE or IL-3 resulted in strong upregulation of basophil CD203c in samples collected in EDTA or heparin, stored at 4 C, and analyzed 24 hours after sample collection.	Heparin	126-133	ectonucleotide pyrophosphatase/phosphodiesterase 3	Homo sapiens	87-93
28191759-3	2017	The treatment with heparin helped cardiomyocyte differentiation consistently reach at least 80% purity (up to 95%) from more than 10 different hPSC lines in chemically defined Dulbecco"s modified Eagle"s medium/F-12-based medium on either Matrigel or defined matrices like vitronectin and Synthemax.	Heparin	19-26	vitronectin	Homo sapiens	273-284
23726297-8	2013	A synergic action of OPN with heparin was also done for all OPN concentrations tested.	Heparin	30-37	osteopontin	Bubalus bubalis	60-63
23597922-0	2013	STAT1 requirement for PKR-induced cell cycle arrest in vascular smooth muscle cells in response to heparin.	Heparin	99-106	signal transducer and activator of transcription 1	Homo sapiens	0-5
23597922-9	2013	In order to understand the mechanism of heparin-induced stabilization of p27(kip1) in VSMC, we examined the involvement of the Signal Transducer and Activator of Transcription-1 (STAT1), which is an important player in mediating antiproliferative effects of IFNs.	Heparin	40-47	signal transducer and activator of transcription 1	Homo sapiens	179-184
23597922-11	2013	PKR activation induced by antiproliferative agent heparin leads to phosphorylation of STAT1 on serine 727, which is essential for the cell cycle block.	Heparin	50-57	signal transducer and activator of transcription 1	Homo sapiens	86-91
23597922-12	2013	STAT1 null VSMCs are largely defective in heparin-induced cell cycle arrest and in PKR null cells the STAT1 phosphorylation in response to heparin was absent.	Heparin	42-49	signal transducer and activator of transcription 1	Homo sapiens	0-5
23597922-12	2013	STAT1 null VSMCs are largely defective in heparin-induced cell cycle arrest and in PKR null cells the STAT1 phosphorylation in response to heparin was absent.	Heparin	139-146	signal transducer and activator of transcription 1	Homo sapiens	0-5
23597922-12	2013	STAT1 null VSMCs are largely defective in heparin-induced cell cycle arrest and in PKR null cells the STAT1 phosphorylation in response to heparin was absent.	Heparin	139-146	signal transducer and activator of transcription 1	Homo sapiens	102-107
23597922-13	2013	These results establish that heparin causes STAT1 phosphorylation on serine 727 via activation of PKR and that this event is required for the G1 arrest in VSMC.	Heparin	29-36	signal transducer and activator of transcription 1	Homo sapiens	44-49
17458940-3	2007	The anti-inflammatory and anti-metastatic activities of heparin have partly been related to the inhibition of P-selectin binding.	Heparin	56-63	selectin P	Homo sapiens	110-120
17458940-4	2007	Here we apply a quartz crystal microbalance (QCM) biosensor to determine the kinetic constants of heparin and other sulfated polysaccharides binding to immobilized P-selectin.	Heparin	98-105	selectin P	Homo sapiens	164-174
27865770-4	2017	For both these SAA peptides, binding to lysophospholipids inhibited heparin-induced amyloid-like fibril formation by stabilizing the alpha-helical structure.	Heparin	68-75	serum amyloid A1 cluster	Homo sapiens	15-18
17458940-13	2007	Structurally, highly charged compounds with a slow off-rate, such as heparin or glucan sulfates, appear as potent candidates for P-selectin inhibition.	Heparin	69-76	selectin P	Homo sapiens	129-139
17374638-0	2007	Cell adhesion to fibrillin-1: identification of an Arg-Gly-Asp-dependent synergy region and a heparin-binding site that regulates focal adhesion formation.	Heparin	94-101	fibrillin 1	Homo sapiens	17-28
27368065-2	2017	The aim of the present study was to evaluate the risk of post-polypectomy bleeding (PPB) in patients receiving heparin-bridging therapy.	Heparin	111-118	histatin 1	Homo sapiens	84-87
27368065-6	2017	The incidence of PPB per patient was significantly higher in the HB group (22.2% vs 1.9%, P &lt; 0.0001), and multivariate analysis showed that heparin-bridging therapy was an independent risk factor for PPB (OR 9.80, 95% CI 4.23-22.3, P &lt; 0.0001).	Heparin	144-151	histatin 1	Homo sapiens	17-20
27368065-6	2017	The incidence of PPB per patient was significantly higher in the HB group (22.2% vs 1.9%, P &lt; 0.0001), and multivariate analysis showed that heparin-bridging therapy was an independent risk factor for PPB (OR 9.80, 95% CI 4.23-22.3, P &lt; 0.0001).	Heparin	144-151	histatin 1	Homo sapiens	204-207
27368065-10	2017	CONCLUSIONS: Heparin-bridging therapy is associated with a high risk of PPB regardless of polyp size.	Heparin	13-20	histatin 1	Homo sapiens	72-75
23399388-6	2013	In this study, we examined the inhibitory action of C1-inhibitor (C1-inh), antithrombin (AT) and alpha(2)-macroglobulin (alpha(2)M) on MASP-1 and MASP-2, and studied the inhibition of the lectin pathway in normal human serum in the presence and absence of heparin using C3 and C4 deposition assays.	Heparin	256-263	serpin family G member 1	Homo sapiens	52-58
23399388-8	2013	We found that in the presence of heparin both C1-inh and AT are equally efficient inhibitors of the lectin pathway.	Heparin	33-40	serpin family G member 1	Homo sapiens	46-52
23576524-9	2013	Although the HRG retained binding to heparin and phosphatidic acid, it did not interact with necrotic cells or other cellular lipids.	Heparin	37-44	histidine rich glycoprotein	Homo sapiens	13-16
23494009-0	2013	Covalently linking heparin to antithrombin enhances prothrombinase inhibition on activated platelets.	Heparin	19-26	coagulation factor X	Homo sapiens	52-66
23494009-1	2013	Factor (F)Xa within the prothrombinase complex is protected from inhibition by unfractionated heparin (UFH), enoxaparin and fondaparinux.	Heparin	94-101	coagulation factor X	Homo sapiens	24-38
23494009-1	2013	Factor (F)Xa within the prothrombinase complex is protected from inhibition by unfractionated heparin (UFH), enoxaparin and fondaparinux.	Heparin	103-106	coagulation factor X	Homo sapiens	24-38
28580572-0	2017	The impact of low molecular weight heparin on obstetric outcomes among unexplained recurrent miscarriages complicated with methylenetetrahydrofolate reductase gene polymorphism.	Heparin	35-42	methylenetetrahydrofolate reductase	Homo sapiens	123-158
28580572-3	2017	The aim of this study is to analyze the impact of low molecular weight heparin on obstetric outcomes of recurrent miscarriage patients complicated with methylenetetrahydrofolate reductase gene polymorphism.	Heparin	71-78	methylenetetrahydrofolate reductase	Homo sapiens	152-187
28580572-10	2017	CONCLUSIONS: The current study demonstrated that low molecular weight heparin improved the live birth rates among unex-plained recurrent miscarriage patients complicated with methylenetetrahydrofolate reductase gene polymorphisms.	Heparin	70-77	methylenetetrahydrofolate reductase	Homo sapiens	175-210
22358112-6	2013	After intravesical heparin or HA treatment, incidence of grades 3-4 bladder inflammation and tissue ICAM-1 level were only significantly lower in HA group (P = 0.017, P = 0.021, respectively), but not in heparin group (P = 0.12, P = 0.798, respectively).	Heparin	19-26	intercellular adhesion molecule 1	Rattus norvegicus	100-106
17374638-3	2007	An adjacent heparin-binding site, which supports focal adhesion formation, was mapped to the fibrillin-1 TB5 motif.	Heparin	12-19	fibrillin 1	Homo sapiens	93-104
17348690-6	2007	In comparison with heparin, Ihog and Shh exhibited a lower affinity for HS than for heparin, and CDO and Hh exhibit negligible binding to HS.	Heparin	84-91	sonic hedgehog signaling molecule	Homo sapiens	37-40
17348690-7	2007	This study clearly demonstrates Shh and Ihog are heparin and HS binding proteins and that both molecules preferentially bind heparin or HS having a high level of sulfation.	Heparin	49-56	sonic hedgehog signaling molecule	Homo sapiens	32-35
23603906-0	2013	The choline-binding protein PspC of Streptococcus pneumoniae interacts with the C-terminal heparin-binding domain of vitronectin.	Heparin	91-98	vitronectin	Homo sapiens	117-128
17397238-10	2007	Among these ligands, heparin exhibits the greatest stabilizing effect on FGF20, increasing the Tm by more than 10 degrees C.	Heparin	21-28	fibroblast growth factor 20	Homo sapiens	73-78
23603906-3	2013	In this study, we identified PspC as a vitronectin-binding protein interacting with the C-terminal heparin-binding domain of vitronectin.	Heparin	99-106	vitronectin	Homo sapiens	39-50
23603906-3	2013	In this study, we identified PspC as a vitronectin-binding protein interacting with the C-terminal heparin-binding domain of vitronectin.	Heparin	99-106	vitronectin	Homo sapiens	125-136
17253189-5	2007	The binding of Sg-II to PSA and PCI is influenced by pH, ionic strength, heparin, negatively charged dextran sulfate, divalent cations, and particularly by Zn 2 +.	Heparin	73-80	semenogelin 2	Homo sapiens	15-20
23273911-3	2013	We focused on the extracellular matrix and developed a heparin-conjugated gelatin (Hep-gela).	Heparin	55-62	DNL-type zinc finger	Homo sapiens	83-86
17253189-5	2007	The binding of Sg-II to PSA and PCI is influenced by pH, ionic strength, heparin, negatively charged dextran sulfate, divalent cations, and particularly by Zn 2 +.	Heparin	73-80	kallikrein related peptidase 3	Homo sapiens	24-27
23460609-9	2013	Lastly, MZ, but not follicular, B cells adoptively transferred into B-cell-deficient muMT mice responded to PF4/heparin complex challenge by producing PF4/heparin-specific antibodies of IgG2b and IgG3 isotypes.	Heparin	155-162	immunoglobulin heavy constant gamma 2B	Mus musculus	186-191
17167048-0	2007	Analysis of inhibition rate enhancement by covalent linkage of antithrombin to heparin as a potential predictor of reaction mechanism.	Heparin	79-86	serpin family C member 1	Homo sapiens	63-75
23307015-8	2013	RESULTS: BMP6 specifically bound to heparin and induced Smad1/5/8 phosphorylation which was inhibited by heparin.	Heparin	105-112	SMAD family member 1	Rattus norvegicus	56-63
23269380-1	2013	PURPOSE: The study sought to synthesize anionic peptide-conjugated tissue plasminogen activator (tPA) for its targeted/triggered delivery, where tPA"s activity would be masked in the circulation and regenerated at the thrombus site by a commonly used anticoagulant, heparin, to minimize tPA associated bleeding complications.	Heparin	266-273	chromosome 20 open reading frame 181	Homo sapiens	67-95
17167048-1	2007	Antithrombin (AT) inhibition of coagulation enzymes is catalyzed by unfractionated heparin (UFH) and other heparinoids.	Heparin	83-90	serpin family C member 1	Homo sapiens	0-12
23269380-1	2013	PURPOSE: The study sought to synthesize anionic peptide-conjugated tissue plasminogen activator (tPA) for its targeted/triggered delivery, where tPA"s activity would be masked in the circulation and regenerated at the thrombus site by a commonly used anticoagulant, heparin, to minimize tPA associated bleeding complications.	Heparin	266-273	chromosome 20 open reading frame 181	Homo sapiens	97-100
17167048-1	2007	Antithrombin (AT) inhibition of coagulation enzymes is catalyzed by unfractionated heparin (UFH) and other heparinoids.	Heparin	92-95	serpin family C member 1	Homo sapiens	0-12
23269380-1	2013	PURPOSE: The study sought to synthesize anionic peptide-conjugated tissue plasminogen activator (tPA) for its targeted/triggered delivery, where tPA"s activity would be masked in the circulation and regenerated at the thrombus site by a commonly used anticoagulant, heparin, to minimize tPA associated bleeding complications.	Heparin	266-273	chromosome 20 open reading frame 181	Homo sapiens	145-148
23269380-1	2013	PURPOSE: The study sought to synthesize anionic peptide-conjugated tissue plasminogen activator (tPA) for its targeted/triggered delivery, where tPA"s activity would be masked in the circulation and regenerated at the thrombus site by a commonly used anticoagulant, heparin, to minimize tPA associated bleeding complications.	Heparin	266-273	chromosome 20 open reading frame 181	Homo sapiens	145-148
17167048-6	2007	In comparison, UFH or ATH heparin binding (evidence of a template mechanism) was only observed with thrombin, tissue factor, FIXa and FXIa.	Heparin	15-18	coagulation factor III, tissue factor	Homo sapiens	110-123
23269380-4	2013	The masking of tPA-activity via steric hindrance created by albumin, and subsequent regeneration with therapeutic dose of heparin was tested by enzymatic assay.	Heparin	122-129	chromosome 20 open reading frame 181	Homo sapiens	15-18
23269380-10	2013	Complexation with HSA-protamine masked ~60% of tPA activity which was fully regenerated by heparin.	Heparin	91-98	chromosome 20 open reading frame 181	Homo sapiens	47-50
17167048-6	2007	In comparison, UFH or ATH heparin binding (evidence of a template mechanism) was only observed with thrombin, tissue factor, FIXa and FXIa.	Heparin	26-33	coagulation factor III, tissue factor	Homo sapiens	110-123
23269380-12	2013	In lysing human clot, the camouflage could mask tPA-activity until it was triggered at a heparin level of 0.4U/mL.	Heparin	89-96	chromosome 20 open reading frame 181	Homo sapiens	48-51
23269380-13	2013	CONCLUSION: Oligoanion-modified tPA could be used for targeted/triggered delivery where its enzymatic activity could be masked by HSA-protamine conjugate and successfully regenerated by therapeutic dose of heparin.	Heparin	206-213	chromosome 20 open reading frame 181	Homo sapiens	32-35
23318174-3	2013	Unexpectedly, we observed that Sox2 is strongly adsorbed by heparin and by the fibroblasts without the R9 PTD.	Heparin	60-67	SRY-box transcription factor 2	Homo sapiens	31-35
17109891-8	2007	RESULTS: The expression of E-cadherin was significantly reduced to 46.7% (complete loss of staining) in the taurolidine/heparin group.	Heparin	120-127	cadherin 1	Rattus norvegicus	27-37
23166320-6	2013	The N-terminal heparin-binding motif of p17 partially overlaps the CXCR1-binding domain.	Heparin	15-22	C-X-C motif chemokine receptor 1	Homo sapiens	67-72
23959669-0	2013	Over-dialysis plasma RANTES increase depends on heparin dose and cardiovascular disease status.	Heparin	48-55	C-C motif chemokine ligand 5	Homo sapiens	21-27
23959669-7	2013	About 25% RANTES increase after 10 min of HD positively correlated with the dose of both heparins and HD duration.	Heparin	89-97	C-C motif chemokine ligand 5	Homo sapiens	10-16
23160925-4	2013	We therefore wanted to test whether heparins have an impact on the chemokines CXCL9 and CXCL10 as well as the IFN-gamma signalling in human breast cancer cells in vitro.	Heparin	36-44	C-X-C motif chemokine ligand 10	Homo sapiens	88-94
17156576-2	2006	This review focuses on five diseases caused by serpin dysfunction: variants of antithrombin III lose their ability to interact with heparin; the alpha1-antitrypsin Pittsburgh mutation causes a change in target proteinase; the alpha1-antitrypsin Z mutation and neuroserpin, polymerisation of which lead to cellular cytotoxicity; and a loss of maspin expression resulting in cancer.	Heparin	132-139	serpin family C member 1	Homo sapiens	79-95
23160925-8	2013	UFH dose dependently inhibited the effect of IFN-gamma on the secretion and expression of CXCL9 and CXCL10.	Heparin	0-3	C-X-C motif chemokine ligand 10	Homo sapiens	100-106
23160925-10	2013	As a reason for these heparin effects, we could show that the IFN-gamma-induced phosphorylation of STAT1 was modulated by heparins, caused by an interaction with the cellular binding of IFN-gamma.	Heparin	22-29	signal transducer and activator of transcription 1	Homo sapiens	99-104
23160925-10	2013	As a reason for these heparin effects, we could show that the IFN-gamma-induced phosphorylation of STAT1 was modulated by heparins, caused by an interaction with the cellular binding of IFN-gamma.	Heparin	122-130	signal transducer and activator of transcription 1	Homo sapiens	99-104
16709700-7	2006	The addition of P-selectin blockade abolished any increase in platelet-monocyte aggregates associated with heparin.	Heparin	107-114	selectin P	Homo sapiens	16-26
23122594-0	2012	Enhanced anti-angiogenesis and anti-tumor activity of endostatin by chemical modification with polyethylene glycol and low molecular weight heparin.	Heparin	140-147	collagen, type XVIII, alpha 1	Mus musculus	54-64
23186339-7	2012	LPL was releasable by heparin, indicating localization on cell surfaces.	Heparin	22-29	lipoprotein lipase	Mus musculus	0-3
22963465-8	2012	We observed that heparin mimetic peptide nanofibers demonstrate better binding profiles to VEGF, hepatocyte growth factor (HGF), and fibroblast growth factor-2 (FGF-2) than control peptide nanofibers.	Heparin	17-24	hepatocyte growth factor	Rattus norvegicus	97-121
22963465-8	2012	We observed that heparin mimetic peptide nanofibers demonstrate better binding profiles to VEGF, hepatocyte growth factor (HGF), and fibroblast growth factor-2 (FGF-2) than control peptide nanofibers.	Heparin	17-24	hepatocyte growth factor	Rattus norvegicus	123-126
23407680-3	2012	In this study the mature part of human bone morphogenetic protein-7 (BMP-7) was engineered through substitution of the BMP-7 N-terminal sequence by heparin-binding site of BMP-2.	Heparin	148-155	bone morphogenetic protein 7	Homo sapiens	39-67
23407680-3	2012	In this study the mature part of human bone morphogenetic protein-7 (BMP-7) was engineered through substitution of the BMP-7 N-terminal sequence by heparin-binding site of BMP-2.	Heparin	148-155	bone morphogenetic protein 7	Homo sapiens	69-74
23040778-11	2012	UFH could exert protective effects by inhibiting expression of MMP-2 and MMP-9 in serum and lung tissue, in both mRNA and protein expression.	Heparin	0-3	matrix metallopeptidase 9	Rattus norvegicus	73-78
22920789-1	2012	Fibroblast growth factor 9 (FGF9), an important member of the fibroblast growth factor (FGF) family, can bind with high affinity to FGFR3 in a heparin-dependent approach.	Heparin	143-150	fibroblast growth factor 9	Homo sapiens	0-26
22920789-1	2012	Fibroblast growth factor 9 (FGF9), an important member of the fibroblast growth factor (FGF) family, can bind with high affinity to FGFR3 in a heparin-dependent approach.	Heparin	143-150	fibroblast growth factor 9	Homo sapiens	28-32
22920789-1	2012	Fibroblast growth factor 9 (FGF9), an important member of the fibroblast growth factor (FGF) family, can bind with high affinity to FGFR3 in a heparin-dependent approach.	Heparin	143-150	fibroblast growth factor receptor 3	Homo sapiens	132-137
22759380-4	2012	In vitro maturation of cumulus oocyte complexes in the presence of exogenous heparin, which antagonizes HSPG signaling, prevented cumulus expansion and blocked the induction of cumulus-specific matrix genes, Has2 and Tnfaip6, whereas conversely, the mural granulosa-specific genes, Lhcgr and Cyp11a1, were strongly up-regulated.	Heparin	77-84	syndecan 2	Homo sapiens	104-108
22759380-4	2012	In vitro maturation of cumulus oocyte complexes in the presence of exogenous heparin, which antagonizes HSPG signaling, prevented cumulus expansion and blocked the induction of cumulus-specific matrix genes, Has2 and Tnfaip6, whereas conversely, the mural granulosa-specific genes, Lhcgr and Cyp11a1, were strongly up-regulated.	Heparin	77-84	TNF alpha induced protein 6	Homo sapiens	217-224
22759380-6	2012	Exogenous growth differentiation factor (GDF)-9 reversed these heparin effects; furthermore, GDF9 strongly bound to heparin sepharose.	Heparin	63-70	growth differentiation factor 9	Homo sapiens	10-47
22759380-6	2012	Exogenous growth differentiation factor (GDF)-9 reversed these heparin effects; furthermore, GDF9 strongly bound to heparin sepharose.	Heparin	116-123	growth differentiation factor 9	Homo sapiens	10-47
22820186-5	2012	The PPARdelta agonist GW501516 had no effect on LPL mRNA, but increased ANGPTL4 mRNA and caused a marked reduction of the heparin-releasable LPL activity concomitantly with accumulation of inactive, monomeric LPL in the medium.	Heparin	122-129	peroxisome proliferator activated receptor delta	Homo sapiens	4-13
22773834-2	2012	Heparin is a commonly used anticoagulant drug that inhibits the activities of factors Xa and IIa (also known as thrombin) to prevent blood clot formation.	Heparin	0-7	coagulation factor X	Homo sapiens	78-96
22504297-5	2012	Furthermore, rat embryonic fibroblasts (REFs) plated on fibronectin fragments lacking the heparin-binding domain that interacts with syndecan-4 showed much lower RhoA activation than that in cells plated on full-length fibronectin, indicating that RhoA is involved in syndecan-4-mediated cell adhesion signaling.	Heparin	90-97	ras homolog family member A	Rattus norvegicus	162-166
22504297-5	2012	Furthermore, rat embryonic fibroblasts (REFs) plated on fibronectin fragments lacking the heparin-binding domain that interacts with syndecan-4 showed much lower RhoA activation than that in cells plated on full-length fibronectin, indicating that RhoA is involved in syndecan-4-mediated cell adhesion signaling.	Heparin	90-97	ras homolog family member A	Rattus norvegicus	248-252
22920489-4	2012	Unfractionated heparin traditionally has been the most commonly used anticoagulant but is fast being replaced by relatively newer agents like LMWH, direct thrombin inhibitors, and Factor Xa inhibitors.	Heparin	15-22	coagulation factor X	Homo sapiens	180-189
22539676-6	2012	Similarly to BSP proteins from other species, rec-BSPH1 bound to gelatin, heparin, phosphatidylcholine liposomes, and sperm.	Heparin	74-81	binder of sperm protein homolog 1	Mus musculus	50-55
22471560-0	2012	Bivalent and co-operative binding of complement factor H to heparan sulfate and heparin.	Heparin	80-87	complement factor H	Homo sapiens	37-56
22471560-4	2012	Ultracentrifugation showed that FH formed up to 63% of well-defined oligomers with purified heparin fragments (equivalent to S-domains), and indicated a dissociation constant K(d) of approximately 0.5 muM.	Heparin	92-99	complement factor H	Homo sapiens	32-34
22471560-5	2012	Unchanged FH structures that are bivalently cross-linked at SCR-7 and SCR-20 with heparin explained the sedimentation coefficients of the FH-heparin oligomers.	Heparin	82-89	complement factor H	Homo sapiens	10-12
22471560-5	2012	Unchanged FH structures that are bivalently cross-linked at SCR-7 and SCR-20 with heparin explained the sedimentation coefficients of the FH-heparin oligomers.	Heparin	82-89	complement factor H	Homo sapiens	138-140
22669117-11	2012	RESULTS: Heparin 25 and 125 mug/mL significantly inhibited the proliferation, arrested the cells in G(1) phase, and suppressed BrdU incorporation and Ki67 expression in PC-3M cells compared with the model group.	Heparin	9-16	antigen identified by monoclonal antibody Ki 67	Mus musculus	150-154
22669117-17	2012	Heparin 25 and 125 mug/mL decreased the protein expression of vimentin and 14-3-3 zeta/delta and the mRNA expression of alpha(v)-integrin.	Heparin	0-7	vimentin	Mus musculus	62-70
22669117-17	2012	Heparin 25 and 125 mug/mL decreased the protein expression of vimentin and 14-3-3 zeta/delta and the mRNA expression of alpha(v)-integrin.	Heparin	0-7	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta polypeptide	Mus musculus	75-86
22669117-20	2012	CONCLUSION: Heparin inhibited PC-3M cell proliferation in vitro and B16-F10-luc-G5 cells metastasis in nude mice by inhibition of vimentin, 14-3-3 zeta/delta, and alpha(v)-integrin expression.	Heparin	12-19	vimentin	Mus musculus	130-138
22669117-20	2012	CONCLUSION: Heparin inhibited PC-3M cell proliferation in vitro and B16-F10-luc-G5 cells metastasis in nude mice by inhibition of vimentin, 14-3-3 zeta/delta, and alpha(v)-integrin expression.	Heparin	12-19	tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta polypeptide	Mus musculus	140-151
21898414-7	2012	In addition, heparin induces ERK1/2 phosphorylation and inhibitors of Ras and MEK decreased heparin-dependent HSPG synthesis.	Heparin	13-20	CD44 molecule (Indian blood group)	Homo sapiens	110-114
21898414-7	2012	In addition, heparin induces ERK1/2 phosphorylation and inhibitors of Ras and MEK decreased heparin-dependent HSPG synthesis.	Heparin	92-99	CD44 molecule (Indian blood group)	Homo sapiens	110-114
21898414-10	2012	In conclusion, the heparin-induced up-regulation of HSPG expression is associated with the phosphorylation of focal adhesion proteins and Ras/Raf/MEK/ERK MAP and Ca(2+) /NO pathways.	Heparin	19-26	CD44 molecule (Indian blood group)	Homo sapiens	52-56
22155502-8	2012	Although both approaches resulted in a phenotype consistent with CD56(bright) stage IV NK cells, heparin-based cultures favored the development of CD56(+)CD16(+) cells, whereas stroma produced more NK cell immunoglobulin-like receptor-expressing NK cells, both of which are markers of terminal maturation.	Heparin	97-104	Fc gamma receptor IIIa	Homo sapiens	154-158
22231174-0	2012	Standard subcutaneous dosing of unfractionated heparin for venous thromboembolism prophylaxis in surgical ICU patients leads to subtherapeutic factor Xa inhibition.	Heparin	47-54	coagulation factor X	Homo sapiens	143-152
22231174-12	2012	CONCLUSIONS: Standard of care subcutaneous dosing of unfractionated heparin for VTE prophylaxis in surgical ICU patients leads to subtherapeutic levels of factor Xa inhibition.	Heparin	68-75	coagulation factor X	Homo sapiens	155-164
22315264-3	2012	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes.	Heparin	0-3	coagulation factor X	Homo sapiens	160-169
22081368-4	2012	The recently developed direct factor Xa inhibitors (the xabans) appear to offer promise as alternatives to the heparins.	Heparin	111-119	coagulation factor X	Homo sapiens	30-39
22210566-0	2012	Circulating brain-derived neurotrophic factor concentration is downregulated by intralipid/heparin infusion or high-fat meal in young healthy male subjects.	Heparin	91-98	brain derived neurotrophic factor	Homo sapiens	12-45
22137027-12	2012	The oligomeric FH-heparin complexes clarify a two-site interaction model of FH with host-cell surfaces.	Heparin	18-25	complement factor H	Homo sapiens	15-17
21740405-1	2012	New direct and indirect acting factor Xa (FXa) and thrombin inhibitors are being developed to overcome the downsides of the conventional anticoagulants - unfractionated and low molecular weight heparins and vitamin K antagonists.	Heparin	194-202	coagulation factor X	Homo sapiens	31-40
21740405-1	2012	New direct and indirect acting factor Xa (FXa) and thrombin inhibitors are being developed to overcome the downsides of the conventional anticoagulants - unfractionated and low molecular weight heparins and vitamin K antagonists.	Heparin	194-202	coagulation factor X	Homo sapiens	42-45
22654952-0	2012	Heparin increases HLA-G levels in primary antiphospholipid syndrome.	Heparin	0-7	major histocompatibility complex, class I, G	Homo sapiens	18-23
22654952-1	2012	OBJECTIVES: The aim of this study was to investigate the HLA-G serum levels in Primary Antiphospholipid Syndrome (PAPS) patients, its impact on clinical and laboratory findings, and heparin treatment.	Heparin	182-189	major histocompatibility complex, class I, G	Homo sapiens	57-62
22654952-7	2012	Interestingly, patients treated with heparin had higher HLA-G levels than ones who were not treated with this medication (5 (0-22.9) versus 1.8 (0-16) ng/mL, P = 0.038).	Heparin	37-44	major histocompatibility complex, class I, G	Homo sapiens	56-61
22654952-8	2012	Furthermore, patients on heparin who experienced obstetric events had a trend to increased HLA-G levels compared to patients who were not on heparin and did not have obstetric events (5.8 (0-22.9) versus 2 (0-15.2) ng/mL, P = 0.05).	Heparin	25-32	major histocompatibility complex, class I, G	Homo sapiens	91-96
22654952-10	2012	We also demonstrated that heparin increases HLA-G levels and may increase tolerance towards autoantigens.	Heparin	26-33	major histocompatibility complex, class I, G	Homo sapiens	44-49
22042649-6	2012	By combining NT-3 with heparin during the protein incorporation process, a sustained release of NT-3 was obtained (~96% by day 28).	Heparin	23-30	neurotrophin 3	Homo sapiens	96-100
22427833-8	2012	It also displays a concentration-dependent inhibition of thrombin that is accelerated by heparin.	Heparin	89-96	coagulation factor II, thrombin	Bos taurus	57-65
22174307-1	2011	In this issue of Blood, Yau and colleagues provide evidence that guide catheter thrombosis in patients undergoing percutaneous coronary intervention (PCI) is initiated by contact system activation, and that unfractionated heparin is more effective than fondaparinux at limiting catheter occlusions because heparin-antithrombin complexes are able to target multiple points along the coagulation cascade, as opposed to the smaller fractionated heparins and heparinoids that provide higher selectivity for factor Xa.	Heparin	222-229	coagulation factor X	Homo sapiens	503-512
21979436-2	2011	Because sFlt1 has a heparin-binding site, we investigated whether or not heparin releases sFlt1 from the extracellular matrix.	Heparin	20-27	FMS-like tyrosine kinase 1	Mus musculus	8-13
21979436-4	2011	sFlt1 was increased directly after heparin administration (from 254 to 13,440 pg/mL) and returned to baseline within 10 hours.	Heparin	35-42	FMS-like tyrosine kinase 1	Mus musculus	0-5
21979436-5	2011	Umbilical veins and endothelial cells treated with heparin released sFlt1.	Heparin	51-58	FMS-like tyrosine kinase 1	Mus musculus	68-73
21979436-7	2011	Mice treated with heparin had elevated sFlt1 serum levels.	Heparin	18-25	FMS-like tyrosine kinase 1	Mus musculus	39-44
21979436-9	2011	CONCLUSIONS: Heparin releases sFlt1 by displacing the sFlt1 heparin-binding site from heparan sulfate proteoglycans.	Heparin	13-20	FMS-like tyrosine kinase 1	Mus musculus	30-35
21979436-9	2011	CONCLUSIONS: Heparin releases sFlt1 by displacing the sFlt1 heparin-binding site from heparan sulfate proteoglycans.	Heparin	13-20	FMS-like tyrosine kinase 1	Mus musculus	54-59
21979436-9	2011	CONCLUSIONS: Heparin releases sFlt1 by displacing the sFlt1 heparin-binding site from heparan sulfate proteoglycans.	Heparin	60-67	FMS-like tyrosine kinase 1	Mus musculus	30-35
21979436-9	2011	CONCLUSIONS: Heparin releases sFlt1 by displacing the sFlt1 heparin-binding site from heparan sulfate proteoglycans.	Heparin	60-67	FMS-like tyrosine kinase 1	Mus musculus	54-59
21872908-10	2011	RESULTS: The fluorogenic anti-FXa assay was found to have the broadest therapeutic range of 0-1 U/ml with CVs of&lt;5% for UFH and tinzaparin and CVs&lt;9% for enoxaparin.	Heparin	123-126	coagulation factor X	Homo sapiens	30-33
22012070-5	2011	In this assay, direct factor Xa (FXa) inhibitors such as edoxaban and antithrombin (AT)-dependent anticoagulants such as heparin did not increase, but simply suppressed TG.	Heparin	121-128	coagulation factor X	Homo sapiens	22-31
22012070-5	2011	In this assay, direct factor Xa (FXa) inhibitors such as edoxaban and antithrombin (AT)-dependent anticoagulants such as heparin did not increase, but simply suppressed TG.	Heparin	121-128	coagulation factor X	Homo sapiens	33-36
22122911-0	2011	Sequence similarity between the erythrocyte binding domain of the Plasmodium vivax Duffy binding protein and the V3 loop of HIV-1 strain MN reveals a functional heparin binding motif involved in binding to the Duffy antigen receptor for chemokines.	Heparin	161-168	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	210-247
22122911-4	2011	A peptide including the HBM of PvDBP had similar affinity for heparin as RANTES and V3 loop peptides, and could be specifically inhibited from heparin binding by the same polyanions that inhibit DBP binding to DARC.	Heparin	143-150	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	210-214
22122911-6	2011	Three other members of the DBP family have an HBM sequence that is necessary for erythrocyte binding, however only the protein which binds to DARC, the P. knowlesi alpha protein, is inhibited by heparin from binding to erythrocytes.	Heparin	195-202	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	142-146
22122911-8	2011	CONCLUSION: The HBMs of DBPs that bind to DARC have similar heparin binding affinities as some V3 loop peptides and chemokines, are responsible for specific sulfated polysaccharide inhibition of parasite binding and invasion of red blood cells, and are more likely to bind to negative charges on the receptor than cell surface glycosaminoglycans.	Heparin	60-67	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	42-46
21826315-5	2011	Optical tweezer measurements show that the rupture force required to disrupt the heparin-VEGF-VEGFR-2 interaction increases from 3-8 pN to 6-12 pN when a covalent bond is introduced between VEGF and heparin.	Heparin	81-88	kinase insert domain receptor	Homo sapiens	94-101
21652703-16	2011	The binding sequences for PEDF and heparin/HSPG also overlapped with the covalent cross-linking sites between collagen molecules.	Heparin	35-42	syndecan 2	Homo sapiens	43-47
21569756-0	2011	Identification of regions responsible for heparin-induced amyloidogenesis of human serum amyloid A using its fragment peptides.	Heparin	42-49	serum amyloid A1 cluster	Homo sapiens	83-98
21569756-4	2011	In the present study, amyloidogenic properties of synthetic fragment peptides corresponding to the N-terminal (residues 1-27), central (residues 43-63), and C-terminal (residues 77-104) regions of SAA molecule induced by heparin were examined using fluorescence, circular dichroism (CD), and electron microscopy.	Heparin	221-228	serum amyloid A1 cluster	Homo sapiens	197-200
21569756-5	2011	Fluorescence and CD measurements demonstrated that SAA (1-27) peptide is evidently involved in heparin-induced amyloidogenesis.	Heparin	95-102	serum amyloid A1 cluster	Homo sapiens	51-54
21569756-9	2011	These results suggest that the N-terminal region plays a crucial role as a rigid core and the central region facilitates the elongation of fibrils in heparin-induced amyloidogenesis of SAA molecule.	Heparin	150-157	serum amyloid A1 cluster	Homo sapiens	185-188
21395445-5	2011	After 7 days of subcutaneous implantation in immunodeficient mice, heparin-immobilized PCL scaffolds with VEGF induced significantly high density of blood vessel formation.	Heparin	67-74	vascular endothelial growth factor A	Mus musculus	106-110
21395445-11	2011	EPCs accelerated the vascularization of heparin-immobilized PCL scaffolds in the presence of VEGF.	Heparin	40-47	vascular endothelial growth factor A	Mus musculus	93-97
21562164-7	2011	Heparin promoted tryptase tetramer formation and protected tryptase from degradation by CTSB and CTSL.	Heparin	0-7	cathepsin B	Homo sapiens	88-92
21401902-9	2011	Factor Xa based assays may be particularly sensitive to certain heparin binding defects, and sensitivity of assays to both heparin binding and reactive site defects can be improved by shortening the incubation time with enzyme.	Heparin	64-71	coagulation factor X	Homo sapiens	0-9
21600981-7	2011	These findings indicate that heparinized vascular grafts may promote elastin formation and regulate restenosis, in addition to heparin"s well-established antithrombotic properties.	Heparin	29-36	elastin	Homo sapiens	69-76
21600981-8	2011	Given the increase in elastin mRNA level and the increase in extracellular elastin present, our data suggests that there may be multiple levels of elastin regulation that are mediated by heparin treatment.	Heparin	187-194	elastin	Homo sapiens	22-29
21600981-8	2011	Given the increase in elastin mRNA level and the increase in extracellular elastin present, our data suggests that there may be multiple levels of elastin regulation that are mediated by heparin treatment.	Heparin	187-194	elastin	Homo sapiens	75-82
21600981-8	2011	Given the increase in elastin mRNA level and the increase in extracellular elastin present, our data suggests that there may be multiple levels of elastin regulation that are mediated by heparin treatment.	Heparin	187-194	elastin	Homo sapiens	75-82
21805445-4	2011	Among various functions of HRG, its interactions with heparin/heparan sulfate, fibrinogen, and plasminogen are thought to be intimately related to its roles in the coagulation and fibrinolytic systems.	Heparin	54-61	histidine rich glycoprotein	Homo sapiens	27-30
20853445-5	2011	Herein, by using heparin, a membrane-impermeant inositol trisphosphate receptor (IP3R) blocker, we explored the contribution of presynaptic and postsynaptic IP3-sensitive calcium stores to the ganglionic LTP.	Heparin	17-24	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	81-85
27704481-8	2016	Similarly, unfractionated heparins and low molecular weight heparins counteracted permeability increased by HBP in vitro.	Heparin	26-34	azurocidin 1	Homo sapiens	108-111
27704481-8	2016	Similarly, unfractionated heparins and low molecular weight heparins counteracted permeability increased by HBP in vitro.	Heparin	60-68	azurocidin 1	Homo sapiens	108-111
27704481-12	2016	Heparins are potential inhibitors of HBP-induced increases in permeability.	Heparin	0-8	azurocidin 1	Homo sapiens	37-40
27502551-1	2016	Heparin/heparan sulfate (HS) glycosaminoglycans are required for Slit-Robo cellular responses.	Heparin	0-7	roundabout 1	Drosophila melanogaster	70-74
27582494-6	2016	TIMP-3 K26A/K45A retained higher affinity for sulfated glycosaminoglycans than K42A/K110A and exhibited increased affinity for ADAMTS-5 in the presence of heparin.	Heparin	155-162	TIMP metallopeptidase inhibitor 3	Homo sapiens	0-6
27582494-6	2016	TIMP-3 K26A/K45A retained higher affinity for sulfated glycosaminoglycans than K42A/K110A and exhibited increased affinity for ADAMTS-5 in the presence of heparin.	Heparin	155-162	ADAM metallopeptidase with thrombospondin type 1 motif 5	Homo sapiens	127-135
27338096-4	2016	Like other serpin-protease partners, C1-INH interaction with C1s is accelerated by polyanions such as heparin.	Heparin	102-109	serpin family G member 1	Homo sapiens	37-43
27338096-11	2016	In summary, like heparin, polyP is a naturally occurring cofactor for the C1s:C1-INH interaction and thus an important regulator of complement activation.	Heparin	17-24	serpin family G member 1	Homo sapiens	78-84
27369043-4	2016	Three different blood collection tubes (lithium-heparin tubes, CPT with sodium citrate and CPT with sodium heparin) were evaluated, with PBMC isolated through lithium-heparin tubes/lymphoprep displaying reduced basal and increased stimulation induced phosphorylation compared to the other two methods.	Heparin	100-114	choline phosphotransferase 1	Homo sapiens	91-94
27990411-5	2016	The cell adhesion to LL-37 was partially inhibited by specific Mac-1 antagonists, including mAb against the alphaM integrin subunit and neutrophil inhibitory factor, and completely blocked when anti-Mac-1 antibodies were combined with heparin, suggesting that cell surface heparan sulfate proteoglycans act cooperatively with integrin Mac-1.	Heparin	235-242	integrin subunit alpha M	Homo sapiens	63-68
26947349-0	2016	Advanced Interfere Treatment of Diabetic Cardiomyopathy Rats by aFGF-Loaded Heparin-Modified Microbubbles and UTMD Technique.	Heparin	76-83	fibroblast growth factor 1	Rattus norvegicus	64-68
26947349-1	2016	This study aims to investigate the preclinical performance and mechanism of a novel strategy of aFGF-loaded heparin-modified microbubbles (aFGF-HMB) combined with ultrasound-targeted microbubble destruction (UTMD) technique for diabetic cardiomyopathy (DCM) prevention.	Heparin	108-115	fibroblast growth factor 1	Rattus norvegicus	96-100
26947349-1	2016	This study aims to investigate the preclinical performance and mechanism of a novel strategy of aFGF-loaded heparin-modified microbubbles (aFGF-HMB) combined with ultrasound-targeted microbubble destruction (UTMD) technique for diabetic cardiomyopathy (DCM) prevention.	Heparin	108-115	fibroblast growth factor 1	Rattus norvegicus	139-143
26874675-5	2016	The inhibitory capacity of C1-INH for the CP is potentiated by heparin and other glycosaminoglycans, but no data exist for the LP and AP.	Heparin	63-70	serpin family G member 1	Homo sapiens	27-33
27105909-0	2016	Heparin interactions with apoA1 and SAA in inflammation-associated HDL.	Heparin	0-7	apolipoprotein A-I	Mus musculus	26-31
27105909-0	2016	Heparin interactions with apoA1 and SAA in inflammation-associated HDL.	Heparin	0-7	serum amyloid A cluster	Mus musculus	36-39
27105909-4	2016	We report herein that the polysaccharide heparin interacts with both apoA1 and SAA in HDL isolated from plasma of inflamed mice.	Heparin	41-48	apolipoprotein A-I	Mus musculus	69-74
27105909-4	2016	We report herein that the polysaccharide heparin interacts with both apoA1 and SAA in HDL isolated from plasma of inflamed mice.	Heparin	41-48	serum amyloid A cluster	Mus musculus	79-82
27105909-7	2016	Mass spectrometry analysis of peptides derived from chemically crosslinked HDL-SAA particles detected multiple crosslinks between apoA1 and SAA, indicating close proximity (within 25 A) of these two proteins on the HDL surface, providing a molecular and structural mechanism for the simultaneous binding of heparin to apoA1 and SAA.	Heparin	307-314	serum amyloid A cluster	Mus musculus	79-82
27105909-7	2016	Mass spectrometry analysis of peptides derived from chemically crosslinked HDL-SAA particles detected multiple crosslinks between apoA1 and SAA, indicating close proximity (within 25 A) of these two proteins on the HDL surface, providing a molecular and structural mechanism for the simultaneous binding of heparin to apoA1 and SAA.	Heparin	307-314	serum amyloid A cluster	Mus musculus	140-143
27105909-7	2016	Mass spectrometry analysis of peptides derived from chemically crosslinked HDL-SAA particles detected multiple crosslinks between apoA1 and SAA, indicating close proximity (within 25 A) of these two proteins on the HDL surface, providing a molecular and structural mechanism for the simultaneous binding of heparin to apoA1 and SAA.	Heparin	307-314	serum amyloid A cluster	Mus musculus	140-143
27097800-6	2016	We found heparin to be the strongest binding host for CCL7 with a 0.323 nM dissociation constant.	Heparin	9-16	C-C motif chemokine ligand 7	Homo sapiens	54-58
27097800-7	2016	Our experimental approach indicates conjugation of heparin to a polymer backbone (using either bovine serum albumin or poly (ethylene glycol) as the base polymer) can be used as a delivery system capable of providing sustained concentrations of CCL7 in a therapeutically useful range up to a month in vitro.	Heparin	51-58	C-C motif chemokine ligand 7	Homo sapiens	245-249
27097314-6	2016	We found that VEGF-A and FGF-2, acting in synergy with HIV-Tat and heparin, affected the cytoskeletal structure and permeability of REc through changes in Rho-A, Src, and Rac-1 activity.	Heparin	67-74	Rac family small GTPase 1	Homo sapiens	171-176
27069129-0	2016	Unfractionated Heparin Selectively Modulates the Expression of CXCL8, CCL2 and CCL5 in Endometrial Carcinoma Cells.	Heparin	15-22	C-C motif chemokine ligand 5	Homo sapiens	79-83
27069129-5	2016	UFH attenuated the secretion of CXCL8 and CCL2, and enhanced that of CCL5.	Heparin	0-3	C-C motif chemokine ligand 5	Homo sapiens	69-73
27069129-7	2016	CONCLUSION: UFH has selective modulating effects on the secretion of CXCL8, CCL2 and CCL5 in different endometrial adenocarcinoma cell lines.	Heparin	12-15	C-C motif chemokine ligand 5	Homo sapiens	85-89
26939028-5	2016	Andexanet alfa is a recombinant modified factor Xa that can bind and reverse oral and parenteral factor Xa inhibitors, including rivaroxaban, apixaban and edoxaban, and low molecular weight heparin.	Heparin	190-197	coagulation factor X	Homo sapiens	41-50
26317490-6	2016	Heparin and iota-carrageenan blocked binding and infection of all tumor lines tested, implying that tumor cell binding is HSPG-dependent.	Heparin	0-7	syndecan 2	Homo sapiens	122-126
26317490-7	2016	A survey using a panel of modified heparins indicates that N-sulfation and, to a lesser degree, O-6 sulfation of the surface HSPG on the tumors are important for HPV binding.	Heparin	35-43	syndecan 2	Homo sapiens	125-129
26790955-10	2016	This is the first study to demonstrate that kallistatin"s heparin-binding site is essential for inhibiting Wnt-mediated effects, and its active site plays a key role in regulating miR-21, miR-203, miR-34a and SOCS3 synthesis in breast cancer cells.	Heparin	58-65	serpin family A member 4	Homo sapiens	44-55
26998625-8	2016	Attenuating intracellular calcium concentration with EGTA, heparin or procaine decreased POX-induced upregulation of calpain 1, calpain 2, caspase-12 and caspase-3, and reduced POX-induced cyt c release.	Heparin	59-66	caspase 3	Mus musculus	154-163
26490079-1	2015	MicroRNA (miRNA, miR) measurements in patients with coronary heart disease are hampered by the confounding effects of medication commonly used in cardiovascular patients such as statins, antiplatelet drugs, and heparin administration.	Heparin	211-218	membrane associated ring-CH-type finger 8	Homo sapiens	10-13
21370880-0	2011	Characterization of annexin A1 glycan binding reveals binding to highly sulfated glycans with preference for highly sulfated heparan sulfate and heparin.	Heparin	145-152	annexin A1	Homo sapiens	20-30
21370880-5	2011	Using heparin/heparan sulfate microarrays, highly sulfated heparan sulfate/heparin were identified as preferred ligands of annexin A1.	Heparin	6-13	annexin A1	Homo sapiens	123-133
21370880-5	2011	Using heparin/heparan sulfate microarrays, highly sulfated heparan sulfate/heparin were identified as preferred ligands of annexin A1.	Heparin	75-82	annexin A1	Homo sapiens	123-133
21370880-6	2011	Binding of annexin A1 to heparin/heparan sulfate is calcium- but not magnesium-dependent.	Heparin	25-32	annexin A1	Homo sapiens	11-21
20558775-0	2011	Heparin inhibits pulmonary artery smooth muscle cell proliferation through guanine nucleotide exchange factor-H1/RhoA/Rho kinase/p27.	Heparin	0-7	cyclin-dependent kinase inhibitor 1B	Mus musculus	129-132
20558775-2	2011	Our previous studies found that heparin inhibition of pulmonary artery SMC (PASMC) proliferation and pulmonary hypertension was dependent on p27 up-regulation.	Heparin	32-39	cyclin-dependent kinase inhibitor 1B	Mus musculus	141-144
21170647-4	2011	Heparin inhibited the stimulatory effect of GcMAF on PBMCs.	Heparin	0-7	GC vitamin D binding protein	Homo sapiens	44-49
21288929-6	2011	Oversulfated chondroitin sulfate from different sources as well as heparin by-products produced activation of prekallikrein to kallikrein at variable rates as measured by the generation of kallikrein.	Heparin	67-74	kallikrein related peptidase 4	Homo sapiens	113-123
21288929-6	2011	Oversulfated chondroitin sulfate from different sources as well as heparin by-products produced activation of prekallikrein to kallikrein at variable rates as measured by the generation of kallikrein.	Heparin	67-74	kallikrein related peptidase 4	Homo sapiens	127-137
21088675-0	2011	Lipid-heparin infusion suppresses the IL-10 response to trauma in subcutaneous adipose tissue in humans.	Heparin	6-13	interleukin 10	Homo sapiens	38-43
21088675-7	2011	In contrast, the level of IL-10, an anti-inflammatory cytokine, was significantly reduced during the final hour of lipid-heparin infusion (saline: 449.2 +- 105.9 vs. lipid-heparin: 65.4 +- 15.4 pg/ml; P = 0.02).	Heparin	121-128	interleukin 10	Homo sapiens	26-31
21088675-7	2011	In contrast, the level of IL-10, an anti-inflammatory cytokine, was significantly reduced during the final hour of lipid-heparin infusion (saline: 449.2 +- 105.9 vs. lipid-heparin: 65.4 +- 15.4 pg/ml; P = 0.02).	Heparin	172-179	interleukin 10	Homo sapiens	26-31
16709700-8	2006	CONCLUSIONS: In vitro and in vivo unfractionated heparin is associated with increased platelet-monocyte aggregation through a P-selectin-dependent mechanism.	Heparin	49-56	selectin P	Homo sapiens	126-136
21220417-3	2011	Heparin produced 20-100-fold accelerations of ZPI reactions with factor Xa and factor XIa to yield second order rate constants approaching the physiologically significant diffusion limit (k(a) = 10(6) to 10(7) M(-1) s(-1)).	Heparin	0-7	coagulation factor X	Homo sapiens	65-74
21220417-5	2011	Maximal accelerations of ZPI-factor Xa reactions required calcium, which augmented the heparin acceleration by relieving Gla domain inhibition as previously shown for heparin bridging of the antithrombin-factor Xa reaction.	Heparin	87-94	coagulation factor X	Homo sapiens	29-38
16882661-0	2006	Crystallographic analysis of calcium-dependent heparin binding to annexin A2.	Heparin	47-54	annexin A2	Homo sapiens	66-76
21220417-5	2011	Maximal accelerations of ZPI-factor Xa reactions required calcium, which augmented the heparin acceleration by relieving Gla domain inhibition as previously shown for heparin bridging of the antithrombin-factor Xa reaction.	Heparin	87-94	coagulation factor X	Homo sapiens	204-213
16940049-8	2006	Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity.	Heparin	233-240	serpin family C member 1	Homo sapiens	114-126
21147501-1	2011	This study investigates the effect of surface cross-linked heparin on vascular endothelial growth factor (VEGF)-mediated angiogenesis in porous polycaprolactone (PCL) scaffolds in vivo.	Heparin	59-66	vascular endothelial growth factor A	Mus musculus	70-104
21147501-1	2011	This study investigates the effect of surface cross-linked heparin on vascular endothelial growth factor (VEGF)-mediated angiogenesis in porous polycaprolactone (PCL) scaffolds in vivo.	Heparin	59-66	vascular endothelial growth factor A	Mus musculus	106-110
21147501-2	2011	We tested the hypothesis that VEGF delivered by scaffolds coated with a sub-micron thick layer of immobilized heparin would accelerate angiogenesis.	Heparin	110-117	vascular endothelial growth factor A	Mus musculus	30-34
16940049-8	2006	Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity.	Heparin	233-240	serpin family C member 1	Homo sapiens	305-310
17043951-6	2006	Anticoagulant heparan sulfate proteoglycans (aHSPG), like heparin, possess a pentasaccharide sequence which binds and activates antithrombin III.	Heparin	58-65	serpin family C member 1	Homo sapiens	128-144
21048021-6	2011	When human plasma was fractionated by denaturing heparin affinity chromatography, VN was isolated in a biologically active form that supported rapid spreading of urothelial cells in vitro under serum-free conditions.	Heparin	49-56	vitronectin	Homo sapiens	82-84
21048021-8	2011	A novel form of VN, isolated from the same heparin affinity chromatography column and designated as the VN(c) chromatomer, also supported cell spreading but failed to interact with SPARC.	Heparin	43-50	vitronectin	Homo sapiens	16-18
21086021-1	2011	Heparin compounds, to include fractionated and unfractionated preparations, exert both antithrombotic and antiinflammatory effects through combined inhibition of factor Xa and thrombin.	Heparin	0-7	coagulation factor X	Homo sapiens	162-171
16966848-8	2006	Heparin infusion was started when the antithrombin value was &gt; 100% and remained stable for more than 12 hours and the amount of bleeding was &lt; 2 ml/kg for more than 3 consecutive hours; then heparin infusion was started at 2 UI/kg/h via the oxygenator (target ACT was not &lt; 150 seconds).	Heparin	0-7	serpin family C member 1	Homo sapiens	38-50
21086021-9	2011	The ability of heparin compounds to affect the prothrombotic and proinflammatory states which characterize ACS may involve factor Xa-related modulation of platelet activation and expression.	Heparin	15-22	coagulation factor X	Homo sapiens	123-132
20659908-0	2011	Effects of unfractioned heparin and low-molecular-weight heparin on osteoprotegerin and RANKL plasma levels in haemodialysis patients.	Heparin	24-31	TNF superfamily member 11	Homo sapiens	88-93
20659908-0	2011	Effects of unfractioned heparin and low-molecular-weight heparin on osteoprotegerin and RANKL plasma levels in haemodialysis patients.	Heparin	57-64	TNF superfamily member 11	Homo sapiens	88-93
22013445-6	2011	Factor-specific anticoagulants have been proven safe and effective, and recently factor Xa inhibitors have emerged as a treatment alternative to heparins and VKA.	Heparin	145-153	coagulation factor X	Homo sapiens	81-90
21052646-1	2011	Heparin-immobilized microspheres were included in microdialysis sampling perfusion fluids under both in vitro and in vivo conditions to improve the recovery of different cytokines, acidic fibroblast growth factor, vascular endothelial growth factor, monocyte chemoattractant protein-1 (or CCL2), and regulation upon activation normal T cell express sequence (or CCL5).	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	181-212
21052646-1	2011	Heparin-immobilized microspheres were included in microdialysis sampling perfusion fluids under both in vitro and in vivo conditions to improve the recovery of different cytokines, acidic fibroblast growth factor, vascular endothelial growth factor, monocyte chemoattractant protein-1 (or CCL2), and regulation upon activation normal T cell express sequence (or CCL5).	Heparin	0-7	C-C motif chemokine ligand 5	Rattus norvegicus	362-366
22180365-2	2011	We have previously reported that heparin competitively inhibits the binding activity of bone morphogenic protein-2 (BMP-2) to BMP and the BMP receptor (BMPR) and suppresses BMP-2 osteogenic activity.	Heparin	33-40	bone morphogenetic protein receptor, type 1A	Mus musculus	138-150
19748137-9	2010	Unfractionated heparin (UFH) was the major anticoagulant during TRA and TRI (88.76% in 2006 vs. 99.10% in 2007,).	Heparin	15-22	T cell receptor alpha locus	Homo sapiens	64-67
19748137-9	2010	Unfractionated heparin (UFH) was the major anticoagulant during TRA and TRI (88.76% in 2006 vs. 99.10% in 2007,).	Heparin	24-27	T cell receptor alpha locus	Homo sapiens	64-67
26733269-0	2015	The Anti-Factor Xa Range For Low Molecular Weight Heparin Thromboprophylaxis.	Heparin	50-57	coagulation factor X	Homo sapiens	9-18
26359493-0	2015	Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States.	Heparin	111-118	ribonuclease P/MRP subunit p14	Homo sapiens	64-67
26359493-1	2015	Past studies have suggested that a key feature of the mechanism of heparin allosteric activation of the anticoagulant serpin, antithrombin, is the release of the reactive center loop P14 residue from a native state stabilizing interaction with the hydrophobic core.	Heparin	67-74	ribonuclease P/MRP subunit p14	Homo sapiens	183-186
26359493-4	2015	The variants exhibited basal reactivities with factors Xa and IXa, heparin affinities and thermal stabilities that were dramatically altered from wild type, consistent with the P14 mutations perturbing native state stability and shifting an allosteric equilibrium between native and activated states.	Heparin	67-74	ribonuclease P/MRP subunit p14	Homo sapiens	177-180
26335350-9	2015	Afterwards, an affinity CE method was used to investigate the interactions of two proteins, namely HSA and vitronectin, with three ligands namely enoxaparin sodium, unfractionated heparin, and pentosan polysulfate sodium.	Heparin	180-187	vitronectin	Homo sapiens	107-118
16856890-0	2006	Comparison of the anticoagulant effect of a direct thrombin inhibitor and a low molecular weight heparin in an acquired antithrombin deficiency in children with acute lymphoblastic leukaemia treated with L-asparaginase: an in vitro study.	Heparin	97-104	serpin family C member 1	Homo sapiens	120-132
26581538-4	2015	We report the case of a woman with chronic kidney disease and a high pretest probability for heparin-induced thrombocytopenia who was acutely treated with apixaban, an oral selective factor Xa inhibitor.	Heparin	93-100	coagulation factor X	Homo sapiens	183-192
20623672-4	2010	In the work described here, LBL-produced col/hep coating growth is initialized by deposition of a layer of poly-L-lysine on a titanium surface, which is negatively charged after treatment with NaOH, followed by formation of a multilayer film formed by alternating deposition of negatively charged heparin and positively charged collagen using electrostatic interaction.	Heparin	297-304	DNL-type zinc finger	Homo sapiens	45-48
21060749-6	2010	Thrombolysis In Myocardial Infarction (TIMI) with major bleeding was observed in LMHW and UFH with Gp IIb/IIIa inhibitor (1/219 [0.5%] vs 1/257 [0.4%], P=1.00).	Heparin	90-93	integrin subunit alpha 2b	Homo sapiens	99-105
21060749-7	2010	For patients with STEMI managed with a primary PCI and Gp IIb/IIIa inhibitor, LMWH is more beneficial than UFH.	Heparin	107-110	integrin subunit alpha 2b	Homo sapiens	55-61
16884719-0	2006	Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site.	Heparin	97-104	serpin family C member 1	Homo sapiens	25-37
20628058-1	2010	The activation of antithrombin (AT) by heparin facilitates the exosite-dependent interaction of the serpin with factors IXa (FIXa) and Xa (FXa), thereby improving the rate of reactions by 300- to 500-fold.	Heparin	39-46	coagulation factor X	Homo sapiens	139-142
26116756-9	2015	Additional experiments with multiple cell types indicated that SRI 29365 antiviral activity correlates with the binding of cell surface heparin by full-length G protein.	Heparin	136-143	sorcin	Homo sapiens	63-66
25979342-5	2015	We defined interactions and structural requirements for heparin/HS interactions with VEGF receptor (VEGFR)-1, NRP-1, and VEGF165 in complex with VEGFR-2 and NRP-1.	Heparin	56-63	kinase insert domain receptor	Homo sapiens	145-152
25979342-7	2015	We further show that VEGF165, VEGFR-2, and monomeric NRP-1 bind weakly to heparin alone yet show synergistic binding to heparin when presented together in various combinations.	Heparin	74-81	kinase insert domain receptor	Homo sapiens	30-37
25979342-7	2015	We further show that VEGF165, VEGFR-2, and monomeric NRP-1 bind weakly to heparin alone yet show synergistic binding to heparin when presented together in various combinations.	Heparin	120-127	kinase insert domain receptor	Homo sapiens	30-37
25813285-9	2015	Unfractionated heparin and LMWHs attenuated the TNF-alpha-mediated induction of CXCL8 and enhanced CXCL5, CCL2, and CCL5.	Heparin	15-22	C-X-C motif chemokine ligand 5	Homo sapiens	99-104
20573803-5	2010	In addition, we found that the presence of heparin can markedly inhibit HRG-enhanced necrotic cell clearance by THP-1 cells, possibly by blocking the ability of HRG to interact with necrotic cells as well as THP-1 cells.	Heparin	43-50	histidine rich glycoprotein	Homo sapiens	72-75
20573803-5	2010	In addition, we found that the presence of heparin can markedly inhibit HRG-enhanced necrotic cell clearance by THP-1 cells, possibly by blocking the ability of HRG to interact with necrotic cells as well as THP-1 cells.	Heparin	43-50	histidine rich glycoprotein	Homo sapiens	161-164
16884719-1	2006	We investigate the hypothesis that heparin activates antithrombin (AT) by relieving electrostatic strain within helix D. Mutation of residues K125 and R129 to either Ala or Glu abrogated heparin binding, but did not activate AT towards inhibition of factors IXa or Xa.	Heparin	35-42	serpin family C member 1	Homo sapiens	53-65
20573803-6	2010	Thus, these data suggest that HRG can aid the phagocytosis of necrotic cells via a HS-dependent pathway, and this process can be regulated by the presence of certain HRG ligands, such as heparin.	Heparin	187-194	histidine rich glycoprotein	Homo sapiens	30-33
20573803-6	2010	Thus, these data suggest that HRG can aid the phagocytosis of necrotic cells via a HS-dependent pathway, and this process can be regulated by the presence of certain HRG ligands, such as heparin.	Heparin	187-194	histidine rich glycoprotein	Homo sapiens	166-169
20600001-5	2010	We provide compelling evidence for the involvement of the heparin binding domain of vitronectin in the oligomerization process and show that such oligomerization reinforces the activity of vitronectin in cell adhesion and spreading.	Heparin	58-65	vitronectin	Homo sapiens	84-95
20600001-5	2010	We provide compelling evidence for the involvement of the heparin binding domain of vitronectin in the oligomerization process and show that such oligomerization reinforces the activity of vitronectin in cell adhesion and spreading.	Heparin	58-65	vitronectin	Homo sapiens	189-200
25832311-3	2015	Especially the oral direct FXa and FIIa inhibitors overcome many of the shortcomings of heparins and vitamin K antagonists (VKAs).	Heparin	88-96	coagulation factor X	Homo sapiens	27-30
16735126-6	2006	These data suggest that 2-O and N sulfation of heparin may be of greater importance to CCL2-heparin binding than 6-O sulfation.	Heparin	47-54	C-C motif chemokine ligand 2	Homo sapiens	87-91
25680756-3	2015	When platelet aggregation tests (PATs) were performed with platelet-rich plasma (PRP), a shorter lag time was measured in 131RR donors compared to individuals with the HR and HH genotypes in response to HIT plasma or 5B9, a recently developed humanized monoclonal antibody to PF4/heparin.	Heparin	280-287	olfactory receptor family 5 subfamily B member 1 pseudogene	Homo sapiens	214-220
16720575-9	2006	When taken together, these findings suggest that heparin enhances IL-11-induced STAT3 activation and thus osteoclast formation, by a mechanism that is independent of STAT3 Ser-727 phosphorylation but that involves up-regulation of the MAPK pathway.	Heparin	49-56	interleukin 11	Homo sapiens	66-71
20301214-0	2010	beta-Sheet aggregation of kisspeptin-10 is stimulated by heparin but inhibited by amphiphiles.	Heparin	57-64	KiSS-1 metastasis-suppressor	Mus musculus	26-36
17044598-4	2006	Heparin may have an important role in LPL redistribution, as its concentration in blood cells was declined in all the patients.	Heparin	0-7	lipoprotein lipase	Homo sapiens	38-41
20301214-4	2010	Here we show that heparin induces kisspeptin to form beta-sheet rich amyloid aggregates both at neutral (pH 7.0) and slightly acidic (pH 5.2) conditions.	Heparin	18-25	KiSS-1 metastasis-suppressor	Mus musculus	34-44
20301214-8	2010	Thus kisspeptin can aggregate under physiologically relevant conditions provided heparin is present, but the process is highly sensitive to the presence of amphiphiles, highlighting the very dynamic nature of the peptide conformation and suggesting that kisspeptin aggregation is a biologically regulatable process.	Heparin	81-88	KiSS-1 metastasis-suppressor	Mus musculus	5-15
20432446-3	2010	Here we report the effects of low-concentration (1 microg/ml) heparin on activation of several kinases and subsequent induction of the c-fos gene in mesangial cells in response to the calcium ionophore, ionomycin, in the absence of serum factors.	Heparin	62-69	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	135-140
20432446-6	2010	Our data support a mechanism whereby heparin acts at the cell surface to suppress downstream targets of CaMK-II, including EGFR, leading in turn to a decrease in Erk- (but not c-Src-) dependent induction of c-fos.	Heparin	37-44	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	207-212
25770404-1	2015	OBJECTIVES: This study investigated the relationship between anti-factor Xa (anti-FXa) and activated partial thromboplastin time (aPTT) for monitoring intravenous unfractionated heparin (IV-UFH) in patients with continuous-flow left ventricular assist devices (CF-LVADs).	Heparin	178-185	coagulation factor X	Homo sapiens	82-85
25770404-14	2015	Use of aPTT and anti-FXa to guide heparin therapy may lead to different estimates of heparin concentration in the same patient.	Heparin	34-41	coagulation factor X	Homo sapiens	21-24
25770404-14	2015	Use of aPTT and anti-FXa to guide heparin therapy may lead to different estimates of heparin concentration in the same patient.	Heparin	85-92	coagulation factor X	Homo sapiens	21-24
25595736-3	2015	Here, we showed that induction of PF4/heparin-specific antibodies by PF4/heparin complexes was markedly impaired in mice depleted of CD4 T cells by anti-CD4 antibodies.	Heparin	38-45	CD4 antigen	Mus musculus	133-136
25595736-3	2015	Here, we showed that induction of PF4/heparin-specific antibodies by PF4/heparin complexes was markedly impaired in mice depleted of CD4 T cells by anti-CD4 antibodies.	Heparin	38-45	CD4 antigen	Mus musculus	153-156
25595736-4	2015	Furthermore, Rag1-deficient recipient mice produced PF4/heparin-specific antibodies upon PF4/heparin challenge when reconstituted with a mixture of wild-type splenic B cells and splenocytes from B-cell-deficient (muMT) mice but not splenocytes from T- and B-cell-deficient (Rag1 knockout) mice.	Heparin	56-63	recombination activating 1	Mus musculus	13-17
16809785-7	2006	Electron microscopy studies revealed that MS2 affinity-selected B complexes exhibit a rhombic shape with a maximum dimension of 420 A and are structurally more homogeneous than B complexes treated with heparin.	Heparin	202-209	MS2	Homo sapiens	42-45
25595736-4	2015	Furthermore, Rag1-deficient recipient mice produced PF4/heparin-specific antibodies upon PF4/heparin challenge when reconstituted with a mixture of wild-type splenic B cells and splenocytes from B-cell-deficient (muMT) mice but not splenocytes from T- and B-cell-deficient (Rag1 knockout) mice.	Heparin	93-100	recombination activating 1	Mus musculus	13-17
21567519-4	2010	The [PEG-LMWH/VEGF] hydrogel (PEG = poly(ethylene glycol), LMWH = low molecular weight heparin) correspondingly prompted increases in VEGFR-2 phosphorylation and proliferation of PAE/KDR cells.	Heparin	87-94	kinase insert domain receptor	Homo sapiens	134-141
16709175-6	2006	Here, we summarize the progress made in understanding the interaction between heparin and heparan sulphate and NK1, NK2 and HGF/SF and we discuss their role in HGF/SF-Met signalling.	Heparin	78-85	tachykinin receptor 1	Homo sapiens	111-114
20441964-2	2010	A fluorogenic anti-factor Xa (anti-FXa) assay has been developed for the determination of unfractionated heparin (UFH), low molecular weight heparins (LMWHs), namely enoxaparin and tinzaparin, and the synthetic heparinoid danaparoid, in commercial human pooled plasma.	Heparin	105-112	coagulation factor X	Homo sapiens	35-38
25759505-9	2015	Moreover, heparin was shown to bind to ephrin-B3 and to restrain infection of permissive cells in vitro.	Heparin	10-17	ephrin B3	Homo sapiens	39-48
25489725-0	2015	PAPP-A and IGFBP-4 fragment levels in patients with ST-elevation myocardial infarction treated with heparin and PCI.	Heparin	100-107	insulin like growth factor binding protein 4	Homo sapiens	11-18
20441964-2	2010	A fluorogenic anti-factor Xa (anti-FXa) assay has been developed for the determination of unfractionated heparin (UFH), low molecular weight heparins (LMWHs), namely enoxaparin and tinzaparin, and the synthetic heparinoid danaparoid, in commercial human pooled plasma.	Heparin	114-117	coagulation factor X	Homo sapiens	35-38
16768833-4	2006	Total and heparin-releasable LPL and lipogenic enzyme activities (acetyl-CoA carboxylase (ACC); fatty acid synthase (FAS); glucose-6-phosphate dehydrogenase (G6PDH); and malic enzyme (ME)) were assessed.	Heparin	10-17	lipoprotein lipase	Homo sapiens	29-32
20441964-2	2010	A fluorogenic anti-factor Xa (anti-FXa) assay has been developed for the determination of unfractionated heparin (UFH), low molecular weight heparins (LMWHs), namely enoxaparin and tinzaparin, and the synthetic heparinoid danaparoid, in commercial human pooled plasma.	Heparin	141-149	coagulation factor X	Homo sapiens	35-38
20441964-3	2010	The assay was based on the complexation of heparin-spiked plasmas with exogenous FXa at a concentration of 4nM in the presence of 0.9microM of the fluorogenic substrate methylsulfonyl-D-cyclohexylalanyl-glycyl-arginine-7-amino-4-methylcoumarin acetate (Pefafluor FXa).	Heparin	43-50	coagulation factor X	Homo sapiens	81-84
20441964-3	2010	The assay was based on the complexation of heparin-spiked plasmas with exogenous FXa at a concentration of 4nM in the presence of 0.9microM of the fluorogenic substrate methylsulfonyl-D-cyclohexylalanyl-glycyl-arginine-7-amino-4-methylcoumarin acetate (Pefafluor FXa).	Heparin	43-50	coagulation factor X	Homo sapiens	263-266
20394361-7	2010	We show that R444 provides the most important charge-charge interaction within a C-terminal heparin-binding subsite of CFH approximately 7 whereas side chains of R404, K405, and K388 are the predominant contributors to an N-terminal binding subsite located in the immediate vicinity of residue 402, which is implicated in age-related macular degeneration (AMD).	Heparin	92-99	complement factor H	Homo sapiens	119-122
20093158-0	2010	Efficient revascularization by VEGF administration via heparin-functionalized nanoparticle-fibrin complex.	Heparin	55-62	vascular endothelial growth factor A	Mus musculus	31-35
20093158-1	2010	We investigated the angiogenic bioactivity and therapeutic angiogenic effect of vascular endothelial growth factor (VEGF) administration by the heparin-functionalized nanoparticle-fibrin gel complex.	Heparin	144-151	vascular endothelial growth factor A	Mus musculus	80-114
20093158-1	2010	We investigated the angiogenic bioactivity and therapeutic angiogenic effect of vascular endothelial growth factor (VEGF) administration by the heparin-functionalized nanoparticle-fibrin gel complex.	Heparin	144-151	vascular endothelial growth factor A	Mus musculus	116-120
25562836-6	2015	Heparin blocked the binding of HMGB1 to the surface of macrophages, and suppressed the phosphorylation of p38 and ERK1/2, but not JNK; TNF-alpha secretion was also decreased.	Heparin	0-7	mitogen-activated protein kinase 8	Mus musculus	130-133
25723475-0	2015	Low molecular weight heparin (LMWH) improves peritoneal function and inhibits peritoneal fibrosis possibly through suppression of HIF-1alpha, VEGF and TGF-beta1.	Heparin	21-28	hypoxia inducible factor 1 subunit alpha	Rattus norvegicus	130-140
25462840-6	2015	Finally, vascular endothelial growth factor (VEGF) was incorporated into the gelatin derivative by binding with the heparin in the gelatin derivative, and an injectable gel with controlled VEGF release was formed by an enzymatic catalytic reaction with hydrogen peroxide (H2O2) and horseradish peroxidase (HRP).	Heparin	116-123	vascular endothelial growth factor A	Mus musculus	9-43
25462840-6	2015	Finally, vascular endothelial growth factor (VEGF) was incorporated into the gelatin derivative by binding with the heparin in the gelatin derivative, and an injectable gel with controlled VEGF release was formed by an enzymatic catalytic reaction with hydrogen peroxide (H2O2) and horseradish peroxidase (HRP).	Heparin	116-123	vascular endothelial growth factor A	Mus musculus	45-49
25462840-8	2015	Binding VEGF to heparin stabilizes this growth factor, protects it from denaturation and proteolytic degradation and subsequently prolongs the sustained release.	Heparin	16-23	vascular endothelial growth factor A	Mus musculus	8-12
25462840-12	2015	Deeper and denser cell infiltration and angiogenesis in the heparin-modified gelatin/VEGF gels were observed compared to the controls after being subcutaneously injected in the dorsal side of the mice for 2 weeks.	Heparin	60-67	vascular endothelial growth factor A	Mus musculus	85-89
25453957-0	2015	LHT7, a chemically modified heparin, inhibits multiple stages of angiogenesis by blocking VEGF, FGF2 and PDGF-B signaling pathways.	Heparin	28-35	platelet derived growth factor subunit B	Homo sapiens	105-111
20093158-4	2010	These results show the enhanced angiogenic potential of VEGF administration by the proposed heparin-functionalized nanoparticle-fibrin gel complex.	Heparin	92-99	vascular endothelial growth factor A	Mus musculus	56-60
25130770-7	2015	We further showed that HCII could up-regulate cancer cell migration through the activation of PI3K, which acts upstream of Rac1 and Cdc42, and this effect could be blocked by heparin.	Heparin	175-182	Rac family small GTPase 1	Homo sapiens	123-127
16500040-6	2006	The results indicate that the MUC1 SEA domain originated from heparin sulfate proteoglycan of basement membrane (HSPG2; perlecan), an inducer of tumor cell growth.	Heparin	62-69	heparan sulfate proteoglycan 2	Homo sapiens	113-118
20402553-7	2010	TAKE HOME MESSAGE: Oral administration, predictable anticoagulant responses, low potential for drug-drug interactions and first published clinical data render direct thrombin and factor Xa inhibitors good candidates to replace oral vitamin K antagonist and low molecular weight heparins for DVT treatment.	Heparin	278-286	coagulation factor X	Homo sapiens	179-188
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	32-39	C-X-C motif chemokine receptor 4	Rattus norvegicus	75-80
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	32-39	C-X-C motif chemokine receptor 4	Rattus norvegicus	116-121
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	187-194	C-X-C motif chemokine receptor 4	Rattus norvegicus	75-80
25353308-1	2015	BACKGROUND: Histidine-rich glycoprotein (HRG) regulates coagulation through its ability to bind and neutralize heparins.	Heparin	111-119	histidine rich glycoprotein	Homo sapiens	12-39
20201787-5	2010	We also found that butanoylated heparin significantly inhibited CXCL12 and CXCR4 expression, suggesting that CXCL12/CXCR4 axis may be involved in regulation of tumor growth inhibition by heparin.	Heparin	187-194	C-X-C motif chemokine receptor 4	Rattus norvegicus	116-121
25353308-1	2015	BACKGROUND: Histidine-rich glycoprotein (HRG) regulates coagulation through its ability to bind and neutralize heparins.	Heparin	111-119	histidine rich glycoprotein	Homo sapiens	41-44
16517611-0	2006	Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.	Heparin	125-132	serpin family C member 1	Homo sapiens	58-70
25353308-2	2015	HRG associates with Zn(2+) to stimulate HRG-heparin complex formation.	Heparin	44-51	histidine rich glycoprotein	Homo sapiens	0-3
25353308-2	2015	HRG associates with Zn(2+) to stimulate HRG-heparin complex formation.	Heparin	44-51	histidine rich glycoprotein	Homo sapiens	40-43
25353308-9	2015	Also Zn(2+) binding was shown to increase the affinity with which HRG interacts with unfractionated heparins, but had no effect on its interaction with low molecular weight heparin (~ 6850 Da).	Heparin	100-108	histidine rich glycoprotein	Homo sapiens	66-69
25353308-9	2015	Also Zn(2+) binding was shown to increase the affinity with which HRG interacts with unfractionated heparins, but had no effect on its interaction with low molecular weight heparin (~ 6850 Da).	Heparin	100-107	histidine rich glycoprotein	Homo sapiens	66-69
20215909-2	2010	Heparin exerts its major effect via antithrombin, converting antithrombin to a more efficient inhibitor of circulating thrombin (factor IIa), factor Xa, factor IXa, factor XIIa, and kallikrein.	Heparin	0-7	kallikrein related peptidase 4	Homo sapiens	119-192
16517611-1	2006	We previously showed that conformational activation of the anticoagulant serpin, antithrombin, by heparin generates new exosites in strand 3 of beta-sheet C, which promote the reaction of the inhibitor with the target proteases, factor Xa and factor IXa.	Heparin	98-105	serpin family C member 1	Homo sapiens	81-93
19642141-7	2010	Furthermore, we observed that Huh7 cell migration and invasion induced by the chemokine are strongly inhibited by heparin, by beta-D-xyloside treatment of cells and by anti-syndecan-1 and -4 antibodies.	Heparin	114-121	MIR7-3 host gene	Homo sapiens	30-34
19906646-0	2010	Structural characterization of the E2 domain of APL-1, a Caenorhabditis elegans homolog of human amyloid precursor protein, and its heparin binding site.	Heparin	132-139	Amyloid-beta-like protein	Caenorhabditis elegans	48-53
19928997-3	2010	Adhesion of HaCaT cells to dermatopontin was inhibited by both EDTA and heparin and was mediated in part by alpha3beta1 integrin.	Heparin	72-79	dermatopontin	Homo sapiens	27-40
25447524-4	2014	Furthermore, DNA and heparin compete for binding to ficolin-2.	Heparin	21-28	ficolin 2	Homo sapiens	52-61
25389143-6	2014	In the mixed treatment comparison models, when compared with unfractionated heparin plus GpIIb/IIIa inhibitor, unfractionated heparin was associated with a higher risk of major adverse cardiovascular events (relative risk 1.49 (95% confidence interval 1.21 to 1.84), as were bivalirudin (relative risk 1.34 (1.01 to 1.78)) and fondaparinux (1.78 (1.01 to 3.14)).	Heparin	126-133	integrin subunit alpha 2b	Homo sapiens	89-94
16619025-0	2006	Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation.	Heparin	29-36	serpin family C member 1	Homo sapiens	0-12
25377080-1	2014	The factor Xa inhibitor apixaban is one of the novel anticoagulants to emerge as alternatives to long-standing standards of care that include low-molecular-weight heparin and warfarin.	Heparin	163-170	coagulation factor X	Homo sapiens	4-13
20686243-1	2010	Plasma hyaluronan-binding protein (PHBP), a serine protease that can activate coagulation factor VII and prourokinase, circulates as a single-chain form (pro-PHBP), and is autoproteolytically converted to an active two-chain form with the aid of an effector such as spermidine and heparin.	Heparin	281-288	hyaluronan binding protein 2	Homo sapiens	0-33
20686243-1	2010	Plasma hyaluronan-binding protein (PHBP), a serine protease that can activate coagulation factor VII and prourokinase, circulates as a single-chain form (pro-PHBP), and is autoproteolytically converted to an active two-chain form with the aid of an effector such as spermidine and heparin.	Heparin	281-288	hyaluronan binding protein 2	Homo sapiens	35-39
16619025-0	2006	Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation.	Heparin	29-36	serpin family C member 1	Homo sapiens	83-95
19940766-12	2010	Coincidently, the expression of MMP-2 in the atherosclerotic lesions in the heparin group was 49.3% lower than that in the control group (P&lt;0.001).	Heparin	76-83	matrix metallopeptidase 2	Mus musculus	32-37
16619025-2	2006	One of the principal regulatory mechanisms involves heparin activation of the serpin antithrombin (AT).	Heparin	52-59	serpin family C member 1	Homo sapiens	85-97
19940766-13	2010	CONCLUSION: Heparin can inhibit the production of MMP-2 in the atherosclerotic lesions and improve the atherosclerotic lesions in LDLr(-/-) mice.	Heparin	12-19	matrix metallopeptidase 2	Mus musculus	50-55
25115442-9	2014	The heparin-binding domain of GEP was mapped to RRH(555-557) in the C-terminal region.	Heparin	4-11	retinal pigment epithelium-derived rhodopsin homolog	Homo sapiens	48-51
16711739-2	2006	Only the twisted boat conformation allowed the biologically active pentasaccharide unit of heparin (DEFGH) to bind to antithrombin.	Heparin	91-98	serpin family C member 1	Homo sapiens	118-130
25176127-5	2014	The sulfation pattern was crucial for these activities because monosulfated or truncated heparin had a reduced ability to bind to TIMP-3 and increase its affinity for ADAMTS-5.	Heparin	89-96	TIMP metallopeptidase inhibitor 3	Homo sapiens	130-136
25176127-5	2014	The sulfation pattern was crucial for these activities because monosulfated or truncated heparin had a reduced ability to bind to TIMP-3 and increase its affinity for ADAMTS-5.	Heparin	89-96	ADAM metallopeptidase with thrombospondin type 1 motif 5	Homo sapiens	167-175
19940766-13	2010	CONCLUSION: Heparin can inhibit the production of MMP-2 in the atherosclerotic lesions and improve the atherosclerotic lesions in LDLr(-/-) mice.	Heparin	12-19	low density lipoprotein receptor	Mus musculus	130-134
19819167-11	2010	CONCLUSIONS: This series demonstrates that short-term re-exposure to heparin during urgent CPB for heart transplantation or MCSD placement is safe despite the presence of thrombocytopenia and Hep/PF4 antibodies.	Heparin	69-76	DNL-type zinc finger	Homo sapiens	192-195
16676077-5	2006	In patients with no concomitant heparin, 28-day mortality was lower with antithrombin than with placebo (37.8% vs. 43.6%; absolute reduction: 5.8%; risk ratio: 0.860 [0.725-1.019]), which increased until day-90 (44.9% vs. 52.5%; absolute reduction: 7.6%; risk ratio: 0.851 [0.735-0.987]).	Heparin	32-39	serpin family C member 1	Homo sapiens	73-85
19909247-3	2009	Heparin-binding VEGF-A isoforms are critical for survival: mice engineered to express exclusively the non-heparin-binding VEGF(120) have diminished vascular branching during embryonic development and die from postnatal angiogenesis defects shortly after birth.	Heparin	106-113	vascular endothelial growth factor A	Mus musculus	16-22
19909247-3	2009	Heparin-binding VEGF-A isoforms are critical for survival: mice engineered to express exclusively the non-heparin-binding VEGF(120) have diminished vascular branching during embryonic development and die from postnatal angiogenesis defects shortly after birth.	Heparin	106-113	vascular endothelial growth factor A	Mus musculus	16-20
25259688-6	2014	Also, migration studies were performed in matrigel cultures, where oligodendrocyte progenitor cells were placed at a certain distance of a FGF8-soaked heparin bead.	Heparin	151-158	fibroblast growth factor 8	Mus musculus	139-143
16676077-10	2006	In the treatment of severe sepsis, high-dose antithrombin may sufficiently protect against development of venous thromboembolism when no concomitant heparin is given.	Heparin	149-156	serpin family C member 1	Homo sapiens	45-57
25259688-8	2014	Furthermore, a similar effect was observed in an in vivo demyelinating mouse model, where oligodendrocyte progenitor cells were observed migrating towards the FGF8-soaked heparin beads where they were grafted.	Heparin	171-178	fibroblast growth factor 8	Mus musculus	159-163
19967150-7	2009	We show that sulfated galactan interacts with the heparin-binding exosite of FXa and Arg-236 and Lys-240 of this site are critical residues for this interaction, as observed for heparin.	Heparin	50-57	coagulation factor X	Homo sapiens	77-80
19967150-7	2009	We show that sulfated galactan interacts with the heparin-binding exosite of FXa and Arg-236 and Lys-240 of this site are critical residues for this interaction, as observed for heparin.	Heparin	178-185	coagulation factor X	Homo sapiens	77-80
19967150-8	2009	Thus, sulfated galactan and heparin have similar high-affinity and specificity for interaction with FXa, though they have differences in their chemical structures.	Heparin	28-35	coagulation factor X	Homo sapiens	100-103
16314835-5	2006	These fragments also inhibited Erk1/2 kinase activation induced by soluble heparin-binding EGF and AR.	Heparin	75-82	epidermal growth factor	Mus musculus	91-94
19786011-0	2009	Histidine-rich glycoprotein inhibited high mobility group box 1 in complex with heparin-induced angiogenesis in matrigel plug assay.	Heparin	80-87	histidine rich glycoprotein	Homo sapiens	0-27
19786011-3	2009	Additionally, we reported that high mobility group box 1 (HMGB1) in complex with heparin induces angiogenesis; therefore, we examined the effect of HRG on heparin-dependent HMGB1-induced angiogenesis in the present study.	Heparin	155-162	histidine rich glycoprotein	Homo sapiens	148-151
19786011-4	2009	HRG completely inhibited angiogenesis induced by HMGB1 in complex with heparin.	Heparin	71-78	histidine rich glycoprotein	Homo sapiens	0-3
19786011-5	2009	HRG inhibited the diffusion of a complex of HMGB1 with heparin from matrigel into surrounding tissue.	Heparin	55-62	histidine rich glycoprotein	Homo sapiens	0-3
19786011-6	2009	HRG also competed with HMGB1 for heparin binding in vitro.	Heparin	33-40	histidine rich glycoprotein	Homo sapiens	0-3
19786011-8	2009	These results strongly suggested that HRG might be an inhibitor of angiogenesis induced by growth factors with heparin binding activity and that HRG may be a potential drug for angiogenic diseases, including tumor growth.	Heparin	111-118	histidine rich glycoprotein	Homo sapiens	38-41
19933047-0	2009	Heparin and suramin alter plitidepsin uptake via inhibition of GPCR coupled signaling.	Heparin	0-7	vomeronasal 1 receptor 17 pseudogene	Homo sapiens	63-67
19933047-6	2009	Further work showed that plitidepsin binds to G-Protein Coupled Receptors (GPCRs), since GPCR and GRK (GPCR kinases) inhibitors suramin and heparin respectively, markedly reduce the drug uptake and its cytotoxic activity.	Heparin	140-147	vomeronasal 1 receptor 17 pseudogene	Homo sapiens	75-79
19933047-6	2009	Further work showed that plitidepsin binds to G-Protein Coupled Receptors (GPCRs), since GPCR and GRK (GPCR kinases) inhibitors suramin and heparin respectively, markedly reduce the drug uptake and its cytotoxic activity.	Heparin	140-147	vomeronasal 1 receptor 17 pseudogene	Homo sapiens	89-93
25003700-4	2014	Kallikrein is also activated by the presence of an oversulfated contaminant recently found in preparations of the drug heparin.	Heparin	119-126	kallikrein related peptidase 4	Homo sapiens	0-10
24583690-1	2014	This study presents the development of a simple, label-free, sensitive, and selective detection system for heparin based on the use of a complex of 20-repeat adenosine (A20) and coralyne.	Heparin	107-114	immunoglobulin kappa variable 1-27	Homo sapiens	169-172
24583690-5	2014	The presence of heparin and the formation of the coralyne-heparin complex caused coralyne to be removed from the A20-corlayne complex.	Heparin	16-23	immunoglobulin kappa variable 1-27	Homo sapiens	113-116
24583690-5	2014	The presence of heparin and the formation of the coralyne-heparin complex caused coralyne to be removed from the A20-corlayne complex.	Heparin	58-65	immunoglobulin kappa variable 1-27	Homo sapiens	113-116
24583690-8	2014	Under optimal conditions (5 muM coralyne, 1 muM poly A20, and 10mM HEPES), this probe exhibited high selectivity (&gt;90-fold) toward heparin over hyaluronic acid and chondroitin sulfate.	Heparin	134-141	immunoglobulin kappa variable 1-27	Homo sapiens	53-56
24719423-6	2014	However, IGF2BP1 binding was also inhibited by high concentrations of heparin, suggesting that it bound the bait nonspecifically.	Heparin	70-77	insulin like growth factor 2 mRNA binding protein 1	Homo sapiens	9-16
16556679-7	2006	We demonstrate that heparin, like epidermal growth factor (EGF) and heparin-binding EGF (HB-EGF), elicits phosphorylation of the EGF receptor and activation of the phosphatidyl inositol 3-kinase (PI3K)-, the extracellular signal-related kinase 1/2 (ERK1/2)- and the c-Jun NH2 terminal kinase (JNK)-signal transduction pathways in primary villous trophoblast.	Heparin	20-27	heparin binding EGF like growth factor	Homo sapiens	68-87
16556679-7	2006	We demonstrate that heparin, like epidermal growth factor (EGF) and heparin-binding EGF (HB-EGF), elicits phosphorylation of the EGF receptor and activation of the phosphatidyl inositol 3-kinase (PI3K)-, the extracellular signal-related kinase 1/2 (ERK1/2)- and the c-Jun NH2 terminal kinase (JNK)-signal transduction pathways in primary villous trophoblast.	Heparin	20-27	heparin binding EGF like growth factor	Homo sapiens	89-95
19700767-4	2009	Two other family members, PRELP and chondroadherin, have distinctly different clusters of basic amino acids in their N and C termini, respectively, and PRELP is known to bind to heparin via this domain.	Heparin	178-185	proline and arginine rich end leucine rich repeat protein	Homo sapiens	152-157
16373616-2	2006	This is mainly because of the need for cumbersome heparin injections, which are necessary for LPL measurements.	Heparin	50-57	lipoprotein lipase	Homo sapiens	94-97
24816808-10	2014	Heparin/NAH (10 mg/kg) improved the lethality rate, blood gas, MPO activity, lung edema and pathological score.	Heparin	0-7	myeloperoxidase	Mus musculus	63-66
16470783-2	2006	In the course of optimizing CE separation conditions for FBP purified from cow"s milk we discovered a novel specific heparin-binding activity of FBP by affinity CE.	Heparin	117-124	folate receptor alpha	Bos taurus	57-60
19549924-5	2009	A sequence motif in SAA responsible for this conversion was identified that contains a pH-sensitive heparin/HS-binding site, functions as a ligand for a cell surface receptor, and acts as a structural focal point for SAA aggregation.	Heparin	100-107	serum amyloid A1 cluster	Homo sapiens	20-23
19549924-5	2009	A sequence motif in SAA responsible for this conversion was identified that contains a pH-sensitive heparin/HS-binding site, functions as a ligand for a cell surface receptor, and acts as a structural focal point for SAA aggregation.	Heparin	100-107	serum amyloid A1 cluster	Homo sapiens	217-220
16470783-2	2006	In the course of optimizing CE separation conditions for FBP purified from cow"s milk we discovered a novel specific heparin-binding activity of FBP by affinity CE.	Heparin	117-124	folate receptor alpha	Bos taurus	145-148
19664058-4	2009	FSAP is activated by an auto-catalytic mechanism, which is amplified by heparin.	Heparin	72-79	hyaluronan binding protein 2	Homo sapiens	0-4
24730525-2	2014	Fgf10 mediates biological responses by activating Fgf receptor 2b (Fgfr2b) with heparin/heparan sulfate in a paracrine manner.	Heparin	80-87	fibroblast growth factor 10	Mus musculus	0-5
16470783-4	2006	Prior complexation of FBP with folate abolished heparin binding, and thus folate competes with heparin for binding to FBP.	Heparin	48-55	folate receptor alpha	Bos taurus	22-25
24357546-5	2014	Heparin increased gene expression of chain initiation and modification enzymes including EXT1 and NDST1, as well as core proteins SDC2 and GPC6.	Heparin	0-7	syndecan 2	Homo sapiens	130-134
19664058-6	2009	Heparin was effective in binding to and activating FSAP in a size- and charge density-dependent manner.	Heparin	0-7	hyaluronan binding protein 2	Homo sapiens	51-55
19664058-7	2009	Polyphosphate was more potent than heparin with regard to its interactions with FSAP.	Heparin	35-42	hyaluronan binding protein 2	Homo sapiens	80-84
16470783-4	2006	Prior complexation of FBP with folate abolished heparin binding, and thus folate competes with heparin for binding to FBP.	Heparin	48-55	folate receptor alpha	Bos taurus	118-121
19664058-8	2009	Heparin was also an effective co-factor for inhibition of FSAP by plasminogen activator inhibitor 1 (PAI-1) and antithrombin, whereas polyphosphate served as co-factor for the inhibition of FSAP by PAI-1 only.	Heparin	0-7	hyaluronan binding protein 2	Homo sapiens	58-62
16470783-4	2006	Prior complexation of FBP with folate abolished heparin binding, and thus folate competes with heparin for binding to FBP.	Heparin	95-102	folate receptor alpha	Bos taurus	22-25
16470783-4	2006	Prior complexation of FBP with folate abolished heparin binding, and thus folate competes with heparin for binding to FBP.	Heparin	95-102	folate receptor alpha	Bos taurus	118-121
19727205-9	2009	These results suggested that heparin"s anti-inflammatory effects can be partly explained by its blocking of the interaction between HMGB1 or S100A12 and RAGE.	Heparin	29-36	advanced glycosylation end-product specific receptor	Homo sapiens	153-157
19727205-10	2009	On the other hand, heparin would be a promising effective remedy against RAGE-related inflammatory disorders.	Heparin	19-26	advanced glycosylation end-product specific receptor	Homo sapiens	73-77
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	15-22	coagulation factor X	Homo sapiens	89-98
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	15-22	coagulation factor X	Homo sapiens	100-103
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	24-27	coagulation factor X	Homo sapiens	89-98
24650612-3	2014	Nowadays, four new inhibitors of factor Xa are used orally (rivaroxaban, apixaban, edoxaban, betrixaban), and they are at least as efficient as heparins and vitamin K antagonists.	Heparin	144-152	coagulation factor X	Homo sapiens	33-42
24650612-4	2014	The objective is to substitute these indirect inhibitors of factor Xa (heparins, low molecular weight heparins and fondaparinux) in the prevention of venous and arterial thromboembolic episodes.	Heparin	71-79	coagulation factor X	Homo sapiens	60-69
24650612-4	2014	The objective is to substitute these indirect inhibitors of factor Xa (heparins, low molecular weight heparins and fondaparinux) in the prevention of venous and arterial thromboembolic episodes.	Heparin	102-110	coagulation factor X	Homo sapiens	60-69
24832898-6	2014	In the presence of heparin, a well-known activator of FGF signaling, cystic morphology with lumen expansion was observed in cultures containing FGF1, FGF7, or FGF10, but growth arrest was observed in cultures containing FGF2 or FGF9.	Heparin	19-26	fibroblast growth factor 10	Mus musculus	159-164
19543696-1	2009	Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa).	Heparin	24-27	coagulation factor X	Homo sapiens	100-103
19543696-2	2009	Low molecular weight heparins (LMWH) primarily enhance AT inhibition of FXa.	Heparin	21-29	coagulation factor X	Homo sapiens	72-75
24482188-0	2014	Antitumor effects of heparin-polyethyleneimine nanogels delivering claudin-3-targeted short hairpin RNA combined with low-dose cisplatin on ovarian cancer.	Heparin	21-28	claudin 3	Mus musculus	67-76
16475811-2	2006	Previously, we have identified the proteases that generate the amyloidogenic fragments from the full-length gelsolin variants and demonstrated that heparin is capable of accelerating gelsolin amyloidogenesis.	Heparin	148-155	gelsolin	Homo sapiens	108-116
18996625-1	2009	Antithrombin, a plasma glycoprotein serpin, requires conformational activation by heparin to induce an anticoagulant effect, which is mediated through accelerated factor Xa inhibition.	Heparin	82-89	coagulation factor X	Homo sapiens	163-172
16475811-2	2006	Previously, we have identified the proteases that generate the amyloidogenic fragments from the full-length gelsolin variants and demonstrated that heparin is capable of accelerating gelsolin amyloidogenesis.	Heparin	148-155	gelsolin	Homo sapiens	183-191
18996625-4	2009	A tetrahydroisoquinoline-based scaffold was designed to mimic four critical anionic groups of the key trisaccharide DEF constituting the sequence-specific pentasaccharide DEFGH in heparin.	Heparin	180-187	UTP25 small subunit processome component	Homo sapiens	116-119
24744754-9	2014	The bivalent interaction of CFH-heparin was observed by ultracentrifugation, and binding studies of CFH fragments with heparin-coated sensor chips.	Heparin	32-39	complement factor H	Homo sapiens	28-31
16475811-3	2006	Herein, we identify the structural features of heparin that promote the 8 kDa disease-associated gelsolin fragments (residues 173-243) generated at the cell surface to form amyloid.	Heparin	47-54	gelsolin	Homo sapiens	97-105
16475811-4	2006	In conjunction with electron microscopy analyses, our kinetic studies demonstrate that heparin efficiently accelerates the formation of gelsolin amyloid by enabling intermolecular beta-sheet formation.	Heparin	87-94	gelsolin	Homo sapiens	136-144
24625558-13	2014	The Gpm1 vitronectin interaction is inhibited by heparin and the interaction is also ionic strength dependent.	Heparin	49-56	vitronectin	Homo sapiens	9-20
19343519-4	2009	Association rate constants k (on) for the interaction of carp and rainbow trout AT III with bovine trypsin and thrombin were about 1.3 x 10(4)-7.9 x 10(5) M(-1) s(-1) without and &gt;10(7) M(-1) s(-1) in presence of heparin; so antithrombins require the presence of heparin to become effective proteinase inhibitors.	Heparin	216-223	coagulation factor II, thrombin	Bos taurus	111-119
16223363-4	2006	In the present study, we demonstrate that, in the FGF (fibroblast growth factor)-FGFR (FGF receptor) system, multimers of the minimal complex composed of two FGF1 and two FGFR2 protomers can form on a single chain of the co-receptor heparin.	Heparin	233-240	fibroblast growth factor receptor 2	Homo sapiens	171-176
19343519-4	2009	Association rate constants k (on) for the interaction of carp and rainbow trout AT III with bovine trypsin and thrombin were about 1.3 x 10(4)-7.9 x 10(5) M(-1) s(-1) without and &gt;10(7) M(-1) s(-1) in presence of heparin; so antithrombins require the presence of heparin to become effective proteinase inhibitors.	Heparin	266-273	coagulation factor II, thrombin	Bos taurus	111-119
24398330-0	2014	Glycol-split nonanticoagulant heparins are inhibitors of hepcidin expression in vitro and in vivo.	Heparin	30-38	hepcidin antimicrobial peptide	Mus musculus	57-65
24398330-2	2014	We previously reported that heparins are efficient hepcidin inhibitors both in vitro and in vivo, but their anticoagulant activity limits therapeutic use.	Heparin	28-36	hepcidin antimicrobial peptide	Mus musculus	51-59
19375502-8	2009	Heparin prevented both extracellular matrix association and cell surface binding of MMP-28 suggesting that both are via heparan sulphate proteoglycans.	Heparin	0-7	matrix metallopeptidase 28	Homo sapiens	84-90
24406213-4	2014	This microsphere delivery system is based on the formation of a heparin-BMP-7 nanocomplex, first coated with Tetronic( ) and further entrapped in a biodegradable polyester matrix.	Heparin	64-71	bone morphogenetic protein 7	Homo sapiens	72-77
16223363-7	2006	However, the doublet of complexes appears to be less co-operative than the formation of the 2:2:1 FGF1:FGFR2:heparin complex, suggesting that this mechanism is one of a number of weaker interactions that might be involved in the formation of a focal complex on the cell surface.	Heparin	109-116	fibroblast growth factor receptor 2	Homo sapiens	103-108
19195682-1	2009	Low-molecular-weight heparins (LMWH) exert their anticoagulant effect by accelerating anti-thrombin (AT) inactivation of factor Xa (fXa) and thrombin.	Heparin	21-29	coagulation factor X	Homo sapiens	121-130
16233946-1	2006	Heparin binding to human low density lipoproteins (LDL) and the effect of heparin on the ability of LDL to bind to the LDL receptor has been investigated.	Heparin	74-81	low density lipoprotein receptor	Homo sapiens	119-131
19195682-1	2009	Low-molecular-weight heparins (LMWH) exert their anticoagulant effect by accelerating anti-thrombin (AT) inactivation of factor Xa (fXa) and thrombin.	Heparin	21-29	coagulation factor X	Homo sapiens	132-135
19166810-5	2009	Here, we show that the protease in charge of the N-t cleavage of Reelin requires the activity of certain proprotein convertase family for maturation and has strong affinity for heparin.	Heparin	177-184	reelin	Homo sapiens	65-71
18358478-11	2008	CONCLUSIONS: The pro-thrombotic phenotype of CRPtg mice was suppressed by aspirin/heparin, revealing CRP"s influence on neointimal growth after trans-femoral arterial wire-injury.	Heparin	82-89	C-reactive protein, pentraxin-related	Mus musculus	45-48
24333628-2	2014	Here, we describe the development of apical sodium-dependent bile acid transporter (ASBT)-targeted high-affinity oligomeric bile acid substrates that mediate the transmembrane transport of low molecular weight heparin (LMWH).	Heparin	210-217	solute carrier family 10 member 2	Rattus norvegicus	37-82
24333628-2	2014	Here, we describe the development of apical sodium-dependent bile acid transporter (ASBT)-targeted high-affinity oligomeric bile acid substrates that mediate the transmembrane transport of low molecular weight heparin (LMWH).	Heparin	210-217	solute carrier family 10 member 2	Rattus norvegicus	84-88
24240869-3	2014	Our results show that delivery of triglycerides and nonesterified fatty acids by infusion of Intralipid + heparin (IH) for 8 h increased the amplitude of INa by 43% and shifted its activation threshold by -5 mV, closer to the resting membrane potential.	Heparin	106-113	internexin neuronal intermediate filament protein alpha	Canis lupus familiaris	154-157
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	coagulation factor XII	Homo sapiens	82-86
16233946-8	2006	Furthermore, the presence of heparin inhibits LDL binding to the intact LDL receptor that might have consequences on the cholesterol metabolism in vivo.	Heparin	29-36	low density lipoprotein receptor	Homo sapiens	72-84
24266905-8	2014	The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p &lt; 0.0001 for F1+2 ).	Heparin	4-11	coagulation factor XII	Homo sapiens	196-200
16325769-8	2006	Finally, a FTDP-17 mutation was identified that could complement heparin to generate assembly kinetics similar to that of wild-type tau with both inducers.	Heparin	65-72	microtubule associated protein tau	Homo sapiens	11-18
24349317-0	2013	Functional characterization of ECP-heparin interaction: a novel molecular model.	Heparin	35-42	ribonuclease A family member 3	Homo sapiens	31-34
24349317-6	2013	To validate our prediction, mutant ECPs including ECP Q40A, H64A, R105A, and double mutant ECP Q40A/H64A were generated, and their binding affinity for heparins were measured by isothermal titration calorimetry (ITC).	Heparin	152-160	ribonuclease A family member 3	Homo sapiens	35-38
24349317-7	2013	Weaker binding of ECP Q40A/H64A of all heparin variants suggested that Gln(40)-His(64) clamp contributed to ECP-heparin interaction significantly.	Heparin	39-46	ribonuclease A family member 3	Homo sapiens	18-21
18835720-2	2008	Besides reducing significantly (p&lt;0.001) the influx of inflammatory cells to injury site in a model of acute inflammation, shrimp heparin-like compound was able to reduce the matrix metalloproteinase (MMPs) activity in the peritoneal lavage of inflamed animals.	Heparin	133-140	matrix metallopeptidase 9	Homo sapiens	204-208
18669635-6	2008	Heparin disrupted tropoelastin binding but did not disrupt N- and C-terminal fibrillin-1 interactions.	Heparin	0-7	elastin	Homo sapiens	18-30
18593710-4	2008	The objective of this study was to locate the heparin binding site of ECP by site-directed mutagenesis and construction of a synthetic peptide derived from this region.	Heparin	46-53	ribonuclease A family member 3	Homo sapiens	70-73
18593710-5	2008	Synthetic heparin with &gt; or =5 monosaccharide units showed strong inhibition of ECP binding to the cell surface.	Heparin	10-17	ribonuclease A family member 3	Homo sapiens	83-86
18593710-6	2008	Analysis of ECP mt1 (R34A/W35A/R36A/K38A) showed that these charged and aromatic residues were involved in ECP binding to heparin and the cell surface.	Heparin	122-129	ribonuclease A family member 3	Homo sapiens	12-15
18593710-6	2008	Analysis of ECP mt1 (R34A/W35A/R36A/K38A) showed that these charged and aromatic residues were involved in ECP binding to heparin and the cell surface.	Heparin	122-129	ribonuclease A family member 3	Homo sapiens	107-110
18593710-10	2008	Thus, the tight interaction between ECP and heparin acts as the primary step for ECP endocytosis.	Heparin	44-51	ribonuclease A family member 3	Homo sapiens	81-84
24349317-7	2013	Weaker binding of ECP Q40A/H64A of all heparin variants suggested that Gln(40)-His(64) clamp contributed to ECP-heparin interaction significantly.	Heparin	39-46	ribonuclease A family member 3	Homo sapiens	108-111
24349317-8	2013	Our in silico and in vitro data together demonstrate that ECP uses not only major heparin binding region but also use other surrounding residues to interact with heparin.	Heparin	82-89	ribonuclease A family member 3	Homo sapiens	58-61
24349317-8	2013	Our in silico and in vitro data together demonstrate that ECP uses not only major heparin binding region but also use other surrounding residues to interact with heparin.	Heparin	162-169	ribonuclease A family member 3	Homo sapiens	58-61
18449906-5	2008	Interestingly, heparin induces glycogen synthase kinase-3beta (GSK-3beta) inhibition, beta-catenin stabilization and morphological differentiation in both N2a cells and in rat primary hippocampal neuronal cultures.	Heparin	15-22	catenin (cadherin associated protein), beta 1	Mus musculus	86-98
16417632-7	2006	RESULTS: Our results show that the binding of VEGF, FGF-1, and certain chemokines (SDF-1 and SLC) to immobilized heparin was abolished or greatly diminished by pre-treating the heparin with HSulf-2.	Heparin	177-184	sulfatase 2	Homo sapiens	190-197
18449906-6	2008	We also show that heparin modulates Wnt-3a-induced stabilization of beta-catenin.	Heparin	18-25	catenin (cadherin associated protein), beta 1	Mus musculus	68-80
16417632-8	2006	Furthermore, HSulf-2 released these soluble proteins from their association with heparin.	Heparin	81-88	sulfatase 2	Homo sapiens	13-20
16417632-10	2006	CONCLUSION: Our results validate Sulf-2 as a new tool for deciphering the sulfation requirements in the interaction of protein ligands with heparin/HSPGs and expand the range of potential biological activities of this enzyme.	Heparin	140-147	sulfatase 2	Homo sapiens	33-39
16139336-6	2006	RESULTS: Compared with those treated with bivalirudin, patients treated with UFH+E exhibited a 45% decrease in the capacity of platelets to bind fibrinogen (p=0.006) but a 2-fold increase in platelet surface expression of P-selectin (p=0.04) in samples taken from the coronary ostium before PCI.	Heparin	77-80	selectin P	Homo sapiens	222-232
18766266-7	2008	Thrombin that was pre-incubated with heparin also failed to induced Ca(2+) transients in BAECs.	Heparin	37-44	coagulation factor II, thrombin	Bos taurus	0-8
23981772-0	2013	The heparin-binding domains of IGFBP-2 mediate its inhibitory effect on preadipocyte differentiation and fat development in male mice.	Heparin	4-11	insulin-like growth factor binding protein 2	Mus musculus	31-38
23981772-3	2013	IGFBP-2 contains 2 heparin-binding domains (HBD), which are localized in the linker region (HBD1) and C-terminal region (HBD2) of IGFBP-2.	Heparin	19-26	insulin-like growth factor binding protein 2	Mus musculus	0-7
23981772-3	2013	IGFBP-2 contains 2 heparin-binding domains (HBD), which are localized in the linker region (HBD1) and C-terminal region (HBD2) of IGFBP-2.	Heparin	19-26	insulin-like growth factor binding protein 2	Mus musculus	130-137
16139336-8	2006	CONCLUSIONS: Increased platelet surface expression of P-selectin, augmented platelet-leukocyte aggregation in vivo, and consequent activation of leukocytes was seen before PCI in blood from patients treated with UFH+E compared with bivalirudin.	Heparin	212-215	selectin P	Homo sapiens	54-64
24273488-5	2013	RESULTS: Compared to control cultures, the 5-factor combination with heparin induced significantly (p &lt;= 0.05) higher numbers of: CFU-MKs and CD41+ cells on days 7 and 14; CD41+ cells displaying hyperploidy levels (&gt;=8N) on day 14; platelets on day 14.	Heparin	69-76	integrin subunit alpha 2b	Homo sapiens	145-149
24273488-5	2013	RESULTS: Compared to control cultures, the 5-factor combination with heparin induced significantly (p &lt;= 0.05) higher numbers of: CFU-MKs and CD41+ cells on days 7 and 14; CD41+ cells displaying hyperploidy levels (&gt;=8N) on day 14; platelets on day 14.	Heparin	69-76	integrin subunit alpha 2b	Homo sapiens	175-179
24273488-7	2013	CONCLUSION: Heparin can significantly enhance the stimulating effects of a combination of TPO, SCF, FL, IL-6, and IL-11 supplemented with autologous serum on CFU-MK, MK, and platelet production from CB CD34+ cells.	Heparin	12-19	KIT ligand	Homo sapiens	95-98
23897813-3	2013	The suppressive effect of CD82 is dependent on the heparin-binding domain of the ligand.	Heparin	51-58	CD82 molecule	Homo sapiens	26-30
23897813-4	2013	Deletion of the C-terminal cytoplasmic domain of CD82 (CD82DeltaC mutant) inhibits endocytic trafficking of the tetraspanin and compromises its activity toward heparin-binding EGF-activated EGFR.	Heparin	160-167	CD82 molecule	Homo sapiens	49-53
23897813-4	2013	Deletion of the C-terminal cytoplasmic domain of CD82 (CD82DeltaC mutant) inhibits endocytic trafficking of the tetraspanin and compromises its activity toward heparin-binding EGF-activated EGFR.	Heparin	160-167	CD82 molecule	Homo sapiens	55-72
23897813-8	2013	Our data identify CD82 as a new regulator of c-Cbl, which discriminatively controls the activity of this E3 ubiquitin ligase toward heparin-binding ligand-EGFR pairs.	Heparin	132-139	CD82 molecule	Homo sapiens	18-22
25206517-4	2013	However, neuronal morphology was visible, and microtubule-associated protein-2 expression and acetylcholine levels increased following induction with heparin alone or heparin combined with basic fibroblast growth factor.	Heparin	150-157	microtubule associated protein 2	Homo sapiens	46-78
25206517-4	2013	However, neuronal morphology was visible, and microtubule-associated protein-2 expression and acetylcholine levels increased following induction with heparin alone or heparin combined with basic fibroblast growth factor.	Heparin	167-174	microtubule associated protein 2	Homo sapiens	46-78
18434447-3	2008	We hypothesized that swimming would stimulate TAG turnover rate to fuel working muscles and that heparin would reduce flux by releasing lipoprotein lipase (LPL) from endothelial cells.	Heparin	97-104	lipoprotein lipase	Oncorhynchus mykiss	136-154
18434447-3	2008	We hypothesized that swimming would stimulate TAG turnover rate to fuel working muscles and that heparin would reduce flux by releasing lipoprotein lipase (LPL) from endothelial cells.	Heparin	97-104	lipoprotein lipase	Oncorhynchus mykiss	156-159
18434447-6	2008	The fact that heparin causes a 50% decrease in baseline TAG turnover rate suggests that fish LPL must be bound to the endothelium for normal tissue uptake of fatty acids supplied by lipoproteins, as in mammals.	Heparin	14-21	lipoprotein lipase	Oncorhynchus mykiss	93-96
18560570-11	2008	In vitro experiments demonstrated a direct binding of EGF to sFRP-3 both on heparin and on the surface of CHO cells where the molecule had been membrane anchored.	Heparin	76-83	frizzled related protein L homeolog	Xenopus laevis	61-67
18574281-6	2008	Dosing of IV UFH should prolong the activated partial thromboplastin time (aPTT) to a range that corresponds to an anti-factor Xa assay (anti-FXa) level of 0.35 to 0.7 U/mL, whereas LMWH should achieve an anti-FXa level of 0.5 to 1.0 U/mL 4 h after an injection for twice-daily dosing.	Heparin	13-16	coagulation factor X	Homo sapiens	142-145
18574281-6	2008	Dosing of IV UFH should prolong the activated partial thromboplastin time (aPTT) to a range that corresponds to an anti-factor Xa assay (anti-FXa) level of 0.35 to 0.7 U/mL, whereas LMWH should achieve an anti-FXa level of 0.5 to 1.0 U/mL 4 h after an injection for twice-daily dosing.	Heparin	13-16	coagulation factor X	Homo sapiens	210-213
16303928-8	2005	Binding inhibition studies showed that hexasaccharides of heparin had a lower affinity for opticin than larger oligosaccharides; the sulfate groups of heparin contributed variably to opticin binding, with the group at ring position two of iduronate contributing least; and chondroitin sulfate A and B bound to opticin, whereas binding to chondroitin sulfate C and hyaluronan was not observed.	Heparin	151-158	opticin	Homo sapiens	183-190
23782690-0	2013	Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers.	Heparin	85-92	EGF containing fibulin extracellular matrix protein 1	Homo sapiens	0-21
16303928-8	2005	Binding inhibition studies showed that hexasaccharides of heparin had a lower affinity for opticin than larger oligosaccharides; the sulfate groups of heparin contributed variably to opticin binding, with the group at ring position two of iduronate contributing least; and chondroitin sulfate A and B bound to opticin, whereas binding to chondroitin sulfate C and hyaluronan was not observed.	Heparin	151-158	opticin	Homo sapiens	183-190
16303928-9	2005	CONCLUSIONS: Opticin binds to heparin, HS, chondroitin 4-sulfate, and dermatan sulfate, the binding affinity being dependent on sulfation pattern and oligosaccharide chain length.	Heparin	30-37	opticin	Homo sapiens	13-20
18219588-2	2008	HRG ligands include Zn2+, tropomyosin, heparin and heparan sulphate, plasminogen, plasmin, fibrinogen, thrombospondin, IgG, FcgR, and complement.	Heparin	39-46	histidine rich glycoprotein	Homo sapiens	0-3
16157224-0	2005	Selectively desulfated heparin inhibits P-selectin-mediated adhesion of human melanoma cells.	Heparin	23-30	selectin P	Homo sapiens	40-50
18424754-5	2008	C3a and C4a were best generated from C3 and C4, respectively, by monomeric beta-tryptase in the presence of low molecular weight dextran sulfate or heparin at acidic pH.	Heparin	148-155	complement C3	Homo sapiens	0-3
18006516-8	2008	Several single-point mutations within ACA8 sequence A56-T63 significantly alter the enzyme response to heparin, suggesting that heparin interaction with this site may be involved in ACA8 activation.	Heparin	103-110	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	182-186
18006516-8	2008	Several single-point mutations within ACA8 sequence A56-T63 significantly alter the enzyme response to heparin, suggesting that heparin interaction with this site may be involved in ACA8 activation.	Heparin	128-135	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	38-42
18006516-8	2008	Several single-point mutations within ACA8 sequence A56-T63 significantly alter the enzyme response to heparin, suggesting that heparin interaction with this site may be involved in ACA8 activation.	Heparin	128-135	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	182-186
18045667-0	2008	Linear diffusion of thrombin and factor Xa along the heparin molecule explains the effects of extended heparin chain lengths.	Heparin	53-60	coagulation factor X	Homo sapiens	33-42
18045667-0	2008	Linear diffusion of thrombin and factor Xa along the heparin molecule explains the effects of extended heparin chain lengths.	Heparin	103-110	coagulation factor X	Homo sapiens	33-42
23421467-2	2013	Low molecular weight heparin (LMWH) has an antagonistic effect on the RAGE axis and is also reported to exert an antitumor effect beyond the known activity of anticoagulation.	Heparin	21-28	advanced glycosylation end-product specific receptor	Homo sapiens	70-74
23571852-10	2013	The pro-tumourigenic contribution of the heparin/HS interactomes was verified in cells in which HSPG synthesis was blocked using beta-xyloside.	Heparin	41-48	syndecan 2	Homo sapiens	96-100
23641666-8	2013	The efficacy of selected peptoids as agents for neutralization of the anticoagulant activity of heparin was assayed by the Coatest method, which measures restoration of the activity of the serine protease factor Xa (FXa).	Heparin	96-103	coagulation factor X	Homo sapiens	216-219
18045667-3	2008	RESULTS: The Kd of thrombin or factor Xa is constant when expressed in terms of the concentration of sugar units, i.e. the enzymes bind the better the longer the heparin.	Heparin	162-169	coagulation factor X	Homo sapiens	31-40
17655843-10	2007	In conclusion, alpha(2A)-adrenoreceptor activates ERK and Akt in intestinal cells by a common pathway which depends on PI3-kinase activation and results from EGF receptor transactivation, via an autocrine/paracrine pathway implying MMP activation and heparin-binding-EGF shedding.	Heparin	251-258	adrenoceptor alpha 2A	Homo sapiens	15-39
17766586-6	2007	FGF-BP expression was enhanced in ATII cells by coculture with RLF cells and least suppressed by desulfated heparin.	Heparin	108-115	fibroblast growth factor binding protein 1	Rattus norvegicus	0-6
16157224-1	2005	Accumulating evidence has suggested that one of the mechanisms by which heparin inhibits metastasis is by blocking the P-selectin-based interaction of platelets with tumor cells.	Heparin	72-79	selectin P	Homo sapiens	119-129
16157224-2	2005	Here we demonstrate that the sulfate groups at C6/N and especially C6, but not C2 and C3, of heparin play a critical role in P-selectin recognition and that 2-O,3-O-desulfated heparin can block P-selectin-mediated A375 human melanoma cell adhesion.	Heparin	93-100	selectin P	Homo sapiens	125-135
17904541-3	2007	RESULTS: : Active MMP-2 and MMP-9 mean concentrations were similar in serum and in plasma-citrate, higher in plasma EDTA than in serum, in plasma-heparin and in plasma-citrate, and lower in plasma-heparin than in serum and plasma-citrate.	Heparin	146-153	matrix metallopeptidase 9	Homo sapiens	28-33
17904541-3	2007	RESULTS: : Active MMP-2 and MMP-9 mean concentrations were similar in serum and in plasma-citrate, higher in plasma EDTA than in serum, in plasma-heparin and in plasma-citrate, and lower in plasma-heparin than in serum and plasma-citrate.	Heparin	197-204	matrix metallopeptidase 9	Homo sapiens	28-33
22212466-10	2013	Compared to UFH treatment, the adenosine diphosphate (ADP) and thrombin receptor-activating peptide (TRAP)-induced thrombospondin expression post-PCI was reduced when bivalirudin was administrated during intervention.	Heparin	12-15	TRAP	Homo sapiens	63-99
22212466-10	2013	Compared to UFH treatment, the adenosine diphosphate (ADP) and thrombin receptor-activating peptide (TRAP)-induced thrombospondin expression post-PCI was reduced when bivalirudin was administrated during intervention.	Heparin	12-15	TRAP	Homo sapiens	101-105
16157224-2	2005	Here we demonstrate that the sulfate groups at C6/N and especially C6, but not C2 and C3, of heparin play a critical role in P-selectin recognition and that 2-O,3-O-desulfated heparin can block P-selectin-mediated A375 human melanoma cell adhesion.	Heparin	93-100	selectin P	Homo sapiens	194-204
23557564-3	2013	METHODS: Heparin-conjugated polycaprolactone (hPCL) and polyurethane (PU)-collagen type I composite was used as the inner and outer layers, respectively.	Heparin	9-16	PHD finger protein 1	Homo sapiens	46-50
16157224-2	2005	Here we demonstrate that the sulfate groups at C6/N and especially C6, but not C2 and C3, of heparin play a critical role in P-selectin recognition and that 2-O,3-O-desulfated heparin can block P-selectin-mediated A375 human melanoma cell adhesion.	Heparin	176-183	selectin P	Homo sapiens	194-204
16157224-3	2005	Our findings show that chemical modification of heparin, especially 2-O,3-O-desulfation, may result in a therapeutic agent that is anti-metastatic because it blocks unwanted P-selectin-dependent adhesion but that lacks dose-limiting anticoagulant effects.	Heparin	48-55	selectin P	Homo sapiens	174-184
18025279-7	2007	The fact that RANTES/CCL5-induced migration and invasion of Huh7 cells are both strongly inhibited by anti-CCR1 antibodies and heparin, as well as by beta-d-xyloside treatment of the cells, suggests that CCR1 and glycosaminoglycans are involved in these events.	Heparin	127-134	C-C motif chemokine ligand 5	Homo sapiens	14-20
16395490-7	2005	DISCUSSION, CONCLUSION: Our findings suggest that among women with recurrent IVF failures anti-annexin V antibody positivity is less prevalent than APC-resistance, lupus anticoagulant (LA) or elevated levels of antibodies against cardiolipin, beta(2)-glycoprotein-1 and that the IVF-result of women with APC-R, LA or with elevated levels of antibodies against annexin V, cardiolipin or beta(2)-glycoprotein might be positively influenced by low molecular weight heparin.	Heparin	462-469	annexin A5	Homo sapiens	95-104
18025279-7	2007	The fact that RANTES/CCL5-induced migration and invasion of Huh7 cells are both strongly inhibited by anti-CCR1 antibodies and heparin, as well as by beta-d-xyloside treatment of the cells, suggests that CCR1 and glycosaminoglycans are involved in these events.	Heparin	127-134	C-C motif chemokine ligand 5	Homo sapiens	21-25
18025279-7	2007	The fact that RANTES/CCL5-induced migration and invasion of Huh7 cells are both strongly inhibited by anti-CCR1 antibodies and heparin, as well as by beta-d-xyloside treatment of the cells, suggests that CCR1 and glycosaminoglycans are involved in these events.	Heparin	127-134	MIR7-3 host gene	Homo sapiens	60-64
17655281-6	2007	In the presence of heparin (or other highly charged polysaccharides), we demonstrate that siHTbeta formed a well-defined complex with the heparin (siHTbeta-HC) that reacted 70-fold faster with alpha2-AP than siHTbeta and also hydrolyzed model substrates and fibrinogen.	Heparin	138-145	serpin family F member 2	Homo sapiens	193-202
23341458-6	2013	N-terminal sequencing indicated that pro-BMP-2 was cleaved by FSAP at the canonical PC cleavage site, giving rise to mature BMP-2 (Arg(282) Gln(283)), as well as in the N-terminal heparin binding region of mature BMP-2, generating a truncated mature BMP-2 peptide (Arg(289) Lys(290)).	Heparin	180-187	hyaluronan binding protein 2	Homo sapiens	62-66
16253639-7	2005	In conjunction, LPLS447X carriers were characterized by a 2.4-fold increase in pre-heparin LPL mass (P&lt;.0001).	Heparin	83-90	lipoprotein lipase	Homo sapiens	16-19
22805545-0	2013	Heparin administration leads to rapid decrease in plasma matrix metalloproteinase-9.	Heparin	0-7	matrix metallopeptidase 9	Homo sapiens	57-83
17874721-0	2007	[Determination of factor Xa inhibition doses of low-molecular heparin, nadroparin and reviparin in urological patients].	Heparin	62-69	coagulation factor X	Homo sapiens	18-27
17874721-1	2007	BACKGROUND/AIM: The inhibition of factor Xa (FX) by the use of low-molecular heparin (LMH) is important clinical procedure in patients with moderate and high risk for the development of venous thromboembolism (VTE) and pulmonary embolism (PE).	Heparin	77-84	coagulation factor X	Homo sapiens	34-43
23448611-1	2013	The aim of our study was to observe the influence of low molecular Weight heparin (LMWH) on systemic inflammation, including high mobility group box 1 protein (HMGB1) and protective effect on acute lung injury induced by cecal ligation and puncture(CLP).	Heparin	74-81	high mobility group box 1	Rattus norvegicus	125-150
16331886-1	2005	Sulf-2 is an endosulfatase with activity against glucosamine-6-sulfate modifications within subregions of intact heparin.	Heparin	113-120	sulfatase 2	Homo sapiens	0-6
23448611-1	2013	The aim of our study was to observe the influence of low molecular Weight heparin (LMWH) on systemic inflammation, including high mobility group box 1 protein (HMGB1) and protective effect on acute lung injury induced by cecal ligation and puncture(CLP).	Heparin	74-81	high mobility group box 1	Rattus norvegicus	160-165
23907946-7	2013	Already the lowest concentration of UFH caused 2.5-fold increase in OPG gene expression while higher UFH concentrations substantially increased RANKL mRNA level.	Heparin	101-104	TNF superfamily member 11	Homo sapiens	144-149
23907946-10	2013	Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis.	Heparin	14-21	TNF superfamily member 11	Homo sapiens	84-89
23907946-10	2013	Of the tested heparin formulas UFH seems to be the most potent in altering the OPG, RANKL and vWF axis.	Heparin	31-34	TNF superfamily member 11	Homo sapiens	84-89
22335484-3	2012	The present study was aimed at examining the acrosin activity variations in LPC-induced acrosome exocytosis and its regulation by tyrosine kinase, protein kinase C (PKC) and voltage-dependent calcium channels (VDCC) in spermatozoa previously capacitated with heparin or quercetin.	Heparin	259-266	acrosin	Bos taurus	45-52
22335484-6	2012	It was observed that LPC induced acrosome exocytosis and increased the activity of acrosin in spermatozoa previously capacitated with heparin.	Heparin	134-141	acrosin	Bos taurus	83-90
22335484-7	2012	In heparin/LPC-treated samples, it was observed that the inhibition of tyrosine kinase and PKC blocked the acrosome exocytosis and the acrosin activity (p &lt; 0.05).	Heparin	3-10	acrosin	Bos taurus	135-142
17325231-1	2007	The major vascular endothelial growth factor (VEGF) isoforms are splice variants from a single gene that differ in their extent of heparin affinity due to the absence of the heparin binding domain in the smallest isoform (mouse VEGF120, human VEGF121).	Heparin	131-138	vascular endothelial growth factor A	Mus musculus	10-44
17325231-1	2007	The major vascular endothelial growth factor (VEGF) isoforms are splice variants from a single gene that differ in their extent of heparin affinity due to the absence of the heparin binding domain in the smallest isoform (mouse VEGF120, human VEGF121).	Heparin	131-138	vascular endothelial growth factor A	Mus musculus	46-50
17325231-1	2007	The major vascular endothelial growth factor (VEGF) isoforms are splice variants from a single gene that differ in their extent of heparin affinity due to the absence of the heparin binding domain in the smallest isoform (mouse VEGF120, human VEGF121).	Heparin	174-181	vascular endothelial growth factor A	Mus musculus	10-44
17325231-1	2007	The major vascular endothelial growth factor (VEGF) isoforms are splice variants from a single gene that differ in their extent of heparin affinity due to the absence of the heparin binding domain in the smallest isoform (mouse VEGF120, human VEGF121).	Heparin	174-181	vascular endothelial growth factor A	Mus musculus	46-50
17629847-1	2007	Prothrombinase-induced clotting time (PiCT) determines the anticoagulant effects of heparins, low molecular weight heparins (LMWHs), and direct thrombin inhibitors.	Heparin	84-92	coagulation factor X	Homo sapiens	0-14
17629847-1	2007	Prothrombinase-induced clotting time (PiCT) determines the anticoagulant effects of heparins, low molecular weight heparins (LMWHs), and direct thrombin inhibitors.	Heparin	115-123	coagulation factor X	Homo sapiens	0-14
17485301-2	2007	Heparin is a mixture of sulfated mucopolysaccharide with heterogeneity and is capable of forming multiple complexes with platelet factor 4 (PF4), released from activated platelets.	Heparin	0-7	platelet factor 4	Bos taurus	140-143
17476038-7	2007	Patients treated with heparin were significantly more likely to be treated with GP IIb/IIIa inhibitors (91% vs 25%; p = 0.001).	Heparin	22-29	integrin subunit alpha 2b	Homo sapiens	80-86
22335484-8	2012	Under these conditions, in heparin-capacitated spermatozoa, the LPC provokes an acrosin activity increase that is independent of calcium influx through VDCC Type L. In cryopreserved bovine spermatozoa, LPC might require modulation, mainly tyrosine kinase participation with respect to PKC activity to induce acrosome exocytosis and increase acrosin activity.	Heparin	27-34	acrosin	Bos taurus	80-87
23186339-5	2012	Heparin injections were used to discriminate between intracellular and extracellular LPL.	Heparin	0-7	lipoprotein lipase	Mus musculus	85-88
17339340-3	2007	Here, we present the crystal structures of FGF19 alone and FGF23 in complex with sucrose octasulfate, a disaccharide chemically related to heparin.	Heparin	139-146	fibroblast growth factor 23	Homo sapiens	59-64
15812639-3	2005	We present experimental results using SPR for the interaction of insulin-like growth factor-I (IGF-I) with one of its binding proteins, IGF binding protein-3 (IGFBP-3), and show that the dissociation, even with the addition of soluble heparin in the dissociation phase, does not exhibit the expected exponential decay characteristic of a 1:1 binding reaction.	Heparin	235-242	insulin like growth factor binding protein 3	Homo sapiens	136-157
17339340-4	2007	The conformation of the heparin-binding region between beta strands 10 and 12 in FGF19 and FGF23 diverges completely from the common conformation adopted by paracrine-acting FGFs.	Heparin	24-31	fibroblast growth factor 23	Homo sapiens	91-96
17339340-7	2007	Klotho/betaKlotho have evolved as a compensatory mechanism for the poor ability of heparin/heparan sulfate to promote binding of FGF19, -21, and -23 to their cognate receptors.	Heparin	83-90	klotho	Homo sapiens	0-6
17339340-7	2007	Klotho/betaKlotho have evolved as a compensatory mechanism for the poor ability of heparin/heparan sulfate to promote binding of FGF19, -21, and -23 to their cognate receptors.	Heparin	83-90	klotho beta	Homo sapiens	7-17
16142335-4	2005	Animal studies using non-anti-coagulant heparin (NAC heparin) suggest that it is possible to separate the anti-metastatic and anti-coagulant activities of heparin.	Heparin	40-47	synuclein alpha	Homo sapiens	49-52
17039513-0	2007	Platelet GPIIb/IIIa antagonist, XV459, in heparin-induced thrombocytopenia.	Heparin	42-49	integrin subunit alpha 2b	Homo sapiens	9-14
23227470-2	2012	Critically ill patients have significantly lower plasma anti-factor-Xa activity levels compared with control patients after administration of subcutaneous heparin.	Heparin	155-162	coagulation factor X	Homo sapiens	61-70
23227470-3	2012	The clinical relevance of the different anti-factor-Xa levels after prophylactic doses of low molecular weight heparin (LMWH) in critically ill patients is not completely understood.	Heparin	111-118	coagulation factor X	Homo sapiens	45-54
23547469-12	2012	Peptide P41-52 competed with CDF for heparin binding, while peptides P53-60 and P60-71 had no significant activity.	Heparin	37-44	erythrocyte membrane protein band 4.1	Homo sapiens	8-11
17039513-5	2007	In this study, the ability of a novel platelet GPIIb/IIIa antagonist, a free acid form of roxifiban (XV459), to block platelet activation/aggregation in response to highly characterized heparin-PF4 antibody-positive plasma/heparin was examined using light transmittance aggregometry, serotonin release, and (125)I-fibrinogen binding assays to human platelets.	Heparin	186-193	integrin subunit alpha 2b	Homo sapiens	47-52
17039513-9	2007	The platelet GPIIb/IIIa receptor antagonist (XV459) might be of potential benefit in the management of thrombotic thrombocytopenia produced by heparin and/or related glycosaminoglycans.	Heparin	143-150	integrin subunit alpha 2b	Homo sapiens	13-18
16142335-4	2005	Animal studies using non-anti-coagulant heparin (NAC heparin) suggest that it is possible to separate the anti-metastatic and anti-coagulant activities of heparin.	Heparin	53-60	synuclein alpha	Homo sapiens	49-52
16142335-6	2005	NAC heparins have clinical potential because they could be administered at a higher dose, thereby fully exploiting the anti-metastatic component of heparin activity, and because they could be used with cancer patients with bleeding complications, where the use of heparin is currently precluded.	Heparin	4-11	synuclein alpha	Homo sapiens	0-3
17292392-6	2007	DADLE"s effect was abrogated by either metalloproteinase inhibitor III (MPI) or the diphtheria toxin mutant CRM-197 which blocks heparin-binding EGF shedding indicating that DADLE signals through EGFR transactivation.	Heparin	129-136	epidermal growth factor receptor	Oryctolagus cuniculus	196-200
17303003-7	2007	In fatty milk-induced hyperlipidemic mice, the post-heparin plasma activities of lipoprotein lipase (LPL), hepatic lipase (HL), and total lipase (TL) significantly increased after treatment with 10-20 mg/kg osthole for 3 weeks (P&lt; 0.05 or P&lt; 0.01).	Heparin	52-59	lipoprotein lipase	Mus musculus	81-99
22378222-5	2012	Diffusion studies with VEGF121, a non-heparin binding variant of VEGF, showed robust diffusion with or without SOS.	Heparin	38-45	vascular endothelial growth factor A	Bos taurus	23-27
22821930-0	2012	Heparin disrupts the CXCR4/SDF-1 axis and impairs the functional capacity of bone marrow-derived mononuclear cells used for cardiovascular repair.	Heparin	0-7	chemokine (C-X-C motif) receptor 4	Mus musculus	21-26
22821930-9	2012	Mechanistically, heparin binds to both, the chemoattractant SDF-1 and its receptor, chemokine receptor 4 (CXCR4), blocking CXCR4 internalization as well as SDF-1/CXCR4 signaling after SDF-1 stimulation.	Heparin	17-24	chemokine (C-X-C motif) receptor 4	Mus musculus	106-111
22821930-9	2012	Mechanistically, heparin binds to both, the chemoattractant SDF-1 and its receptor, chemokine receptor 4 (CXCR4), blocking CXCR4 internalization as well as SDF-1/CXCR4 signaling after SDF-1 stimulation.	Heparin	17-24	chemokine (C-X-C motif) receptor 4	Mus musculus	123-128
22821930-9	2012	Mechanistically, heparin binds to both, the chemoattractant SDF-1 and its receptor, chemokine receptor 4 (CXCR4), blocking CXCR4 internalization as well as SDF-1/CXCR4 signaling after SDF-1 stimulation.	Heparin	17-24	chemokine (C-X-C motif) receptor 4	Mus musculus	123-128
22821930-10	2012	CONCLUSIONS: Heparin blocks SDF-1/CXCR4 signaling by binding to the ligand as well as the receptor, thereby interfering with migration and homing of BMCs.	Heparin	13-20	chemokine (C-X-C motif) receptor 4	Mus musculus	34-39
17303003-7	2007	In fatty milk-induced hyperlipidemic mice, the post-heparin plasma activities of lipoprotein lipase (LPL), hepatic lipase (HL), and total lipase (TL) significantly increased after treatment with 10-20 mg/kg osthole for 3 weeks (P&lt; 0.05 or P&lt; 0.01).	Heparin	52-59	lipoprotein lipase	Mus musculus	101-104
16142335-6	2005	NAC heparins have clinical potential because they could be administered at a higher dose, thereby fully exploiting the anti-metastatic component of heparin activity, and because they could be used with cancer patients with bleeding complications, where the use of heparin is currently precluded.	Heparin	148-155	synuclein alpha	Homo sapiens	0-3
22815489-6	2012	Preincubation of factor H with exogenous heparin and pretreatment of PTECs with heparitinase abolished the binding to PTECs.	Heparin	41-48	complement factor H	Homo sapiens	17-25
16181411-4	2005	Accordingly, we show that treatment of cerebellar granule neurons (CGNs) with heparin inhibits NCAM-mediated outgrowth.	Heparin	78-85	neural cell adhesion molecule 1	Homo sapiens	95-99
17380210-3	2007	By inhibiting both free and clot-bound factor Xa complexes, the oral factor Xa inhibitors prolong activated partial thromboplastin time and prothrombin times in a dose-dependent manner without the need for antithrombin, thus differing from drugs such as fondaparinux, heparin, etc.	Heparin	268-275	coagulation factor X	Homo sapiens	39-48
17380210-3	2007	By inhibiting both free and clot-bound factor Xa complexes, the oral factor Xa inhibitors prolong activated partial thromboplastin time and prothrombin times in a dose-dependent manner without the need for antithrombin, thus differing from drugs such as fondaparinux, heparin, etc.	Heparin	268-275	coagulation factor X	Homo sapiens	69-78
22761431-0	2012	Long isoform mouse selenoprotein P (Sepp1) supplies rat myoblast L8 cells with selenium via endocytosis mediated by heparin binding properties and apolipoprotein E receptor-2 (ApoER2).	Heparin	116-123	selenoprotein P	Mus musculus	19-34
16286530-4	2005	RESEARCH METHODS AND PROCEDURES: LPL and HL activities were determined in post-heparin plasma in a sample of 197 men and 209 women, 60 to 87 years of age.	Heparin	79-86	lipoprotein lipase	Homo sapiens	33-36
22761431-0	2012	Long isoform mouse selenoprotein P (Sepp1) supplies rat myoblast L8 cells with selenium via endocytosis mediated by heparin binding properties and apolipoprotein E receptor-2 (ApoER2).	Heparin	116-123	selenoprotein P	Mus musculus	36-41
22758395-0	2012	Improving the cardio protective effect of aFGF in ischemic myocardium with ultrasound-mediated cavitation of heparin modified microbubbles: preliminary experiment.	Heparin	109-116	fibroblast growth factor 1	Rattus norvegicus	42-46
22758395-2	2012	This paper was to investigate the feasibility of acidic fibroblast growth factor (aFGF) intravenous delivery to the ischemic myocardium of rats by ultrasonic microbubbles modified with heparin.	Heparin	185-192	fibroblast growth factor 1	Rattus norvegicus	49-80
22758395-2	2012	This paper was to investigate the feasibility of acidic fibroblast growth factor (aFGF) intravenous delivery to the ischemic myocardium of rats by ultrasonic microbubbles modified with heparin.	Heparin	185-192	fibroblast growth factor 1	Rattus norvegicus	82-86
17230619-15	2007	The rate of VEGF positive expression was higher in normal saline group than in N-desulfated heparin treated group (90% vs 20%, P &lt; 0.05).	Heparin	92-99	vascular endothelial growth factor A	Mus musculus	12-16
17230619-16	2007	VEGF mRNA expression was significantly inhibited by N-desulfated heparin and was higher in normal saline group than in N-desulfated heparin group (Ct value 19.51 +/- 1.01 vs 22.55 +/- 1.36, P &lt; 0.05).	Heparin	65-72	vascular endothelial growth factor A	Mus musculus	0-4
17230619-16	2007	VEGF mRNA expression was significantly inhibited by N-desulfated heparin and was higher in normal saline group than in N-desulfated heparin group (Ct value 19.51 +/- 1.01 vs 22.55 +/- 1.36, P &lt; 0.05).	Heparin	132-139	vascular endothelial growth factor A	Mus musculus	0-4
17230619-19	2007	CONCLUSION: N-desulfated heparin can inhibit metastasis of gastric cancer by suppressing tumor VEGF expression and tumor angiogenesis, but has no obvious anticoagulant activity.	Heparin	25-32	vascular endothelial growth factor A	Mus musculus	95-99
21898414-2	2012	Previously, we have shown that heparin stimulates the synthesis and modifies the sulfation pattern of this HSPG.	Heparin	31-38	CD44 molecule (Indian blood group)	Homo sapiens	107-111
16270635-1	2005	Heparin is the current mainstay drug for anticoagulation during cardiac surgery, but it requires normal levels of antithrombin (AT) for optimal anticoagulation.	Heparin	0-7	serpin family C member 1	Homo sapiens	114-126
21898414-3	2012	Here the molecular mechanisms involved in the up-regulation of HSPG synthesis by heparin in endothelial cells were decoded.	Heparin	81-88	CD44 molecule (Indian blood group)	Homo sapiens	63-67
21898414-5	2012	We observed that the up-regulation of HSPG synthesis evoked by heparin is dependent on the interaction of heparin with integrin since RGD peptide abolishes the effect.	Heparin	63-70	CD44 molecule (Indian blood group)	Homo sapiens	38-42
21898414-5	2012	We observed that the up-regulation of HSPG synthesis evoked by heparin is dependent on the interaction of heparin with integrin since RGD peptide abolishes the effect.	Heparin	106-113	CD44 molecule (Indian blood group)	Homo sapiens	38-42
22540147-1	2012	High-molecular weight heparins promote the protein Z-dependent protease inhibitor (ZPI) inhibition of factors Xa (FXa) and XIa (FXIa) by a template mechanism.	Heparin	22-30	coagulation factor X	Homo sapiens	114-117
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	41-48	coagulation factor X	Homo sapiens	132-135
22540147-5	2012	By contrast, the mutants interacted with heparin with a lower affinity and the ~48-fold heparin-mediated enhancement in the rate of FXa inhibition by ZPI was reduced to ~30-fold for ZPI-3A, ~15-fold for ZPI-D-helix(alpha1-PI), and ~8-fold for ZPI-CD-helix(alpha1-PI).	Heparin	88-95	coagulation factor X	Homo sapiens	132-135
22321833-5	2012	Conversely, an anti-CD44 function-blocking antibody and CD44 siRNA suppressed the migration of trophoblast cells in the presence of heparin in a similar scratch assay.	Heparin	132-139	CD44 molecule (Indian blood group)	Homo sapiens	20-24
22321833-5	2012	Conversely, an anti-CD44 function-blocking antibody and CD44 siRNA suppressed the migration of trophoblast cells in the presence of heparin in a similar scratch assay.	Heparin	132-139	CD44 molecule (Indian blood group)	Homo sapiens	56-60
22321833-6	2012	Furthermore, both heparin treatment and in vitro scratch wounding induced the phosphorylation of p21-activated kinase 1 (PAK1), whereas the anti-CD44-v3 antibody suppressed the heparin-induced phosphorylation of PAK1 in trophoblast cells.	Heparin	177-184	CD44 molecule (Indian blood group)	Homo sapiens	145-149
22513007-5	2012	In this concern, we examined the angiogenic response of higher molecular weight Heparin (15 kDa) of different concentrations using late CAM assay.	Heparin	80-87	calmodulin 2	Gallus gallus	136-139
16905191-6	2007	KCP additionally enhances virion binding to permissive cells through a heparin/heparan sulfate-binding site located at the N-terminus of the protein.	Heparin	71-78	kielin cysteine rich BMP regulator	Homo sapiens	0-3
17071189-2	2006	Heparin-binding growth-associated molecule (HBGAM) binds to cell receptors that are relatively more robust on endothelial cells, and it may confer endothelial cell selectivity to potent angiogens such as fibroblast growth factor-1 (FGF-1).	Heparin	0-7	fibroblast growth factor 1	Canis lupus familiaris	204-230
17071189-2	2006	Heparin-binding growth-associated molecule (HBGAM) binds to cell receptors that are relatively more robust on endothelial cells, and it may confer endothelial cell selectivity to potent angiogens such as fibroblast growth factor-1 (FGF-1).	Heparin	0-7	fibroblast growth factor 1	Canis lupus familiaris	232-237
17102832-1	2006	BACKGROUND: Heparin with adjunctive glycoprotein IIb/IIIa platelet receptor (GP IIb/IIIa) inhibitors has demonstrated its effectiveness in patients with acute coronary syndrome (ACS) undergoing percutaneous coronary intervention (PCI).	Heparin	12-19	integrin subunit alpha 2b	Homo sapiens	77-83
22513007-9	2012	Angiogenesis refers to formation of new blood vessels from the existing ones and occurrence of new blood vessels at the treated area strongly confirms that heparin of 15 kDa molecular weight has the ability to induce angiogenesis on CAM vascular bed in a dose dependent manner.	Heparin	156-163	calmodulin 2	Gallus gallus	233-236
22227436-3	2012	We demonstrate that HS isolated from a bone marrow stromal cell line (HS-5) and heparin each enhances BMP-2-induced osteogenesis in C2C12 myoblasts through increased ALP activity and osteocalcin mRNA expression.	Heparin	80-87	bone morphogenetic protein 2	Bos taurus	102-107
16128566-0	2005	Importance of tryptophan 49 of antithrombin in heparin binding and conformational activation.	Heparin	47-54	serpin family C member 1	Homo sapiens	31-43
22227436-5	2012	Heparin and HS5 influence BMP-2 activity by (i) prolonging BMP-2 half-life, (ii) reducing interactions between BMP-2 with its antagonist noggin, and (iii) modulating BMP2 distribution on the cell surface.	Heparin	0-7	bone morphogenetic protein 2	Bos taurus	26-31
22227436-5	2012	Heparin and HS5 influence BMP-2 activity by (i) prolonging BMP-2 half-life, (ii) reducing interactions between BMP-2 with its antagonist noggin, and (iii) modulating BMP2 distribution on the cell surface.	Heparin	0-7	bone morphogenetic protein 2	Bos taurus	59-64
22227436-5	2012	Heparin and HS5 influence BMP-2 activity by (i) prolonging BMP-2 half-life, (ii) reducing interactions between BMP-2 with its antagonist noggin, and (iii) modulating BMP2 distribution on the cell surface.	Heparin	0-7	bone morphogenetic protein 2	Bos taurus	59-64
22227436-5	2012	Heparin and HS5 influence BMP-2 activity by (i) prolonging BMP-2 half-life, (ii) reducing interactions between BMP-2 with its antagonist noggin, and (iii) modulating BMP2 distribution on the cell surface.	Heparin	0-7	bone morphogenetic protein 2	Bos taurus	166-170
22178588-6	2012	All 4 forms of HGF/SF induced similar levels of DNA synthesis in human hepatocytes; 1K1 and NK1 required heparin, an HSPG analogue, for full agonistic activity.	Heparin	105-112	syndecan 2	Homo sapiens	117-121
16972797-1	2006	Recently a novel plasma serine protease with high affinity to hyaluronic acid and glycosaminoglycans, such as heparin and heparan sulfate, has been described and termed hyaluronan-binding protease (HABP).	Heparin	110-117	hyaluronan binding protein 2	Homo sapiens	169-196
16972797-1	2006	Recently a novel plasma serine protease with high affinity to hyaluronic acid and glycosaminoglycans, such as heparin and heparan sulfate, has been described and termed hyaluronan-binding protease (HABP).	Heparin	110-117	hyaluronan binding protein 2	Homo sapiens	198-202
16879306-4	2006	ECP was found to damage PSC at micromolar concentrations; the effect was blocked by specific antibodies and heparin, and was more severe than the one caused by similar concentrations of RNase A, suggesting that the cationic nature of ECP, and not its ribonuclease activity, is involved in toxicity.	Heparin	108-115	ribonuclease A family member 3	Homo sapiens	0-3
16128566-1	2005	Tryptophan 49 of antithrombin, the primary inhibitor of blood clotting proteinases, has previously been implicated in binding the allosteric activator, heparin, by chemical modification and mutagenesis studies.	Heparin	152-159	serpin family C member 1	Homo sapiens	17-29
22318724-12	2012	Direct repulsion between the electronegative exon 7-encoded residues of the heparin binding domain and the electronegative L1 loop found only in Nrp2 is found to significantly contribute to the observed selectivity.	Heparin	76-83	neuropilin 2	Homo sapiens	145-149
16128566-3	2005	Here, we provide a detailed thermodynamic and kinetic characterization of heparin binding to a Trp49 to Lys variant of antithrombin and suggest a model for how Trp49 participates in heparin binding and activation.	Heparin	74-81	serpin family C member 1	Homo sapiens	119-131
16729969-2	2006	Heparin which inhibits pulmonary artery smooth muscle cell (PASMC) proliferation increases the levels of two CDKIs, p21 and p27, although only p27 is important in inhibition of PASMC growth in vitro and in vivo.	Heparin	0-7	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	116-119
16128566-5	2005	Rapid kinetics analyses showed that the mutation minimally affected the initial weak binding of heparin to antithrombin or the rate constant for the subsequent conformational activation of the serpin.	Heparin	96-103	serpin family C member 1	Homo sapiens	107-119
16729969-2	2006	Heparin which inhibits pulmonary artery smooth muscle cell (PASMC) proliferation increases the levels of two CDKIs, p21 and p27, although only p27 is important in inhibition of PASMC growth in vitro and in vivo.	Heparin	0-7	cyclin-dependent kinase inhibitor 1B	Mus musculus	124-127
16729969-2	2006	Heparin which inhibits pulmonary artery smooth muscle cell (PASMC) proliferation increases the levels of two CDKIs, p21 and p27, although only p27 is important in inhibition of PASMC growth in vitro and in vivo.	Heparin	0-7	cyclin-dependent kinase inhibitor 1B	Mus musculus	143-146
16765113-6	2006	This difference was ameliorated when GP IIb/IIIa inhibitors were used consistently in a previous trial that compared bivalirudin with heparin during PCI (4.6% vs 6.7%, p=0.322).	Heparin	134-141	integrin subunit alpha 2b	Homo sapiens	37-43
22294539-5	2012	This case report describes first time use of GP IIb/IIIa inhibitor and IABP with heparin, in a patient just after spinal surgery.	Heparin	81-88	integrin subunit alpha 2b	Homo sapiens	45-51
22040724-2	2012	The potentiation of C1-INH by heparin and other glycosaminoglycans (GAGs) regulates a broad spectrum of C1-INH activities in vivo both in normal and disease states.	Heparin	30-37	serpin family G member 1	Homo sapiens	20-26
22040724-2	2012	The potentiation of C1-INH by heparin and other glycosaminoglycans (GAGs) regulates a broad spectrum of C1-INH activities in vivo both in normal and disease states.	Heparin	30-37	serpin family G member 1	Homo sapiens	104-110
22040724-3	2012	SCOPE OF RESEARCH: We have studied the potentiation of human C1-INH by heparin using Surface Plasmon Resonance (SPR), circular dichroism (CD) and a functional assay.	Heparin	71-78	serpin family G member 1	Homo sapiens	61-67
22040724-5	2012	MAJOR CONCLUSIONS: Our SPR experiments conducted in three different design versions showed marked acceleration in C1-INH interactions with complement protease C1s as a result of potentiation of C1-INH by heparin (from 5- to 11-fold increase of the association rate).	Heparin	204-211	serpin family G member 1	Homo sapiens	114-120
15905187-2	2005	Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin"s ability to inhibit proliferation, migration, capillary-like tube formation, basic fibroblast growth factor (bFGF) signaling, and perlecan gene expression in bFGF-stimulated human umbilical vein endothelial cells.	Heparin	13-20	serpin family C member 1	Homo sapiens	55-67
22040724-5	2012	MAJOR CONCLUSIONS: Our SPR experiments conducted in three different design versions showed marked acceleration in C1-INH interactions with complement protease C1s as a result of potentiation of C1-INH by heparin (from 5- to 11-fold increase of the association rate).	Heparin	204-211	serpin family G member 1	Homo sapiens	194-200
22040724-8	2012	GENERAL SIGNIFICANCE: This is the first report that directly demonstrates a significant acceleration of the C1-INH interactions with C1s due to heparin by using a consecutive double capture SPR approach.	Heparin	144-151	serpin family G member 1	Homo sapiens	108-114
16443677-12	2006	These results suggest that 1) vascular dysfunction associated with aging is mediated in part by increased levels of superoxide, 2) gene transfer of ECSOD reduces vascular superoxide and dysfunction in old rats, and 3) beneficial effects of ECSOD in old rats require the heparin-binding domain of ECSOD.	Heparin	270-277	superoxide dismutase 3	Rattus norvegicus	148-153
16443677-12	2006	These results suggest that 1) vascular dysfunction associated with aging is mediated in part by increased levels of superoxide, 2) gene transfer of ECSOD reduces vascular superoxide and dysfunction in old rats, and 3) beneficial effects of ECSOD in old rats require the heparin-binding domain of ECSOD.	Heparin	270-277	superoxide dismutase 3	Rattus norvegicus	240-245
16443677-12	2006	These results suggest that 1) vascular dysfunction associated with aging is mediated in part by increased levels of superoxide, 2) gene transfer of ECSOD reduces vascular superoxide and dysfunction in old rats, and 3) beneficial effects of ECSOD in old rats require the heparin-binding domain of ECSOD.	Heparin	270-277	superoxide dismutase 3	Rattus norvegicus	240-245
16683212-11	2006	CONCLUSIONS: In routine clinical practice, patients treated with GP IIb/IIIa inhibitors have slightly improved outcomes and similar bleeding risks with LMWH than with UFH.	Heparin	167-170	integrin subunit alpha 2b	Homo sapiens	65-71
16716081-6	2006	To clarify the role of heparin in regulating BACE1, we examined the effect of heparin on the activity of recombinant human BACE1 (rBACE1) in vitro.	Heparin	78-85	beta-secretase 1	Rattus norvegicus	130-136
22514695-0	2012	Complement C1 esterase inhibitor levels linked to infections and contaminated heparin-associated adverse events.	Heparin	78-85	serpin family G member 1	Homo sapiens	11-32
16716081-7	2006	Low concentrations (1 microg/mL) of heparin were found to stimulate rBACE1, increasing enzyme V(max) and decreasing the K(M).	Heparin	36-43	beta-secretase 1	Rattus norvegicus	68-74
15905187-4	2005	Surprisingly, mutation of Lys114, which blocks anticoagulant activation of antithrombin by heparin, caused the native protein to acquire antiproliferative activity without the need for conformational change.	Heparin	91-98	serpin family C member 1	Homo sapiens	75-87
16716081-9	2006	Heparin affinity chromatography demonstrated that heparin interacted strongly with the zymogen form of rBACE1 and bound to a peptide homologous to the N-terminal pro sequence of BACE1.	Heparin	0-7	beta-secretase 1	Rattus norvegicus	103-109
16716081-9	2006	Heparin affinity chromatography demonstrated that heparin interacted strongly with the zymogen form of rBACE1 and bound to a peptide homologous to the N-terminal pro sequence of BACE1.	Heparin	50-57	beta-secretase 1	Rattus norvegicus	103-109
15905187-5	2005	Together, these results indicate that the heparin-binding site of antithrombin is of crucial importance for mediating the serpin"s antiangiogenic activity and that heparin activation of native antithrombin constitutes an antiangiogenic switch that is responsible for turning off the antiangiogenic activity of the native serpin.	Heparin	42-49	serpin family C member 1	Homo sapiens	66-78
22171396-5	2004	In addition, the HSPG contain stretches of the disaccharide GlcNS6S-IdoA2S (HS(NS4F5); these motifs are abundantly found in heparin, but have limited presence in the HS of normal tissues) that inhibit cell proliferation and induce apoptosis but do not affect the attachment of cells to collagen I (5).	Heparin	124-131	syndecan 2	Homo sapiens	17-21
15905187-5	2005	Together, these results indicate that the heparin-binding site of antithrombin is of crucial importance for mediating the serpin"s antiangiogenic activity and that heparin activation of native antithrombin constitutes an antiangiogenic switch that is responsible for turning off the antiangiogenic activity of the native serpin.	Heparin	164-171	serpin family C member 1	Homo sapiens	193-205
16100743-9	2005	In conclusion, the purified heparinase could selectively degrade heparin into oligosaccharides and the interaction between G-CSF and heparin was correlated with the chain length of heparin.	Heparin	28-35	colony stimulating factor 3	Homo sapiens	123-128
21696361-3	2011	FGF10 mediates biological responses by activating FGF receptor 2b (FGFR2b) with heparin/heparan sulfate in a paracrine manner.	Heparin	80-87	fibroblast growth factor 10	Mus musculus	0-5
16263173-3	2006	Factor H is composed of 20 short consensus repeats (SCRs); two heparin-binding sites have been identified within SCR 7 and SCR 20 and a third site is thought to exist within or near SCR 13.	Heparin	63-70	complement factor H	Homo sapiens	0-8
16263173-4	2006	Using an extensive series of recombinant fH fragments and heparin affinity chromatography, we have localized the third heparin-binding domain to SCR 9.	Heparin	119-126	complement factor H	Homo sapiens	41-43
16263173-5	2006	A recombinant fH fragment containing both SCR 7 and SCR 9 exhibited higher affinity for heparin than SCR 7 alone, suggesting that the individual heparin-binding sites interact simultaneously with heparin to create a higher avidity interaction.	Heparin	88-95	complement factor H	Homo sapiens	14-16
16263173-5	2006	A recombinant fH fragment containing both SCR 7 and SCR 9 exhibited higher affinity for heparin than SCR 7 alone, suggesting that the individual heparin-binding sites interact simultaneously with heparin to create a higher avidity interaction.	Heparin	145-152	complement factor H	Homo sapiens	14-16
16263173-5	2006	A recombinant fH fragment containing both SCR 7 and SCR 9 exhibited higher affinity for heparin than SCR 7 alone, suggesting that the individual heparin-binding sites interact simultaneously with heparin to create a higher avidity interaction.	Heparin	145-152	complement factor H	Homo sapiens	14-16
16442624-0	2006	The Kaposi"s sarcoma-associated herpesvirus complement control protein (KCP) binds to heparin and cell surfaces via positively charged amino acids in CCP1-2.	Heparin	86-93	KCP	Human gammaherpesvirus 8	72-75
16442624-3	2006	We report here that KCP also binds to heparin at physiological ionic strength.	Heparin	38-45	kielin cysteine rich BMP regulator	Homo sapiens	20-23
16442624-5	2006	In silico molecular docking of heparin to KCP confirmed the experimental data, and further explored the heparin binding site, enabling us to present a model of the KCP-heparin interaction.	Heparin	31-38	kielin cysteine rich BMP regulator	Homo sapiens	42-45
16442624-5	2006	In silico molecular docking of heparin to KCP confirmed the experimental data, and further explored the heparin binding site, enabling us to present a model of the KCP-heparin interaction.	Heparin	31-38	kielin cysteine rich BMP regulator	Homo sapiens	164-167
16442624-5	2006	In silico molecular docking of heparin to KCP confirmed the experimental data, and further explored the heparin binding site, enabling us to present a model of the KCP-heparin interaction.	Heparin	104-111	kielin cysteine rich BMP regulator	Homo sapiens	164-167
16442624-5	2006	In silico molecular docking of heparin to KCP confirmed the experimental data, and further explored the heparin binding site, enabling us to present a model of the KCP-heparin interaction.	Heparin	104-111	kielin cysteine rich BMP regulator	Homo sapiens	164-167
16442624-6	2006	Furthermore, the docking analysis also yielded insights of the KCP structure, by indicating that the angle between CCP domains 1-2 during the initial binding of heparin is more extended than in the model we have previously presented.	Heparin	161-168	kielin cysteine rich BMP regulator	Homo sapiens	63-66
21930949-3	2011	Despite efforts to model heparin binding based on known apo crystal structures, the mechanism of heparin-induced APP/APLP dimerization has not been established experimentally.	Heparin	97-104	amyloid beta precursor like protein 1	Homo sapiens	117-121
21930949-4	2011	Here we report the crystal structure of a complex between heparin and the E2 domain of APLP1, which harbors the conserved high affinity heparin binding site of the full-length molecule.	Heparin	58-65	amyloid beta precursor like protein 1	Homo sapiens	87-92
21930949-4	2011	Here we report the crystal structure of a complex between heparin and the E2 domain of APLP1, which harbors the conserved high affinity heparin binding site of the full-length molecule.	Heparin	136-143	amyloid beta precursor like protein 1	Homo sapiens	87-92
21880887-2	2011	SUMMARY: The administration of low-molecular-weight heparins to obese patients (body mass index [BMI] of &gt;=30 kg/m(2)) at the dose recommended for VTE prophylaxis has been reported to result in increased thromboembolic events and decreased anti-factor Xa levels, and some evidence indicates that weight-based dosing adjustments may be appropriate.	Heparin	52-60	coagulation factor X	Homo sapiens	248-257
16100743-9	2005	In conclusion, the purified heparinase could selectively degrade heparin into oligosaccharides and the interaction between G-CSF and heparin was correlated with the chain length of heparin.	Heparin	65-72	colony stimulating factor 3	Homo sapiens	123-128
21741028-3	2011	To determine whether apoE antagonism would protect against septic mortality in mice, apoE-LDLR binding was antagonized using heparin, which can inhibit apoE"s LDLR-binding site.	Heparin	125-132	low density lipoprotein receptor	Mus musculus	90-94
16100743-9	2005	In conclusion, the purified heparinase could selectively degrade heparin into oligosaccharides and the interaction between G-CSF and heparin was correlated with the chain length of heparin.	Heparin	65-72	colony stimulating factor 3	Homo sapiens	123-128
21741028-3	2011	To determine whether apoE antagonism would protect against septic mortality in mice, apoE-LDLR binding was antagonized using heparin, which can inhibit apoE"s LDLR-binding site.	Heparin	125-132	low density lipoprotein receptor	Mus musculus	159-163
21741028-9	2011	LDLR+/+ fibroblasts displayed decreased uptake of apoE when treated concurrently with heparin for 12 hours.	Heparin	86-93	low density lipoprotein receptor	Mus musculus	0-4
16115201-5	2005	In contrast, a non-heparin binding alkaline phosphatase-tagged human endostatin lacking R27 and R139 bound to specific tissue structures.	Heparin	19-26	collagen type XVIII alpha 1 chain	Homo sapiens	69-79
21496084-10	2011	The addition of heparin significantly reduced levels of IGF-1, TNF-alpha and TGF-beta, and significantly elevated levels of IL-1ra.	Heparin	16-23	interleukin 1 receptor antagonist	Equus caballus	124-130
16841652-1	2006	It is possible to successfully determine both the activity against activated factor Xa in animals plasma after heparins administration and specific activity against activated factor Xa of new anticoagulants by means of the domestic diagnostic kit "Reachrom-Heparin" developed by the company "Renam".	Heparin	111-119	coagulation factor X	Homo sapiens	77-86
16601834-1	2006	Plasminogen activator inhibitor type 1 (PAI-1), the primary inhibitor of plasminogen activators, also forms high molecular weight complexes with either thrombin or factor Xa (FXa) in the presence of heparin, resulting in the loss of mutual activities of enzyme and inhibitor.	Heparin	199-206	coagulation factor X	Homo sapiens	164-173
16601834-1	2006	Plasminogen activator inhibitor type 1 (PAI-1), the primary inhibitor of plasminogen activators, also forms high molecular weight complexes with either thrombin or factor Xa (FXa) in the presence of heparin, resulting in the loss of mutual activities of enzyme and inhibitor.	Heparin	199-206	coagulation factor X	Homo sapiens	175-178
16601834-6	2006	In the presence of vitronectin (Vn), the inhibition of thrombin and FXa by PAI-1 was further promoted by both types of heparin but to a significantly lesser extent with LMW-heparin.	Heparin	119-126	vitronectin	Homo sapiens	19-30
16601834-6	2006	In the presence of vitronectin (Vn), the inhibition of thrombin and FXa by PAI-1 was further promoted by both types of heparin but to a significantly lesser extent with LMW-heparin.	Heparin	119-126	vitronectin	Homo sapiens	32-34
16086057-0	2005	[Effects of low molecular weight heparin on vascular endothelial growth factor expression of early diabetic nephropathy].	Heparin	33-40	vascular endothelial growth factor A	Rattus norvegicus	44-78
16601834-6	2006	In the presence of vitronectin (Vn), the inhibition of thrombin and FXa by PAI-1 was further promoted by both types of heparin but to a significantly lesser extent with LMW-heparin.	Heparin	119-126	coagulation factor X	Homo sapiens	68-71
16601834-7	2006	We then analyzed the possible enhancing effect of heparin on tissue plasminogen activator (tPA)-induced fibrinolysis.	Heparin	50-57	chromosome 20 open reading frame 181	Homo sapiens	61-89
21715329-4	2011	To help explain how these proteins interact with heparin, we have determined the crystal structure of the E2 domain of APLP1 in complex with sucrose octasulfate (SOS).	Heparin	49-56	amyloid beta precursor like protein 1	Homo sapiens	119-124
21715329-8	2011	Comparison with a lower resolution APP structure shows that all key heparin binding residues are conserved and identically positioned, suggesting that APLP1 and APP may bind heparin similarly.	Heparin	68-75	amyloid beta precursor like protein 1	Homo sapiens	151-156
21715329-8	2011	Comparison with a lower resolution APP structure shows that all key heparin binding residues are conserved and identically positioned, suggesting that APLP1 and APP may bind heparin similarly.	Heparin	174-181	amyloid beta precursor like protein 1	Homo sapiens	151-156
21715329-10	2011	However, mutating a pair of conserved basic residues (equivalent to Arg-414 and Arg-415 of APLP1) immediately adjacent to the heparin binding site affects both the maturation and the processing of APP.	Heparin	126-133	amyloid beta precursor like protein 1	Homo sapiens	91-96
21564417-0	2011	Antitumoral efficacy by systemic delivery of heparin conjugated polyethylenimine-plasmid interleukin-15 complexes in murine models of lung metastasis.	Heparin	45-52	interleukin 15	Mus musculus	89-103
16507336-5	2006	All three ADAMTS-5 isoforms bound to sulfated GAGs (heparin and chondroitin sulfate (CS)).	Heparin	52-59	ADAM metallopeptidase with thrombospondin type 1 motif 5	Homo sapiens	10-18
16343444-2	2006	Heparan sulfate glucosaminyl N-deacetylase/N-sulfotransferase isoform 2 (NDST-2), a key enzyme in the biosynthesis of heparin, contains two distinct activities.	Heparin	118-125	N-deacetylase and N-sulfotransferase 2	Homo sapiens	29-71
16343444-2	2006	Heparan sulfate glucosaminyl N-deacetylase/N-sulfotransferase isoform 2 (NDST-2), a key enzyme in the biosynthesis of heparin, contains two distinct activities.	Heparin	118-125	N-deacetylase and N-sulfotransferase 2	Homo sapiens	73-79
16086057-1	2005	OBJECTIVE: To investigate the effects of low molecular weight heparin (LMWH) on vascular endothelial growth factor (VEGF) expression of early diabetic nephropathy.	Heparin	62-69	vascular endothelial growth factor A	Rattus norvegicus	80-114
21538828-5	2011	The surface exhibited anti factor Xa activity, thus confirming the presence of bounded heparin that kept some biological activity.	Heparin	87-94	coagulation factor X	Homo sapiens	27-36
16086057-1	2005	OBJECTIVE: To investigate the effects of low molecular weight heparin (LMWH) on vascular endothelial growth factor (VEGF) expression of early diabetic nephropathy.	Heparin	62-69	vascular endothelial growth factor A	Rattus norvegicus	116-120
16078853-0	2005	Mechanism of poly(acrylic acid) acceleration of antithrombin inhibition of thrombin: implications for the design of novel heparin mimics.	Heparin	122-129	serpin family C member 1	Homo sapiens	48-60
21376632-12	2011	After the removal of heparin, the i-STAT 1"s ACT values became significantly lower than those measured on the Medtronic ACTR II (p &lt; 0.001).	Heparin	21-28	signal transducer and activator of transcription 1	Homo sapiens	36-42
16322261-1	2005	We have previously shown that part of the heparin-binding domain of the vascular endothelial growth factor (VEGF), designated HBDt, localizes very selectively to surfaces of the endothelial cells of i.t blood vessels.	Heparin	42-49	vascular endothelial growth factor A	Mus musculus	72-106
16322261-1	2005	We have previously shown that part of the heparin-binding domain of the vascular endothelial growth factor (VEGF), designated HBDt, localizes very selectively to surfaces of the endothelial cells of i.t blood vessels.	Heparin	42-49	vascular endothelial growth factor A	Mus musculus	108-112
15941584-7	2005	The surface-bound heparin is shown to possess anti-coagulant activity in the range of 4.80-6.39 mIU/cm2 as determined by a chromogenic anti-Factor Xa assay.	Heparin	18-25	coagulation factor X	Homo sapiens	140-149
21220249-5	2011	Like heparin, thrombin and FXa cause an increase in IGF-I in ESCs, suggesting an action of heparin independent from its anticoagulatory effects.	Heparin	91-98	coagulation factor X	Homo sapiens	27-30
16078853-1	2005	The bridging mechanism of antithrombin inhibition of thrombin is a dominant mechanism contributing a massive approximately 2500-fold acceleration in the reaction rate and is also a key reason for the clinical usage of heparin.	Heparin	218-225	serpin family C member 1	Homo sapiens	26-38
15941584-9	2005	The proposed polymeric coatings are capable of functioning by two complementary anti-thrombotic mechanisms, one based on the potent anti-platelet activity of NO, and the other the result of the ability of immobilized heparin to inhibit Factor Xa and thrombin (Factor IIa).	Heparin	217-224	coagulation factor X	Homo sapiens	236-245
16568610-2	2005	The decrease of intercell reserve heparin content and increase of the background and post-heparin levels of blood serum LPL activity were indicated after two hours food load.	Heparin	90-97	lipoprotein lipase	Homo sapiens	120-123
16125968-5	2005	Identification of GPR30 as a Gs-coupled 7TM receptor that triggers release of heparin-binding EGF establishes its role in cell signaling cascades initiated by estrogens, and explains their capacity to activate second messengers and promote EGF-like effects.	Heparin	78-85	G protein-coupled estrogen receptor 1	Homo sapiens	18-23
16102727-7	2005	A mutant of the heparin-binding site of PEDF (Hep-mut PEDF) suppressed tumor growth.	Heparin	16-23	DNL-type zinc finger	Homo sapiens	46-49
21306770-4	2011	TRAIL-loaded nanoparticles (NPs) were prepared by mixing PEGylated heparin (PEG-HE), poly-L-lysine (PLL), and TRAIL.	Heparin	67-74	tumor necrosis factor (ligand) superfamily, member 10	Mus musculus	0-5
16568610-3	2005	The role of two factors, endogenic heparin being one of them, in the increase of postprandial LPL activity of blood serum were discussed.	Heparin	35-42	lipoprotein lipase	Homo sapiens	94-97
15892971-4	2005	vFGF had strong affinity to heparin, a property important for FGF signaling via an FGF receptor.	Heparin	28-35	fibroblast growth factor	Autographa californica nucleopolyhedrovirus	1-4
21372140-4	2011	In the current study, we postulated that IGFBP-2 increased bone mass partly through the activity of its heparin-binding domain (HBD).	Heparin	104-111	insulin-like growth factor binding protein 2	Mus musculus	41-48
21220417-8	2011	Taken together, these results suggest that whereas protein Z, lipid, and calcium cofactors promote ZPI inhibition of membrane-associated factor Xa, heparin activates ZPI to inhibit free factor Xa as well as factor XIa and therefore may play a physiologically and pharmacologically important role in ZPI anticoagulant function.	Heparin	148-155	coagulation factor X	Homo sapiens	186-195
21088136-0	2011	PRT-060318, a novel Syk inhibitor, prevents heparin-induced thrombocytopenia and thrombosis in a transgenic mouse model.	Heparin	44-51	spleen tyrosine kinase	Mus musculus	20-23
16027123-2	2005	The biological activity of granulocyte-macrophage colony-stimulating factor (GM-CSF) is modulated by the sulfated glycosaminoglycans (GAGs) heparan sulfate and heparin.	Heparin	160-167	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	77-83
16027123-9	2005	Binding assays on heparin-Sepharose showed that, at acidic pH, the triple mutant mGM-CSF binds to immobilized heparin with significantly higher affinity than wild type (WT) mGM-CSF and that neither protein binds to the column at neutral pH.	Heparin	18-25	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	81-88
16113752-5	2005	Based on standard laboratory methods for the chromogenic determination of the anti-factor Xa activity of low molecular weight heparin several chromogenic substrate assays were published for monitoring.	Heparin	126-133	coagulation factor X	Homo sapiens	83-92
15892971-4	2005	vFGF had strong affinity to heparin, a property important for FGF signaling via an FGF receptor.	Heparin	28-35	fibroblast growth factor	Autographa californica nucleopolyhedrovirus	62-65
15917224-9	2005	Changes in plasmin activity have been observed previously at sites of TSG-6 expression, and the results presented here suggest that TSG-6 is likely to contribute to matrix remodeling, at least in part, through down-regulation of the protease network, especially in locations containing heparin/heparan sulfate proteoglycans.	Heparin	286-293	TNF alpha induced protein 6	Homo sapiens	132-137
15917224-10	2005	The differential effects of HA and heparin on TSG-6 function provide a mechanism for its regulation and functional partitioning in particular tissue microenvironments.	Heparin	35-42	TNF alpha induced protein 6	Homo sapiens	46-51
16004430-1	2005	Binding interactions between low molecular weight heparin (LMWH) and heparin-binding peptides (HBP) have been applied as a strategy for the assembly of hydrogels that are capable of sequestering growth factors and delivering them in a controlled manner.	Heparin	50-57	azurocidin 1	Homo sapiens	69-93
16004430-1	2005	Binding interactions between low molecular weight heparin (LMWH) and heparin-binding peptides (HBP) have been applied as a strategy for the assembly of hydrogels that are capable of sequestering growth factors and delivering them in a controlled manner.	Heparin	50-57	azurocidin 1	Homo sapiens	95-98
15952792-4	2005	We recently found novel heparin-binding VEGFs in snake venom, designated VEGF-Fs, which specifically recognize KDR, rather than other VEGF receptors.	Heparin	24-31	kinase insert domain receptor	Homo sapiens	111-114
21295276-4	2011	In Fgf4- and heparin-supplemented culture conditions, Tet1-depleted ESCs activate the trophoblast stem cell lineage determinant Elf5 and can colonize the placenta in midgestation embryo chimeras.	Heparin	13-20	tet methylcytosine dioxygenase 1	Mus musculus	54-58
21295276-4	2011	In Fgf4- and heparin-supplemented culture conditions, Tet1-depleted ESCs activate the trophoblast stem cell lineage determinant Elf5 and can colonize the placenta in midgestation embryo chimeras.	Heparin	13-20	E74-like factor 5	Mus musculus	128-132
21168205-0	2011	Effects of calcium, magnesium, low-dose aspirin and low-molecular-weight heparin on the release of PP13 from placental explants.	Heparin	73-80	galectin 13	Homo sapiens	99-103
15935280-2	2005	Interaction of transglutaminase with heparin might mimic the physiological binding to membrane heparan sulfates, accounting for the limited but significant fraction of enzyme exposed at cell surface to crosslink ECM proteins.	Heparin	37-44	multimerin 1	Homo sapiens	212-215
16013009-8	2005	These changes occurred in parallel with a potentiation of the VEGF-related NO production by both heparins.	Heparin	97-105	vascular endothelial growth factor A	Bos taurus	62-66
16013009-14	2005	By changing the way the VEGF intracellular signaling is driven, heparin could act as a stabilizing factor for the endothelium, without stimulating vessel proliferation.	Heparin	64-71	vascular endothelial growth factor A	Bos taurus	24-28
21212510-0	2011	Binding affinities of NKG2D and CD94 to sialyl Lewis X-expressing N-glycans and heparin.	Heparin	80-87	killer cell lectin like receptor D1	Homo sapiens	32-36
15760954-1	2005	BACKGROUND: The objective of this study was to investigate the comparative effects of heparin-binding epidermal growth factor-like growth factor (HB-EGF) on the growth of cultured human leiomyoma cells and myometrial cells.	Heparin	86-93	heparin binding EGF like growth factor	Homo sapiens	146-152
21212510-1	2011	Lectin-like receptors natural killer group 2D (NKG2D) and CD94 on natural killer (NK) cells bind to alpha2,3-NeuAc-containing N-glycans and heparin/heparan sulfate (HS).	Heparin	140-147	killer cell lectin like receptor D1	Homo sapiens	58-62
21147877-4	2011	We used primary adult rat cardiomyocytes and demonstrate that adiponectin increased LPL translocation to the cell surface where it could be released at least partly in its active form, as evidenced by measuring basal and heparin-releasable LPL activity.	Heparin	221-228	adiponectin, C1Q and collagen domain containing	Rattus norvegicus	62-73
16320108-5	2005	ICAM-1 expression in resting state, in the presence of TNF-alpha or after the application of heparin or hyaluronan was determined by flow cytometry.	Heparin	93-100	intercellular adhesion molecule 1	Rattus norvegicus	0-6
16320108-10	2005	The introduction of heparin caused a decrease in ICAM-1 expression, however hyaluronan did not affect the expression.	Heparin	20-27	intercellular adhesion molecule 1	Rattus norvegicus	49-55
15839662-5	2005	Therefore, this case is different than that described for the controversial recognition of heparin-like saccharides by AT-III, which seems to recognize just one conformation of the iduronic acid residues.	Heparin	91-98	serpin family C member 1	Homo sapiens	119-125
15658103-2	2005	METHODS: Ultrathin multiorganic layers were assembled on a platinum coil through successive deposition of cationic polyethylenimine and anionic heparin, and then bFGF was immobilized through an affinity interaction with heparin.	Heparin	220-227	fibroblast growth factor 2	Canis lupus familiaris	162-166
20939056-0	2010	Synthetic elastin hydrogels that are coblended with heparin display substantial swelling, increased porosity, and improved cell penetration.	Heparin	52-59	elastin	Homo sapiens	10-17
20939056-7	2010	Hydrogel swelling studies showed that each of the hydrogels contracted as the temperature was raised from 4 C to 37 C; synthetic elastin-heparin was least affected by temperature with a contraction of only 22.4 +- 1.2%, which would facilitate its transition from cold storage to body temperature.	Heparin	137-144	elastin	Homo sapiens	129-136
15960266-6	2005	RESULTS: CD34+CD41a+ cells was expanded (4.0 +/- 1.7) folds on day 7 in TPO (50 ng/ml) group and (10.5 +/- 4.8) fold in TPO combined with IL-11 group; after heparin was joined in on day 0, a more significantly elevated expansion was found in the heparin, TPO, and IL-11 group [(29.9 +/- 6.4) folds than the above two groups; P &lt; 0.05].	Heparin	157-164	CD34 antigen	Mus musculus	9-13
20950840-5	2010	In patients on unfractionated heparin (UFH), significantly lower anti-FXa activity [median=0.29IU/mL (range:0.04-1.15) vs. 0.39 (0.05-1.25), n=89, p&lt;0.0001] and shorter aPTT were measured in partial-draw tubes.	Heparin	30-37	coagulation factor X	Homo sapiens	70-73
20950840-5	2010	In patients on unfractionated heparin (UFH), significantly lower anti-FXa activity [median=0.29IU/mL (range:0.04-1.15) vs. 0.39 (0.05-1.25), n=89, p&lt;0.0001] and shorter aPTT were measured in partial-draw tubes.	Heparin	39-42	coagulation factor X	Homo sapiens	70-73
15668190-9	2005	RESULTS: UFH and, to a lesser extent, dalteparin potentiated platelet aggregation induced by ADP, PAF, 5HT, U46619, epinephrine and TRAP in a concentration-dependent manner but inhibited aggregation induced by collagen.	Heparin	9-12	TRAP	Homo sapiens	132-136
15668190-10	2005	Cangrelor effectively opposed the potentiating effects of heparins on sustained aggregation induced by ADP, PAF, 5HT, U46619 and TRAP but had less effect on epinephrine-induced aggregation, whereas A2P5P was more effective at blocking both the initial phase of ADP-induced aggregation and the aggregation response to epinephrine, reflecting the differences in G protein coupling between the agonist receptors.	Heparin	58-66	TRAP	Homo sapiens	129-133
15572165-4	2004	Recent evidence support this notion: first, the presence of two heparin-binding domains in ColQ that interact with heparan sulfate proteoglycans (HSPGs) at the synaptic basal lamina; and second, a knockout mouse for perlecan, a HSPG concentrated in nerve-muscle contact, in which absence of asymmetric AChE at the NMJ is observed.	Heparin	64-71	collagen-like tail subunit (single strand of homotrimer) of asymmetric acetylcholinesterase	Mus musculus	91-95
15624282-7	2004	Administration of GpIIb/IIIa in addition to thrombolytics, aspirin and heparin was associated with a significant reduction in the combined criteria by 17% (95% CI: 10% - 23%) and a significant excess of major bleeding by 69% (95% CI: 38% - 109%).	Heparin	71-78	integrin subunit alpha 2b	Homo sapiens	18-23
15543318-3	2004	The results show that the anticoagulant effects of the latter three heparins under conditions approximating physiologic are exerted almost exclusively by acceleration of the inactivation of thrombin, factor Xa and factor IXa to near diffusion-controlled rate constants of approximately 10(6) - 10(7) M(-1).s(-1).	Heparin	68-76	coagulation factor X	Homo sapiens	200-224
20729553-0	2010	Binding of procollagen C-proteinase enhancer-1 (PCPE-1) to heparin/heparan sulfate: properties and role in PCPE-1 interaction with cells.	Heparin	59-66	procollagen C-endopeptidase enhancer protein	Mus musculus	11-46
20729553-0	2010	Binding of procollagen C-proteinase enhancer-1 (PCPE-1) to heparin/heparan sulfate: properties and role in PCPE-1 interaction with cells.	Heparin	59-66	procollagen C-endopeptidase enhancer protein	Mus musculus	48-54
20729553-4	2010	PCPE-1 consists of two CUB domains that bind to the procollagen C-propeptides and are required for PCP enhancing activity, and one NTR domain that binds heparin.	Heparin	153-160	procollagen C-endopeptidase enhancer protein	Mus musculus	0-6
15960266-6	2005	RESULTS: CD34+CD41a+ cells was expanded (4.0 +/- 1.7) folds on day 7 in TPO (50 ng/ml) group and (10.5 +/- 4.8) fold in TPO combined with IL-11 group; after heparin was joined in on day 0, a more significantly elevated expansion was found in the heparin, TPO, and IL-11 group [(29.9 +/- 6.4) folds than the above two groups; P &lt; 0.05].	Heparin	246-253	CD34 antigen	Mus musculus	9-13
20735427-9	2010	AGEs-induced exocytosis was inhibited by an anti-RAGE antibody and by low molecular weight heparin, a known RAGE antagonist.	Heparin	91-98	long intergenic non-protein coding RNA 914	Homo sapiens	108-112
15664348-3	2005	This heparin-viscose fiber material was used for purifying antithrombin III (AT III) from human plasma.	Heparin	5-12	serpin family C member 1	Homo sapiens	59-75
15457395-11	2004	In case of pre-interventional application of the GP IIb/IIIa receptor inhibitor 22.3 % of patients revealed normal (TIMI-3) flow of the IRA before PCI, compared to 14.9 % TIMI-3 flow with 5000 IE Heparin/500 mg aspirin alone (p &lt; 0.05).	Heparin	196-203	integrin subunit alpha 2b	Homo sapiens	49-55
15664348-3	2005	This heparin-viscose fiber material was used for purifying antithrombin III (AT III) from human plasma.	Heparin	5-12	serpin family C member 1	Homo sapiens	77-83
15726889-6	2004	Studies were also conducted on the effect of the two fucoidans and heparin on the activation of Glu-Plg by t-PA using 0.05M Tris buffer pH 7.4 containing 0.1 M NaCl.	Heparin	67-74	chromosome 20 open reading frame 181	Homo sapiens	107-111
15681103-5	2005	The lipolytic capacity was determined as the change in LPL activity and mass following a bolus dose of 100 IU x kg BW(-1) heparin sodium.	Heparin	122-136	lipoprotein lipase	Homo sapiens	55-58
15109301-0	2004	Octasaccharide is the minimal length unit required for efficient binding of cyclophilin B to heparin and cell surface heparan sulphate.	Heparin	93-100	peptidylprolyl isomerase B	Homo sapiens	76-89
15109301-8	2004	We then demonstrated that heparin-derived octasaccharides and higher degree of polymerization oligosaccharides inhibited the interaction between CyPB and fluorophore-labelled HS chains purified from T-lymphocytes, and strongly reduced the HS-dependent pro-adhesive activity of CyPB.	Heparin	26-33	peptidylprolyl isomerase B	Homo sapiens	145-149
20566960-2	2010	In this study, we investigated the role and mechanisms of kallistatin in inhibiting endothelial inflammation through its heparin-binding domain.	Heparin	121-128	serpin family A member 4	Homo sapiens	58-69
20566960-3	2010	We showed that recombinant wild-type kallistatin dose-dependently competed with tumor necrosis factor (TNF)-alpha binding to TNF-alpha receptor in endothelial cells, whereas kallistatin mutant at the heparin-binding domain had no effect.	Heparin	200-207	serpin family A member 4	Homo sapiens	37-48
20566960-3	2010	We showed that recombinant wild-type kallistatin dose-dependently competed with tumor necrosis factor (TNF)-alpha binding to TNF-alpha receptor in endothelial cells, whereas kallistatin mutant at the heparin-binding domain had no effect.	Heparin	200-207	serpin family A member 4	Homo sapiens	174-185
20566960-4	2010	Kallistatin, but not kallistatin mutant at the heparin-binding domain, abrogated TNF-alpha-induced endothelial cell activation, as evidenced by inhibition of TNF receptor 1-associated death domain protein activation, inhibitor of nuclear factor kappaB-alpha degradation, nuclear factor kappaB translocation, and p38 mitogen-activated protein kinase phosphorylation, as well as cell adhesion molecule and cytokine expression.	Heparin	47-54	serpin family A member 4	Homo sapiens	0-11
20566960-8	2010	These results indicate that kallistatin"s heparin-binding site plays an essential role in preventing TNF-alpha-mediated endothelial activation and reducing vascular endothelial growth factor-induced vascular permeability, resulting in attenuation of vascular inflammation in cultured endothelial cells and animal models.	Heparin	42-49	serpin family A member 4	Homo sapiens	28-39
15109301-8	2004	We then demonstrated that heparin-derived octasaccharides and higher degree of polymerization oligosaccharides inhibited the interaction between CyPB and fluorophore-labelled HS chains purified from T-lymphocytes, and strongly reduced the HS-dependent pro-adhesive activity of CyPB.	Heparin	26-33	peptidylprolyl isomerase B	Homo sapiens	277-281
15681103-9	2005	The heparin-induced rises in LPL activity and LPL mass were similar (n.s.)	Heparin	4-11	lipoprotein lipase	Homo sapiens	29-32
15681103-9	2005	The heparin-induced rises in LPL activity and LPL mass were similar (n.s.)	Heparin	4-11	lipoprotein lipase	Homo sapiens	46-49
15691886-1	2005	Insulin-like growth factor binding proteins (IGFBPs) -3 and -5 are known to interact with various components of the extracellular matrix (ECM; e.g. heparin and heparan sulphate) and this interaction is believed to affect the affinity of both IGFBP species for their cognate ligands--IGF-I and -II.	Heparin	148-155	insulin-like growth factor binding protein 3	Mus musculus	45-51
15333044-10	2004	CONCLUSIONS: These results indicate that the sulfated heparin-like semi-synthetic derivatives K5-OS and K5-N, OS epi are able to inhibit both expression and production of inflammatory cytokines, whereas they do not influence the anti-inflammatory cytokine IL-10, suggesting a potential role for these products as modulators of inflammatory reactions.	Heparin	54-61	interleukin 10	Homo sapiens	256-261
15177934-7	2004	Thus, transactivation of EGFR by NT involved heparin-binding EGF (HB-EGF or amphiregulin) rather than EGF.	Heparin	45-52	amphiregulin	Homo sapiens	76-88
20398703-4	2010	Surface plasmon resonance (SPR) experiments revealed that BSA-Tat-NLS binds to the HSPG analogue heparin.	Heparin	97-104	CD44 molecule (Indian blood group)	Homo sapiens	83-87
19309545-11	2010	In the heparin group, the expressions of endogenous tPA and MMP-9 obviously increased, while their content and activity had significant differences compared with that of the control group (p&lt;0.01).	Heparin	7-14	matrix metallopeptidase 9	Rattus norvegicus	60-65
19309545-12	2010	CONCLUSION: Endogenous tPA, through enhancement of MMP-9 expression and proteolytic activation, plays an important role in the pathogenesis of hemorrhagic transformation after cerebral reperfusion induced by heparin.	Heparin	208-215	matrix metallopeptidase 9	Rattus norvegicus	51-56
19910109-3	2010	When these treated tumors were re-injected into nude mice and treatment with the neutralizing antibody cocktail plus heparin was repeated, the growth of the twice-treated tumors became HGF-independent, suggesting a possible switch in dominant signaling pathways.	Heparin	117-124	hepatocyte growth factor	Mus musculus	185-188
15277203-3	2004	A second goal was to determine whether effects of ECSOD are dependent on the heparin-binding domain of the enzyme, which facilitates binding of ECSOD to the outside of cells.	Heparin	77-84	superoxide dismutase 3	Rattus norvegicus	50-55
15277203-3	2004	A second goal was to determine whether effects of ECSOD are dependent on the heparin-binding domain of the enzyme, which facilitates binding of ECSOD to the outside of cells.	Heparin	77-84	superoxide dismutase 3	Rattus norvegicus	144-149
15249683-8	2004	Digestion of A1A2A3 by plasma ADAMTS13 was enhanced to a similar extent by a recombinant mutant fragment of platelet GPIbalpha that binds with high affinity to domain A1 or by heparin.	Heparin	176-183	glycoprotein Ib platelet subunit alpha	Homo sapiens	117-126
20153045-7	2010	Because heparin is known to bind growth factors, we incorporated hepatocyte growth factor (HGF)-an important liver signaling molecule - into the hydrogel.	Heparin	8-15	hepatocyte growth factor	Rattus norvegicus	65-89
20153045-7	2010	Because heparin is known to bind growth factors, we incorporated hepatocyte growth factor (HGF)-an important liver signaling molecule - into the hydrogel.	Heparin	8-15	hepatocyte growth factor	Rattus norvegicus	91-94
16003952-5	2005	The p-BPB did not reduce significantly the myotoxic activity induced by the PLA2, but the anhydrous acetic acid treatment and the pre-incubation of PLA2 with heparin reduced significantly its effects.	Heparin	158-165	phospholipase A2 group IIA	Gallus gallus	148-152
20153045-8	2010	HGF release from heparin hydrogel matrix was analyzed using enzyme linked immunoassay (ELISA) and was shown to occur in a controlled manner with only 40% of GF molecules released after 30 days in culture.	Heparin	17-24	hepatocyte growth factor	Rattus norvegicus	0-3
19959474-3	2010	The squamous cell carcinoma antigens (serpins B3 and B4) are tumor-associated proteins that can inhibit papain-like cysteine proteases, including cathepsins L, K, and S. In this study, we show that SCCA-1 (B3) and SCCA-2 (B4) can bind heparin as demonstrated by affinity chromatography, native PAGE gel shifts, and intrinsic fluorescence quenching.	Heparin	235-242	immunoglobulin kappa variable 4-1	Homo sapiens	198-209
15183770-6	2004	Heparin immobilized in this way was able to interact with four different heparin-binding proteins tested, i.e., TSG-6, chemokines IL-8 and KC, and complement factor H.	Heparin	0-7	TNF alpha induced protein 6	Homo sapiens	112-117
15183770-6	2004	Heparin immobilized in this way was able to interact with four different heparin-binding proteins tested, i.e., TSG-6, chemokines IL-8 and KC, and complement factor H.	Heparin	0-7	complement factor H	Homo sapiens	130-166
20432946-6	2010	Kal protein was purified from the supernatant with Phenyl Superose and Heparin Sepharose FF chromatograph.	Heparin	71-78	serpin family A member 4	Homo sapiens	0-3
15588892-4	2005	After targeting the complex to the clot site, t-PA activity was restored by administration of protamine, a clinical heparin antidote.	Heparin	116-123	plasminogen activator, tissue type	Rattus norvegicus	46-50
19940140-6	2010	We demonstrated that high N-sulfate density and the presence of 2-O- and 3-O-sulfates determine binding of CyPB, as evidenced by competitive experiments with heparin derivatives, soluble HS, and anti-HS antibodies.	Heparin	158-165	peptidylprolyl isomerase B	Homo sapiens	107-111
16156690-1	2005	Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin.	Heparin	139-146	serpin family C member 1	Homo sapiens	108-120
15478462-5	2004	This model of SAA suggests that proposed binding sites for laminin, fibronectin, and calcium are segregated to one face of the molecule and that the heparin/heparan binding site is found in the putatively disordered region of the protein.	Heparin	149-156	serum amyloid A1 cluster	Homo sapiens	14-17
15096041-7	2004	The weak binding affinity of the FGFR1-heparin interaction suggests that in this model, FGFR and HSPG are unbound in the absence of FGF ligand.	Heparin	39-46	CD44 molecule (Indian blood group)	Homo sapiens	97-101
20423535-2	2010	Several studies show that critically ill patients have significantly lower plasma anti-factor-Xa activity levels compared to control patients after administration of subcutaneous heparin.	Heparin	179-186	coagulation factor X	Homo sapiens	87-96
16474289-4	2005	Prolonged hypothermic extracorporeal circulation and the high intraoperative blood loss (over 35 ml/kg bw) lead to an appreciable decrease in antithrombin III and protein C activity which results in activation of disseminated intravascular blood coagulation in the early postoperative period and ineffectiveness of heparin therapy.	Heparin	315-322	serpin family C member 1	Homo sapiens	142-158
19637375-4	2010	Heparin and fragmin enhanced SCF-induced proliferation of chlorate-treated TF-1 cells, in which the biosynthesis of endogenous sulfated polysaccharides was blocked, on noncoated plates at a range of concentrations (2-8 microg/mL).	Heparin	0-7	KIT ligand	Homo sapiens	29-32
14977886-7	2004	Moreover, unfractionated heparin promoted the antiproliferative effect of FSAP on VSMC and was essential for the inhibition of VSMC migration.	Heparin	25-32	hyaluronan binding protein 2	Homo sapiens	74-78
15819171-4	2005	At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin.	Heparin	15-22	serpin family C member 1	Homo sapiens	33-45
15321411-2	2004	The effects of differences in coagulation status on the action of heparin cannot be measured by specific laboratory tests such as aPTT or anti-Factor Xa assay.	Heparin	66-73	coagulation factor X	Homo sapiens	143-152
19542565-4	2009	ANGPTL4 potently inhibited nonstabilized LPL as well as heparin-stabilized LPL but not GPIHBP1-stabilized LPL.	Heparin	56-63	lipoprotein lipase	Mus musculus	75-78
19542565-4	2009	ANGPTL4 potently inhibited nonstabilized LPL as well as heparin-stabilized LPL but not GPIHBP1-stabilized LPL.	Heparin	56-63	lipoprotein lipase	Mus musculus	75-78
15567452-4	2005	METHODS: We performed a clinical pharmacokinetic trial to compare the variability in peak antithrombin effect between subcutaneous unfractionated heparin and various LMWHs, all given in recommended weight-adjusted treatment doses.	Heparin	146-153	serpin family C member 1	Homo sapiens	90-102
19542565-6	2009	ANGPTL3 also inhibited heparin-stabilized LPL but with less potency than nonstabilized LPL.	Heparin	23-30	lipoprotein lipase	Mus musculus	42-45
19925675-0	2009	Topical recombinant thrombin at a concentration of 1000 IU/mL reliably shortens in vivo TTH and delivers durable hemostasis in the presence of heparin anticoagulation and clopidogrel platelet inhibition in a rabbit model of vascular bleeding.	Heparin	143-150	prothrombin	Oryctolagus cuniculus	20-28
15125370-15	2004	Elevation of cTnI is comparable both in use of unfractionated heparin during PTCA and in use of low-molecular heparin during PTCA.	Heparin	62-69	troponin I3, cardiac type	Homo sapiens	13-17
15738677-7	2005	The negative control polymers showed little to no initial cell attachment, and the addition of soluble heparin to the medium reduced initial cell adhesion on both the HBP2 and HBP2:RGD surfaces.	Heparin	103-110	BBX high mobility group box domain containing	Homo sapiens	167-171
14670838-12	2004	Heparin may inhibit the mitogenic effects of thrombin and FXa in human SMCs by preventing bFGF binding to FGFR-1.	Heparin	0-7	coagulation factor X	Homo sapiens	58-61
23105443-16	2004	The clinical tolerability and the efficacy of low molecular weight heparins has established that inhibition of further thrombin generation, by blocking factor Xa alone can be an effective way of preventing thrombus growth without inactivating thrombin.	Heparin	67-75	coagulation factor X	Homo sapiens	152-161
15570557-0	2004	Evaluation of a chromogenic assay to measure the factor Xa inhibitory activity of unfractionated heparin in canine plasma.	Heparin	97-104	coagulation factor X	Homo sapiens	49-58
15570557-2	2004	Factor Xa inhibitory assays (to measure anti-Xa activity) are used to adjust UFH dosage and define safe and effective regimens for specific thrombotic disorders in humans.	Heparin	77-80	coagulation factor X	Homo sapiens	0-9
14532267-1	2003	We have previously shown that exosites in antithrombin outside the P6-P3" reactive loop region become available upon heparin activation to promote rapid inhibition of the target proteases, factor Xa and factor IXa.	Heparin	117-124	coagulation factor X	Homo sapiens	189-213
14623248-6	2003	Treatment of cells with high salt, protamine, heparin, or suramin released significant VEGF, suggesting that heparan sulfate proteoglycan might be sequestering some of the VEGF.	Heparin	46-53	vascular endothelial growth factor A	Mus musculus	87-91
14623248-6	2003	Treatment of cells with high salt, protamine, heparin, or suramin released significant VEGF, suggesting that heparan sulfate proteoglycan might be sequestering some of the VEGF.	Heparin	46-53	vascular endothelial growth factor A	Mus musculus	172-176
19540231-16	2009	Heparin abolished responses to Vn, IGFBP-5 and non-glycosylated IGFBP-3, but only partially inhibited the response to glycosylated IGFBP-3.	Heparin	0-7	vitronectin	Homo sapiens	31-33
20137277-11	2009	The P(alb), TNF-alpha, IL-6 and vWF of heparin treatment group were (0.28 +/- 0.04), (1.92 +/- 0.35) microg/L, (1.22 +/- 0.13) ng/ml and (24.9 +/- 4.0) U/L respectively.	Heparin	39-46	von Willebrand factor	Rattus norvegicus	32-35
19893601-7	2009	VEGF-A165 possessing a heparin-binding domain showed a pattern of heparin-dependent angiogenic activity similar to that of HMGB1.	Heparin	23-30	vascular endothelial growth factor A	Mus musculus	0-6
19555665-0	2009	NKG2D and CD94 bind to heparin and sulfate-containing polysaccharides.	Heparin	23-30	killer cell lectin like receptor D1	Homo sapiens	10-14
19555665-6	2009	Mutagenesis revealed that (152)Y and (199)Y of NKG2D and (144)F, (160)N, and (166)C of CD94 were critical for binding to heparin-BSA.	Heparin	121-128	killer cell lectin like receptor D1	Homo sapiens	87-91
19555665-7	2009	The present manuscript provides the first evidence that NKG2D and CD94 bind to heparin and sulfate-containing polysaccharides.	Heparin	79-86	killer cell lectin like receptor D1	Homo sapiens	66-70
19415899-3	2009	The relative heparin-binding affinity of recombinant laminin alpha chain LG45 proteins was as follows: alpha5 &gt; alpha4 &gt; alpha1 &gt; alpha2 and alpha3.	Heparin	13-20	immunoglobulin binding protein 1	Homo sapiens	115-121
19461929-5	2009	METHODS: The neural retina was surgically removed from Xenopus laevis tadpoles at stages 51-54, and a heparin-coated bead soaked in fibroblast growth factor 2 (FGF-2) was introduced in the eyes to induce regeneration.	Heparin	102-109	fibroblast growth factor 2 L homeolog	Xenopus laevis	132-158
19461929-5	2009	METHODS: The neural retina was surgically removed from Xenopus laevis tadpoles at stages 51-54, and a heparin-coated bead soaked in fibroblast growth factor 2 (FGF-2) was introduced in the eyes to induce regeneration.	Heparin	102-109	fibroblast growth factor 2 L homeolog	Xenopus laevis	160-165
15738677-7	2005	The negative control polymers showed little to no initial cell attachment, and the addition of soluble heparin to the medium reduced initial cell adhesion on both the HBP2 and HBP2:RGD surfaces.	Heparin	103-110	BBX high mobility group box domain containing	Homo sapiens	176-180
14575696-4	2003	To shed light on the mechanism of PF4, studies of HS/heparin-catalyzed fXa inactivation by AT were undertaken.	Heparin	53-60	coagulation factor X	Homo sapiens	71-74
15557365-9	2004	Neutralizing HB-EGF antibodies or heparin treatment to sequester HB-EGF resulted in significant inhibition of pressure-induced MT.	Heparin	34-41	heparin-binding EGF-like growth factor	Mus musculus	65-71
14511765-1	2003	In the blood coagulation cascade, human antithrombin III (hAT III) acts as an inhibitor of serine proteases such as thrombin and factor Xa, and this anticoagulatory glycoprotein requires the binding of heparin for its activation.	Heparin	202-209	coagulation factor X	Homo sapiens	129-138
14517701-11	2003	Pig factor H has two major binding sites for heparin, as the two constructs representing SCR 1-7 and SCR 15-20 proteins, but not the SCR 1-4 protein, bind heparin.	Heparin	45-52	complement factor H	Homo sapiens	4-12
14517701-11	2003	Pig factor H has two major binding sites for heparin, as the two constructs representing SCR 1-7 and SCR 15-20 proteins, but not the SCR 1-4 protein, bind heparin.	Heparin	155-162	complement factor H	Homo sapiens	4-12
19127344-6	2009	Inhibition of HGF binding to heparin by protamine was confirmed using heparin-coated sepharose.	Heparin	29-36	hepatocyte growth factor	Rattus norvegicus	14-17
19127344-8	2009	CONCLUSION: The enhancing effect of protamine on the mitogenic activity of HGF on hepatocytes requires pretreatment with protamine for a short period presumably required for its binding to cell-surface heparin, implying possible regulation of c-met autophosphorylation by HSPG.	Heparin	202-209	hepatocyte growth factor	Rattus norvegicus	75-78
15480797-6	2004	KGF treatment alone at doses less than 500 ng/ml did not induce permanent vaginal changes but such changes did occur in vaginae treated with heparin plus as little as 10 ng/ml KGF.	Heparin	141-148	fibroblast growth factor 7	Mus musculus	0-3
19074504-1	2009	Binding affinities of chemically modified heparins for human stem cell factor (SCF) were examined using fragmin/protamine microparticles (F/P MPs) and an enzyme-linked immunosorbent assay (ELISA).	Heparin	42-50	KIT ligand	Homo sapiens	61-77
19074504-1	2009	Binding affinities of chemically modified heparins for human stem cell factor (SCF) were examined using fragmin/protamine microparticles (F/P MPs) and an enzyme-linked immunosorbent assay (ELISA).	Heparin	42-50	KIT ligand	Homo sapiens	79-82
19074504-2	2009	The binding of SCF to F/P MP-coated plates was inhibited with high concentrations of heparin and fragmin, but not others.	Heparin	85-92	KIT ligand	Homo sapiens	15-18
12941037-4	2003	In buffer, heparin and SanOrg123781A inhibited FXa and thrombin at similar concentrations [concentration inhibiting 50% (IC50) of Xa and IIa activity were, respectively: heparin 120 +/- 7 and 3 +/- 1 ng mL-1; SanOrg123781A 77 +/- 5 and 4 +/- 1 ng mL-1].	Heparin	11-18	coagulation factor X	Homo sapiens	47-50
12941037-4	2003	In buffer, heparin and SanOrg123781A inhibited FXa and thrombin at similar concentrations [concentration inhibiting 50% (IC50) of Xa and IIa activity were, respectively: heparin 120 +/- 7 and 3 +/- 1 ng mL-1; SanOrg123781A 77 +/- 5 and 4 +/- 1 ng mL-1].	Heparin	170-177	coagulation factor X	Homo sapiens	47-50
12941037-7	2003	We showed that heparin and SanOrg123781A were able to inhibit fragment F1+2 generation induced by clot-bound FXa with IC50 values of 2 +/- 0.5 micro g mL-1 and 0.6 +/- 0.2 micro g mL-1, respectively.	Heparin	15-22	coagulation factor X	Homo sapiens	109-112
12810718-7	2003	We also find no evidence for an interaction between DCC and heparin and instead demonstrate that a loop on the fifth fibronectin type III repeat of DCC previously implicated in mediating interactions with heparin is important for sNetrin binding.	Heparin	205-212	DCC netrin 1 receptor	Homo sapiens	148-151
12810718-8	2003	Since netrin binds heparin, our results suggest that interactions between DCC and heparin are probably mediated by netrin.	Heparin	19-26	DCC netrin 1 receptor	Homo sapiens	74-77
12810718-8	2003	Since netrin binds heparin, our results suggest that interactions between DCC and heparin are probably mediated by netrin.	Heparin	82-89	DCC netrin 1 receptor	Homo sapiens	74-77
12773530-11	2003	This phenotype, as well as the location of the disulfide bridges between the serpin and the non-serpin domain of C1-Inh, suggests that the function of the N-terminal region may be similar to one of the effects of heparin in antithrombin III, maintenance of the metastable serpin conformation.	Heparin	213-220	serpin family G member 1	Homo sapiens	113-119
19173304-7	2009	CLEC3A has a basic sequence in the NH(2)-terminal domain and showed a strong heparin-binding activity.	Heparin	77-84	C-type lectin domain family 3 member A	Homo sapiens	0-6
19178150-0	2009	Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor.	Heparin	22-29	serpin family G member 1	Homo sapiens	173-185
19178150-0	2009	Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor.	Heparin	95-102	serpin family G member 1	Homo sapiens	173-185
19178150-1	2009	Heparin accelerates inhibition of factor XIa (fXIa) by the serpins antithrombin (AT) and C1-inhibitor (C1-INH) by more than 2 orders of magnitude.	Heparin	0-7	serpin family G member 1	Homo sapiens	89-101
19178150-1	2009	Heparin accelerates inhibition of factor XIa (fXIa) by the serpins antithrombin (AT) and C1-inhibitor (C1-INH) by more than 2 orders of magnitude.	Heparin	0-7	serpin family G member 1	Homo sapiens	103-109
19178150-5	2009	In reactions with C1-INH, Arg-171 was the most critical residue contributing approximately 2-3-fold to heparin-mediated inhibition of CD-WT.	Heparin	103-110	serpin family G member 1	Homo sapiens	18-24
19178150-9	2009	These results suggest that basic residues of the fXIa 170 loop form a heparin-binding site and that the accelerating effect of heparin on inhibition of fXIa by AT or C1-INH may be mediated by charge neutralization and/or allosteric mechanisms that overcome the repulsive inhibitory interactions of serpins with basic residues on the fXIa 148 and 37 loops.	Heparin	127-134	serpin family G member 1	Homo sapiens	166-172
12799194-4	2003	In contrast, for phospholipase Cgamma(1) (PLCgamma(1)) and the adaptor molecule Shb to be maximally tyrosine-phosphorylated, cells had to be stimulated with both FGF-2 and heparin (100 ng/ml).	Heparin	172-179	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1	Cricetulus griseus	17-40
12871328-1	2003	Antithrombin and its cofactor, heparin, target both the product of prothrombin activation by prothrombinase, thrombin, as well as the enzyme responsible for the reaction, factor (F)Xa.	Heparin	31-38	coagulation factor X	Homo sapiens	93-107
15253930-1	2004	Heparan sulfate/heparin N-deacetylase/N-sulfotransferase-1 (NDST-1) is a critical enzyme involved in heparan sulfate/heparin biosynthesis.	Heparin	16-23	N-deacetylase and N-sulfotransferase 1	Rattus norvegicus	60-66
12871328-9	2003	Therefore, in the presence of unfractionated heparin, fondaparinux, or enoxaparin, prothrombinase is profoundly protected from antithrombin.	Heparin	45-52	coagulation factor X	Homo sapiens	83-97
12948833-1	2003	In the blood coagulation cascade, heparin activates human plasma antithrombin III (hAT III), resulting in the inhibition of factor Xa.	Heparin	34-41	coagulation factor X	Homo sapiens	124-133
19219378-2	2009	The fact that the N-terminal domain of TSP-1 (heparin-binding domain or HBD) is recognized by a plethora of cell receptors, all of them engaged in proangiogenic responses, strongly suggests that the proteolytic cleavage of HBD may be relevant in certain pathophysiological conditions.	Heparin	46-53	HBD	Homo sapiens	72-75
15253930-1	2004	Heparan sulfate/heparin N-deacetylase/N-sulfotransferase-1 (NDST-1) is a critical enzyme involved in heparan sulfate/heparin biosynthesis.	Heparin	117-124	N-deacetylase and N-sulfotransferase 1	Rattus norvegicus	60-66
19219378-2	2009	The fact that the N-terminal domain of TSP-1 (heparin-binding domain or HBD) is recognized by a plethora of cell receptors, all of them engaged in proangiogenic responses, strongly suggests that the proteolytic cleavage of HBD may be relevant in certain pathophysiological conditions.	Heparin	46-53	HBD	Homo sapiens	223-226
15527497-0	2004	Lipoprotein lipase in hemodialysis patients: indications that low molecular weight heparin depletes functional stores, despite low plasma levels of the enzyme.	Heparin	83-90	lipoprotein lipase	Homo sapiens	0-18
19140680-0	2009	Heparin enhances the inhibition of factor Xa by protein C inhibitor in the presence but not in the absence of Ca2+.	Heparin	0-7	coagulation factor X	Homo sapiens	35-44
19140680-3	2009	In this study, heparin was found to enhance PCI inhibition of factor Xa up to 42-fold in the presence of a physiological Ca(2+) concentration, whereas no heparin-induced activation was observed in the absence of Ca(2+).	Heparin	15-22	coagulation factor X	Homo sapiens	62-71
12729931-2	2003	A similar procedure for isolation of Cyt b directly from intact neutrophils by a combination of heparin and immunoaffinity chromatography is also presented.	Heparin	96-103	mitochondrially encoded cytochrome b	Homo sapiens	37-42
19140680-4	2009	These results thus show that factor Xa adds to the group of proteases whose inhibition by PCI is enhanced by heparin and that such inhibition contributes to the anticoagulant properties of PCI by a Ca(2+)-dependent mechanism.	Heparin	109-116	coagulation factor X	Homo sapiens	29-38
12947723-0	2003	[Factor Xa inhibitory assay to detect plasma heparin concentrations during and after cardiopulmonary bypass].	Heparin	45-52	coagulation factor X	Homo sapiens	1-10
15527497-3	2004	When heparin is infused, there is a peak of LPL activity accompanied by a reduction in triglycerides (TG) during the first hour, followed by a decrease in LPL activity to a stable plateau during the remaining session while TG increase towards and beyond baseline.	Heparin	5-12	lipoprotein lipase	Homo sapiens	44-47
19196184-9	2009	We further show the relevance of synthetic HS/heparin for the binding of NCRs to tumor cells and for NCR-mediated activation of natural killer cells.	Heparin	46-53	Neutrophil migration (granulocyte glycoprotein)	Homo sapiens	73-76
15527497-3	2004	When heparin is infused, there is a peak of LPL activity accompanied by a reduction in triglycerides (TG) during the first hour, followed by a decrease in LPL activity to a stable plateau during the remaining session while TG increase towards and beyond baseline.	Heparin	5-12	lipoprotein lipase	Homo sapiens	155-158
15527497-5	2004	It has been argued that low molecular weight (LMW) heparins cause less disturbance of the LPL system than conventional heparin does.	Heparin	51-59	lipoprotein lipase	Homo sapiens	90-93
12678189-8	2003	During medication with GP IIb/IIIa inhibitor, the patients received a reduced heparin dosage for 24 hours.	Heparin	78-85	integrin subunit alpha 2b	Homo sapiens	23-29
15527497-5	2004	It has been argued that low molecular weight (LMW) heparins cause less disturbance of the LPL system than conventional heparin does.	Heparin	51-58	lipoprotein lipase	Homo sapiens	90-93
19109427-3	2009	We compared the inhibitory effects of two adhesion modulatory proteins, fibulin-1 and tenascin-C, both of which bind to the C-terminal heparin-binding (HepII) domain of fibronectin (FN) but are structurally distinct.	Heparin	135-142	tenascin C	Homo sapiens	86-96
15527497-7	2004	RESULTS: The shape of the curve for LPL activity resembled that during the earlier dialyses with conventional heparin, but the values were lower during dialysis with dalteparin.	Heparin	110-117	lipoprotein lipase	Homo sapiens	36-39
18835636-8	2009	Incubation with 10 and 20 microg/mL OPN produced more (P&lt;0.01) capacitated sperm (14.4 and 13.6%, respectively) than the untreated control group (8.3%), but both untreated sperm and those treated with OPN had significantly fewer capacitated sperm than those treated with 0.01 mM of heparin (30.5%).	Heparin	285-292	secreted phosphoprotein 1	Bos taurus	36-39
19010776-1	2009	We have previously shown that residues Tyr-253 and Glu-255 in the serpin antithrombin function as exosites to promote the inhibition of factor Xa and factor IXa when the serpin is conformationally activated by heparin.	Heparin	210-217	coagulation factor X	Homo sapiens	136-160
12612134-9	2003	In mice, CLA-induced inhibition of heparin-releasable LPL and glucose metabolism may be the most important early steps leading to subsequent body fat reduction.	Heparin	35-42	lipoprotein lipase	Mus musculus	54-57
12659638-0	2003	A heparin binding synthetic peptide from human HIP / RPL29 fails to specifically differentiate between anticoagulantly active and inactive species of heparin.	Heparin	2-9	ribosomal protein L29	Homo sapiens	53-58
19013448-4	2009	Heparin, which is known to translocate PACE4 in the extracellular matrix into the medium, and an antibody specific for the catalytic domain of PACE4, both reduced the branching morphogenesis and AQP5 expression in the SMG.	Heparin	0-7	aquaporin 5	Rattus norvegicus	195-199
15527497-13	2004	CONCLUSION: These results indicate that LMW heparins disturb the LPL system as much or more than conventional heparin does.	Heparin	44-52	lipoprotein lipase	Homo sapiens	65-68
15527497-13	2004	CONCLUSION: These results indicate that LMW heparins disturb the LPL system as much or more than conventional heparin does.	Heparin	44-51	lipoprotein lipase	Homo sapiens	65-68
15298984-4	2004	EC-SOD is found in high levels in the extracellular matrix of lung alveoli because of its positively charged heparin-binding domain.	Heparin	109-116	superoxide dismutase 3, extracellular	Mus musculus	0-6
18990693-9	2009	Molecular modeling shows a structural disruption in the region of RCP that corresponds to the KCP-heparin-binding site.	Heparin	98-105	kielin cysteine rich BMP regulator	Homo sapiens	94-97
14728074-12	2003	CONCLUSION: The GP IIb/IIIa receptor antagonist abciximab, when used with aspirin and heparin, has demonstrated efficacy in reducing the short- and long-term risk of ischemic complications in patients with ischemic heart disease undergoing percutaneous coronary intervention, when used with aspirin and heparin.	Heparin	86-93	integrin subunit alpha 2b	Homo sapiens	16-22
14728074-12	2003	CONCLUSION: The GP IIb/IIIa receptor antagonist abciximab, when used with aspirin and heparin, has demonstrated efficacy in reducing the short- and long-term risk of ischemic complications in patients with ischemic heart disease undergoing percutaneous coronary intervention, when used with aspirin and heparin.	Heparin	303-310	integrin subunit alpha 2b	Homo sapiens	16-22
15298984-9	2004	The EC-SOD in the BALF was predominantly in the proteolyzed form, which lacks the heparin-binding domain.	Heparin	82-89	superoxide dismutase 3, extracellular	Mus musculus	4-10
14529393-4	2003	Despite of the success of intravenous acute GPIIb/IIIa blockade when given in conjunction with heparin, chronic oral GPIIb/IIIa antagonists with or without aspirin failed in various cardiovascular settings.	Heparin	95-102	integrin subunit alpha 2b	Homo sapiens	44-49
20339323-0	2009	Effects of nadroparin, enoxaparin, and unfractionated heparin on endogenous factor Xa and IIa formation and on thrombelastometry profiles.	Heparin	54-61	coagulation factor X	Homo sapiens	76-85
15570242-4	2004	In this study we sought to investigate the time- and dose-dependent relationships between release of TFPI and lipoprotein lipase (LPL) in respons to UFH and LMWH and to investigate whether the selective depletion of TFPI by UFH but not by LMWH is related to differential urinary excretion of TFPI.	Heparin	149-152	lipoprotein lipase	Homo sapiens	110-128
20339323-1	2009	Measurements of anti-FXa or anti-FIIa (thrombin) activities are conventional tests for biological monitoring of low molecular weight heparin (LMWH) or unfractionated heparin treatment.	Heparin	133-140	coagulation factor X	Homo sapiens	21-24
15570242-4	2004	In this study we sought to investigate the time- and dose-dependent relationships between release of TFPI and lipoprotein lipase (LPL) in respons to UFH and LMWH and to investigate whether the selective depletion of TFPI by UFH but not by LMWH is related to differential urinary excretion of TFPI.	Heparin	149-152	lipoprotein lipase	Homo sapiens	130-133
20339323-3	2009	The effects of increasing amounts of nadroparin, enoxaparin, or unfractionated heparin on the time-course of FXa or FIIa formation were investigated in tissue factor activated platelet-poor plasma using a subsampling technique and chromogenic substrates.	Heparin	79-86	coagulation factor X	Homo sapiens	109-112
15496673-5	2004	Enzymatic removal of heparan sulfates from cultured neurons and a mutation in the heparin-binding domain of NCAM diminished synaptogenic activity of neuronally expressed PSA-NCAM, suggesting that interaction of NCAM with heparan sulfate proteoglycans mediates this activity.	Heparin	82-89	neural cell adhesion molecule 1	Homo sapiens	108-112
20339323-7	2009	Compared with equivalent anti-FXa activity, unfractionated heparin is markedly more efficient in suppressing the formation of FXa and FIIa than the LMWHs.	Heparin	59-66	coagulation factor X	Homo sapiens	126-129
14533856-3	2003	This study shows a material-dependent increase of hsp70 levels in plasma following contact of fresh heparinized whole human blood with three different biomaterials (PVC, heparin-coated PVC, Silicone).	Heparin	100-107	heat shock protein family A (Hsp70) member 4	Homo sapiens	50-55
12540961-2	2003	Here, the anti-fXa and anti-prothrombinase activities of DX-9065a which is an active-site directed inhibitor of fXa, and therapeutic heparins which are dependent on antithrombin (AT) for their anticoagulant function, were studied in amidolytic and proteolytic activity assays.	Heparin	133-141	coagulation factor X	Homo sapiens	28-42
15496673-5	2004	Enzymatic removal of heparan sulfates from cultured neurons and a mutation in the heparin-binding domain of NCAM diminished synaptogenic activity of neuronally expressed PSA-NCAM, suggesting that interaction of NCAM with heparan sulfate proteoglycans mediates this activity.	Heparin	82-89	neural cell adhesion molecule 1	Homo sapiens	174-178
12475226-0	2002	A kinetics and modeling study of RANTES(9-68) binding to heparin reveals a mechanism of cooperative oligomerization.	Heparin	57-64	C-C motif chemokine ligand 5	Homo sapiens	33-39
18983497-6	2009	This activity required the heparin-binding domain of Bev"s target, vascular endothelial growth factor (VEGF).	Heparin	27-34	vascular endothelial growth factor A	Mus musculus	67-101
18983497-6	2009	This activity required the heparin-binding domain of Bev"s target, vascular endothelial growth factor (VEGF).	Heparin	27-34	vascular endothelial growth factor A	Mus musculus	103-107
15496673-5	2004	Enzymatic removal of heparan sulfates from cultured neurons and a mutation in the heparin-binding domain of NCAM diminished synaptogenic activity of neuronally expressed PSA-NCAM, suggesting that interaction of NCAM with heparan sulfate proteoglycans mediates this activity.	Heparin	82-89	neural cell adhesion molecule 1	Homo sapiens	174-178
18845532-6	2008	Indeed, plasma LPL levels peaked very rapidly (within 1 min) after heparin in control mice.	Heparin	67-74	lipoprotein lipase	Mus musculus	15-18
18845532-7	2008	In contrast, plasma LPL levels in Gpihbp1(-/-) mice were much lower 1 min after heparin and increased slowly over 15 min.	Heparin	80-87	lipoprotein lipase	Mus musculus	20-23
18845532-11	2008	The differences in LPL release after intravenous heparin and Intralipid strongly suggest that GPIHBP1 represents an important binding site for LPL in vivo.	Heparin	49-56	lipoprotein lipase	Mus musculus	19-22
18845532-11	2008	The differences in LPL release after intravenous heparin and Intralipid strongly suggest that GPIHBP1 represents an important binding site for LPL in vivo.	Heparin	49-56	lipoprotein lipase	Mus musculus	143-146
12475226-3	2002	In the study presented here, we analyzed the binding of heparin to RANTES(9-68), a N-terminally truncated form of the CC-chemokine RANTES.	Heparin	56-63	C-C motif chemokine ligand 5	Homo sapiens	67-73
12475226-3	2002	In the study presented here, we analyzed the binding of heparin to RANTES(9-68), a N-terminally truncated form of the CC-chemokine RANTES.	Heparin	56-63	C-C motif chemokine ligand 5	Homo sapiens	131-137
12475226-4	2002	Using biochemical and surface plasmon resonance (BIAcore system) approaches, we showed that the RANTES(9-68)-heparin interaction was characterized by a complex binding model that involved dimerization of the chemokine through a mechanism of positive cooperativity.	Heparin	109-116	C-C motif chemokine ligand 5	Homo sapiens	96-102
12475226-5	2002	Since RANTES(9-68) remains monomeric in solution, we concluded that heparin induced chemokine dimerization.	Heparin	68-75	C-C motif chemokine ligand 5	Homo sapiens	6-12
12475226-8	2002	This engineered oligosaccharide bound RANTES(9-68) much better than a natural heparin fragment of the same length, further supporting the interaction process and the proposed structural model.	Heparin	78-85	C-C motif chemokine ligand 5	Homo sapiens	38-44
18926810-5	2008	MMP-9 and TIMP-2 expression were strongly affected by heparin, with significant increase of their content and gelatinolytic activity both in time- and in dose-dependent fashion.	Heparin	54-61	matrix metallopeptidase 9	Homo sapiens	0-5
18926810-5	2008	MMP-9 and TIMP-2 expression were strongly affected by heparin, with significant increase of their content and gelatinolytic activity both in time- and in dose-dependent fashion.	Heparin	54-61	TIMP metallopeptidase inhibitor 2	Homo sapiens	10-16
15234978-4	2004	Both surface plasmon resonance analysis and enzyme-linked immunosorbent assay revealed that MDP1 bound to HA, heparin, and chondroitin sulfate.	Heparin	110-117	magnesium dependent phosphatase 1	Homo sapiens	92-96
18926810-7	2008	CONCLUSIONS: Heparin has direct and indirect effects, altering MMP/TIMP complexes circulating in blood, and increasing the release of TIMP-2.	Heparin	13-20	TIMP metallopeptidase inhibitor 2	Homo sapiens	134-140
18645041-8	2008	However, deimination decreased heparin binding properties of both CXCL10 and CXCL11.	Heparin	31-38	C-X-C motif chemokine ligand 10	Homo sapiens	66-72
18645041-8	2008	However, deimination decreased heparin binding properties of both CXCL10 and CXCL11.	Heparin	31-38	C-X-C motif chemokine ligand 11	Homo sapiens	77-83
12473563-1	2002	BACKGROUND: Plasma concentrations of hepatocyte growth factor (HGF), a powerful angiogenic growth factor inducible by heparin, increase in thrombus-associated disorders such as myocardial infarction and unstable angina.	Heparin	118-125	hepatocyte growth factor	Rattus norvegicus	37-61
12473563-1	2002	BACKGROUND: Plasma concentrations of hepatocyte growth factor (HGF), a powerful angiogenic growth factor inducible by heparin, increase in thrombus-associated disorders such as myocardial infarction and unstable angina.	Heparin	118-125	hepatocyte growth factor	Rattus norvegicus	63-66
12473563-7	2002	Intravenous heparin immediately increased plasma HGF in both Wistar (38.02+/-2.08 ng/mL versus 1.11+/-0.70 ng/mL in untreated rats, P&lt;0.0001) and Ws rats (36.39+/-4.15 ng/mL versus 0.66+/-0.18 ng/mL in NS-treated rats, P&lt;0.0001).	Heparin	12-19	hepatocyte growth factor	Rattus norvegicus	49-52
15234978-5	2004	Utilizing synthetic peptides, we next defined heparin-binding site of 20 amino acids from 31 to 50 of MDP1, which is responsible for the specific DNA-binding site of MDP1.	Heparin	46-53	magnesium dependent phosphatase 1	Homo sapiens	102-106
12478357-7	2002	Heparin anticoagulation may be ineffective because the rate of coagulation that occurs on the surfaces of dysfunctional endothelial surfaces exceeds the capacity of heparin/antithrombin-III inhibitor complexes to bind and block the factor Xa and thrombin that are generated on these surfaces.	Heparin	0-7	coagulation factor X	Homo sapiens	232-241
15234978-5	2004	Utilizing synthetic peptides, we next defined heparin-binding site of 20 amino acids from 31 to 50 of MDP1, which is responsible for the specific DNA-binding site of MDP1.	Heparin	46-53	magnesium dependent phosphatase 1	Homo sapiens	166-170
15231514-1	2004	Heparin is a major anticoagulant with activity mediated primarily through its interaction with antithrombin (AT).	Heparin	0-7	serpin family C member 1	Homo sapiens	95-107
12440956-7	2002	These particular domains are conserved in all FHRs identified so far, include contact points for C3b, heparin and microbial surface proteins and represent a "hot-spot" for gene mutations in patients that suffer from the Factor H-associated form of haemolytic uraemic syndrome.	Heparin	102-109	complement factor H	Homo sapiens	220-228
18941937-1	2008	We report a case of cerebral venous thrombosis (CVT) due to tyrotoxicosis in a patient with methylenetetrahydro-folate-reductase (MTHFR) gene polymorphism C677T, (genotype 677TT), in which discontinuation of intravenous heparin was followed by clinical and radiological worsening despite warfarin treatment.	Heparin	220-227	methylenetetrahydrofolate reductase	Homo sapiens	92-128
18941937-1	2008	We report a case of cerebral venous thrombosis (CVT) due to tyrotoxicosis in a patient with methylenetetrahydro-folate-reductase (MTHFR) gene polymorphism C677T, (genotype 677TT), in which discontinuation of intravenous heparin was followed by clinical and radiological worsening despite warfarin treatment.	Heparin	220-227	methylenetetrahydrofolate reductase	Homo sapiens	130-135
18766266-8	2008	Furthermore, thrombin-induced NO production, as assessed with DAF-2 fluorescence, was suppressed in heparinase III-treated BAECs and by the pre-incubation of thrombin with heparin.	Heparin	100-107	coagulation factor II, thrombin	Bos taurus	13-21
18585707-7	2008	Interestingly, heparin was able to reduce the binding of LTBP-4 to FN.	Heparin	15-22	latent transforming growth factor beta binding protein 4	Homo sapiens	57-63
12391246-4	2002	Fucoidin, heparin/heparin sulfate, N-acetyl-D-glucosamine, mannose-6-phosphate, and laminarin were found to inhibit adhesion of T84 cells to CD11b/CD18.	Heparin	10-17	integrin subunit alpha M	Homo sapiens	141-146
15302778-1	2004	BACKGROUND: Unfractionated heparin (UFH) is the most widely used antithrombin during percutaneous coronary intervention (PCI).	Heparin	27-34	serpin family C member 1	Homo sapiens	65-77
12371960-8	2002	Cyr61 protein was analyzed by capture with heparin beads followed by Western blotting.	Heparin	43-50	cellular communication network factor 1	Rattus norvegicus	0-5
18411283-6	2008	Moreover, CXCL11-(5-73) is a CXCR3 antagonist and interestingly shows enhanced affinity to heparin.	Heparin	91-98	C-X-C motif chemokine ligand 11	Homo sapiens	10-16
15302778-1	2004	BACKGROUND: Unfractionated heparin (UFH) is the most widely used antithrombin during percutaneous coronary intervention (PCI).	Heparin	36-39	serpin family C member 1	Homo sapiens	65-77
15177934-7	2004	Thus, transactivation of EGFR by NT involved heparin-binding EGF (HB-EGF or amphiregulin) rather than EGF.	Heparin	45-52	heparin binding EGF like growth factor	Homo sapiens	66-72
18359766-0	2008	Structural and functional analysis of slit and heparin binding to immunoglobulin-like domains 1 and 2 of Drosophila Robo.	Heparin	47-54	roundabout 1	Drosophila melanogaster	116-120
18359766-6	2008	Mutation of conserved basic residues in IG1 (Lys-69, Arg-117, Lys-122, Lys-123), but not in IG2, reduced binding of Robo IG1-5 to heparin, in full agreement with the Robo-heparin co-crystal structure.	Heparin	130-137	roundabout 1	Drosophila melanogaster	116-120
18540049-2	2008	Sucrose octasulfate (SOS), a chemical analogue of heparin, has been demonstrated to activate FGF signalling pathways.	Heparin	50-57	fibroblast growth factor 1	Rattus norvegicus	93-96
12351884-1	2002	Crystals of RANTES (regulated on activation normal T-cell expressed) have been grown in the presence of heparin-derived sulphated oligosaccharides which cause RANTES to aggregate severely.	Heparin	104-111	C-C motif chemokine ligand 5	Homo sapiens	12-18
12351884-1	2002	Crystals of RANTES (regulated on activation normal T-cell expressed) have been grown in the presence of heparin-derived sulphated oligosaccharides which cause RANTES to aggregate severely.	Heparin	104-111	C-C motif chemokine ligand 5	Homo sapiens	159-165
12239166-8	2002	Heparin was also found to enhance IL-11"s ability to induce the expression of both receptor activator of nuclear factor-kappaB ligand (RANKL) and glycoprotein (gp) 130.	Heparin	0-7	interleukin 11	Mus musculus	34-39
12357044-6	2002	BSSL bound avidly to rat intestinal microvesicle membranes and the binding was inhibited by addition of free heparin or heparin fragments.	Heparin	109-116	carboxyl ester lipase	Rattus norvegicus	0-4
12357044-6	2002	BSSL bound avidly to rat intestinal microvesicle membranes and the binding was inhibited by addition of free heparin or heparin fragments.	Heparin	120-127	carboxyl ester lipase	Rattus norvegicus	0-4
12451678-4	2002	Moreover, inhibitors of LPL and HTL induce almost complete reduction of increased LIP activity in post-heparin serum as measured by enzymatic assays.	Heparin	103-110	SMG1 nonsense mediated mRNA decay associated PI3K related kinase	Homo sapiens	82-85
15194626-11	2004	The addition of antithrombin (0.2 units/ml) to heparinized blood samples further prolonged ACTs, but the difference was not statistically significant when compared with heparin alone.	Heparin	47-54	serpin family C member 1	Homo sapiens	16-28
12238925-10	2002	A molecular docking study suggests plausible binding of CS in the extended heparin binding site, which is adjacent to the binding domain for the reference trisaccharide DEF.	Heparin	75-82	UTP25 small subunit processome component	Homo sapiens	169-172
18215125-13	2008	Recombinant neurobin processed 17-kDa FGF-2 (fibroblast growth factor-2) at several P(1) lysine and arginine positions to distinct fragments, in a heparin-inhibitable manner, but did not cleave FGF-7, laminin or fibronectin.	Heparin	147-154	transmembrane protease, serine 11c	Mus musculus	12-20
18325345-5	2008	NaPaC completely inhibited the heparin binding to VEGF165, NRP-1 and VEGFR2.	Heparin	31-38	kinase insert domain receptor	Homo sapiens	69-75
18325345-7	2008	These results suggested that heparin binding sites of VEGFR2 and NRP-1 were different from those of VEGF165.	Heparin	29-36	kinase insert domain receptor	Homo sapiens	54-60
15246840-8	2004	Interestingly, the addition of heparin to EGF neurospheres, which had no effects on EGF stability or growth rates, increased the numbers of neurons generated to that seen for FGF-2/heparin neurospheres.	Heparin	31-38	epidermal growth factor	Homo sapiens	42-45
12204897-7	2002	Total protein, cell number, and FGF-2 protein expression and mRNA of FGF-1, -2, and FGF receptor-2 detected by reverse transcriptase-polymerase chain reaction were decreased by heparin.	Heparin	177-184	fibroblast growth factor 1	Rattus norvegicus	69-74
15246840-8	2004	Interestingly, the addition of heparin to EGF neurospheres, which had no effects on EGF stability or growth rates, increased the numbers of neurons generated to that seen for FGF-2/heparin neurospheres.	Heparin	181-188	epidermal growth factor	Homo sapiens	42-45
18156656-2	2008	Unlike heparin it does not interact with other coagulation factors and is able to inhibit thrombin associated with clots.	Heparin	7-14	coagulation factor II, thrombin	Bos taurus	90-98
15262930-1	2004	ShdA is a large outer membrane protein of the autotransporter family whose passenger domain binds the extracellular matrix proteins fibronectin and collagen I, possibly by mimicking the host ligand heparin.	Heparin	198-205	fibronectin 1	Bos taurus	132-143
18327406-9	2008	In contrast, in the presence of LBP, both UFH and LMWH demonstrated dose-dependent pro-inflammatory effects at all heparin concentrations.	Heparin	42-45	lipopolysaccharide binding protein	Homo sapiens	32-35
18327406-9	2008	In contrast, in the presence of LBP, both UFH and LMWH demonstrated dose-dependent pro-inflammatory effects at all heparin concentrations.	Heparin	115-122	lipopolysaccharide binding protein	Homo sapiens	32-35
12000310-6	2002	The CD spectra of the heparin-HC2 peptide complex did not show any significant alpha-helix content, different from the situation with peptide AT3D, for which complex-formation with heparin resulted in 24% alpha-helix content.	Heparin	22-29	CYCS pseudogene 38	Homo sapiens	30-33
12172443-2	2002	Selective factor Xa inhibition is a new antithrombotic approach designed to avoid difficulties associated with heparins and other current anticoagulants.	Heparin	111-119	coagulation factor X	Homo sapiens	10-19
15265919-3	2004	Previous studies have shown that tryptase binds tightly to heparin, and that heparin is required in the assembly of the tryptase tetramer as well as for stabilization of the active tetramer.	Heparin	77-84	tryptase alpha/beta 1	Mus musculus	120-128
18065761-5	2008	In silico docking calculations partnered with our crystal structures support the importance of arginine residues in positions 29, 42, and 77 in binding sulfate groups of the dp8 and dp10 forms of heparin.	Heparin	196-203	dipeptidyl peptidase 8	Homo sapiens	174-177
15265919-4	2004	Because the interaction of tryptase with heparin is optimal at acidic pH, we investigated in this study whether His residues are of importance for the heparin binding, tetramerization, and activation of the tryptase mouse mast cell protease 6.	Heparin	41-48	tryptase alpha/beta 1	Mus musculus	27-35
12168126-1	2002	OBJECTIVE: Neonates who are treated with low-molecular-weight heparin require repeated venipunctures to monitor anti-factor Xa (anti-FXa) levels.	Heparin	62-69	coagulation factor X	Homo sapiens	133-136
12168126-7	2002	When 0.5, 3.0, or 4.0 ml of blood was cleared from the UAC before withdrawing the test sample, heparin contaminated the test (anti-FXa levels &gt; or = 0.1 U/ml) in 66%, 16%, and 8% of samples, respectively.	Heparin	95-102	coagulation factor X	Homo sapiens	131-134
15265919-10	2004	Taken together, this study shows that surface-exposed histidines mediate the interaction of mast cell tryptase with heparin and are of critical importance in the formation of active tryptase tetramers.	Heparin	116-123	tryptase alpha/beta 1	Mus musculus	102-110
15334855-2	2004	When given intravenously, UFH quickly binds to and activates antithrombin, which then inhibits several activated factors in the clotting cascade.	Heparin	26-29	serpin family C member 1	Homo sapiens	61-73
12113804-0	2002	Synthesis of betaglycan-type tetraosyl hexapeptide: a possible precursor regulating enzymatic elongation toward heparin.	Heparin	112-119	transforming growth factor beta receptor 3	Homo sapiens	13-23
12113804-1	2002	TETRAOSYL HEXAPEPTIDE, A PART OF THE SEQUENCE OF BETAGLYCAN: beta-D-GlcA-(1--&gt;3)-beta-D-Gal-(1--&gt;3)-beta-D-Gal-(1--&gt;4)-beta-D-Xyl-(1--&gt;O-SerGlyTrpProAspGly (1), which was designed as a probe for glycan elongation toward heparin, was synthesized in a stereocontrolled manner.	Heparin	232-239	transforming growth factor beta receptor 3	Homo sapiens	37-59
12151311-10	2002	We concluded that the absence of VEGF 164 and 188 isoforms impairs lung microvascular development and delays airspace maturation, indicating an essential role for heparin-binding VEGF isoforms in normal lung development.	Heparin	163-170	vascular endothelial growth factor A	Mus musculus	179-183
12211411-3	2002	Understanding the heparin structure led to the development of LMWHs, synthetic heparinomimetics, antithrombin and anti-Factor Xa agents.	Heparin	18-25	coagulation factor X	Homo sapiens	119-128
18484795-2	2008	Intravenous GP IIb/IIIa antagonists abciximab, tirofiban and eptifibatide have demonstrated efficacy in acute coronary syndromes when combined with heparin, aspirin, clopidogrel and percutanous coronary interventions.	Heparin	148-155	integrin subunit alpha 2b	Homo sapiens	12-18
18369865-1	2008	Heparins are negatively charged polydispersed linear polysaccharides which have the ability to bind a wide range of biomolecules including enzymes, serine protease inhibitors, growth factors, extracellular matrix proteins, DNA modification enzymes and hormone receptors.	Heparin	0-8	complement component 1, s subcomponent 1	Mus musculus	148-163
18045667-6	2008	CONCLUSION: The data fit a model in which thrombin and factor Xa bind at a random site on the heparin chain and, via one-dimensional diffusion, reach the AT that is bound to its specific binding site on the heparin.	Heparin	94-101	coagulation factor X	Homo sapiens	55-64
18045667-6	2008	CONCLUSION: The data fit a model in which thrombin and factor Xa bind at a random site on the heparin chain and, via one-dimensional diffusion, reach the AT that is bound to its specific binding site on the heparin.	Heparin	207-214	coagulation factor X	Homo sapiens	55-64
17982312-2	2007	Gln49-PLA2 clotted human plasma dose-dependently from 180.67 +/- 1.86 s to 19.00 +/- 0.58 s, and reduced the re-calcification time from 7.46 +/- 1.17 to 0.75 +/- 0.33 min and the prothrombin time from 12.4 +/- 0.29 s to 6.95 +/- 0.20 s, but it could not activate factor XIII, and the procoagulant effects were inhibited by heparin.	Heparin	323-330	phospholipase A2 group IIA	Homo sapiens	6-10
15238596-0	2004	Efficacy and bleeding complications among patients randomized to enoxaparin or unfractionated heparin for antithrombin therapy in non-ST-Segment elevation acute coronary syndromes: a systematic overview.	Heparin	94-101	serpin family C member 1	Homo sapiens	106-118
17964518-7	2007	The simultaneous administration of FII(a) and heparin further improved all the hemostatic parameters, including decreased kidney fibrin deposition, and none of the rabbits died within 24 h, which indicates that the effects were mediated by degradation of fibrin/fibrinogen together with thrombin inhibition.	Heparin	46-53	prothrombin	Oryctolagus cuniculus	287-295
12154174-5	2002	In fura-2-loaded cells extracellular 2-aminoethoxydiphenyl borate and intracellular heparin (5 mg ml(-1)) both inhibited the global cytoplasmic [Ca(2+)] transient evoked by carbachol, confirming that it was IP(3)R-dependent.	Heparin	84-91	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	207-213
15223398-8	2004	Heparin-coated polyvinylchloride efficiently prevented synthesis of both IL-8 and MCP-1.	Heparin	0-7	C-C motif chemokine ligand 2	Homo sapiens	82-87
11983709-4	2002	In subjecting GRP94 to increasingly stringent chromatographic purification, we report that a GRP94 carboxyl-terminal directed protein kinase activity could be separated from GRP94 by heparin affinity chromatography.	Heparin	183-190	heat shock protein 90 beta family member 1	Homo sapiens	14-19
11983709-4	2002	In subjecting GRP94 to increasingly stringent chromatographic purification, we report that a GRP94 carboxyl-terminal directed protein kinase activity could be separated from GRP94 by heparin affinity chromatography.	Heparin	183-190	heat shock protein 90 beta family member 1	Homo sapiens	93-98
11983709-4	2002	In subjecting GRP94 to increasingly stringent chromatographic purification, we report that a GRP94 carboxyl-terminal directed protein kinase activity could be separated from GRP94 by heparin affinity chromatography.	Heparin	183-190	heat shock protein 90 beta family member 1	Homo sapiens	93-98
17626017-1	2007	The longer splice isoforms of vascular endothelial growth factor-A (VEGF-A), including mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the ability of these isoforms to be deposited in the heparan sulfate-rich extracellular matrix and to interact with the prototype sulfated glycosaminoglycan, heparin.	Heparin	125-132	vascular endothelial growth factor A	Mus musculus	30-66
17626017-1	2007	The longer splice isoforms of vascular endothelial growth factor-A (VEGF-A), including mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the ability of these isoforms to be deposited in the heparan sulfate-rich extracellular matrix and to interact with the prototype sulfated glycosaminoglycan, heparin.	Heparin	125-132	vascular endothelial growth factor A	Mus musculus	68-74
17626017-1	2007	The longer splice isoforms of vascular endothelial growth factor-A (VEGF-A), including mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the ability of these isoforms to be deposited in the heparan sulfate-rich extracellular matrix and to interact with the prototype sulfated glycosaminoglycan, heparin.	Heparin	327-334	vascular endothelial growth factor A	Mus musculus	30-66
15223398-9	2004	Addition of recombinant human complement factor 5a to blood incubated in heparin-coated polyvinylchloride restored IL-8 and MCP-1 production completely and partly, respectively.	Heparin	73-80	C-C motif chemokine ligand 2	Homo sapiens	124-129
17626017-1	2007	The longer splice isoforms of vascular endothelial growth factor-A (VEGF-A), including mouse VEGF164, contain a highly basic heparin-binding domain (HBD), which imparts the ability of these isoforms to be deposited in the heparan sulfate-rich extracellular matrix and to interact with the prototype sulfated glycosaminoglycan, heparin.	Heparin	327-334	vascular endothelial growth factor A	Mus musculus	68-74
17626017-9	2007	Finally, mutations that affect the heparin binding activity also led to an unexpected reduction in the affinity of VEGF164 binding specifically to VEGFR1.	Heparin	35-42	FMS-like tyrosine kinase 1	Mus musculus	147-153
15223398-14	2004	The increase in IL-8 and MCP-1 was prevented by heparin-coated polyvinylchloride.	Heparin	48-55	C-C motif chemokine ligand 2	Homo sapiens	25-30
12094193-6	2002	During period 2, there was an increased use of percutaneous transluminal coronary angioplasty, coronary artery bypass grafting, angiotensin-converting enzyme inhibitors, heparin, and intravenous nitroglycerin.	Heparin	170-177	period circadian regulator 2	Homo sapiens	7-15
15247982-2	2004	Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin.	Heparin	128-135	serpin family C member 1	Homo sapiens	73-85
17557914-5	2007	Compounds (heparin and CRM-197) that specifically interfere with HB-EGF signaling eliminated OxyHb-induced K(V) suppression, suggesting that HB-EGF is the EGFR ligand involved in this pathway.	Heparin	11-18	epidermal growth factor receptor	Oryctolagus cuniculus	155-159
15247982-2	2004	Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin.	Heparin	128-135	serpin family C member 1	Homo sapiens	87-92
15497502-5	2004	Interestingly, the synergistic effect of heparin-like agents toward Fas IgM agonistic antibody-mediated cell death abolished Hsp27 antiapoptotic activity but did not alter much the protection generated by Bcl-2 expression.	Heparin	41-48	heat shock protein family B (small) member 1	Homo sapiens	125-130
17827718-2	2007	In this study, PAF-AH in early colostrum was purified by ammonium sulfate precipitation, and sequential use of butyl-Toyopearl 650M, DEAE-Sepharose, heparin-Sepharose, hydroxyapatite, chelating-Sepharose and Mono Q HPLC column chromatography.	Heparin	149-156	phospholipase A2 group VII	Homo sapiens	15-21
17588949-8	2007	Using affinity co-electrophoresis, we showed that COMP/TSP5, in its calcium-replete conformation, bound to heparin, chondroitin sulfates, and heparan sulfate; this binding was reduced with EDTA treatment of COMP/TSP5.	Heparin	107-114	cartilage oligomeric matrix protein	Homo sapiens	50-59
14707483-0	2002	Heparin inhibits the reconstituted plasma membrane Ca(2+)-ATPase from porcine brain synaptosome.	Heparin	0-7	ATPase plasma membrane Ca2+ transporting 2	Homo sapiens	35-64
14707483-2	2002	Here we examined the effects of heparin on the plasma membrane Ca(2+)-ATPase from porcine brain synaptosome.	Heparin	32-39	ATPase plasma membrane Ca2+ transporting 2	Homo sapiens	47-76
14707483-6	2002	We observed that Ca(2+) affinity kept no obvious changes, but the ATP affinity of plasma membrane Ca(2+)-ATPase was apparently decreased in the presence of heparin.	Heparin	156-163	ATPase plasma membrane Ca2+ transporting 2	Homo sapiens	82-111
12009502-3	2002	We evaluated the effect of heparin on Abeta (1-42) neurotoxicity and on its ability to activate complement and contact system.	Heparin	27-34	amyloid beta precursor protein	Rattus norvegicus	38-43
12009502-4	2002	On differentiated PC12 cells, a reliable model of neuronal cells, heparin at the doses of 10 and 20 microg/ml significantly counteracted Abeta cytotoxicity as assessed by measuring MTT conversion.	Heparin	66-73	amyloid beta precursor protein	Rattus norvegicus	137-142
12009502-5	2002	We then explored the effect of heparin on Abeta (1-42)-induced complement and contact system activation.	Heparin	31-38	amyloid beta precursor protein	Rattus norvegicus	42-47
17588949-8	2007	Using affinity co-electrophoresis, we showed that COMP/TSP5, in its calcium-replete conformation, bound to heparin, chondroitin sulfates, and heparan sulfate; this binding was reduced with EDTA treatment of COMP/TSP5.	Heparin	107-114	cartilage oligomeric matrix protein	Homo sapiens	55-59
15201252-4	2004	UFH was significantly more effective than LMWH at inhibiting P selectin expression (p = 0.001) and platelet derived growth factor release from thrombin activated platelets (p = 0.012).	Heparin	0-3	selectin P	Homo sapiens	61-71
17588944-0	2007	The heparin/heparan sulfate sequence that interacts with cyclophilin B contains a 3-O-sulfated N-unsubstituted glucosamine residue.	Heparin	4-11	peptidylprolyl isomerase B	Homo sapiens	57-70
12009502-6	2002	Abeta (1-42) was incubated with heparin in presence of normal plasma as the source of complement and contact system factors.	Heparin	32-39	amyloid beta precursor protein	Rattus norvegicus	0-5
12009502-8	2002	The present data show that heparin can attenuate neurotoxic and pro-inflammatory activity of Abeta and suggest that this drug could represent a new strategy to reduce the progressive neurodegeneration in AD.	Heparin	27-34	amyloid beta precursor protein	Rattus norvegicus	93-98
15217633-3	2004	Plasma P-selectin was tested by ELISA before heparin administration (day 1), and under heparin treatment (day 7).	Heparin	45-52	selectin P	Homo sapiens	7-17
12056830-3	2002	Extracellular ATP increases Ca(2+) in these cells, and we found that this effect is independent of extracellular Ca(2+) but is blocked by the InsP(3)R antagonist heparin.	Heparin	162-169	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	142-150
17662008-8	2007	In vitro experiments indicate that Copaxone significantly reduced PrP(Sc) binding to both Chinese hamster ovary (CHO) cells and heparin beads and also binds to heparin by itself.	Heparin	128-135	major prion protein	Cricetulus griseus	66-69
15217633-3	2004	Plasma P-selectin was tested by ELISA before heparin administration (day 1), and under heparin treatment (day 7).	Heparin	87-94	selectin P	Homo sapiens	7-17
17540196-10	2007	Patients older than 75 years who received GP IIb/IIIa antagonists and any antithrombotic but not PCI had an increased risk of major bleeding (LMWH 14%, UFH 8.3%).	Heparin	152-155	integrin subunit alpha 2b	Homo sapiens	42-48
12022870-1	2002	The VWF A1 domain seems to possess two heparin binding regions (residues 565-587 and 633-648) displaying positively charged amino acids, but the overall polyanion-A1 domain interaction scheme remains essentially elusive.	Heparin	39-46	von Willebrand factor	Rattus norvegicus	4-7
12022870-9	2002	Our data suggest that two clusters, one at positions 571-573, 578, 579, and 585 and the other at positions 642-645, act in concert for the recognition of heparin, forming a single extended binding surface across the electropositive face of the VWF A1 domain.	Heparin	154-161	von Willebrand factor	Rattus norvegicus	244-247
15217633-11	2004	CONCLUSIONS: P-selectin and HIT antibodies could be useful markers of HIT syndrome-associated thromboses during hospitalization of vascular patients receiving heparin.	Heparin	159-166	selectin P	Homo sapiens	13-23
12022870-10	2002	A structural model of the VWF A1 domain-heparin complex is proposed, taking into account both experimental and computer modeling data.	Heparin	40-47	von Willebrand factor	Rattus norvegicus	26-29
11854268-3	2002	A specific pentasaccharide sequence (H5) in high affinity heparin induces a conformational change in antithrombin that is particularly important for factor Xa (fXa) inhibition.	Heparin	58-65	coagulation factor X	Homo sapiens	149-158
17489664-1	2007	Enoxaparin is a low-molecular-weight heparin (LMWH) derivative that exerts its anticoagulant activity through antithrombin III, an endogenous inhibitor of factor Xa and thrombin IIa.	Heparin	37-44	coagulation factor X	Homo sapiens	155-164
11854268-3	2002	A specific pentasaccharide sequence (H5) in high affinity heparin induces a conformational change in antithrombin that is particularly important for factor Xa (fXa) inhibition.	Heparin	58-65	coagulation factor X	Homo sapiens	160-163
15219196-2	2004	The serpin antithrombin (AT) is an important physiological regulator of FXa activity in an inhibition reaction that is enhanced by heparin.	Heparin	131-138	serpin family C member 1	Homo sapiens	11-23
15199558-3	2004	In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade.	Heparin	82-89	serpin family C member 1	Homo sapiens	107-123
11812795-7	2002	Heparin, a known ligand for FH, specifically inhibited the binding between beta and FH, suggesting that FH has overlapping binding sites for beta and heparin.	Heparin	0-7	complement factor H	Homo sapiens	28-30
11812795-7	2002	Heparin, a known ligand for FH, specifically inhibited the binding between beta and FH, suggesting that FH has overlapping binding sites for beta and heparin.	Heparin	0-7	complement factor H	Homo sapiens	84-86
17461929-1	2007	BACKGROUND: Low-molecular-weight heparins (LMWHs), derived from unfractionated heparin (UFH) by different depolymerization procedures, vary in both their relative abilities to enhance the inhibition of FXa (anti-FXa) and thrombin (anti-FIIa), and in their physicochemical properties.	Heparin	33-41	coagulation factor X	Homo sapiens	202-205
17461929-1	2007	BACKGROUND: Low-molecular-weight heparins (LMWHs), derived from unfractionated heparin (UFH) by different depolymerization procedures, vary in both their relative abilities to enhance the inhibition of FXa (anti-FXa) and thrombin (anti-FIIa), and in their physicochemical properties.	Heparin	33-41	coagulation factor X	Homo sapiens	212-215
17461929-1	2007	BACKGROUND: Low-molecular-weight heparins (LMWHs), derived from unfractionated heparin (UFH) by different depolymerization procedures, vary in both their relative abilities to enhance the inhibition of FXa (anti-FXa) and thrombin (anti-FIIa), and in their physicochemical properties.	Heparin	33-40	coagulation factor X	Homo sapiens	202-205
17461929-1	2007	BACKGROUND: Low-molecular-weight heparins (LMWHs), derived from unfractionated heparin (UFH) by different depolymerization procedures, vary in both their relative abilities to enhance the inhibition of FXa (anti-FXa) and thrombin (anti-FIIa), and in their physicochemical properties.	Heparin	33-40	coagulation factor X	Homo sapiens	212-215
17362990-0	2007	Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin.	Heparin	157-164	complement factor H	Homo sapiens	66-74
11812795-7	2002	Heparin, a known ligand for FH, specifically inhibited the binding between beta and FH, suggesting that FH has overlapping binding sites for beta and heparin.	Heparin	0-7	complement factor H	Homo sapiens	84-86
11812795-7	2002	Heparin, a known ligand for FH, specifically inhibited the binding between beta and FH, suggesting that FH has overlapping binding sites for beta and heparin.	Heparin	150-157	complement factor H	Homo sapiens	84-86
11812795-7	2002	Heparin, a known ligand for FH, specifically inhibited the binding between beta and FH, suggesting that FH has overlapping binding sites for beta and heparin.	Heparin	150-157	complement factor H	Homo sapiens	84-86
11971193-5	2002	They also overexpressed CD9, a tetraspanin that binds to the heparin-binding domain of HB-EGF and is critical for promoting ErbB1 activation by HB-EGF.	Heparin	61-68	CD9 molecule	Homo sapiens	24-27
17229890-4	2007	In a cell culture system, its product facilitated the secretion of heparin-binding epidermal growth factor-like growth factor (HB-EGF), one of the ligands of ErbB4.	Heparin	67-74	heparin binding EGF like growth factor	Gallus gallus	127-133
15199558-3	2004	In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade.	Heparin	82-89	serpin family C member 1	Homo sapiens	125-131
14965340-8	2004	These data indicated that serum levels of endostatin changed in parallel with those of VEGF in response to myocardial ischaemia/reperfusion, and the marked increase in serum HGF levels after reperfusion seemed to be, at least in part, due to heparin administration.	Heparin	242-249	collagen type XVIII alpha 1 chain	Homo sapiens	42-52
16750851-7	2007	In choriocarcinoma cells the heparin effect was also indirect, inducing a significant decrease in TIMP-1 and TIMP-2 protein expressions and mRNAs.	Heparin	29-36	TIMP metallopeptidase inhibitor 2	Homo sapiens	109-115
15233473-7	2004	Moreover, significant increase in phospholipase A2 activity was observed after capacitation by both, the heparin and 25 microM H2O2.	Heparin	105-112	LOC104974671	Bos taurus	34-50
17277743-2	2007	Overexpression of vascular endothelial growth factor-A(188) (VEGF-A(188)), a strongly heparin-binding, endothelial-specific mitogen, leads to severe disturbance of vascular and overall ocular morphology.	Heparin	86-93	vascular endothelial growth factor A	Mus musculus	61-67
15128279-0	2004	Effect of heparin administration to sheep on the release profiles of circulating activin A and follistatin.	Heparin	10-17	follistatin	Ovis aries	95-106
15128279-3	2004	In the present studies, the response to heparin administration was evaluated in the plasma of adult ewes in terms of whether it was dose-dependent, could be neutralized, was responsive to multiple stimulation, and the nature of the activin A and follistatin released.	Heparin	40-47	follistatin	Ovis aries	246-257
17150202-5	2007	Citrate and heparin plasma samples had the lowest Pro-MMP-9 and MMP-9 levels, which correlated with each other.	Heparin	12-19	matrix metallopeptidase 9	Homo sapiens	54-59
15128279-4	2004	Activin A and follistatin were rapidly released by heparin in a dose-dependent manner (25, 100 or 250 IU/kg), with differences in the response as adjudged by peak concentration, timing of the peak and area under the curve.	Heparin	51-58	follistatin	Ovis aries	14-25
17150202-5	2007	Citrate and heparin plasma samples had the lowest Pro-MMP-9 and MMP-9 levels, which correlated with each other.	Heparin	12-19	matrix metallopeptidase 9	Homo sapiens	64-69
15128279-5	2004	The heparin response could be blocked by pretreatment with protamine; conversely protamine injection alone (2 mg/kg) elicited release of follistatin but not activin A. Repeat administration of heparin at three-hourly intervals resulted in activin and follistatin responses to each injection, but each subsequent stimulation increased and extended the responses, consistent with saturation of the heparin clearance mechanism.	Heparin	193-200	follistatin	Ovis aries	137-148
15128279-5	2004	The heparin response could be blocked by pretreatment with protamine; conversely protamine injection alone (2 mg/kg) elicited release of follistatin but not activin A. Repeat administration of heparin at three-hourly intervals resulted in activin and follistatin responses to each injection, but each subsequent stimulation increased and extended the responses, consistent with saturation of the heparin clearance mechanism.	Heparin	193-200	follistatin	Ovis aries	137-148
17257362-0	2007	Catheter lock heparin concentration: effects on tissue plasminogen activator use in tunneled cuffed catheters.	Heparin	14-21	chromosome 20 open reading frame 181	Homo sapiens	48-76
15128279-6	2004	Size exclusion chromatography of plasma samples confirmed that the majority of activin and follistatin released by heparin was a complex, whereas follistatin released by protamine was unbound.	Heparin	115-122	follistatin	Ovis aries	91-102
15010305-2	2004	These two models represent the regular region of heparin lacking one type of O-sulfate group, either at C-6 of glucosamine or at C-2 of iduronate.	Heparin	49-56	complement C2	Homo sapiens	129-132
18300423-4	2007	VEGF-A production is controlled by hypoxia while its retention depends on the C-terminal heparin-binding motifs present in the longer splice-isoforms, VEGF164 and 188.	Heparin	89-96	vascular endothelial growth factor A	Mus musculus	0-6
16515805-0	2007	Heparin chain-length dependence of factor Xa inhibition by antithrombin in plasma.	Heparin	0-7	coagulation factor X	Homo sapiens	35-44
15004848-0	2004	Capillary zone electrophoresis investigation of the interaction between heparin and granulocyte-colony stimulating factor.	Heparin	72-79	colony stimulating factor 3	Homo sapiens	84-121
16515805-2	2007	A direct evaluation of the specific anti-factor Xa (fXa) activity of therapeutic heparins in the physiologically relevant plasma-based clotting assays has not been feasible since thrombin, the final protease of the cascade, is the primary target for inhibition by AT in the presence of heparin.	Heparin	81-89	coagulation factor X	Homo sapiens	41-50
16515805-2	2007	A direct evaluation of the specific anti-factor Xa (fXa) activity of therapeutic heparins in the physiologically relevant plasma-based clotting assays has not been feasible since thrombin, the final protease of the cascade, is the primary target for inhibition by AT in the presence of heparin.	Heparin	81-89	coagulation factor X	Homo sapiens	52-55
16515805-2	2007	A direct evaluation of the specific anti-factor Xa (fXa) activity of therapeutic heparins in the physiologically relevant plasma-based clotting assays has not been feasible since thrombin, the final protease of the cascade, is the primary target for inhibition by AT in the presence of heparin.	Heparin	81-88	coagulation factor X	Homo sapiens	41-50
16515805-2	2007	A direct evaluation of the specific anti-factor Xa (fXa) activity of therapeutic heparins in the physiologically relevant plasma-based clotting assays has not been feasible since thrombin, the final protease of the cascade, is the primary target for inhibition by AT in the presence of heparin.	Heparin	81-88	coagulation factor X	Homo sapiens	52-55
16515805-4	2007	This assay was used to distinguish the anti-fXa activity of different molecular weight heparins from their anti-thrombin activity in clotting assays which were initiated by the triggers of either the extrinsic or intrinsic coagulation pathway.	Heparin	87-95	coagulation factor X	Homo sapiens	44-47
16515805-5	2007	The results suggest that the acceleration of fXa inhibition by AT exhibits a marked heparin chain-length dependence, with fondaparinux (a pentasaccharide) having the lowest and unfractionated heparin having the highest effect.	Heparin	84-91	coagulation factor X	Homo sapiens	45-48
16515805-5	2007	The results suggest that the acceleration of fXa inhibition by AT exhibits a marked heparin chain-length dependence, with fondaparinux (a pentasaccharide) having the lowest and unfractionated heparin having the highest effect.	Heparin	192-199	coagulation factor X	Homo sapiens	45-48
18023704-13	2007	In addition, pro-heparanase can reverse the anti-coagulant effect of unfractionated heparin and the Factor Xa inhibitory activity of low molecular weight heparin (LMWH).	Heparin	154-161	coagulation factor X	Homo sapiens	100-109
16940188-0	2006	Heparin displaces interferon-gamma-inducible chemokines (IP-10, I-TAC, and Mig) sequestered in the vasculature and inhibits the transendothelial migration and arterial recruitment of T cells.	Heparin	0-7	C-X-C motif chemokine ligand 10	Homo sapiens	57-62
16940188-0	2006	Heparin displaces interferon-gamma-inducible chemokines (IP-10, I-TAC, and Mig) sequestered in the vasculature and inhibits the transendothelial migration and arterial recruitment of T cells.	Heparin	0-7	C-X-C motif chemokine ligand 11	Homo sapiens	64-69
16940188-2	2006	We investigated the effects of heparin on the IFN-gamma-inducible chemokines IP-10/CXCL10, I-TAC/CXCL11, and Mig/CXCL9, which play important roles in the vascular recruitment of IFN-gamma-producing Th1 cells through interactions with their cognate receptor, CXCR3.	Heparin	31-38	C-X-C motif chemokine ligand 10	Homo sapiens	77-82
15004848-3	2004	The binding constants of the two different groups of heparins with G-CSF, calculated from the Scatchard plot by regression, were 4.805 x 10(5) M(-1) and 4.579 x 10(5) M(-1), respectively.	Heparin	53-61	colony stimulating factor 3	Homo sapiens	67-72
16940188-4	2006	Plasma levels of IP-10, I-TAC, and Mig increased immediately after heparin administration and diminished promptly after heparin antagonism with protamine.	Heparin	67-74	C-X-C motif chemokine ligand 10	Homo sapiens	17-22
16940188-7	2006	In addition to prolonged treatment decreasing chemokine secretion, heparin rapidly displaced membrane-associated IP-10 from cultured endothelial cells that did not express CXCR3 and reduced the IP-10-dependent transendothelial migration of T helper cells under conditions of venular shear stress.	Heparin	67-74	C-X-C motif chemokine ligand 10	Homo sapiens	113-118
15004848-4	2004	The two binding constants measured are of the same order of magnitude at 10(5) M(-1), indicating that LMWH contains most of the functional groups bound to G-CSF by standard heparin.	Heparin	173-180	colony stimulating factor 3	Homo sapiens	155-160
16940188-7	2006	In addition to prolonged treatment decreasing chemokine secretion, heparin rapidly displaced membrane-associated IP-10 from cultured endothelial cells that did not express CXCR3 and reduced the IP-10-dependent transendothelial migration of T helper cells under conditions of venular shear stress.	Heparin	67-74	C-X-C motif chemokine ligand 10	Homo sapiens	194-199
16940188-9	2006	CONCLUSIONS: Besides inhibiting IFN-gamma responses, heparin has further immunomodulatory effects by competing for binding with IP-10, I-TAC, and Mig on endothelial cells.	Heparin	53-60	C-X-C motif chemokine ligand 10	Homo sapiens	128-133
14687916-4	2004	The inhibitory activity of antithrombin is controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases.	Heparin	93-100	serpin family C member 1	Homo sapiens	27-39
16940188-9	2006	CONCLUSIONS: Besides inhibiting IFN-gamma responses, heparin has further immunomodulatory effects by competing for binding with IP-10, I-TAC, and Mig on endothelial cells.	Heparin	53-60	C-X-C motif chemokine ligand 11	Homo sapiens	135-140
16787919-0	2006	His-384 allotypic variant of factor H associated with age-related macular degeneration has different heparin binding properties from the non-disease-associated form.	Heparin	101-108	complement factor H	Homo sapiens	29-37
16787919-3	2006	Here, using a recombinant construct, we show that amino acid 384 is adjacent to a heparin-binding site in CCP7 of factor H and demonstrate that the allotypic variants differentially recognize heparin.	Heparin	82-89	complement factor H	Homo sapiens	114-122
15123357-8	2004	RESULTS: CCN2 stimulated DNA synthesis and phosphorylation of FAK, Elk-1 and ERK1/2, the latter of which was blocked by heparin.	Heparin	120-127	protein tyrosine kinase 2	Rattus norvegicus	62-65
16787919-3	2006	Here, using a recombinant construct, we show that amino acid 384 is adjacent to a heparin-binding site in CCP7 of factor H and demonstrate that the allotypic variants differentially recognize heparin.	Heparin	192-199	complement factor H	Homo sapiens	114-122
16737974-1	2006	In this study, we present multiple lines of evidence to support a critical role for heparin-bound EGF (epidermal growth factor)-like growth factor (HB-EGF) and tumor necrosis factor-alpha-converting enzyme (TACE) (ADAM17) in the transactivation of EGF receptor (EGFR), ERK phosphorylation, and cellular proliferation induced by the 5-HT(2A) receptor in renal mesangial cells.	Heparin	84-91	ADAM metallopeptidase domain 17	Homo sapiens	160-205
14705167-3	2004	Heparin-based anticoagulants are indirect inhibitors that enhance the proteinase inhibitory activity of a natural anticoagulant, antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	129-141
16737974-1	2006	In this study, we present multiple lines of evidence to support a critical role for heparin-bound EGF (epidermal growth factor)-like growth factor (HB-EGF) and tumor necrosis factor-alpha-converting enzyme (TACE) (ADAM17) in the transactivation of EGF receptor (EGFR), ERK phosphorylation, and cellular proliferation induced by the 5-HT(2A) receptor in renal mesangial cells.	Heparin	84-91	ADAM metallopeptidase domain 17	Homo sapiens	214-220
16729969-6	2006	We found that (a) hypoxic exposure for two weeks significantly inhibited p27 expression and stimulated p18 activity, showing a 98% decrease in p27 and 81% increase in p18; (b) other CDKIs, p21, p57, p15, p16, and p19 were not affected significantly in response to hypoxia; (c) heparin treatment restored p27 expression, but did not influence p18; (d) ERK1/2 and p38 were mediators in heparin upregulation of p27.	Heparin	277-284	cyclin dependent kinase inhibitor 2C	Mus musculus	103-106
16729969-6	2006	We found that (a) hypoxic exposure for two weeks significantly inhibited p27 expression and stimulated p18 activity, showing a 98% decrease in p27 and 81% increase in p18; (b) other CDKIs, p21, p57, p15, p16, and p19 were not affected significantly in response to hypoxia; (c) heparin treatment restored p27 expression, but did not influence p18; (d) ERK1/2 and p38 were mediators in heparin upregulation of p27.	Heparin	384-391	cyclin dependent kinase inhibitor 2C	Mus musculus	103-106
15000687-2	2004	Heparin and pentosan polysulfate stabilized antithrombin III; this resulted in decrease in ultrasonic-induced formation of the aggregate and latent forms.	Heparin	0-7	serpin family C member 1	Homo sapiens	44-60
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	96-103	vascular endothelial growth factor D	Homo sapiens	58-64
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	96-103	neuropilin 2	Homo sapiens	79-82
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	132-139	vascular endothelial growth factor D	Homo sapiens	58-64
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	132-139	neuropilin 2	Homo sapiens	79-82
16816121-4	2006	By in vitro binding studies we found that both VEGF-C and VEGF-D interact with NP2, VEGF-C in a heparin-independent and VEGF-D in a heparin-dependent manner.	Heparin	132-139	vascular endothelial growth factor D	Homo sapiens	120-126
16778722-1	2006	This study was designed to develop methods for monitoring of the selective factor Xa inhibitor fondaparinux sodium (ARIXTRA) based on standard laboratory methods for the chromogenic determination of the anti-factor Xa activity of low molecular weight heparin.	Heparin	251-258	coagulation factor X	Homo sapiens	75-84
16778722-1	2006	This study was designed to develop methods for monitoring of the selective factor Xa inhibitor fondaparinux sodium (ARIXTRA) based on standard laboratory methods for the chromogenic determination of the anti-factor Xa activity of low molecular weight heparin.	Heparin	251-258	coagulation factor X	Homo sapiens	208-217
16637790-7	2006	In the base-case analysis, the use of bivalirudin with provisional GP IIb-IIIa inhibitor therapy dominated the UFH and planned GP IIb-IIIa inhibitor approach: UFH with eptifibatide was 74 US dollars more expensive and 1.2% less effective, and UFH with abciximab was 777 US dollars more expensive and 2.3% less effective.	Heparin	159-162	integrin subunit alpha 2b	Homo sapiens	127-133
16637790-7	2006	In the base-case analysis, the use of bivalirudin with provisional GP IIb-IIIa inhibitor therapy dominated the UFH and planned GP IIb-IIIa inhibitor approach: UFH with eptifibatide was 74 US dollars more expensive and 1.2% less effective, and UFH with abciximab was 777 US dollars more expensive and 2.3% less effective.	Heparin	159-162	integrin subunit alpha 2b	Homo sapiens	127-133
14725788-14	2004	Anti-thrombin III alone was not inhibitory, but in the presence of heparin inhibited both MASP-1 and MASP-2.	Heparin	67-74	MBL associated serine protease 1	Homo sapiens	90-96
16618121-2	2006	It has been demonstrated that a unique pentasaccharide fragment of heparin (H5) activates AT by exposing an exosite on the serpin that is a recognition site for interaction with the basic autolysis loop (residues 143-154) of fXa.	Heparin	67-74	coagulation factor X	Homo sapiens	225-228
16618121-4	2006	To understand the mechanism by which heparin activation of AT improves the reactivity of the serpin with fXa, the H5-catalyzed reaction of AT with fXa, fXa R150A, and fXa S195A was studied using rapid kinetic, surface plasmon resonance, and competitive binding methods.	Heparin	37-44	coagulation factor X	Homo sapiens	105-108
16618121-6	2006	On the other hand, an approximately 70-saccharide, high-affinity heparin-catalyzed AT inhibition of both fXa derivatives showed a saturable dependence on the inhibitor concentration, yielding an identical rate constant of approximately 20 s(-)(1), but different ternary fXa-heparin-AT dissociation constants (K(E,ATH)) of approximately 130 and approximately 1780 nM for wild-type and R150A fXa, respectively.	Heparin	65-72	coagulation factor X	Homo sapiens	105-108
16618121-6	2006	On the other hand, an approximately 70-saccharide, high-affinity heparin-catalyzed AT inhibition of both fXa derivatives showed a saturable dependence on the inhibitor concentration, yielding an identical rate constant of approximately 20 s(-)(1), but different ternary fXa-heparin-AT dissociation constants (K(E,ATH)) of approximately 130 and approximately 1780 nM for wild-type and R150A fXa, respectively.	Heparin	65-72	coagulation factor X	Homo sapiens	270-273
16618121-6	2006	On the other hand, an approximately 70-saccharide, high-affinity heparin-catalyzed AT inhibition of both fXa derivatives showed a saturable dependence on the inhibitor concentration, yielding an identical rate constant of approximately 20 s(-)(1), but different ternary fXa-heparin-AT dissociation constants (K(E,ATH)) of approximately 130 and approximately 1780 nM for wild-type and R150A fXa, respectively.	Heparin	65-72	coagulation factor X	Homo sapiens	270-273
12024108-0	2002	Histidine-rich glycoprotein plus zinc to neutralize heparin.	Heparin	52-59	histidine rich glycoprotein	Homo sapiens	0-27
12024108-1	2002	Histidine-rich glycoprotein (HRG) binds heparin and neutralizes its anticoagulant effect.	Heparin	40-47	histidine rich glycoprotein	Homo sapiens	0-27
12024108-1	2002	Histidine-rich glycoprotein (HRG) binds heparin and neutralizes its anticoagulant effect.	Heparin	40-47	histidine rich glycoprotein	Homo sapiens	29-32
12024108-2	2002	Because zinc greatly enhances this interaction, it is possible that the combination of HRG and zinc could be used as an antidote for heparin.	Heparin	133-140	histidine rich glycoprotein	Homo sapiens	87-90
12024108-3	2002	We have determined the plasma concentrations of HRG and zinc necessary to neutralize clinically relevant concentrations of heparin.	Heparin	123-130	histidine rich glycoprotein	Homo sapiens	48-51
12024108-4	2002	Using a thrombin-time assay, we found that HRG plus zinc can neutralize 0.2 to 4.5 units/mL heparin, although the maximal effect requires an HRG plasma concentration about six times normal and a zinc concentration about 10 times normal.	Heparin	92-99	histidine rich glycoprotein	Homo sapiens	43-46
12024108-6	2002	Whether HRG and zinc can be administered as an antidote for heparin will depend on whether the requisite doses can be achieved without toxicity.	Heparin	60-67	histidine rich glycoprotein	Homo sapiens	8-11
16618121-6	2006	On the other hand, an approximately 70-saccharide, high-affinity heparin-catalyzed AT inhibition of both fXa derivatives showed a saturable dependence on the inhibitor concentration, yielding an identical rate constant of approximately 20 s(-)(1), but different ternary fXa-heparin-AT dissociation constants (K(E,ATH)) of approximately 130 and approximately 1780 nM for wild-type and R150A fXa, respectively.	Heparin	274-281	coagulation factor X	Homo sapiens	105-108
16357320-4	2006	TACI binding appears to require heparan sulfate posttranslational modifications of syndecan-2, because free heparin or pretreatment with heparitinase blocked the interaction.	Heparin	108-115	syndecan 2	Homo sapiens	83-93
15034796-8	2004	Anticoagulants, such as low-molecular-weight heparin, may act to prevent these complications both by interfering with TF-mediated activation of clotting and by directly down-regulating angiogenesis.	Heparin	45-52	coagulation factor III, tissue factor	Homo sapiens	118-120
11832456-6	2002	Apical-to-basal Ca(i)2+ waves were induced by acetylcholine and initiation of these waves was blocked by the InsP3R inhibitor heparin, whereas propagation into the basolateral region was inhibited by the cADPR inhibitor 8-amino-cADPR.	Heparin	126-133	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	109-115
14730971-0	2004	Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change.	Heparin	79-86	serpin family C member 1	Homo sapiens	63-75
11858483-4	2002	The effect of hirudin, the synthetic pentasaccharide SR90107/Org31540 (SP) and heparin were measured on TG in PRP and WB.	Heparin	79-86	proline rich protein 2-like 1	Rattus norvegicus	110-113
24562756-11	2002	Conclusions Of the patients in MITRA and MIR 92% received heparin during AMI.	Heparin	58-65	membrane associated ring-CH-type finger 8	Homo sapiens	41-44
16436387-5	2006	We now show that HRGP330 binds heparin/HS with the same capacity as full-length HRGP, and the binding is Zn(2+)-dependent.	Heparin	31-38	histidine rich glycoprotein	Homo sapiens	17-21
16436387-6	2006	Peptides derived from the His/Pro-rich domain of HRGP downstream of HRGP330 fail to inhibit endothelial cell migration and display a significantly reduced heparin-binding capacity.	Heparin	155-162	histidine rich glycoprotein	Homo sapiens	49-53
16322097-4	2006	The results presented in this study demonstrate that this heparin binding domain (HBD) is the region of Vn that binds to the cysteine loop region of beta3 and that this region is sufficient to mediate the positive effects of Vn on IGF-I signaling.	Heparin	58-65	vitronectin	Homo sapiens	104-106
16633175-4	2006	Here, we report the reconstruction of a frontal bone defect using heparin together with bovine type I collagen, hyaluronic acid, and fibrin as vehicles for BMP-2.	Heparin	66-73	bone morphogenetic protein 2	Bos taurus	156-161
11886166-4	2002	We show that vIL-10 will bind to heparin and use this property to purify vIL-10 from factor Xa cleaved products and trace contaminants using heparin agarose chromatography.	Heparin	33-40	coagulation factor X	Homo sapiens	85-94
14730971-0	2004	Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change.	Heparin	141-148	serpin family C member 1	Homo sapiens	63-75
11886166-4	2002	We show that vIL-10 will bind to heparin and use this property to purify vIL-10 from factor Xa cleaved products and trace contaminants using heparin agarose chromatography.	Heparin	141-148	coagulation factor X	Homo sapiens	85-94
14730971-1	2004	The N-terminal region residues, Lys11, Arg13, and Arg24, of the plasma coagulation inhibitor, antithrombin, have been implicated in binding of the anticoagulant polysaccharide, heparin, from the identification of natural mutants with impaired heparin binding or by the X-ray structure of a complex of the inhibitor with a high-affinity heparin pentasaccharide.	Heparin	177-184	serpin family C member 1	Homo sapiens	94-106
14730971-1	2004	The N-terminal region residues, Lys11, Arg13, and Arg24, of the plasma coagulation inhibitor, antithrombin, have been implicated in binding of the anticoagulant polysaccharide, heparin, from the identification of natural mutants with impaired heparin binding or by the X-ray structure of a complex of the inhibitor with a high-affinity heparin pentasaccharide.	Heparin	243-250	serpin family C member 1	Homo sapiens	94-106
14727968-18	2002	The clinical tolerability and the efficacy of low molecular weight heparins led to the concept that inhibition of further thrombin generation, by blocking factor Xa alone, can be an effective way of preventing thrombus growth without inactivating thrombin.	Heparin	67-75	coagulation factor X	Homo sapiens	155-164
16602274-3	2006	However, cTnI immunoassay results are prone to interference from many substances such as heparin and common drugs.	Heparin	89-96	troponin I3, cardiac type	Homo sapiens	9-13
14730971-6	2004	The N-terminal region of antithrombin is thus critical for high-affinity heparin binding, Lys11 and Arg24 being responsible for maintaining appreciable and comparable binding energy, whereas Arg13 is less important.	Heparin	73-80	serpin family C member 1	Homo sapiens	25-37
14585835-0	2004	Characterization of endostatin binding to heparin and heparan sulfate by surface plasmon resonance and molecular modeling: role of divalent cations.	Heparin	42-49	collagen type XVIII alpha 1 chain	Homo sapiens	20-30
16398531-7	2006	Heparin was covalently bound at a high level (1.11 +/- 0.06 mug/cm(2)) and was shown to be active, with demonstrable Factor Xa inhibition and platelet factor IV binding.	Heparin	0-7	coagulation factor X	Homo sapiens	117-126
14585835-3	2004	Here we determined the kinetics and affinity of the interaction of endostatin with heparin/heparan sulfate and investigated the effects of divalent cations on these interactions and on the biological activities of endostatin.	Heparin	83-90	collagen type XVIII alpha 1 chain	Homo sapiens	67-77
11784325-10	2002	The affinity of ECP for heparin was assessed and found to be reduced when tryptophan residues, one of which is located at a position in the catalytic subsite of ribonuclease in ECP, were modified.	Heparin	24-31	ribonuclease A family member 3	Homo sapiens	16-19
14585835-4	2004	The binding of human recombinant endostatin to heparin and heparan sulfate was studied by surface plasmon resonance using BIAcore technology and further characterized by docking and molecular dynamics simulations.	Heparin	47-54	collagen type XVIII alpha 1 chain	Homo sapiens	33-43
11784325-10	2002	The affinity of ECP for heparin was assessed and found to be reduced when tryptophan residues, one of which is located at a position in the catalytic subsite of ribonuclease in ECP, were modified.	Heparin	24-31	ribonuclease A family member 3	Homo sapiens	177-180
16508209-6	2006	In fact, lipoprotein lipase and hepatic lipase activities in the post-heparin plasma of Angptl3-null mice were 1.57 times and 1.42 times higher than those of wild-type mice, respectively.	Heparin	70-77	lipoprotein lipase	Mus musculus	9-27
14585835-5	2004	Kinetic data, evaluated using a 1:1 interaction model, showed that heparan sulfate bound to and dissociated from endostatin faster than heparin and that endostatin bound to heparin and heparan sulfate with a moderate affinity (K(D) approximately 2 microm).	Heparin	173-180	collagen type XVIII alpha 1 chain	Homo sapiens	153-163
16360197-7	2006	RESULTS AND CONCLUSIONS: The results show clear age-related differences in APTT for the same Anti-Factor Xa heparin concentration.	Heparin	108-115	coagulation factor X	Homo sapiens	98-107
16360197-9	2006	The Anti-Factor IIa activity of heparin for a given Anti-Factor Xa activity also differed between age-specific plasma pools.	Heparin	32-39	coagulation factor X	Homo sapiens	57-66
14585835-7	2004	The binding of endostatin to heparin and heparan sulfate required the presence of divalent cations.	Heparin	29-36	collagen type XVIII alpha 1 chain	Homo sapiens	15-25
15812146-8	2004	Physical binding of VEGF to the heparin may then prevent a rapid clearance from the implant, while the release rate may become coupled to the degradation of the collagen matrix.	Heparin	32-39	vascular endothelial growth factor A	Rattus norvegicus	20-24
17323590-1	2006	The antithrombin binding sequence of heparin, a pentasaccharide, has been synthesized as fondaparinux, an indirect, selective, and reversible factor Xa inhibitor.	Heparin	37-44	coagulation factor X	Homo sapiens	142-151
11782444-2	2002	WISP-1 belongs to the CCN family of growth factors, which are cysteine-rich, heparin-binding, secreted proteins associated with the extracellular matrix, and can interact with cellular integrins.	Heparin	77-84	cellular communication network factor 4	Homo sapiens	0-6
11677228-7	2001	The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa.	Heparin	54-61	coagulation factor X	Homo sapiens	238-247
14691161-1	2004	PURPOSE: To investigate the growth promoting and chemotactic effects of heparin binding epidermal growth factor-like growth factor (HB-EGF), recently shown to be upregulated by ultraviolet irradiation in pterygium-derived epithelium cells (PECs) and pterygium fibroblasts (PFs).	Heparin	72-79	heparin binding EGF like growth factor	Homo sapiens	132-138
11718702-6	2001	RESULTS: MMP-9 showed higher concentrations in serum samples than in heparin plasma and was about threefold higher in serum samples collected in tubes with clot activator than in native serum samples.	Heparin	69-76	matrix metallopeptidase 9	Homo sapiens	9-14
11718702-9	2001	CONCLUSIONS: To optimise the diagnostic validity of the MMP-9 in blood, measurements should be performed in heparin plasma but not in serum.	Heparin	108-115	matrix metallopeptidase 9	Homo sapiens	56-61
11722182-5	2001	Moreover, two interesting findings related to MMP-9 interactions with heparin and TIMP-1 resulted from our studies.	Heparin	70-77	matrix metallopeptidase 9	Homo sapiens	46-51
11533057-0	2001	Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin.	Heparin	42-49	tryptase beta 2	Mus musculus	118-138
11533057-0	2001	Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6: formation of active tryptase monomers in the presence of low molecular weight heparin.	Heparin	218-225	tryptase beta 2	Mus musculus	118-138
11533057-4	2001	The ability of heparin-related saccharides to activate a recombinant murine tryptase, mouse mast cell protease-6 (mMCP-6), was strongly dependent on anionic charge density and size.	Heparin	15-22	tryptase beta 2	Mus musculus	92-112
11533057-4	2001	The ability of heparin-related saccharides to activate a recombinant murine tryptase, mouse mast cell protease-6 (mMCP-6), was strongly dependent on anionic charge density and size.	Heparin	15-22	tryptase beta 2	Mus musculus	114-120
16095917-3	2005	However, co-over-expression of E. coli chaperonins GroEL/GroES solubilized approximately 50% of the protein, which was purified by ion-exchange and heparin-affinity chromatography.	Heparin	148-155	chaperonin GroES	Escherichia coli	57-62
16392680-5	2005	Treatment of normal mice with FR177391 resulted in an increase in heparin-releasable lipoprotein lipase (LPL) activity in the blood and epididymal fat tissue.	Heparin	66-73	lipoprotein lipase	Mus musculus	105-108
16027123-9	2005	Binding assays on heparin-Sepharose showed that, at acidic pH, the triple mutant mGM-CSF binds to immobilized heparin with significantly higher affinity than wild type (WT) mGM-CSF and that neither protein binds to the column at neutral pH.	Heparin	110-117	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	81-88
16027123-10	2005	The fact that even WT mGM-CSF binds to heparin at acidic pH indicates the existence of a distinct, lower affinity heparin-binding site in the protein.	Heparin	39-46	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	22-29
16027123-10	2005	The fact that even WT mGM-CSF binds to heparin at acidic pH indicates the existence of a distinct, lower affinity heparin-binding site in the protein.	Heparin	114-121	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	22-29
16027123-11	2005	Chemical modification of the single histidine residue (His15) located in helix A of WT mGM-CSF with diethyl pyrocarbonate totally abolished binding to immobilized heparin.	Heparin	163-170	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	87-94
16027123-12	2005	Moreover, replacement of His15 for an alanine residue significantly reduced the affinity of mGM-CSF for heparin at pH 5.0 and completely blocked heparin binding to a synthetic peptide corresponding to helix A of GM-CSF.	Heparin	104-111	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	92-99
16027123-12	2005	Moreover, replacement of His15 for an alanine residue significantly reduced the affinity of mGM-CSF for heparin at pH 5.0 and completely blocked heparin binding to a synthetic peptide corresponding to helix A of GM-CSF.	Heparin	104-111	colony stimulating factor 2 (granulocyte-macrophage)	Mus musculus	93-99
16027124-10	2005	It is therefore likely that a heparin-like domain of heparan sulfate/heparin forms a complex with VEGF165 and VEGFR-2 via the exon 7-encoded region, thereby enhancing VEGF165-dependent signaling.	Heparin	30-37	kinase insert domain receptor	Homo sapiens	110-117
11533057-5	2001	The dose-response curve for heparin-induced mMCP-6 activation displayed a bell-shaped appearance, indicating that heparin acts by binding to more than one tryptase monomer simultaneously.	Heparin	28-35	tryptase beta 2	Mus musculus	44-50
11533057-5	2001	The dose-response curve for heparin-induced mMCP-6 activation displayed a bell-shaped appearance, indicating that heparin acts by binding to more than one tryptase monomer simultaneously.	Heparin	114-121	tryptase beta 2	Mus musculus	44-50
11514538-0	2001	Vascular endothelial growth factor 165 (VEGF(165)) activities are inhibited by carboxymethyl benzylamide dextran that competes for heparin binding to VEGF(165) and VEGF(165).KDR Complexes.	Heparin	131-138	kinase insert domain receptor	Homo sapiens	174-177
16027124-10	2005	It is therefore likely that a heparin-like domain of heparan sulfate/heparin forms a complex with VEGF165 and VEGFR-2 via the exon 7-encoded region, thereby enhancing VEGF165-dependent signaling.	Heparin	69-76	kinase insert domain receptor	Homo sapiens	110-117
11514538-7	2001	Moreover, CMDB7 reduces the (125)I-VEGF(165) binding to coated heparin-albumin and prevents a heparin-induced increase in iodinated VEGF(165) binding to soluble (125)I-KDR-Fc chimera.	Heparin	94-101	kinase insert domain receptor	Homo sapiens	168-171
14694164-4	2004	Trifluoroethanol at concentrations of up to 20% (vol/vol) caused fibril extension of heparin-stabilized seeds, inducing a subtle change in the tertiary structure of beta(2)-microglobulin and stabilizing the fibrils at a neutral pH.	Heparin	85-92	beta-2-microglobulin	Homo sapiens	165-186
11514538-9	2001	In the presence of VEGF(165), (125)I-KDR-Fc binding to heparin is enhanced, and under these conditions, CMDB7 interferes with KDR binding.	Heparin	55-62	kinase insert domain receptor	Homo sapiens	37-40
11514538-10	2001	These data indicate that CMDB7 effectively inhibits the VEGF(165) activities by interfering with heparin binding to VEGF(165) and VEGF(165).KDR complexes but not by direct interactions with KDR.	Heparin	97-104	kinase insert domain receptor	Homo sapiens	140-143
11500500-4	2001	The formation of the high affinity complex required Arg-142, Lys-143, Arg-145, Lys-146, and Arg-147 from apoE and N- and 6-O-sulfo groups of the glucosamine units from the heparin fragment.	Heparin	172-179	DEAH-box helicase 40	Homo sapiens	92-99
16014615-2	2005	The goals of this study were to determine whether 1) gene transfer of extracellular superoxide dismutase (ecSOD) reduces levels of superoxide and improves endothelial function in the aorta and mesenteric artery in rats with heart failure, and 2) the heparin-binding domain (HBD) of ecSOD, by which ecSOD binds to cells, is required for protective effects of ecSOD.	Heparin	250-257	superoxide dismutase 3	Rattus norvegicus	70-104
16014615-2	2005	The goals of this study were to determine whether 1) gene transfer of extracellular superoxide dismutase (ecSOD) reduces levels of superoxide and improves endothelial function in the aorta and mesenteric artery in rats with heart failure, and 2) the heparin-binding domain (HBD) of ecSOD, by which ecSOD binds to cells, is required for protective effects of ecSOD.	Heparin	250-257	superoxide dismutase 3	Rattus norvegicus	106-111
14679575-4	2003	ATIII-alpha and ATIII-beta-fractions preseparated by heparin affinity chromatography showed an analogous but shifted spot pattern consisting each of one major and three minor isoforms.	Heparin	53-60	serpin family C member 1	Homo sapiens	0-5
16079449-9	2005	A trend towards statistical significance was observed in the 6-month secondary re-intervention and limb salvage rates (10.7% versus 18.8%; p = 0.0501 and 93.9% versus 88.5%; p = 0.053) in the DTI-GP IIb-IIIa versus the UFH group, respectively.	Heparin	219-222	integrin subunit alpha 2b	Homo sapiens	196-202
16233851-6	2005	These findings indicate that 6-DSH and 2-DSH have the same ability to promote the growth of human NSPCs as intact heparin.	Heparin	114-121	dishevelled segment polarity protein 1 pseudogene 1	Homo sapiens	41-44
16233851-7	2005	Our results suggest that these two novel heparin derivates, especially 6-DSH, could be used in clinical applications for ex vivo human NSPC culture, as a lower-risk growth co-adjuvant than intact heparin.	Heparin	41-48	dishevelled segment polarity protein 1 pseudogene 1	Homo sapiens	73-76
15919224-6	2005	We show that Hlp/LBP, besides laminin, also binds heparin and heparan sulfate.	Heparin	50-57	lipopolysaccharide binding protein	Homo sapiens	17-20
11591377-4	2001	ADR7 and ADR22 have an affinity of 180 pM and 370 pM respectively for mouse MCP-1, they can antagonise MCP-1 binding to heparin and specifically antagonise MCP-1 induced chemotaxis in a cell based assay.	Heparin	120-127	chemokine (C-C motif) ligand 2	Mus musculus	76-81
11591377-4	2001	ADR7 and ADR22 have an affinity of 180 pM and 370 pM respectively for mouse MCP-1, they can antagonise MCP-1 binding to heparin and specifically antagonise MCP-1 induced chemotaxis in a cell based assay.	Heparin	120-127	chemokine (C-C motif) ligand 2	Mus musculus	103-108
11591377-4	2001	ADR7 and ADR22 have an affinity of 180 pM and 370 pM respectively for mouse MCP-1, they can antagonise MCP-1 binding to heparin and specifically antagonise MCP-1 induced chemotaxis in a cell based assay.	Heparin	120-127	chemokine (C-C motif) ligand 2	Mus musculus	103-108
11560562-13	2001	CONCLUSIONS: Co-medication with UFH attenuated platelet inhibition during treatment with GPIIb/IIIa-antagonists, but these effects were not seen with the low molecular weight heparin reviparin.	Heparin	32-35	integrin subunit alpha 2b	Homo sapiens	89-94
11560299-3	2001	Abciximab and heparin were administered according to guidelines of the Evaluation of PTCA [percutaneous transluminal coronary angioplasty] to Improve Long-Term Outcome With Abciximab GP IIb/IIIa Blockade (EPILOG).	Heparin	14-21	integrin subunit alpha 2b	Homo sapiens	183-189
14679575-4	2003	ATIII-alpha and ATIII-beta-fractions preseparated by heparin affinity chromatography showed an analogous but shifted spot pattern consisting each of one major and three minor isoforms.	Heparin	53-60	serpin family C member 1	Homo sapiens	16-21
15939289-8	2005	The secreted EDN was purified to a purity of 98 % by the use of SP Sepharose FF ion-exchange chromatography and Sepharose-heparin Hi Trap affinity chromatography.	Heparin	122-129	collagen, type XVIII, alpha 1	Mus musculus	13-16
11520060-7	2001	Furthermore, syndecan-2 induced stronger adhesion to collagen type I, specifically inhibited by heparin.	Heparin	96-103	syndecan 2	Homo sapiens	13-23
14638802-10	2003	SCR 7 contains a heparin binding site, and heparin was found to inhibit FHL-1 binding to Fba.	Heparin	17-24	four and a half LIM domains 1	Homo sapiens	72-77
11437360-3	2001	Heparin is known to bind to vitronectin.	Heparin	0-7	vitronectin	Homo sapiens	28-39
11437360-5	2001	Previous studies demonstrated that heparin diminishes vitronectin inhibition of complement activity.	Heparin	35-42	vitronectin	Homo sapiens	54-65
15895163-9	2005	Recently it was demonstrated that ixolaris binds to heparin-binding exosite of FXa, thus impairing the recognition of prothrombin by the enzyme.	Heparin	52-59	coagulation factor X	Homo sapiens	79-82
11437360-8	2001	2DARE allowed simultaneous determination of binding affinity of heparin for vitronectin as well as the M(r) of the heparin species.	Heparin	64-71	vitronectin	Homo sapiens	76-87
14638802-10	2003	SCR 7 contains a heparin binding site, and heparin was found to inhibit FHL-1 binding to Fba.	Heparin	17-24	F-box protein 3	Homo sapiens	89-92
11437360-9	2001	In the 2DARE experiment, the interaction of heparin with vitronectin caused retardation of the movement of the heparin through the tube gel in the first dimension.	Heparin	44-51	vitronectin	Homo sapiens	57-68
11437360-12	2001	2DARE analysis of the interaction of heparin with vitronectin clearly demonstrated that a sub-population of heparin chains with M(r) &gt; 8000 bound vitronectin with high affinity whereas most high M(r) chains and all lower M(r) chains showed little to no affinity for vitronectin.	Heparin	37-44	vitronectin	Homo sapiens	50-61
15603815-3	2005	The four osteoblast-adhesive peptides discussed in this paper are mapped on the 339-364 sequence (339MAPRPSLAKKQRFRHRNRKGYRSQRG364) located in the primary heparin-binding site of human vitronectin (HVP).	Heparin	155-162	vitronectin	Homo sapiens	185-196
16013009-0	2005	Modulation of the effect of vascular endothelial growth factor on endothelial cells by heparin: critical role of nitric oxide-mediated mechanisms.	Heparin	87-94	vascular endothelial growth factor A	Bos taurus	28-62
11437360-12	2001	2DARE analysis of the interaction of heparin with vitronectin clearly demonstrated that a sub-population of heparin chains with M(r) &gt; 8000 bound vitronectin with high affinity whereas most high M(r) chains and all lower M(r) chains showed little to no affinity for vitronectin.	Heparin	37-44	vitronectin	Homo sapiens	149-160
14638802-10	2003	SCR 7 contains a heparin binding site, and heparin was found to inhibit FHL-1 binding to Fba.	Heparin	43-50	four and a half LIM domains 1	Homo sapiens	72-77
11437360-12	2001	2DARE analysis of the interaction of heparin with vitronectin clearly demonstrated that a sub-population of heparin chains with M(r) &gt; 8000 bound vitronectin with high affinity whereas most high M(r) chains and all lower M(r) chains showed little to no affinity for vitronectin.	Heparin	37-44	vitronectin	Homo sapiens	149-160
16013009-2	2005	In particular, further insight is needed into the interaction of heparin with the potent heparin-binding angiogenic factor, vascular endothelial growth factor (VEGF).	Heparin	65-72	vascular endothelial growth factor A	Bos taurus	124-158
16013009-2	2005	In particular, further insight is needed into the interaction of heparin with the potent heparin-binding angiogenic factor, vascular endothelial growth factor (VEGF).	Heparin	65-72	vascular endothelial growth factor A	Bos taurus	160-164
11437360-12	2001	2DARE analysis of the interaction of heparin with vitronectin clearly demonstrated that a sub-population of heparin chains with M(r) &gt; 8000 bound vitronectin with high affinity whereas most high M(r) chains and all lower M(r) chains showed little to no affinity for vitronectin.	Heparin	108-115	vitronectin	Homo sapiens	50-61
14638802-10	2003	SCR 7 contains a heparin binding site, and heparin was found to inhibit FHL-1 binding to Fba.	Heparin	43-50	F-box protein 3	Homo sapiens	89-92
11437360-12	2001	2DARE analysis of the interaction of heparin with vitronectin clearly demonstrated that a sub-population of heparin chains with M(r) &gt; 8000 bound vitronectin with high affinity whereas most high M(r) chains and all lower M(r) chains showed little to no affinity for vitronectin.	Heparin	108-115	vitronectin	Homo sapiens	149-160
11437360-12	2001	2DARE analysis of the interaction of heparin with vitronectin clearly demonstrated that a sub-population of heparin chains with M(r) &gt; 8000 bound vitronectin with high affinity whereas most high M(r) chains and all lower M(r) chains showed little to no affinity for vitronectin.	Heparin	108-115	vitronectin	Homo sapiens	149-160
16013009-3	2005	This study aimed to examine the effect of heparin on VEGF-mediated EC responses.	Heparin	42-49	vascular endothelial growth factor A	Bos taurus	53-57
15697227-8	2005	Enzymatic digestion of heparan sulfate proteoglycan (HSPG) with heparinase I and addition of heparin and poly-l-lysin as competitors of HSPG and HSPG ligands, respectively, resulted in a significant loss in liposome internalization.	Heparin	64-71	CD44 molecule (Indian blood group)	Homo sapiens	23-51
15697227-8	2005	Enzymatic digestion of heparan sulfate proteoglycan (HSPG) with heparinase I and addition of heparin and poly-l-lysin as competitors of HSPG and HSPG ligands, respectively, resulted in a significant loss in liposome internalization.	Heparin	64-71	CD44 molecule (Indian blood group)	Homo sapiens	53-57
15699163-5	2005	Using a fluorescence-based assay, we showed that clinically used heparin preparations significantly enhance the ability of LBP to catalytically disaggregate and transfer LPS to CD14, the LPS receptor.	Heparin	65-72	lipopolysaccharide binding protein	Homo sapiens	123-126
11505077-1	2001	Danaparoid and heparin, on the basis of anti-activated factor X (anti-FXa) activity, were equipotent in accelerating the rate of interaction of FXa and antithrombin III.	Heparin	15-22	serpin family C member 1	Rattus norvegicus	152-168
11451924-9	2001	Heparin as low as 0.01 mg/mL significantly downregulated expression of TGF-beta(1) and FGF-1-stimulated FGF-2 and FGFR-1.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	87-92
16707926-4	2005	We previously found novel heparin-binding VEGFs, designated VEGF-F that specifically recognizes KDR in snake venoms.	Heparin	26-33	kinase insert domain receptor	Homo sapiens	96-99
14675100-4	2003	Stimulation of P2X1 with alpha,beta-Me-ATP resulted in shape change and small aggregate formation in heparin-anticoagulated platelet preparations.	Heparin	101-108	purinergic receptor P2X 1	Homo sapiens	15-19
15583751-6	2004	PMN and monocyte activation, reflected by increased surface expression of the CD11b adhesion molecule, was induced by HIT plasma in a heparin-dependent manner.	Heparin	134-141	integrin subunit alpha M	Homo sapiens	78-83
11451924-9	2001	Heparin as low as 0.01 mg/mL significantly downregulated expression of TGF-beta(1) and FGF-1-stimulated FGF-2 and FGFR-1.	Heparin	0-7	Fibroblast growth factor receptor 1	Rattus norvegicus	114-120
11399083-1	2001	Factor H (FH) is a regulatory cofactor for the protease factor I in the breakdown of C3b in the complement system of immune defence, and binds to heparin and other polyanionic substrates.	Heparin	146-153	complement factor H	Homo sapiens	0-8
11399083-1	2001	Factor H (FH) is a regulatory cofactor for the protease factor I in the breakdown of C3b in the complement system of immune defence, and binds to heparin and other polyanionic substrates.	Heparin	146-153	complement factor H	Homo sapiens	10-12
14719183-0	2003	Modulation of antithrombin-protease interactions by semisynthetic low-molecular-weight heparins with different sulfation patterns.	Heparin	87-95	serpin family C member 1	Homo sapiens	14-26
11399083-15	2001	These bent-back domain structures may correspond to conformational flexibility in FH and enable the multiple FH binding sites for C3 and heparin to come into close proximity.	Heparin	137-144	complement factor H	Homo sapiens	82-84
11399083-15	2001	These bent-back domain structures may correspond to conformational flexibility in FH and enable the multiple FH binding sites for C3 and heparin to come into close proximity.	Heparin	137-144	complement factor H	Homo sapiens	109-111
11401583-7	2001	We show that the heparin antagonists Polybrene and protamine are potent inhibitors of both human lung tryptase and of recombinant mouse tryptase (mouse mast cell protease 6).	Heparin	17-24	tryptase beta 2	Mus musculus	152-172
11380263-1	2001	Activation of antithrombin by high-affinity heparin as an inhibitor of factor Xa has been ascribed to an allosteric switch between two conformations of the reactive center loop.	Heparin	44-51	coagulation factor X	Homo sapiens	71-80
15546573-1	2004	BACKGROUND: Through site-directed mutagenesis we have created a favorable fibroblast growth factor-1 (FGF-1) mutant (S130K) and linked it to a heparin-binding growth-associated molecule (HBGAM) to form the chimera S130K-HBGAM creating a heparin-independent, endothelial cell (EC)-specific mitogen.	Heparin	143-150	fibroblast growth factor 1	Canis lupus familiaris	74-100
15546573-1	2004	BACKGROUND: Through site-directed mutagenesis we have created a favorable fibroblast growth factor-1 (FGF-1) mutant (S130K) and linked it to a heparin-binding growth-associated molecule (HBGAM) to form the chimera S130K-HBGAM creating a heparin-independent, endothelial cell (EC)-specific mitogen.	Heparin	143-150	fibroblast growth factor 1	Canis lupus familiaris	102-107
15546573-1	2004	BACKGROUND: Through site-directed mutagenesis we have created a favorable fibroblast growth factor-1 (FGF-1) mutant (S130K) and linked it to a heparin-binding growth-associated molecule (HBGAM) to form the chimera S130K-HBGAM creating a heparin-independent, endothelial cell (EC)-specific mitogen.	Heparin	237-244	fibroblast growth factor 1	Canis lupus familiaris	74-100
15546573-1	2004	BACKGROUND: Through site-directed mutagenesis we have created a favorable fibroblast growth factor-1 (FGF-1) mutant (S130K) and linked it to a heparin-binding growth-associated molecule (HBGAM) to form the chimera S130K-HBGAM creating a heparin-independent, endothelial cell (EC)-specific mitogen.	Heparin	237-244	fibroblast growth factor 1	Canis lupus familiaris	102-107
11373076-0	2001	Heparin-enhanced zymographic detection of matrilysin and collagenases.	Heparin	0-7	matrix metallopeptidase 7	Rattus norvegicus	42-52
11373076-2	2001	In this report, heparin was used to enhance the zymographic assays for MMP-7, -1, and -13.	Heparin	16-23	matrix metallopeptidase 7	Rattus norvegicus	71-89
14607764-3	2003	It is a pentasaccharide mimicking the site where heparin binds to antithrombin III (1).	Heparin	49-56	serpin family C member 1	Homo sapiens	66-82
11373076-3	2001	With the addition of heparin to the enzyme sample, MMP-7 can be detected at a level of 30 pg in transferrin zymography and MMP-1 and -13 can be detected at a level of 0.2 ng in gelatin zymography.	Heparin	21-28	matrix metallopeptidase 7	Rattus norvegicus	51-56
15191947-0	2004	The homozygous FcgammaRIIIa-158V genotype is a risk factor for heparin-induced thrombocytopenia in patients with antibodies to heparin-platelet factor 4 complexes.	Heparin	63-70	Fc gamma receptor IIIa	Homo sapiens	15-27
15191947-1	2004	We hypothesized that Fcgamma receptor IIIa (FcgammaRIIIa), a polymorphic receptor for the Fc portion of immunoglobulin G (IgG) other than FcgammaRIIa, was involved in heparin-induced thrombocytopenia (HIT).	Heparin	167-174	Fc gamma receptor IIIa	Homo sapiens	21-42
15191947-1	2004	We hypothesized that Fcgamma receptor IIIa (FcgammaRIIIa), a polymorphic receptor for the Fc portion of immunoglobulin G (IgG) other than FcgammaRIIa, was involved in heparin-induced thrombocytopenia (HIT).	Heparin	167-174	Fc gamma receptor IIIa	Homo sapiens	44-56
14566786-4	2003	We demonstrate that the blood compatibility of a surface with regard to coagulation, complement, and platelet activation can be improved by increasing the heparin surface concentration in the 6-12 pmol antithrombin/cm2 concentration interval.	Heparin	155-162	serpin family C member 1	Homo sapiens	202-214
15262496-8	2004	Like K8.1, Orf51 could bind to agarose-conjugated heparin, implicating this molecule in viral attachment to cells.	Heparin	50-57	keratin 81	Homo sapiens	5-9
14966081-0	2004	Heparin affects signaling pathways stimulated by fibroblast growth factor-1 and -2 in type II cells.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	49-82
14966081-2	2004	Heparin, a model for sulfated components of basement membrane matrices, is known to inhibit fibroblast growth factor (FGF)-2-stimulated DNA synthesis as well as gene expression of FGF-2 and its receptor in AT2 cells.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	118-121
14966081-5	2004	High-dose heparin reduced FGF-1- or FGF-2-stimulated phosphorylation of mitogen-activated protein kinase kinases (MEK1/2), p44/42 mitogen-activated protein kinases (MAPK/ERK1/2), stress-activated protein kinase/c-Jun NH(2)-terminal kinase, Akt/protein kinase B, and p90(RSK).	Heparin	10-17	fibroblast growth factor 1	Rattus norvegicus	26-31
15069070-0	2004	Identification and kinetics analysis of a novel heparin-binding site (KEDK) in human tenascin-C.	Heparin	48-55	tenascin C	Homo sapiens	85-95
15069070-2	2004	The aims of the present study were to examine the affinity of fibronectin type III repeats of TN-C fragments (TNIII) for heparin, to investigate the role of the TNIII4 domains in the binding of TN-C to heparin, and to delineate a sequence of amino acids within the TNIII4 domain, which mediates cooperative heparin binding.	Heparin	121-128	tenascin C	Homo sapiens	94-98
11397719-3	2001	We have recently shown that in the presence of heparin, lipolysis of LDL with bee venom PLA(2) induces aggregation and fusion of the particles.	Heparin	47-54	phospholipase A2 group IIA	Homo sapiens	88-93
11349012-3	2001	To discriminate between the coagulation-independent protective TNF effect and a potential protective procoagulant TNF effect, formation of peritoneal adhesions after CLP was inhibited with heparin, hirudin, or urokinase.	Heparin	189-196	leucine-rich repeat LGI family, member 4	Mus musculus	166-169
11290592-3	2001	There are conflicting results as to whether anticoagulant heparins can catalyze the antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged membrane surfaces, and calcium ion), which is the physiologically relevant form of the proteinase responsible for the activation of prothrombin to thrombin during the blood coagulation process.	Heparin	58-66	coagulation factor X	Homo sapiens	111-120
11290592-3	2001	There are conflicting results as to whether anticoagulant heparins can catalyze the antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged membrane surfaces, and calcium ion), which is the physiologically relevant form of the proteinase responsible for the activation of prothrombin to thrombin during the blood coagulation process.	Heparin	58-66	coagulation factor X	Homo sapiens	128-142
11290592-4	2001	In this study, a novel assay system was developed to compare the catalytic effect of different molecular-weight heparins in the antithrombin inhibition of factor Xa, either in free form or assembled into the prothrombinase complex during the process of prothrombin activation.	Heparin	112-120	coagulation factor X	Homo sapiens	155-164
11290592-4	2001	In this study, a novel assay system was developed to compare the catalytic effect of different molecular-weight heparins in the antithrombin inhibition of factor Xa, either in free form or assembled into the prothrombinase complex during the process of prothrombin activation.	Heparin	112-120	coagulation factor X	Homo sapiens	208-222
11290592-5	2001	This assay takes advantage of the unique property of a recombinant mutant antithrombin, which, similar to the wild-type antithrombin, rapidly inhibits factor Xa, but not thrombin, in the presence of heparin.	Heparin	199-206	coagulation factor X	Homo sapiens	151-160
11599124-10	2001	These results indicate that heparin and HS inhibited ET-1-induced ERK activation, resulting in suppression of Elk-1 phosphorylation, and lead to inhibition of c-fos gene expression through SRF-independent manner.	Heparin	28-35	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	159-164
15069070-2	2004	The aims of the present study were to examine the affinity of fibronectin type III repeats of TN-C fragments (TNIII) for heparin, to investigate the role of the TNIII4 domains in the binding of TN-C to heparin, and to delineate a sequence of amino acids within the TNIII4 domain, which mediates cooperative heparin binding.	Heparin	202-209	tenascin C	Homo sapiens	194-198
15069070-2	2004	The aims of the present study were to examine the affinity of fibronectin type III repeats of TN-C fragments (TNIII) for heparin, to investigate the role of the TNIII4 domains in the binding of TN-C to heparin, and to delineate a sequence of amino acids within the TNIII4 domain, which mediates cooperative heparin binding.	Heparin	202-209	tenascin C	Homo sapiens	194-198
14566788-0	2003	Interactions of antithrombin and proteins in the plasma contact activation system with immobilized functional heparin.	Heparin	110-117	serpin family C member 1	Homo sapiens	16-28
14686601-13	2003	Heparin inhibited TF by &gt;90%, but prolonged TEG-r by 97.4+/-1.6 min (1 U ml(-1)); FEPP inhibited TF by &gt;90% (100 microg ml(-1)) and prolonged TEG-r by 73.7+/-8.4 min (10 microg ml(-1)).	Heparin	0-7	coagulation factor III, tissue factor	Homo sapiens	18-20
14741048-6	2004	Using surface-plasmon-resonance-based sensor technology (Biacore), we demonstrate that TRAP ECD has higher affinity for heparin (K(D)=40 nM) compared with the A domain (K(D)=79 nM).	Heparin	120-127	TRAP	Homo sapiens	87-91
15111862-5	2004	Heparin activity of the explanted silyl-heparin grafts was determined by using an antithrombin-III based thrombin binding assay.	Heparin	0-7	serpin family C member 1	Canis lupus familiaris	82-98
11106649-2	2001	In human embryonic kidney 293 cells, the heparin-binding enzymes sPLA(2)-IIA, -IID, and -V promote stimulus-dependent arachidonic acid release and prostaglandin E(2) production in a manner dependent on the heparan sulfate proteoglycan glypican.	Heparin	41-48	phospholipase A2 group IIA	Homo sapiens	65-72
11098058-0	2001	Alternative splicing of the first F3 domain from chicken collagen XIV affects cell adhesion and heparin binding.	Heparin	96-103	collagen type XIV alpha 1 chain	Gallus gallus	57-69
11098058-10	2001	When full-length collagen XIV polypeptides that either contain or lack the first F3 domain are tested on heparin-Sepharose, a pronounced difference in their relative affinity is observed.	Heparin	105-112	collagen type XIV alpha 1 chain	Gallus gallus	17-29
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Heparin	6-13	AGBL carboxypeptidase 3	Homo sapiens	127-131
11113133-7	2001	Addition of heparin, which competes for the binding of TSP2 to LRP coreceptor proteoglycans, inhibited adhesion of control but not TSP2-null cells, and a blocking antibody to LRP as well as the LRP inhibitor, receptor-associated protein, also inhibited adhesion and increased MMP2 levels only in control fibroblasts.	Heparin	12-19	low density lipoprotein receptor-related protein 1	Mus musculus	63-66
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Heparin	188-195	AGBL carboxypeptidase 3	Homo sapiens	127-131
14686601-13	2003	Heparin inhibited TF by &gt;90%, but prolonged TEG-r by 97.4+/-1.6 min (1 U ml(-1)); FEPP inhibited TF by &gt;90% (100 microg ml(-1)) and prolonged TEG-r by 73.7+/-8.4 min (10 microg ml(-1)).	Heparin	0-7	coagulation factor III, tissue factor	Homo sapiens	100-102
15066178-11	2004	Furthermore, when acidic residues of the homologous proteinase PAPP-A2 (Asp1547, Glu1555 and Glu1567) were introduced into the corresponding positions in the sequence of PAPP-A, located in each of the three basic clusters of CCP3, binding to heparin was strongly impaired and cell surface binding was abrogated.	Heparin	242-249	AGBL carboxypeptidase 3	Homo sapiens	225-229
11113133-7	2001	Addition of heparin, which competes for the binding of TSP2 to LRP coreceptor proteoglycans, inhibited adhesion of control but not TSP2-null cells, and a blocking antibody to LRP as well as the LRP inhibitor, receptor-associated protein, also inhibited adhesion and increased MMP2 levels only in control fibroblasts.	Heparin	12-19	matrix metallopeptidase 2	Mus musculus	276-280
11223514-0	2001	Structure of fibroblast growth factor 9 shows a symmetric dimer with unique receptor- and heparin-binding interfaces.	Heparin	90-97	fibroblast growth factor 9	Homo sapiens	13-39
15085057-4	2004	Especially the additional value of GP IIb/IIIa inhibition on top of an aggressive antithrombotic therapy (including aspirin, heparins, and clopidogrel) requires further clarification.	Heparin	125-133	integrin subunit alpha 2b	Homo sapiens	35-41
14707146-3	2004	We detected lymphotactin-heparin binding by NMR and mapped this interaction to a narrow surface that wraps around the protein.	Heparin	25-32	X-C motif chemokine ligand 1	Homo sapiens	12-24
14707146-4	2004	Substitutions in and around this binding site and surface plasmon resonance analysis of heparin binding affinity identified two arginine residues of lymphotactin as critical for glycosaminoglycan binding.	Heparin	88-95	X-C motif chemokine ligand 1	Homo sapiens	149-161
11231277-6	2001	Aggrecanase activity generated by synovium in vitro and recombinant ADAMTS-5 cleaved aggrecan extensively, resulting in aggrecan fragments similar to those generated by chondrocyte-derived aggrecanases, and the activity was inhibited by heparin.	Heparin	237-244	ADAM metallopeptidase with thrombospondin type 1 motif 5	Homo sapiens	68-76
14561895-6	2003	In cross-linking experiments, HN bound IGFBP-3 but did not compete with IGF-I-IGFBP-3 binding; competitive ligand dot blot experiments revealed the 18-aa heparin-binding domain of IGFBP-3 as the binding site for HN.	Heparin	154-161	amyloid beta (A4) precursor protein	Mus musculus	151-153
11170730-0	2001	Heparin coinfusion during convection-enhanced delivery (CED) increases the distribution of the glial-derived neurotrophic factor (GDNF) ligand family in rat striatum and enhances the pharmacological activity of neurturin.	Heparin	0-7	neurturin	Rattus norvegicus	211-220
15061416-9	2004	Contaminated tap water had been used to dilute alcohol for skin antisepsis and for decontamination of the caps of heparin vials.	Heparin	114-121	nuclear RNA export factor 1	Homo sapiens	13-16
12812518-4	2003	Lipoprotein lipase (LPL) and hepatic lipase (HL) activities were determined in post-heparin plasma 9 h postprandially and on another occasion under fasting conditions.	Heparin	84-91	lipoprotein lipase	Homo sapiens	0-18
15030172-5	2004	Heparin sepharose purified preparation of 72 kDa progelatinase is composed of two distinct population of zymogens: a 72 kDa progelatinase tightly complexed with TIMP-2 (an ambient tissue inhibitor of metalloprotease in the smooth muscle plasma membrane), and a native 72 kDa progelatinase free of any detectable TIMP-2.	Heparin	0-7	TIMP metallopeptidase inhibitor 2	Bos taurus	161-167
15030172-5	2004	Heparin sepharose purified preparation of 72 kDa progelatinase is composed of two distinct population of zymogens: a 72 kDa progelatinase tightly complexed with TIMP-2 (an ambient tissue inhibitor of metalloprotease in the smooth muscle plasma membrane), and a native 72 kDa progelatinase free of any detectable TIMP-2.	Heparin	0-7	TIMP metallopeptidase inhibitor 2	Bos taurus	312-318
14502551-6	2003	We show here that, similar to antithrombin, a member of the FGF family, FGF7, selectively captures anti-Factor Xa and anti-Factor IIa activity from commercially and clinically applied heparin mixtures.	Heparin	184-191	serpin family C member 1	Homo sapiens	30-42
12860985-1	2003	The serpin antithrombin is a slow thrombin inhibitor that requires heparin to enhance its reaction rate.	Heparin	67-74	serpin family C member 1	Homo sapiens	11-23
14570890-0	2004	Mice expressing only covalent dimeric heparin binding-deficient lipoprotein lipase: muscles inefficiently secrete dimeric enzyme.	Heparin	38-45	lipoprotein lipase	Mus musculus	64-82
14570890-3	2004	By creating a mouse line that expresses covalent dimers of heparin-binding deficient LpL (hLpLHBM-Dimer) in muscle, we confirmed in vivo that linking two LpL monomers in a head to tail configuration creates a functional LpL.	Heparin	59-66	lipoprotein lipase	Mus musculus	85-88
14570890-3	2004	By creating a mouse line that expresses covalent dimers of heparin-binding deficient LpL (hLpLHBM-Dimer) in muscle, we confirmed in vivo that linking two LpL monomers in a head to tail configuration creates a functional LpL.	Heparin	59-66	lipoprotein lipase	Mus musculus	91-94
14570890-3	2004	By creating a mouse line that expresses covalent dimers of heparin-binding deficient LpL (hLpLHBM-Dimer) in muscle, we confirmed in vivo that linking two LpL monomers in a head to tail configuration creates a functional LpL.	Heparin	59-66	lipoprotein lipase	Mus musculus	91-94
12832413-0	2003	Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide.	Heparin	86-93	serpin family C member 1	Homo sapiens	54-66
14723347-2	2003	The absorption enhancing activity of these compounds (phytolaccosides B, D2, E, F, G and I) was determined by changes in transepithelial electrical resistance (TEER) and the transport amount of heparin disaccharide, the major repeating unit of heparin, across Caco-2 cell monolayers.	Heparin	194-201	immunoglobulin heavy diversity 2-15	Homo sapiens	73-90
12832413-9	2003	Thus, Ca2+ promotes heparin-catalyzed inhibition of f.IXa and f.Xa by antithrombin by augmenting the template mechanism.	Heparin	20-27	serpin family C member 1	Homo sapiens	70-82
14596625-1	2003	Recent studies have demonstrated the existence of a Ca(2+)-dependent heparin-binding site on factor Xa.	Heparin	69-76	coagulation factor X	Homo sapiens	93-102
12832413-10	2003	These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa.	Heparin	28-35	serpin family C member 1	Homo sapiens	78-90
14596625-2	2003	To characterize this heparin-binding site, the extrinsic fluorescence of fluorescein-labeled, active site-blocked factor Xa was monitored as it was titrated with glycosaminoglycans of various sulfate content and chain length.	Heparin	21-28	coagulation factor X	Homo sapiens	114-123
12832413-10	2003	These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa.	Heparin	28-35	serpin family C member 1	Homo sapiens	185-197
14575696-8	2003	It is proposed that PF4 inhibited the sequence of events recapitulated in the template mechanism describing heparin-dependent inhibition of fXa.	Heparin	108-115	coagulation factor X	Homo sapiens	140-143
12832413-10	2003	These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa.	Heparin	156-163	serpin family C member 1	Homo sapiens	78-90
12832413-10	2003	These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa.	Heparin	156-163	serpin family C member 1	Homo sapiens	185-197
13129712-2	2003	METHODS AND RESULTS: The rhES gene was efficiently expressed in the yeast strain, and heparin affinity chromatography yielded highly purified endostatin identified by Western blotting, which proved to significantly inhibit the growth of the ECV-304 cells in vitro and also the growth of the lung adenocarcinoma Astc-a-1 in nude mice.	Heparin	86-93	collagen type XVIII alpha 1 chain	Homo sapiens	142-152
12919181-1	2003	AIMS: To investigate the pharmacodynamic interaction of unfractionated heparin (UFH) and acetylic salicylic acid (ASA) on YM337, a monoclonal humanized antibody of the platelet GPIIb/IIIa receptor.	Heparin	71-78	integrin subunit alpha 2b	Homo sapiens	177-182
12919181-1	2003	AIMS: To investigate the pharmacodynamic interaction of unfractionated heparin (UFH) and acetylic salicylic acid (ASA) on YM337, a monoclonal humanized antibody of the platelet GPIIb/IIIa receptor.	Heparin	80-83	integrin subunit alpha 2b	Homo sapiens	177-182
12943500-3	2003	Low molecular weight heparins (LMWH) have several advantages over UF heparin therapy, making them attractive alternatives for use in combination with GP IIb/IIIa inhibitors.	Heparin	21-29	integrin subunit alpha 2b	Homo sapiens	150-156
12941037-9	2003	Moreover, both heparin and SanOrg123781A significantly inhibited fibrinopeptide A generated by the action of clot-bound thrombin on fibrinogen but also by free thrombin generated from prothrombin by clot-bound FXa with IC50 values of 4 +/- 0.6 and 1 +/- 0.1 micro g mL-1, respectively.	Heparin	15-22	coagulation factor X	Homo sapiens	210-213
12886459-5	2003	On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times).	Heparin	19-26	serpin family C member 1	Homo sapiens	135-147
12877649-0	2003	Can bivalirudin and provisional GP IIb/IIIa blockade REPLACE heparin and planned glycoprotein IIb/IIIa blockade during percutaneous coronary intervention?	Heparin	61-68	integrin subunit alpha 2b	Homo sapiens	32-38
12918125-9	2003	Using heparin, an antagonist of IP(3)R, almost abolished the peak increase in [Ca(2+)]i.	Heparin	6-13	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	32-38
12960955-9	2003	Triglycerides (TGs) decreased when the heparin infusion was started, as expected from the high circulating LPL activities.	Heparin	39-46	lipoprotein lipase	Homo sapiens	107-110
12689334-0	2003	Interaction of the 268-282 region of glycoprotein Ibalpha with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII.	Heparin	67-74	glycoprotein Ib platelet subunit alpha	Homo sapiens	37-57
12960955-12	2003	This study indicates that LMW heparin compared with conventional heparin causes as much or more depletion of LPL and subsequent impairment of TG clearing.	Heparin	30-37	lipoprotein lipase	Homo sapiens	109-112
12964742-1	2003	A new method using a combination of electrospray ionization mass spectrometry (ESI-MS) and tandem mass spectrometry (MSn) was developed for the identification and quantitative analysis of eight heparan sulfate (HS)- and heparin-derived delta-disaccharides obtained by enzymatic depolymerization.	Heparin	220-227	moesin	Bos taurus	117-120
12620813-4	2003	2-APB and heparin abolished norepinephrine (10 microM; 0 Ca2+)-evoked Ca2+ transients but increased caffeine (10 mM; 0 Ca2+) transients in fura 2-loaded myocytes.	Heparin	10-17	LOW QUALITY PROTEIN: carbonic anhydrase 2	Cavia porcellus	57-60
12620813-4	2003	2-APB and heparin abolished norepinephrine (10 microM; 0 Ca2+)-evoked Ca2+ transients but increased caffeine (10 mM; 0 Ca2+) transients in fura 2-loaded myocytes.	Heparin	10-17	LOW QUALITY PROTEIN: carbonic anhydrase 2	Cavia porcellus	70-73
12620813-4	2003	2-APB and heparin abolished norepinephrine (10 microM; 0 Ca2+)-evoked Ca2+ transients but increased caffeine (10 mM; 0 Ca2+) transients in fura 2-loaded myocytes.	Heparin	10-17	LOW QUALITY PROTEIN: carbonic anhydrase 2	Cavia porcellus	70-73
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	12-19	coagulation factor III, tissue factor	Homo sapiens	43-56
12808176-1	2003	BACKGROUND: Heparin inhibits prothrombotic tissue factor (TF) and releases its inhibitor, tissue factor pathway inhibitor (TFPI), from the endothelium, but repeated administration of heparin depletes vascular stores of TFPI.	Heparin	12-19	coagulation factor III, tissue factor	Homo sapiens	58-60
12808176-8	2003	In patients switched to UFH, TF levels remained unchanged compared with pre-randomization values, TFPI increased at each interval of HD sessions (all P&lt;0.035) and PF 1+2 increased pre-dialysis (P=0.015).	Heparin	24-27	coagulation factor III, tissue factor	Homo sapiens	29-31
12736188-5	2003	Although native SOD2 has no affinity for heparin, SOD2/3 binds to a heparin-agarose column.	Heparin	68-75	superoxide dismutase 2	Rattus norvegicus	50-56
12695507-1	2003	Covalent antithrombin-heparin (ATH) complexes, formed spontaneously between antithrombin (AT) and unfractionated standard heparin (H), have a potent ability to catalyze the inhibition of factor Xa (or thrombin) by added AT.	Heparin	22-29	serpin family C member 1	Homo sapiens	9-21
12695507-1	2003	Covalent antithrombin-heparin (ATH) complexes, formed spontaneously between antithrombin (AT) and unfractionated standard heparin (H), have a potent ability to catalyze the inhibition of factor Xa (or thrombin) by added AT.	Heparin	22-29	serpin family C member 1	Homo sapiens	76-88
12764609-0	2003	Histidine-rich glycoprotein plus zinc reverses growth inhibition of vascular smooth muscle cells by heparin.	Heparin	100-107	histidine rich glycoprotein	Homo sapiens	0-27
12773489-8	2003	Treatment of CD95-stimulated T cells with hIIA PLA2 resulted in the release of arachidonic acid but not oleic acid from cells and this release was blocked by heparin and heparinase III.	Heparin	158-165	Fas cell surface death receptor	Homo sapiens	13-17
12764609-3	2003	In this study, we have examined the effect of histidine-rich glycoprotein (HRG), a relatively abundant serum glycoprotein (~100 micrograms/ml in human serum), on the growth inhibition of cultured vascular SMC by heparin.	Heparin	212-219	histidine rich glycoprotein	Homo sapiens	46-73
12764609-3	2003	In this study, we have examined the effect of histidine-rich glycoprotein (HRG), a relatively abundant serum glycoprotein (~100 micrograms/ml in human serum), on the growth inhibition of cultured vascular SMC by heparin.	Heparin	212-219	histidine rich glycoprotein	Homo sapiens	75-78
12764609-5	2003	HRG reversed heparin-induced SMC growth inhibition in a dose dependent manner; 75% restoration of cell growth was observed when 100 micrograms/ml of HRG was co-added with 100 micrograms/ml heparin.	Heparin	13-20	histidine rich glycoprotein	Homo sapiens	0-3
12764609-5	2003	HRG reversed heparin-induced SMC growth inhibition in a dose dependent manner; 75% restoration of cell growth was observed when 100 micrograms/ml of HRG was co-added with 100 micrograms/ml heparin.	Heparin	13-20	histidine rich glycoprotein	Homo sapiens	149-152
12764609-5	2003	HRG reversed heparin-induced SMC growth inhibition in a dose dependent manner; 75% restoration of cell growth was observed when 100 micrograms/ml of HRG was co-added with 100 micrograms/ml heparin.	Heparin	189-196	histidine rich glycoprotein	Homo sapiens	0-3
12764609-8	2003	These findings indicate that HRG, in combination with the zinc ion, plays a role in modulating the SMC growth response in pathophysiological states and explain the lack of success of heparin as a therapeutic anti-restenosis drug in clinical trials.	Heparin	183-190	histidine rich glycoprotein	Homo sapiens	29-32
12808489-6	2003	The matrix metalloproteinase-1 secretory response of fibroblasts to low-density lipoprotein was attenuated by heparin, which inhibits low-density lipoprotein uptake through the low-density lipoprotein-receptor.	Heparin	110-117	matrix metallopeptidase 1	Homo sapiens	4-30
12701115-3	2003	Eosinophil granule proteins and purified eosinophil peroxidase markedly reduced the anticoagulant properties of the mast cell tryptase/heparin complex.	Heparin	135-142	tryptase delta 1	Homo sapiens	116-134
12701115-4	2003	Moreover, eosinophil peroxidase by itself functioned as a powerful procoagulant and also inhibited the anticoagulant actions of heparin in a chromogenic assay for antithrombin III/factor Xa activity.	Heparin	128-135	coagulation factor X	Homo sapiens	180-189
12729722-6	2003	The maize holoenzyme is about 10 times more sensitive towards CK2 inhibitor heparin, on the other hand, it is stimulated only 0% by polylysine as compared to the human counterpart.	Heparin	76-83	Calcium-dependent protein kinase 6	Zea mays	62-65
12556525-5	2003	The binding of L-selectin to isolated collagen XVIII was specifically inhibited by an anti-L-selectin monoclonal antibody, EDTA, treatment of the collagen XVIII with heparitinase or heparin but not by chemically desulfated heparin.	Heparin	182-189	selectin L	Rattus norvegicus	15-25
12697737-4	2003	All three mutations cause reduced binding to the central complement component C3b/C3d to heparin, as well as to endothelial cells.	Heparin	89-96	complement C3	Homo sapiens	78-81
12740133-5	2003	Heparin doses were adjusted to achieve subtherapeutic peak anti-factor Xa heparin activity levels of 0.11-0.25 units/mL.	Heparin	0-7	coagulation factor X	Homo sapiens	64-73
12808489-6	2003	The matrix metalloproteinase-1 secretory response of fibroblasts to low-density lipoprotein was attenuated by heparin, which inhibits low-density lipoprotein uptake through the low-density lipoprotein-receptor.	Heparin	110-117	low density lipoprotein receptor	Homo sapiens	177-209
12626998-10	2003	MEASUREMENTS AND MAIN RESULTS: Expression of GP IIb-IIIa and P-selectin on adenosine diphosphate-activated platelets and platelet-leukocyte aggregation were significantly lower after the passage of blood through the hemofilter in patients receiving an extracorporeal infusion of prostacyclin plus heparin when compared with control patients receiving heparin only.	Heparin	297-304	integrin subunit alpha 2b	Homo sapiens	45-51
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	78-85	serpin family C member 1	Homo sapiens	24-31
12626998-10	2003	MEASUREMENTS AND MAIN RESULTS: Expression of GP IIb-IIIa and P-selectin on adenosine diphosphate-activated platelets and platelet-leukocyte aggregation were significantly lower after the passage of blood through the hemofilter in patients receiving an extracorporeal infusion of prostacyclin plus heparin when compared with control patients receiving heparin only.	Heparin	351-358	integrin subunit alpha 2b	Homo sapiens	45-51
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	24-31
12535616-4	2003	PACE4 binds tightly to heparin and its heparin-binding region was found to be a cationic stretch of amino acids between residues 743 and 760.	Heparin	23-30	proprotein convertase subtilisin/kexin type 6	Homo sapiens	0-5
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	156-163
12535616-6	2003	PACE4 bound to the extracellular fraction was selectively dislodged by heparin into the culture medium.	Heparin	71-78	proprotein convertase subtilisin/kexin type 6	Homo sapiens	0-5
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	156-163
12535616-9	2003	In human placenta, PACE4 is mainly present in syncytiotrophoblasts and can be released by heparin.	Heparin	90-97	proprotein convertase subtilisin/kexin type 6	Homo sapiens	19-24
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	24-31
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	156-163
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	serpin family C member 1	Homo sapiens	156-163
12537186-14	2003	CONCLUSIONS: This study confirms the high frequency of heparin-PF4 antibodies after coronary artery bypass grafting and demonstrates a significantly higher incidence after bovine heparin.	Heparin	55-62	platelet factor 4	Bos taurus	63-66
12948833-6	2003	We prepared a synthetic hAT III (123-139)-coupled affinity chromatography system, and demonstrated that this novel affinity chromatography is useful for fractionation of highly active moieties in LMW-heparins.	Heparin	200-208	serpin family C member 1	Homo sapiens	24-31
12556442-0	2003	Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation.	Heparin	80-87	serpin family C member 1	Homo sapiens	0-16
12549600-7	2003	Preinjection of heparin reduced heart and adipose uptakes of FO and MCT:LCT:FO emulsions with increased uptake by liver, suggesting a role of lipoprotein lipase in catabolism of FO-containing emulsions.	Heparin	16-23	lipoprotein lipase	Mus musculus	142-160
15013268-6	2003	Heparin administration (at the beginning of PCI) resulted in a 65% inhibition of ss-TG (from 10,590 to 2833 ng/ml) and 90% inhibition of f1.2 formation (from 38.7 to 4.2 nmol/l) in shed blood of patients with clopidogrel pretreatment.	Heparin	0-7	coagulation factor XII	Homo sapiens	137-141
12556442-1	2003	The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor"s binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contribute approximately 40 and approximately 60% of the binding free energy, respectively.	Heparin	42-49	serpin family C member 1	Homo sapiens	61-77
12556442-1	2003	The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor"s binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contribute approximately 40 and approximately 60% of the binding free energy, respectively.	Heparin	42-49	serpin family C member 1	Homo sapiens	79-84
12556442-6	2003	In summary, although hydrophobic residues Phe-122 and Phe-121 make minimal contact with the pentasaccharide, they play a critical role in heparin binding and activation of antithrombin by coordinating the P-helix-mediated conformational change and organizing an extensive network of ionic and non-ionic interactions between positively charged heparin binding site residues and the cofactor.	Heparin	138-145	serpin family C member 1	Homo sapiens	172-184
12221095-2	2002	We previously observed that the cortical neuronal cell adhesion mediated by midkine (MK), a heparin (Hep)-binding growth factor, is specifically inhibited by oversulfated chondroitin sulfate-E (CS-E) (Ueoka, C., Kaneda, N., Okazaki, I., Nadanaka, S., Muramatsu, T., and Sugahara, K. (2000) J. Biol.	Heparin	92-99	midkine	Rattus norvegicus	76-83
12221095-2	2002	We previously observed that the cortical neuronal cell adhesion mediated by midkine (MK), a heparin (Hep)-binding growth factor, is specifically inhibited by oversulfated chondroitin sulfate-E (CS-E) (Ueoka, C., Kaneda, N., Okazaki, I., Nadanaka, S., Muramatsu, T., and Sugahara, K. (2000) J. Biol.	Heparin	92-99	midkine	Rattus norvegicus	85-87
12221095-9	2002	The kinetic constants k(a), k(d), and K(d) suggested that MK, PTN, FGF-16, FGF-18, and HB-EGF bound strongly to CS-E, in comparable degrees to the binding to Hep, whereas the intensity of binding of FGF-2 and FGF-10 toward CS-E was lower than that for Hep.	Heparin	158-161	midkine	Rattus norvegicus	58-60
12536119-2	2002	Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex.	Heparin	0-7	coagulation factor X	Homo sapiens	113-122
12536119-2	2002	Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex.	Heparin	0-7	coagulation factor X	Homo sapiens	181-190
12395090-7	2002	Expression of early response genes such as c-fos or Egr1 increased and sustained in the presence of heparin more than that without heparin.	Heparin	100-107	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	45-48
12000310-0	2002	Interaction of heparin with internally quenched fluorogenic peptides derived from heparin-binding consensus sequences, kallistatin and anti-thrombin III.	Heparin	15-22	serpin family A member 4	Homo sapiens	119-130
12353073-3	2002	The variant forms SDS-stable complexes with activated factor X (fXa) and its thermal stability and rate of factor Xa inhibition in the absence of heparin are identical to those of normal antithrombin.	Heparin	146-153	coagulation factor X	Homo sapiens	64-67
12173939-7	2002	However, it fully retains the FGF2-binding ability of the original heparin, as shown by its capacity to protect FGF2 from trypsin cleavage and to prevent the formation of heparan sulfate proteoglycan (HSPG)/FGF2/FGFR1 ternary complexes.	Heparin	67-74	heparan sulfate proteoglycan 2	Gallus gallus	201-205
11334198-0	2001	Evaluation of a new point of care heparin test for cardiopulmonary bypass: the TAS heparin management test.	Heparin	34-41	THAS	Homo sapiens	79-82
11334198-0	2001	Evaluation of a new point of care heparin test for cardiopulmonary bypass: the TAS heparin management test.	Heparin	83-90	THAS	Homo sapiens	79-82
11334198-3	2001	We evaluated a novel point of care device, the TAS (Pharmanetics, Raleigh, NC, USA) heparin management test (HMT), for its suitability in monitoring anticoagulation during CPB.	Heparin	84-91	THAS	Homo sapiens	47-50
12556442-6	2003	In summary, although hydrophobic residues Phe-122 and Phe-121 make minimal contact with the pentasaccharide, they play a critical role in heparin binding and activation of antithrombin by coordinating the P-helix-mediated conformational change and organizing an extensive network of ionic and non-ionic interactions between positively charged heparin binding site residues and the cofactor.	Heparin	343-350	serpin family C member 1	Homo sapiens	172-184
11084032-9	2001	3) An oligonucleotide DNA aptamer, HD22, which binds to the thrombin heparin-binding site (HBS) and inhibits thrombin interaction with GpIbalpha, reduced the apparent k(cat)/K(m) value by about 5-fold.	Heparin	69-76	glycoprotein Ib platelet subunit alpha	Homo sapiens	135-144
12182818-5	2002	Decorin was isolated by a second Q-Sepharose chromatography with affinity chromatographies on heparin-Sepharose and concanavalin A-Sepharose.	Heparin	94-101	decorin	Bos taurus	0-7
12711319-4	2003	In addition, the phosphorylation of the recombinant N in vitro can be blocked by a CK-II inhibitor, heparin.	Heparin	100-107	casein kinase 2 alpha 1	Homo sapiens	83-88
12244482-0	2002	Effects of calcium ions on the interactions between antithrombin and factor Xa mediated by variously sulfated, semisynthetic low-molecular-weight heparins.	Heparin	146-154	coagulation factor X	Homo sapiens	69-78
12244482-1	2002	A homogeneous set of low-molecular weight heparins, chemically modified to yield different degrees of sulfation, were investigated for their ability to interfere with the antithrombin (AT)-factor Xa (FXa) interaction process in the presence or absence of physiological concentrations of calcium ions.	Heparin	42-50	coagulation factor X	Homo sapiens	189-198
12244482-1	2002	A homogeneous set of low-molecular weight heparins, chemically modified to yield different degrees of sulfation, were investigated for their ability to interfere with the antithrombin (AT)-factor Xa (FXa) interaction process in the presence or absence of physiological concentrations of calcium ions.	Heparin	42-50	coagulation factor X	Homo sapiens	200-203
12244482-3	2002	Our data suggest that AT binding to heparin represents the main factor driving the FXa inhibition process.	Heparin	36-43	coagulation factor X	Homo sapiens	83-86
11983709-7	2002	Further purification of GRP94 by anion exchange and heparin affinity chromatography yielded resolution of GRP94 from the aminopeptidase activity.	Heparin	52-59	heat shock protein 90 beta family member 1	Homo sapiens	106-111
11255129-1	2001	Homogeneous casein kinase type 2 (CK2) was obtained from oocytes of Rana temporaria and cells of Drosophila melanogaster by chromatography on heparin-Sepharose, phosphocellulose, and Mono Q columns using a Pharmacia FPLC system.	Heparin	142-149	casein kinase IIalpha	Drosophila melanogaster	34-37
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	0-7	C-C motif chemokine ligand 24	Homo sapiens	56-61
11016923-1	2001	Heparin-like glycosaminogylcans protect human cathepsin B from alkaline pH-induced inactivation.	Heparin	0-7	cathepsin B	Homo sapiens	46-57
12871355-5	2003	RESULTS: The antithrombin activity and the effects on TG and APTT are primarily determined by the concentration of C-domain and independent of the source material (UFH or LMWH) or Mr. High Mr fractions (&gt;15 000) are less active, probably through interaction with non-antithrombin plasma proteins.	Heparin	164-167	serpin family C member 1	Homo sapiens	13-25
11016932-0	2001	Identification of a major heparin-binding site in kallistatin.	Heparin	26-33	serpin family A member 4	Homo sapiens	50-61
11016932-2	2001	The inhibitory activity of kallistatin is blocked upon its binding to heparin.	Heparin	70-77	serpin family A member 4	Homo sapiens	27-38
11016932-3	2001	In this study we attempted to locate the heparin-binding site of kallistatin using synthetic peptides derived from its surface regions and by site-directed mutagenesis of basic residues in these surface regions.	Heparin	41-48	serpin family A member 4	Homo sapiens	65-76
11016932-4	2001	Two synthetic peptides, containing clusters of positive-charged residues, one derived from the F helix and the other from the region encompassing the H helix and C2 sheet of kallistatin, were used to assess their heparin binding activity.	Heparin	213-220	serpin family A member 4	Homo sapiens	174-185
11016932-9	2001	Like kallistatin, the binding activity of K187A/K188A to tissue kallikrein was blocked by heparin, whereas K307A/R308A and K312A/K313A retained significant binding and inhibitory activities in the presence of heparin.	Heparin	90-97	serpin family A member 4	Homo sapiens	5-16
11016932-10	2001	These results indicate that the basic residues, particularly Lys(312)-Lys(313), in the region between the H helix and C2 sheet of kallistatin, comprise a major heparin-binding site responsible for its heparin-suppressed tissue kallikrein binding.	Heparin	160-167	serpin family A member 4	Homo sapiens	130-141
11150552-6	2001	As vitronectin and fibronectin each bind to heparin, these molecules are removed first and the heparin-Sepharose depletion occurs last in the sequence.	Heparin	44-51	vitronectin	Homo sapiens	3-14
11150552-6	2001	As vitronectin and fibronectin each bind to heparin, these molecules are removed first and the heparin-Sepharose depletion occurs last in the sequence.	Heparin	95-102	vitronectin	Homo sapiens	3-14
12071840-6	2002	Treatment of vitronectin in plasma with soluble heparin produced a similar degree of denaturation.	Heparin	48-55	vitronectin	Homo sapiens	13-24
12071840-13	2002	We also demonstrated that the avidity of heparin binding to vitronectin is governed by both the conformational state of the monomer and multimerization of the molecule.	Heparin	41-48	vitronectin	Homo sapiens	60-71
11973346-6	2002	Heparin-agarose-purified p33/30 was identified as histone H1.	Heparin	0-7	H1.0 linker histone	Homo sapiens	50-60
12108544-0	2002	Altered storage of proteases in mast cells from mice lacking heparin: a possible role for heparin in carboxypeptidase A processing.	Heparin	90-97	carboxypeptidase A1, pancreatic	Mus musculus	101-119
12108544-10	2002	This indicates that the processing of pro-CPA to its active form may require the presence of heparin and provides the first insight into a mechanism by which the absence of heparin may cause disturbed secretory granule organisation in mast cells.	Heparin	93-100	carboxypeptidase A1, pancreatic	Mus musculus	42-45
12108544-10	2002	This indicates that the processing of pro-CPA to its active form may require the presence of heparin and provides the first insight into a mechanism by which the absence of heparin may cause disturbed secretory granule organisation in mast cells.	Heparin	173-180	carboxypeptidase A1, pancreatic	Mus musculus	42-45
11832492-7	2002	Previous work established that the heparin-binding domain for HGF/SF is located in the N domain of HGF/SF.	Heparin	35-42	hepatocyte growth factor	Rattus norvegicus	62-68
11832492-7	2002	Previous work established that the heparin-binding domain for HGF/SF is located in the N domain of HGF/SF.	Heparin	35-42	hepatocyte growth factor	Rattus norvegicus	99-105
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	102-109	hepatocyte growth factor	Rattus norvegicus	38-41
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	102-109	hepatocyte growth factor	Rattus norvegicus	38-44
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	169-176	hepatocyte growth factor	Rattus norvegicus	38-41
11832492-8	2002	Additionally, the dimerization of the HGF/SF receptor (c-Met) by the ligand HGF/NK1 is facilitated by heparin and related sulfonated sugars on the cell surface, whereas heparin is not required for HGF/SF-mediated dimerization.	Heparin	169-176	hepatocyte growth factor	Rattus norvegicus	38-44
11123893-0	2000	Multiple domains contribute to heparin/heparan sulfate binding by human HIP/L29.	Heparin	31-38	ribosomal protein L29	Homo sapiens	72-79
11123893-2	2000	These activities are consistent with the proposed function of HIP/L29 as a heparin/heparan sulfate (Hp/HS) binding growth factor that has a preference for anticoagulantly active Hp/HS.	Heparin	75-82	ribosomal protein L29	Homo sapiens	62-69
11881992-1	2002	Conformational activation of antithrombin is a critical mechanism for the inhibition of factor Xa, a proteinase of the blood coagulation cascade, and is typically achieved with heparin, a polyanionic polysaccharide clinically used for anticoagulation.	Heparin	177-184	coagulation factor X	Homo sapiens	88-97
12889361-3	2003	Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen.	Heparin	297-304	serpin family C member 1	Homo sapiens	67-83
11741963-1	2002	Antithrombin requires allosteric activation by heparin for efficient inhibition of its target protease, factor Xa.	Heparin	47-54	coagulation factor X	Homo sapiens	104-113
11741963-2	2002	A pentasaccharide sequence found in heparin activates antithrombin by inducing conformational changes that affect the reactive center of the inhibitor resulting in optimal recognition by factor Xa.	Heparin	36-43	coagulation factor X	Homo sapiens	187-196
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	neuropilin 2	Homo sapiens	28-40
12613542-1	2002	The neuropilin-1 (NRP1) and neuropilin-2 (NRP2) receptors can bind the class 3 semaphorin subfamily and the heparin-binding forms of vascular endothelial growth factor (VEGF) and placenta growth factor (PlGF).	Heparin	108-115	neuropilin 2	Homo sapiens	42-46
10978312-9	2000	Direct interactions of MK with various glycosaminoglycans were then evaluated using surface plasmon resonance, showing that CS-E bound MK as strongly as heparin, followed by other over-sulfated CS isoforms, CS-H and CS-K.	Heparin	153-160	midkine	Rattus norvegicus	23-25
10978312-11	2000	These findings indicate that CS chains containing the E unit as well as heparin-like glycosaminoglycans may be involved in the expression and/or modulation of the multiple neuroregulatory functions of MK such as neuronal adhesion and migration and promotion of neurite outgrowth.	Heparin	72-79	midkine	Rattus norvegicus	201-203
12889361-3	2003	Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen.	Heparin	383-390	serpin family C member 1	Homo sapiens	67-83
12655414-4	2003	Both of their mothers" post-heparin plasma LPL activities were slightly or moderately impaired as well, without a decrease in the LPL mass level.	Heparin	28-35	lipoprotein lipase	Homo sapiens	43-46
11066091-9	2000	Grafting heparin-bound VEGF(164) beads onto lung explants locally stimulates a marked neovascular response within 48 hr in culture.	Heparin	9-16	vascular endothelial growth factor A	Mus musculus	23-27
11054123-9	2000	The distinct Arg/Lys-rich and Met-rich region at positions 10-36 of the PLA2 homolog presumably are involved in its heparin-binding and the cell membrane-interference leading to edema and myotoxicity.	Heparin	116-123	phospholipase A2 group IIA	Homo sapiens	72-76
11009624-0	2000	Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex.	Heparin	17-24	coagulation factor X	Homo sapiens	55-64
10982357-13	2000	The O-sulfate groups of heparin were found to be more important for interaction with gB-1 than gB-2.	Heparin	24-31	gamma-aminobutyric acid type B receptor subunit 1	Homo sapiens	85-89
11682238-1	2002	As a consequence of the outbreak of bovine spongiform encephalopathy (BSE), ruminants materials have been generally banned from the production of heparin.	Heparin	146-153	BSE	Bos taurus	70-73
11689640-8	2001	This revealed that K8.1 binds to heparin with an affinity comparable to that of glycoproteins B and C of herpes simplex virus, which are known to be involved in target cell recognition by binding to cell surface proteoglycans, especially heparan sulfate.	Heparin	33-40	keratin 81	Homo sapiens	19-23
11737582-10	2001	Native and mutant FGF-23s bound heparin.	Heparin	32-39	fibroblast growth factor 23	Homo sapiens	18-24
12606025-0	2003	Heparin-like dextran derivatives as well as glycosaminoglycans inhibit the enzymatic activity of human cathepsin G.	Heparin	0-7	cathepsin G	Homo sapiens	103-114
12581643-0	2003	Structure of beta-antithrombin and the effect of glycosylation on antithrombin"s heparin affinity and activity.	Heparin	81-88	serpin family C member 1	Homo sapiens	18-30
11692092-2	2001	It has been proposed that heparin might play an important role in limiting the inflammatory events associated with asthma and allergic rhinitis by neutralizing inflammatory mediators, such as eosinophil cationic protein and major basic protein, and by limiting eosinophil recruitment.	Heparin	26-33	ribonuclease A family member 3	Homo sapiens	192-219
11692092-4	2001	METHODS: The capacity of heparin to reduce nasal response was studied by evaluating symptom score, eosinophil cationic protein concentration, and eosinophil counts in nasal lavage fluids 10, 60, and 360 minutes after allergen challenge.	Heparin	25-32	ribonuclease A family member 3	Homo sapiens	99-126
11692092-8	2001	The mechanism by which heparin produces its protective activity seems to be related to the neutralization of eosinophil cationic protein as well as to the reduction of eosinophil recruitment.	Heparin	23-30	ribonuclease A family member 3	Homo sapiens	109-136
10965035-9	2000	Nex-1 binds to heparin, heparan sulfate, and chondroitin sulfate but not to chondroitin and chemically N- or O-desulfated heparin.	Heparin	15-22	Annexin	Caenorhabditis elegans	0-5
10821835-8	2000	A heparin-binding defective mutant of Cyr61 was unable to mediate fibroblast adhesion through integrin alpha(6)beta(1) but still mediated endothelial cell adhesion through integrin alpha(V)beta(3), indicating that endothelial cell adhesion through integrin alpha(V)beta(3) is independent of the heparin-binding activity of Cyr61.	Heparin	2-9	integrin subunit alpha V	Homo sapiens	172-196
10821835-8	2000	A heparin-binding defective mutant of Cyr61 was unable to mediate fibroblast adhesion through integrin alpha(6)beta(1) but still mediated endothelial cell adhesion through integrin alpha(V)beta(3), indicating that endothelial cell adhesion through integrin alpha(V)beta(3) is independent of the heparin-binding activity of Cyr61.	Heparin	2-9	integrin subunit alpha V	Homo sapiens	248-272
10926548-7	2000	Heparin induces production of p21, a potent inhibitor of cyclin-dependent kinases, thereby potentially identifying a fundamental mechanism by which heparin inhibits proliferation in smooth muscle-like cells.	Heparin	0-7	KRAS proto-oncogene, GTPase	Rattus norvegicus	30-33
11564606-4	2001	Factor Xa cleaved an additional site within the BTC protein, generating a truncated isoform separable from full-length BTC by heparin-affinity chromatography.	Heparin	126-133	betacellulin	Rattus norvegicus	48-51
12581643-0	2003	Structure of beta-antithrombin and the effect of glycosylation on antithrombin"s heparin affinity and activity.	Heparin	81-88	serpin family C member 1	Homo sapiens	66-78
10926548-7	2000	Heparin induces production of p21, a potent inhibitor of cyclin-dependent kinases, thereby potentially identifying a fundamental mechanism by which heparin inhibits proliferation in smooth muscle-like cells.	Heparin	148-155	KRAS proto-oncogene, GTPase	Rattus norvegicus	30-33
12581643-3	2003	Activation of antithrombin is brought about by a conformational change initiated upon binding heparin or heparan sulphate.	Heparin	94-101	serpin family C member 1	Homo sapiens	14-26
12581643-5	2003	Of the two forms, beta-antithrombin has the higher affinity for heparin and thus functions as the major inhibitor in vivo even though it is the less abundant form.	Heparin	64-71	serpin family C member 1	Homo sapiens	23-35
12581643-7	2003	Here, we describe the most accurate structures of alpha-antithrombin and alpha-antithrombin+heparin pentasaccharide reported to date (2.6A and 2.9A resolution, respectively, both re-refinements using old data), and the structure of beta-antithrombin (2.6A resolution).	Heparin	92-99	serpin family C member 1	Homo sapiens	79-91
11725736-7	2001	Topical bovine thrombin spray was applied to the surgical field in anticipation of early resumption of heparin anticoagulation.	Heparin	103-110	coagulation factor II, thrombin	Bos taurus	15-23
12581643-7	2003	Here, we describe the most accurate structures of alpha-antithrombin and alpha-antithrombin+heparin pentasaccharide reported to date (2.6A and 2.9A resolution, respectively, both re-refinements using old data), and the structure of beta-antithrombin (2.6A resolution).	Heparin	92-99	serpin family C member 1	Homo sapiens	79-91
11668417-0	2001	Effects of sulfation on antithrombin-thrombin/factor Xa interactions in semisynthetic low molecular weight heparins.	Heparin	107-115	coagulation factor X	Homo sapiens	46-55
11951105-6	2000	(3) Contraction of antral muscle cells induced by motilin and gastrin was inhibited by the phospholipase C (PLC) inhibitor U  73122 and the IP(3) receptor antagonist heparin.	Heparin	166-173	motilin	Rattus norvegicus	50-57
11951105-6	2000	(3) Contraction of antral muscle cells induced by motilin and gastrin was inhibited by the phospholipase C (PLC) inhibitor U  73122 and the IP(3) receptor antagonist heparin.	Heparin	166-173	gastrin	Rattus norvegicus	62-69
12581643-10	2003	They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135.	Heparin	62-69	serpin family C member 1	Homo sapiens	79-91
10913257-9	2000	The rate constants for inhibition of thrombin and factor Xa by the complexes between antithrombin and full-length heparin or pentasaccharide were unaffected by both mutations, indicating that neither Lys136 nor Lys139 is involved in heparin activation of the inhibitor.	Heparin	114-121	coagulation factor X	Homo sapiens	50-59
12581643-10	2003	They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135.	Heparin	62-69	serpin family C member 1	Homo sapiens	102-114
10903991-0	2000	Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor.	Heparin	0-7	epidermal growth factor receptor	Rattus norvegicus	89-127
10828022-6	2000	Induction of apoptosis was dependent on the heparin-binding ability of endostatin and the expression of Shb with a functional Src homology 2 (SH2)-domain.	Heparin	44-51	collagen, type XVIII, alpha 1	Mus musculus	71-81
10839770-8	2000	Addition of heparin ( approximately 100 IU/mL) to serial samples from nine acute myocardial infarction patients produced mean cTnT losses of 33% at 1-12 h after onset of chest pain, 17% at 13-48 h, and 7% after 48 h. The changing heparin effects were seen for both cTnT and cTnI during time courses of individual patients with myocardial infarction.	Heparin	12-19	troponin I3, cardiac type	Homo sapiens	274-278
11596736-6	2001	Fat feeding was found to increase heparin-released plasma LPL activity in a dose-dependent fashion.	Heparin	34-41	lipoprotein lipase	Equus caballus	58-61
12581643-10	2003	They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135.	Heparin	168-175	serpin family C member 1	Homo sapiens	79-91
11565896-8	2001	An 80% blockage of the GPIIb/IIIa receptors and suppression of platelet aggregation to less than 20% allows the giving of unfractionated heparin and running CPB in a standard fashion despite HIT and thrombosis.	Heparin	137-144	integrin subunit alpha 2b	Homo sapiens	23-28
12581643-10	2003	They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135.	Heparin	168-175	serpin family C member 1	Homo sapiens	102-114
12576961-14	2003	Heparin administration further increased, in a dose-dependent manner, myeloperoxidase activity and P-selectin expression in the lung in animals with pancreatitis.	Heparin	0-7	myeloperoxidase	Rattus norvegicus	70-85
11373281-0	2001	A unique sequence of the laminin alpha 3 G domain binds to heparin and promotes cell adhesion through syndecan-2 and -4.	Heparin	59-66	syndecan 2	Homo sapiens	102-119
10799289-3	2000	Here we show that a polypeptide encompassing the C-terminal cluster of basic amino acids of netrin-1 (i) adopts an alpha-helical conformation in water-trifluoroethanol mixtures according to circular dichroism experiments and (ii) binds electrostatically to heparin with high affinity under physiological ionic conditions (K(D) = 15 nM for the binding to immobilized heparin according to surface plasmon resonance, K(D) = 50 nM in solution as determined with isothermal titration calorimetry).	Heparin	257-264	netrin 1	Homo sapiens	92-100
10799289-3	2000	Here we show that a polypeptide encompassing the C-terminal cluster of basic amino acids of netrin-1 (i) adopts an alpha-helical conformation in water-trifluoroethanol mixtures according to circular dichroism experiments and (ii) binds electrostatically to heparin with high affinity under physiological ionic conditions (K(D) = 15 nM for the binding to immobilized heparin according to surface plasmon resonance, K(D) = 50 nM in solution as determined with isothermal titration calorimetry).	Heparin	366-373	netrin 1	Homo sapiens	92-100
11749192-11	2001	From the investigated glucan sulfates, mainly C2- and C4-sulfated, linear beta-1,3-glucan sulfates with DS &gt; 1.0 and MW between 18 and 50 kDa proved to be most suitable for a potential use as heparin alternatives.	Heparin	195-202	UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2	Homo sapiens	74-82
12574556-3	2003	Our second goal was to determine whether tissue binding of ECSOD via the heparin-binding domain (HBD) is important for the effect of the enzyme.	Heparin	73-80	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	59-64
11278943-10	2001	In the absence of prothrombin, FVa decreased the second order rate constant for inhibition by the AT-heparin complex from 1.58 x 10(7) m(-1) s(-1), for FXa, Ca(2+), and PCPS, to 7.72 x 10(6) m(-1) s(-1).	Heparin	101-108	coagulation factor X	Homo sapiens	152-155
10883408-5	2000	This fat effect was accompanied by a 247% increase in lipoprotein lipase (LPL) activity in post-heparin plasma.	Heparin	96-103	lipoprotein lipase	Equus caballus	54-72
10883408-5	2000	This fat effect was accompanied by a 247% increase in lipoprotein lipase (LPL) activity in post-heparin plasma.	Heparin	96-103	lipoprotein lipase	Equus caballus	74-77
12507905-6	2003	Mol Biol Cell 1997, 8:287a and Delmolino LM, Stearns NA, Castellot Jr JJ: COP-1, a member of the CCN family, is a heparin-induced growth arrest specific gene in vascular smooth muscle cells.	Heparin	114-121	COP1, E3 ubiquitin ligase	Rattus norvegicus	74-79
10938477-2	2000	The (99m)Tc-FGF-1 retained its representative molecular mass, heparin affinity, cellular binding to both low (Kd = 9.5 nM) and high (Kd = 125 pM) affinity sites, and mitogenic activity.	Heparin	62-69	fibroblast growth factor 1	Rattus norvegicus	12-17
10938477-4	2000	Heparin significantly decreased (99m)Tc-FGF-1 liver uptake and increased urinary excretion.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	40-45
11465671-6	2001	The suppression of T cell proliferation and the enhancement of IL-10 secretion with soluble TSP-1 was inhibited byadding RGDS peptide or heparin.	Heparin	137-144	interleukin 10	Homo sapiens	63-68
12524238-4	2003	METHODS AND RESULTS: The vascular PN-1 formed specific covalent complexes with thrombin involving the catalytic site of the protease, and heparin increased the formation of these complexes.	Heparin	138-145	serpin family E member 2	Rattus norvegicus	34-38
11259264-1	2001	Using a variety of approaches, we have examined the expression of the heparin/heparan sulfate (Hp/HS) interacting protein/ribosomal protein L29 (HIP/RPL29) in mouse uteri during the estrous cycle and early pregnancy.	Heparin	70-77	ribosomal protein L29	Mus musculus	149-154
11259264-2	2001	HIP/RPL29 selectively binds heparin and HS and may promote HS-dependent embryo adhesion.	Heparin	28-35	ribosomal protein L29	Mus musculus	4-9
10848798-1	2000	[14C]-Serotonin release assay (14C-SRA) from platelets is considered to be the most sensitive test for laboratory confirmation of heparin-induced thrombocytopenia (HIT).	Heparin	130-137	steroid receptor RNA activator 1	Homo sapiens	35-38
10977903-1	2000	In vivo experiments on the model of wound healing showed that thrombin and thrombin receptor agonist TRAP-6 stimulated heparin secretion by mast cells in rat subcutaneous fat: the saturation of mast cells with heparin decreased, while degranulation and granulolysis increased.	Heparin	119-126	coagulation factor II (thrombin) receptor	Rattus norvegicus	75-92
10977903-1	2000	In vivo experiments on the model of wound healing showed that thrombin and thrombin receptor agonist TRAP-6 stimulated heparin secretion by mast cells in rat subcutaneous fat: the saturation of mast cells with heparin decreased, while degranulation and granulolysis increased.	Heparin	210-217	coagulation factor II (thrombin) receptor	Rattus norvegicus	75-92
11287471-9	2001	Neurotensin-evoked cationic currents were blocked by heparin, an IP(3) receptor antagonist, and 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid (BAPTA), a fast chelator of Ca(2+).	Heparin	53-60	neurotensin	Rattus norvegicus	0-11
12493698-15	2003	In atretic follicles, the increase and decrease in IGFBP-2 and PAPP-A mRNA expression, respectively, as well as the inhibition of PAPP-A activity by heparin-binding domains present in IGFBP-5 or other proteins, might participate in higher IGFBP-2 levels and a decrease in IGF bioavailability.	Heparin	149-156	pappalysin 1	Bos taurus	130-136
11599124-4	2001	Heparin inhibited ET-1-induced c-fos mRNA expression.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	31-36
11599124-5	2001	Heparin and HS inhibited ET-1-induced activation of c-fos promoter/enhancer in MCs.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	52-57
11599124-6	2001	Although heparin and HS inhibited ET-1-induced activation of the wild-type c-fos serum response element (SRE), the activation of a mutated c-fos SRE that contains an intact binding site for the serum response factor (SRF) but lacks the ternary complex factor (TCF) binding site, was not inhibited.	Heparin	9-16	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	75-80
11134031-0	2001	Hypersulfated low molecular weight heparin with reduced affinity for antithrombin acts as an anticoagulant by inhibiting intrinsic tenase and prothrombinase.	Heparin	35-42	coagulation factor X	Homo sapiens	142-156
11286313-3	2001	There are theoretical grounds to expect LMWHs to be more effective than unfractionated heparin (UFH) in combination with GP IIb/IIIa inhibitors, since UFH, but not LMWH, activates platelets.	Heparin	151-154	integrin subunit alpha 2b	Homo sapiens	121-127
10728020-0	2000	Enoxaparin, a low molecular weight heparin, inhibits platelet-dependent prothrombinase assembly and activity by factor-Xa neutralization.	Heparin	35-42	coagulation factor X	Homo sapiens	72-86
10728020-0	2000	Enoxaparin, a low molecular weight heparin, inhibits platelet-dependent prothrombinase assembly and activity by factor-Xa neutralization.	Heparin	35-42	coagulation factor X	Homo sapiens	112-121
10698712-8	2000	Treatments with high ionic strength and heparinase released latexin from the granules, suggesting that latexin is non-covalently associated with a heparin-like component of the granules.	Heparin	40-47	latexin	Rattus norvegicus	60-67
10698712-8	2000	Treatments with high ionic strength and heparinase released latexin from the granules, suggesting that latexin is non-covalently associated with a heparin-like component of the granules.	Heparin	40-47	latexin	Rattus norvegicus	103-110
10704345-4	2000	This interaction was inhibited if E7 phosphorylation by the rabbit reticulocyte lysate was prevented with heparin, a CKII inhibitor, or if the amino acids Ser-31 and Ser-32 in E7, which are phosphorylated by CKII, were replaced with amino acids that cannot be phosphorylated.	Heparin	106-113	casein kinase II subunit beta	Oryctolagus cuniculus	117-121
10704345-4	2000	This interaction was inhibited if E7 phosphorylation by the rabbit reticulocyte lysate was prevented with heparin, a CKII inhibitor, or if the amino acids Ser-31 and Ser-32 in E7, which are phosphorylated by CKII, were replaced with amino acids that cannot be phosphorylated.	Heparin	106-113	casein kinase II subunit beta	Oryctolagus cuniculus	208-212
15041274-12	2003	CONCLUSIONS: Rapidpoint ENOX times correlate strongly to anti-Xa activities measured by the Stachrom Heparin Assays for citrated whole-blood samples.	Heparin	101-108	JPX transcript, XIST activator	Homo sapiens	24-28
10660568-2	2000	It has been proposed that residues P15 and P14 are expelled from beta-sheet A of antithrombin by heparin binding, permitting better interaction of the reactive center loop with factor Xa.	Heparin	97-104	ribonuclease P/MRP subunit p14	Homo sapiens	43-46
10660568-2	2000	It has been proposed that residues P15 and P14 are expelled from beta-sheet A of antithrombin by heparin binding, permitting better interaction of the reactive center loop with factor Xa.	Heparin	97-104	coagulation factor X	Homo sapiens	177-186
10660581-8	2000	Zymographic measurement of MMP-7 activity is greatly enhanced by heparin.	Heparin	65-72	matrix metallopeptidase 7	Rattus norvegicus	27-32
11222776-7	2001	Using western blot analysis of GH3 nuclear proteins that bind to heparin-Sepharose, we have shown that Ets-1 and GABP, which are MAP kinase substrates, co-purify with complex A, and supershift analysis with specific antisera revealed that complex A contains Ets-1, GABPalpha and GABPbeta1.	Heparin	65-72	ETS proto-oncogene 1, transcription factor	Rattus norvegicus	103-108
12471127-8	2002	Binding of the wild-type SCR15-20, but not the residual binding of the mutated SCR15-20, to C3d was inhibited by heparin.	Heparin	113-120	endogenous retrovirus group K member 13	Homo sapiens	92-95
11180402-0	2001	A synthetic heparin-mimicking polyanionic compound binds to the LDL receptor-related protein and inhibits vascular smooth muscle cell proliferation.	Heparin	12-19	low density lipoprotein receptor-related protein 1	Mus musculus	64-92
10642607-1	2000	The D-glucuronyl C5-epimerase involved in the biosynthesis of heparin and heparan sulfate was investigated with focus on its substrate specificity, its kinetic properties, and a comparison of epimerase preparations from the Furth mastocytoma and bovine liver, which synthesize heparin and heparan sulfate, respectively.	Heparin	62-69	glucuronic acid epimerase	Bos taurus	4-29
12676188-4	2002	Significant platelet activation due to unfractionated heparin could be observed by labeling with anti-GMP 140 (UFH: p=0.009; LMWH: p=0.16).	Heparin	54-61	selectin P	Homo sapiens	102-109
10642607-1	2000	The D-glucuronyl C5-epimerase involved in the biosynthesis of heparin and heparan sulfate was investigated with focus on its substrate specificity, its kinetic properties, and a comparison of epimerase preparations from the Furth mastocytoma and bovine liver, which synthesize heparin and heparan sulfate, respectively.	Heparin	277-284	glucuronic acid epimerase	Bos taurus	4-29
10991942-2	2000	The inhibitory activity of kallistatin is abolished upon heparin binding.	Heparin	57-64	serpin family A member 4	Homo sapiens	27-38
10991942-3	2000	The loop between the H helix and C2 sheet of kallistatin containing clusters of basic amino acid residues has been identified as a heparin-binding site.	Heparin	131-138	serpin family A member 4	Homo sapiens	45-56
10731377-6	2000	Several clinical trials in the past few years have documented the beneficial value of GP IIb/IIIa inhibitors in patients treated with aspirin and heparin, with a significant reduction in the cumulative end-point of death and/or myocardial infarction at 48-96 hours (odds ratio--OR 0.81, 95% confidence interval--CI 0.71-0.92, p &lt; 0.01).	Heparin	146-153	integrin subunit alpha 2b	Homo sapiens	86-92
12676188-4	2002	Significant platelet activation due to unfractionated heparin could be observed by labeling with anti-GMP 140 (UFH: p=0.009; LMWH: p=0.16).	Heparin	111-114	selectin P	Homo sapiens	102-109
10656996-2	2000	After analysis of binding activity using three different methods - ligand blotting, solution phase equilibrium binding and biosensor measurement of real-time on- and off-rates - we report that the mutation of two highly conserved residues within this region (glycine 203 and glutamine 209) reduces the affinity of the binding protein for both IGF-I and IGF-II, while having no effect on heparin binding.	Heparin	387-394	insulin-like growth factor 2	Rattus norvegicus	353-359
11118364-6	2000	Mixing RANTES with each of the glycosaminoglycans did not restore inhibition of MDM-MCSF infection by HIV-1; however, heparin at concentrations that had low antiviral activity for MDM-5d counteracted RANTES anti-HIV-1 activity for these cells, whereas chondroitin sulfate B had no additive effect on that of RANTES.	Heparin	118-125	C-C motif chemokine ligand 5	Homo sapiens	200-206
11118364-6	2000	Mixing RANTES with each of the glycosaminoglycans did not restore inhibition of MDM-MCSF infection by HIV-1; however, heparin at concentrations that had low antiviral activity for MDM-5d counteracted RANTES anti-HIV-1 activity for these cells, whereas chondroitin sulfate B had no additive effect on that of RANTES.	Heparin	118-125	C-C motif chemokine ligand 5	Homo sapiens	200-206
10993887-7	2000	Heparin distinguishes the inhibitory specificity of kallistatin toward kallikrein versus chymotrypsin.	Heparin	0-7	serpin family A member 4	Homo sapiens	52-63
11369259-2	2000	Binding of a full-length heparin chain to this site of factor Xa in the presence of calcium makes a significant contribution to acceleration of the proteinase inhibition by antithrombin through a ternary complex bridging or template mechanism.	Heparin	25-32	coagulation factor X	Homo sapiens	55-64
10728372-8	2000	ASMC and PAC-1 cells but not A10 showed a decrease in c-fos mRNA in response to 1 microgram/ml heparin, and a decrease in the c-Fos content of AP-1 DNA binding activity.	Heparin	95-102	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	54-59
10728372-12	2000	In contrast to A10 and their controls not exposed to continuous heparin, heparin-selected PAC-1 and ASMC showed a diminished ability to induce c-fos in response to serum.	Heparin	73-80	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	143-148
10728372-13	2000	CONCLUSIONS: Smooth muscle cell lines show different responses to the antimitogenic effects of heparin that correlate with the heparin sensitivity of c-Fos/c-Jun expression.	Heparin	95-102	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	150-155
10728372-13	2000	CONCLUSIONS: Smooth muscle cell lines show different responses to the antimitogenic effects of heparin that correlate with the heparin sensitivity of c-Fos/c-Jun expression.	Heparin	127-134	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	150-155
10617625-2	2000	Mouse mast cell protease (mMCP) 6 and mMCP-7 are homologous tryptases stored in granules as macromolecular complexes with heparin and/or chondroitin sulfate E containing serglycin proteoglycans.	Heparin	122-129	tryptase beta 2	Mus musculus	26-33
10617625-2	2000	Mouse mast cell protease (mMCP) 6 and mMCP-7 are homologous tryptases stored in granules as macromolecular complexes with heparin and/or chondroitin sulfate E containing serglycin proteoglycans.	Heparin	122-129	tryptase beta 2	Mus musculus	60-69
10900194-6	2000	The N-terminal domain of human TIMP-3 was expressed and found to bind to heparin with affinity similar to that of full-length mouse TIMP-3.	Heparin	73-80	TIMP metallopeptidase inhibitor 3	Homo sapiens	31-37
10900194-7	2000	The A and B beta-strands of the N-terminal domain of TIMP-3 contain two potential heparin-binding sequences rich in lysine and arginine; these strands should form a double track on the outer surface of TIMP-3.	Heparin	82-89	TIMP metallopeptidase inhibitor 3	Homo sapiens	53-59
10900194-7	2000	The A and B beta-strands of the N-terminal domain of TIMP-3 contain two potential heparin-binding sequences rich in lysine and arginine; these strands should form a double track on the outer surface of TIMP-3.	Heparin	82-89	TIMP metallopeptidase inhibitor 3	Homo sapiens	202-208
12421140-10	2002	The diagnosis of antithrombin deficiency should be established only after other acquired causes of antithrombin deficiency, such as liver disease, consumptive coagulopathy, or heparin therapy, are excluded.	Heparin	176-183	serpin family C member 1	Homo sapiens	17-29
11018553-5	2000	This cross-linked heparin-binding peptide served to immobilize heparin within the matrix, and this immobilized heparin interacted with the neurotrophin and slowed the passive release of the growth factor from the matrix.	Heparin	18-25	brain derived neurotrophic factor	Homo sapiens	139-151
10608507-5	2000	Binding sites in the SAA protein for high density lipoproteins, calcium, laminin, and heparin/heparan-sulfate were described.	Heparin	86-93	serum amyloid A1 cluster	Homo sapiens	21-24
10965119-1	2000	Human EXTL2 is an alpha1,4-N-acetylhexosaminyltransferase involved in the biosynthesis of heparin/heparan sulfate.	Heparin	90-97	exostosin-like glycosyltransferase 2	Mus musculus	6-11
10593896-1	1999	The keratinocyte growth factor (KGF or FGF-7) is unique among its family members both in its target cell specificity and its inhibition by the addition of heparin and the native heparan-sulfate proteoglycan (HSPG), glypican-1 in cells expressing endogenous HSPGs.	Heparin	155-162	CD44 molecule (Indian blood group)	Homo sapiens	208-212
12450065-9	2002	We conclude that tryptase-induced relaxation of rat aorta, most likely via PAR2, is tightly regulated by heparin and cell-surface sialic acid.	Heparin	105-112	F2R like trypsin receptor 1	Rattus norvegicus	75-79
10593896-1	1999	The keratinocyte growth factor (KGF or FGF-7) is unique among its family members both in its target cell specificity and its inhibition by the addition of heparin and the native heparan-sulfate proteoglycan (HSPG), glypican-1 in cells expressing endogenous HSPGs.	Heparin	155-162	glypican 1	Homo sapiens	215-225
10593896-9	1999	Glypican-1 abrogated the stimulatory effect of heparin, and heparin reversed the inhibitory effect of glypican-1, indicating that this HSPG inhibits FGF-7 activities by acting, most likely, as a competitive inhibitor of stimulatory HSPG species for FGF-7.	Heparin	47-54	glypican 1	Homo sapiens	0-10
10593896-9	1999	Glypican-1 abrogated the stimulatory effect of heparin, and heparin reversed the inhibitory effect of glypican-1, indicating that this HSPG inhibits FGF-7 activities by acting, most likely, as a competitive inhibitor of stimulatory HSPG species for FGF-7.	Heparin	47-54	CD44 molecule (Indian blood group)	Homo sapiens	135-139
11155688-3	2000	HSPG is involved in reservation of heparin binding growth factors (HBGF), protection from proteolysis of HBGF, and ligand-receptor interaction in the case of fibroblast growth factors.	Heparin	35-42	syndecan 2	Homo sapiens	0-4
12241544-3	2002	Heparin releases several endothelial proteins, including lipoprotein lipase, hepatic lipase, platelet factor-4 and superoxide dismutase.	Heparin	0-7	lipoprotein lipase	Homo sapiens	57-75
11091973-5	2000	Addition of heparin to cultures decreased the most effective aFGF concentration by 100-fold, from 100 ng ml-1 to 1 ng ml-1.	Heparin	12-19	fibroblast growth factor 1	Rattus norvegicus	61-65
10622723-0	1999	Functional properties of complement factor H-related proteins FHR-3 and FHR-4: binding to the C3d region of C3b and differential regulation by heparin.	Heparin	143-150	complement factor H	Homo sapiens	36-44
10622723-0	1999	Functional properties of complement factor H-related proteins FHR-3 and FHR-4: binding to the C3d region of C3b and differential regulation by heparin.	Heparin	143-150	complement factor H related 3	Homo sapiens	62-67
10622723-0	1999	Functional properties of complement factor H-related proteins FHR-3 and FHR-4: binding to the C3d region of C3b and differential regulation by heparin.	Heparin	143-150	complement factor H related 4	Homo sapiens	72-77
10622723-6	1999	The interaction of FHR-3, but not of FHR4, with opsonised pneumococci was inhibited by heparin.	Heparin	87-94	complement factor H related 3	Homo sapiens	19-24
12110666-2	2002	Previous studies have postulated the presence of a heparin-binding site on the bile salt-dependent lipase (BSDL), whereas two bile salt-binding sites regulate the enzyme activity.	Heparin	51-58	carboxyl ester lipase	Homo sapiens	107-111
10632362-8	1999	Furthermore, cells expressing low levels of beta3 and resistant to conventional adenoviral vectors were susceptible to a vector containing the heparin-binding domain in its fiber, thus suggesting that redirecting vectors to receptors other than CAR may bypass the integrin pathway.	Heparin	143-150	CXADR Ig-like cell adhesion molecule	Homo sapiens	245-248
11027529-3	2000	Adsorption of sPLA(2)-IIA to BMMC was prevented by addition of heparin to the medium.	Heparin	63-70	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	14-25
10974347-5	2000	In this study, we compared the abilities of Intimatan with its parent compound, dermatan sulfate, and with heparin to affect coagulation and to inhibit surface-bound thrombin both in vitro and in vivo, to determine if Intimatan demonstrates a better potential than either other compound in preventing thrombus formation in vivo.	Heparin	107-114	prothrombin	Oryctolagus cuniculus	166-174
10842181-5	2000	The interaction was dependent on the heparin-binding domain of VEGF165 and increased the affinity of VEGF165 for its signaling receptor VEGFR2 or kinase insert domain-containing receptor.	Heparin	37-44	kinase insert domain receptor	Homo sapiens	136-142
10521414-2	1999	Here we have identified a heparin-binding region in the carboxyl-terminal portion of rat Tg and have studied its involvement in megalin binding.	Heparin	26-33	LDL receptor related protein 2	Rattus norvegicus	128-135
10521538-3	1999	Heparin bound to type V collagen, type IX collagen, fibronectin, laminin, and vitronectin; and chondroitin sulfate E bound to type II, type V, and type VII collagen.	Heparin	0-7	vitronectin	Homo sapiens	78-89
12220677-5	2002	The effect of IGFBP-3 on calcium concentrations was dose-dependent and also occurred when IGFBP-3 was complexed with either IGF-I or heparin, suggesting that the receptor binding site is probably located in the least conserved central domain of IGFBP-3.	Heparin	133-140	insulin like growth factor binding protein 3	Homo sapiens	14-21
10471474-4	1999	FAA was isolated by heparin-affinity chromatography and reversed-phase high performance liquid chromatography near homogeneity.	Heparin	20-27	fumarylacetoacetate hydrolase	Bos taurus	0-3
11125607-2	2000	Like standard heparin, these anticoagulants inhibit activation of a number of coagulation enzymes, but low molecular weight heparins have their primary inhibitory effect on factor Xa.	Heparin	124-132	coagulation factor X	Homo sapiens	173-182
10903991-4	2000	In rat SMCs, EGFR phosphorylation and extracellular signal-regulated kinase (ERK) activation in response to thrombin are inhibited not only by the EGFR inhibitor AG1478 and by EGFR blocking antibody but also by heparin and by neutralizing HB-EGF antibody.	Heparin	211-218	epidermal growth factor receptor	Rattus norvegicus	13-17
10903991-4	2000	In rat SMCs, EGFR phosphorylation and extracellular signal-regulated kinase (ERK) activation in response to thrombin are inhibited not only by the EGFR inhibitor AG1478 and by EGFR blocking antibody but also by heparin and by neutralizing HB-EGF antibody.	Heparin	211-218	epidermal growth factor receptor	Rattus norvegicus	147-151
12220677-5	2002	The effect of IGFBP-3 on calcium concentrations was dose-dependent and also occurred when IGFBP-3 was complexed with either IGF-I or heparin, suggesting that the receptor binding site is probably located in the least conserved central domain of IGFBP-3.	Heparin	133-140	insulin like growth factor binding protein 3	Homo sapiens	90-97
10903991-4	2000	In rat SMCs, EGFR phosphorylation and extracellular signal-regulated kinase (ERK) activation in response to thrombin are inhibited not only by the EGFR inhibitor AG1478 and by EGFR blocking antibody but also by heparin and by neutralizing HB-EGF antibody.	Heparin	211-218	epidermal growth factor receptor	Rattus norvegicus	147-151
10903991-7	2000	We conclude from these data that the inhibitory effect of heparin on SMC migration induced by thrombin relies, at least in part, on a blockade of HB-EGF-mediated EGFR transactivation.	Heparin	58-65	epidermal growth factor receptor	Rattus norvegicus	162-166
10464275-6	1999	A characterization of SBP2 biochemical properties reveals that SBP2 binding is sensitive to oxidation and the presence of heparin, rRNA, and poly(G).	Heparin	122-129	SECIS binding protein 2	Homo sapiens	22-26
10464275-6	1999	A characterization of SBP2 biochemical properties reveals that SBP2 binding is sensitive to oxidation and the presence of heparin, rRNA, and poly(G).	Heparin	122-129	SECIS binding protein 2	Homo sapiens	63-67
12220677-5	2002	The effect of IGFBP-3 on calcium concentrations was dose-dependent and also occurred when IGFBP-3 was complexed with either IGF-I or heparin, suggesting that the receptor binding site is probably located in the least conserved central domain of IGFBP-3.	Heparin	133-140	insulin like growth factor binding protein 3	Homo sapiens	90-97
10468150-4	1999	In patients undergoing percutaneous coronary interventions with adjunctive GPIIb/IIIa inhibition, the risk of bleeding, particularly from the femoral vascular access site, may be reduced through the use of low-dose, weight-adjusted heparin (70 U/kg), avoidance of postprocedural heparin, and early vascular sheath removal.	Heparin	232-239	integrin subunit alpha 2b	Homo sapiens	75-80
10465290-9	1999	So, in ovine preovulatory follicles, IGFBP-4 proteolytic degradation both 1) depends on IGFs, and 2) is inhibited by IGFBP-3 via its C-terminal heparin-binding domain as well as by heparin-binding domain containing peptides.	Heparin	144-151	insulin like growth factor binding protein 4	Homo sapiens	37-44
12213490-5	2002	In the adipose tissue of the untreated group, 72% of the LPL was the inactive-monomeric form, which was eluted with 0.4-0.75 M NaCl from the heparin-Sepharose column, and 28% was the active-dimeric form, which was eluted with 0.8-1.2 M NaCl.	Heparin	141-148	lipoprotein lipase	Homo sapiens	57-60
10456887-3	1999	The mechanism involves specific bacterial recruitment of heparin, glycosaminoglycans, or related sulfated polysaccharides, which in turn serve as universal binding sites for a diverse array of mammalian heparin binding proteins, including adhesive glycoproteins (vitronectin and fibronectin), inflammatory (MCP-3, PF-4, and MIP-1alpha) and immunomodulatory (gamma interferon) intermediates, and fibroblast growth factor.	Heparin	57-64	vitronectin	Homo sapiens	263-274
10456887-3	1999	The mechanism involves specific bacterial recruitment of heparin, glycosaminoglycans, or related sulfated polysaccharides, which in turn serve as universal binding sites for a diverse array of mammalian heparin binding proteins, including adhesive glycoproteins (vitronectin and fibronectin), inflammatory (MCP-3, PF-4, and MIP-1alpha) and immunomodulatory (gamma interferon) intermediates, and fibroblast growth factor.	Heparin	57-64	C-C motif chemokine ligand 7	Homo sapiens	307-312
10913474-12	2000	These data indicate a significant in vivo effect of abciximab plus heparin in increasing ACT and decreasing F1.2, results that are consistent with an effect on reducing thrombin generation.	Heparin	67-74	coagulation factor XII	Homo sapiens	108-112
10884521-10	2000	L-N(G)-nitroarginine methyl ester (L-NAME), an inhibitor of NOS activity blocked the cNOS activity activated by heparin and reversed the beneficial effects of heparin on ulcer healing.	Heparin	112-119	nitric oxide synthase 3	Rattus norvegicus	85-89
12231563-4	2002	Here, we present evidence for the first time that the antiproliferative action of heparin is in part mediated by its ability to activate double-stranded RNA-activated protein kinase (PKR), an interferon-induced protein kinase.	Heparin	82-89	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	183-186
11060763-3	2000	Fractionated, or low-molecular weight, heparins (LMWHs) are more selective for coagulation Factor Xa (FXa) over thrombin (FIIa).	Heparin	39-47	coagulation factor X	Homo sapiens	102-105
10460245-5	1999	Agrin is active in cortical neurons at picomolar concentrations, is Ca(2+) dependent, and is inhibited by heparin and staurosporine.	Heparin	106-113	agrin	Homo sapiens	0-5
12231563-5	2002	METHODS AND RESULTS: We have analyzed the VSMC proliferation by cell-cycle analysis and correlated it to the kinase activity of PKR in the presence of heparin.	Heparin	151-158	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	128-131
10505285-10	1999	In contrast, in the recently published OASIS-2 study, outcome in patients with unstable angina pectoris was significantly better with hirudin than with heparin.	Heparin	152-159	cAMP responsive element binding protein 3 like 1	Homo sapiens	39-44
10419453-5	1999	The antithrombin-bound fraction of heparin was required to support the heparin-dependent stimulation of DNA synthesis of endothelial cells by FGF-1.	Heparin	35-42	fibroblast growth factor 1	Rattus norvegicus	142-147
10419453-5	1999	The antithrombin-bound fraction of heparin was required to support the heparin-dependent stimulation of DNA synthesis of endothelial cells by FGF-1.	Heparin	71-78	fibroblast growth factor 1	Rattus norvegicus	142-147
10958307-10	2000	An antibody against a Tg heparin-binding site functionally related to a major megalin-binding site virtually abolished Tg binding to HS and to FRTL-5 cells, supporting the hypothesis that combined interactions of Tg with HSPGs and with megalin are involved in Tg binding to rat thyroid cells.	Heparin	25-32	LDL receptor related protein 2	Rattus norvegicus	78-85
10958307-10	2000	An antibody against a Tg heparin-binding site functionally related to a major megalin-binding site virtually abolished Tg binding to HS and to FRTL-5 cells, supporting the hypothesis that combined interactions of Tg with HSPGs and with megalin are involved in Tg binding to rat thyroid cells.	Heparin	25-32	LDL receptor related protein 2	Rattus norvegicus	236-243
10748121-4	2000	Both np-2 forms bind VEGF(165) with high affinity in the presence of heparin (K(D) 1.3 x 10(-10) m) but not VEGF(121).	Heparin	69-76	neuropilin 2	Homo sapiens	5-9
10748121-5	2000	np-2 also binds the heparin-binding form of placenta growth factor.	Heparin	20-27	neuropilin 2	Homo sapiens	0-4
10793178-7	2000	GP IIb/IIIa inhibitors have been shown to improve angiographic Thrombolysis in Myocardial Infarction (TIMI) 3 flow rates when used as reperfusion therapy given with heparin and aspirin as compared with heparin and aspirin alone.	Heparin	165-172	integrin subunit alpha 2b	Homo sapiens	0-6
12231563-6	2002	Heparin treatment of VSMCs results in activation of PKR by direct binding and results in a block in G1- to S-phase transition.	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	52-55
10404851-10	1999	Patients positive for cTn-I had more unstable angina (p = 0.042) and heparin before PTCA (p = 0.046), and had longest total time (p = 0.004) and single inflation (p = 0.01).	Heparin	69-76	troponin I3, cardiac type	Homo sapiens	22-27
12231563-7	2002	PKR-null cells are largely insensitive to the antiproliferative actions of heparin, and inhibition of PKR in VSMCs results in a partial abrogation of the antiproliferative effects of heparin.	Heparin	183-190	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	102-105
10766793-0	2000	Examination of the function of RANTES, MIP-1alpha, and MIP-1beta following interaction with heparin-like glycosaminoglycans.	Heparin	92-99	C-C motif chemokine ligand 5	Homo sapiens	31-37
12231563-8	2002	CONCLUSIONS: These results invoke the involvement of novel PKR-dependent regulatory pathways in mediating the antiproliferative actions of heparin.	Heparin	139-146	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	59-62
12236772-4	2002	In this study a series of silyl-heparins were synthesized and each of the analogues found to function similar to unmodified heparin relative to their binding of antithrombin III and also the binding of bFGF.	Heparin	32-39	serpin family C member 1	Homo sapiens	161-177
10832659-8	2000	RESULTS: IL 6 and IL 10 release was significantly less (p&lt;0.05) in the heparin-coated group.	Heparin	74-81	interleukin 10	Homo sapiens	18-23
10832659-10	2000	CONCLUSIONS: These results suggest that with the use of heparin-coated circuits there is a lower production of IL 6 and IL 10 from isolated PBMC than with uncoated circuits.	Heparin	56-63	interleukin 10	Homo sapiens	120-125
10659302-2	1999	This hypothesis was tested indirectly by measuring the concentration of plasma TAG and the activity of lipoprotein lipase (LPL) in post heparin plasma.	Heparin	136-143	lipoprotein lipase	Equus caballus	103-121
10659302-2	1999	This hypothesis was tested indirectly by measuring the concentration of plasma TAG and the activity of lipoprotein lipase (LPL) in post heparin plasma.	Heparin	136-143	lipoprotein lipase	Equus caballus	123-126
12009311-2	2002	Antithrombin III (ATIII) was purified from ostrich plasma by heparin-Sepharose and Super Q-650S chromatography.	Heparin	61-68	serpin family C member 1	Homo sapiens	18-23
10659302-9	1999	The changes in plasma lipids were accompanied by a 79% increase in LPL activity in post heparin plasma.	Heparin	88-95	lipoprotein lipase	Equus caballus	67-70
10393214-9	1999	Heparin abolished the effect of HL-145G on SR-BI-mediated HDL-CE selective uptake.Thus, the enhanced uptake of HDL-CE by HL is mediated by both its ligand role, which requires interaction with proteoglycans, and by lipolysis with subsequent HDL particle remodeling.	Heparin	0-7	scavenger receptor class B member 1	Homo sapiens	43-48
10722716-1	2000	Antithrombin requires heparin for efficient inhibition of the final two proteinases of the blood coagulation cascade, factor Xa and thrombin.	Heparin	22-29	coagulation factor X	Homo sapiens	118-127
10660541-15	2000	Altogether, these findings show that thrombin HBS binds to the region of GpIbalpha involving the Asp(272)-Glu(282) segment, protecting the enzyme from the inactivation by the heparin-AT system.	Heparin	175-182	glycoprotein Ib platelet subunit alpha	Homo sapiens	73-82
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	91-98	coagulation factor X	Homo sapiens	127-136
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	91-98	coagulation factor X	Homo sapiens	138-141
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	91-98	coagulation factor X	Homo sapiens	198-201
12124780-3	2002	Ectodomain shedding of heparin-binding epidermal growth factor-like growth factor (HB-EGF) from the cell surface plays an important role in invasion by HT1080 cells.	Heparin	23-30	heparin binding EGF like growth factor	Homo sapiens	83-89
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	218-225	coagulation factor X	Homo sapiens	127-136
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	218-225	coagulation factor X	Homo sapiens	138-141
10652320-1	2000	We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site.	Heparin	218-225	coagulation factor X	Homo sapiens	198-201
10652320-2	2000	Structural data indicate that 7 of the 11 basic residues of the heparin-binding exosite of thrombin are conserved at similar three-dimensional locations in FXa.	Heparin	64-71	coagulation factor X	Homo sapiens	156-159
10883463-0	2000	Heparin reduces serum levels of endothelin-1 and hepatic ischemia reperfusion injury in rabbits.	Heparin	0-7	endothelin-1	Oryctolagus cuniculus	32-44
10883463-2	2000	Heparin was injected into rabbits after inducing partial hepatic ischemia for 1 h. Thereafter, the serum levels of endothelin-1 (ET-1) and liver transaminase, and tissue levels of oxidized and deoxidized hemoglobin (oxHb, deoxHb) in the reperfused liver were analyzed.	Heparin	0-7	endothelin-1	Oryctolagus cuniculus	115-127
10883463-4	2000	The increased serum levels of ET-1 and liver transaminase after reperfusion were significantly reduced by heparin (P &gt; 0.01).	Heparin	106-113	endothelin-1	Oryctolagus cuniculus	30-34
10883463-8	2000	Microscopically, heparin appeared to normalize I/R-induced activation of hepatic stellate cells which are the target cells for ET-1.	Heparin	17-24	endothelin-1	Oryctolagus cuniculus	127-131
10883463-9	2000	These results suggest that heparin improves the hepatic I/R injury caused by sinusoidal microscirculatory disturbances partly via an inhibition of the ET-1 increase.	Heparin	27-34	endothelin-1	Oryctolagus cuniculus	151-155
10359728-6	1999	In fact, the increase in mean arterial blood pressure after inhibition of ecNOS with NG-nitro-L-arginine methyl ester (30 mg/kg) was smaller in heparin-treated animals than in controls (+26.	Heparin	144-151	nitric oxide synthase 3	Rattus norvegicus	74-79
10359728-8	1999	CONCLUSIONS: High-dose heparin can significantly affect vascular reactivity in vivo by downregulation of ecNOS protein expression.	Heparin	23-30	nitric oxide synthase 3	Rattus norvegicus	105-110
10216309-0	1999	Purification, crystallization and preliminary crystallographic studies of a two fibronectin type-III domain segment from chicken tenascin encompassing the heparin- and contactin-binding regions.	Heparin	155-162	avian tenascin X	Gallus gallus	129-137
10222132-10	1999	Taken together, these results indicate that: (A) binding of TSP-1 to fibronectin or heparin is a two-step mechanism where binding to one site leads to conformational changes that enable binding to the second site; (B) TSP-1 in complex with fibronectin or heparin adopts the Ca2+-containing conformation in the absence of Ca2+; and (C) such complexes are highly resistant to cleavage by tPA and, if cleaved by other enzymes, the TSP-1 fragments remain bound to other ECM components.	Heparin	84-91	chromosome 20 open reading frame 181	Homo sapiens	386-389
15992116-1	1999	The antithrombotic efficacy of low molecular weight heparins suggest that specific inhibition of blood coagulation factor Xa (fXa) is an appropriate target for drug discovery.	Heparin	52-60	coagulation factor X	Homo sapiens	115-124
15992116-1	1999	The antithrombotic efficacy of low molecular weight heparins suggest that specific inhibition of blood coagulation factor Xa (fXa) is an appropriate target for drug discovery.	Heparin	52-60	coagulation factor X	Homo sapiens	126-129
10593896-9	1999	Glypican-1 abrogated the stimulatory effect of heparin, and heparin reversed the inhibitory effect of glypican-1, indicating that this HSPG inhibits FGF-7 activities by acting, most likely, as a competitive inhibitor of stimulatory HSPG species for FGF-7.	Heparin	60-67	glypican 1	Homo sapiens	102-112
10593896-9	1999	Glypican-1 abrogated the stimulatory effect of heparin, and heparin reversed the inhibitory effect of glypican-1, indicating that this HSPG inhibits FGF-7 activities by acting, most likely, as a competitive inhibitor of stimulatory HSPG species for FGF-7.	Heparin	60-67	CD44 molecule (Indian blood group)	Homo sapiens	135-139
10328304-0	1999	New synthetic heparin mimetics able to inhibit thrombin and factor Xa.	Heparin	14-21	coagulation factor X	Homo sapiens	60-69
12164862-6	2002	Addition of neutralizing anti-heparin-binding EGF-like growth factor (HB-EGF) antibody, pretreatment with heparin and the metalloproteinase (MMP) inhibitor batimastat blocked FN expression.	Heparin	30-37	heparin binding EGF like growth factor	Homo sapiens	70-76
10081605-2	1999	Midkine (MK) is known to be a member of a family of heparin-binding neurotrophic factors.	Heparin	52-59	midkine	Rattus norvegicus	0-7
10081605-2	1999	Midkine (MK) is known to be a member of a family of heparin-binding neurotrophic factors.	Heparin	52-59	midkine	Rattus norvegicus	9-11
10600606-5	1999	Heparin and mannan also inhibit SDF-1alpha binding to intact CD4(+) CXCR4(+/-) cells, and electroblotted soluble CD4.	Heparin	0-7	C-X-C motif chemokine receptor 4	Homo sapiens	68-73
10585718-4	1999	When fused with the c-jun leucine zipper domain, which binds heparin and forms homodimers, the polypeptide specifically reproduced the mitogenic and morphogenic activities of basic FGF with similar potency (EC50 = 240 pM).	Heparin	61-68	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	20-25
12195696-0	2002	Adverse effect of heparin on antithrombin action during endotoxemia: microhemodynamic and cellular mechanisms.	Heparin	18-25	serpin family C member 1	Homo sapiens	29-41
10363611-13	1999	Using heparin-coated circuits (group C) also led to a significant (p&lt;0.05) IL-10 upregulation (C: peak at 2 h, 1380 pg/ml) and IL-6 suppression (C: peak at 4 h, 290 pg/ml).	Heparin	6-13	interleukin 10	Homo sapiens	78-83
12195696-1	2002	A recent clinical sepsis trial reported a significant reduction in 90-day mortality by antithrombin (AT) exclusively in the subgroup of patients without simultaneous heparin prophylaxis.	Heparin	166-173	serpin family C member 1	Homo sapiens	87-99
11964399-7	2002	Heparin also inhibited N-Shh endocytosis, implicating proteoglycans in the internalization process, as has been described for other megalin ligands.	Heparin	0-7	sonic hedgehog signaling molecule	Homo sapiens	23-28
10091426-0	1999	Recombinant human tissue plasminogen activator without heparin is effective in the treatment of hepatic veno-occlusive disease.	Heparin	55-62	chromosome 20 open reading frame 181	Homo sapiens	18-46
12413592-7	2002	These results suggest that PCI is similar to ATIII and depends upon ternary complex formation with heparin and these specific thrombin exosite-2 residues to accelerate thrombin inhibition.	Heparin	99-106	serpin family C member 1	Homo sapiens	45-50
12096065-7	2002	SLP binding to apical microvillous membranes was weaker and was inhibited by heparin.	Heparin	77-84	septin 9	Rattus norvegicus	0-3
12096065-8	2002	SLP bound more strongly to heparin itself, and this binding was inhibited by glucuronic acid and chondroitin sulfate.	Heparin	27-34	septin 9	Rattus norvegicus	0-3
12096065-9	2002	These data are consistent with the hypothesis that the time spent by secreted SLP in the lamina propria is prolonged by strong interactions with proteins in the basolateral membranes, and in the intestinal lumen by weaker interactions with apical membrane components, including heparin.	Heparin	278-285	septin 9	Rattus norvegicus	78-81
12645893-2	2002	Protein sequence comparisons with the other 10 known antithrombin sequences and with sequences of other serpins have provided striking evidence for the conservation of the heparin activation mechanism and new insight into those residues important for heparin binding, for heparin activation, and for reactive center loop function, as well as an indication of which glycosylation sites might be needed for function.	Heparin	172-179	serpin family C member 1	Homo sapiens	53-65
12645893-2	2002	Protein sequence comparisons with the other 10 known antithrombin sequences and with sequences of other serpins have provided striking evidence for the conservation of the heparin activation mechanism and new insight into those residues important for heparin binding, for heparin activation, and for reactive center loop function, as well as an indication of which glycosylation sites might be needed for function.	Heparin	251-258	serpin family C member 1	Homo sapiens	53-65
12645893-2	2002	Protein sequence comparisons with the other 10 known antithrombin sequences and with sequences of other serpins have provided striking evidence for the conservation of the heparin activation mechanism and new insight into those residues important for heparin binding, for heparin activation, and for reactive center loop function, as well as an indication of which glycosylation sites might be needed for function.	Heparin	251-258	serpin family C member 1	Homo sapiens	53-65
12124681-2	2002	Their action is in contrast to heparin and its derivatives, which inhibit thrombin and other coagulation serine proteases via antithrombin, and to the warfarin-type drugs that interfere with synthesis of the precursors of the coagulation serine proteases.	Heparin	31-38	serpin family C member 1	Homo sapiens	126-138
12087470-7	2002	Furthermore, non-anticoagulant heparin-carrying polystyrene markedly reduced the number of CD34-positive vessels in subcutaneous Lewis lung cancer tumours, indicating a strong inhibition of angiogenesis.	Heparin	31-38	CD34 antigen	Mus musculus	91-95
27264755-2	2002	It is a synthetic pentasaccharide mimicking the site of heparin that binds to antithrombin III (AT).	Heparin	56-63	serpin family C member 1	Homo sapiens	78-94
12028043-0	2002	Tissue factor and tissue factor pathway inhibitor levels in unstable angina patients during short-term low-molecular-weight heparin administration.	Heparin	124-131	coagulation factor III, tissue factor	Homo sapiens	0-13
12028043-8	2002	This study provides evidence that low-molecular-weight heparin (LMWH) administration, in addition to a reduction of hypercoagulability and a mild fibrinolytic activation, is associated with decreased TF levels, so indicating a novel mechanism of interference of LMWH with the haemostatic system.	Heparin	55-62	coagulation factor III, tissue factor	Homo sapiens	200-202
11973346-4	2002	[(35)S]heparin ligand blot assays identified a 33/30 kDa doublet (p33/30) in detergent/high ionic strength extracts and heparin soluble fractions obtained from intact C(2)C(12) myoblasts.	Heparin	7-14	inhibitor of growth family member 1	Homo sapiens	66-69
12004255-7	2002	Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces.	Heparin	61-68	serpin family C member 1	Homo sapiens	0-12
12004255-12	2002	The results of a recent phase 3 clinical trials with high-dose antithrombin in sepsis suggested a beneficial effect in patients who did not concomitantly receive heparin, thereby generating new challenges in the understanding of interactions between antithrombin and heparin or heparin-like proteoglycans.	Heparin	162-169	serpin family C member 1	Homo sapiens	63-75
12004255-12	2002	The results of a recent phase 3 clinical trials with high-dose antithrombin in sepsis suggested a beneficial effect in patients who did not concomitantly receive heparin, thereby generating new challenges in the understanding of interactions between antithrombin and heparin or heparin-like proteoglycans.	Heparin	267-274	serpin family C member 1	Homo sapiens	63-75
11991744-3	2002	Cell attachment of the VLP is efficiently inhibited by soluble heparin and dextran sulfate and less efficiently abrogated by several other glycosaminoglycans (GAGs) including chondroitin sulfate A and chondroitin sulfate B (dermatan sulfate), as determined by deconvolution microscopic immunodetection of the viral gag protein and by quantitative binding studies of metabolically labeled (35)S-VLP.	Heparin	63-70	VHL like	Homo sapiens	23-26
11991744-6	2002	De-sulfated heparins are less efficient than native heparin in inhibiting the Polybrene-mediated binding of VLP, whereas growth of human cells in the presence of sodium chlorate leads to significant reduction of Polybrene-mediated VLP binding.	Heparin	12-20	VHL like	Homo sapiens	108-111
11991744-6	2002	De-sulfated heparins are less efficient than native heparin in inhibiting the Polybrene-mediated binding of VLP, whereas growth of human cells in the presence of sodium chlorate leads to significant reduction of Polybrene-mediated VLP binding.	Heparin	12-19	VHL like	Homo sapiens	108-111
11991744-7	2002	In addition, specific inhibition of VLP binding and infectivity of mature infectious VSV-G-pseudotyped virus is observed in the presence of heparin and HS under Polybrene-free conditions.	Heparin	140-147	VHL like	Homo sapiens	36-39
11978889-8	2002	Heparin therapy resulted in significant improvement in macroscopic and microscopic features of colitis (p &lt; 0.05), accompanied by a partial reduction in myeloperoxidase levels.	Heparin	0-7	myeloperoxidase	Rattus norvegicus	156-171
11796709-4	2002	Heparin affinity chromatography resolved low affinity, inactive LPL displaying ER characteristics from a high affinity, active fraction exhibiting both ER and Golgi forms.	Heparin	0-7	lipoprotein lipase	Homo sapiens	64-67
12091056-1	2002	Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a specific pentasaccharide sequence.	Heparin	50-57	serpin family C member 1	Homo sapiens	0-12
12091056-1	2002	Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a specific pentasaccharide sequence.	Heparin	59-62	serpin family C member 1	Homo sapiens	0-12
11888934-3	2002	In this study, we demonstrate that heparin-binding epidermal growth factor-like growth factor (HB-EGF), a prostate smooth muscle-derived mitogen and survival factor, can evoke NE differentiation in LNCaP human PCa cells.	Heparin	35-42	heparin binding EGF like growth factor	Homo sapiens	95-101
11750290-3	2002	These four heterozygous carriers with one defective LPL allele showed 45-57% of the mean LPL activity and mass in the post-heparin plasma (PHP) observed in normal individuals.	Heparin	123-130	lipoprotein lipase	Homo sapiens	52-55
11750290-3	2002	These four heterozygous carriers with one defective LPL allele showed 45-57% of the mean LPL activity and mass in the post-heparin plasma (PHP) observed in normal individuals.	Heparin	123-130	lipoprotein lipase	Homo sapiens	89-92
11836169-10	2002	INTERPRETATION AND CONCLUSIONS: Lower than expected thrombin inhibition by endogenous antithrombin action after full activation by heparin addition was found to be a common feature in patients who suffered from previous venous thrombotic events, and may reflect a hitherto unrecognized thrombophilic alteration.	Heparin	131-138	serpin family C member 1	Homo sapiens	86-98
11828278-0	2002	Antithrombin III concentrate to treat heparin resistance in patients undergoing cardiac surgery.	Heparin	38-45	serpin family C member 1	Homo sapiens	0-16
11828278-1	2002	OBJECTIVE: The purpose of this report is to describe the clinical use of antithrombin III concentrate in 53 patients who were found, in the operating room before cardiopulmonary bypass, to be heparin resistant.	Heparin	192-199	serpin family C member 1	Homo sapiens	73-89
11828278-7	2002	Administration of antithrombin III concentrate (500 U in 45 patients and 1000 U in 8 patients) resulted in prolongation of the mean activated clotting time from 492 to 789 seconds without additional heparin.	Heparin	199-206	serpin family C member 1	Homo sapiens	18-34
11828278-8	2002	The mean heparin dose response increased from 36.5 to 69.3 s x U(-1) x mL(-1) with antithrombin III treatment.	Heparin	9-16	serpin family C member 1	Homo sapiens	83-99
11828278-10	2002	CONCLUSIONS: On the basis of the criterion used in this report, most of the patients defined as being heparin resistant had subnormal plasma antithrombin III activity.	Heparin	102-109	serpin family C member 1	Homo sapiens	141-157
11828278-11	2002	Treatment with antithrombin III concentrate resulted in potentiation of the heparin effect to meet predetermined activated clotting time thresholds and allow for cardiopulmonary bypass.	Heparin	76-83	serpin family C member 1	Homo sapiens	15-31
11885026-6	2002	Heparin also happens to be a good inhibitor of P-selectin, which is expressed on activated platelets or endothelial cells.	Heparin	0-7	selectin P	Homo sapiens	47-57
11885026-7	2002	We have found that heparin blocks P-selectin-mediated interactions of endogenous platelets with sialylated fucosylated mucins on circulating carcinoma cells and that this reduces tumor cell survival.	Heparin	19-26	selectin P	Homo sapiens	34-44
11714710-7	2002	In addition, both 6-O- and 2-O-desulfated heparin activated FGF-1 signaling via FGFR2 IIIb, whereas neither one stimulated FGF-1 signaling via FGFR1 or FGF-7 via FGFR2 IIIb.	Heparin	42-49	fibroblast growth factor receptor 2	Homo sapiens	80-85
11739083-1	2002	Insulin-like growth factor-binding protein (IGFBP)-3 contains a highly basic COOH-terminal heparin-binding region, the P3 region, which is thought to be important in the binding of IGFBP-3 to endothelial cells.	Heparin	91-98	insulin like growth factor binding protein 3	Homo sapiens	0-52
11754875-4	2002	Heparin (10-300 U/mL) concentration-dependently inhibited the neutrophil migration induced by piratoxin-I, bothropstoxin-II, and N. m. mocambique and A. mellifera venom PLA2s (100 microg/mL each), but failed to affect the migration induced by porcine pancreas PLA2.	Heparin	0-7	phospholipase A2	Apis mellifera	169-173
11801740-13	2002	Data indicate that antithrombin directly inhibits chemokine-stimulated migration of monocytes and lymphocytes via the effects of its heparin-binding site on cell surface syndecan-4 by activation of protein kinase C and Rho signaling.	Heparin	133-140	serpin family C member 1	Homo sapiens	19-31
10048585-5	1999	The 200 kDa protein (p200) is dephosphorylated within 2.5 min after heparin treatment with an IC50 that closely parallels the IC50 for growth inhibition.	Heparin	68-75	AT-rich interaction domain 2	Homo sapiens	21-25
10048585-6	1999	Studies using the tyrosine phosphatase inhibitor, sodium orthovanadate, indicate that heparin blocks p200 phosphorylation by inhibiting a kinase.	Heparin	86-93	AT-rich interaction domain 2	Homo sapiens	101-105
11948705-9	2002	The reduction of E-selectin (-31 +/- 7 vs. -6 +/- 5 and -6 +/- 5%, respectively, P &lt; 0.001) was most prominent in the patients treated by heparin precipitation.	Heparin	141-148	selectin E	Homo sapiens	17-27
10048585-7	1999	Phosphorylation of p200 is not altered in heparin-resistant cells, supporting a role for p200 in mediating the antiproliferative effect of heparin.	Heparin	139-146	AT-rich interaction domain 2	Homo sapiens	19-23
10048585-7	1999	Phosphorylation of p200 is not altered in heparin-resistant cells, supporting a role for p200 in mediating the antiproliferative effect of heparin.	Heparin	139-146	AT-rich interaction domain 2	Homo sapiens	89-93
11728396-4	2001	Starting from a "supersulfated" low-molecular weight heparin, we obtained products with up to 40% of iduronate residues O-sulfated exclusively at C-2 and up to 40% of their glucosamine residues O-sulfated at both C-6 and C-3.	Heparin	53-60	complement C2	Homo sapiens	146-149
10052688-6	1999	The amount of BRCA1 expressed by cells was expressed as a ratio, in percent, calculated as follows: 100x amount of labelled DNA-binding proteins (dpm) that bound specifically to the anti-BRCA1 polyclonal antibodies (K-18)/amount of whole labelled DNA-binding protein (dpm) purified on a heparin column.	Heparin	287-294	BRCA1 DNA repair associated	Homo sapiens	14-19
9882449-2	1999	The studies reported here examined the mechanism whereby heparin enhances C1 esterase inhibitor (C1INH) activity on C1 esterase (C1).	Heparin	57-64	serpin family G member 1	Homo sapiens	74-95
9882449-2	1999	The studies reported here examined the mechanism whereby heparin enhances C1 esterase inhibitor (C1INH) activity on C1 esterase (C1).	Heparin	57-64	serpin family G member 1	Homo sapiens	97-102
9882449-3	1999	The interaction of heparin and heparan sulfate with C1INH was first examined using surface plasmon resonance.	Heparin	19-26	serpin family G member 1	Homo sapiens	52-57
9882449-5	1999	Heparin immobilized at its reducing end interacted with C1INH, giving an association constant (Ka) value of 1.43 x 10(7) M-1, whereas heparin immobilized in midchain afforded a Ka value of 7 x 10(6) M-1.	Heparin	0-7	serpin family G member 1	Homo sapiens	56-61
9882449-7	1999	Next, the augmentation of C1INH by heparin (Mr (av) 13,000), low-molecular-weight (LMW) heparin (Mr (av) 5000), and heparan sulfate (Mr (av) 11,000) was determined.	Heparin	35-42	serpin family G member 1	Homo sapiens	26-31
9882449-10	1999	In contrast, when C1 was present as EAC1, heparin augmented C1INH activity at all C1INH concentrations examined and LMW heparin was up to 1.3 times more effective than heparin.	Heparin	42-49	serpin family G member 1	Homo sapiens	60-65
9882449-10	1999	In contrast, when C1 was present as EAC1, heparin augmented C1INH activity at all C1INH concentrations examined and LMW heparin was up to 1.3 times more effective than heparin.	Heparin	42-49	serpin family G member 1	Homo sapiens	82-87
10502232-2	1999	Studies in patients scheduled for percutaneous coronary intervention and those with unstable angina or non-Q-wave myocardial infarction have shown that a combination of intravenous GP IIb-IIIa inhibitors with aspirin and heparin is associated with a reduction in death or myocardial infarction compared with therapy with aspirin and heparin alone.	Heparin	333-340	integrin subunit alpha 2b	Homo sapiens	181-187
10502235-5	1999	When used in conjunction with aspirin and heparin, GP IIb-IIIa inhibitors have yielded favorable clinical outcomes, reducing the incidence of death, myocardial infarction, and urgent intervention.	Heparin	42-49	integrin subunit alpha 2b	Homo sapiens	51-57
10462449-2	1999	This TrxR1 form was not retained on a heparin affinity matrix, it contained one selenium per subunit, was highly active catalytically, and showed strong cross-reactivity with anti-rat liver TrxR1 polyclonal antibodies.	Heparin	38-45	thioredoxin reductase 1	Homo sapiens	5-10
10462449-9	1999	Affinity of purified fully active TrxR1 to heparin could be induced by reduction with NADPH or tris-(2-carboxyethyl)phosphine (TCEP).	Heparin	43-50	thioredoxin reductase 1	Homo sapiens	34-39
11795306-6	2001	HB-EGF-dependent EGFR activation is blocked by heparin, a growth inhibitor of SMCs in vitro and in vivo.	Heparin	47-54	heparin binding EGF like growth factor	Homo sapiens	0-6
10695486-7	1999	In addition heparin and particular antiaggregatory drugs inhibiting platelet activation by blocking the GPIIb/IIIa receptor, the common pathway for platelet aggregation, are applied to prevent thrombus formation.	Heparin	12-19	integrin subunit alpha 2b	Homo sapiens	104-109
9890310-6	1999	By zymography, MMP-2 was significantly increased after treatment with PPS (P &lt; 0.001) and heparin (P &lt; 0.05).	Heparin	93-100	matrix metallopeptidase 2	Mus musculus	15-20
10074643-5	1999	After 90 min simulated ECC, the heparin-coated systems showed significantly higher platelet count, lower platelet-factor 4 release, reduced contact activation (factor XIIa and kallikrein), and lower neutrophil elastase levels (p &lt; 0.05), compared to the noncoated oxygenator group.	Heparin	32-39	kallikrein related peptidase 4	Homo sapiens	176-186
10462498-6	1999	Further analysis showed that ruthenium red and heparin differentially inhibit RANTES-, SDF-1alpha-, or MDC-induced calcium mobilization in IL-2-activated NK cells.	Heparin	47-54	C-C motif chemokine ligand 5	Rattus norvegicus	78-84
11748680-8	2001	Their binding activity to antithrombin III was not proportional to the content of heparin immobilized, and heparin-PGMA-I was the most efficient affinity medium for antithrombin III.	Heparin	107-114	serpin family C member 1	Homo sapiens	165-181
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	0-7	coagulation factor X	Homo sapiens	103-112
10433728-1	1999	Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin.	Heparin	166-173	coagulation factor X	Homo sapiens	103-112
10532207-3	1999	Because cross-linking of the activated platelet receptor glycoprotein (GP) IIb-IIIa by plasma fibrinogen represents the final common pathway to coronary thrombus formation, several GP IIb-IIIa inhibitors have been developed as a potentially more effective antithrombotic therapy than agents currently used for this purpose, namely aspirin and heparin.	Heparin	343-350	integrin subunit alpha 2b	Homo sapiens	181-187
10393102-3	1999	This release was Ca2+-dependent and was blocked by antibodies against the RyR or CE, by the RyR inhibitor dantrolene, and by a seven-amino-acid peptide fragment corresponding to positions 4689-4697 of the RyR, but not by heparin, an Ins(1,4,5)P3-receptor antagonist.	Heparin	221-228	carbonic anhydrase 2	Homo sapiens	17-20
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Heparin	29-36	heparin cofactor 2	Oryctolagus cuniculus	9-28
9837939-6	1998	Both heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate had fast bimolecular rate constants of 1.4 x 10(7) M-1 s-1 and 1.3 x 10(7) M-1 s-1, respectively, for reaction with thrombin.	Heparin	5-12	prothrombin	Oryctolagus cuniculus	190-198
19078327-3	1998	We recommend the use of a factor Xa inhibition test to regulate heparin in this patient population.	Heparin	64-71	coagulation factor X	Homo sapiens	26-35
19078327-4	1998	This test measures the ability of heparin, as a cofactor of antithrombin III, to inMbit the catalytic function of factor Xa in plasma.	Heparin	34-41	coagulation factor X	Homo sapiens	114-123
9813019-2	1998	We examined the effect of heparin on inhibition of FXIa by the inhibitors C1-inhibitor (C1-INH) and antithrombin III (ATIII).	Heparin	26-33	serpin family G member 1	Homo sapiens	74-86
9813019-2	1998	We examined the effect of heparin on inhibition of FXIa by the inhibitors C1-inhibitor (C1-INH) and antithrombin III (ATIII).	Heparin	26-33	serpin family G member 1	Homo sapiens	88-94
9813019-3	1998	Second order rate constants for inhibition in the absence of heparin were 1.57 x 10(3) and 0.91 x 10(3) M-1 s-1 for C1-INH and ATIII, respectively.	Heparin	61-68	serpin family G member 1	Homo sapiens	116-122
9853400-4	1998	When the sialidase activities were measured using natural substrates, the sialidase activities for the (alpha2-3) and (alpha2-6) sialyllactoses, and colominic acid, were markedly inhibited by heparin and sulfatide similar to 4-MU-NeuAc, although the fetuin sialidase activity was not significantly influenced by them.	Heparin	192-199	immunoglobulin binding protein 1	Homo sapiens	119-127
10456621-7	1999	A decrease in F1+2 was observed during heparin and warfarin treatment (II, 1.7 nmol/ml; III, 1.0 nmol/ml; IV, 0.7 nmol/ml; versus I, 3.5 nmol/ml; P&lt;0.01).	Heparin	39-46	coagulation factor XII	Homo sapiens	14-18
11748680-10	2001	All the three heparin-PGMA beads were exploited for the separation of antithrombin III from human plasma.	Heparin	14-21	serpin family C member 1	Homo sapiens	70-86
10403394-0	1999	Spin-trapping agent alpha-phenyl N-tert-butylnitrone binds to trypsin and enhances heparin-induced inhibition of amidolytic activity and structural degradation of the enzyme.	Heparin	83-90	spindlin 1	Homo sapiens	0-4
11748259-6	2001	Both heparin and the low-molecular weight heparin enoxaparin significantly inhibited MPO binding and protein nitrotyrosine (NO(2)Tyr) formation in both cultured endothelial cells and rat aortic tissues.	Heparin	5-12	myeloperoxidase	Rattus norvegicus	85-88
9809888-6	1998	When GP IIb/IIIa inhibitors are used, weight-adjusted heparin dosing can be decreased to 70 units/kg to achieve a target ACT of 200 seconds with either the HemoTec or Hemochron device.	Heparin	54-61	integrin subunit alpha 2b	Homo sapiens	5-11
11748259-6	2001	Both heparin and the low-molecular weight heparin enoxaparin significantly inhibited MPO binding and protein nitrotyrosine (NO(2)Tyr) formation in both cultured endothelial cells and rat aortic tissues.	Heparin	42-49	myeloperoxidase	Rattus norvegicus	85-88
10334872-5	1999	Heparin, at high concentrations, can prevent the inhibition of tryptase by MPO.	Heparin	0-7	tryptase delta 1	Homo sapiens	63-71
10334872-7	1999	These data suggest that MPO inhibits tryptase by interfering with the heparin stabilization of tryptase tetramer.	Heparin	70-77	tryptase delta 1	Homo sapiens	37-45
11737589-8	2001	Addition of neutralizing anti-HB-EGF antibody, as well as pretreatment with heparin or the metalloproteinase inhibitor batimastat abolished induction of FN expression by Ang II.	Heparin	76-83	fibronectin 1	Mus musculus	153-155
10334872-7	1999	These data suggest that MPO inhibits tryptase by interfering with the heparin stabilization of tryptase tetramer.	Heparin	70-77	tryptase delta 1	Homo sapiens	95-103
10341219-0	1999	Teneurin-1, a vertebrate homologue of the Drosophila pair-rule gene ten-m, is a neuronal protein with a novel type of heparin-binding domain.	Heparin	118-125	teneurin transmembrane protein 1	Homo sapiens	0-10
9731752-4	1998	FGF-1 in the culture medium produced a dose-dependent increase in the number and length of neurites produced by spiral ganglion neurons, a response that was enhanced by heparin.	Heparin	169-176	fibroblast growth factor 1	Rattus norvegicus	0-5
9671710-0	1998	Human thioredoxin reductase from HeLa cells: selective alkylation of selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin.	Heparin	172-179	2,4-dienoyl-CoA reductase 1	Homo sapiens	143-148
10341219-6	1999	We show that recombinantly expressed proteins containing the YD-repeats of teneurin-1 bind to heparin.	Heparin	94-101	teneurin transmembrane protein 1	Homo sapiens	75-85
11533057-10	2001	Our results suggest a model for tryptase tetramer formation that involves bridging of tryptase monomers by heparin or other highly sulfated polysaccharides of sufficient chain length.	Heparin	107-114	tryptase alpha/beta 1	Mus musculus	86-94
10222132-8	1999	Cleavage by thrombin or tissue plasminogen activator (tPA) showed that Ca2+-depleted TSP-1, when bound to fibronectin or to heparin, yielded proteolytic cleavage patterns typical of the Ca2+-containing form.	Heparin	124-131	chromosome 20 open reading frame 181	Homo sapiens	54-57
10408366-8	1999	The factor H-like protein 1 (FHL-1) or reconectin shares the complement regulatory functions with factor H and interacts with heparin.	Heparin	126-133	complement factor H	Homo sapiens	4-12
9642241-7	1998	However, in the presence of an optimum concentration of heparin ( approximately 50 nM) the inactivation rate constant of FXa in the presence of Ca2+ (k2 = 4.4 x 10(7) M-1 s-1) was 13-fold higher than the rate constant in the absence of Ca2+ (k2 = 3.5 x 10(6) M-1 s-1).	Heparin	56-63	coagulation factor X	Homo sapiens	121-124
9642241-9	1998	The additional cofactor effect of heparin with all FXa derivatives was a bell-shaped curve, which disappeared if the ionic strength of the reaction was increased to approximately 0.4.	Heparin	34-41	coagulation factor X	Homo sapiens	51-54
9642241-10	1998	These results suggest that although the major effect of heparin in acceleration of FXa inactivation is through a heparin-induced conformational change in the reactive site loop of AT, the template effect of heparin, nevertheless, contributes significantly to rapid FXa inactivation at physiological Ca2+.	Heparin	56-63	coagulation factor X	Homo sapiens	83-86
9642241-10	1998	These results suggest that although the major effect of heparin in acceleration of FXa inactivation is through a heparin-induced conformational change in the reactive site loop of AT, the template effect of heparin, nevertheless, contributes significantly to rapid FXa inactivation at physiological Ca2+.	Heparin	56-63	coagulation factor X	Homo sapiens	265-268
9642241-10	1998	These results suggest that although the major effect of heparin in acceleration of FXa inactivation is through a heparin-induced conformational change in the reactive site loop of AT, the template effect of heparin, nevertheless, contributes significantly to rapid FXa inactivation at physiological Ca2+.	Heparin	113-120	coagulation factor X	Homo sapiens	83-86
9642241-10	1998	These results suggest that although the major effect of heparin in acceleration of FXa inactivation is through a heparin-induced conformational change in the reactive site loop of AT, the template effect of heparin, nevertheless, contributes significantly to rapid FXa inactivation at physiological Ca2+.	Heparin	113-120	coagulation factor X	Homo sapiens	265-268
9642241-10	1998	These results suggest that although the major effect of heparin in acceleration of FXa inactivation is through a heparin-induced conformational change in the reactive site loop of AT, the template effect of heparin, nevertheless, contributes significantly to rapid FXa inactivation at physiological Ca2+.	Heparin	113-120	coagulation factor X	Homo sapiens	83-86
9642241-10	1998	These results suggest that although the major effect of heparin in acceleration of FXa inactivation is through a heparin-induced conformational change in the reactive site loop of AT, the template effect of heparin, nevertheless, contributes significantly to rapid FXa inactivation at physiological Ca2+.	Heparin	113-120	coagulation factor X	Homo sapiens	265-268
9632653-0	1998	The basic domain in HIV-1 Tat protein as a target for polysulfonated heparin-mimicking extracellular Tat antagonists.	Heparin	69-76	Tat	Human immunodeficiency virus 1	26-29
9632653-0	1998	The basic domain in HIV-1 Tat protein as a target for polysulfonated heparin-mimicking extracellular Tat antagonists.	Heparin	69-76	Tat	Human immunodeficiency virus 1	101-104
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	293-300	LDL receptor related protein associated protein 1	Rattus norvegicus	169-196
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	293-300	LDL receptor related protein associated protein 1	Rattus norvegicus	198-201
10201667-8	1999	Twenty units per kilogram of heparin significantly reduced the increase of F1+2 after relocation of the hip joint (P &lt; 0.001).	Heparin	29-36	coagulation factor XII	Homo sapiens	75-79
10323280-2	1999	The antithrombin III-stimulated release of big endothelin-1 and endothelin-1 (1.7-fold and 1.3-fold over baseline) was abolished by nicardipine (L-type Ca2+ channel blocker), heparin, and N-acetyl heparin (a derivative devoid of antithrombin affinity), whereas staurosporine and genistein (inhibitors of protein kinase C and tyrosine kinase, respectively) were ineffective.	Heparin	175-182	serpin family C member 1	Rattus norvegicus	4-20
9632653-5	1998	Dissociation of the GST-TatR49/52/53/55/56/57A.heparin complex occurred at ionic strength significantly lower than that required to dissociate the GST-Tat.heparin complex.	Heparin	47-54	Tat	Human immunodeficiency virus 1	24-27
9632653-5	1998	Dissociation of the GST-TatR49/52/53/55/56/57A.heparin complex occurred at ionic strength significantly lower than that required to dissociate the GST-Tat.heparin complex.	Heparin	155-162	Tat	Human immunodeficiency virus 1	24-27
11705698-2	2001	This study tests the hypothesis that proteolytic removal of the heparin-binding domain of EC-SOD results in clearance of the enzyme from the extracellular matrix of pulmonary tissues and leads to a loss of antioxidant protection.	Heparin	64-71	superoxide dismutase 3, extracellular	Mus musculus	90-96
9616153-9	1998	Additional studies indicated that, in the presence of phospholipid vesicles, heparin and dextran sulfate dramatically accelerate PC activation by fXa by also reducing the Km.	Heparin	77-84	coagulation factor X	Homo sapiens	146-149
10323280-3	1999	Thus, (i) the antithrombin III-induced release of endothelins requires extracellular Ca2+, but not protein kinase C or tyrosine kinase activation, and (ii) heparin binding to antithrombin III is not necessary for its inhibitory effect.	Heparin	156-163	serpin family C member 1	Rattus norvegicus	175-191
10080937-2	1999	To further characterize the enzymatic properties of CPZ, the enzyme was purified using Arg- and heparin-affinity columns.	Heparin	96-103	carboxypeptidase Z	Homo sapiens	52-55
11705698-10	2001	These results indicate that injuries leading to pulmonary fibrosis have a significant effect on EC-SOD distribution due to proteolytic removal of the heparin-binding domain and may be important in enhancing pulmonary injuries by altering the oxidant/antioxidant balance in alveolar interstitial spaces.	Heparin	150-157	superoxide dismutase 3, extracellular	Mus musculus	96-102
9603953-6	1998	Both sPLA2s-IIA and -V, but not sPLA2-IIC, were heparin-binding PLA2s that exhibited significant affinity for cell-surface proteoglycans, and site-directed mutations in residues responsible for their membrane association or catalytic activity markedly reduced their ability to release AA from activated cells.	Heparin	48-55	phospholipase A2 group IIA	Homo sapiens	5-10
11760675-1	2001	UNLABELLED: We report a case of renal vein thrombosis, treated with heparin and thrombolytic therapy, in a patient who was heterozygous for both factor V Leiden and prothrombin mutations.	Heparin	68-75	coagulation factor V	Homo sapiens	145-160
9636912-9	1998	CONCLUSIONS: Heparin-coated CPB circuits reduced TPA release in this homogeneous CABG population with routine heparin/protamine management.	Heparin	13-20	chromosome 20 open reading frame 181	Homo sapiens	49-52
9636912-9	1998	CONCLUSIONS: Heparin-coated CPB circuits reduced TPA release in this homogeneous CABG population with routine heparin/protamine management.	Heparin	110-117	chromosome 20 open reading frame 181	Homo sapiens	49-52
12160213-1	1999	Midkine (MK) is a new member of the family of heparin-binding neurotrophic factors.	Heparin	46-53	midkine	Rattus norvegicus	0-7
12160213-1	1999	Midkine (MK) is a new member of the family of heparin-binding neurotrophic factors.	Heparin	46-53	midkine	Rattus norvegicus	9-11
10516434-11	1999	Because many growth factors and cytokines interact with cells via heparin/heparan sulfate-proteoglycan, RPL29/HIP may play an important role on the cell surface by modulating interactions between cells and extracellular molecules.	Heparin	66-73	ribosomal protein L29	Homo sapiens	104-113
11564011-10	2001	RESULTS: Enoxaparin and heparin significantly ameliorated the severity of dinitrobenzene sulphonic acid- and iodoacetamide-induced colitis as demonstrated by a decrease in mucosal lesion area, colonic weight and mucosal myeloperoxidase and nitric oxide synthase activities.	Heparin	24-31	myeloperoxidase	Rattus norvegicus	220-235
9620142-10	1998	RESULTS: Heparin leached off all grafts in plasma (mean values: HBGA, 83.4 U of heparin/ml; HBGB-8, 4 U of heparin/ml; HBGB-6, 6.2 U of heparin/ml).	Heparin	9-16	hemoglobin subunit gamma 1	Homo sapiens	64-68
9620142-11	1998	In normal saline, the mean heparin concentrations were lower (HBGA, 10.8 U of heparin/ml; HBGB-8, 0 U of heparin/ml; HBGB-6, 0.01 U of heparin/ml.	Heparin	27-34	hemoglobin subunit gamma 1	Homo sapiens	62-66
9558322-9	1998	Computational docking of the peptide onto the X-ray structure of thrombin suggests that the phosphate may interact with basic residues at the rim of the heparin binding site of thrombin.	Heparin	153-160	coagulation factor II, thrombin	Bos taurus	65-73
9558322-9	1998	Computational docking of the peptide onto the X-ray structure of thrombin suggests that the phosphate may interact with basic residues at the rim of the heparin binding site of thrombin.	Heparin	153-160	coagulation factor II, thrombin	Bos taurus	177-185
10926265-14	1999	The anticoagulant effect of heparin is usually monitored by the APTT, a test that is sensitive to the inhibitory effects of heparin on thrombin, factor Xa.	Heparin	28-35	coagulation factor X	Homo sapiens	145-154
10926265-14	1999	The anticoagulant effect of heparin is usually monitored by the APTT, a test that is sensitive to the inhibitory effects of heparin on thrombin, factor Xa.	Heparin	124-131	coagulation factor X	Homo sapiens	145-154
9841882-5	1998	We first provide evidence that the CyPB binding to heparin-Sepharose is prevented by soluble sulphated glycosaminoglycans (GAG), raising the interesting possibility that such interactions may occur on the T-cell surface.	Heparin	51-58	peptidylprolyl isomerase B	Homo sapiens	35-39
9558116-6	1998	When factor H was mixed with PMNs, 1.4 to 3.8-fold more cells adhered to immobilized heparin or chondroitin A.	Heparin	85-92	complement factor H	Homo sapiens	5-13
11668418-5	2001	This indicates that heparins can influence cellular signaling in SMC via an antithrombin-II (AT-III)-independent mechanism.	Heparin	20-28	serpin family C member 1	Homo sapiens	76-91
9558116-7	1998	In addition, augmented adhesion of PMNs was measured when factor H, but not HSA or C9, was absorbed to wells that were first coated with heparin or chondroitin A.	Heparin	137-144	complement factor H	Homo sapiens	58-66
9826600-4	1998	Both InsP3R expression products consistently behaved like those of the native type-1 receptor isoform isolated from cerebellum in terms of their InsP3, Ca2+, and heparin sensitivity.	Heparin	162-169	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	5-11
11668418-5	2001	This indicates that heparins can influence cellular signaling in SMC via an antithrombin-II (AT-III)-independent mechanism.	Heparin	20-28	serpin family C member 1	Homo sapiens	93-99
9916505-6	1998	H16 mAb specifically bound to heparin, heparan sulfate and human umbilical vascular endothelial cells (HUVEC).	Heparin	30-37	H1.6 linker histone, cluster member	Homo sapiens	0-3
9916505-7	1998	The binding of H16 mAb to HUVEC was specifically inhibited by heparin.	Heparin	62-69	H1.6 linker histone, cluster member	Homo sapiens	15-18
11535494-10	2001	Activity of vWF-cp is unusually stable during incubation at 37 degrees C; its in vitro half-life in citrated human plasma, heparin plasma, or serum is longer than 1 week.	Heparin	123-130	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	12-18
9916505-8	1998	Further, H16 mAb inhibited the binding of antithrombin III to heparin in a dose dependent manner.	Heparin	62-69	H1.6 linker histone, cluster member	Homo sapiens	9-12
9546743-7	1998	In vitro binding studies of 125I-perlecan to a 17-amino acid synthetic peptide sequence of HIP, which has a high affinity and specificity for heparin/heparan sulfate, indicates that perlecan binds to the HIP peptide with high affinity (KDapp = 0.6 nM) and in a heparin-inhibitable manner.	Heparin	142-149	ribosomal protein L29	Homo sapiens	91-94
9546743-7	1998	In vitro binding studies of 125I-perlecan to a 17-amino acid synthetic peptide sequence of HIP, which has a high affinity and specificity for heparin/heparan sulfate, indicates that perlecan binds to the HIP peptide with high affinity (KDapp = 0.6 nM) and in a heparin-inhibitable manner.	Heparin	142-149	ribosomal protein L29	Homo sapiens	204-207
9546743-7	1998	In vitro binding studies of 125I-perlecan to a 17-amino acid synthetic peptide sequence of HIP, which has a high affinity and specificity for heparin/heparan sulfate, indicates that perlecan binds to the HIP peptide with high affinity (KDapp = 0.6 nM) and in a heparin-inhibitable manner.	Heparin	261-268	ribosomal protein L29	Homo sapiens	91-94
9546743-7	1998	In vitro binding studies of 125I-perlecan to a 17-amino acid synthetic peptide sequence of HIP, which has a high affinity and specificity for heparin/heparan sulfate, indicates that perlecan binds to the HIP peptide with high affinity (KDapp = 0.6 nM) and in a heparin-inhibitable manner.	Heparin	261-268	ribosomal protein L29	Homo sapiens	204-207
9639548-0	1998	Basic fibroblast growth factor-mediated lymphangiogenesis of lymphatic endothelial cells isolated from dog thoracic ducts: effects of heparin.	Heparin	134-141	fibroblast growth factor 2	Canis lupus familiaris	0-30
9822691-7	1998	In contrast, only those residues on the interfacial binding site of hIIa-PLA2 are involved in binding to membranes; 2) the relative ability of these mutants to hydrolyze cellular phospholipids when enzymes were added exogenously to CHO-K1, NIH-3T3, and RAW 264.7 cells correlates with their relative in vitro affinity for vesicles and not with their affinity for heparin and heparan sulfate.	Heparin	363-370	phospholipase A2 group IIA	Homo sapiens	73-77
9639548-4	1998	The bFGF (10 ng/ml) caused a significant induction of proliferation and migration of the LEC, the induction of which was augmented dose-dependently by an additional treatment with heparin ranging from 1 to 100 microg/ml.	Heparin	180-187	fibroblast growth factor 2	Canis lupus familiaris	4-8
11535495-6	2001	In this study, the purification of human vWF-cleaving protease from a commercial preparation of factor VIII/vWF concentrate by means of several column chromatographic steps, including 2 steps of heparin-Sepharose column, is reported.	Heparin	195-202	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	41-62
9639548-7	1998	Heparin (10 microg/ml) accelerated both processes of bFGF-mediated lymphangiogenesis of the LEC.	Heparin	0-7	fibroblast growth factor 2	Canis lupus familiaris	53-57
11528374-0	2001	Lipoprotein lipase during continuous heparin infusion: tissue stores become partially depleted.	Heparin	37-44	lipoprotein lipase	Homo sapiens	0-18
9639548-8	1998	These findings suggest that the cultured LEC isolated from dog thoracic ducts have an ability to form lymphatic capillary-like tubes in response to bFGF and that heparin accelerates dose-dependently the process of the bFGF-mediated neovascularization of lymph vessels.	Heparin	162-169	fibroblast growth factor 2	Canis lupus familiaris	218-222
21235922-0	1998	Binding sites on native and multimeric vitronectin exhibit similar affinity for heparin the influence of self-association and multivalence on ligand binding.	Heparin	80-87	vitronectin	Homo sapiens	39-50
21235922-1	1998	A previously accepted model for the morphoregulatory activity of vitronectin is based on the idea that the heparin-binding site is buried within the circulating, monomeric form of vitronectin and that it is exposed on conversion to the multimeric form by denaturation or incorporation into the extracellular matrix.	Heparin	107-114	vitronectin	Homo sapiens	65-76
21235922-1	1998	A previously accepted model for the morphoregulatory activity of vitronectin is based on the idea that the heparin-binding site is buried within the circulating, monomeric form of vitronectin and that it is exposed on conversion to the multimeric form by denaturation or incorporation into the extracellular matrix.	Heparin	107-114	vitronectin	Homo sapiens	180-191
21235922-2	1998	New evidence indicates that the heparin-binding sites are similarly exposed in the two forms of vitronectin and supports an alternative model for apparently altered heparin affinity.	Heparin	32-39	vitronectin	Homo sapiens	96-107
21235922-3	1998	Differences in the heparin-binding properties of circulating and matrix-associated vitronectin result from an increased number of binding sites on the multivalent matrix form.	Heparin	19-26	vitronectin	Homo sapiens	83-94
21235922-4	1998	By analogy with other instances in which multivalent binding interactions increase functional affinity for carbohydrates or lectins, the self-association of vitronectin into a multimeric form allows effective neutralization of heparin at the endothelial surface in the vicinity of a thrombus.	Heparin	227-234	vitronectin	Homo sapiens	157-168
9501087-6	1998	The high affinity of endostatin for heparin is explained by the presence of an extensive basic patch formed by 11 arginine residues.	Heparin	36-43	collagen, type XVIII, alpha 1	Mus musculus	21-31
9840289-2	1998	The study was carried out by analyzing the activity of the two drugs on: (1) extracellular and intracellular Tat protein, introduced into HL3T1 cells containing an integrated HIV-1 LTR/CAT plasmid; (2) binding of Tat to 3H-labeled heparin and to 14C-labeled PNU145156E; and (3) the angiogenic response induced in vivo by culture medium conditioned by T53c14 cells, which release extracellular Tat.	Heparin	231-238	Tat	Human immunodeficiency virus 1	213-216
9840289-2	1998	The study was carried out by analyzing the activity of the two drugs on: (1) extracellular and intracellular Tat protein, introduced into HL3T1 cells containing an integrated HIV-1 LTR/CAT plasmid; (2) binding of Tat to 3H-labeled heparin and to 14C-labeled PNU145156E; and (3) the angiogenic response induced in vivo by culture medium conditioned by T53c14 cells, which release extracellular Tat.	Heparin	231-238	Tat	Human immunodeficiency virus 1	213-216
9815269-6	1998	This is supported by affinity chromatography studies, which showed that RANTES could be eluted specifically by heparin from a mAb 4A12 immunoaffinity matrix.	Heparin	111-118	C-C motif chemokine ligand 5	Homo sapiens	72-78
9825824-1	1998	BACKGROUND: Previously, it has been demonstrated that heparin inhibits major histocompatibility complex (MHC) class II and intercellular adhesion molecule-1 (ICAM-1) expression on interferon-gamma (IFN-gamma)-stimulated human umbilical vein endothelial cells (HUVECs).	Heparin	54-61	intercellular adhesion molecule 1	Homo sapiens	123-156
9825824-1	1998	BACKGROUND: Previously, it has been demonstrated that heparin inhibits major histocompatibility complex (MHC) class II and intercellular adhesion molecule-1 (ICAM-1) expression on interferon-gamma (IFN-gamma)-stimulated human umbilical vein endothelial cells (HUVECs).	Heparin	54-61	intercellular adhesion molecule 1	Homo sapiens	158-164
9825824-6	1998	RESULTS: Heparin was able to inhibit the up-regulation of MHC and ICAM-1 in a dose-dependent fashion on both IFN-gamma-stimulated HUVECs and PTECs.	Heparin	9-16	intercellular adhesion molecule 1	Homo sapiens	66-72
11528374-10	2001	We conclude that when heparin releases LPL into plasma, the lipase becomes liable to be taken up and degraded by the liver.	Heparin	22-29	lipoprotein lipase	Homo sapiens	39-42
11382778-1	2001	The 39-kDa receptor-associated protein (RAP) is a specialized chaperone for members of the low density lipoprotein receptor gene family, which also binds heparin.	Heparin	154-161	LDL receptor related protein associated protein 1	Homo sapiens	4-38
9480871-0	1998	Heparin inhibits Ca2+/calmodulin-dependent kinase II activation and c-fos induction in mesangial cells.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	68-73
9480871-2	1998	In particular, heparin partially suppresses the ability of quiescent RMCs to enter the cell cycle and induce c-fos expression.	Heparin	15-22	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	109-114
9480871-4	1998	However, we have also shown that heparin suppresses c-fos expression in response to ionophores such as ionomycin, an event independent of mitogen-activated protein kinase [Miralem, Wang, Whiteside and Templeton (1996) J. Biol.	Heparin	33-40	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	52-57
11382778-1	2001	The 39-kDa receptor-associated protein (RAP) is a specialized chaperone for members of the low density lipoprotein receptor gene family, which also binds heparin.	Heparin	154-161	LDL receptor related protein associated protein 1	Homo sapiens	40-43
11382778-3	2001	Here we generated a series of truncated and site-directed RAP mutants in order to define the sites within RAP that are important for interacting with heparin and low density lipoprotein receptor-related protein (LRP).	Heparin	150-157	LDL receptor related protein associated protein 1	Homo sapiens	106-109
9480871-13	1998	Heparin (1 microg/ml) suppressed ionomycin-dependent c-fos induction.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	53-58
11382778-4	2001	We found that high affinity binding of RAP to heparin is mediated by the carboxyl-terminal repeat of RAP, whereas both the carboxyl-terminal repeat and a combination of amino and central repeats exhibit high affinity binding to LRP.	Heparin	46-53	LDL receptor related protein associated protein 1	Homo sapiens	39-42
9541411-1	1998	The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa.	Heparin	15-22	coagulation factor X	Homo sapiens	160-169
11382778-4	2001	We found that high affinity binding of RAP to heparin is mediated by the carboxyl-terminal repeat of RAP, whereas both the carboxyl-terminal repeat and a combination of amino and central repeats exhibit high affinity binding to LRP.	Heparin	46-53	LDL receptor related protein associated protein 1	Homo sapiens	101-104
11382778-5	2001	Several motifs were found to mediate the binding of RAP to heparin, and each contained a cluster of basic amino acids; among them, an intact R(282)VSR(285)SR(287)EK(289) motif is required for high affinity binding of RAP to heparin, whereas two other motifs, R(203)LR(205)R(206) and R(314)ISR(317)AR(319), also contribute to this interaction.	Heparin	59-66	LDL receptor related protein associated protein 1	Homo sapiens	52-55
11382778-5	2001	Several motifs were found to mediate the binding of RAP to heparin, and each contained a cluster of basic amino acids; among them, an intact R(282)VSR(285)SR(287)EK(289) motif is required for high affinity binding of RAP to heparin, whereas two other motifs, R(203)LR(205)R(206) and R(314)ISR(317)AR(319), also contribute to this interaction.	Heparin	59-66	LDL receptor related protein associated protein 1	Homo sapiens	217-220
9542658-2	1998	Emerging evidence suggests, moreover, that the membrane proteoglycan, CD44, is a cofactor for the interaction of heparin-binding ligands with their receptors.	Heparin	113-120	CD44 molecule (Indian blood group)	Homo sapiens	70-74
11382778-5	2001	Several motifs were found to mediate the binding of RAP to heparin, and each contained a cluster of basic amino acids; among them, an intact R(282)VSR(285)SR(287)EK(289) motif is required for high affinity binding of RAP to heparin, whereas two other motifs, R(203)LR(205)R(206) and R(314)ISR(317)AR(319), also contribute to this interaction.	Heparin	224-231	LDL receptor related protein associated protein 1	Homo sapiens	52-55
9518874-2	1998	Uniquely among known EGF-like growth factors, its mitogenic activity is inhibited by soluble heparin, but heparin-like molecules on the cell surface and/or in extracellular matrix appear to be necessary for amphiregulin to exert its biological effect.	Heparin	93-100	EGF	Ovis aries	21-24
9518874-2	1998	Uniquely among known EGF-like growth factors, its mitogenic activity is inhibited by soluble heparin, but heparin-like molecules on the cell surface and/or in extracellular matrix appear to be necessary for amphiregulin to exert its biological effect.	Heparin	106-113	amphiregulin	Ovis aries	207-219
9518874-5	1998	Both EGF and transforming growth factor-alpha (TGF-alpha) significantly (P &lt; 0.001) increased DNA synthesis in the presence of heparin.	Heparin	130-137	EGF	Ovis aries	5-8
9518874-8	1998	The heparin antagonist, hexadimethrine, inhibited DNA synthesis, but, in the presence of amphiregulin, approximately equivalent concentrations of heparin overcame this inhibitory effect.	Heparin	146-153	amphiregulin	Ovis aries	89-101
9518874-9	1998	In the presence of heparin, TGF-alpha showed synergistic interactions with insulin or IGF-I.	Heparin	19-26	LOC105613195	Ovis aries	75-82
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	lipoprotein lipase	Mus musculus	38-41
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	interleukin 11	Mus musculus	88-93
11382778-5	2001	Several motifs were found to mediate the binding of RAP to heparin, and each contained a cluster of basic amino acids; among them, an intact R(282)VSR(285)SR(287)EK(289) motif is required for high affinity binding of RAP to heparin, whereas two other motifs, R(203)LR(205)R(206) and R(314)ISR(317)AR(319), also contribute to this interaction.	Heparin	224-231	LDL receptor related protein associated protein 1	Homo sapiens	217-220
9787229-3	1998	In our study, 14 patients with ischaemic central (CRVO) or branch (BRVO) retinal vein occlusion who presented with severe visual loss and recent onset of symptoms were treated with a low dose (50 mg) of recombinant tissue plasminogen activator (rt-PA) and intravenous heparin.	Heparin	268-275	chromosome 20 open reading frame 181	Homo sapiens	215-243
11382778-7	2001	We conclude that electrostatic interactions likely contribute significantly in the binding of RAP to both heparin and LRP and that high affinity interaction with both heparin and LRP appears to require mostly overlapping sequence motifs within RAP.	Heparin	106-113	LDL receptor related protein associated protein 1	Homo sapiens	94-97
9354625-9	1997	The endothelial cell binding sites for IL-8, RANTES, and MCP-1 were deduced to be glycosaminoglycans since competition assays showed the biphasic curves and micromolar IC50 values seen in studies with immobilized heparin, and mRNA for known chemokine receptors was not detected.	Heparin	213-220	C-C motif chemokine ligand 5	Homo sapiens	45-51
11683790-5	2001	Thrombophilia screen demonstrated the presence of protein S deficiency and Factor V Leiden as the prothrombotic factors, together with the demonstration of antiplatelet factor 4 antibodies, which confirms the diagnosis of heparin-induced thrombocytopenia (type II).	Heparin	222-229	coagulation factor V	Homo sapiens	75-90
9342064-3	1997	The binding of extracellular Tat to heparan sulfate proteoglycans (HSPG) was determined by using trypsin, heparin or heparinase in pulse-chase experiments, by gel shift and competition assays with radiolabeled heparin, and by heparin-affinity chromatography.	Heparin	106-113	syndecan 2	Homo sapiens	67-71
9342064-3	1997	The binding of extracellular Tat to heparan sulfate proteoglycans (HSPG) was determined by using trypsin, heparin or heparinase in pulse-chase experiments, by gel shift and competition assays with radiolabeled heparin, and by heparin-affinity chromatography.	Heparin	117-124	syndecan 2	Homo sapiens	67-71
9342064-3	1997	The binding of extracellular Tat to heparan sulfate proteoglycans (HSPG) was determined by using trypsin, heparin or heparinase in pulse-chase experiments, by gel shift and competition assays with radiolabeled heparin, and by heparin-affinity chromatography.	Heparin	117-124	syndecan 2	Homo sapiens	67-71
9342064-4	1997	The mapping of the Tat binding site to heparin was defined by functional assays of rescue of Tat-defective HIV-1 proviruses.	Heparin	39-46	Tat	Human immunodeficiency virus 1	19-22
9342064-4	1997	The mapping of the Tat binding site to heparin was defined by functional assays of rescue of Tat-defective HIV-1 proviruses.	Heparin	39-46	Tat	Human immunodeficiency virus 1	93-96
11457455-4	2001	We have analysed the sequences of worm and fly FGFs and FGFRs and used the recently determined crystal structure of the human FGF1-FGFR2-heparin ternary complex [Pellegrini, L., Burke, D.F., von Delft, F., Mulloy, B. and Blundell, T.L.	Heparin	137-144	fibroblast growth factor receptor 2	Homo sapiens	131-136
11427199-0	2001	Effects of the heparin-mimicking compound RG-13577 on lipoprotein lipase and on lipase mediated binding of LDL to cells.	Heparin	15-22	lipoprotein lipase	Homo sapiens	54-72
9393979-6	1997	Upon addition of heparin, mFGF-10 protein was released into the media.	Heparin	17-24	fibroblast growth factor 10	Mus musculus	26-33
9329435-0	1997	Acquired inhibitors to factors V and X after exposure to topical thrombin: interference with monitoring of low molecular weight heparin and warfarin.	Heparin	128-135	coagulation factor II, thrombin	Bos taurus	65-73
11427199-1	2001	Lipoprotein lipase (LPL) has high affinity for heparin and heparin-like compounds.	Heparin	47-54	lipoprotein lipase	Homo sapiens	0-18
11427199-1	2001	Lipoprotein lipase (LPL) has high affinity for heparin and heparin-like compounds.	Heparin	47-54	lipoprotein lipase	Homo sapiens	20-23
9276466-3	1997	Recombinant HRG bound heparin and fibrinogen while alpha2-HS did not.	Heparin	22-29	histidine rich glycoprotein	Homo sapiens	12-15
11441984-12	2001	Furthermore, the release of TFPI by heparin is mediated by non-antithrombin III binding fragments.	Heparin	36-43	serpin family C member 1	Homo sapiens	63-79
11468002-13	2001	Heparin dose-dependently inhibited histamine release induced by sera and plasma, and by basophil agonists such as anti-IgE, formyl-methionyl-leucyl-phenilalanine, and interleukin (IL)-3.	Heparin	0-7	interleukin 3	Homo sapiens	167-185
9200390-4	1997	The 30-day mortality rate with accelerated TPA was 0.063 versus 0.073 with streptokinase and subcutaneously administered heparin and 0.074 with streptokinase and intravenously administered heparin.	Heparin	121-128	chromosome 20 open reading frame 181	Homo sapiens	43-46
9153200-0	1997	Zinc as a cofactor for heparin neutralization by histidine-rich glycoprotein.	Heparin	23-30	histidine rich glycoprotein	Homo sapiens	49-76
11382921-0	2001	COP-1, a member of the CCN family, is a heparin-induced growth arrest specific gene in vascular smooth muscle cells.	Heparin	40-47	COP1, E3 ubiquitin ligase	Rattus norvegicus	0-5
9153200-1	1997	We have studied the ability of histidine-rich glycoprotein (HRG) to neutralize the anticoagulant activity of heparin in plasma and in a purified component clotting assay.	Heparin	109-116	histidine rich glycoprotein	Homo sapiens	31-58
9153200-1	1997	We have studied the ability of histidine-rich glycoprotein (HRG) to neutralize the anticoagulant activity of heparin in plasma and in a purified component clotting assay.	Heparin	109-116	histidine rich glycoprotein	Homo sapiens	60-63
9153200-4	1997	Zinc concentrations as low as 1.25 microM revealed HRG to be a powerful competitor of antithrombin for heparin in the purified component assays.	Heparin	103-110	histidine rich glycoprotein	Homo sapiens	51-54
9153200-5	1997	HRG binding of heparin also was shown by affinity chromatography of HRG from immobilized heparin in the presence and absence of zinc.	Heparin	15-22	histidine rich glycoprotein	Homo sapiens	0-3
9153200-5	1997	HRG binding of heparin also was shown by affinity chromatography of HRG from immobilized heparin in the presence and absence of zinc.	Heparin	15-22	histidine rich glycoprotein	Homo sapiens	68-71
9153200-5	1997	HRG binding of heparin also was shown by affinity chromatography of HRG from immobilized heparin in the presence and absence of zinc.	Heparin	89-96	histidine rich glycoprotein	Homo sapiens	0-3
9153200-5	1997	HRG binding of heparin also was shown by affinity chromatography of HRG from immobilized heparin in the presence and absence of zinc.	Heparin	89-96	histidine rich glycoprotein	Homo sapiens	68-71
9153200-7	1997	Investigation of other divalent cations (copper and magnesium) indicated that augmentation of heparin binding by HRG in the presence of antithrombin was restricted to zinc.	Heparin	94-101	histidine rich glycoprotein	Homo sapiens	113-116
11382921-8	2001	Cop-1 mRNA is expressed at high levels in heparin treated VSMC and COP-1 protein is secreted into culture medium.	Heparin	42-49	COP1, E3 ubiquitin ligase	Rattus norvegicus	0-5
11274177-0	2001	Characterization of the D-glucuronyl C5-epimerase involved in the biosynthesis of heparin and heparan sulfate.	Heparin	82-89	glucuronyl C5-epimerase	Mus musculus	24-49
9144519-7	1997	VEGF and bFGF in AIDS-KS-CM were distinguished by heparin-affinity chromatography.	Heparin	50-57	vascular endothelial growth factor A	Oryctolagus cuniculus	0-4
9187023-2	1997	Heparin augments the inhibitory activity of antithrombin (AT) towards thrombin, factor Xa (FXa) and other activated clotting enzymes.	Heparin	0-7	coagulation factor X	Homo sapiens	80-89
9187023-2	1997	Heparin augments the inhibitory activity of antithrombin (AT) towards thrombin, factor Xa (FXa) and other activated clotting enzymes.	Heparin	0-7	coagulation factor X	Homo sapiens	91-94
9187023-3	1997	Tissue factor pathway inhibitor (TFPI) is an endogenous heparin releasable three domain Kunitz-type coagulation inhibitor which inhibits the crucial tissue factor-factor VIIa (TF-FVIIa) dependent coagulation pathway in the presence of FXa.	Heparin	56-63	coagulation factor X	Homo sapiens	235-238
9111037-0	1997	Interaction of HIV-1 Tat protein with heparin.	Heparin	38-45	Tat	Human immunodeficiency virus 1	21-24
11434690-6	2001	The formation of leukocyte-platelet-aggregates induced by HIT plasma in the presence of heparin was (i) independent of the healthy blood donor FcgammaRIIa polymorphism, (ii) correlated with the levels of anti H-PF4 IgG antibodies contained in the patients" plasma, and to a lesser extent to anti H-PF4 IgM antibodies, and (iii) was mediated by P-selectin.	Heparin	88-95	selectin P	Homo sapiens	344-354
9111037-6	1997	Here we demonstrate that heparin binds specifically to recombinant HIV-1 Tat produced as glutathione S-transferase (GST) fusion protein and immobilized on glutathione-agarose beads.	Heparin	25-32	Tat	Human immunodeficiency virus 1	73-76
9111037-7	1997	Heparin and heparan sulfate (HS), but not dermatan sulfate, chondroitin sulfates A and C, hyaluronic acid, and K5 polysaccharide, competed with 3H-labeled heparin for binding to immobilized GST-Tat and inhibited HIV-LTR transactivation induced by extracellular GST-Tat.	Heparin	0-7	Tat	Human immunodeficiency virus 1	265-268
11342462-0	2001	Induction of monocyte tissue factor expression by antibodies to heparin-platelet factor 4 complexes developed in heparin-induced thrombocytopenia.	Heparin	64-71	coagulation factor III, tissue factor	Homo sapiens	22-35
9092537-5	1997	While heparin forms complexes with monomeric plasma Vn and induces conformational changes, a reduction in ionic strength is required for induction of multimerization.	Heparin	6-13	vitronectin	Homo sapiens	52-54
9092537-6	1997	In addition, heparin serves as a template for the assembly of type 1 plasminogen activator inhibitor-induced disulfide-linked Vn multimers.	Heparin	13-20	vitronectin	Homo sapiens	126-128
9120000-7	1997	Moreover, it abrogated heparin-mediated dimerization of FGF-2 and FGFR1, as well as FGF-2 mitogenic activity in HS-deficient F32 lymphoid cells.	Heparin	23-30	Fibroblast growth factor receptor 1	Rattus norvegicus	66-71
11278930-0	2001	Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence.	Heparin	0-7	serpin family C member 1	Homo sapiens	36-48
11278930-2	2001	Heparin activates the primary serpin inhibitor of blood clotting proteinases, antithrombin, both by an allosteric conformational change mechanism that specifically enhances factor Xa inactivation and by a ternary complex bridging mechanism that promotes the inactivation of thrombin and other target proteinases.	Heparin	0-7	serpin family C member 1	Homo sapiens	78-90
9027362-4	1997	By Western blotting with an antiserum to human amphiregulin, two molecular weight forms, 27 and 51 kDa were detected in sheep mammary gland microsomal preparations, in a mammary gland extract after heparin affinity chromatography and in a medium conditioned by mammary epithelial cells.	Heparin	198-205	amphiregulin	Homo sapiens	47-59
11358513-7	2001	Heparin, but not other glycosaminoglycans, enhanced dramatically the ability of hK3 but not hK2 to degrade IGFBP-3 and IGFBP-4.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	107-114
8939794-7	1997	Preincubating cells with sulfated polymers such as dextran sulfate (Mr 5000 and 8000), pentosan sulfate and heparin decreased binding of vitronectin, lactoferrin, and thrombospondin.	Heparin	108-115	vitronectin	Homo sapiens	137-148
11342582-2	2001	To test these hypotheses in vivo, we created mice expressing a human LpL minigene (hLpL(HBM)) carrying a mutated heparin-binding site.	Heparin	113-120	lipoprotein lipase	Homo sapiens	83-87
9028720-5	1997	We also observed that protamine effects on chemotaxis, proliferation and c-fos expression are inhibited by heparin that human insulin stimulates cell proliferation and 3H-thymidine incorporation (ANOVA, p &lt; 0.0001) at concentrations equal to or greater than 480 pmol/l and that these effects of insulin persist in the presence of protamine.	Heparin	107-114	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	73-78
11342582-5	2001	hLpL(HBM) rapidly lost activity during a 37 degrees C incubation, confirming a requirement for heparin binding to stabilize LPL: Nevertheless, expression of hLpL(HBM) prevented the neonatal demise of LpL knockout mice.	Heparin	95-102	lipoprotein lipase	Homo sapiens	0-4
11342582-5	2001	hLpL(HBM) rapidly lost activity during a 37 degrees C incubation, confirming a requirement for heparin binding to stabilize LPL: Nevertheless, expression of hLpL(HBM) prevented the neonatal demise of LpL knockout mice.	Heparin	95-102	lipoprotein lipase	Homo sapiens	124-127
11342582-5	2001	hLpL(HBM) rapidly lost activity during a 37 degrees C incubation, confirming a requirement for heparin binding to stabilize LPL: Nevertheless, expression of hLpL(HBM) prevented the neonatal demise of LpL knockout mice.	Heparin	95-102	lipoprotein lipase	Homo sapiens	157-161
9297604-3	1997	Comparison of kallikrein-like activity on glass using citrate or heparinized plasma demonstrated enhanced activity in the presence of heparin.	Heparin	65-72	kallikrein related peptidase 4	Homo sapiens	14-24
11342582-5	2001	hLpL(HBM) rapidly lost activity during a 37 degrees C incubation, confirming a requirement for heparin binding to stabilize LPL: Nevertheless, expression of hLpL(HBM) prevented the neonatal demise of LpL knockout mice.	Heparin	95-102	lipoprotein lipase	Homo sapiens	1-4
11559998-5	2001	Administration of a standard heparin is accompanied by exhaustion of the antithrombin activity of the blood and depression of fibrinolysis, which event comes to be especially dangerous in the arterial vessels.	Heparin	29-36	serpin family C member 1	Homo sapiens	73-85
9013915-12	1997	Clinical trials are warranted to assess whether GP IIb/IIIa antagonists may allow patients with HAAb to safely receive heparin.	Heparin	119-126	integrin subunit alpha 2b	Homo sapiens	48-54
9469634-5	1997	Trp49-modified AT III, which lacks affinity for heparin, did not prevent LPS-induced pulmonary vascular injury.	Heparin	48-55	serpin family C member 1	Rattus norvegicus	15-21
8824227-0	1996	Protein kinase C alpha expression is required for heparin inhibition of rat smooth muscle cell proliferation in vitro and in vivo.	Heparin	50-57	protein kinase C, alpha	Rattus norvegicus	0-22
8824227-3	1996	The membrane-associated intracellular PKC activity increased following stimulation of cultured rat SMCs with fetal calf serum and was suppressed by heparin in a time- and dose-dependent manner.	Heparin	148-155	protein kinase C, alpha	Rattus norvegicus	38-41
8824227-4	1996	Heparin acted through a selective inhibition of the PKC-alpha since preincubation of the cells with a 20-mer phosphorothioate PKC-alpha antisense oligodeoxynucleotide (ODN) eliminated the heparin effect.	Heparin	0-7	protein kinase C, alpha	Rattus norvegicus	52-61
8824227-4	1996	Heparin acted through a selective inhibition of the PKC-alpha since preincubation of the cells with a 20-mer phosphorothioate PKC-alpha antisense oligodeoxynucleotide (ODN) eliminated the heparin effect.	Heparin	0-7	protein kinase C, alpha	Rattus norvegicus	126-135
8808643-5	1996	The Kd of monoclonal IgG2b autoantibodies for heparin was approximately 10(-8)M. Anti-heparin antibodies were precipitating, and were not polyreactive.	Heparin	46-53	immunoglobulin heavy constant gamma 2B	Mus musculus	21-26
8915999-3	1996	The alignment revealed that the functional amino acid sequences reported as the cell attachment site, the heparin binding site, the region involved in glycosylation, and plasminogen activator inhibitor I-binding domain were conserved in the porcine putative Vn.	Heparin	106-113	vitronectin	Homo sapiens	258-260
10102493-9	1998	The appearance of thrombin in the injured vessel wall can also be inhibited by heparin treatment, but this requires heparin to be circulating in plasma at the time of excision of the injured vessel wall.	Heparin	79-86	prothrombin	Oryctolagus cuniculus	18-26
10102493-9	1998	The appearance of thrombin in the injured vessel wall can also be inhibited by heparin treatment, but this requires heparin to be circulating in plasma at the time of excision of the injured vessel wall.	Heparin	116-123	prothrombin	Oryctolagus cuniculus	18-26
10102493-11	1998	This effect of thrombin can be inhibited by AT, an inhibition that is increased by heparin in a concentration-dependent manner.	Heparin	83-90	prothrombin	Oryctolagus cuniculus	15-23
9843181-1	1998	The activation of rabbit platelets by rabbit plasma clots, and the inhibition of clot-associated thrombin by heparin:antithrombin III, recombinant hirudin (rHV2Lys47) and argatroban, a low molecular weight thrombin inhibitor, was studied.	Heparin	109-116	prothrombin	Oryctolagus cuniculus	97-105
9843181-5	1998	Heparin was less active against clot-associated thrombin (IC50) = 69 +/- 9 mU/ml) than against thrombin in solution (IC50 = 15 +/- 5 mU/ml).	Heparin	0-7	prothrombin	Oryctolagus cuniculus	48-56
8798437-9	1996	In this study, we isolated a novel growth-promoting component, chondromodulin II, which has a lower heparin affinity, from the dissociative extracts of fetal bovine epiphyseal cartilage.	Heparin	100-107	leukocyte cell derived chemotaxin 2	Bos taurus	63-80
11278631-0	2001	A novel anti-angiogenic form of antithrombin with retained proteinase binding ability and heparin affinity.	Heparin	90-97	serpin family C member 1	Homo sapiens	32-44
9014007-0	1996	Influence of glycoproteins B, C and D on the conversion of virus-to-cell attachment from heparin sensitivity to resistance.	Heparin	89-96	atypical chemokine receptor 1 (Duffy blood group)	Homo sapiens	13-37
9801974-6	1998	In the same patients, the effect of heparin, 1 to 5 IU/mL, on the HMT was assessed in vitro.	Heparin	36-43	histamine N-methyltransferase	Homo sapiens	66-69
9798991-12	1998	These results indicated that addition of this novel thrombin (and kallikrein) inhibitor to heparin preserved platelet counts, decreased platelet secretion, and provided the additional benefit of partially blocking neutrophil activation during simulated extracorporeal circulation.	Heparin	91-98	kallikrein related peptidase 4	Homo sapiens	66-76
8810636-9	1996	Acidic fibroblast growth factor, which also binds KGF receptors, in the presence of heparin mimicked the effect of KGF on branching.	Heparin	84-91	fibroblast growth factor 1	Rattus norvegicus	0-31
11294809-4	2001	Injection of this virus produced a high level of Ec-SOD in the liver, which was redistributed to the heart and other organs by injection of heparin.	Heparin	140-147	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	49-55
8810636-9	1996	Acidic fibroblast growth factor, which also binds KGF receptors, in the presence of heparin mimicked the effect of KGF on branching.	Heparin	84-91	fibroblast growth factor 7	Rattus norvegicus	50-53
8810636-9	1996	Acidic fibroblast growth factor, which also binds KGF receptors, in the presence of heparin mimicked the effect of KGF on branching.	Heparin	84-91	fibroblast growth factor 7	Rattus norvegicus	115-118
8695803-5	1996	The high M(r) fractions contain conformationally and structurally altered Vn capable of interacting with heparin, and this form is distinct from plasma Vn and purified denatured Vn.	Heparin	105-112	vitronectin	Homo sapiens	74-76
8695803-9	1996	Thus, platelet Vn is stored in a structurally and functionally distinct form from the molecule in plasma, raising the possibility that platelet-derived heparin-binding competent Vn will accumulate in areas of vascular injury.	Heparin	152-159	vitronectin	Homo sapiens	15-17
9739164-19	1998	Degradation of both forms of vitronectin was inhibited with arginine-glycine-aspartic acid peptides, an anti-alphavbeta5 antibody and heparin.	Heparin	134-141	vitronectin	Homo sapiens	29-40
11287128-0	2001	Antithrombin binding of low molecular weight heparins and inhibition of factor Xa.	Heparin	45-53	serpin family C member 1	Homo sapiens	0-12
9755834-6	1998	Differences between danaparoid and heparin were observed in their effects on the plasma AT-III level and clotting time.	Heparin	35-42	serpin family C member 1	Rattus norvegicus	88-94
9716161-4	1998	These effects which occurred in a time-dependent manner were significant in the first 1-2 h of incubation and reached a maximum after 6 to 9 h. The GP IIb-1IIa receptor antagonist SR121566A which has been shown to block platelet aggregation induced by a wide variety of agonists including HIT serum/heparin, reduced in a dose-dependent manner the HIT serum/heparin-induced, platelet mediated expression and release of the above mentioned proteins.	Heparin	299-306	integrin subunit alpha 2b	Homo sapiens	148-154
9716161-4	1998	These effects which occurred in a time-dependent manner were significant in the first 1-2 h of incubation and reached a maximum after 6 to 9 h. The GP IIb-1IIa receptor antagonist SR121566A which has been shown to block platelet aggregation induced by a wide variety of agonists including HIT serum/heparin, reduced in a dose-dependent manner the HIT serum/heparin-induced, platelet mediated expression and release of the above mentioned proteins.	Heparin	357-364	integrin subunit alpha 2b	Homo sapiens	148-154
9642241-2	1998	It is believed that heparin accelerates factor Xa (FXa) inactivation by antithrombin (AT) by conformationally activating the inhibitor rather than by bridging AT and FXa in a ternary complex (template effect).	Heparin	20-27	coagulation factor X	Homo sapiens	51-54
8695803-9	1996	Thus, platelet Vn is stored in a structurally and functionally distinct form from the molecule in plasma, raising the possibility that platelet-derived heparin-binding competent Vn will accumulate in areas of vascular injury.	Heparin	152-159	vitronectin	Homo sapiens	178-180
8837315-4	1996	After the rapid disappearance of the h-rTFPI complex from plasma, an intravenous injection of heparin resulted in a release of h-rTFPI/factor Xa complex into plasma.	Heparin	94-101	coagulation factor X	Homo sapiens	135-144
8837315-5	1996	However, the recovery of heparin-releasable h-rTFPI/factor Xa decreased significantly in a time-dependent manner.	Heparin	25-32	coagulation factor X	Homo sapiens	52-61
8693000-5	1996	Here, the binding of four recombinant agrin isoforms to heparin, to alpha-dystroglycan (a component of an agrin receptor), and to myoblasts was tested.	Heparin	56-63	agrin	Homo sapiens	38-43
8693000-6	1996	The presence of a four-amino acid insert at the y site is necessary and sufficient to confer heparin binding ability to agrin.	Heparin	93-100	agrin	Homo sapiens	120-125
8693000-7	1996	Moreover, the binding of agrin to alpha-dystroglycan is inhibited by heparin when this insert is present.	Heparin	69-76	agrin	Homo sapiens	25-30
8693000-8	1996	Agrin binding to the cell surface showed analogous properties: heparin inhibits the binding of only those agrin isoforms containing this four-amino acid insert.	Heparin	63-70	agrin	Homo sapiens	0-5
8693000-8	1996	Agrin binding to the cell surface showed analogous properties: heparin inhibits the binding of only those agrin isoforms containing this four-amino acid insert.	Heparin	63-70	agrin	Homo sapiens	106-111
8693000-9	1996	The results show that alternative splicing of agrin regulates its binding to heparin and suggest that agrin"s interaction with alpha-dystroglycan may be modulated by cell surface glycosaminoglycans in an isoform-dependent manner.	Heparin	77-84	agrin	Homo sapiens	46-51
8679610-2	1996	A heparin-induced conformational change is required to convert antithrombin from a slow to a fast inhibitor of factor Xa.	Heparin	2-9	coagulation factor X	Homo sapiens	111-120
8679610-7	1996	1, 423-425] that the reactive center residue P14 is inserted into beta-sheet A in native antithrombin and is displaced from the beta-sheet by heparin binding, thereby altering the conformation of the reactive center and making it a better target for factor Xa binding.	Heparin	142-149	ribonuclease P/MRP subunit p14	Homo sapiens	45-48
8679610-7	1996	1, 423-425] that the reactive center residue P14 is inserted into beta-sheet A in native antithrombin and is displaced from the beta-sheet by heparin binding, thereby altering the conformation of the reactive center and making it a better target for factor Xa binding.	Heparin	142-149	coagulation factor X	Homo sapiens	250-259
9642241-4	1998	To test the possibility that the anionic Gla domain of FXa, when not neutralized by Ca2+ ions, prevents heparin binding to FXa, the heparin and pentasaccharide dependence of FXa inactivation by AT in both the absence (100 microM EDTA) and presence of Ca2+ (2.5 mM) was studied using wild-type FXa and a FXa derivative that lacks the Gla domain (GDFXa).	Heparin	104-111	coagulation factor X	Homo sapiens	55-58
9642241-4	1998	To test the possibility that the anionic Gla domain of FXa, when not neutralized by Ca2+ ions, prevents heparin binding to FXa, the heparin and pentasaccharide dependence of FXa inactivation by AT in both the absence (100 microM EDTA) and presence of Ca2+ (2.5 mM) was studied using wild-type FXa and a FXa derivative that lacks the Gla domain (GDFXa).	Heparin	132-139	coagulation factor X	Homo sapiens	55-58
9700855-11	1998	Heparin inhibition of platelet PT activity was additive to that of c7E3 Fab.	Heparin	0-7	coagulation factor X	Homo sapiens	31-33
11287128-1	2001	Fluorescence and stopped flow methods were used to compare clinically used heparins with regard to their ability to bind to antithrombin and to accelerate the inactivation of factor Xa.	Heparin	75-83	serpin family C member 1	Homo sapiens	124-136
9655588-7	1998	These angiogenic factors bind heparin and seem to belong to the fibroblast growth factor (FGF) and vascular endothelial growth factor (VEGF) families of proteins.	Heparin	30-37	vascular endothelial growth factor A	Bos taurus	99-133
9655588-7	1998	These angiogenic factors bind heparin and seem to belong to the fibroblast growth factor (FGF) and vascular endothelial growth factor (VEGF) families of proteins.	Heparin	30-37	vascular endothelial growth factor A	Bos taurus	135-139
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	57-64	serpin family C member 1	Homo sapiens	13-25
8840224-4	1996	Soluble heparin and heparan sulfate inhibited both C3a and TCC formation, but surface-conjugated heparin had only a minor effect.	Heparin	8-15	complement C3	Homo sapiens	51-54
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	57-64	serpin family C member 1	Homo sapiens	248-260
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	127-134	serpin family C member 1	Homo sapiens	13-25
9694594-0	1998	Identification and characterization of a heparin binding site within the NC1 domain of chicken collagen XIV.	Heparin	41-48	collagen type XIV alpha 1 chain	Gallus gallus	95-107
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	127-134	serpin family C member 1	Homo sapiens	248-260
8670795-5	1996	Analysis of the primary structural features further characterized neuroserpin as a heparin-independent, functional inhibitor of a trypsin-like serine protease.	Heparin	83-90	serpin family I member 1	Gallus gallus	66-77
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	136-139	serpin family C member 1	Homo sapiens	13-25
8840000-2	1996	Previous studies have shown that heparin binds to TFPI at two sites and enhances the inhibitory activity of TFPI towards factor Xa.	Heparin	33-40	coagulation factor X	Homo sapiens	121-130
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	136-139	serpin family C member 1	Homo sapiens	248-260
8840000-6	1996	Heparin enhanced the inhibitory activity of TFPI towards factor Xa even in the presence of factor VIIa-tissue factor complexes in solution phase.	Heparin	0-7	coagulation factor X	Homo sapiens	57-66
9553135-9	1998	As the zeta2 fragment lacks the fibrinogen recognition site, the P1-P3 residues or the intact cleavage site, specific recognition of the macromolecular substrate by the exosite in prothrombinase is achieved through substrate regions, distinct from the fibrinogen recognition or heparin-binding sites, and spatially removed from structures surrounding the scissile bond.	Heparin	278-285	coagulation factor X	Homo sapiens	180-194
9602028-5	1998	Throughout the brain, there was also substantial non-parenchymal labelling of [125I]-glial cell line-derived neurotrophic factor, possibly associated with extracellular matrix components, meninges and vasculature due to the heparin binding properties of glial cell line-derived neurotrophic factor.	Heparin	224-231	glial cell derived neurotrophic factor	Macaca mulatta	85-128
8690451-4	1996	In contrast to previous studies, HRG binding was largely inhibited by 50 micrograms/ml heparin, both in the absence and in the presence of zinc, suggesting that HRG interacts primarily through glycosaminoglycans on the T-cell surface.	Heparin	87-94	histidine rich glycoprotein	Homo sapiens	33-36
8690451-4	1996	In contrast to previous studies, HRG binding was largely inhibited by 50 micrograms/ml heparin, both in the absence and in the presence of zinc, suggesting that HRG interacts primarily through glycosaminoglycans on the T-cell surface.	Heparin	87-94	histidine rich glycoprotein	Homo sapiens	161-164
8690466-0	1996	Stem cell factor-dependent human cord blood derived mast cells express alpha- and beta-tryptase, heparin and chondroitin sulphate.	Heparin	97-104	KIT ligand	Homo sapiens	0-16
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	127-134	serpin family C member 1	Homo sapiens	13-25
11287128-2	2001	Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin.	Heparin	127-134	serpin family C member 1	Homo sapiens	248-260
8795010-0	1996	Heparin-binding capacity of the HIV-1 NEF-protein allows one-step purification and biochemical characterization.	Heparin	0-7	Nef	Human immunodeficiency virus 1	38-41
8795010-1	1996	Recombinant Nef-protein of HIV-1 Bru derived from Escherichia coli revealed heparin-binding activity.	Heparin	76-83	Nef	Human immunodeficiency virus 1	12-15
9531294-9	1998	Finally, the interaction between rFHL-1 and purified M5 protein was inhibited by heparin, which binds FH via SCR 7.	Heparin	81-88	four and a half LIM domains 1	Rattus norvegicus	33-39
11287128-4	2001	The rate of factor Xa inhibition by antithrombin increased with the concentration of the examined heparins to the same limiting value, but the concentration required for maximal acceleration depended on the preparation.	Heparin	98-106	serpin family C member 1	Homo sapiens	36-48
9494108-1	1998	Heparin tightly binds cathepsin G and so protects the enzyme from inhibition by alpha1-antichymotrypsin, alpha1-proteinase inhibitor and eglin c, three proteins which do not bind heparin [Ermolieff J., Boudier C., Laine A., Meyer B. and Bieth J.G.	Heparin	0-7	serpin family A member 3	Homo sapiens	80-103
11287128-6	2001	In contrast, in the presence of Ca UFH accelerated the inhibition of factor Xa by antithrombin 10-fold more efficiently than comparable concentrations of the high affinity fractions of enoxaparin and fragmin.	Heparin	35-38	serpin family C member 1	Homo sapiens	82-94
9497380-5	1998	Heparin partially inhibited receptor aggregation induced by both agrin and anti-muscle-specific kinase antibodies.	Heparin	0-7	agrin	Homo sapiens	65-70
11287128-8	2001	In conclusion, under physiologic conditions the anti-factor Xa activity of heparin results from a composite effect of chain length and the content of material with high affinity to antithrombin.	Heparin	75-82	serpin family C member 1	Homo sapiens	181-193
9669748-5	1998	In vitro experiments on the inhibition of factor Xa by TFPI enhanced with native and chemically modified heparins afforded similar results.	Heparin	105-113	coagulation factor X	Homo sapiens	42-51
8626663-8	1996	Functional characterization of the calpain-hydrolyzed Vn revealed that while the type 1 plasminogen activator inhibitor binding activity was unchanged, the heparin and cell binding functions were destroyed.	Heparin	156-163	vitronectin	Homo sapiens	54-56
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	158-165	serpin family C member 1	Homo sapiens	118-130
8732755-12	1996	Two heparin binding sites are suggested on the PSA surface and could explain the enhanced complex formation between PSA and PCI, while inhibiting the formation of the ACT-PSA complex, PSA, hK2, and their preliminary complexes with ACT should facilitate the understanding and prediction of structural and functional properties for these important proteins also with respect to prostate diseases.	Heparin	4-11	RBPJ pseudogene 3	Homo sapiens	189-192
9622211-0	1998	Tissue factor pathway inhibitor and anti-FXa kinetic profiles of a new low-molecular-mass heparin, Bemiparin, at therapeutic subcutaneous doses.	Heparin	90-97	coagulation factor X	Homo sapiens	41-44
9622211-1	1998	Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins.	Heparin	19-27	coagulation factor X	Homo sapiens	50-53
11254909-1	2001	As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF).	Heparin	158-165	selectin P	Homo sapiens	219-229
11106649-4	2001	Heparin nonbinding sPLA(2)-X liberates arachidonic acid most likely from the phosphatidylcholine-rich outer plasma membrane in a glypican-independent manner.	Heparin	0-7	phospholipase A2, group X	Rattus norvegicus	19-28
8793597-3	1996	Indicators of inflammation (i.e. cytokine levels, elastase and complement components) are decreased when using heparin bonded circuits compared to conventional bypass circuits.	Heparin	111-118	TNF receptor superfamily member 8	Homo sapiens	33-41
11171125-6	2001	Furthermore, we demonstrate that the alteration of acidic amino acid residues in MIP-1alpha influences the affinity of its interactions with heparin as these residues are progressively neutralized, leading to an enhanced binding affinity for heparin.	Heparin	141-148	C-C motif chemokine ligand 3	Homo sapiens	81-91
8651503-4	1996	The biological activity of the immobilized heparin (or hydrolyzed heparin) was measured in terms of its inactivation of blood coagulation factor Xa.	Heparin	43-50	coagulation factor X	Homo sapiens	138-147
8651503-4	1996	The biological activity of the immobilized heparin (or hydrolyzed heparin) was measured in terms of its inactivation of blood coagulation factor Xa.	Heparin	66-73	coagulation factor X	Homo sapiens	138-147
8651503-5	1996	It was found that the covalently anchored hydrolyzed heparin was not biologically active, but the immobilized heparin was able to inactivate factor Xa.	Heparin	110-117	coagulation factor X	Homo sapiens	141-150
9492085-7	1998	125I labeled Tg bound to megalin was released by EDTA and heparin; the released product was shown by SDS-PAGE and autoradiography to be 660 kD (dimeric) Tg.	Heparin	58-65	LDL receptor related protein 2	Rattus norvegicus	25-32
9543101-4	1998	Mac-1 (CD11b/CD18), a monocytic counter-receptor for intercellular adhesion molecule-1 (ICAM-1), that also binds to heparin, is present on Mono Mac 6 but not on U937 cells, and may thus explain these differences in adhesion.	Heparin	116-123	integrin subunit alpha M	Homo sapiens	0-5
9543101-4	1998	Mac-1 (CD11b/CD18), a monocytic counter-receptor for intercellular adhesion molecule-1 (ICAM-1), that also binds to heparin, is present on Mono Mac 6 but not on U937 cells, and may thus explain these differences in adhesion.	Heparin	116-123	integrin subunit alpha M	Homo sapiens	7-12
9543101-4	1998	Mac-1 (CD11b/CD18), a monocytic counter-receptor for intercellular adhesion molecule-1 (ICAM-1), that also binds to heparin, is present on Mono Mac 6 but not on U937 cells, and may thus explain these differences in adhesion.	Heparin	116-123	intercellular adhesion molecule 1	Homo sapiens	88-94
9458769-4	1998	Because a cell surface heparin-like substance can bind to HGF and protamine has an affinity for heparin, protamine may affect HGF pharmacokinetics.	Heparin	23-30	hepatocyte growth factor	Rattus norvegicus	58-61
9458769-4	1998	Because a cell surface heparin-like substance can bind to HGF and protamine has an affinity for heparin, protamine may affect HGF pharmacokinetics.	Heparin	23-30	hepatocyte growth factor	Rattus norvegicus	126-129
17177827-3	1996	After 60 minutes of ischemia and at the onset of reperfusion, rats in the acidic fibroblast growth factor-treated group received 2.6 microg of acidic fibroblast growth factor/rat in 50 microl of phosphate-buffered saline solution containing 0.1% heparin (w/v) through the jugular vein, whereas the rats in the phosphate-buffered saline solution-treated group received the same vehicle without acidic fibroblast growth factor.	Heparin	246-253	fibroblast growth factor 1	Rattus norvegicus	74-105
8621410-8	1996	These results contrast with previous observations which have indicated that the binding of 125I-VEGF165 to the flk-1 receptor is strongly dependent on heparin-like molecules.	Heparin	151-158	kinase insert domain receptor	Homo sapiens	111-116
8621410-11	1996	Heparin or cell surface heparan sulfates restored the flk-1 binding ability of damaged VEGF165 but not the receptor binding ability of damaged VEGF121.	Heparin	0-7	kinase insert domain receptor	Homo sapiens	54-59
9763204-7	1998	We found the presence of TGFbeta2, but not TGFbeta1, in the heparin bound fraction, and the inhibitory effect was detected in the heparin-bound fraction.	Heparin	60-67	transforming growth factor beta 2	Homo sapiens	25-33
11171125-6	2001	Furthermore, we demonstrate that the alteration of acidic amino acid residues in MIP-1alpha influences the affinity of its interactions with heparin as these residues are progressively neutralized, leading to an enhanced binding affinity for heparin.	Heparin	242-249	C-C motif chemokine ligand 3	Homo sapiens	81-91
11241131-5	2001	The translocation to the cytoskeleton of Rap2, a guanosine triphosphate-binding protein, was measured from platelets aggregating in response to heparin and other agonists.	Heparin	144-151	RAP2A, member of RAS oncogene family	Homo sapiens	41-45
9927235-2	1998	Metabolic acidosis due to addition of hydrochloric acid (10 micromol/ml blood) or lactic acid (5.5 micromol/ml) to heparin blood (N=12) caused significant activation of C3a and C5a compared to control (both p=0.002).	Heparin	115-122	complement C3	Homo sapiens	169-172
8634431-3	1996	When factor Xa is added to mixtures containing TFPI, prothrombin, calcium ions, and nonactivated platelets or factor V and phospholipids, TFPI significantly reduces subsequent thrombin generation, and the inhibitory effect is enhanced by heparin.	Heparin	238-245	coagulation factor X	Homo sapiens	5-14
8634431-4	1996	If factor Xa is preincubated with calcium ions and thrombin-activated platelets or factor Va and phospholipids to permit formation of prothrombinase before the addition of prothrombin and physiologic concentrations of TFPI (&lt; 8 nmol/L), minimal inhibition of thrombin generation occurs, even in the presence of heparin.	Heparin	314-321	coagulation factor X	Homo sapiens	3-12
11241131-12	2001	Heparin-mediated aggregation requires an intact integrin and ligand and leads to Rap2 translocation to the cytoskeleton-an outside-in signal of ligand engagement.	Heparin	0-7	RAP2A, member of RAS oncogene family	Homo sapiens	81-85
9369950-0	1997	Heparin suppresses sgk, an early response gene in proliferating vascular smooth muscle cells.	Heparin	0-7	serum/glucocorticoid regulated kinase 1	Homo sapiens	19-22
9369950-5	1997	Here we demonstrate that heparin inhibits the expression of the early response gene sgk (serum and glucocorticoid-regulated kinase).	Heparin	25-32	serum/glucocorticoid regulated kinase 1	Homo sapiens	84-87
8882470-1	1996	Elastin expression in cultured vascular smooth muscle cell (VSMC) was found to be enhanced by potent inhibitors of VSMC proliferation including minoxidil, heparin and retinoic acid.	Heparin	155-162	elastin	Homo sapiens	0-7
9369950-6	1997	The expression of sgk is not inhibited by chondroitin sulfate, a nonantiproliferative glycosaminoglycan, suggesting that sgk suppression may play a functional role in the antiproliferative effect of heparin.	Heparin	199-206	serum/glucocorticoid regulated kinase 1	Homo sapiens	18-21
11067857-5	2001	Interestingly, a mutant annexin II lacking its C-terminal 16, 13, or 9 amino acids was unable to bind to F-actin but still retained its ability to interact with both anionic phospholipids and heparin.	Heparin	192-199	annexin A2	Homo sapiens	24-34
9369950-6	1997	The expression of sgk is not inhibited by chondroitin sulfate, a nonantiproliferative glycosaminoglycan, suggesting that sgk suppression may play a functional role in the antiproliferative effect of heparin.	Heparin	199-206	serum/glucocorticoid regulated kinase 1	Homo sapiens	121-124
9369950-8	1997	Expression of sgk mRNA diminishes with increasing concentrations of heparin.	Heparin	68-75	serum/glucocorticoid regulated kinase 1	Homo sapiens	14-17
9359845-0	1997	N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA.	Heparin	94-101	arginase 2	Homo sapiens	19-23
9359845-4	1997	Natural hLF lacking the first two N-terminal amino acids (Gly1-Arg2) showed reactivities of one-half, two-thirds, one-third and one-third towards heparin, lipid A, hLZ and DNA respectively compared with N-terminally intact hLF.	Heparin	146-153	arginase 2	Homo sapiens	63-67
9359845-8	1997	These results show that the N-terminal stretch of four consecutive arginine residues, Arg2-Arg3-Arg4-Arg5, has a decisive role in the interaction of hLF with heparin, lipid A, hLZ and DNA.	Heparin	158-165	arginase 2	Homo sapiens	86-90
8622662-5	1996	The sca protein contained both N- and O-linked carbohydrates and interacted with heparin.	Heparin	81-88	scabrous	Drosophila melanogaster	4-7
8907299-4	1996	Heparins exert their anticoagulant effect by enhancing ATIII inhibitory action on factor Xa and thrombin, which results in decreased factor X activation, prothrombinase formation, prothrombin activation and thrombin generation.	Heparin	0-8	coagulation factor X	Homo sapiens	82-91
11087737-4	2001	However, the rate of inhibition by antithrombin III in the presence of submaximal concentrations of heparin is reduced for all the enzymes.	Heparin	100-107	serpin family C member 1	Homo sapiens	35-51
11368341-5	2001	Native, but not denatured, BSSL bound avidly to heparin and several of the heparin variants.	Heparin	48-55	carboxyl ester lipase	Homo sapiens	27-31
8703307-8	1996	In both the plasma samples taken with heparin as well as with serum, more ECP was released at a higher temperature.	Heparin	38-45	ribonuclease A family member 3	Homo sapiens	74-77
8652906-7	1996	The sulphated glycosaminoglycans which were critical in FGF-2-induced proliferation were strictly HSPG, as an addition of heparin in cell culture medium can restore FGF-2 mitogenic activity.	Heparin	122-129	syndecan 2	Homo sapiens	98-102
8601723-4	1996	At 37 degree C and pH 7.2, radioactively labeled MIP-1 beta, RANTES, and heparanase bound to confluent layers of resting keratinocytes in a saturable and an heparan sulfate- or heparin-dependent manner, and thereby induced the adhesion of resting CD4+ T cells to keratinocytes.	Heparin	177-184	C-C motif chemokine ligand 5	Homo sapiens	61-67
9164657-9	1996	Binding and degradation of vitronectin were also sensitive to the addition of exogenous heparin, suggesting that the heparin binding domain of vitronectin was mediating binding to the matrix.	Heparin	88-95	vitronectin	Homo sapiens	27-38
9164657-9	1996	Binding and degradation of vitronectin were also sensitive to the addition of exogenous heparin, suggesting that the heparin binding domain of vitronectin was mediating binding to the matrix.	Heparin	88-95	vitronectin	Homo sapiens	143-154
9164657-9	1996	Binding and degradation of vitronectin were also sensitive to the addition of exogenous heparin, suggesting that the heparin binding domain of vitronectin was mediating binding to the matrix.	Heparin	117-124	vitronectin	Homo sapiens	27-38
9164657-9	1996	Binding and degradation of vitronectin were also sensitive to the addition of exogenous heparin, suggesting that the heparin binding domain of vitronectin was mediating binding to the matrix.	Heparin	117-124	vitronectin	Homo sapiens	143-154
9403071-1	1997	The human ribosomal protein L29, which we reported previously, was subsequently shown to have the same nucleotide sequence as that of cell surface heparin/heparan sulfate-binding protein, designated HP/HS interacting protein.	Heparin	147-154	ribosomal protein L29	Homo sapiens	10-31
9374673-4	1997	At an HGF dose (1.46 nmol/kg), which completely saturates the high-affinity component, CLplasma was almost completely reduced when HGF was premixed with heparin.	Heparin	153-160	hepatocyte growth factor	Rattus norvegicus	6-9
9374673-6	1997	Saturation of CLplasma for HGF premixed with heparin was monophasic and nonlinear only at the lowest HGF doses.	Heparin	45-52	hepatocyte growth factor	Rattus norvegicus	101-104
9374673-7	1997	In vitro, high-affinity binding of [35S]heparin to HGF was found, showing that one HGF molecule binds to the penta- or hexasaccharide unit.	Heparin	40-47	hepatocyte growth factor	Rattus norvegicus	51-54
9374673-7	1997	In vitro, high-affinity binding of [35S]heparin to HGF was found, showing that one HGF molecule binds to the penta- or hexasaccharide unit.	Heparin	40-47	hepatocyte growth factor	Rattus norvegicus	83-86
9374673-8	1997	Because mitogenic activity of HGF has been reported in the presence of heparin, these results suggest that heparin mainly inhibits low-affinity HGF uptake by complexing with HGF, whereas its effect on RME is relatively minor.	Heparin	71-78	hepatocyte growth factor	Rattus norvegicus	30-33
9374673-8	1997	Because mitogenic activity of HGF has been reported in the presence of heparin, these results suggest that heparin mainly inhibits low-affinity HGF uptake by complexing with HGF, whereas its effect on RME is relatively minor.	Heparin	107-114	hepatocyte growth factor	Rattus norvegicus	30-33
9374673-8	1997	Because mitogenic activity of HGF has been reported in the presence of heparin, these results suggest that heparin mainly inhibits low-affinity HGF uptake by complexing with HGF, whereas its effect on RME is relatively minor.	Heparin	107-114	hepatocyte growth factor	Rattus norvegicus	144-147
9374673-8	1997	Because mitogenic activity of HGF has been reported in the presence of heparin, these results suggest that heparin mainly inhibits low-affinity HGF uptake by complexing with HGF, whereas its effect on RME is relatively minor.	Heparin	107-114	hepatocyte growth factor	Rattus norvegicus	144-147
9410906-1	1997	Amphiregulin (AR) is a heparin-binding, heparin-inhibited member of the epidermal growth factor (EGF) family and an autocrine growth factor for human keratinocytes.	Heparin	23-30	amphiregulin	Homo sapiens	0-12
9410906-1	1997	Amphiregulin (AR) is a heparin-binding, heparin-inhibited member of the epidermal growth factor (EGF) family and an autocrine growth factor for human keratinocytes.	Heparin	23-30	amphiregulin	Homo sapiens	14-16
9410906-1	1997	Amphiregulin (AR) is a heparin-binding, heparin-inhibited member of the epidermal growth factor (EGF) family and an autocrine growth factor for human keratinocytes.	Heparin	40-47	amphiregulin	Homo sapiens	0-12
9410906-1	1997	Amphiregulin (AR) is a heparin-binding, heparin-inhibited member of the epidermal growth factor (EGF) family and an autocrine growth factor for human keratinocytes.	Heparin	40-47	amphiregulin	Homo sapiens	14-16
9074719-6	1996	By in vitro and ex vivo experiments in mice, heparin and other glycosaminoglycans were shown to stimulate megakaryocytopoiesis by acting synergistically with thrombopoietin and interleukin 6, and in the other hand by neutralizing inhibitors of megakaryocytopoiesis such as platelet factor 4 and transforming growth factor beta.	Heparin	45-52	thrombopoietin	Mus musculus	158-172
11179981-7	2001	Heparin, a known in vitro activator of PKR, enhanced eIF2alpha phosphorylation by PKR mutants lacking their entire N-terminal sequences, including the dsRBDs.	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	39-42
7499205-6	1995	Both inhibitory peptides contain highly basic, putative heparin-binding domains and heparin partially reversed the inhibitory effects of rhIGFBP-3 on 125I-rhIGFBP-4 proteolysis.	Heparin	56-63	insulin like growth factor binding protein 4	Homo sapiens	137-164
7499205-6	1995	Both inhibitory peptides contain highly basic, putative heparin-binding domains and heparin partially reversed the inhibitory effects of rhIGFBP-3 on 125I-rhIGFBP-4 proteolysis.	Heparin	84-91	insulin like growth factor binding protein 4	Homo sapiens	137-164
9362073-11	1997	Depletion of matrix TSP by heparin treatment correlated with decreased microspike formation and cell motility.	Heparin	27-34	CTR9 homolog, Paf1/RNA polymerase II complex component	Mus musculus	20-23
9327758-8	1997	However, heparin only attenuated the response to repeated injury, with a partial decrease in intima-media wet weight and its DNA and elastin content and in I/M thickness ratio.	Heparin	9-16	elastin	Rattus norvegicus	133-140
11179981-7	2001	Heparin, a known in vitro activator of PKR, enhanced eIF2alpha phosphorylation by PKR mutants lacking their entire N-terminal sequences, including the dsRBDs.	Heparin	0-7	eukaryotic translation initiation factor 2 alpha kinase 2	Homo sapiens	82-85
9327758-9	1997	PCNA labeling showed that heparin inhibited the proliferative activity in medial cells much more strongly than in intimal cells.	Heparin	26-33	proliferating cell nuclear antigen	Rattus norvegicus	0-4
11158049-4	2001	The measurements of the whole putative LPL activity have been achieved after injection of heparin, a procedure that releases LPL from endothelium.	Heparin	90-97	lipoprotein lipase	Homo sapiens	39-42
7593208-4	1995	Hepatocyte growth factor increased proliferation in a dose-dependent fashion prior to 48 hr with half-maximal stimulation at approximately 3 ng/ml; in addition, heparin enhanced this activity.	Heparin	161-168	hepatocyte growth factor	Rattus norvegicus	0-24
11158049-4	2001	The measurements of the whole putative LPL activity have been achieved after injection of heparin, a procedure that releases LPL from endothelium.	Heparin	90-97	lipoprotein lipase	Homo sapiens	125-128
9379121-6	1997	The OE2-induced increase in PCNA-labelling index in all the cell types had a tendency to increase as the result of heparin action.	Heparin	115-122	proliferating cell nuclear antigen	Rattus norvegicus	28-32
11254842-11	2001	CONCLUSION: These data indicate that TFPI release by heparin probably has an important role in the suppression of the tissue factor-dependent coagulation pathway during CPB.	Heparin	53-60	coagulation factor III, tissue factor	Homo sapiens	118-131
8590307-6	1995	The recombinant mutant MCP-3 was purified to homogeneity by adsorption on silicic acid, affinity chromatography on heparin-Sepharose, and reversed-phase HPLC.	Heparin	115-122	C-C motif chemokine ligand 7	Homo sapiens	23-28
10172669-1	1995	Alteplase (recombinant tissue plasminogen activator; rt-PA) is a thrombolytic agent that when given in an accelerated regimen with intravenous heparin has survival advantages compared with streptokinase in the treatment of acute myocardial infarction, as shown by the results of the Global Utilisation of Streptokinase and Tissue Plasminogen Activator for Occluded Coronary Arteries (GUSTO) trial.	Heparin	143-150	chromosome 20 open reading frame 181	Homo sapiens	23-51
8562843-0	1995	Suppression of F1+2 (thrombin) generation in patients with DVT requires increased doses of heparin.	Heparin	91-98	coagulation factor XII	Homo sapiens	15-19
9301637-10	1997	Removal of candidate heparin-binding and acute-phase proteins by immunodepletion indicated that vitronectin plays an important role in the nonspecific binding of UFH in patient plasma.	Heparin	162-165	vitronectin	Homo sapiens	96-107
9279319-2	1997	Although heparin has no mitogenic potential of its own, it is an important aFGF cofactor in vitro and may also be capable of stimulating angiogenesis.	Heparin	9-16	fibroblast growth factor 1	Rattus norvegicus	75-79
9279319-9	1997	CONCLUSIONS: The increased vascularization and mitogenic activity demonstrated by these respective studies suggest that angiogenesis is significantly accelerated by the administration of heparin alone and is accelerated to a greater extent by the administration of aFGF with or without heparin.	Heparin	187-194	fibroblast growth factor 1	Rattus norvegicus	265-269
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	74-81	serpin family C member 1	Homo sapiens	42-54
9218427-5	1997	TGF-beta2.alpha2-macroglobulin complexes are more refractory to heparin/heparan sulfate, and those involving TGF-beta3 cannot be affected.	Heparin	64-71	transforming growth factor beta 2	Homo sapiens	0-9
9282310-6	1997	In the presence of heparin (5 U/ml), aFGF exerts its effect over a wide range of concentrations (0.1-10 ng/ml) in a dose-dependent manner.	Heparin	19-26	fibroblast growth factor 1	Canis lupus familiaris	37-41
7664675-6	1995	The half-life of 5DIII was approximately 3 h. Heparin was required for full acidic fibroblast growth factor activity.	Heparin	46-53	iodothyronine deiodinase 3	Rattus norvegicus	17-22
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	74-81	serpin family C member 1	Homo sapiens	147-159
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	116-123	serpin family C member 1	Homo sapiens	42-54
9240301-6	1997	We detected significant increases in F1 + 2 levels in both groups and increases in plasmin-alpha 2-antiplasmin complexes in the heparin-coated group at cessation of bypass, but no intergroup differences were observed.	Heparin	128-135	serpin family F member 2	Homo sapiens	91-110
7588746-9	1995	We have previously shown that heparin potentiates the catalytic activity of RMCP-1 and, in the present study, we show that the mechanism for chymase activation involves a sixfold reduction of the Km,app value of RMCP-1 for the chromogenic substrate S-2586.	Heparin	30-37	mast cell protease 1	Rattus norvegicus	141-148
11288878-1	2001	Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex.	Heparin	116-123	serpin family C member 1	Homo sapiens	147-159
11288878-2	2001	To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics, which structurally are very similar to the genuine polysaccharide.	Heparin	103-110	serpin family C member 1	Homo sapiens	70-82
11288878-2	2001	To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics, which structurally are very similar to the genuine polysaccharide.	Heparin	153-160	serpin family C member 1	Homo sapiens	70-82
8560417-0	1995	Characterization of a cDNA for rhesus monkey protein C inhibitor--evidence for N-terminal involvement in heparin stimulation.	Heparin	105-112	serpin family A member 5	Macaca mulatta	45-64
11465877-1	2001	UNLABELLED: Reviparin (reviparin sodium) is a low molecular weight heparin (LMWH) that catalyses the inactivation of factors Xa and IIa by binding to antithrombin, which ultimately leads to the inhibition of the clotting cascade.	Heparin	67-74	serpin family C member 1	Homo sapiens	150-162
7548155-5	1995	Examination of heparin binding using affinity chromatography indicated that while native HSC70 binds heparin, native HSP70 does not.	Heparin	15-22	heat shock protein family A (Hsp70) member 8	Homo sapiens	89-94
7548155-5	1995	Examination of heparin binding using affinity chromatography indicated that while native HSC70 binds heparin, native HSP70 does not.	Heparin	101-108	heat shock protein family A (Hsp70) member 8	Homo sapiens	89-94
7548155-6	1995	Treatment of the heparin-unbound fraction with heat or urea led to enhanced HSP70 binding to heparin affinity columns.	Heparin	17-24	heat shock protein family A (Hsp70) member 4	Homo sapiens	76-81
7548155-6	1995	Treatment of the heparin-unbound fraction with heat or urea led to enhanced HSP70 binding to heparin affinity columns.	Heparin	93-100	heat shock protein family A (Hsp70) member 4	Homo sapiens	76-81
7548155-7	1995	Soluble LIGRKKT peptide or anti-FN-C/H-II IgG also significantly inhibited heparin binding to HSC70 that had been purified by heparin affinity chromatography.	Heparin	75-82	heat shock protein family A (Hsp70) member 8	Homo sapiens	94-99
29512538-4	1997	Carbohydrade binding specificity studies showed that on molar basis MBP was feebly inhibited by lactose and strongly inhibited by heparin.	Heparin	130-137	myelin basic protein	Rattus norvegicus	68-71
9151824-7	1997	Furthermore, heparin effectively competes the interaction of M-T7 with the chemokine RANTES but not with rabbit gamma interferon.	Heparin	13-20	C-C motif chemokine ligand 5	Homo sapiens	85-91
7548155-7	1995	Soluble LIGRKKT peptide or anti-FN-C/H-II IgG also significantly inhibited heparin binding to HSC70 that had been purified by heparin affinity chromatography.	Heparin	126-133	heat shock protein family A (Hsp70) member 8	Homo sapiens	94-99
11103165-0	2000	Delivery of low molecular weight heparin for prophylaxis against deep vein thrombosis using a novel, needle-less injection device (J-Tip).	Heparin	33-40	TOR signaling pathway regulator	Homo sapiens	133-136
7548155-8	1995	Finally, Western blot analysis of HSC70 purified by heparin affinity chromatography demonstrated that polyclonal anti-FN-C/H-II IgG could recognize HSC70.	Heparin	52-59	heat shock protein family A (Hsp70) member 8	Homo sapiens	34-39
7548155-8	1995	Finally, Western blot analysis of HSC70 purified by heparin affinity chromatography demonstrated that polyclonal anti-FN-C/H-II IgG could recognize HSC70.	Heparin	52-59	heat shock protein family A (Hsp70) member 8	Homo sapiens	148-153
7548155-9	1995	These data demonstrate that LIGRK or LIGRR represent a a common heparin binding motif in fibronectin, HSP70, and HSC70, and are consistent with a proposed role for heparin or similar polyanionic structures in the function of the 70 kDa heat-shock proteins.	Heparin	64-71	heat shock protein family A (Hsp70) member 4	Homo sapiens	102-107
7548155-9	1995	These data demonstrate that LIGRK or LIGRR represent a a common heparin binding motif in fibronectin, HSP70, and HSC70, and are consistent with a proposed role for heparin or similar polyanionic structures in the function of the 70 kDa heat-shock proteins.	Heparin	64-71	heat shock protein family A (Hsp70) member 8	Homo sapiens	113-118
8690721-0	1995	Modulation of elastin expression by heparin is dependent on the growth condition of vascular smooth muscle cells: up-regulation of elastin expression by heparin in the proliferating cells is mediated by the inhibition of protein kinase C activity.	Heparin	36-43	elastin	Homo sapiens	14-21
8690721-0	1995	Modulation of elastin expression by heparin is dependent on the growth condition of vascular smooth muscle cells: up-regulation of elastin expression by heparin in the proliferating cells is mediated by the inhibition of protein kinase C activity.	Heparin	153-160	elastin	Homo sapiens	14-21
8690721-0	1995	Modulation of elastin expression by heparin is dependent on the growth condition of vascular smooth muscle cells: up-regulation of elastin expression by heparin in the proliferating cells is mediated by the inhibition of protein kinase C activity.	Heparin	153-160	elastin	Homo sapiens	131-138
8690721-1	1995	The effect of heparin on elastin expression in the proliferating and quiescent phases of growth of smooth muscle cells was studied.	Heparin	14-21	elastin	Homo sapiens	25-32
8690721-2	1995	Heparin stimulated elastin synthesis and its mRNA level 2-3 fold in the proliferating cells while it inhibited the cell proliferation.	Heparin	0-7	elastin	Homo sapiens	19-26
8690721-3	1995	The inhibition of cell proliferation and the stimulation of elastin expression by heparin in the proliferating cells were mimicked by a potent protein kinase C antagonist, H-7, but not by H-89, W-7, and HA1004, suggesting that the effect of heparin is mediated by the inhibition of protein kinase C. In contrast, heparin inhibited elastin synthesis and its mRNA level slightly but exhibited no effect on cell proliferation in the growth-arrested cells.	Heparin	82-89	elastin	Homo sapiens	60-67
8690721-3	1995	The inhibition of cell proliferation and the stimulation of elastin expression by heparin in the proliferating cells were mimicked by a potent protein kinase C antagonist, H-7, but not by H-89, W-7, and HA1004, suggesting that the effect of heparin is mediated by the inhibition of protein kinase C. In contrast, heparin inhibited elastin synthesis and its mRNA level slightly but exhibited no effect on cell proliferation in the growth-arrested cells.	Heparin	82-89	elastin	Homo sapiens	331-338
8690721-4	1995	This result indicates that heparin reciprocally affects elastin expression depending on the growth state of smooth muscle cells.	Heparin	27-34	elastin	Homo sapiens	56-63
8690721-5	1995	Heparin thus exerts a complex influence on elastin expression in smooth muscle cells.	Heparin	0-7	elastin	Homo sapiens	43-50
9171870-1	1997	The synthetic pentasaccharide (1) corresponding to the heparin sequence which binds to, and activates, antithrombin III (AT III) is a potent antithrombotic compound in several animal models of venous thrombosis.	Heparin	55-62	serpin family C member 1	Rattus norvegicus	103-119
9171870-1	1997	The synthetic pentasaccharide (1) corresponding to the heparin sequence which binds to, and activates, antithrombin III (AT III) is a potent antithrombotic compound in several animal models of venous thrombosis.	Heparin	55-62	serpin family C member 1	Rattus norvegicus	121-127
9164872-8	1997	Using vitronectin-derived synthetic peptides as well as mutant forms of recombinant osteonectin, we found that the heparin-binding region of vitronectin interacted with the C-terminal region of osteonectin that contains a high-affinity Ca2+-binding site with counter-adhesive properties.	Heparin	115-122	vitronectin	Homo sapiens	6-17
9164872-8	1997	Using vitronectin-derived synthetic peptides as well as mutant forms of recombinant osteonectin, we found that the heparin-binding region of vitronectin interacted with the C-terminal region of osteonectin that contains a high-affinity Ca2+-binding site with counter-adhesive properties.	Heparin	115-122	vitronectin	Homo sapiens	141-152
9324398-2	1997	The essential role of the nerve growth factor in inducing the release of heparin and histamine into the blood and its contribution to the activation of other components of fibrinolysis and the antithrombine system is shown.	Heparin	73-80	nerve growth factor	Mus musculus	26-45
9166893-1	1997	Vitronectin is a multifunctional serum protein which provides a unique regulatory link between cell adhesion, humoral defense mechanism and the hemostatic system, and the heparin-binding properties of vitronectin are thought to have participated in various functional aspects.	Heparin	171-178	vitronectin	Homo sapiens	0-11
9166893-1	1997	Vitronectin is a multifunctional serum protein which provides a unique regulatory link between cell adhesion, humoral defense mechanism and the hemostatic system, and the heparin-binding properties of vitronectin are thought to have participated in various functional aspects.	Heparin	171-178	vitronectin	Homo sapiens	201-212
11041873-0	2000	Mechanism for activation of mouse mast cell tryptase: dependence on heparin and acidic pH for formation of active tetramers of mouse mast cell protease 6.	Heparin	68-75	tryptase alpha/beta 1	Mus musculus	44-52
9083085-4	1997	In this study, we demonstrate that the amino-terminal (N) domain retains the heparin-binding properties of full-length HGF/SF.	Heparin	77-84	hepatocyte growth factor	Cricetulus griseus	119-125
8589205-10	1995	The activation of GP IIb-IIIa occurred despite the patients receiving aspirin and heparin.	Heparin	82-89	integrin subunit alpha 2b	Homo sapiens	18-24
7593255-12	1995	Addition of anti-TGF-beta 1 antibodies, plasminogen activator inhibitor-1 (PAI-1), or the thrombin inhibitory combination of heparin and anti-thrombin III (AT III) to the cells at the time of scraping blocked about 50% of the increase in bFGF mRNA; the effects of these agents were not additive.	Heparin	125-132	coagulation factor II, thrombin	Bos taurus	90-98
7797488-3	1995	The binding of 125I-VEGF165 to the VEGF receptors of endothelial cells, and the heparin-dependent binding of 125I-VEGF165 to a soluble extracellular domain of the VEGF receptor KDR/flk-1, were inhibited by the angiogenesis inhibitor platelet factor-4 (PF4).	Heparin	80-87	kinase insert domain receptor	Homo sapiens	177-180
11041873-10	2000	When heparin was added at pH 6.0, enzymatically active higher molecular weight complexes were formed, e.g., a dominant approximately 200 kDa complex that may correspond to tryptase tetramers.	Heparin	5-12	tryptase alpha/beta 1	Mus musculus	172-180
7797488-3	1995	The binding of 125I-VEGF165 to the VEGF receptors of endothelial cells, and the heparin-dependent binding of 125I-VEGF165 to a soluble extracellular domain of the VEGF receptor KDR/flk-1, were inhibited by the angiogenesis inhibitor platelet factor-4 (PF4).	Heparin	80-87	kinase insert domain receptor	Homo sapiens	181-186
9096801-6	1997	In conclusion, heparin coating of artificial surfaces has a substantial effect, reducing the expression of molecules involved in cellular adhesion and activation (CD11b and CD45), and the increase of these molecules by unmodified surfaces is complement dependent.	Heparin	15-22	integrin subunit alpha M	Homo sapiens	163-168
11041873-13	2000	The present paper thus indicates a crucial role for heparin in the formation of active mast cell tryptase.	Heparin	52-59	tryptase alpha/beta 1	Mus musculus	97-105
9096801-6	1997	In conclusion, heparin coating of artificial surfaces has a substantial effect, reducing the expression of molecules involved in cellular adhesion and activation (CD11b and CD45), and the increase of these molecules by unmodified surfaces is complement dependent.	Heparin	15-22	protein tyrosine phosphatase receptor type C	Homo sapiens	173-177
9096801-7	1997	In contrast, up-regulation of other surface molecules (CD14 and CD16) seems to be independent of heparin coating and complement activation and, thus, might be regulated by other mechanisms.	Heparin	97-104	Fc gamma receptor IIIa	Homo sapiens	64-68
9167024-0	1997	In vitro inhibition of heparin-induced platelet aggregation in plasma from patients with HIT by SR 121566, a newly developed Gp IIb/IIIa antagonist.	Heparin	23-30	integrin subunit alpha 2b	Homo sapiens	125-131
7538463-7	1995	Heparin alone inhibited IGFBP-4 proteolysis by more than 60%.	Heparin	0-7	insulin like growth factor binding protein 4	Homo sapiens	24-31
7769270-6	1995	Addition of heparin with KGF produced a further increase in MMP-9 activity, with heparin alone having no effect.	Heparin	12-19	matrix metallopeptidase 9	Homo sapiens	60-65
7769270-7	1995	Precoating of polycarbonate membranes with matrix components showed that fibronectin and an engineered poly-RGD molecule substrate were required for KGF plus heparin to increase MMP-9 activity.	Heparin	158-165	matrix metallopeptidase 9	Homo sapiens	178-183
9062364-8	1997	Heparin at the concentration that neutralized the function of amphiregulin, or antibodies against TGFalpha or HB-EGF also reduced the release of PGE2 from IFN-gamma-stimulated NHBECs.	Heparin	0-7	amphiregulin	Homo sapiens	62-74
11009624-2	2000	Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa.	Heparin	0-7	serpin family C member 1	Homo sapiens	49-61
9131716-0	1997	Effects of heparin coating on the expression of CD11b, CD11c and CD62L by leucocytes in extracorporeal circulation in vitro.	Heparin	11-18	integrin subunit alpha M	Homo sapiens	48-53
9131716-6	1997	Heparin coating reduced the increase in CD11b and CD11c on granulocytes (p &lt; 0.02 at 2 h), but the delayed increase in CD11c on monocytes and the delayed downregulation of CD62L on granulocytes and monocytes did not reach statistical significance.	Heparin	0-7	integrin subunit alpha M	Homo sapiens	40-45
7612053-1	1995	Low-anticoagulant heparin (LA-heparin) obtained by affinity chromatography on antithrombin III Sepharose inhibits the proliferation of cultured arterial smooth muscle cells in an in vitro bioassay system as effectively as standard heparin.	Heparin	18-25	serpin family C member 1	Rattus norvegicus	78-94
11009624-2	2000	Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa.	Heparin	146-153	serpin family C member 1	Homo sapiens	49-61
7612053-1	1995	Low-anticoagulant heparin (LA-heparin) obtained by affinity chromatography on antithrombin III Sepharose inhibits the proliferation of cultured arterial smooth muscle cells in an in vitro bioassay system as effectively as standard heparin.	Heparin	30-37	serpin family C member 1	Rattus norvegicus	78-94
11009624-3	2000	To provide direct evidence for this bridging mechanism, we studied the heparin-catalyzed reaction of antithrombin with factor Xa, Gla-domainless factor Xa (GDFXa), and a heparin binding exosite mutant of GDFXa in the absence and presence of calcium using rapid kinetic methods.	Heparin	71-78	serpin family C member 1	Homo sapiens	101-113
9034134-3	1997	A subsequent treatment of the tissues with 1 microg/ml PRL caused a 76% increase in heparin-releasable LPL (hrLPL) activity after 24 hr.	Heparin	84-91	prolactin	Mus musculus	55-58
11009624-4	2000	The pseudo-first-order rate constant for factor Xa inhibition by antithrombin complexed with a long-chain approximately 70-saccharide heparin showed a saturable dependence on inhibitor concentration in the presence but not in the absence of 2.5 mM Ca(2+), indicating the formation of an intermediate heparin-serpin-proteinase encounter complex with a dissociation constant of approximately 90 nM prior to formation of the stable serpin-proteinase complex with a rate constant of approximately 20 s(-1).	Heparin	134-141	serpin family C member 1	Homo sapiens	65-77
9034134-3	1997	A subsequent treatment of the tissues with 1 microg/ml PRL caused a 76% increase in heparin-releasable LPL (hrLPL) activity after 24 hr.	Heparin	84-91	lipoprotein lipase	Mus musculus	103-106
7537691-0	1995	FGF-1 is a heparin-independent mitogen for rat hepatocytes.	Heparin	11-18	fibroblast growth factor 1	Rattus norvegicus	0-5
11009624-7	2000	These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism.	Heparin	51-58	serpin family C member 1	Homo sapiens	232-244
7537691-1	1995	We have found that in the primary culture of rat hepatocytes, the potent mitogenic activity of native FGF-1 is independent of heparin.	Heparin	126-133	fibroblast growth factor 1	Rattus norvegicus	102-107
7537691-4	1995	For both cell types, however, it is demonstrated that either endogenous or exogenous heparan sulfate/heparin moieties are essential for FGF-1 to establish receptor binding and mitogen action.	Heparin	101-108	fibroblast growth factor 1	Rattus norvegicus	136-141
11009624-7	2000	These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism.	Heparin	224-231	serpin family C member 1	Homo sapiens	232-244
11089917-6	2000	Lipoprotein lipase (LpL) which binds LDL was also able to interact with high affinity with decorin and its glycosaminoglycan-free core protein, both interactions being heparin-sensitive.	Heparin	168-175	lipoprotein lipase	Homo sapiens	0-18
8586627-7	1995	In addition, a combination of heparin with HGF further accelerated the effects of HGF described above, possibly due to the decrease of HGF clearance.	Heparin	30-37	hepatocyte growth factor	Rattus norvegicus	82-85
8586627-7	1995	In addition, a combination of heparin with HGF further accelerated the effects of HGF described above, possibly due to the decrease of HGF clearance.	Heparin	30-37	hepatocyte growth factor	Rattus norvegicus	82-85
8993240-5	1997	Heparin coating, however, reduced maximum values of C3b/c (446 +/- 212 nmol/L versus 632 +/- 264 nmol/L with uncoated ECC; p = 0.0037) and maximum C4b/c values (92 +/- 48 nmol/L versus 172 +/- 148 nmol/L with uncoated ECC; p = 0.0069).	Heparin	0-7	complement C3	Homo sapiens	52-55
11089917-6	2000	Lipoprotein lipase (LpL) which binds LDL was also able to interact with high affinity with decorin and its glycosaminoglycan-free core protein, both interactions being heparin-sensitive.	Heparin	168-175	lipoprotein lipase	Homo sapiens	20-23
10961890-6	2000	Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner.	Heparin	8-15	Fc gamma receptor Ia	Homo sapiens	140-144
9070173-9	1997	CONCLUSION: The decrease in platelet deposition on the FG/FGF-1/ heparin-coated grafts vs preclotted grafts is not due to heparin and is not specific to canine or human platelets.	Heparin	65-72	fibroblast growth factor 1	Canis lupus familiaris	58-63
9489431-0	1997	[The effect of heparin on eosinophil chemotaxis induced by Rantes and FMLP].	Heparin	15-22	C-C motif chemokine ligand 5	Homo sapiens	59-65
9489431-6	1997	In order to explore the mechanism involved in these protective effects we studied the influence of heparin on eosinophil chemotaxis induced by Rantes and FMLP.	Heparin	99-106	C-C motif chemokine ligand 5	Homo sapiens	143-149
9156408-0	1997	Pharmacokinetic properties of LMW-heparin-tyramine fractions with high or low affinity to antithrombin III in the rat.	Heparin	34-41	serpin family C member 1	Rattus norvegicus	90-106
9003378-0	1996	Lactoferrin regulates the activity of heparin proteoglycan-bound mast cell chymase: characterization of the binding of heparin to lactoferrin.	Heparin	38-45	mast cell protease 1	Rattus norvegicus	75-82
9003378-3	1996	In the search for alternative mechanisms in the regulation of RMCP-1 activity, we hypothesized that heparin antagonists, by interfering with the RMCP-1/heparin PG interaction, might influence the activity of heparin-bound mast cell chymase.	Heparin	100-107	mast cell protease 1	Rattus norvegicus	232-239
8952699-8	1996	The 55-60 kDa glycosylated AR isoform, like lower Mr AR isoforms, is able to bind to heparin and to stimulate the growth of MCF-10A cells by interacting with the EGF receptor.	Heparin	85-92	amphiregulin	Homo sapiens	27-29
8952699-8	1996	The 55-60 kDa glycosylated AR isoform, like lower Mr AR isoforms, is able to bind to heparin and to stimulate the growth of MCF-10A cells by interacting with the EGF receptor.	Heparin	85-92	amphiregulin	Homo sapiens	53-55
7659852-4	1995	The changes in each parameter were determined chiefly by the activity of lipoprotein lipase, which was measured in plasma collected after the intravenous injection of heparin and did not appear to be influenced by intestinal fat absorption.	Heparin	167-174	lipoprotein lipase	Canis lupus familiaris	73-91
7656159-7	1995	Immunocytochemical investigation also confirmed that heparin could inhibit the expression of nuclear oncogene c-fos and c-jun in the MsC stimulated by PMA.	Heparin	53-60	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	110-115
7730327-3	1995	Here we show that a lower affinity of FGFR1 alpha for heparin parallels the lower affinity for FGF-1.	Heparin	54-61	fibroblast growth factor 1	Rattus norvegicus	95-100
7730327-4	1995	A mutant of FGFR1 alpha in which the sequence between Loops I and II was deleted exhibits high affinity for both FGF-1 and heparin and other properties of the FGFR1 beta isoform, which include resistance to degradation by trypsin and display of specific antibody epitopes.	Heparin	123-130	Fibroblast growth factor receptor 1	Rattus norvegicus	12-17
10993477-6	2000	The loss of heparin-binding affinity of EC-SOD type C with high affinity for heparin occurred in kidney of obese mice.	Heparin	12-19	superoxide dismutase 3, extracellular	Mus musculus	40-46
7596134-0	1995	Protection by ITF 1300, a heparin ion-pair complex, against arrhythmias induced by regional ischemia and reperfusion in the isolated rat heart: possible mechanism of action.	Heparin	26-33	trefoil factor 3	Rattus norvegicus	14-17
7892570-0	1995	[Is the assessment of prothrombin fragment F1+2 for monitoring of heparin therapy in patients with deep vein thrombosis useful?].	Heparin	66-73	coagulation factor XII	Homo sapiens	43-47
7892570-1	1995	Prothrombin fragments (F1+2) can be used to monitor oral anticoagulation; their generation is also suppressed by heparin.	Heparin	113-120	coagulation factor XII	Homo sapiens	23-27
8954887-7	1996	Recombinant TP2 was purified from the soluble extract of E. coli using nickel-agarose and heparin-agarose chromatography and was shown to be identical to native rat TP2 as revealed by immunoblotting with anti-rat TP2 antibodies and radioactive 65Zn-blotting.	Heparin	90-97	transition protein 2	Rattus norvegicus	12-15
8910598-1	1996	The binding of heparin to antithrombin greatly accelerates the rate of inhibition of the target proteinases thrombin and factor Xa.	Heparin	15-22	coagulation factor X	Homo sapiens	121-130
8910598-2	1996	Acceleration of the rate of inhibition of factor Xa involves a conformational change in antithrombin that is translated from the heparin binding site to the reactive center loop.	Heparin	129-136	coagulation factor X	Homo sapiens	42-51
8873656-9	1996	Combined death or disabling stroke occurred less often with accelerated TPA in all but the oldest patients, who showed a weak trend toward a lower incidence with streptokinase plus subcutaneous heparin: odds ratio 1.13; 95% confidence interval 0.6, 2.1.	Heparin	194-201	chromosome 20 open reading frame 181	Homo sapiens	72-75
7892570-4	1995	The amount of heparin given was stable from day 1-5; the fact of a transient increase in F1+2 might thus indicate that heparin doses routinely used are too low for the treatment of hypercoagulability in deep venous thrombosis in patients.	Heparin	119-126	coagulation factor XII	Homo sapiens	89-93
7892570-6	1995	In conclusion, F1+2 may be useful for monitoring heparin treatment and oral anticoagulation in deep venous thrombosis patients from a laboratory point of view.	Heparin	49-56	coagulation factor XII	Homo sapiens	15-19
10993477-6	2000	The loss of heparin-binding affinity of EC-SOD type C with high affinity for heparin occurred in kidney of obese mice.	Heparin	77-84	superoxide dismutase 3, extracellular	Mus musculus	40-46
8808643-0	1996	Autoimmune MRL mice express high-affinity IgG2b monoclonal autoantibodies to heparin.	Heparin	77-84	immunoglobulin heavy constant gamma 2B	Mus musculus	42-47
10937578-3	2000	Heparin"s capacity to stabilize recombinant LEDGF in the face of various stresses (heat, pH, proteolysis), to potentiate its growth-enhancing properties, and to enable transport of LEDGF into the nucleus of mouse lens epithelial cells has been characterized.	Heparin	0-7	PC4 and SFRS1 interacting protein 1	Mus musculus	44-49
8855297-6	1996	The results demonstrate (i) that factor H has at least three sites that bind C3b, (ii) that one of these sites is located in SCR domains 1-4, as has been shown by others, (iii) that a second site exists in the domain 6-10 region, (iv) that a third site resides in the SCR 16-20 region, and (v) that two heparin binding sites exist in factor H, one near SCR 13 and another in the SCR 6-10 region.	Heparin	303-310	complement factor H	Homo sapiens	33-41
8855297-6	1996	The results demonstrate (i) that factor H has at least three sites that bind C3b, (ii) that one of these sites is located in SCR domains 1-4, as has been shown by others, (iii) that a second site exists in the domain 6-10 region, (iv) that a third site resides in the SCR 16-20 region, and (v) that two heparin binding sites exist in factor H, one near SCR 13 and another in the SCR 6-10 region.	Heparin	303-310	complement C3	Homo sapiens	77-80
7539644-1	1995	This communication is concerned with the binding specificity of the leukocyte-adhesion molecule L-selectin (leukocyte homing receptor) towards structurally defined sulphated oligosaccharides of the blood group Le(a) and Le(x) series, and of the glycosaminoglycan series heparin, chondroitin sulphate and keratan sulphate.	Heparin	270-277	selectin L	Rattus norvegicus	96-106
7532176-4	1995	b-FGF and HB-EGF binding to HS-modified CD44 was eliminated by pretreating the protein with heparitinase or by blocking with free heparin.	Heparin	130-137	CD44 molecule (Indian blood group)	Homo sapiens	40-44
8830777-12	1996	All TN-Y variants isolated bind to heparin under physiologically relevant conditions that may indicate an important function retained in all tenascins.	Heparin	35-42	avian tenascin X	Gallus gallus	4-8
10937578-3	2000	Heparin"s capacity to stabilize recombinant LEDGF in the face of various stresses (heat, pH, proteolysis), to potentiate its growth-enhancing properties, and to enable transport of LEDGF into the nucleus of mouse lens epithelial cells has been characterized.	Heparin	0-7	PC4 and SFRS1 interacting protein 1	Mus musculus	181-186
8718884-6	1996	The acid protease cathepsin D generated fragments of 31-33.5 kDa from the COOH-terminal heparin-binding domain of Fn which possessed high immunoreactivity with anti-CS-1.	Heparin	88-95	chorionic somatomammotropin hormone 1	Homo sapiens	165-169
8663360-0	1996	Heparin inhibits mitogen-activated protein kinase-dependent and -independent c-fos induction in mesangial cells.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	77-82
8663360-1	1996	Heparin suppresses mitogenic responses in renal mesangial cells, and when quiescent mesangial cells are stimulated with serum, heparin blocks the induction of c-fos seen at 15 min.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	159-164
8663360-1	1996	Heparin suppresses mitogenic responses in renal mesangial cells, and when quiescent mesangial cells are stimulated with serum, heparin blocks the induction of c-fos seen at 15 min.	Heparin	127-134	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	159-164
8663360-2	1996	Because heparin is taken up by cells over a much longer time course, we addressed mechanisms whereby extracellular heparin might suppress c-fos induction at such early times.	Heparin	115-122	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	138-143
8663360-6	1996	Heparin (1 microg/ml) suppressed the induction of c-fos initiated by all three treatments.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	50-55
8663360-12	1996	We conclude that heparin suppresses induction of c-fos in mesangial cells by blocking at least two different points in signal transduction cascades, one upstream of MAPK and the other independent of MAPK, but dependent on intracellular Ca2+.	Heparin	17-24	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	49-54
7815550-5	1995	On the basis of the results of attachment, penetration, and heparin competition assays, the heterologous HBD mediated heparan sulfate-dependent virus attachment, but not to fully wild-type levels.	Heparin	60-67	HBD	Homo sapiens	105-108
7819186-8	1995	Likewise, polyanionic inhibitors of the CK2 catalytic activity, such as heparin, poly(U), and copoly(Glu:Tyr) polypeptides, can compete for and inhibit the binding of DNA to CK2 alpha.	Heparin	72-79	casein kinase 2 alpha 2	Homo sapiens	174-183
7749138-1	1995	Amphiregulin (AR) is an epidermal growth factor (EGF)-related peptide that operates exclusively through the EGF receptor and that can bind to heparin.	Heparin	142-149	amphiregulin	Homo sapiens	0-12
7749138-1	1995	Amphiregulin (AR) is an epidermal growth factor (EGF)-related peptide that operates exclusively through the EGF receptor and that can bind to heparin.	Heparin	142-149	amphiregulin	Homo sapiens	14-16
7528211-6	1994	268, 2984-2988) that heparin potentiates the mitogenic activity of acidic FGF (aFGF) but inhibits that of the keratinocyte growth factor (KGF) in cells that express the KGF receptor (KGFR).	Heparin	21-28	fibroblast growth factor 1	Rattus norvegicus	67-77
7528211-6	1994	268, 2984-2988) that heparin potentiates the mitogenic activity of acidic FGF (aFGF) but inhibits that of the keratinocyte growth factor (KGF) in cells that express the KGF receptor (KGFR).	Heparin	21-28	fibroblast growth factor 1	Rattus norvegicus	79-83
7528211-6	1994	268, 2984-2988) that heparin potentiates the mitogenic activity of acidic FGF (aFGF) but inhibits that of the keratinocyte growth factor (KGF) in cells that express the KGF receptor (KGFR).	Heparin	21-28	fibroblast growth factor 7	Rattus norvegicus	138-141
10937578-5	2000	Porcine heparin was used to stabilize GST-LEDGF.	Heparin	8-15	PC4 and SFRS1 interacting protein 1	Mus musculus	42-47
7528211-6	1994	268, 2984-2988) that heparin potentiates the mitogenic activity of acidic FGF (aFGF) but inhibits that of the keratinocyte growth factor (KGF) in cells that express the KGF receptor (KGFR).	Heparin	21-28	fibroblast growth factor 7	Rattus norvegicus	169-172
7528211-8	1994	To gain an insight into the mechanism by which heparin modulates the biological activity of aFGF and KGF, we studied the effect of heparin and cell-associated heparan sulfates on the binding of these two growth factors to the KGFR.	Heparin	47-54	fibroblast growth factor 1	Rattus norvegicus	92-96
7528211-8	1994	To gain an insight into the mechanism by which heparin modulates the biological activity of aFGF and KGF, we studied the effect of heparin and cell-associated heparan sulfates on the binding of these two growth factors to the KGFR.	Heparin	47-54	fibroblast growth factor 7	Rattus norvegicus	101-104
8625852-3	1996	To further test this hypothesis, we have compared the ability of differentially active agrin isoforms to interact with a model component of proteoglycans, heparin, as well as with the putative proteoglycan alpha-dystroglycan.	Heparin	155-162	agrin	Homo sapiens	87-92
8625852-4	1996	We demonstrate that an alternately spliced exon (encoding the sequence lysine, serine, arginine, lysine: Y site) is necessary for agrin-heparin interactions.	Heparin	136-143	agrin	Homo sapiens	130-135
8636243-0	1996	Heparin induces dimerization and confers proliferative activity onto the hepatocyte growth factor antagonists NK1 and NK2.	Heparin	0-7	hepatocyte growth factor	Mus musculus	110-113
7528211-10	1994	Low concentrations of heparin inhibited the binding of KGF to the KGFR.	Heparin	22-29	fibroblast growth factor 7	Rattus norvegicus	55-58
10937578-9	2000	RESULTS: Heparin, at concentrations as low as 7.1 mg/ml, protected GST-LEDGF from degradation and increased the yield of the full-size fusion protein in a prokaryotic system.	Heparin	9-16	PC4 and SFRS1 interacting protein 1	Mus musculus	71-76
7528211-11	1994	By contrast, similar concentrations of heparin enhanced the binding of aFGF to this receptor.	Heparin	39-46	fibroblast growth factor 1	Rattus norvegicus	71-75
8636243-14	1996	Interestingly, NK1, which is an HGF antagonist in hepatocytes in normal conditions, was converted to a partial agonist by adding heparin to the culture medium.	Heparin	129-136	hepatocyte growth factor	Mus musculus	15-18
8636243-20	1996	Mechanistic studies revealed that heparin increased the binding of NK1 to BaF3-hMet cells, stabilized NK1, and induced dimerization of NK1.	Heparin	34-41	hepatocyte growth factor	Mus musculus	67-70
7528211-16	1994	Heparin restored the high affinity binding of aFGF to chlorate-treated cells and completely abolished the high affinity binding of KGF.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	46-50
10937578-12	2000	CONCLUSIONS: Heparin protected GST-LEDGF from degradation under various stress conditions and facilitated transport of GST-LEDGF into the nucleus.	Heparin	13-20	PC4 and SFRS1 interacting protein 1	Mus musculus	35-40
7528211-16	1994	Heparin restored the high affinity binding of aFGF to chlorate-treated cells and completely abolished the high affinity binding of KGF.	Heparin	0-7	fibroblast growth factor 7	Rattus norvegicus	131-134
8636243-20	1996	Mechanistic studies revealed that heparin increased the binding of NK1 to BaF3-hMet cells, stabilized NK1, and induced dimerization of NK1.	Heparin	34-41	hepatocyte growth factor	Mus musculus	102-105
8636243-20	1996	Mechanistic studies revealed that heparin increased the binding of NK1 to BaF3-hMet cells, stabilized NK1, and induced dimerization of NK1.	Heparin	34-41	hepatocyte growth factor	Mus musculus	102-105
10937578-12	2000	CONCLUSIONS: Heparin protected GST-LEDGF from degradation under various stress conditions and facilitated transport of GST-LEDGF into the nucleus.	Heparin	13-20	PC4 and SFRS1 interacting protein 1	Mus musculus	123-128
8636243-22	1996	Consistent with that model, a large portion of the NK1 binding to mink lung cells could be blocked by heparin.	Heparin	102-109	hepatocyte growth factor	Mus musculus	51-54
8636243-24	1996	These data show that the activity of NK1 and NK2 can be modulated by heparin and other related glycosaminoglycans to induce proliferation in cells expressing c-Met.	Heparin	69-76	hepatocyte growth factor	Mus musculus	37-40
8607674-3	1996	RESULTS: Heparin-coated extracorporeal circuits significantly reduced circulating complement activation product C3b/c and soluble C5b-9 concentrations at the end of cardiopulmonary bypass and after protamine sulfate administration compared with the uncoated circuits, but not iC3, C4b/c, or C3a concentrations.	Heparin	9-16	complement C3	Homo sapiens	112-115
8607674-3	1996	RESULTS: Heparin-coated extracorporeal circuits significantly reduced circulating complement activation product C3b/c and soluble C5b-9 concentrations at the end of cardiopulmonary bypass and after protamine sulfate administration compared with the uncoated circuits, but not iC3, C4b/c, or C3a concentrations.	Heparin	9-16	complement C3	Homo sapiens	291-294
8603535-5	1996	Specifically, heparin was shown to inhibit the induction of class II MHC antigens and the up-regulation of intercellular adhesion molecule-1 (ICAM-1) produced by treatment of cultured human endothelial cells with IFN-gamma.	Heparin	14-21	intercellular adhesion molecule 1	Homo sapiens	107-140
8603535-5	1996	Specifically, heparin was shown to inhibit the induction of class II MHC antigens and the up-regulation of intercellular adhesion molecule-1 (ICAM-1) produced by treatment of cultured human endothelial cells with IFN-gamma.	Heparin	14-21	intercellular adhesion molecule 1	Homo sapiens	142-148
7991602-7	1994	These results directly demonstrate that HB-EGF but not EGF requires heparin or cell surface HSPG for binding and activation of the EGF receptor and that HB-EGF receptor interactions can be tightly regulated by the available local concentration of heparin-like molecules.	Heparin	247-254	proheparin-binding EGF-like growth factor	Cricetulus griseus	40-46
7991602-7	1994	These results directly demonstrate that HB-EGF but not EGF requires heparin or cell surface HSPG for binding and activation of the EGF receptor and that HB-EGF receptor interactions can be tightly regulated by the available local concentration of heparin-like molecules.	Heparin	247-254	proheparin-binding EGF-like growth factor	Cricetulus griseus	153-159
7961933-9	1994	The second-order inhibition rate constants k2/Ki* were 4300, 700, and 52 M-1 S-1 for alpha 1-antichymotrypsin, alpha 1-antitrypsin, and eglin c, respectively, indicating that, if heparin is present in vivo, the two former physiological inhibitors will be unable to prevent cathepsin G-mediated proteolysis.	Heparin	179-186	serpin family A member 3	Homo sapiens	85-109
7524763-5	1994	Although +/+ CMCs were berberine sulfate-negative when cultured with rmIL-3 alone, +/+ CMCs became berberine sulfate-positive when cultured in the presence of both rmIL-3 and NGF, which suggests increased heparin content.	Heparin	205-212	nerve growth factor	Mus musculus	164-178
10900049-5	2000	Phosphorylation of the MP was decreased by addition of kinase inhibitors such as heparin, suramin and quercetin, which are known to be effective for casein kinase II (CK II).	Heparin	81-88	casein kinase 2 alpha 1	Homo sapiens	149-165
7843648-2	1994	An ELISA was developed for directly measuring the expression of glycoprotein IIb/IIIa (GPIIb/IIIa) on platelets in the presence and absence of ADP and under the influence of various heparins.	Heparin	182-190	integrin subunit alpha 2b	Homo sapiens	87-97
7843648-4	1994	Heparin also induced the expression of GPIIb/IIIa without prior stimulation with ADP.	Heparin	0-7	integrin subunit alpha 2b	Homo sapiens	39-44
7843648-6	1994	These results suggested that heparin(oid)s modulate the expression of GPIIb/IIIa with ADP as a mediator, and that protamine sulfate is contraindicated as an antidote in heparin-induced thrombocytopenia.	Heparin	29-36	integrin subunit alpha 2b	Homo sapiens	70-75
8607994-3	1996	Here, we compared binding of agrin isoforms to heparin, alpha-dystroglycan, and cultured myotubes.	Heparin	47-54	agrin	Homo sapiens	29-34
10900049-5	2000	Phosphorylation of the MP was decreased by addition of kinase inhibitors such as heparin, suramin and quercetin, which are known to be effective for casein kinase II (CK II).	Heparin	81-88	casein kinase 2 alpha 1	Homo sapiens	167-172
8604044-6	1996	Internal [Ca2+] is markedly and specifically increased by direct intracellular injection of NADH, and this effect is blocked by heparin, further implicating IP3R stores.	Heparin	128-135	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	157-161
7929392-5	1994	Both APLP1 and APLP2 bound heparin-Sepharose and had NaCl elution profiles similar to that of APP.	Heparin	27-34	amyloid beta precursor like protein 1	Homo sapiens	5-10
7929434-2	1994	The D-glucuronyl C-5 epimerase involved in the biosynthesis of heparin/heparan sulfate was purified from the high speed supernatant fraction of a homogenate of bovine liver by chromatography on immobilized O-desulfated heparin, red Sepharose, phenyl Sepharose, and concanavalin A-Sepharose.	Heparin	63-70	glucuronic acid epimerase	Bos taurus	4-30
8596049-5	1996	HPLC purification with subsequent N-terminal sequencing and mass spectrometric analysis showed that the heparin-binding Eo-chemotactic peak corresponded to the chemokine [Tyr-RANTES]66 that also contained [Ser-RANTES]68 as contaminant, whereas the nonheparin-binding activity was identified as granulocyte-macrophage CSF (GM-CSF) by the use of neutralizing Abs.	Heparin	104-111	C-C motif chemokine ligand 5	Homo sapiens	175-181
7929434-2	1994	The D-glucuronyl C-5 epimerase involved in the biosynthesis of heparin/heparan sulfate was purified from the high speed supernatant fraction of a homogenate of bovine liver by chromatography on immobilized O-desulfated heparin, red Sepharose, phenyl Sepharose, and concanavalin A-Sepharose.	Heparin	219-226	glucuronic acid epimerase	Bos taurus	4-30
10899436-8	2000	Several missense mutations also have a stimulatory effect on heparin-induced tau filament formation.	Heparin	61-68	microtubule associated protein tau	Homo sapiens	77-80
7929459-3	1994	Synthetic peptides corresponding to residues 8-26, 26-44, and 68-84 of AR were tested for their ability to compete for the binding of AR to immobilized heparin.	Heparin	152-159	amphiregulin	Homo sapiens	71-73
7929459-3	1994	Synthetic peptides corresponding to residues 8-26, 26-44, and 68-84 of AR were tested for their ability to compete for the binding of AR to immobilized heparin.	Heparin	152-159	amphiregulin	Homo sapiens	134-136
8596049-5	1996	HPLC purification with subsequent N-terminal sequencing and mass spectrometric analysis showed that the heparin-binding Eo-chemotactic peak corresponded to the chemokine [Tyr-RANTES]66 that also contained [Ser-RANTES]68 as contaminant, whereas the nonheparin-binding activity was identified as granulocyte-macrophage CSF (GM-CSF) by the use of neutralizing Abs.	Heparin	104-111	C-C motif chemokine ligand 5	Homo sapiens	210-216
8576258-7	1996	Analysis of the PC12 cells after the addition of FGF1 plus heparin or FGF2 demonstrated a significant increase in the level of FGF1 expression with the same time course as the appearance of the neuritic extensions.	Heparin	59-66	fibroblast growth factor 1	Rattus norvegicus	127-131
10898281-3	2000	A continuous infusion of antithrombin concentrate was used successfully, following failure of plasma, to correct the heparin resistance.	Heparin	117-124	serpin family C member 1	Homo sapiens	25-37
8780172-2	1996	Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF), is a 45 kD heparin-binding, endothelial cell (EC) specific mitogen with a putative N-linked glycosylation site.	Heparin	104-111	vascular endothelial growth factor A	Bos taurus	36-40
8780172-2	1996	Vascular endothelial growth factor (VEGF), also known as vascular permeability factor (VPF), is a 45 kD heparin-binding, endothelial cell (EC) specific mitogen with a putative N-linked glycosylation site.	Heparin	104-111	vascular endothelial growth factor A	Bos taurus	87-90
8772226-1	1995	Two forms of histidine-rich glycoprotein (HRG) were detected on SDS-PAGE by silver staining and immunoblotting after isolation of the protein from pooled plasma using immuno-affinity chromatography followed by chromatography with heparin-Sepharose.	Heparin	230-237	histidine rich glycoprotein	Homo sapiens	13-40
8772226-1	1995	Two forms of histidine-rich glycoprotein (HRG) were detected on SDS-PAGE by silver staining and immunoblotting after isolation of the protein from pooled plasma using immuno-affinity chromatography followed by chromatography with heparin-Sepharose.	Heparin	230-237	histidine rich glycoprotein	Homo sapiens	42-45
8578546-5	1995	Observations suggest that AT III may promote the release of PGl2 from endothelial cells by interacting with heparin-like glycosaminoglycans in vivo, consistent with previous observations in cultured endothelial cells.	Heparin	108-115	serpin family C member 1	Rattus norvegicus	26-32
7943290-5	1994	Treatment of proliferating endothelial cells with heparin (0-900 micrograms/ml) induced a dose-dependent decrease in endothelial HSPG content, whereas the fibronectin content was unaltered.	Heparin	50-57	CD44 molecule (Indian blood group)	Homo sapiens	129-133
7943290-10	1994	Our results indicate that heparin-induced loss of HSPG may cause the increase in endothelial permeability.	Heparin	26-33	CD44 molecule (Indian blood group)	Homo sapiens	50-54
7532447-6	1994	PCI-thrombin in the presence or absence of heparin bound plastic absorbed vitronectin, but neither PCI alone nor PCI-APC bound.	Heparin	43-50	vitronectin	Homo sapiens	74-85
7532447-7	1994	Vitronectin also decreased the inhibition rate of PCI-thrombin and PCI-APC in the presence of low concentrations of heparin.	Heparin	116-123	vitronectin	Homo sapiens	0-11
7899138-11	1994	We synthesized N-oleoyl heparin derivative (3 oleoyl groups/one molecule of heparin); such a lipophilic glycosaminoglycan (LipoGAG), although acting as an elastin protecting agent, possessed lower HNE inhibitory capacity as compared with heparin.	Heparin	24-31	elastin	Homo sapiens	155-162
7992254-1	1994	The common unfractionated heparin preparations (UFH) accelerate inhibition of most of the enzymes in the coagulation cascade, while low-molecular mass heparin (LMMH) mainly accelerates inhibition of activated coagulation factor X (FXa).	Heparin	151-158	coagulation factor X	Homo sapiens	209-229
7992254-5	1994	At a heparin concentration of 0.5 or 1.0 FXa-inhibiting IU/ml, the formation of TAT and FPA was substantial and always much more increased with LMMH than with UFH.	Heparin	5-12	coagulation factor X	Homo sapiens	41-44
8056513-7	1994	Furthermore, BRECs synthesize and secrete into their own culture medium a mitogen related to VAS-VEGF as far as two factors are concerned: chromatographic behavior on heparin-affinity columns, and cross-reactivity with recombinant VAS-VEGF to the binding to its receptors or antibodies.	Heparin	167-174	vascular endothelial growth factor A	Bos taurus	97-101
10898281-7	2000	This antithrombin variant has been previously reported (antithrombin Budapest 3) and results in reduced binding of heparin to antithrombin.	Heparin	115-122	serpin family C member 1	Homo sapiens	5-17
7932105-2	1994	We described an amidolytic method for determining the anticoagulant activity of commercially available low molecular-weight heparin (LMWH) with the use of factor Xa (FXa) and thrombin (FIIa), and a chromogenic peptidyl substrate, S-2222 or S-2238.	Heparin	124-131	coagulation factor X	Homo sapiens	155-164
7592779-7	1995	VEGF from conditioned medium of v-raf transformed NIH 3T3 cells was partially purified by chromatography on heparin-Sepharose.	Heparin	108-115	vascular endothelial growth factor A	Mus musculus	0-4
10898281-7	2000	This antithrombin variant has been previously reported (antithrombin Budapest 3) and results in reduced binding of heparin to antithrombin.	Heparin	115-122	serpin family C member 1	Homo sapiens	56-68
7578276-13	1995	The suppressive effects of OSF and heparin on LPS-induced PAI-1 release may result from the inhibition of LPS binding to the cell surface HSPG.	Heparin	35-42	syndecan 2	Homo sapiens	138-142
7932105-2	1994	We described an amidolytic method for determining the anticoagulant activity of commercially available low molecular-weight heparin (LMWH) with the use of factor Xa (FXa) and thrombin (FIIa), and a chromogenic peptidyl substrate, S-2222 or S-2238.	Heparin	124-131	coagulation factor X	Homo sapiens	166-169
10898281-7	2000	This antithrombin variant has been previously reported (antithrombin Budapest 3) and results in reduced binding of heparin to antithrombin.	Heparin	115-122	serpin family C member 1	Homo sapiens	56-68
10949727-6	2000	Mean finger blood flow recovery time improved, and serum levels of circulating ICAM-1, VCAM-1 and E-selectin were lower at completion of heparin therapy, but changes did not reach statistical significance.	Heparin	137-144	selectin E	Homo sapiens	98-108
8033893-4	1994	The two proteins both neutralized the antithrombin-III-dependent inhibitory activity of heparin.	Heparin	88-95	serpin family C member 1	Rattus norvegicus	38-54
7965660-9	1994	Caprylic (C8), capric (C10), lauric (C12), and stearic (C18) hydrazide derivatives of heparin were prepared using this approach.	Heparin	86-93	chromosome 12 open reading frame 57	Homo sapiens	23-26
8608187-10	1995	The results indicate that phospholipase A2 activation is involved in the phorbol ester-mediated increase in colony formation, since, of the different agents applied, only staurosporine, an inhibitor of protein kinase C, and mepacrine and heparin, putative inhibitors of phospholipase A2, were capable of abolishing phorbol ester-mediated effects.	Heparin	238-245	phospholipase A2, group IB, pancreas	Mus musculus	26-42
19002816-5	2000	One transgenic rabbit showed up to 3-foldincreased LPL activity in post-heparin plasma compared to thatin nontransgenic rabbits.	Heparin	72-79	lipoprotein lipase	Oryctolagus cuniculus	51-54
17147660-2	1995	A single subcutaneous injection of TGF-beta(2) in collagen/heparin gel carrier promoted markedly more extensive development of connective tissue than TGF-beta(1) at the site of injection in both neonatal and adult mice.	Heparin	59-66	hemoglobin, beta adult minor chain	Mus musculus	39-46
7559767-0	1995	Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1).	Heparin	0-7	integrin subunit alpha M	Homo sapiens	57-62
7559767-0	1995	Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1).	Heparin	0-7	integrin subunit alpha M	Homo sapiens	64-69
7559767-4	1995	Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans.	Heparin	0-7	integrin subunit alpha M	Homo sapiens	42-47
7559767-4	1995	Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans.	Heparin	0-7	integrin subunit alpha M	Homo sapiens	101-106
7559767-4	1995	Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated glycosaminoglycans.	Heparin	115-122	integrin subunit alpha M	Homo sapiens	101-106
8024582-0	1994	Butyrylcholinesterase amphiphilic forms of the mucosal cells of rat intestine bind heparin.	Heparin	83-90	butyrylcholinesterase	Rattus norvegicus	0-21
8024582-4	1994	Increasing concentrations of heparin resulted in higher sizes of heparin-BChE complex.	Heparin	29-36	butyrylcholinesterase	Rattus norvegicus	73-77
8024582-5	1994	These properties of intestinal BChE may be related to the possible occurrence of endogenous heparin in this tissue.	Heparin	92-99	butyrylcholinesterase	Rattus norvegicus	31-35
8013625-3	1994	In contrast, Mab V58A4 was shown to react with larger HBD fragments (50-60 kDa) that were present in platelet or endothelial cell extracts and could be retained on a heparin-Sepharose column at low salt concentrations.	Heparin	166-173	HBD	Homo sapiens	54-57
8203472-5	1994	By in situ hybridization, the transcripts for elastin nd biglycan were primarily localized to smooth muscle cells in the intima and were diminished by heparin in proportion to the decrease in intimal mass.	Heparin	151-158	elastin	Rattus norvegicus	46-53
8091393-6	1994	Heparin and sera from patients with HAT stimulated GT platelets in the same manner as determined by 14C-serotonin release and the changes in phosphorylation of p20 and p47.	Heparin	0-7	tubulin polymerization promoting protein family member 3	Homo sapiens	160-163
7559767-5	1995	Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1.	Heparin	62-69	integrin subunit alpha M	Homo sapiens	116-121
7632944-10	1995	Heparins with high and low antithrombin III affinities stimulated 45Ca release equally well.	Heparin	0-8	serpin family C member 1	Rattus norvegicus	27-43
11002391-8	2000	Inhibition experiments in SEM revealed uptake of heparin-plasma-treated SP via FcgammaRI on INFgamma-stimulated U937 cells, but could not exclude possible participation of CR3.	Heparin	49-56	Fc gamma receptor Ia	Homo sapiens	79-88
8533979-0	1995	Pharmacokinetics of heparin and its pharmacodynamic effect on plasma lipoprotein lipase activity and coagulation in healthy horses.	Heparin	20-27	lipoprotein lipase	Equus caballus	69-87
7622503-4	1995	Incubation of HGF with 0.1, 1.0, and 10 micrograms/ml of heparin, heparan sulfate, or dextran sulfate resulted in a concentration-dependent increase in mitogenic potency in a primary rat hepatocyte bioassay, whereas sodium sulfate or fucoidan did not.	Heparin	57-64	hepatocyte growth factor	Rattus norvegicus	14-17
7622503-6	1995	A series of chemically sulfated malto-oligosaccharides varying in unit size and charge was tested in the bioassay in order to provide additional insights into the nature of the HGF-heparin interaction.	Heparin	181-188	hepatocyte growth factor	Rattus norvegicus	177-180
8588942-7	1995	A high affinity heparin binding site was identified within a region conserved in rodent and human APP, APLP1 and APLP2.	Heparin	16-23	amyloid beta precursor like protein 1	Homo sapiens	103-108
8168536-2	1994	Heparin avidly bound cationic PLA2s including human secretory class II PLA2 and thereby inhibited their hydrolysis of phospholipids in the mixed micelles.	Heparin	0-7	phospholipase A2 group IIA	Homo sapiens	30-35
8168536-2	1994	Heparin avidly bound cationic PLA2s including human secretory class II PLA2 and thereby inhibited their hydrolysis of phospholipids in the mixed micelles.	Heparin	0-7	phospholipase A2 group IIA	Homo sapiens	30-34
8168536-3	1994	Initial velocity measurements indicated that heparin behaved as a competitive inhibitor for human secretory class II PLA2 and closely related A.h. blomhoffii PLA2 and A.p.	Heparin	45-52	phospholipase A2 group IIA	Homo sapiens	117-121
8168536-3	1994	Initial velocity measurements indicated that heparin behaved as a competitive inhibitor for human secretory class II PLA2 and closely related A.h. blomhoffii PLA2 and A.p.	Heparin	45-52	phospholipase A2 group IIA	Homo sapiens	158-162
8168536-5	1994	In particular, heparin showed the highest specificity for human secretory class II PLA2.	Heparin	15-22	phospholipase A2 group IIA	Homo sapiens	83-87
8168536-6	1994	In the absence of deoxycholic acid in mixed micelles, A.h. blomhoffii PLA2 was also strongly inhibited by heparin.	Heparin	106-113	phospholipase A2 group IIA	Homo sapiens	70-74
8168536-8	1994	Both kinetic measurements and fluorescence measurements of PLA2-bound 8-anilino-1-naphthalene sulfonate in the presence of varying amounts of heparin showed that a heparin molecule bound about seven molecules of PLA2.	Heparin	164-171	phospholipase A2 group IIA	Homo sapiens	59-63
8168536-8	1994	Both kinetic measurements and fluorescence measurements of PLA2-bound 8-anilino-1-naphthalene sulfonate in the presence of varying amounts of heparin showed that a heparin molecule bound about seven molecules of PLA2.	Heparin	164-171	phospholipase A2 group IIA	Homo sapiens	212-216
8168536-9	1994	When positive charges of four lysines in the amino-terminal region of A.h. blomhoffii PLA2 were neutralized by limited carbamoylation, heparin neither bound the carbamoylated A.h. blomhoffii PLA2 nor inhibited the hydrolysis of Triton X-100/dilauroylglycerophosphocholine mixed micelles by the carbamoylated A.h. blomhoffii PLA2 that retained 50% activity of native A.h. blomhoffii PLA2.	Heparin	135-142	phospholipase A2 group IIA	Homo sapiens	86-90
8168536-12	1994	These results indicate that the inhibition of human secretory class II PLA2 and related cationic PLA2s by heparin originates from the interaction of heparin with cationic residues in the amino-terminal region that forms a part of interfacial binding site.	Heparin	106-113	phospholipase A2 group IIA	Homo sapiens	71-75
8168536-12	1994	These results indicate that the inhibition of human secretory class II PLA2 and related cationic PLA2s by heparin originates from the interaction of heparin with cationic residues in the amino-terminal region that forms a part of interfacial binding site.	Heparin	106-113	phospholipase A2 group IIA	Homo sapiens	97-102
8168536-12	1994	These results indicate that the inhibition of human secretory class II PLA2 and related cationic PLA2s by heparin originates from the interaction of heparin with cationic residues in the amino-terminal region that forms a part of interfacial binding site.	Heparin	149-156	phospholipase A2 group IIA	Homo sapiens	71-75
8168536-12	1994	These results indicate that the inhibition of human secretory class II PLA2 and related cationic PLA2s by heparin originates from the interaction of heparin with cationic residues in the amino-terminal region that forms a part of interfacial binding site.	Heparin	149-156	phospholipase A2 group IIA	Homo sapiens	97-102
8168536-13	1994	In addition, unique structural features of human secretory class II PLA2, together with its unique mode of interaction with heparin, suggest that this PLA2 might have an additional heparin-binding site.	Heparin	124-131	phospholipase A2 group IIA	Homo sapiens	68-72
8168536-13	1994	In addition, unique structural features of human secretory class II PLA2, together with its unique mode of interaction with heparin, suggest that this PLA2 might have an additional heparin-binding site.	Heparin	124-131	phospholipase A2 group IIA	Homo sapiens	151-155
8168536-13	1994	In addition, unique structural features of human secretory class II PLA2, together with its unique mode of interaction with heparin, suggest that this PLA2 might have an additional heparin-binding site.	Heparin	181-188	phospholipase A2 group IIA	Homo sapiens	68-72
7637394-3	1995	We gave 2, 3, 5 and 5 mg/day/body of recombinant tissue plasminogen activator (tPA) followed by heparin and prostaglandin E1 (PGE1) effectively and without significant side effect on days 9, 10, 13 and 14, respectively.	Heparin	96-103	chromosome 20 open reading frame 181	Homo sapiens	49-77
7794926-9	1995	Heparin, which binds to CKII alpha, inhibited the binding of CKII to HSP90-Sepharose.	Heparin	0-7	casein kinase 2 alpha 2	Homo sapiens	24-34
10764763-1	2000	The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln.	Heparin	118-125	serpin family C member 1	Homo sapiens	44-56
7794926-12	1995	These results indicate that HSP90, DNA, and heparin compete with each other for binding to a common site of CKII alpha.	Heparin	44-51	casein kinase 2 alpha 2	Homo sapiens	108-118
7539103-6	1995	PKR variants completely lacking RBD-1 were largely unresponsive to dsRNA in activation assays but could be activated by heparin.	Heparin	120-127	eukaryotic translation initiation factor 2-alpha kinase 2	Mus musculus	0-3
7759497-8	1995	Plasma heparin-releasable LPL activity was 43% lower in +/- versus +/+ adult animals.	Heparin	7-14	lipoprotein lipase	Mus musculus	26-29
8029801-2	1994	We used this model to test the antithrombotic activity of the prothrombinase complex inhibitors factor rXai and its chemical analog glutamyl-glycyl-arginyl chloromethyl ketone inactivated human factor Xa (EGR-Xai), along with the thrombin inhibitors D-phenylalanyl-prolyl-arginyl chloromethyl ketone (PPACK) and heparin.	Heparin	312-319	coagulation factor X	Homo sapiens	194-203
8110198-1	1994	Neutrophil-membrane-associated NADPH-cytochrome c reductase and cytochrome b558 were separately eluted and highly purified by a combination of ion-exchange Sepharose, N-amino-octylagarose, 2",5"-ADP-Sepharose and heparin-Sepharose column chromatographies.	Heparin	213-220	mitochondrially encoded cytochrome b	Homo sapiens	64-76
7509344-2	1994	Vascular endothelial growth factor (VEGF) is a heparin-binding, endothelial cell-specific mitogen.	Heparin	47-54	vascular endothelial growth factor A	Oryctolagus cuniculus	0-34
7509344-2	1994	Vascular endothelial growth factor (VEGF) is a heparin-binding, endothelial cell-specific mitogen.	Heparin	47-54	vascular endothelial growth factor A	Oryctolagus cuniculus	36-40
10764763-2	2000	R129H and R129Q antithrombins bound pentasaccharide and full-length heparins containing the antithrombin recognition sequence with similar large reductions in affinity ranging from 400- to 2500-fold relative to the control serpin, corresponding to a loss of 28-35% of the binding free energy.	Heparin	68-76	serpin family C member 1	Homo sapiens	16-28
10764763-4	2000	Rapid kinetic studies showed that the mutation minimally affected the initial low affinity binding of heparin to antithrombin, but greatly affected the subsequent conformational activation of the serpin leading to high affinity heparin binding, although not enough to disfavor activation.	Heparin	102-109	serpin family C member 1	Homo sapiens	113-125
7749861-0	1995	Synthetic analogues of the antithrombin III-binding pentasaccharide sequence of heparin.	Heparin	80-87	serpin family C member 1	Rattus norvegicus	27-43
7749861-2	1995	The synthetic pentasaccharide Org 31540/SR 90107A represents the antithrombin III (ATIII) binding region of heparin and accelerates the ATIII-mediated inhibition of coagulation factor Xa.	Heparin	108-115	serpin family C member 1	Rattus norvegicus	65-81
10764763-4	2000	Rapid kinetic studies showed that the mutation minimally affected the initial low affinity binding of heparin to antithrombin, but greatly affected the subsequent conformational activation of the serpin leading to high affinity heparin binding, although not enough to disfavor activation.	Heparin	228-235	serpin family C member 1	Homo sapiens	113-125
7749861-2	1995	The synthetic pentasaccharide Org 31540/SR 90107A represents the antithrombin III (ATIII) binding region of heparin and accelerates the ATIII-mediated inhibition of coagulation factor Xa.	Heparin	108-115	serpin family C member 1	Rattus norvegicus	83-88
8300582-2	1994	HB-EGF and EGF appear to act on target cells utilizing the same receptor, but HB-EGF is distinguishable from EGF by its strong affinity for heparin.	Heparin	140-147	proheparin-binding EGF-like growth factor	Cricetulus griseus	78-84
8300582-4	1994	Mutagenesis and protease digestion studies of the recombinant HB-EGF, coupled with heparin-binding analyses of synthetic peptides, indicated that the sequences within HB-EGF mediating its interaction with heparin are located primarily in a stretch of 21 amino acids characterized by a high content of lysine and arginine residues.	Heparin	83-90	proheparin-binding EGF-like growth factor	Cricetulus griseus	167-173
10764763-5	2000	Consistent with these findings, the mutant antithrombin was normally activated by heparin for accelerated inhibition of factor Xa and thrombin.	Heparin	82-89	serpin family C member 1	Homo sapiens	43-55
8300582-4	1994	Mutagenesis and protease digestion studies of the recombinant HB-EGF, coupled with heparin-binding analyses of synthetic peptides, indicated that the sequences within HB-EGF mediating its interaction with heparin are located primarily in a stretch of 21 amino acids characterized by a high content of lysine and arginine residues.	Heparin	205-212	proheparin-binding EGF-like growth factor	Cricetulus griseus	62-68
8300582-4	1994	Mutagenesis and protease digestion studies of the recombinant HB-EGF, coupled with heparin-binding analyses of synthetic peptides, indicated that the sequences within HB-EGF mediating its interaction with heparin are located primarily in a stretch of 21 amino acids characterized by a high content of lysine and arginine residues.	Heparin	205-212	proheparin-binding EGF-like growth factor	Cricetulus griseus	167-173
7662509-9	1995	In both beta 2AR- and beta 1AR-expressing cells, heparin inhibited the reduction in Vmax and the PKA inhibitor blocked the increase in EC50.	Heparin	49-56	adrenoceptor beta 2	Homo sapiens	8-17
7538367-4	1995	Peptides of 18 amino acids were synthesized, corresponding to a common basic region of IGFBP-3 (P3), IGFBP-5 and IGFBP-6 (P6) which contained a heparin binding sequence.	Heparin	144-151	insulin like growth factor binding protein 6	Homo sapiens	113-120
8300582-5	1994	Most of this heparin-binding domain lies in an amino-terminal region of HB-EGF that has no counterpart in EGF, but a portion of the 21-residue sequence extends into the EGF-like region of HB-EGF.	Heparin	13-20	proheparin-binding EGF-like growth factor	Cricetulus griseus	72-78
10764763-6	2000	These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state.	Heparin	84-91	serpin family C member 1	Homo sapiens	106-118
8300582-5	1994	Most of this heparin-binding domain lies in an amino-terminal region of HB-EGF that has no counterpart in EGF, but a portion of the 21-residue sequence extends into the EGF-like region of HB-EGF.	Heparin	13-20	proheparin-binding EGF-like growth factor	Cricetulus griseus	188-194
8300582-6	1994	In addition, the mutagenesis and synthetic peptide studies indicated that sequences in HB-EGF lying outside of the 21-residue stretch can also influence the interaction with heparin.	Heparin	174-181	proheparin-binding EGF-like growth factor	Cricetulus griseus	87-93
10849447-11	2000	Recombinant ADAM 12-S partially purified from conditioned medium on a heparin-Sepharose column also proteolyzed IGFBP-3.	Heparin	70-77	insulin like growth factor binding protein 3	Homo sapiens	112-119
8300582-7	1994	Finally, a synthetic peptide derived from the 21-residue stretch was found to compete with HB-EGF for binding to Chinese hamster ovary cells, suggesting that the heparin-binding sequences in HB-EGF may also mediate the interaction of this factor with cell surface heparan sulfate proteoglycan.	Heparin	162-169	proheparin-binding EGF-like growth factor	Cricetulus griseus	91-97
8300582-7	1994	Finally, a synthetic peptide derived from the 21-residue stretch was found to compete with HB-EGF for binding to Chinese hamster ovary cells, suggesting that the heparin-binding sequences in HB-EGF may also mediate the interaction of this factor with cell surface heparan sulfate proteoglycan.	Heparin	162-169	proheparin-binding EGF-like growth factor	Cricetulus griseus	191-197
7734144-5	1994	Heparin augmented VEGF binding to KDR-expressing cells (ABAE and WM35), but inhibited VEGF binding to FLT1-expressing cells (SK-MEL-37 and WM9).	Heparin	0-7	kinase insert domain receptor	Homo sapiens	34-37
7510011-0	1994	Heparin potentiation of the effect of acidic fibroblast growth factor on astrocytes and neurons.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	38-69
7510011-2	1994	The effects of aFGF on both astrocytes and neurons were significantly potentiated by heparin.	Heparin	85-92	fibroblast growth factor 1	Rattus norvegicus	15-19
7510011-3	1994	The effect of aFGF (2 ng/ml) with heparin (10 mu g/ml) on the survival of neurons was a hundredfold more potent than that of aFGF (200 ng/ml) without heparin.	Heparin	34-41	fibroblast growth factor 1	Rattus norvegicus	14-18
7510011-3	1994	The effect of aFGF (2 ng/ml) with heparin (10 mu g/ml) on the survival of neurons was a hundredfold more potent than that of aFGF (200 ng/ml) without heparin.	Heparin	150-157	fibroblast growth factor 1	Rattus norvegicus	14-18
7899863-1	1994	Anti-Factor Xa methods have been generally accepted for the monitoring of heparin treatment, mainly due to their sensitivity to LMW heparin and excellent performance on automated equipment.	Heparin	74-81	coagulation factor X	Homo sapiens	5-14
7899863-1	1994	Anti-Factor Xa methods have been generally accepted for the monitoring of heparin treatment, mainly due to their sensitivity to LMW heparin and excellent performance on automated equipment.	Heparin	132-139	coagulation factor X	Homo sapiens	5-14
7629026-0	1995	Heparin-induced release of extracellular-superoxide dismutase form (V) to plasma.	Heparin	0-7	superoxide dismutase 3	Rattus norvegicus	27-61
7629026-2	1995	A prominent feature of EC-SOD is its affinity for heparin.	Heparin	50-57	superoxide dismutase 3	Rattus norvegicus	23-29
7629026-5	1995	of heparin/kg body weight into two healthy volunteers led to an immediate rise of serum EC-SOD level by 2.4-2.8-fold.	Heparin	3-10	superoxide dismutase 3	Rattus norvegicus	88-94
7629026-8	1995	The in vivo experiment using rats and an in vitro experiment strongly suggested the EC-SOD released into the plasma reconstituted the interaction with glycocalyx on the vascular endothelial cell surface in accordance with the elimination of heparin from the vascular system.	Heparin	241-248	superoxide dismutase 3	Rattus norvegicus	84-90
7649820-3	1995	The antiparasitic drug, suramin (a heparin analogue) inhibits binding of various growth factors (e.g. PDGF, bFGF, TGF-beta, EGF, IGF-I, IGF-II) to their receptors in vitro.	Heparin	35-42	insulin-like growth factor 2	Rattus norvegicus	136-142
8262929-11	1993	At optimal concentrations, the major mechanism of heparin action is also a reduction in the Ki of the initial encounter complex between factor Xa and rTFPI.	Heparin	50-57	coagulation factor X	Homo sapiens	136-145
10852711-0	2000	Interaction with heparin and matrix metalloproteinase 2 cleavage expose a cryptic anti-adhesive site of fibronectin.	Heparin	17-24	fibronectin 1	Mus musculus	104-115
8165607-6	1993	The plasma HRG of the proposita and 9 of her family members displayed abnormal binding to heparin, as assessed in a crossed affinity immuno-electrophoresis system: the usual increase in mobility after binding to heparin was absent.	Heparin	90-97	histidine rich glycoprotein	Homo sapiens	11-14
8165607-6	1993	The plasma HRG of the proposita and 9 of her family members displayed abnormal binding to heparin, as assessed in a crossed affinity immuno-electrophoresis system: the usual increase in mobility after binding to heparin was absent.	Heparin	212-219	histidine rich glycoprotein	Homo sapiens	11-14
7603970-3	1995	The activated thrombin was isolated by a single Heparin-Sepharose affinity chromatography step.	Heparin	48-55	coagulation factor II, thrombin	Bos taurus	14-22
10852711-1	2000	We recently found that fibronectin (FN) had a functional site [YTIYVIAL sequence in the heparin-binding domain 2 (Hep 2)] that was capable of suppressing the integrin-mediated cell adhesion to extracellular matrix.	Heparin	88-95	fibronectin 1	Mus musculus	23-34
10852711-1	2000	We recently found that fibronectin (FN) had a functional site [YTIYVIAL sequence in the heparin-binding domain 2 (Hep 2)] that was capable of suppressing the integrin-mediated cell adhesion to extracellular matrix.	Heparin	88-95	fibronectin 1	Mus musculus	36-38
7814368-4	1995	The folded protein was purified by heparin affinity chromatography and activated to thrombin with Echis carinatus snake venom.	Heparin	35-42	coagulation factor II, thrombin	Bos taurus	84-92
8306092-8	1993	The 111In-eosinophil accumulation induced by other inflammatory stimuli (compound 48/80, platelet activating factor, interleukin-8 and in a passive cutaneous anaphylaxis reaction) was also suppressed by locally-injected heparin.	Heparin	220-227	interleukin-8	Cavia porcellus	117-130
10852711-7	2000	Additionally, both the urea and heparin treatments made the Hep 2 fragment and intact FN much more accessible to the polyclonal antibody (alphaIII14A), with a recognition site near the anti-adhesive site of FN.	Heparin	32-39	fibronectin 1	Mus musculus	86-88
10852711-7	2000	Additionally, both the urea and heparin treatments made the Hep 2 fragment and intact FN much more accessible to the polyclonal antibody (alphaIII14A), with a recognition site near the anti-adhesive site of FN.	Heparin	32-39	fibronectin 1	Mus musculus	207-209
10997602-3	2000	In our laboratory we observed that a chronic infusion of Intralipid plus heparin in rats significantly decreased the insulin dependent-glucose uptake, as well as GLUT4 gene expression in muscular tissue.	Heparin	73-80	solute carrier family 2 member 4	Rattus norvegicus	162-167
7504009-1	1993	The multifunctional adhesive glycoprotein vitronectin (VN) undergoes a unique conformational transition from the plasma form into a multimeric form that represents the reactive heparin-binding form.	Heparin	177-184	vitronectin	Homo sapiens	42-53
7504009-1	1993	The multifunctional adhesive glycoprotein vitronectin (VN) undergoes a unique conformational transition from the plasma form into a multimeric form that represents the reactive heparin-binding form.	Heparin	177-184	vitronectin	Homo sapiens	55-57
7504009-3	1993	Time-dependent direct binding of radiolabeled VNmult to the luminal face of endothelial cells at 37 degrees C was observed which was competed by heparin, whereas plasma VN showed hardly any binding.	Heparin	145-152	vitronectin	Homo sapiens	46-48
7692967-0	1993	High molecular weight kininogen potentiates the heparin-accelerated inhibition of plasma kallikrein by antithrombin: role for antithrombin in the regulation of kallikrein.	Heparin	48-55	kallikrein related peptidase 4	Homo sapiens	89-99
7692967-1	1993	The effects of previously characterized interactions of high molecular weight kininogen (H-kininogen) with plasma kallikrein and with heparin on the regulation of kallikrein by the heparin-activated inhibitor, antithrombin, were investigated.	Heparin	134-141	kallikrein related peptidase 4	Homo sapiens	163-173
7692967-2	1993	H-kininogen, at levels sufficient to fully complex kallikrein, greatly potentiated the acceleration of antithrombin inhibition of kallikrein produced by heparin with high affinity for antithrombin.	Heparin	153-160	kallikrein related peptidase 4	Homo sapiens	51-61
7692967-2	1993	H-kininogen, at levels sufficient to fully complex kallikrein, greatly potentiated the acceleration of antithrombin inhibition of kallikrein produced by heparin with high affinity for antithrombin.	Heparin	153-160	kallikrein related peptidase 4	Homo sapiens	130-140
7692967-3	1993	At I = 0.15, pH 7.4, 25 degrees C, kininogen thus maximally increased the heparin enhancement of the second-order rate constant for the antithrombin-kallikrein reaction from 13-fold (1.6 x 10(2) M-1 s-1 to 2.1 x 10(3) M-1 s-1) to 1200-fold (1.9 x 10(5) M-1 s-1).	Heparin	74-81	kallikrein related peptidase 4	Homo sapiens	149-159
8118427-1	1993	A soluble protein kinase (PK) was purified from bovine and human follicular fluids (FF) by ultrafiltration through a PM-10 membrane followed by chromatography on heparin-agarose, DEAE-cellulose and cellulose phosphate columns.	Heparin	162-169	protein kinase cAMP-activated catalytic subunit beta	Bos taurus	10-24
8118427-1	1993	A soluble protein kinase (PK) was purified from bovine and human follicular fluids (FF) by ultrafiltration through a PM-10 membrane followed by chromatography on heparin-agarose, DEAE-cellulose and cellulose phosphate columns.	Heparin	162-169	protein kinase cAMP-activated catalytic subunit beta	Bos taurus	26-28
7888254-6	1995	When heparin was used in combination with tissue plasminogen activator, streptokinase, or urokinase at their therapeutic concentrations there was a significant inhibition of superoxide generation (70%, 30%, and 25%, respectively).	Heparin	5-12	chromosome 20 open reading frame 181	Homo sapiens	42-70
7813328-11	1995	Heparin presents an aspecific "nonfunctional" binding to plasma proteins such as fibrinogen, factor VIII, vitronectin, and fibronectin.	Heparin	0-7	vitronectin	Homo sapiens	106-117
8589511-3	1995	Cleaved, low affinity heparin (C-heparin) with factor Xa inhibition activity of 107 to 130 IU/mg, was prepared by partial deaminative cleavage of commercial crude heparin, and high-affinity heparin (HA-heparin) with factor Xa inhibition activity of 550 to 1000 IU/mg was prepared by fractionation of C-heparin using agarose-ATIII affinity chromatography.	Heparin	22-29	coagulation factor X	Homo sapiens	47-56
8589511-3	1995	Cleaved, low affinity heparin (C-heparin) with factor Xa inhibition activity of 107 to 130 IU/mg, was prepared by partial deaminative cleavage of commercial crude heparin, and high-affinity heparin (HA-heparin) with factor Xa inhibition activity of 550 to 1000 IU/mg was prepared by fractionation of C-heparin using agarose-ATIII affinity chromatography.	Heparin	22-29	coagulation factor X	Homo sapiens	216-225
8589511-3	1995	Cleaved, low affinity heparin (C-heparin) with factor Xa inhibition activity of 107 to 130 IU/mg, was prepared by partial deaminative cleavage of commercial crude heparin, and high-affinity heparin (HA-heparin) with factor Xa inhibition activity of 550 to 1000 IU/mg was prepared by fractionation of C-heparin using agarose-ATIII affinity chromatography.	Heparin	33-40	coagulation factor X	Homo sapiens	47-56
8589511-3	1995	Cleaved, low affinity heparin (C-heparin) with factor Xa inhibition activity of 107 to 130 IU/mg, was prepared by partial deaminative cleavage of commercial crude heparin, and high-affinity heparin (HA-heparin) with factor Xa inhibition activity of 550 to 1000 IU/mg was prepared by fractionation of C-heparin using agarose-ATIII affinity chromatography.	Heparin	33-40	coagulation factor X	Homo sapiens	47-56
8589511-3	1995	Cleaved, low affinity heparin (C-heparin) with factor Xa inhibition activity of 107 to 130 IU/mg, was prepared by partial deaminative cleavage of commercial crude heparin, and high-affinity heparin (HA-heparin) with factor Xa inhibition activity of 550 to 1000 IU/mg was prepared by fractionation of C-heparin using agarose-ATIII affinity chromatography.	Heparin	33-40	coagulation factor X	Homo sapiens	47-56
8589511-5	1995	Anticoagulant activity of the heparin immobilized surfaces was determined by chromogenic assay for the inhibition of factor Xa.	Heparin	30-37	coagulation factor X	Homo sapiens	117-126
7753456-0	1995	Monitoring of heparins in haemodialysis using an anti-factor-Xa-specific whole-blood clotting assay.	Heparin	14-22	coagulation factor X	Homo sapiens	54-63
7660139-12	1995	The apparent ED50 of heparin was found to be 4 times higher in the r-TF system.	Heparin	21-28	tissue factor	Oryctolagus cuniculus	69-71
8223431-6	1993	Both p31 and p27 bind quantitatively to heparin-Sepharose and can be displaced from the cell surface and extracellular matrix by soluble heparin.	Heparin	40-47	unconventional SNARE in the ER 1 homolog (S. cerevisiae)	Mus musculus	5-8
8223431-6	1993	Both p31 and p27 bind quantitatively to heparin-Sepharose and can be displaced from the cell surface and extracellular matrix by soluble heparin.	Heparin	40-47	cyclin-dependent kinase inhibitor 1B	Mus musculus	13-16
10809774-4	2000	We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region.	Heparin	183-190	serpin family C member 1	Homo sapiens	52-64
8167903-4	1993	Heparin (50 micrograms/ml) attenuated the induction by serum of bFGF mRNA, tPA mRNA, and tPA secretion.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	75-78
8167903-4	1993	Heparin (50 micrograms/ml) attenuated the induction by serum of bFGF mRNA, tPA mRNA, and tPA secretion.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	89-92
8167903-5	1993	Nonanticoagulant heparin also attenuated serum induction of bFGF and tPA mRNA levels.	Heparin	17-24	chromosome 20 open reading frame 181	Homo sapiens	69-72
7528103-5	1994	In two cell lines lacking endogenous heparan sulfate, exogenous heparin is required for FGFR dimerization, tyrosine kinase activation, c-fos mRNA transcription, and cell proliferation.	Heparin	64-71	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	135-140
7811385-7	1994	Furthermore, heparin, an inhibitor of biological activity of HGF, inhibited the mitogenic activity of 3T3-L1 CM.	Heparin	13-20	hepatocyte growth factor	Mus musculus	61-64
7891388-5	1994	Heparin-binding fractions of FCS obtained by heparin-Sepharose chromatography synergized with TGF-beta 1 and beta 2 to produce a mitogenic response.	Heparin	0-7	hemoglobin, beta adult minor chain	Mus musculus	109-115
7891388-5	1994	Heparin-binding fractions of FCS obtained by heparin-Sepharose chromatography synergized with TGF-beta 1 and beta 2 to produce a mitogenic response.	Heparin	45-52	hemoglobin, beta adult minor chain	Mus musculus	109-115
10809774-4	2000	We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region.	Heparin	284-291	serpin family C member 1	Homo sapiens	52-64
7693680-8	1993	A synthetic peptide comprising the central heparin binding region of VN (residues 348-361) not only bound to plasma VN but induced its multimerization also in plasma.	Heparin	43-50	vitronectin	Homo sapiens	69-71
7693680-8	1993	A synthetic peptide comprising the central heparin binding region of VN (residues 348-361) not only bound to plasma VN but induced its multimerization also in plasma.	Heparin	43-50	vitronectin	Homo sapiens	116-118
10809774-5	2000	The crystal structure resembles native antithrombin except in the hinge and heparin binding regions.	Heparin	76-83	serpin family C member 1	Homo sapiens	39-51
7525111-2	1994	Vascular endothelial growth factor (VEGF) is a heparin-binding, endothelial cell-specific mitogen.	Heparin	47-54	vascular endothelial growth factor A	Oryctolagus cuniculus	0-34
11096663-2	2000	Similarly, the low molecular weight heparin (LMWH), enoxaparin, has demonstrated superior efficacy when compared with unfractionated heparin (UFH) in the treatment of patients with non-ST elevation ACS.	Heparin	36-43	1-aminocyclopropane-1-carboxylate synthase homolog (inactive)	Homo sapiens	198-201
7525111-2	1994	Vascular endothelial growth factor (VEGF) is a heparin-binding, endothelial cell-specific mitogen.	Heparin	47-54	vascular endothelial growth factor A	Oryctolagus cuniculus	36-40
7929392-6	1994	As previously reported for APP, zinc increased the recovery of APLP1 and APLP2 upon heparin-Sepharose chromatography.	Heparin	84-91	amyloid beta precursor like protein 1	Homo sapiens	63-68
7929459-5	1994	Both soluble heparin and heparan sulfate inhibited AR-induced mitogenesis in MCF-10A human mammary epithelial cells with an IC50 of 5 and 2 micrograms/ml, respectively, whereas soluble chondroitin sulfate had only a slight inhibitory effect.	Heparin	13-20	amphiregulin	Homo sapiens	51-53
7918495-0	1994	Kinetics of the inhibition of factor Xa and the tissue factor-factor VIIa complex by the tissue factor pathway inhibitor in the presence and absence of heparin.	Heparin	152-159	coagulation factor X	Homo sapiens	30-39
7917699-2	1994	Recombinant tissue plasminogen activator was given locally into the proximal end of the shunt as two bolus injections of 0.1 mg/kg and two bolus injections of 0.2 mg/kg over 10 minutes, followed by a continuous infusion of 1.4 mg/kg/day for 16 hours and 0.7 mg/kg/day for 18 hours with systemic low dose heparin 5 IU/kg/h.	Heparin	304-311	chromosome 20 open reading frame 181	Homo sapiens	12-40
8408042-7	1993	Oligonucleotide ASGII also blocked the appearance of a heparin-releasable group II PLA2 in the culture supernatants of P388D1 cells.	Heparin	55-62	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	83-87
8408042-8	1993	The disappearance of this protein correlated with reduced PGE2 production by activated cells, indicating that an extracellular heparin-associated pool of group II PLA2 is involved in prostaglandin production by P388D1 cells.	Heparin	127-134	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	163-167
8292716-6	1993	Heparin and Ca2+ together, but not individually, enhance the rate of factor Xa inhibition by full-length TFPI.	Heparin	0-7	coagulation factor X	Homo sapiens	69-78
8292716-7	1993	The effect of heparin is concentration dependent and biphasic (maximal between 0.1 and 1.0 unit/ml) suggesting that the acceleration of factor Xa inhibition occurs at least in part through a "template" mechanism.	Heparin	14-21	coagulation factor X	Homo sapiens	136-145
7505345-9	1993	3) Inflammatory reactants such as fibrinogen, alpha 2-PI,alpha 2-macroglobulin and alpha 1-antitrypsin decreased more significantly during this heparin-urokinase-pulse combined therapy than during our previous combined therapy consisting of only heparin and urokinase.	Heparin	144-151	serpin family F member 2	Homo sapiens	46-56
8204123-11	1993	CONCLUSIONS: The findings of this large-scale trial indicate that accelerated t-PA given with intravenous heparin provides a survival benefit over previous standard thrombolytic regimens.	Heparin	106-113	chromosome 20 open reading frame 181	Homo sapiens	78-82
8344959-7	1993	Heparin and heparan sulfate, but not chondroitin sulfate, inhibited N-syndecan-bFGF binding.	Heparin	0-7	syndecan 3	Rattus norvegicus	68-78
8013074-0	1994	Heparin decreases activator protein-1 binding to DNA in part by posttranslational modification of Jun B.	Heparin	0-7	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	18-37
10777674-3	2000	The affinity of the C-terminal domain for heparin was about 500-fold lower than that of full-length LPL (K(d) = 1.3 microM compared to 3.1 nM).	Heparin	42-49	lipoprotein lipase	Homo sapiens	100-103
8013074-4	1994	Treatment of cells with heparin suppresses the expression of Jun B, one of the components of AP-1.	Heparin	24-31	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	93-97
7507412-3	1993	Vitronectin fragments obtained by formic acid cleavage were separated by heparin-affinity chromatography followed by gel filtration chromatography.	Heparin	73-80	vitronectin	Homo sapiens	0-11
7507412-8	1993	These results indicate that there are two collagen-binding sites in the vitronectin molecule; one located close to the heparin-binding domain in the COOH-terminal half and the other located in the NH2-terminal half of vitronectin.	Heparin	119-126	vitronectin	Homo sapiens	72-83
10777674-7	2000	We conclude that the C-terminal folding domain contributes only moderately to the heparin affinity of full-length LPL, whereas the domain appears important for tethering triglyceride-rich lipoproteins to heparin-bound LPL.	Heparin	82-89	lipoprotein lipase	Homo sapiens	114-117
10764593-3	2000	Furthermore, NAP-1 and NAP-2 phosphorylation in crude HeLa cell extracts is abolished by heparin, a specific inhibitor of CKII.	Heparin	89-96	casein kinase 2 alpha 1	Homo sapiens	122-126
8325382-4	1993	DRP was purified from the high alkaline extract of lung membranes using heparin-agarose column chromatography followed by anti-DRP immunoaffinity column chromatography.	Heparin	72-79	utrophin	Homo sapiens	0-3
10725457-5	2000	We report here that hsp40, hsp60, hsc70, hsp70, hsp84, hsp86, and gp96 (grp94) but not BiP (grp78) and calreticulin can be separated from a single tumor sample in one step using heparin-agarose chromatography.	Heparin	178-185	heat shock protein 90 alpha family class B member 1	Homo sapiens	48-53
8252580-3	1993	To test the hypothesis that the antiproliferative effect of heparin in vivo may be related to an inhibition of proto-oncogene expression, the effects of pretreatment with heparin on the expression of the c-myc, c-fos and c-jun proto-oncogenes were examined in a rabbit model of balloon denudation.	Heparin	171-178	myc proto-oncogene protein	Oryctolagus cuniculus	204-209
10735780-3	2000	We examined the expression of a secretion marker (P-selectin) and an aggregation marker (activated fibrinogen receptor GP IIb-IIIa) on normal platelets in response to heparin, heparinase 1, and protamine in vitro using whole blood flow cytometry.	Heparin	167-174	selectin P	Homo sapiens	50-60
7685013-2	1993	Previous studies have demonstrated that the conformationally altered, heparin binding form of vitronectin is removed from the matrix by receptor-mediated endocytosis and degraded through a lysosomal pathway (Panetti, T. S., and McKeown-Longo, P. J.	Heparin	70-77	vitronectin	Homo sapiens	94-105
10735780-4	2000	Unfractionated heparin increased adenosine diphosphate-induced expression of P-selectin and GP IIb-IIIa in a dose-dependent manner.	Heparin	15-22	selectin P	Homo sapiens	77-87
7685028-1	1993	Vitronectin is a structurally labile molecule with a native, non-heparin binding form and a conformationally altered, heparin binding form.	Heparin	65-72	vitronectin	Homo sapiens	0-11
10735780-8	2000	In contrast, protamine antagonized the effect of heparin on GP IIb-IIIa expression but potentiated the effect of heparin on P-selectin expression.	Heparin	113-120	selectin P	Homo sapiens	124-134
7685028-1	1993	Vitronectin is a structurally labile molecule with a native, non-heparin binding form and a conformationally altered, heparin binding form.	Heparin	118-125	vitronectin	Homo sapiens	0-11
7685028-7	1993	Heparin and thrombospondin inhibited the degradation of altered vitronectin.	Heparin	0-7	vitronectin	Homo sapiens	64-75
10760814-9	2000	We show that FHL-1 presents a higher binding affinity for S. pyogenes than factor H because it carries a hydrophobic, high-affinity, GAS binding site in addition to the heparin binding site in SCR7.	Heparin	169-176	four and a half LIM domains 1	Homo sapiens	13-18
7685028-8	1993	The degradation of native vitronectin was induced by addition of gamma-thrombin which exposes vitronectin"s cryptic heparin-binding domain.	Heparin	116-123	vitronectin	Homo sapiens	26-37
7685028-8	1993	The degradation of native vitronectin was induced by addition of gamma-thrombin which exposes vitronectin"s cryptic heparin-binding domain.	Heparin	116-123	vitronectin	Homo sapiens	94-105
8100744-4	1993	The baseline expression of CD11b and CD18 on unstimulated neutrophils was similar in heparin and EDTA anti-coagulated blood but the response to activation with fMLP was significantly less for the EDTA anti-coagulated samples (p &lt; 0.01 in paired t-test).	Heparin	85-92	integrin subunit alpha M	Homo sapiens	27-32
8509711-8	1993	The addition of heparin to J774 cells resulted in a 6-fold increase in lipoprotein lipase (LPL) activity in the media, and significantly enhanced the ability of Type IV VLDL to induce cellular triglyceride accumulation (P &lt; 0.01), but significantly decreased cellular cholesteryl ester content (P &lt; 0.025).	Heparin	16-23	lipoprotein lipase	Mus musculus	71-89
8509711-8	1993	The addition of heparin to J774 cells resulted in a 6-fold increase in lipoprotein lipase (LPL) activity in the media, and significantly enhanced the ability of Type IV VLDL to induce cellular triglyceride accumulation (P &lt; 0.01), but significantly decreased cellular cholesteryl ester content (P &lt; 0.025).	Heparin	16-23	lipoprotein lipase	Mus musculus	91-94
10762062-6	2000	In the presence of CKII inhibitor, heparin or poly(Glu.Tyr), both phosphorylation and enhancement of phosphatase activity of CPTP1 and HPTP1B were mostly blocked.	Heparin	35-42	casein kinase 2 alpha 1	Homo sapiens	19-23
8466349-7	1993	There was a significant reduction of C3a generation after protamine administration in patients perfused with heparin-coated circuits, and there was a decrease of complement hemolytic capacity in pooled human serum incubated with heparin-coated tubing.	Heparin	109-116	complement C3	Homo sapiens	37-40
10715105-3	2000	The mutation was selective as demonstrated by normal activation and inhibition, except in the presence of subsaturating heparin where the rate of inhibition by antithrombin III (ATIII) was 15% of normal.	Heparin	120-127	serpin family C member 1	Homo sapiens	160-176
7682219-5	1993	A related sequence, KKQRFRHRNRKG, present in the heparin-binding domain of an alpha v beta 5 ligand, vitronectin, also bound alpha v beta 5 in affinity chromatography and, in combination with an RGD peptide, was an inhibitor of cell attachment to vitronectin.	Heparin	49-56	vitronectin	Homo sapiens	101-112
7682219-5	1993	A related sequence, KKQRFRHRNRKG, present in the heparin-binding domain of an alpha v beta 5 ligand, vitronectin, also bound alpha v beta 5 in affinity chromatography and, in combination with an RGD peptide, was an inhibitor of cell attachment to vitronectin.	Heparin	49-56	vitronectin	Homo sapiens	247-258
8469925-4	1993	Biochemical characterization revealed that the IgG2b inducing activity in RA-SF has the following properties: it is a protein, sensitive to pH &gt; 11 and &lt; 4, which is precipitated by 50% of saturated ammonium sulphate and has a molecular weight of 50-70 kDa; it binds to Cibacron-blue and heparin and its activity is not mediated by immunoglobulins or immune complexes, which are present in RA-SF.	Heparin	294-301	immunoglobulin heavy constant gamma 2B	Mus musculus	47-52
10715105-3	2000	The mutation was selective as demonstrated by normal activation and inhibition, except in the presence of subsaturating heparin where the rate of inhibition by antithrombin III (ATIII) was 15% of normal.	Heparin	120-127	serpin family C member 1	Homo sapiens	178-183
8454634-3	1993	As a prerequisite, we analyzed the optimal conditions for DNA binding of the PBP by assaying the stability of the interaction against increasing concentrations of salt, dithiothreitol, and heparin.	Heparin	189-196	phosphatidylethanolamine binding protein 1	Homo sapiens	77-80
10879181-2	2000	The result showed that the chemical magnifying effect of PEG improved the grafting of heparin on the material surface.	Heparin	86-93	progestagen associated endometrial protein	Homo sapiens	57-60
8388347-5	1993	Heparin increases the rate of inactivation of FXa and of tissue factor-F VIIa by TFPI.	Heparin	0-7	coagulation factor X	Homo sapiens	46-49
8478044-0	1993	Heparin has an inhibitory effect on endothelin-1 synthesis and release by endothelial cells.	Heparin	0-7	endothelin 1	Bos taurus	36-48
10681554-6	2000	To distinguish between binding to monomeric (inactive) and dimeric (catalytically active) forms of LPL, affinity chromatography on heparin columns was conducted, which showed that native LDL bound to the monomeric LPL, whereas oxidized LDL, irrespective of the type of modification (Cu(2+), 2, 2"-azobis(2-amidinopropane)hydrochloride, hypochlorite, or soybean 15-lipoxygenase), bound preferably to dimeric LPL.	Heparin	131-138	lipoprotein lipase	Homo sapiens	99-102
8478044-1	1993	We studied the inhibitory effects of heparin on basal and agonist-induced endothelin-1 biosynthesis and release from cultured bovine endothelial cells.	Heparin	37-44	endothelin 1	Bos taurus	74-86
8478044-2	1993	Heparin dose-dependently and similarly inhibited endothelin-1 release, inositol trisphosphate production, and intracellular free Ca2+ levels stimulated by thrombin.	Heparin	0-7	endothelin 1	Bos taurus	49-61
8478044-2	1993	Heparin dose-dependently and similarly inhibited endothelin-1 release, inositol trisphosphate production, and intracellular free Ca2+ levels stimulated by thrombin.	Heparin	0-7	coagulation factor II, thrombin	Bos taurus	155-163
8478044-4	1993	Heparin completely blocked phorbol ester-induced endothelin-1 release, whereas it had a partial inhibitory effect on endothelin-1 release stimulated by angiotensin and vasopressin.	Heparin	0-7	endothelin 1	Bos taurus	49-61
8478044-5	1993	Northern blot analysis using complementary DNA for bovine preproendothelin-1 as a probe revealed that heparin reduced not only the basal but also the stimulated expression of preproendothelin-1 messenger RNA by thrombin and phorbol ester.	Heparin	102-109	endothelin 1	Bos taurus	58-76
8478044-5	1993	Northern blot analysis using complementary DNA for bovine preproendothelin-1 as a probe revealed that heparin reduced not only the basal but also the stimulated expression of preproendothelin-1 messenger RNA by thrombin and phorbol ester.	Heparin	102-109	endothelin 1	Bos taurus	175-193
8478044-5	1993	Northern blot analysis using complementary DNA for bovine preproendothelin-1 as a probe revealed that heparin reduced not only the basal but also the stimulated expression of preproendothelin-1 messenger RNA by thrombin and phorbol ester.	Heparin	102-109	coagulation factor II, thrombin	Bos taurus	211-219
8478044-6	1993	These data suggest that heparin, in addition to its antithrombin effect, has an inhibitory effect on the biosynthesis and release of endothelin-1, possibly by inhibiting protein kinase C-dependent pathway.	Heparin	24-31	endothelin 1	Bos taurus	133-145
10660541-0	2000	The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III.	Heparin	81-88	serpin family C member 1	Homo sapiens	185-201
10660541-0	2000	The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III.	Heparin	153-160	serpin family C member 1	Homo sapiens	185-201
8470045-2	1993	Heparin was used to accelerate the inhibition of thrombin by antithrombin III, and annexin V was used to inhibit the assembly of the prothrombinase complex on phospholipid surfaces, thereby blocking thrombin generation.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	49-57
8470045-2	1993	Heparin was used to accelerate the inhibition of thrombin by antithrombin III, and annexin V was used to inhibit the assembly of the prothrombinase complex on phospholipid surfaces, thereby blocking thrombin generation.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	65-73
10665801-11	2000	Since heparin reduced paw oedema induced by PLA2 from Naja mocambique mocambique venom it is likely that this sPLA2 is similar to the novel heparin-sensitive PLA2 found in mast cells.	Heparin	6-13	phospholipase A2	Apis mellifera	44-48
8361901-4	1993	The authors suggest that such a course of this interaction results from the stimulating action of heparin added in adequate concentration on protein release from platelet alpha granulations--which bound GP II b/III a complex with collagen.	Heparin	98-105	integrin subunit alpha 2b	Homo sapiens	203-210
7507688-5	1993	Activity was further defined as fibroblast growth factor (FGF)-like by its strong affinity to heparin, partial neutralisation by antibodies to acidic FGF (aFGF) and partial co-elution with aFGF on salt elution from heparin.	Heparin	215-222	fibroblast growth factor 1	Rattus norvegicus	189-193
8362268-3	1993	In the plasma-based assays, heparin exhibited strong inhibition in both thrombin and Factor Xa-based assays, whereas pentasaccharide was only active in Factor Xa-based assays and lactobionic acid was only active in thrombin-based assays.	Heparin	28-35	coagulation factor X	Homo sapiens	85-94
8362268-4	1993	In the AT III supplemented systems, heparin was able to inhibit strongly both Factor Xa and thrombin, while pentasaccharide could only inhibit Factor Xa.	Heparin	36-43	coagulation factor X	Homo sapiens	78-87
10665801-11	2000	Since heparin reduced paw oedema induced by PLA2 from Naja mocambique mocambique venom it is likely that this sPLA2 is similar to the novel heparin-sensitive PLA2 found in mast cells.	Heparin	6-13	phospholipase A2	Apis mellifera	111-115
10632394-7	2000	In the experiment with plasma proteins, the PRT and APTT were significantly prolonged for both the heparin-immobilized PET (PET-He) and the PET-I-H, suggesting the binding of immobilized heparin to antithrombin III.	Heparin	99-106	serpin family C member 1	Homo sapiens	198-214
1334488-10	1992	Heparin blocks kallistatin"s complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein"s activity.	Heparin	0-7	serpin family A member 4	Homo sapiens	15-26
1443139-6	1992	In the presence of excess HGF, the heparin-washable 125I-HGF, the heparin-resistant and acid-washable 125I-HGF, and the internalized 125I-HGF dropped to 54, 31, and 32% of the control values.	Heparin	35-42	hepatocyte growth factor	Rattus norvegicus	26-29
1443139-6	1992	In the presence of excess HGF, the heparin-washable 125I-HGF, the heparin-resistant and acid-washable 125I-HGF, and the internalized 125I-HGF dropped to 54, 31, and 32% of the control values.	Heparin	35-42	hepatocyte growth factor	Rattus norvegicus	57-60
10632394-7	2000	In the experiment with plasma proteins, the PRT and APTT were significantly prolonged for both the heparin-immobilized PET (PET-He) and the PET-I-H, suggesting the binding of immobilized heparin to antithrombin III.	Heparin	187-194	serpin family C member 1	Homo sapiens	198-214
1443139-6	1992	In the presence of excess HGF, the heparin-washable 125I-HGF, the heparin-resistant and acid-washable 125I-HGF, and the internalized 125I-HGF dropped to 54, 31, and 32% of the control values.	Heparin	35-42	hepatocyte growth factor	Rattus norvegicus	57-60
1443139-6	1992	In the presence of excess HGF, the heparin-washable 125I-HGF, the heparin-resistant and acid-washable 125I-HGF, and the internalized 125I-HGF dropped to 54, 31, and 32% of the control values.	Heparin	35-42	hepatocyte growth factor	Rattus norvegicus	57-60
10958381-11	2000	Only heparin inhibited both MMP-1 and MMP-2/MMP-9 activity.	Heparin	5-12	matrix metallopeptidase 1	Homo sapiens	28-33
1443139-6	1992	In the presence of excess HGF, the heparin-washable 125I-HGF, the heparin-resistant and acid-washable 125I-HGF, and the internalized 125I-HGF dropped to 54, 31, and 32% of the control values.	Heparin	66-73	hepatocyte growth factor	Rattus norvegicus	26-29
1443139-7	1992	The presence of at least two binding sites for HGF on the liver cell surfaces was made clear: the heparin-washable site and the heparin-resistant and acid-washable binding site, considered to have higher affinity for HGF.	Heparin	98-105	hepatocyte growth factor	Rattus norvegicus	47-50
1443139-7	1992	The presence of at least two binding sites for HGF on the liver cell surfaces was made clear: the heparin-washable site and the heparin-resistant and acid-washable binding site, considered to have higher affinity for HGF.	Heparin	128-135	hepatocyte growth factor	Rattus norvegicus	47-50
10958381-13	2000	The ability of heparin to inhibit fibroblast chemotaxis may account for the inhibitory effect of heparin on MMP activity.	Heparin	15-22	matrix metallopeptidase 1	Homo sapiens	108-111
1522124-0	1992	Heparin inhibition of autonomous growth implicates amphiregulin as an autocrine growth factor for normal human mammary epithelial cells.	Heparin	0-7	amphiregulin	Homo sapiens	51-63
10958381-13	2000	The ability of heparin to inhibit fibroblast chemotaxis may account for the inhibitory effect of heparin on MMP activity.	Heparin	97-104	matrix metallopeptidase 1	Homo sapiens	108-111
1522124-5	1992	The EGF-independent growth of HMECs was blocked by the addition of heparin or a monoclonal anti-EGF receptor antibody to the culture medium, implicating AR as an autocrine growth mediator.	Heparin	67-74	amphiregulin	Homo sapiens	153-155
10736978-10	2000	), of the reduced stay in the Intensive Care Unit, of the riduced risk involved with problems of bleeding and the need of repeated operative procedures make this method fundamental in patients with reduced plasma levels of ATIII such as coronary patients who are under heparin treatment for several days.	Heparin	269-276	serpin family C member 1	Homo sapiens	223-228
1503326-14	1992	CONCLUSION: Low-molecular-weight heparinoid, given in a fixed dose of 750 anti-factor Xa units subcutaneously twice daily, is more effective than subcutaneous low-dose heparin for the prevention of deep vein thrombosis in patients with acute ischemic stroke.	Heparin	33-40	coagulation factor X	Homo sapiens	79-88
11098115-3	2000	wt carboxyl-terminal heparin-binding domain of fibronectin.	Heparin	21-28	fibronectin 1	Rattus norvegicus	47-58
1507222-5	1992	Here, we describe that, in vitro and with the non-hydrolyzable analogue ATP gamma S, RNA and heparin can also induce both the structural transition and the enzymatic activation of RecA to LexA cleavage in accordance with the model.	Heparin	93-100	RAD51 recombinase	Homo sapiens	180-184
10577463-2	1999	Antithrombin therapy with unfractionated heparin has several important disadvantages, such as a variable anticoagulant effect, sensitivity to platelet factor 4, an inability to inhibit clot-bound thrombin, and the potential to cause thrombocytopenia.	Heparin	41-48	serpin family C member 1	Homo sapiens	0-12
1433988-4	1992	The deleted form of recombinant HGF (rHGF) had slightly lower heparin binding affinity than the intact form.	Heparin	62-69	hepatocyte growth factor	Rattus norvegicus	37-41
10611948-6	1999	Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities.	Heparin	65-72	serpin family C member 1	Homo sapiens	33-38
1322691-2	1992	The anti-factor Xa and anti-thrombin activities were measured directly, by assessing the heparin-dependent pseudo-first order rate constants of inactivation of human factor Xa or thrombin.	Heparin	89-96	coagulation factor X	Homo sapiens	166-175
1322691-5	1992	That is, 1.5 mM calcium stimulated the UF standard heparin-catalysed inactivation of factor Xa 2.1-2.4 times.	Heparin	51-58	coagulation factor X	Homo sapiens	85-94
1322691-7	1992	Thus, the largest effects of calcium in the inactivation reaction of factor Xa is seen with UF standard heparin.	Heparin	104-111	coagulation factor X	Homo sapiens	69-78
1376146-1	1992	The present study describes that the collagen-binding activity of vitronectin in human serum increases by treatment with heparin, heating and urea.	Heparin	121-128	vitronectin	Homo sapiens	66-77
1376146-4	1992	Endogenous vitronectin in human serum became considerably bound to collagen when the serum was boiled in 4-8 M urea for 5 min and mixed with heparin (0.5-5 micrograms/ml).	Heparin	141-148	vitronectin	Homo sapiens	11-22
1373506-4	1992	The specificity of the immunological cross-reactivity of Vn-F to rabbit polyclonal antibodies made to human Vn is demonstrated by competition experiments using pure human Vn and monospecific antibodies generated toward Vn-F. Vn-F possesses affinities for glass and heparin that are identical to those of human Vn.	Heparin	265-272	vitronectin	Homo sapiens	57-59
1311318-7	1992	We found that heparin, a beta ARK inhibitor, ablated short term agonist-induced desensitization of alpha 2AAR, while such desensitization was unaffected by inhibition of protein kinase A.	Heparin	14-21	adrenoceptor alpha 2A	Homo sapiens	99-109
10611948-6	1999	Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities.	Heparin	65-72	serpin family C member 1	Homo sapiens	84-89
10611948-6	1999	Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities.	Heparin	129-136	serpin family C member 1	Homo sapiens	33-38
1582998-1	1992	We previously demonstrated that human keratinocyte cultures proliferate in the absence of polypeptide growth factors (autonomous growth) and that this autonomous growth is blocked by interaction of heparin with a human keratinocyte-derived autocrine factor (KAF) which we identified as amphiregulin (AR).	Heparin	198-205	amphiregulin	Homo sapiens	286-298
1582998-1	1992	We previously demonstrated that human keratinocyte cultures proliferate in the absence of polypeptide growth factors (autonomous growth) and that this autonomous growth is blocked by interaction of heparin with a human keratinocyte-derived autocrine factor (KAF) which we identified as amphiregulin (AR).	Heparin	198-205	amphiregulin	Homo sapiens	300-302
10611948-6	1999	Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities.	Heparin	129-136	serpin family C member 1	Homo sapiens	84-89
10636462-3	1999	The efficacy of UTM on thromboplastin-induced disseminated intravascular coagulation produced in ATIII-decreased rats was almost the same as that in normal rats, whereas unfractionated (UF)-heparin remarkably diminished its effect in ATIII-decreased rats.	Heparin	190-197	serpin family C member 1	Homo sapiens	234-239
1370815-0	1992	Binding of vitronectin-thrombin-antithrombin III complex to human endothelial cells is mediated by the heparin binding site of vitronectin.	Heparin	103-110	vitronectin	Homo sapiens	11-22
1370815-0	1992	Binding of vitronectin-thrombin-antithrombin III complex to human endothelial cells is mediated by the heparin binding site of vitronectin.	Heparin	103-110	vitronectin	Homo sapiens	127-138
10607857-8	1999	The biological potencies of these compounds were assessed in ex vivo experiments where their ability to compete with antithrombin for binding heparin was determined.	Heparin	142-149	serpin family C member 1	Homo sapiens	117-129
1730778-0	1992	Lymphocyte CD44 binds the COOH-terminal heparin-binding domain of fibronectin.	Heparin	40-47	CD44 molecule (Indian blood group)	Homo sapiens	11-15
10581250-5	1999	Furthermore, CypA binds directly to heparan via a domain rich in basic residues similar to known heparin-binding motifs.	Heparin	97-104	peptidylprolyl isomerase A	Homo sapiens	13-17
1730778-15	1992	Moreover, inhibition studies showed that binding of a lymphoblastoid cell line, KCA, to heparin binding peptides from COOH-terminal heparin binding fragment of fibronectin was mediated via CD44.	Heparin	88-95	CD44 molecule (Indian blood group)	Homo sapiens	189-193
1579892-1	1992	Using biochemically defined conditions on a fast kinetic centrifugal analyzer the effect of recombinant hirudin (rH) and unfractionated heparin (UH) on thrombin and factor Xa generation was investigated.	Heparin	136-143	coagulation factor X	Homo sapiens	165-174
10600487-4	1999	Heparin, an inhibitor of VSMC proliferation, inhibited the serum-induced loss of caveolin-1 and caveolin-2.	Heparin	0-7	caveolin 2	Homo sapiens	96-106
1554154-3	1992	Their results show that HRG, like PF 4, has an affinity, not only for heparin, but also for DS.	Heparin	70-77	histidine rich glycoprotein	Homo sapiens	24-27
10600487-5	1999	In addition, heparin caused an increase in both caveolin-1 and caveolin-2 localization to caveolae-enriched sucrose gradient membrane fractions when compared to serum alone.	Heparin	13-20	caveolin 2	Homo sapiens	63-73
10562536-0	1999	Structural basis and potential role of heparin/heparan sulfate binding to the angiogenesis inhibitor endostatin.	Heparin	39-46	collagen type XVIII alpha 1 chain	Homo sapiens	101-111
1283855-3	1992	Oral treatment with aFGF, in the presence of heparin, reduced (ED50 value = 30.2 micrograms/kg/day) the acetic-acid-induced gastric ulcer area, when assessed 1 week later.	Heparin	45-52	fibroblast growth factor 1	Rattus norvegicus	20-24
1340207-7	1992	Chondrocyte-conditioned medium increased endothelial cell proliferation in vitro (a specific bio-assay for basic FGF and related peptides); and the mitogenic activity was removed from conditioned medium by incubation with heparin-Sepharose demonstrating that this was due to heparin-binding protein(s).	Heparin	222-229	azurocidin 1	Homo sapiens	275-298
1730747-15	1992	In the present report, we show that heparin selectively repressed TPA-inducible AP-1-mediated gene expression.	Heparin	36-43	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	80-84
10562536-4	1999	Analyses with various heparin fragments demonstrated a minimum size (12mer) for efficient binding to endostatin and a crucial role of 2-O- and 6-O-sulfation.	Heparin	22-29	collagen type XVIII alpha 1 chain	Homo sapiens	101-111
1730747-17	1992	Inhibition of AP-1-mediated trans-activation occurred with heparin and pentosan polysulfate but not with chondroitin sulfate A or C. Heparin-binding peptides or heparitinase I addition to nuclear lysates of heparin-treated cells allowed enhanced recovery of endogenous AP-1-specific DNA binding activity.	Heparin	59-66	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	14-18
8006018-3	1994	Addition of heparin prior to or after agonist stimulation inhibited the release, indicating the activation of the Ins-1,4,5-P3-dependent Ca2+ channels by the agonist.	Heparin	12-19	forkhead box M1	Homo sapiens	114-119
1730747-17	1992	Inhibition of AP-1-mediated trans-activation occurred with heparin and pentosan polysulfate but not with chondroitin sulfate A or C. Heparin-binding peptides or heparitinase I addition to nuclear lysates of heparin-treated cells allowed enhanced recovery of endogenous AP-1-specific DNA binding activity.	Heparin	207-214	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	14-18
10553008-3	1999	The hypothesis that cld, like lec23, affects the folding/assembly of nascent LPL was confirmed by showing that in cell lines homozygous for these mutations (Cld and Lec23, respectively), the majority of LPL was inactive, displayed heterogeneous aggregation, and had a decreased affinity for heparin.	Heparin	291-298	lipase maturation factor 1	Mus musculus	20-23
8189220-13	1994	Collectively, these results suggest that heparin-Sepharose chromatography can efficiently separate two pharmacologically, biochemically and immunologically distinct populations of AT2 receptors.	Heparin	41-48	serine (or cysteine) peptidase inhibitor, clade B, member 9d	Mus musculus	180-183
8085247-1	1994	Heparin (HEP) prevents thrombus formation (TF) and thrombus growth (TG), by accelerating thrombin (THR) inhibition by antithrombin III (ATIII).	Heparin	0-7	prothrombin	Oryctolagus cuniculus	89-97
8085247-1	1994	Heparin (HEP) prevents thrombus formation (TF) and thrombus growth (TG), by accelerating thrombin (THR) inhibition by antithrombin III (ATIII).	Heparin	9-12	prothrombin	Oryctolagus cuniculus	89-97
8182050-0	1994	Interaction of heparin with rat mast cell protease 1.	Heparin	15-22	mast cell protease 1	Rattus norvegicus	32-52
1812786-7	1991	Modulation of PTPase activity by orthovanadate, heparin, Zn2+, and EDTA gave similar results in both assays.	Heparin	48-55	acid phosphatase 1	Bos taurus	14-20
1724341-1	1991	We tested acid and basic fibroblast growth factor (aFGF and bFGF), members of the heparin binding FGF family, for their ability to stimulate bone resorption as measured by the release of previously incorporated 45Ca from cultured fetal rat long bones in the presence and absence of heparin.	Heparin	82-89	fibroblast growth factor 1	Rattus norvegicus	51-55
1724341-1	1991	We tested acid and basic fibroblast growth factor (aFGF and bFGF), members of the heparin binding FGF family, for their ability to stimulate bone resorption as measured by the release of previously incorporated 45Ca from cultured fetal rat long bones in the presence and absence of heparin.	Heparin	282-289	fibroblast growth factor 1	Rattus norvegicus	51-55
1665594-3	1991	Pseudo-first order rate constants of inactivation of factor Xa and thrombin by antithrombin III were determined as function of heparin concentration, in the presence of 4.0 mM CaCl2.	Heparin	127-134	coagulation factor X	Homo sapiens	53-62
1665594-6	1991	Analysis of CY216 subfractions, obtained by gel filtration, showed that the heparin molecules of the upper region of the molecular weight distribution are responsible for the anti-thrombin, but also to a large extent for the anti-factor Xa activities.	Heparin	76-83	coagulation factor X	Homo sapiens	230-239
7921790-8	1994	Further fractionation of the HDL2-HDL3 bound activity on heparin-agarose established that 70% of the recovered activity was bound to the apo-E containing HDL.	Heparin	57-64	high density lipoprotein (HDL) level 2	Mus musculus	29-33
7921790-8	1994	Further fractionation of the HDL2-HDL3 bound activity on heparin-agarose established that 70% of the recovered activity was bound to the apo-E containing HDL.	Heparin	57-64	high density lipoprotein (HDL) level 3	Mus musculus	34-38
10551503-0	1999	Rapid detection of heparin-induced platelet antibodies with particle gel immunoassay (ID-HPF4) Early and acute diagnosis is needed to prevent thromboembolic complications in heparin-induced thrombocytopenia.	Heparin	19-26	zinc finger protein 85	Homo sapiens	89-93
8042187-3	1994	IC50 of argatroban on factor Xa-induced aggregation was 5-7 times higher than that on thrombin-induced aggregation, while IC50 of heparin in the presence of antithrombin III on factor Xa-induced aggregation was 90-200 times higher than that on thrombin-induced aggregation.	Heparin	130-137	prothrombin	Oryctolagus cuniculus	161-169
8042187-4	1994	This finding suggests that argatroban inhibits thrombin generating on the platelet surface more efficiently than heparin, and this may be one of the reasons for the higher efficacy of argatroban in arterial thrombosis as compared with heparin.	Heparin	235-242	prothrombin	Oryctolagus cuniculus	47-55
8157673-3	1994	Abundant hLPL transcripts were detected in RNA from different tissues of transgenic mice which resulted in an increase in post-heparin plasma LPL activity of approximately 154%.	Heparin	127-134	lipoprotein lipase	Mus musculus	10-13
1655335-4	1991	Heparin and heparan sulphate also strongly inhibited human leucocyte elastase activity towards insoluble human lung elastin, as determined by an e.l.i.s.a.	Heparin	0-7	elastin	Homo sapiens	116-123
1655335-9	1991	These results suggest that heparin and heparan sulphate, as components of cellular and basement membranes, are likely to have a role in protecting structural proteins, such as elastin, from the proteolytic activity of human leucocyte elastase.	Heparin	27-34	elastin	Homo sapiens	176-183
1810305-4	1991	This lack of regioselectivity in the reaction of 2 (and 12) contrasts markedly with the high affinity of the reagent for HO-3 of residues of alpha-L-idopyranosyluronic acid present in a modified form of heparin.	Heparin	203-210	histidyl-tRNA synthetase 2, mitochondrial	Homo sapiens	121-125
10726029-9	1999	This was soon followed by experiments with antithrombin drugs such as hirudin and argatroban as replacements for heparin in the HIT-HITT syndrome.	Heparin	113-120	serpin family C member 1	Homo sapiens	43-55
2065676-7	1991	MCP activity from virally infected L929 cells was concentrated and purified by sequential adsorption to controlled pore glass, heparin-Sepharose chromatography, ion-exchange FPLC and reversed-phase HPLC.	Heparin	127-134	complement component (3b/4b) receptor 1-like	Mus musculus	0-3
10726037-2	1999	The low molecular weight heparins, originally thought to be useful alternatives to heparin because of their smaller size, show platelet activation and aggregation responses in platelet heparin-induced thrombocytopenia serum systems (P-selectin expression, microparticle formation, serotonin release, platelet aggregation).	Heparin	25-33	selectin P	Homo sapiens	233-243
10726037-2	1999	The low molecular weight heparins, originally thought to be useful alternatives to heparin because of their smaller size, show platelet activation and aggregation responses in platelet heparin-induced thrombocytopenia serum systems (P-selectin expression, microparticle formation, serotonin release, platelet aggregation).	Heparin	25-32	selectin P	Homo sapiens	233-243
8149517-13	1994	In addition, they suggest an additional mechanism for the apparent superiority of hirudin over heparin as a thrombin inhibitor at sites of arterial injury.	Heparin	95-102	prothrombin	Oryctolagus cuniculus	108-116
10726041-7	1999	The endothelial damage markers of soluble thrombomodulin, soluble P-selectin (p &lt; 0.05 vs. normal), plasminogen activator inhibitor-1 and tissue factor were elevated in heparin-induced thrombocytopenia and antiphospholipid antibody syndrome patients.	Heparin	172-179	thrombomodulin	Homo sapiens	42-56
8168536-13	1994	In addition, unique structural features of human secretory class II PLA2, together with its unique mode of interaction with heparin, suggest that this PLA2 might have an additional heparin-binding site.	Heparin	181-188	phospholipase A2 group IIA	Homo sapiens	151-155
1718949-5	1991	A kinetical study demonstrated that rat factor Xa was strongly inhibited by rat antithrombin III, with a Ki of 2.2 x 10(-11) M, in the presence of heparin.	Heparin	147-154	coagulation factor X	Homo sapiens	40-49
10726041-7	1999	The endothelial damage markers of soluble thrombomodulin, soluble P-selectin (p &lt; 0.05 vs. normal), plasminogen activator inhibitor-1 and tissue factor were elevated in heparin-induced thrombocytopenia and antiphospholipid antibody syndrome patients.	Heparin	172-179	selectin P	Homo sapiens	66-76
1718949-5	1991	A kinetical study demonstrated that rat factor Xa was strongly inhibited by rat antithrombin III, with a Ki of 2.2 x 10(-11) M, in the presence of heparin.	Heparin	147-154	serpin family C member 1	Rattus norvegicus	80-96
8168536-14	1994	Although the heparin-PLA2 binding diminished as the ionic strength of reaction medium increased, the inhibition of human secretory class II PLA2 by heparin remained significant at the physiological ionic strength.	Heparin	13-20	phospholipase A2 group IIA	Homo sapiens	21-25
8168536-15	1994	An estimated value of inhibition constant (Ki) was 0.1 microM under physiological conditions, which suggests that a normal pharmaceutical dose of heparin might inhibit human secretory class II PLA2 and regulate its biological effects.	Heparin	146-153	phospholipase A2 group IIA	Homo sapiens	193-197
8138579-1	1994	Amphiregulin, a member of the epidermal growth factor family with heparin binding affinity, functions as a natural regulator of keratinocyte growth.	Heparin	66-73	amphiregulin	Homo sapiens	0-12
8138579-8	1994	Exogenous heparin in the absence of chlorate, however, nearly completely inhibited growth under autocrine conditions and in the presence of recombinant amphiregulin.	Heparin	10-17	amphiregulin	Homo sapiens	152-164
8052962-7	1994	At doses of rhs-TM and heparin which were equally effective at inhibiting the decrease in platelet count and fibrinogen level in control rats treated with TF, only rhs-TM remained effective in preventing DIC in rats with reduced ATIII levels.	Heparin	23-30	coagulation factor III, tissue factor	Rattus norvegicus	155-157
8052962-9	1994	Therefore, rhs-TM effectively inhibits coagulation independent of ATIII levels, in contrast to heparin, which depends on the ATIII level.	Heparin	95-102	serpin family C member 1	Rattus norvegicus	125-130
8052970-2	1994	Thrombin adsorbed to either sulfopropyl-Sephadex or heparin-Sepharose bound &gt; 95% of 125I-r-hirudin and the complex remained bound to the matrix.	Heparin	52-59	prothrombin	Oryctolagus cuniculus	0-8
1718949-6	1991	However, in the absence of heparin, the second order rate constant for the inhibition of rat factor Xa by rat antithrombin III was 2.6 x 10(4) M-1.min-1, which was one forty-third that for the inhibition of human factor Xa by human antithrombin III.	Heparin	27-34	coagulation factor X	Homo sapiens	93-102
1718949-6	1991	However, in the absence of heparin, the second order rate constant for the inhibition of rat factor Xa by rat antithrombin III was 2.6 x 10(4) M-1.min-1, which was one forty-third that for the inhibition of human factor Xa by human antithrombin III.	Heparin	27-34	serpin family C member 1	Rattus norvegicus	110-126
1827689-6	1991	Weak MLR responses, as detected by lymphokine production, could be considerably amplified by irradiating (250-1000 cGy) the responder cells and by adding heparin (1-10 U/ml) to the cultures.	Heparin	154-161	ribosomal protein SA	Mus musculus	5-8
10505692-3	1999	Incubation with calcitriol (10(-8) M) for up to 4 d resulted in a time-dependent significant increase in heparin-releasable LPL activity (LPLa) accompanied by a significant increase in LPL mRNA.	Heparin	105-112	lipoprotein lipase	Homo sapiens	124-127
1849357-3	1991	Here we demonstrate the purification of HGF from human placenta with heparin-agarose chromatography and TSK-heparin high-pressure liquid chromatography and describe the distribution of placental HGF by immunohistochemistry using a polyclonal antibody to HGF.	Heparin	108-115	tsukushi, small leucine rich proteoglycan	Homo sapiens	104-107
8125158-5	1994	The enhancements were abolished by omitting heparin-PE or washing the HGF-treated substrates with 1 M NaCl, suggesting the immobilization of HGF to substrates through heparin.	Heparin	44-51	hepatocyte growth factor	Rattus norvegicus	141-144
8125158-8	1994	Both type I collagen and laminin substrates containing heparin-PE bound higher amounts of HGF than the respective control substrates, whereas neither of the substrates containing chondroitin sulfate-PE did.	Heparin	55-62	hepatocyte growth factor	Rattus norvegicus	90-93
10505692-3	1999	Incubation with calcitriol (10(-8) M) for up to 4 d resulted in a time-dependent significant increase in heparin-releasable LPL activity (LPLa) accompanied by a significant increase in LPL mRNA.	Heparin	105-112	lipoprotein lipase	Homo sapiens	138-141
10497166-0	1999	Importance of the P2 glycine of antithrombin in target proteinase specificity, heparin activation, and the efficiency of proteinase trapping as revealed by a P2 Gly --&gt; Pro mutation.	Heparin	79-86	serpin family C member 1	Homo sapiens	32-44
8049525-7	1994	In addition, heparin treatment of LNCaP cells inhibits androgen-stimulated cell growth further suggesting that amphiregulin can mediate androgen-stimulated LNCaP proliferation.	Heparin	13-20	amphiregulin	Homo sapiens	111-123
1905846-4	1991	During CPB, tPA increased to 20.34 ng/ml (SD 9.17) before protamine infusion, and 16.93 ng/ml (SD 8.13) after heparin neutralization.	Heparin	110-117	chromosome 20 open reading frame 181	Homo sapiens	12-15
1703436-3	1991	Recently, it has been demonstrated that the PAI-1-binding site on vitronectin is adjacent to a heparin-binding site (Preissner et al., 1990).	Heparin	95-102	vitronectin	Homo sapiens	66-77
8029789-6	1994	The results thus suggest that the Factor Xa-based antithrombin III activity method provides more valid results in patients on heparin therapy.	Heparin	126-133	coagulation factor X	Homo sapiens	34-43
10497166-1	1999	A sequence-specific heparin pentasaccharide activates the serpin, antithrombin, to inhibit factor Xa through an allosteric mechanism, whereas full-length heparin chains containing this sequence further activate the serpin to inhibit thrombin by an alternative bridging mechanism.	Heparin	20-27	serpin family C member 1	Homo sapiens	66-78
8308035-1	1994	Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis.	Heparin	81-88	pancreatic lipase	Homo sapiens	29-46
10517752-7	1999	M(2) function was acutely restored by removal of MBP with heparin.	Heparin	58-65	myelin basic protein	Cavia porcellus	49-52
7911722-1	1994	1 beta 2-Adrenoceptor agonists may exacerbate asthma by reducing the release of the anti-proliferative and anti-inflammatory molecule, heparin from mast cells in the airway.	Heparin	135-142	adrenoceptor beta 2	Homo sapiens	2-21
1824742-2	1991	Pre-treatment of swine with a thromboxane A2 receptor antagonist has been reported to prevent the pulmonary hypertensive response occasionally seen after protamine reversal of heparin anticoagulation.	Heparin	176-183	TBXA2R	Sus scrofa	30-53
2277084-26	1990	B104 adhesion to FN-C/H II and CS1 differs in sensitivity to heparin, yet each peptide inhibited adhesion to the other peptide, suggesting cell adhesion is somehow related at the cellular level.	Heparin	61-68	chorionic somatomammotropin hormone 1	Homo sapiens	31-34
2128972-9	1990	These data demonstrate that heparin interacts with HOMC, and increases the fibrinolytic capacity in these cells by selectively increasing the production of tPA.	Heparin	28-35	chromosome 20 open reading frame 181	Homo sapiens	156-159
10499652-0	1999	Gabexate mesilate and antithrombin III for intraoperative anticoagulation in heparin pretreated patients.	Heparin	77-84	serpin family C member 1	Homo sapiens	22-38
2122251-2	1990	BACKGROUND: We report the results of the Heparin-Aspirin Reperfusion Trial, a collaborative study comparing early intravenous heparin with oral aspirin as adjunctive treatment when recombinant tissue plasminogen activator (rt-PA) is used for coronary thrombolysis during acute myocardial infarction.	Heparin	41-48	chromosome 20 open reading frame 181	Homo sapiens	193-221
7507851-0	1994	Keratinocyte growth factor and fibroblast growth factor action on DNA synthesis in rat and human hepatocytes: modulation by heparin.	Heparin	124-131	fibroblast growth factor 7	Rattus norvegicus	0-26
7507851-3	1994	Here we have tested the activity of KGF, acidic fibroblast growth factor (aFGF), and basic fibroblast growth factor (bFGF) on normal adult rat and human hepatocytes and their modulation by heparin.	Heparin	189-196	fibroblast growth factor 7	Rattus norvegicus	36-39
7507851-6	1994	Addition of heparin inhibited the KGF response.	Heparin	12-19	fibroblast growth factor 7	Rattus norvegicus	34-37
10460149-11	1999	In contrast, VIIaQ217A association with antithrombin III in the presence of heparin was the fastest among the variants with a second-order rate constant of 2.31 (x10(3) M(-)(1) min(-)(1)), as compared to 0.47 and 1.47 for VIIaQ217E and wild-type VIIa, respectively.	Heparin	76-83	serpin family C member 1	Homo sapiens	40-56
8307153-4	1994	The specificity of GSK3 alpha was similar to GSK3 beta, but with the synthetic peptide substrate heparin stimulated the dephosphorylated form of GSK3 alpha (6-fold) more than GSK3 beta (1.8-fold).	Heparin	97-104	glycogen synthase kinase-3 alpha	Oryctolagus cuniculus	19-29
8307153-4	1994	The specificity of GSK3 alpha was similar to GSK3 beta, but with the synthetic peptide substrate heparin stimulated the dephosphorylated form of GSK3 alpha (6-fold) more than GSK3 beta (1.8-fold).	Heparin	97-104	glycogen synthase kinase-3 alpha	Oryctolagus cuniculus	145-155
8280781-0	1994	Arg-129 plays a specific role in the conformation of antithrombin and in the enhancement of factor Xa inhibition by the pentasaccharide sequence of heparin.	Heparin	148-155	coagulation factor X	Homo sapiens	92-101
8279543-4	1993	With the use of a ligand blot method, LPL specifically bound to a heparin-releasable, 116-kDa protein on mouse-derived brown fat adipose cell (BFC-1 beta) and rat adipocyte membranes.	Heparin	66-73	lipoprotein lipase	Mus musculus	38-41
7504635-11	1993	When heparin (10 micrograms/ml) was included along with bFGF in serum-free medium, tenascin production was further enhanced.	Heparin	5-12	tenascin C	Rattus norvegicus	83-91
1700081-0	1990	Inhibition of agrin-induced acetylcholine-receptor aggregation by heparin, heparan sulfate, and other polyanions.	Heparin	66-73	agrin	Homo sapiens	14-19
1700081-2	1990	We found that heparin, heparan sulfate, and a wide variety of other polyanions also inhibited agrin-induced AChR aggregation.	Heparin	14-21	agrin	Homo sapiens	94-99
1698787-13	1990	These results indicate that the exposure of the glycosaminoglycan-binding domain in VN may allow the concomitant binding of PAI-1 and heparin-like molecules to this region of the VN molecule.	Heparin	134-141	vitronectin	Homo sapiens	84-86
1698787-13	1990	These results indicate that the exposure of the glycosaminoglycan-binding domain in VN may allow the concomitant binding of PAI-1 and heparin-like molecules to this region of the VN molecule.	Heparin	134-141	vitronectin	Homo sapiens	179-181
2403299-7	1990	Since lipoprotein lipase has a similar size as hepatic triacylglycerol lipase, the disproportionate amount of lipoprotein lipase in lymph as compared to hepatic triacylglycerol lipase could be due to heparin crossing the capillary endothelium and displacing lipoprotein lipase from peripheral cells.	Heparin	200-207	lipoprotein lipase	Canis lupus familiaris	110-128
1696913-0	1990	The phosphorylation of the two-chain form of vitronectin by protein kinase A is heparin dependent.	Heparin	80-87	vitronectin	Homo sapiens	45-56
1696913-4	1990	Heparin or heparan sulfate are shown here to modulate the conformation of clipped vitronectin at physiological pH, exposing Ser378 and allowing its stoichiometric phosphorylation by the kinase.	Heparin	0-7	vitronectin	Homo sapiens	82-93
8227019-9	1993	Although rat EC-SOD has a high sequence homology with the catalytic center and the polybasic heparin-binding site near the COOH terminus of human EC-SOD C, its NH2-terminal sequence and the sequences flanking the heparin-binding site differ substantially.	Heparin	93-100	superoxide dismutase 3	Rattus norvegicus	13-19
10393815-6	1999	In contrast, K27, 30Q/R31Q-FGF2, K128Q/K138Q-FGF2 and R118,129Q/K119,128Q-FGF2 exerted a significant uPA-inducing and morphogenic activity in an ERK1/2-dependent manner only in the presence of heparin.	Heparin	193-200	keratin 27	Bos taurus	13-16
8227019-9	1993	Although rat EC-SOD has a high sequence homology with the catalytic center and the polybasic heparin-binding site near the COOH terminus of human EC-SOD C, its NH2-terminal sequence and the sequences flanking the heparin-binding site differ substantially.	Heparin	213-220	superoxide dismutase 3	Rattus norvegicus	13-19
1696913-5	1990	At this pH the two-chain form of vitronectin in plasma exhibits a higher affinity for heparin, and behaves as a flexible molecule, which can conformationally respond to heparin and heparan sulfate, effectors involved in vitronectin function.	Heparin	86-93	vitronectin	Homo sapiens	33-44
1696913-5	1990	At this pH the two-chain form of vitronectin in plasma exhibits a higher affinity for heparin, and behaves as a flexible molecule, which can conformationally respond to heparin and heparan sulfate, effectors involved in vitronectin function.	Heparin	169-176	vitronectin	Homo sapiens	33-44
1696913-5	1990	At this pH the two-chain form of vitronectin in plasma exhibits a higher affinity for heparin, and behaves as a flexible molecule, which can conformationally respond to heparin and heparan sulfate, effectors involved in vitronectin function.	Heparin	169-176	vitronectin	Homo sapiens	220-231
8232430-5	1993	RESULTS: The rate of patency of the infarct-related artery at 90 minutes was highest in the group given accelerated-dose t-PA and heparin (81 percent), as compared with the group given streptokinase and subcutaneous heparin (54 percent, P &lt; 0.001), the group given streptokinase and intravenous heparin (60 percent, P &lt; 0.001), and the group given combination therapy (73 percent, P = 0.032).	Heparin	216-223	chromosome 20 open reading frame 181	Homo sapiens	121-125
8232430-5	1993	RESULTS: The rate of patency of the infarct-related artery at 90 minutes was highest in the group given accelerated-dose t-PA and heparin (81 percent), as compared with the group given streptokinase and subcutaneous heparin (54 percent, P &lt; 0.001), the group given streptokinase and intravenous heparin (60 percent, P &lt; 0.001), and the group given combination therapy (73 percent, P = 0.032).	Heparin	216-223	chromosome 20 open reading frame 181	Homo sapiens	121-125
10393815-6	1999	In contrast, K27, 30Q/R31Q-FGF2, K128Q/K138Q-FGF2 and R118,129Q/K119,128Q-FGF2 exerted a significant uPA-inducing and morphogenic activity in an ERK1/2-dependent manner only in the presence of heparin.	Heparin	193-200	plasminogen activator, urokinase	Bos taurus	101-104
8232430-9	1993	Measures of left ventricular function paralleled the rate of patency at 90 minutes; ventricular function was best in the group given t-PA with heparin and in patients with normal flow through the infarct-related artery irrespective of treatment group.	Heparin	143-150	chromosome 20 open reading frame 181	Homo sapiens	133-137
2166377-1	1990	Since low molecular weight heparin is used for the prevention of thromboembolism, the coagulation laboratories are in need of a simple, reliable and practicable test for factor Xa inhibition in order to monitor the effect of low molecular heparin in plasma.	Heparin	27-34	coagulation factor X	Homo sapiens	170-179
10414365-13	1999	Binding of vitronectin and lactoferrin was efficiently inhibited by preincubating of staphylococcal cells with sulphated carbohydrate compounds as heparin, dextran sulphate and fucoidan, but not by other non-sulphated highly charged glycoconjugates such as hyaluronic acid.	Heparin	147-154	lactotransferrin	Bos taurus	27-38
1966669-0	1990	The effect of heparin and other glycosaminoglycans on levels of tissue plasminogen activator and plasminogen activator inhibitor in cultured human umbilical vein endothelial cells.	Heparin	14-21	chromosome 20 open reading frame 181	Homo sapiens	64-92
8228255-11	1993	Heparin or an antibody recognizing the heparin-binding domain of type II PLA2 also suppressed the MC-degranulating activity, probably due to inhibition of binding of PLA2 to the cells.	Heparin	0-7	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	73-77
8228255-11	1993	Heparin or an antibody recognizing the heparin-binding domain of type II PLA2 also suppressed the MC-degranulating activity, probably due to inhibition of binding of PLA2 to the cells.	Heparin	0-7	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	166-170
8228255-11	1993	Heparin or an antibody recognizing the heparin-binding domain of type II PLA2 also suppressed the MC-degranulating activity, probably due to inhibition of binding of PLA2 to the cells.	Heparin	39-46	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	73-77
8228255-11	1993	Heparin or an antibody recognizing the heparin-binding domain of type II PLA2 also suppressed the MC-degranulating activity, probably due to inhibition of binding of PLA2 to the cells.	Heparin	39-46	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	166-170
8228255-12	1993	The interaction between heparan sulfate on cell surface and the heparin-binding domain of type II PLA2 may be important for the induction of exocytosis.	Heparin	64-71	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	98-102
8128425-3	1993	As an alternative we define a unit of heparin in terms of anti-factor Xa- and antithrombin-activity that is independent of the heparin standard and of the assay method, but that is based upon a quantitative description of the catalytic effect of heparin on AT III mediated thrombin- and factor Xa breakdown.	Heparin	38-45	coagulation factor X	Homo sapiens	63-72
8128425-3	1993	As an alternative we define a unit of heparin in terms of anti-factor Xa- and antithrombin-activity that is independent of the heparin standard and of the assay method, but that is based upon a quantitative description of the catalytic effect of heparin on AT III mediated thrombin- and factor Xa breakdown.	Heparin	38-45	coagulation factor X	Homo sapiens	287-296
8128425-4	1993	Expression of the results of existing anti-factor Xa- and antithrombin tests in terms of these units will allow to express heparin levels in plasma in terms of concentrations of active anticoagulant material.	Heparin	123-130	coagulation factor X	Homo sapiens	43-52
2164262-0	1990	The inhibition of intrinsic prothrombinase and its generation by heparin and four derivatives in prothrombin poor plasma.	Heparin	65-72	coagulation factor X	Homo sapiens	28-42
2164262-1	1990	The effect of different heparins and a synthetic pentasaccharide on the inhibition of intrinsic prothrombinase and of its generation was studied by a new technique, using a defibrinated prothrombin poor human plasma, supplemented with phospholipids and calcium.	Heparin	24-32	coagulation factor X	Homo sapiens	96-110
2164262-9	1990	On the other hand, anti-IIa activity of heparins could be responsible for the inhibition of prothrombinase generation.	Heparin	40-48	coagulation factor X	Homo sapiens	92-106
2363127-0	1990	Pharmacological profile of the chemically synthesized antithrombin III binding fragment of heparin (pentasaccharide) in rats.	Heparin	91-98	serpin family C member 1	Rattus norvegicus	54-70
2327990-4	1990	Complex-formation between kallikrein and the binding protein is inhibited by heparin, whereas that between kallikrein and alpha 1-antitrypsin is heparin-resistant.	Heparin	77-84	kallikrein related peptidase 4	Homo sapiens	26-36
8226843-9	1993	We find that the InsP3 receptor antagonist heparin (500 micrograms/ml) blocks Ca2+ oscillations induced by both CCK (5-20 pM) and JMV 180 (10-40 nM), whereas de-N-sulfated heparin (500 micrograms/ml), which does not affect InsP3 binding to its receptor, fails to inhibit the responses to the two agonists.	Heparin	43-50	cholecystokinin	Mus musculus	112-115
10342830-3	1999	We previously reported that ovarian PA1 cells constitutively secrete FS and show a decreased proliferation rate in response to exogenous activin only if cell surface associated FS is first removed by heparin treatment.	Heparin	200-207	inhibin subunit beta E	Homo sapiens	137-144
8223431-6	1993	Both p31 and p27 bind quantitatively to heparin-Sepharose and can be displaced from the cell surface and extracellular matrix by soluble heparin.	Heparin	137-144	unconventional SNARE in the ER 1 homolog (S. cerevisiae)	Mus musculus	5-8
8223431-6	1993	Both p31 and p27 bind quantitatively to heparin-Sepharose and can be displaced from the cell surface and extracellular matrix by soluble heparin.	Heparin	137-144	cyclin-dependent kinase inhibitor 1B	Mus musculus	13-16
2327990-4	1990	Complex-formation between kallikrein and the binding protein is inhibited by heparin, whereas that between kallikrein and alpha 1-antitrypsin is heparin-resistant.	Heparin	145-152	kallikrein related peptidase 4	Homo sapiens	107-117
2160449-9	1990	However, the acceleration by heparin or dextran sulfate for the inhibition of Factor Xa, Factor XIa, and plasma kallikrein was not significant.	Heparin	29-36	coagulation factor X	Homo sapiens	78-87
8231204-8	1993	When human plasma was incubated for 5 minutes with rabbit pericardium at reduced heparin concentrations, we found significant generation of thrombin (p &lt; 0.05) and plasmin (p &lt; 0.05).	Heparin	81-88	prothrombin	Oryctolagus cuniculus	140-148
33771558-6	2021	The VEGFR2 binding sites on fibronectin show great similarity to the VEGF binding sites, as they were also exposed upon heparin-induced conformational changes in fibronectin, and the interaction was enhanced at acidic pH.	Heparin	120-127	kinase insert domain receptor	Homo sapiens	4-10
10348900-4	1999	[3H]Heparin labeled with this reagent crosslinked to antithrombin III very specifically but not to ovalbumin, as analyzed by the Bio-imaging Analyzer System (BAS, Fuji Photo Film, Tokyo).	Heparin	4-11	serpin family C member 1	Homo sapiens	53-69
10229666-0	1999	An IKLLI-containing peptide derived from the laminin alpha1 chain mediating heparin-binding, cell adhesion, neurite outgrowth and proliferation, represents a binding site for integrin alpha3beta1 and heparan sulphate proteoglycan.	Heparin	76-83	laminin subunit alpha 1	Rattus norvegicus	45-59
33588972-5	2021	RESULTS: The percentage of anti-factor Xa levels outside therapeutic range was lower in the subcutaneous low-molecular-weight heparin group compared with the percentage of activated partial thromboplastin times outside therapeutic range in the intravenous unfractionated heparin group (40% versus 90%, p < 0.001).	Heparin	126-133	coagulation factor X	Homo sapiens	32-41
8376384-3	1993	Furthermore, CCK-JMV-180 accelerates Ca2+ influx into cells microinjected with the inositol 1,4,5-trisphosphate receptor antagonist heparin and into acini loaded with the Ca(2+)-chelating agent BAPTA (1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid).	Heparin	132-139	cholecystokinin	Rattus norvegicus	13-16
10359094-0	1999	Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments.	Heparin	56-63	microtubule associated protein tau	Homo sapiens	35-42
8287449-0	1993	Cytotoxic effects of vascular smooth muscle cells of the chimeric toxin, heparin binding TGF alpha-Pseudomonas exotoxin.	Heparin	73-80	transforming growth factor alpha	Rattus norvegicus	89-98
8287449-11	1993	CONCLUSIONS: The presence of a heparin binding domain increases the smooth muscle cell cytotoxicity of the TGF alpha fusion toxin, perhaps because HB-TGF alpha-PE4EKDEL functions as a molecule with two ligands.	Heparin	31-38	transforming growth factor alpha	Rattus norvegicus	107-116
8287449-11	1993	CONCLUSIONS: The presence of a heparin binding domain increases the smooth muscle cell cytotoxicity of the TGF alpha fusion toxin, perhaps because HB-TGF alpha-PE4EKDEL functions as a molecule with two ligands.	Heparin	31-38	transforming growth factor alpha	Rattus norvegicus	150-159
33232799-0	2021	BMP6 binding to heparin and heparan sulfate is mediated by N-terminal and C-terminal clustered basic residues.	Heparin	16-23	bone morphogenetic protein 6	Cricetulus griseus	0-4
33232799-6	2021	Monomeric wild-type BMP6 and mutants were produced, substituting the basic residues with non-charged ones, and their affinity to the heparin-column was measured.	Heparin	133-140	bone morphogenetic protein 6	Cricetulus griseus	20-24
33232799-7	2021	The BMP6-heparin interaction was also predicted at atomic level by in silico molecular dynamics.	Heparin	9-16	bone morphogenetic protein 6	Cricetulus griseus	4-8
33232799-8	2021	RESULTS: N-terminal and C-terminal BMP6 peptides showed high heparin affinity in solid-phase assays.	Heparin	61-68	bone morphogenetic protein 6	Cricetulus griseus	35-39
33232799-9	2021	The mutation of the two sites (R5L, R6S, R7L and K126N, K127N, R129S) abolished the heparin-binding activity of the recombinant monomeric BMP6.	Heparin	84-91	bone morphogenetic protein 6	Cricetulus griseus	138-142
33232799-12	2021	CONCLUSIONS: In BMP6, N-terminal (R5, R6, R7) and C-terminal (K126, K127, R129) domains mediate the interaction with heparin and HS.	Heparin	117-124	bone morphogenetic protein 6	Cricetulus griseus	16-20
33232799-13	2021	GENERAL SIGNIFICANCE: This study provides the molecular mechanism supporting the use of heparin to sequester BMP6 and inhibit hepcidin expression, a novel clinical approach for high-hepcidin iron disorders.	Heparin	88-95	bone morphogenetic protein 6	Cricetulus griseus	109-113
34725832-2	2022	The objective of this study was to evaluate the effectiveness and safety of two anticoagulation protocols using conventional (0.3-0.7 IU/mL) vs. restricted (0.2-0.5 IU/mL) anti-factor Xa (anti-Xa) targets for the management of unfractionated heparin (UFH) in adult ECMO patients.	Heparin	251-254	coagulation factor X	Homo sapiens	177-186
8403851-10	1993	Lecithin:cholesterol acyl transferase is active in plasma and hepatic lipase and lipoprotein lipase are evident in post-heparin plasma.	Heparin	120-127	lipoprotein lipase	Equus caballus	81-99
8367447-4	1993	In the present study, heparin-Sepharose chromatography was used to partially purify solubilized N1E-115 membranes to produce an enriched population of AT2 receptors.	Heparin	22-29	serine (or cysteine) peptidase inhibitor, clade B, member 9d	Mus musculus	151-154
10427858-1	1999	In the early eighties, following breakthroughs in oligosaccharide chemistry, the total chemical synthesis of pentasaccharides has been achieved, representing the antithrombin binding domain of heparin (the active site).	Heparin	193-200	serpin family C member 1	Homo sapiens	162-174
34955533-3	2021	As a plasma protein, HRG has been reported to regulate vascular biology, including coagulation, fibrinolysis and angiogenesis, through its binding with several ligands (heparin, FXII, fibrinogen, thrombospondin, and plas-minogen) and interaction with many types of cells (endothelial cells, erythrocytes, neutrophils and platelets).	Heparin	169-176	histidine rich glycoprotein	Homo sapiens	21-24
8349739-5	1993	A similar inhibition of migration occurred when BASMC were treated with a synthetic peptide (P21) corresponding to the sequence of the putative heparin-binding domain of HB-EGF.	Heparin	144-151	proheparin-binding EGF-like growth factor	Cricetulus griseus	170-176
10427858-3	1999	In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group.	Heparin	89-96	serpin family C member 1	Homo sapiens	62-74
34895060-9	2021	Inhibiting HBP expression by injecting heparin before AP can alleviate pancreatic necrosis and inhibit F4/80 labeled M1 macrophage infiltration and IL-6, TNF-alpha, and iNOS mRNA expression.	Heparin	39-46	adhesion G protein-coupled receptor E1	Mus musculus	103-108
10427858-3	1999	In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group.	Heparin	89-96	serpin family C member 1	Homo sapiens	164-176
10375169-6	1999	In this study, we have also found that OKGK improved hyperlipidemia in the CPM-induced hyperlipidemia model in rabbits, mainly due to an increase in heparin-releasable heart LPL activity and postheparin plasma LPL activity.	Heparin	149-156	lipoprotein lipase	Oryctolagus cuniculus	174-177
34537241-7	2021	Competitive SPR inhibition analysis of PpFucCS, IbFucCS, and IbSF against heparin binding to wild type S-protein showed IC50 values (in the nM range) 6, 25, and 6 times more efficient than heparin, respectively.	Heparin	74-81	vitronectin	Homo sapiens	103-112
8328965-1	1993	A cytosolic phospholipase A2 (PLA2) has been purified to homogeneity from the human monocytic tumour cell line THP-1 by a combination of ion-exchange, heparin-agarose and hydrophobic-interaction chromatography and non-denaturing PAGE.	Heparin	151-158	phospholipase A2 group IVA	Homo sapiens	2-28
8328965-1	1993	A cytosolic phospholipase A2 (PLA2) has been purified to homogeneity from the human monocytic tumour cell line THP-1 by a combination of ion-exchange, heparin-agarose and hydrophobic-interaction chromatography and non-denaturing PAGE.	Heparin	151-158	phospholipase A2 group IIA	Homo sapiens	30-34
10195936-0	1999	Effect of cardiopulmonary bypass and heparin on plasma levels of Lp(a) and Apo(a) fragments.	Heparin	37-44	aminopeptidase O (putative)	Homo sapiens	75-78
8489237-0	1993	Effects of heparin and other glycosaminoglycans on elastin production by cultured neonatal rat lung fibroblasts.	Heparin	11-18	elastin	Rattus norvegicus	51-58
8489237-4	1993	Heparin decreases the soluble elastin content of the culture medium while increasing the soluble elastin content of the cell layer.	Heparin	0-7	elastin	Rattus norvegicus	30-37
8489237-4	1993	Heparin decreases the soluble elastin content of the culture medium while increasing the soluble elastin content of the cell layer.	Heparin	0-7	elastin	Rattus norvegicus	97-104
8489237-6	1993	Some of these effects may result from the binding of heparin to soluble elastin at physiological concentrations of NaCl.	Heparin	53-60	elastin	Rattus norvegicus	72-79
8489237-7	1993	The galactosamine-containing glycosaminoglycans, chondroitin sulfate and dermatan sulfate, differ from heparin in that they increase the quantity of soluble elastin in the culture medium and decrease the deposition of insoluble elastin in the extracellular matrix.	Heparin	103-110	elastin	Rattus norvegicus	157-164
34404617-4	2021	Heparin inhibits the CXCR4/SDF1 axis, as does plerixafor.	Heparin	0-7	C-X-C motif chemokine receptor 4	Homo sapiens	21-26
8386317-7	1993	The phospho-CREB (P-CREB) phosphatase activity present in nuclear extracts coelutes with protein Ser/Thr phosphatase type 2A (PP2A) on Mono Q, amino-hexyl Sepharose, and heparin agarose columns and was chromatographically resolved from nuclear protein Ser/Thr-phosphatase type 1 (PP1).	Heparin	170-177	cAMP responsive element binding protein 1	Homo sapiens	12-16
34555698-0	2021	Heparin induced thrombocytopenia in relation to SARS-CoV-2 infection and ABO blood group.	Heparin	0-7	ABO, alpha 1-3-N-acetylgalactosaminyltransferase and alpha 1-3-galactosyltransferase	Homo sapiens	73-88
10075702-0	1999	Heparin-induced conformational change in microtubule-associated protein Tau as detected by chemical cross-linking and phosphopeptide mapping.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	41-75
34153666-0	2021	The ERK/CREB/PTN/syndecan-3 pathway involves in heparin-mediated neuro-protection and neuro-regeneration against cerebral ischemia-reperfusion injury following cardiac arrest.	Heparin	48-55	syndecan 3	Rattus norvegicus	17-27
34153666-2	2021	Here, we aimed to explore the role of pleiotrophin (PTN)/syndecan-3 pathway in heparin therapy for CIR-CA.	Heparin	79-86	syndecan 3	Rattus norvegicus	57-67
8386317-7	1993	The phospho-CREB (P-CREB) phosphatase activity present in nuclear extracts coelutes with protein Ser/Thr phosphatase type 2A (PP2A) on Mono Q, amino-hexyl Sepharose, and heparin agarose columns and was chromatographically resolved from nuclear protein Ser/Thr-phosphatase type 1 (PP1).	Heparin	170-177	cAMP responsive element binding protein 1	Homo sapiens	20-24
8487783-6	1993	Of the 22 complement proteins examined, 13 bound heparin (C1q, C2, C4, C4bp, C1INH, B, D, H, P, C6, C8, C9, and vitronectin) while 9 did not bind heparin (C1r, C1s, C3, Factor I, C5, C7, C3b, Ba and Bb).	Heparin	49-56	vitronectin	Homo sapiens	112-123
8483924-7	1993	Heparin ligand blot analysis demonstrated that RAP but not gp330 binds heparin.	Heparin	71-78	LDL receptor related protein associated protein 1	Rattus norvegicus	47-50
7682159-3	1993	It has been assumed that these two stages of terminal complement complex (TCC) inhibition take place through charge interactions between the heparin-binding region of vitronectin and homologous cysteine-rich sequences of the late complement proteins C6, C7, C8 and C9.	Heparin	141-148	vitronectin	Homo sapiens	167-178
34153666-9	2021	In terms of the mechanism, heparin upregulated the expression of ERK, CREB, NF200, BDNF, NGF, PTN and syndecan-3 in the rat brains.	Heparin	27-34	brain-derived neurotrophic factor	Rattus norvegicus	83-87
34166830-5	2021	General linear regression models were run to predict rates of DVT, PE, and reoperation due to bleeding from UFH dosing regimen while controlling for age at surgery, sex, VTE history, craniotomy for tumor resection, surgery duration, length of stay, reoperation, infections, and IDH/MGMT mutations.	Heparin	108-111	O-6-methylguanine-DNA methyltransferase	Homo sapiens	282-286
10100868-0	1999	Interaction of heparin with annexin V.	Heparin	15-22	annexin A5	Homo sapiens	28-37
34204611-10	2021	We further show that the cytotoxicity of FGF-SAP in U2OS cells was reduced when cells were co-treated with heparin to compete out binding to HSPG, demonstrating that the cytotoxic effect was due to internalization by HSPGs.	Heparin	107-114	syndecan 2	Homo sapiens	141-145
8455594-8	1993	The Env/K-FGF fusion protein expressed by the MFS virus has retained all of the biological properties of native K-FGF, including secretion, mitogenic activity, heparin binding, and neutralization by anti-K-FGF antibodies.	Heparin	160-167	endogenous retrovirus group K member 20	Homo sapiens	4-7
7679097-3	1993	Heparin binding activity was mapped to two different tenascin segments: one comprising the fourth and fifth fibronectin type III domains, and to TNfbg, the fibrinogen-like terminal knob.	Heparin	0-7	tenascin C	Homo sapiens	53-61
10100868-1	1999	The energetics and kinetics of the interaction of heparin with the Ca2+ and phospholipid binding protein annexin V, was examined and the minimum oligosaccharide sequence within heparin that binds annexin V was identified.	Heparin	50-57	annexin A5	Homo sapiens	105-114
35623497-6	2022	Using peptides of individual repeats, we show that R2, like R3, forms seed-competent fibrils when assembled in the presence of heparin.	Heparin	127-134	CD1e molecule	Homo sapiens	51-62
10100868-1	1999	The energetics and kinetics of the interaction of heparin with the Ca2+ and phospholipid binding protein annexin V, was examined and the minimum oligosaccharide sequence within heparin that binds annexin V was identified.	Heparin	50-57	annexin A5	Homo sapiens	196-205
8428956-5	1993	Its responsiveness toward the usual PTP activators (e.g. spermine) or inhibitors (e.g. vanadate, molybdate, heparin, or Zn2+) varied considerably with the nature of the substrates involved.	Heparin	108-115	protein tyrosine phosphatase non-receptor type 22	Homo sapiens	36-39
10100868-1	1999	The energetics and kinetics of the interaction of heparin with the Ca2+ and phospholipid binding protein annexin V, was examined and the minimum oligosaccharide sequence within heparin that binds annexin V was identified.	Heparin	177-184	annexin A5	Homo sapiens	105-114
35220018-6	2022	Heparin-bile acid based conjugates, as ECM-mimicking component, were synthesized to selectively target the TEC marker doppel and doppel/VEGFR2 axis.	Heparin	0-7	kinase insert domain receptor	Homo sapiens	136-142
10100868-1	1999	The energetics and kinetics of the interaction of heparin with the Ca2+ and phospholipid binding protein annexin V, was examined and the minimum oligosaccharide sequence within heparin that binds annexin V was identified.	Heparin	177-184	annexin A5	Homo sapiens	196-205
35377938-7	2022	Meta-analyses indicated that the ABO association was independent of PF4/heparin IgG levels and was stronger when functional assay-positive cases were compared to antibody-positive (functional assay-negative) controls than to antibody-negative controls.	Heparin	72-79	ABO, alpha 1-3-N-acetylgalactosaminyltransferase and alpha 1-3-galactosyltransferase	Homo sapiens	33-36
10100868-3	1999	Analysis of the data obtained from surface plasmon resonance afforded a Kd of approximately 21 nM for the interaction of annexin V with end-chain immobilized heparin and a Kd of approximately 49 nM for the interaction with end-chain immobilized heparan sulfate.	Heparin	158-165	annexin A5	Homo sapiens	121-130
8476991-3	1993	This study shows that complement activation caused by poly(methyl methacrylate) can be diminished by end-point heparin attachment, as demonstrated by a significant reduction in the generation of C3a and fluid phase terminal complement complexes.	Heparin	111-118	complement C3	Homo sapiens	195-198
10100868-4	1999	Isothermal titration calorimetry showed the minimum annexin V binding oligosaccharide sequence within heparin corresponds to an octasaccharide sequence.	Heparin	102-109	annexin A5	Homo sapiens	52-61
10024677-4	1999	Addition of exogenous TGF-alpha, EGF, AR, or HB-EGF with heparin accelerated cell proliferation.	Heparin	57-64	epidermal growth factor	Homo sapiens	33-36
8430072-7	1993	The increased efficacy was blocked by heparin and was further increased by cell culture in 1% (vs. 10%) fetal bovine serum, suggesting that the effect may, at least in part, be mediated via the LDL receptor.	Heparin	38-45	low density lipoprotein receptor	Mus musculus	194-206
35053249-7	2022	These data provided the rationale for designing experiments in rats subjected to blast injury and hemorrhage, to explore the effect of HMGB1 inhibition by CX-01 (2-O, 3-O desulfated heparin).	Heparin	182-189	high mobility group box 1	Rattus norvegicus	135-140
10024677-4	1999	Addition of exogenous TGF-alpha, EGF, AR, or HB-EGF with heparin accelerated cell proliferation.	Heparin	57-64	heparin binding EGF like growth factor	Homo sapiens	45-51
10065869-0	1999	Heparin inhibits proliferation of myometrial and leiomyomal smooth muscle cells through the induction of alpha-smooth muscle actin, calponin h1 and p27.	Heparin	0-7	interferon alpha inducible protein 27	Homo sapiens	148-151
35224154-2	2022	HRGP ligands includes heme, Zn2+, thrombospondin, plasmin/plasminogen, heparin/heparan sulfate, fibrinogen, tropomyosin, IgG, FcgammaR, C1q.	Heparin	71-78	histidine rich glycoprotein	Homo sapiens	0-4
8416739-4	1993	VPF was isolated from serum-free tumor cell conditioned medium using heparin-Sepharose affinity chromatography.	Heparin	69-76	vascular endothelial growth factor A	Mus musculus	0-3
10065869-8	1999	Taken together, these results indicate that heparin inhibits the proliferation of myometrial and leiomyomal SMC through the induction of alpha-SMA, calponin h1 and p27.	Heparin	44-51	interferon alpha inducible protein 27	Homo sapiens	164-167
10348708-0	1999	Effects of heparin and related sulfated polysaccharides on tissue factor expression induced by mitogenic and non-mitogenic factors in human vascular smooth muscle cells.	Heparin	11-18	coagulation factor III, tissue factor	Homo sapiens	59-72
8380742-14	1993	The deleted form of recombinant HGF (rHGF) expressed in CHO cells had slightly lower heparin-binding affinity than did the intact form.	Heparin	85-92	hepatocyte growth factor	Cricetulus griseus	32-35
8380742-14	1993	The deleted form of recombinant HGF (rHGF) expressed in CHO cells had slightly lower heparin-binding affinity than did the intact form.	Heparin	85-92	hepatocyte growth factor	Rattus norvegicus	37-41
1334488-2	1992	A novel human tissue kallikrein inhibitor designated as kallistatin has been purified from plasma to apparent homogeneity by polyethylene glycol fractionation and successive chromatography on heparin-Agarose, DEAE-Sepharose, hydroxylapatite, and phenyl-Superose columns.	Heparin	192-199	serpin family A member 4	Homo sapiens	56-67
1472067-7	1992	Heparin inhibited phosphorylation of the D4 peptide or phosvitin by CKI alpha.	Heparin	0-7	casein kinase II subunit beta	Oryctolagus cuniculus	55-64
10348708-5	1999	We evaluated the inhibitory effect of heparin on the expression of TF induced by various mitogenic (FCS, PDGF-BB and EGF) and non-mitogenic (bacterial LPS) agents.	Heparin	38-45	coagulation factor III, tissue factor	Homo sapiens	67-69
9870465-6	1998	RESULTS: Within a 3-1000 microg/ml concentration range, heparin inhibited gene expression and release of FN by 10% fetal calf serum (FCS)-stimulated MC in a concentration-dependent manner.	Heparin	56-63	fibronectin 1	Rattus norvegicus	105-107
1385412-0	1992	Heparin-binding properties of vitronectin are linked to complex formation as illustrated by in vitro polymerization and binding to the terminal complement complex.	Heparin	0-7	vitronectin	Homo sapiens	30-41
9870465-7	1998	At concentrations of 300 and 1000 microg/ml, heparin inhibited fibronectin mRNA levels in TGF-beta1 (6 ng/ml) stimulated cells.	Heparin	45-52	fibronectin 1	Rattus norvegicus	63-74
1385412-5	1992	Plasma VN circulates mainly as a 65/75-kDa monomer containing a cryptic heparin-binding site which is exposed upon a conformational change induced by different stimuli, such as coagulation, heating, adsorption to surfaces, or exposure to acids, urea, or other denaturating agents.	Heparin	72-79	vitronectin	Homo sapiens	7-9
9870465-10	1998	CONCLUSIONS: Heparin inhibited MC growth and fibronectin production.	Heparin	13-20	fibronectin 1	Rattus norvegicus	45-56
1385412-6	1992	In the present study, VN was demonstrated to expose its heparin-binding site and its conformationally dependent 8E6 epitope when incorporated into the terminal complement complex.	Heparin	56-63	vitronectin	Homo sapiens	22-24
1385412-7	1992	We suggest that exposure of the heparin-binding site and a putative hydrophobic binding site of VN are linked events dependent upon the same conformational change.	Heparin	32-39	vitronectin	Homo sapiens	96-98
9839225-1	1998	A heparin-binding peptide was isolated from a proteolytic hydrolysate of bovine lactoferrin by affinity chromatography using an immobilized heparin column.	Heparin	2-9	lactotransferrin	Bos taurus	80-91
1385412-9	1992	Such a link might also explain why purified heparin-binding VN spontaneously forms polymers.	Heparin	44-51	vitronectin	Homo sapiens	60-62
1385412-10	1992	The heparin-binding site may be involved in the elimination of multimolecular complexes containing VN.	Heparin	4-11	vitronectin	Homo sapiens	99-101
9763552-6	1998	Both antithrombin variants had an exceptional (25-fold) increase in heparin affinity and this, together with an increased inhibitory activity against factor Xa, provides evidence of the direct linkage of A-sheet opening to the conformational basis of heparin binding and activation.	Heparin	68-75	serpin family C member 1	Homo sapiens	5-17
1451229-2	1992	She had been treated with prophylactic, subcutaneous heparin and aspirin throughout her pregnancy.	Heparin	53-60	Src homology 2 domain containing E	Homo sapiens	0-3
9763552-6	1998	Both antithrombin variants had an exceptional (25-fold) increase in heparin affinity and this, together with an increased inhibitory activity against factor Xa, provides evidence of the direct linkage of A-sheet opening to the conformational basis of heparin binding and activation.	Heparin	251-258	serpin family C member 1	Homo sapiens	5-17
1335615-7	1992	Since the bleeding effect of Heparin or LHG is considered mainly due to its anti-thrombin activity, PS may be used as an agent to neutralize LHG, as in the case of Heparin, when bleeding happens to occur during LHG treatment.	Heparin	29-36	prothrombin	Oryctolagus cuniculus	81-89
9760299-4	1998	Injection of this virus (2x10(8) pfu/kg IV) produced high levels of Ec-SOD in the liver, which could be redistributed to the heart and other organs by injection of heparin.	Heparin	164-171	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	68-74
1448772-7	1992	Elevated F1+2 concentration before the beginning of heparin therapy (1.25 nM/l) decreased to 0.77 nM/l (p &lt; 0.0001) after 1 day of therapy.	Heparin	52-59	coagulation factor XII	Homo sapiens	9-13
1448774-7	1992	The limited effect of heparin is likely due to fibrin impairing the ability of heparin/antithrombin III to inactivate thrombin.	Heparin	22-29	prothrombin	Oryctolagus cuniculus	91-99
9727035-5	1998	Rat skeletal muscle laminins partially purified by heparin-agarose affinity chromatography also bound alpha-dystroglycan without sensitivity to heparin.	Heparin	51-58	dystroglycan 1	Rattus norvegicus	102-120
1409574-10	1992	Our model of heparin bound to PF4 has the anionic polysaccharide perpendicular to the alpha-helices, wrapped about the tetramer along the ring of positive charge, and salt linked to all four lysines on the helix of each monomer.	Heparin	13-20	platelet factor 4	Bos taurus	30-33
9727035-8	1998	Most interestingly, the alpha-dystroglycan binding activity of residual laminins expressed in merosin-deficient dy/dy skeletal muscle was inhibited dramatically (69 +/- 19%) by heparin.	Heparin	177-184	dystroglycan 1	Rattus norvegicus	24-42
9748565-0	1998	Mechanism of factor IXa inhibition by antithrombin in the presence of unfractionated and low molecular weight heparins and fucoidan.	Heparin	110-118	serpin family C member 1	Homo sapiens	38-50
1517248-1	1992	A fundamental property of the secretory tetrameric extracellular superoxide dismutase (EC-SOD) is its affinity for heparin and analogues, in vivo, mediating attachment to heparan sulfate proteoglycans located on cell surfaces and in the connective tissue matrix.	Heparin	115-122	superoxide dismutase 3	Rattus norvegicus	87-93
9748565-1	1998	Heparin exerts its anticoagulant activity by catalysing the inhibition of coagulation proteases by antithrombin (AT).	Heparin	0-7	serpin family C member 1	Homo sapiens	99-111
9748565-3	1998	The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan.	Heparin	181-188	serpin family C member 1	Homo sapiens	82-94
9748565-3	1998	The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan.	Heparin	245-253	serpin family C member 1	Homo sapiens	82-94
9748565-4	1998	Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol.	Heparin	106-113	serpin family C member 1	Homo sapiens	53-65
9748565-4	1998	Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol.	Heparin	106-113	serpin family C member 1	Homo sapiens	190-202
9801822-1	1998	We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom.	Heparin	151-158	serpin family C member 1	Homo sapiens	107-123
1517248-2	1992	EC-SOD is in vivo heterogeneous with regard to heparin affinity and can be divided into subclasses; A which lacks heparin affinity, B with intermediate affinity, and C with strong heparin affinity.	Heparin	47-54	superoxide dismutase 3	Rattus norvegicus	0-6
1517248-2	1992	EC-SOD is in vivo heterogeneous with regard to heparin affinity and can be divided into subclasses; A which lacks heparin affinity, B with intermediate affinity, and C with strong heparin affinity.	Heparin	114-121	superoxide dismutase 3	Rattus norvegicus	0-6
1517248-2	1992	EC-SOD is in vivo heterogeneous with regard to heparin affinity and can be divided into subclasses; A which lacks heparin affinity, B with intermediate affinity, and C with strong heparin affinity.	Heparin	114-121	superoxide dismutase 3	Rattus norvegicus	0-6
1517248-10	1992	We conclude that the cluster of six basic amino acids forms the essential part of the heparin-binding domain and that the composition of the four subunits in the EC-SOD tetramer determines the affinity for heparin.	Heparin	86-93	superoxide dismutase 3	Rattus norvegicus	162-168
1510155-3	1992	Vasopressin evoked a [Ca2+]i transient even in the absence of extracellular Ca2+, and intracellular perfusion with heparin completely blocked the response to vasopressin stimulation.	Heparin	115-122	carbonic anhydrase 2	Homo sapiens	22-25
1376317-0	1992	Mapping of binding sites for heparin, plasminogen activator inhibitor-1, and plasminogen to vitronectin"s heparin-binding region reveals a novel vitronectin-dependent feedback mechanism for the control of plasmin formation.	Heparin	29-36	vitronectin	Homo sapiens	145-156
1376317-2	1992	The direct binding of heparin, plasminogen as well as PAI-1 in its latent and active form to immobilized VN was studied in the absence or presence of competitors.	Heparin	22-29	vitronectin	Homo sapiens	105-107
9801822-1	1998	We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom.	Heparin	151-158	serpin family C member 1	Homo sapiens	125-131
1376317-4	1992	Utilizing synthetic peptides encompassing overlapping sequences of the heparin-binding domain of VN, adjacent heparin and PAI-1-binding sites were localized within the sequence 348-370 of VN.	Heparin	71-78	vitronectin	Homo sapiens	188-190
1376317-4	1992	Utilizing synthetic peptides encompassing overlapping sequences of the heparin-binding domain of VN, adjacent heparin and PAI-1-binding sites were localized within the sequence 348-370 of VN.	Heparin	110-117	vitronectin	Homo sapiens	97-99
1376317-4	1992	Utilizing synthetic peptides encompassing overlapping sequences of the heparin-binding domain of VN, adjacent heparin and PAI-1-binding sites were localized within the sequence 348-370 of VN.	Heparin	110-117	vitronectin	Homo sapiens	188-190
10420071-1	1998	Unfractionated heparin (UFH) exerts its anticoagulant properties by increasing the inactivation of thrombin and activated factor X by antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	134-150
10078261-0	1992	C3a and C5a anaphylatoxins bind to heparin-based sorbent in low density lipoprotein apheresis: in vitro and in vivo investigations.	Heparin	35-42	complement C3	Homo sapiens	0-3
10420071-1	1998	Unfractionated heparin (UFH) exerts its anticoagulant properties by increasing the inactivation of thrombin and activated factor X by antithrombin III.	Heparin	24-27	serpin family C member 1	Homo sapiens	134-150
10078261-10	1992	The removal of C3a and C5a anaphylatoxins by heparin-based sorbent should be regarded as an advantage of this type of plasmasorbent.	Heparin	45-52	complement C3	Homo sapiens	15-18
9759919-1	1998	The modulatory effect of heparin and dextran sulfate 500,000 (sulfated polysaccharides) was studied on ATPDase and 5"-nucleotidase activities.	Heparin	25-32	ectonucleoside triphosphate diphosphohydrolase 1	Homo sapiens	103-110
1628222-1	1992	The extracellular matrix protein heparin sulfate proteoglycans (HSPG) has been found in the neurofibrillary pathology of Alzheimer disease.	Heparin	33-40	syndecan 2	Homo sapiens	64-68
9688635-6	1998	Competitive binding studies suggest that the kringle 1, 4, and 5 domains of Glu-Pg and the heparin-binding domain of IGFBP-3 participate in forming the IGFBP-3/Glu-Pg complex, and other studies show that Glu-Pg in this complex is activated at a normal rate by tissue Pg activator.	Heparin	91-98	insulin like growth factor binding protein 3	Homo sapiens	117-124
1520630-5	1992	Heparin affinity chromatography on radio-iodinated cell lysates followed by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulphate revealed a 130 kD heparin binding protein.	Heparin	0-7	azurocidin 1	Homo sapiens	171-194
9688635-6	1998	Competitive binding studies suggest that the kringle 1, 4, and 5 domains of Glu-Pg and the heparin-binding domain of IGFBP-3 participate in forming the IGFBP-3/Glu-Pg complex, and other studies show that Glu-Pg in this complex is activated at a normal rate by tissue Pg activator.	Heparin	91-98	insulin like growth factor binding protein 3	Homo sapiens	152-159
9597549-6	1998	Murine IL-2 unlike its human counterpart fails to bind to heparin.	Heparin	58-65	interleukin 2	Mus musculus	7-11
1579960-9	1992	CONCLUSIONS: When 100 mg of recombinant tissue plasminogen activator was given within the first 6 hours of acute stroke together with heparin the incidence of deleterious hemorrhage was less than 10%.	Heparin	134-141	chromosome 20 open reading frame 181	Homo sapiens	40-68
9525959-3	1998	The membrane-associated platelet CKII kinase was partially purified using heparin-agarose, phosphocellulose, and ion exchange chromatography.	Heparin	74-81	casein kinase 2 alpha 1	Homo sapiens	33-37
1622334-4	1992	ECP levels in serum or heparin plasma increased time-dependently until 2 hr.	Heparin	23-30	ribonuclease A family member 3	Homo sapiens	0-3
9597517-2	1998	The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex.	Heparin	29-36	serpin family C member 1	Homo sapiens	75-91
1622334-7	1992	ECP levels were always in the order of serum greater than heparin plasma greater than EDTA plasma.	Heparin	58-65	ribonuclease A family member 3	Homo sapiens	0-3
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	44-51	coagulation factor X	Homo sapiens	118-127
9597517-2	1998	The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex.	Heparin	29-36	serpin family C member 1	Homo sapiens	225-241
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	94-101	coagulation factor X	Homo sapiens	118-127
1321995-1	1992	The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses.	Heparin	94-101	coagulation factor X	Homo sapiens	118-127
9592979-5	1998	RESULTS: The industrial batches show a purity higher than 99% with approximately 95% native heparin binding ATIII.	Heparin	92-99	serpin family C member 1	Homo sapiens	108-113
1371276-2	1992	Previous experiments have shown that heparin inhibits induction of c-fos and c-myc protooncogene mRNA in rat VSMC stimulated by phorbol 12-myristate 13-acetate (PMA) but not when stimulated by epidermal growth factor (EGF) (Pukac, L. A., Castellot, J. J., Wright, T. C., Caleb, B. L., and Karnovsky, M. J.	Heparin	37-44	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	67-72
1371276-6	1992	Heparin inhibited serum stimulation of c-fos mRNA in control VSMC, but heparin did not inhibit the smaller but significant serum stimulation of c-fos mRNA in PKC down-regulated VSMC, indicating that heparin may selectively inhibit PKC-dependent, but not PKC-independent, stimulation of gene expression.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	39-44
1320301-4	1992	We also observed that heparin and other sulfated polysaccharides had an accelerating effect on thrombin cleavage of recombinant scu-PA. Their effect was concentration-dependent and then reversed at high levels.	Heparin	22-29	prothrombin	Oryctolagus cuniculus	95-103
1385732-7	1992	To determine the mechanism by which heparin enhanced alternative pathway activity, binding studies with radiolabeled factor B and factor H were performed.	Heparin	36-43	complement factor H	Homo sapiens	130-138
1385732-11	1992	These data demonstrate that heparin immobilized onto CA hemodialysis membrane enhances C3 activation but produces low levels of C3a in the fluid phase because of high surface adsorption of the anaphylatoxin.	Heparin	28-35	complement C3	Homo sapiens	128-131
1319617-1	1992	Effects of zinc and calcium ions on the heparin-neutralizing abilities of histidine-rich glycoprotein (HRG) and platelet factor 4 (PF4) were examined.	Heparin	40-47	histidine rich glycoprotein	Homo sapiens	74-101
1319617-1	1992	Effects of zinc and calcium ions on the heparin-neutralizing abilities of histidine-rich glycoprotein (HRG) and platelet factor 4 (PF4) were examined.	Heparin	40-47	histidine rich glycoprotein	Homo sapiens	103-106
1319617-2	1992	Both HRG and PF4 effectively neutralized the ability of heparin to accelerate the activated protein C (APC) and the thrombin inhibitions by protein C inhibitor (PCI).	Heparin	56-63	histidine rich glycoprotein	Homo sapiens	5-8
1319617-3	1992	the heparin-neutralizing ability of HRG in the APC inhibition by PCI, however, was decreased in a Ca(2+)-dependent manner and apparently lost at 1 mM Ca2+, while it was enhanced by Zn2+ regardless of the presence or absence of Ca2+.	Heparin	4-11	histidine rich glycoprotein	Homo sapiens	36-39
1391202-5	1992	Heparin interactions with the anion-binding site of the high molecular weight recognition center in the alpha-thrombin molecule did not significantly influence the values of the kinetic constants for the enzyme inhibition by SA-152.	Heparin	0-7	coagulation factor II, thrombin	Bos taurus	110-118
1525562-4	1992	It showed the essential features of casein kinase II activity: utilization of GTP in addition to ATP as a phosphate donor, strong inhibition by heparin, preference for acidic protein substrates, salt-induced binding to phosphocellulose, and salt-dependent deaggregation.	Heparin	144-151	casein kinase II, alpha chain 2	Arabidopsis thaliana	36-52
1724341-6	1991	These results indicate that both aFGF and bFGF can stimulate bone resorption by a prostaglandin-independent mechanism, particularly in the presence of heparin.	Heparin	151-158	fibroblast growth factor 1	Rattus norvegicus	33-37
1814436-5	1991	The resulting construct is able to drive the expression of a high amount of FGF-6 protein in Escherichia coli, which can be solubilized and purified through heparin-Sepharose chromatography and high salt elution.	Heparin	157-164	fibroblast growth factor 6	Mus musculus	76-81
1719529-1	1991	Mouse vitronectin (Vn) was isolated from serum by heparin affinity chromatography.	Heparin	50-57	vitronectin	Mus musculus	19-21
1804351-2	1991	Thrombin was modified with FITC in the presence of heparin and was separated from heparin and free FITC by gel-filtration at HPLC yielding FITC-labeled alpha-thrombin with intact additional recognition binding site for high molecular substrates and cell receptors.	Heparin	51-58	coagulation factor II, thrombin	Bos taurus	0-8
1720904-0	1991	Limited proteolysis of vitronectin by plasmin destroys heparin binding activity.	Heparin	55-62	vitronectin	Homo sapiens	23-34
1720904-7	1991	This minimal proteolysis destroyed the binding of [3H]-heparin to VN and reversed the neutralization of heparin by VN.	Heparin	55-62	vitronectin	Homo sapiens	66-68
1720904-7	1991	This minimal proteolysis destroyed the binding of [3H]-heparin to VN and reversed the neutralization of heparin by VN.	Heparin	104-111	vitronectin	Homo sapiens	115-117
1834337-3	1991	The catheter was removed after 30 min and heparin treatment was continued for 24 h. Alpha-2-antiplasmin was initially reduced by 13% and normalized 2 h after SET, indicating that only small amounts of free plasmin were liberated during thrombolysis.	Heparin	42-49	serpin family F member 2	Homo sapiens	84-103
1716635-3	1991	Immunoblotting of crude and heparin-bound embryo extracts revealed faint bands at the expected 17-18-kD and predominant bands at an apparent molecular mass of 26 to 28-kD (despite reducing conditions) using multiple specific antibodies for aFGF and bFGF.	Heparin	28-35	fibroblast growth factor 1	Rattus norvegicus	240-244
1771613-0	1991	Comparison of the effects of heparin and hirudin on thrombin binding to the normal and the de-endothelialized rabbit aorta in vitro.	Heparin	29-36	prothrombin	Oryctolagus cuniculus	52-60
1771613-1	1991	The properties of heparin and hirudin to inhibit thrombin from binding to the freshly-excised rabbit aorta wall were compared in vitro.	Heparin	18-25	prothrombin	Oryctolagus cuniculus	49-57
1771613-2	1991	When aorta segments were incubated with 125I-thrombin (4.4 +/- 0.4 nM) in the presence of heparin or hirudin, both anticoagulants inhibited 125I-thrombin binding to the endothelium in a concentration-dependent manner (IC50: 0.1 USP U heparin/ml; 0.1 ATU hirudin/ml).	Heparin	90-97	prothrombin	Oryctolagus cuniculus	45-53
1771613-2	1991	When aorta segments were incubated with 125I-thrombin (4.4 +/- 0.4 nM) in the presence of heparin or hirudin, both anticoagulants inhibited 125I-thrombin binding to the endothelium in a concentration-dependent manner (IC50: 0.1 USP U heparin/ml; 0.1 ATU hirudin/ml).	Heparin	90-97	prothrombin	Oryctolagus cuniculus	145-153
1771613-2	1991	When aorta segments were incubated with 125I-thrombin (4.4 +/- 0.4 nM) in the presence of heparin or hirudin, both anticoagulants inhibited 125I-thrombin binding to the endothelium in a concentration-dependent manner (IC50: 0.1 USP U heparin/ml; 0.1 ATU hirudin/ml).	Heparin	234-241	prothrombin	Oryctolagus cuniculus	45-53
1771613-2	1991	When aorta segments were incubated with 125I-thrombin (4.4 +/- 0.4 nM) in the presence of heparin or hirudin, both anticoagulants inhibited 125I-thrombin binding to the endothelium in a concentration-dependent manner (IC50: 0.1 USP U heparin/ml; 0.1 ATU hirudin/ml).	Heparin	234-241	prothrombin	Oryctolagus cuniculus	145-153
1771613-3	1991	Endothelium-bound 125I-thrombin was displaced by either heparin (50% liberated at 4.1 U/ml) or hirudin (0.4 U/ml).	Heparin	56-63	prothrombin	Oryctolagus cuniculus	23-31
1771613-4	1991	Using de-endothelialized aortas, heparin inhibited thrombin binding by the exposed subendothelium (IC50: 1.8 U/ml) whereas hirudin was without effect.	Heparin	33-40	prothrombin	Oryctolagus cuniculus	51-59
1771613-6	1991	These observations suggest that both heparin and hirudin mask the binding site on thrombin to the endothelial cell membrane.	Heparin	37-44	prothrombin	Oryctolagus cuniculus	82-90
1771613-7	1991	A separate site on thrombin must bind to the subendothelium because only heparin inhibits binding.	Heparin	73-80	prothrombin	Oryctolagus cuniculus	19-27
1873225-2	1991	However, whereas heparin significantly decreased the plasma levels of F 1 + 2 and of TAT complexes in less than 3 d. D-dimer levels were not significantly altered.	Heparin	17-24	coagulation factor XII	Homo sapiens	70-77
1873225-4	1991	These results indicate that heparin improves the hypercoagulable state associated with a deep vein thrombosis within the first days of treatment as indicated by TAT and F 1 + 2.	Heparin	28-35	coagulation factor XII	Homo sapiens	169-176
2070046-1	1991	Inhibition of prothrombinase by antithrombin III (ATIII) and heparin was investigated in a continuous-flow system.	Heparin	61-68	coagulation factor X	Homo sapiens	14-28
2070046-9	1991	Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly.	Heparin	15-22	coagulation factor X	Homo sapiens	133-147
2070046-9	1991	Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly.	Heparin	15-22	coagulation factor X	Homo sapiens	262-276
2070046-9	1991	Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly.	Heparin	57-64	coagulation factor X	Homo sapiens	133-147
2070046-9	1991	Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly.	Heparin	57-64	coagulation factor X	Homo sapiens	262-276
2070046-10	1991	The findings reported here support the notion that regulation of prothrombinase by heparin under in vivo conditions occurs at the stage of its formation, ie, through inhibition of free factor Xa and/or the generation of factor Va, rather than by direct inhibition of the prothrombinase activity.	Heparin	83-90	coagulation factor X	Homo sapiens	65-79
2070046-10	1991	The findings reported here support the notion that regulation of prothrombinase by heparin under in vivo conditions occurs at the stage of its formation, ie, through inhibition of free factor Xa and/or the generation of factor Va, rather than by direct inhibition of the prothrombinase activity.	Heparin	83-90	coagulation factor X	Homo sapiens	271-285
1709100-6	1991	The insulin-binding sites of laminin and vitronectin were located in the A chain and in the heparin-binding domain, respectively.	Heparin	92-99	vitronectin	Mus musculus	41-52
2040287-4	1991	The recombinant CKII alpha subunit was purified by DEAE-cellulose chromatography, followed by phosphocellulose and heparin-agarose chromatography.	Heparin	115-122	casein kinase 2 alpha 2	Homo sapiens	16-26
1897961-11	1991	Binding of gp 80 to heparin-agarose or fibrin-Sepharose, however, was inhibited in the presence of added fibronectin or the monoclonal antibody.	Heparin	20-27	clusterin	Canis lupus familiaris	11-16
1897961-11	1991	Binding of gp 80 to heparin-agarose or fibrin-Sepharose, however, was inhibited in the presence of added fibronectin or the monoclonal antibody.	Heparin	20-27	fibronectin 1	Canis lupus familiaris	105-116
2019790-3	1991	We have also reported that dermatan sulfate, which catalyzes thrombin inhibition by heparin cofactor II, inhibits thrombus growth in rabbits more effectively than heparin.	Heparin	84-91	prothrombin	Oryctolagus cuniculus	61-69
1878883-4	1991	spectroscopy showed that sulfation occurred selectively at C-3 of residue 7, to give a new polymer that may be described as a 3-sulfate analog of heparin.	Heparin	146-153	complement C3	Homo sapiens	59-62
1706595-1	1991	This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis.	Heparin	116-123	coagulation factor X	Homo sapiens	190-199
1706595-1	1991	This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis.	Heparin	146-153	coagulation factor X	Homo sapiens	190-199
1706595-3	1991	1 mol/mol), that it is targeted to one site (Ser-378) at the C-terminal edge of the heparin-binding domain, and that it distinguishes between the two physiologically occurring forms of vitronectin: the one-chain (75 kDa) form, and the nicked two-chain (65 + 10 kDa) form, held together by an interchain disulphide bridge.	Heparin	84-91	vitronectin	Homo sapiens	185-196
1992009-4	1991	Acidic FGF and bFGF from extracts of nervous tissue were found to differ considerably in their relative dependencies upon heparin to potentiate their mitogenic activities: the effect of aFGF was strongly dependent upon heparin, whereas the effect of bFGF was only slightly potentiated by heparin.	Heparin	122-129	fibroblast growth factor 1	Rattus norvegicus	186-190
1992009-5	1991	Heparin was also found to stimulate differentially the mitogenic activity of extracts prepared from different areas of the nervous system, indicating that spinal cord, cortex, pituitary, and optic nerve contained different ratios of aFGF to bFGF, whereas sciatic nerve contained extremely high levels of only aFGF.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	233-237
1992009-5	1991	Heparin was also found to stimulate differentially the mitogenic activity of extracts prepared from different areas of the nervous system, indicating that spinal cord, cortex, pituitary, and optic nerve contained different ratios of aFGF to bFGF, whereas sciatic nerve contained extremely high levels of only aFGF.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	309-313
2018206-0	1991	In vitro studies of the interaction between heparin and eosinophil cationic protein.	Heparin	44-51	ribonuclease A family member 3	Homo sapiens	56-83
2018206-3	1991	The present in vitro study shows that ECP can inactivate the anticoagulant activity of heparin probably by the formation of a complex between the two molecules.	Heparin	87-94	ribonuclease A family member 3	Homo sapiens	38-41
2268268-11	1990	Heparin prolonged by 15 s and 45 s the time required to demonstrate Factor V activation in CAP supplemented with Factor Xa and thrombin respectively.	Heparin	0-7	coagulation factor X	Homo sapiens	113-122
2268268-17	1990	The availability of Factor Xa markedly moderates the ability of heparin to inhibit Factor V activation.	Heparin	64-71	coagulation factor X	Homo sapiens	20-29
2128972-0	1990	Heparin stimulates fibrinolysis in mesothelial cells by selective induction of tissue-plasminogen activator but not plasminogen activator inhibitor-1 synthesis.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	79-107
2128972-2	1990	Heparin (100 U/ml) as well as pentosan polysulfate (300 micrograms/ml) stimulated tPA synthesis by HOMC 2.9-4.5-fold.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	82-85
2128972-3	1990	Heparin-induced tPA production was dose- and time-dependent and was inhibited by cycloheximide.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	16-19
2248954-1	1990	Factor Xa modified by reductive methylation (greater than 92%) loses the capacity to bind heparin as determined both by gel chromatography and by sedimentation equilibrium ultracentrifugation.	Heparin	90-97	coagulation factor X	Homo sapiens	0-9
2248954-5	1990	These findings provide direct evidence that the interaction of factor Xa with heparin is not involved in the heparin-enhanced inhibition of this enzyme.	Heparin	78-85	coagulation factor X	Homo sapiens	63-72
1964634-11	1990	After intravenous administration of low molecular weight heparin, the half-life of the anti-factor Xa activity is considerably longer than for unfractionated heparin, while the anti-factor IIa half-lives are similar.	Heparin	57-64	coagulation factor X	Homo sapiens	92-101
2394942-0	1990	The importance of anti-factor Xa and antithrombin activities of low molecular weight heparins.	Heparin	85-93	coagulation factor X	Homo sapiens	23-32
2166682-8	1990	Binding of Ins 1,3,4,5-P4 was maximal in the pH range between 4.5 and 6, was stable with Ca2+ concentration varied from 1 nM to 1 mM, and was suppressed by heparin (IC50 about 2 nM).	Heparin	156-163	forkhead box M1	Homo sapiens	11-16
2364492-1	1990	Heparin liberates FPR-thrombin from the endothelium in vivo.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	22-30
2364492-2	1990	Thrombin rapidly binds to and saturates rabbit aorta endothelium in vitro, a process that depends on pericellular glycosaminoglycans and that is inhibited by heparin.	Heparin	158-165	prothrombin	Oryctolagus cuniculus	0-8
2364492-4	1990	The binding characteristics of thrombin and FPR-thrombin to heparin-Sepharose and to the endothelial surface of rabbit aorta segments in vitro were compared.	Heparin	60-67	prothrombin	Oryctolagus cuniculus	31-39
2364492-4	1990	The binding characteristics of thrombin and FPR-thrombin to heparin-Sepharose and to the endothelial surface of rabbit aorta segments in vitro were compared.	Heparin	60-67	prothrombin	Oryctolagus cuniculus	48-56
2364492-9	1990	Heparin, administered at various times after 125I-FPR-thrombin, liberated a significant proportion of 125I-FPR-thrombin from the endothelial surface into the plasma compartment as shown by a pronounced "spike" on the plasma curve, a concomitant loss of radioactivity from the lung and from the aorta endothelium, and analysis of the radioactive components of plasma taken before and after heparin injection.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	54-62
2364492-9	1990	Heparin, administered at various times after 125I-FPR-thrombin, liberated a significant proportion of 125I-FPR-thrombin from the endothelial surface into the plasma compartment as shown by a pronounced "spike" on the plasma curve, a concomitant loss of radioactivity from the lung and from the aorta endothelium, and analysis of the radioactive components of plasma taken before and after heparin injection.	Heparin	0-7	prothrombin	Oryctolagus cuniculus	111-119
2364492-10	1990	Thus, FPR-thrombin was cleared rapidly from the circulation, and endothelium-bound FPR-thrombin was released into the circulation by heparin.	Heparin	133-140	prothrombin	Oryctolagus cuniculus	87-95
2116167-6	1990	t-PA and generated plasmin bound to the liposome surface heparin were protected from inhibition by plasminogen activator inhibitor type 1 and alpha 2-plasmin inhibitor, respectively.	Heparin	57-64	serpin family F member 2	Homo sapiens	142-167
1692629-8	1990	The binding site for sialic acid appears to reside on factor H, since factor H bound to heparin-agarose and to sialic acid-bearing fetuinagarose, whereas C3b bound to neither under the same conditions.	Heparin	88-95	complement factor H	Homo sapiens	54-62
1692629-8	1990	The binding site for sialic acid appears to reside on factor H, since factor H bound to heparin-agarose and to sialic acid-bearing fetuinagarose, whereas C3b bound to neither under the same conditions.	Heparin	88-95	complement factor H	Homo sapiens	70-78
2363127-1	1990	The antithrombotic and haemostatic effects of a pentasaccharide, the chemically synthesized antithrombin III (AT-III) binding fragment of heparin (PENTA), were investigated in rats in comparison with heparin.	Heparin	138-145	serpin family C member 1	Rattus norvegicus	92-108
2363127-1	1990	The antithrombotic and haemostatic effects of a pentasaccharide, the chemically synthesized antithrombin III (AT-III) binding fragment of heparin (PENTA), were investigated in rats in comparison with heparin.	Heparin	138-145	serpin family C member 1	Rattus norvegicus	110-116
2099192-0	1990	Heparin inhibits c-fos and c-myc mRNA expression in vascular smooth muscle cells.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	17-22
2099192-2	1990	In this paper we show that heparin suppressed the induction of c-fos and c-myc mRNA in rat and calf VSMC.	Heparin	27-34	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	63-68
2099192-5	1990	The effect of heparin on c-fos mRNA induction was selective for specific mitogens, as heparin inhibited c-fos mRNA induction in phorbol 12-myristate 13-acetate (TPA) stimulated but not epidermal growth factor (EGF) stimulated VSMC.	Heparin	14-21	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	25-30
2099192-5	1990	The effect of heparin on c-fos mRNA induction was selective for specific mitogens, as heparin inhibited c-fos mRNA induction in phorbol 12-myristate 13-acetate (TPA) stimulated but not epidermal growth factor (EGF) stimulated VSMC.	Heparin	14-21	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	104-109
2099192-5	1990	The effect of heparin on c-fos mRNA induction was selective for specific mitogens, as heparin inhibited c-fos mRNA induction in phorbol 12-myristate 13-acetate (TPA) stimulated but not epidermal growth factor (EGF) stimulated VSMC.	Heparin	86-93	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	25-30
2099192-5	1990	The effect of heparin on c-fos mRNA induction was selective for specific mitogens, as heparin inhibited c-fos mRNA induction in phorbol 12-myristate 13-acetate (TPA) stimulated but not epidermal growth factor (EGF) stimulated VSMC.	Heparin	86-93	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	104-109
2347871-8	1990	In addition, a portion of the surface-bound heparin maintains its original bioactivity as determined by recalcification times, thrombin times, and Factor Xa assays.	Heparin	44-51	prothrombin	Oryctolagus cuniculus	127-135
2106684-0	1990	Fractionation of heparin by chromatography on a tissue plasminogen activator-Sepharose column.	Heparin	17-24	chromosome 20 open reading frame 181	Homo sapiens	48-76
2106684-1	1990	Heparin stimulates the activity of tissue plasminogen activator (t-PA) and binds to t-PA.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	65-69
2106684-3	1990	This procedure selectively links the t-PA to the column because the acetylated heparin has no free amino groups.	Heparin	79-86	chromosome 20 open reading frame 181	Homo sapiens	37-41
2106684-5	1990	The t-PA column separates heparin into two fractions, one with low affinity for t-PA and one with high affinity.	Heparin	26-33	chromosome 20 open reading frame 181	Homo sapiens	4-8
2106684-7	1990	However, the fractions differ in their ability to stimulate t-PA: the low-affinity heparin has no effect on the activity of t-PA, whereas the high-affinity heparin enhances this activity.	Heparin	83-90	chromosome 20 open reading frame 181	Homo sapiens	60-64
2106684-7	1990	However, the fractions differ in their ability to stimulate t-PA: the low-affinity heparin has no effect on the activity of t-PA, whereas the high-affinity heparin enhances this activity.	Heparin	156-163	chromosome 20 open reading frame 181	Homo sapiens	60-64
2106684-8	1990	These heparin fractions will be useful in characterizing the biochemical basis and physiological consequences of the heparin--t-PA interaction.	Heparin	6-13	chromosome 20 open reading frame 181	Homo sapiens	126-130
2106684-8	1990	These heparin fractions will be useful in characterizing the biochemical basis and physiological consequences of the heparin--t-PA interaction.	Heparin	117-124	chromosome 20 open reading frame 181	Homo sapiens	126-130
2104849-13	1990	Chromatography studies with heparin-Sepharose indicated that at least some of the lipoprotein lipase in cld/cld cells was dimerized.	Heparin	28-35	lipoprotein lipase	Mus musculus	82-100
2155017-3	1990	The LMW heparin dose necessary (anti FXa-activity) for effective anticoagulation was two thirds of the standard heparin dose.	Heparin	8-15	coagulation factor X	Homo sapiens	37-40
22374861-4	2012	Heparin was given at prophylactic dosage in patients at low risk and at fixed subtherapeutic doses (3,800 or 4,000 UI anti-FXa, b.i.d.)	Heparin	0-7	coagulation factor X	Homo sapiens	123-126
34287985-8	2022	The prolongation of INR was related to the high heparin level in the perfusate (anti-FXa > 3 U/ml).	Heparin	48-55	coagulation factor X	Homo sapiens	85-88
10684486-5	1998	Heparin increased PLT CD62 expression, which was significantly more pronounced in group 1 patients with plasma heparin levels less than 0.7 U/mL and ACT of 222 +/- 52 seconds compared with group 2 patients with heparin levels greater than 0.7 U/mL and ACT of 365 +/- 86 seconds (8 +/- 9 v -1 +/- 4% change in resulting PLTs, P =.01, and 11 +/- 12 v 1 +/- 6% increase in adenosine diphosphate (ADP) [5 microM]-stimulated PLTs, P =.02).	Heparin	0-7	selectin P	Homo sapiens	22-26
34601007-4	2022	Moreover, we found that the heparin-binding motif-containing regions of Cfl1, i.e., Cfl19-25, Cfl134-51 and Cfl1108-125, like rCfl1, were also able to bind to LPS and LTA and to inhibit the bacterial growth.	Heparin	28-35	cofilin 1	Rattus norvegicus	126-131
9521646-0	1998	Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin.	Heparin	103-110	serpin family C member 1	Homo sapiens	29-41
34868360-7	2022	Heparin binding epidermal growth factor (EGF)-like growth factor, transforming growth factor beta1 (TGFB1) and thyroid hormone receptor alpha (THRA) mRNA expression was higher in HER2-positive patients (P=0.026, P<0.001 and P<0.001).	Heparin	0-7	thyroid hormone receptor alpha	Homo sapiens	111-141
9521646-1	1998	Regulation of the inhibitory activity of antithrombin, the principal inhibitor of the blood-clotting proteinases factor Xa and thrombin, is accomplished by binding to heparin.	Heparin	167-174	serpin family C member 1	Homo sapiens	41-53
34868360-7	2022	Heparin binding epidermal growth factor (EGF)-like growth factor, transforming growth factor beta1 (TGFB1) and thyroid hormone receptor alpha (THRA) mRNA expression was higher in HER2-positive patients (P=0.026, P<0.001 and P<0.001).	Heparin	0-7	thyroid hormone receptor alpha	Homo sapiens	143-147
9521646-2	1998	We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa.	Heparin	214-221	serpin family C member 1	Homo sapiens	18-30
9521646-2	1998	We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa.	Heparin	214-221	serpin family C member 1	Homo sapiens	236-248
9521646-3	1998	By derivatization of this cysteine with a bulky group, fluorescein, the antithrombin became permanently and fully activated toward reaction with factor Xa in a manner analogous to heparin activation, albeit as a substrate.	Heparin	180-187	serpin family C member 1	Homo sapiens	72-84
9521646-4	1998	These findings establish a structural basis for the mechanism of heparin activation of antithrombin against factor Xa in agreement with that proposed from an X-ray structure of antithrombin.	Heparin	65-72	serpin family C member 1	Homo sapiens	87-99
34905596-10	2022	Moreover, CXCR7-agonist regulated heparin-induced thrombocytopenia-(HIT)-sera/IgG-induced platelet and neutrophil activation, heparin induced platelet aggregation-(HIPA), generation of COX-1-(TxA2), 12-LOX-(12-HETE) derived thrombo-inflammatory lipids, platelet-neutrophil aggregate formation, and thrombo-inflammatory secretion (sCD40L, IL-1beta, IFN-gamma, TNF-alpha, sP-selectin, IL-8, tissue factor-TF) ex vivo.	Heparin	34-41	atypical chemokine receptor 3	Homo sapiens	10-15
9521646-4	1998	These findings establish a structural basis for the mechanism of heparin activation of antithrombin against factor Xa in agreement with that proposed from an X-ray structure of antithrombin.	Heparin	65-72	serpin family C member 1	Homo sapiens	177-189
9541411-7	1998	When the heparin pentasaccharide is bound to antithrombin prior to incubation with thermolysin, it protects the N-terminal cleavage site, implying that segment 22-46 moves to interact with heparin in the conformational change and thus stabilizes the complex.	Heparin	189-196	serpin family C member 1	Homo sapiens	45-57
9468491-2	1998	We investigated the effect of VEGF on heparin-binding epidermal growth factor-like growth factor (HB-EGF) expression in human umbilical vein endothelial cells.	Heparin	38-45	heparin binding EGF like growth factor	Homo sapiens	98-104
33183091-1	2021	OBJECTIVE: To illustrate the effect of corticosteroids and heparin, respectively, on Coronavirus Disease 2019 (COVID-19) patients" CD8+ T cells and D-Dimer.	Heparin	59-66	CD8a molecule	Homo sapiens	131-134
33183091-4	2021	Segmented regression was performed to examine the influence of corticosteroids and heparin upon CD8+ T cell and D-Dimer, respectively.	Heparin	83-90	CD8a molecule	Homo sapiens	96-99
9570475-11	1998	The [14C]5-HT release caused by these phospholipase A2 homologues were reduced by p-bromophenacyl bromide and heparin (50 IU/ml).	Heparin	110-117	phospholipase A2 group IB	Rattus norvegicus	38-54
9570475-13	1998	Since heparin greatly reduced the oedematogenic activity of these phospholipase A2 homologues, it is likely that the cationic charge of these substances plays a major role in the mast cell activation.	Heparin	6-13	phospholipase A2 group IB	Rattus norvegicus	66-82
34259662-17	2021	CONCLUSIONS: We observed a high prevalence of reduced coagulation factor XII activity in adult patients on extracorporeal membrane oxygenation, which may confound activated partial thromboplastin time measurements and limit its clinical usefulness for monitoring and titrating anticoagulation with unfractionated heparin.	Heparin	313-320	coagulation factor XII	Homo sapiens	54-76
9461624-6	1998	We therefore conclude that a major portion of extracellular collagen-tailed AChE is extractable from rat and Torpedo synaptic basal lamina by high ionic strength and heparin buffers, although some non-extractable AChE activity remains associated with the junctional regions.	Heparin	166-173	acetylcholinesterase	Rattus norvegicus	76-80
34884486-11	2021	Preincubation with heparin, autotaxin (ATX) inhibitor HA130 or lysophosphatidic acid (LPA) receptor antagonist Ki16425 reduced PLA1A-induced-secretion of IL-8.	Heparin	19-26	phospholipase A1 member A	Homo sapiens	127-132
9651145-6	1998	Heparin strikingly enhanced antithrombin III"s inhibition of Xa and resulted in complete abrogation of the complex formation between h-rTFPI and Xa in the absence or presence of acidic phospholipids.	Heparin	0-7	serpin family C member 1	Homo sapiens	28-44
9651145-7	1998	Furthermore, antithrombin III induced dissociation of the preformed h-rTFPI/Xa complex in the presence of heparin.	Heparin	106-113	serpin family C member 1	Homo sapiens	13-29
9651145-8	1998	These results suggest that in the presence of heparin, antithrombin III interferes with the catabolism of TFPI mediated via Xa.	Heparin	46-53	serpin family C member 1	Homo sapiens	55-71
34816442-2	2022	This study aimed to: (i) develop a PK/PD model for UFH, quantified by anti-factor Xa assay and the UFH effect measured by activated partial thromboplastin time (aPTT) (ii) evaluate pediatric UFH infusions in achieving anti-factor Xa (0.3 - 0.7 IU/mL) therapeutic target by simulations.	Heparin	51-54	coagulation factor X	Homo sapiens	75-84
34816442-2	2022	This study aimed to: (i) develop a PK/PD model for UFH, quantified by anti-factor Xa assay and the UFH effect measured by activated partial thromboplastin time (aPTT) (ii) evaluate pediatric UFH infusions in achieving anti-factor Xa (0.3 - 0.7 IU/mL) therapeutic target by simulations.	Heparin	51-54	coagulation factor X	Homo sapiens	223-232
34580885-7	2022	As a result, the LPL activity in post-heparin plasma was substantially increased, and postprandial plasma triglyceride clearance was significantly enhanced, while plasma triglyceride levels were decreased.	Heparin	38-45	lipoprotein lipase	Mus musculus	17-20
9485079-5	1998	Beta2-GPI was purified by heparin/cationic-exchange chromatography and was biotinylated or used to purify beta2-GPI-specific antibodies by affinity chromatography.	Heparin	26-33	apolipoprotein H	Homo sapiens	0-9
34604133-9	2021	Results: Anti-factor Xa levels showed a moderate correlation with heparin dose, whereas the other tests showed a weak correlation.	Heparin	66-73	coagulation factor X	Homo sapiens	14-23
9445371-6	1998	The study with a heparin-Sepharose column showed that 3T3-L1 adipocytes contained three forms of LPL.	Heparin	17-24	lipoprotein lipase	Homo sapiens	97-100
34604133-13	2021	Conclusions: Anti-factor Xa levels correlate better to heparin dose than activated clotting time.	Heparin	55-62	coagulation factor X	Homo sapiens	18-27
34604133-14	2021	The use of anti-factor Xa assay instead of activated clotting time for dosing of unfractionated heparin could reduce thrombotic complications in neonates with congenital diaphragmatic hernia on ECMO support.	Heparin	96-103	coagulation factor X	Homo sapiens	16-25
34153666-9	2021	In terms of the mechanism, heparin upregulated the expression of ERK, CREB, NF200, BDNF, NGF, PTN and syndecan-3 in the rat brains.	Heparin	27-34	syndecan 3	Rattus norvegicus	102-112
34153666-11	2021	CONCLUSION: Heparin attenuates the secondary brain injury induced by CA-CPR through regulating the ERK/CREB-mediated PTN/syndecan-3 pathway.	Heparin	12-19	syndecan 3	Rattus norvegicus	121-131
34489931-0	2021	Selective Binding of Heparin/Heparan Sulfate Oligosaccharides to Factor H and Factor H-Related Proteins: Therapeutic Potential for C3 Glomerulopathies.	Heparin	21-28	complement factor H	Homo sapiens	65-73
34489931-0	2021	Selective Binding of Heparin/Heparan Sulfate Oligosaccharides to Factor H and Factor H-Related Proteins: Therapeutic Potential for C3 Glomerulopathies.	Heparin	21-28	complement factor H	Homo sapiens	78-86
9445371-20	1998	These findings indicate that LPL synthesized in chlorate-treated cells can be processed to be fully active, but chlorate-treated cells are unable to transport LPL to the Golgi and accumulate inactive LPL with a lower affinity for heparin in the ER.	Heparin	230-237	lipoprotein lipase	Homo sapiens	29-32
34489931-13	2021	Addition of 2-O-desulfated heparin significantly reduced FHR1- and FHR5-mediated C3b deposition on ciGEnCs.	Heparin	27-34	complement factor H related 5	Homo sapiens	67-71
9521111-0	1998	Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin-induced conformers of antithrombin.	Heparin	79-86	serpin family C member 1	Homo sapiens	109-121
34489931-13	2021	Addition of 2-O-desulfated heparin significantly reduced FHR1- and FHR5-mediated C3b deposition on ciGEnCs.	Heparin	27-34	complement C3	Homo sapiens	81-84
9521111-1	1998	A pentasaccharide (PS) fragment of heparin capable of activating antithrombin (AT) markedly accelerates the inhibition of factor Xa by AT, but has insignificant effect on inhibition of thrombin.	Heparin	35-42	serpin family C member 1	Homo sapiens	65-77
9466731-6	1998	The stimulatory effects of thrombin (10 U/ml) can be inhibited by antithrombin III (2 U/ml) (a natural thrombin inhibitor) with heparin (2 U/ml), PPACK (D-Phe-Pro-ArgCH2Cl) (20-50 microg/ml) (a serine protease inhibitor), and PGE2 (0.5-1.0 microg/ml).	Heparin	128-135	serpin family C member 1	Homo sapiens	66-82
34179075-5	2021	The binding of heparin/HS to SV2-S is mainly determined by its overall sulfation with potential, minor contribution of specific SV2-S binding motifs.	Heparin	15-22	synaptic vesicle glycoprotein 2A	Homo sapiens	29-32
34179075-6	2021	The higher binding affinity of SV2-S G614 mutant to heparin and upregulated HS expression may be one of the mechanisms underlying the higher infectivity of the SARS-CoV-2 G614 variant and the high vulnerability of lung cancer patients to SARS-CoV-2 infection, respectively.	Heparin	52-59	synaptic vesicle glycoprotein 2A	Homo sapiens	31-34
34070790-4	2021	Structural constraint of OPN, by immobilization or by addition of heparin, is required for its strong ligation of CD44.	Heparin	66-73	CD44 molecule (Indian blood group)	Homo sapiens	114-118
9515777-7	1998	Interaction of AT III with heparin-like glycosaminoglycans (GAGs) on the endothelial cell surface appears to be important for this effect.	Heparin	27-34	serpin family C member 1	Homo sapiens	15-21
35594144-9	2022	We also investigated the effect of C-mannosylation on the folding and heparin-binding capacity of the Plasmodium falciparum TRAP TSR domain in silico, which suggested that this phenotype should be due to its involvement in the global stabilization of TSR residue side chain interactions.	Heparin	70-77	TRAP	Homo sapiens	124-128
9515777-8	1998	Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs.	Heparin	0-7	serpin family C member 1	Homo sapiens	46-52
9515777-8	1998	Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs.	Heparin	0-7	serpin family C member 1	Homo sapiens	67-73
35513125-0	2022	Soluble alpha-klotho and heparin modulate the pathologic cardiac actions of fibroblast growth factor 23 in chronic kidney disease.	Heparin	25-32	fibroblast growth factor 23	Homo sapiens	76-103
9515777-8	1998	Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs.	Heparin	113-120	serpin family C member 1	Homo sapiens	46-52
35513125-3	2022	A recent structural analysis revealed that the complex of FGF23 and FGFR1, the physiologic FGF23 receptor in the kidney, includes soluble alpha-klotho (klotho) and heparin, which both act as co-factors for FGF23/FGFR1 signaling.	Heparin	164-171	fibroblast growth factor 23	Homo sapiens	58-63
9515777-8	1998	Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs.	Heparin	113-120	serpin family C member 1	Homo sapiens	67-73
35513125-3	2022	A recent structural analysis revealed that the complex of FGF23 and FGFR1, the physiologic FGF23 receptor in the kidney, includes soluble alpha-klotho (klotho) and heparin, which both act as co-factors for FGF23/FGFR1 signaling.	Heparin	164-171	fibroblast growth factor 23	Homo sapiens	206-211
35513125-4	2022	Here, we investigated whether soluble klotho, a circulating protein with cardio-protective properties, and heparin, a factor that is routinely infused into patients with kidney failure during the hemodialysis procedure, regulate FGF23/FGFR4 signaling and effects in cardiac myocytes.	Heparin	107-114	fibroblast growth factor 23	Homo sapiens	229-234
9407097-3	1997	We have recently shown that full-length recombinant tau assembles into Alzheimer-like filaments upon incubation with heparin.	Heparin	117-124	microtubule associated protein tau	Homo sapiens	52-55
35513125-5	2022	We developed a plate-based binding assay to quantify affinities of specific FGF23/FGFR interactions, and found that soluble klotho and heparin mediate FGF23 binding to distinct FGFR isoforms.	Heparin	135-142	fibroblast growth factor 23	Homo sapiens	76-81
35513125-5	2022	We developed a plate-based binding assay to quantify affinities of specific FGF23/FGFR interactions, and found that soluble klotho and heparin mediate FGF23 binding to distinct FGFR isoforms.	Heparin	135-142	fibroblast growth factor 23	Homo sapiens	151-156
35513125-6	2022	Heparin specifically mediated FGF23 binding to FGFR4, and increased FGF23 stimulatory effects on hypertrophic growth and contractility in isolated cardiac myocytes.	Heparin	0-7	fibroblast growth factor 23	Homo sapiens	30-35
35513125-6	2022	Heparin specifically mediated FGF23 binding to FGFR4, and increased FGF23 stimulatory effects on hypertrophic growth and contractility in isolated cardiac myocytes.	Heparin	0-7	fibroblast growth factor 23	Homo sapiens	68-73
35513125-7	2022	When repetitively injected into two different mouse models with elevated serum FGF23 levels, heparin aggravated cardiac hypertrophy.	Heparin	93-100	fibroblast growth factor 23	Mus musculus	79-84
35513125-9	2022	Thus, soluble klotho and heparin act as independent FGF23 co-receptors with opposite effects on the pathologic actions of FGF23, with soluble klotho reducing and heparin increasing FGF23-induced cardiac hypertrophy.	Heparin	25-32	fibroblast growth factor 23	Mus musculus	52-57
35229724-7	2022	GPIHBP1 trafficking across ECs in the mutant mice was normalized by disrupting LPL-HSPG electrostatic interactions with either heparin or an AD peptide.	Heparin	127-134	lipoprotein lipase	Mus musculus	79-82
35242277-7	2022	Here, we used pharmacological inhibitors and transfection with siRNA to evaluate whether matrix metalloprotease (MMP)2/9, heparin-binding- (HB-) epidermal growth factor (EGF), EGF receptor (EGFR), PI3K/Akt, MAPKs, and transcription factor AP-1 participated in the S1P-induced COX-2/PGE2 system determined by Western blotting, real-time polymerase chain reaction (RT-PCR), chromatin immunoprecipitation (ChIP), and promoter-reporter assays in HCFs.	Heparin	122-129	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	239-243
9407097-4	1997	Heparin also promotes phosphorylation of tau by a number of protein kinases, prevents tau from binding to taxol-stabilized microtubules, and produces rapid disassembly of microtubules assembled from tau and tubulin.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	41-44
9407097-4	1997	Heparin also promotes phosphorylation of tau by a number of protein kinases, prevents tau from binding to taxol-stabilized microtubules, and produces rapid disassembly of microtubules assembled from tau and tubulin.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	86-89
9407097-4	1997	Heparin also promotes phosphorylation of tau by a number of protein kinases, prevents tau from binding to taxol-stabilized microtubules, and produces rapid disassembly of microtubules assembled from tau and tubulin.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	86-89
34655821-2	2022	The ability to monitor low-molecular-weight heparin by obtaining anti-factor Xa (anti-Xa) serum levels provides an opportunity to evaluate safety and efficacy.	Heparin	44-51	coagulation factor X	Homo sapiens	70-79
9405673-0	1997	The anticoagulant activation of antithrombin by heparin.	Heparin	48-55	serpin family C member 1	Homo sapiens	32-44
9405673-6	1997	Concomitant conformational changes at the heparin binding site explain both the initial tight binding of antithrombin to the heparans and the subsequent release of the antithrombin-protease complex into the circulation.	Heparin	42-49	serpin family C member 1	Homo sapiens	105-117
9405673-6	1997	Concomitant conformational changes at the heparin binding site explain both the initial tight binding of antithrombin to the heparans and the subsequent release of the antithrombin-protease complex into the circulation.	Heparin	42-49	serpin family C member 1	Homo sapiens	168-180
9405673-8	1997	This clear definition of the binding site will provide a structural basis for developing heparin analogues that are more specific toward their intended target antithrombin and therefore less likely to exhibit side effects.	Heparin	89-96	serpin family C member 1	Homo sapiens	159-171
9422339-6	1997	A chemically modified heparin with low affinity for antithrombin III was added ex vivo or in vivo to displace heparin bound nonspecifically to plasma proteins.	Heparin	22-29	serpin family C member 1	Homo sapiens	52-68
9422339-6	1997	A chemically modified heparin with low affinity for antithrombin III was added ex vivo or in vivo to displace heparin bound nonspecifically to plasma proteins.	Heparin	110-117	serpin family C member 1	Homo sapiens	52-68
9360977-0	1997	The efficient catabolism of thrombin-protease nexin 1 complexes is a synergistic mechanism that requires both the LDL receptor-related protein and cell surface heparins.	Heparin	160-168	serpin family E member 2	Homo sapiens	37-53
9360977-5	1997	Since Th-PN1 complexes retain a high-affinity for heparin after complex formation, unlike several of the other SERPINs, we tested the possibility that cell surface heparins were involved in initial complex binding.	Heparin	50-57	serpin family E member 2	Homo sapiens	9-12
9360977-6	1997	Soluble heparin was found to be a potent inhibitor of the binding of Th-PN1 to the cell surface and greatly facilitated the dissociation of Th-PN1 complexes pre-bound in the absence of soluble heparin.	Heparin	8-15	serpin family E member 2	Homo sapiens	72-75
9360977-6	1997	Soluble heparin was found to be a potent inhibitor of the binding of Th-PN1 to the cell surface and greatly facilitated the dissociation of Th-PN1 complexes pre-bound in the absence of soluble heparin.	Heparin	8-15	serpin family E member 2	Homo sapiens	143-146
9360977-9	1997	These data demonstrate the sizable contribution of cell surface heparins to Thrombin-PN1 complex binding and support a model in which these heparins act to concentrate the complexes at the cell surface facilitating their subsequent LRP-dependent endocytosis.	Heparin	64-72	serpin family E member 2	Homo sapiens	85-88
9511991-0	1997	Capillary zone electrophoresis for the study of the binding of antithrombin to low-affinity heparin.	Heparin	92-99	serpin family C member 1	Homo sapiens	63-75
9511991-2	1997	To evaluate the applicability of the CZE technique to this problem, we explored the interaction between antithrombin and low-affinity heparin.	Heparin	134-141	serpin family C member 1	Homo sapiens	104-116
9511991-3	1997	In a series of CZE experiments we demonstrated that the mobility of antithrombin increases gradually as increased concentrations of low-affinity heparin were added to the electrolyte.	Heparin	145-152	serpin family C member 1	Homo sapiens	68-80
9365110-7	1997	It is proposed that the interaction of CBP-I with the conserved heparin-binding domains found on most chemokines represents a novel mechanism for altering multiple chemokine functions in vivo.	Heparin	64-71	annexin A5	Homo sapiens	39-44
9391721-1	1997	The aim of this work was to clarify the role of urokinase-type plasminogen activator (uPA) on the profibrinolytic activity of heparin, chemically modified heparins [partially: N-desulfated (N-des), N-desulfated N-acetylated (N-des N-ac), O-desulfated (O-des), O/N-desulfated N-acetylated (O/N-des N-ac)] and heparan sulfate.	Heparin	126-133	plasminogen activator, urokinase	Mus musculus	48-84
9391721-1	1997	The aim of this work was to clarify the role of urokinase-type plasminogen activator (uPA) on the profibrinolytic activity of heparin, chemically modified heparins [partially: N-desulfated (N-des), N-desulfated N-acetylated (N-des N-ac), O-desulfated (O-des), O/N-desulfated N-acetylated (O/N-des N-ac)] and heparan sulfate.	Heparin	126-133	plasminogen activator, urokinase	Mus musculus	86-89
9391721-1	1997	The aim of this work was to clarify the role of urokinase-type plasminogen activator (uPA) on the profibrinolytic activity of heparin, chemically modified heparins [partially: N-desulfated (N-des), N-desulfated N-acetylated (N-des N-ac), O-desulfated (O-des), O/N-desulfated N-acetylated (O/N-des N-ac)] and heparan sulfate.	Heparin	155-163	plasminogen activator, urokinase	Mus musculus	48-84
9391721-1	1997	The aim of this work was to clarify the role of urokinase-type plasminogen activator (uPA) on the profibrinolytic activity of heparin, chemically modified heparins [partially: N-desulfated (N-des), N-desulfated N-acetylated (N-des N-ac), O-desulfated (O-des), O/N-desulfated N-acetylated (O/N-des N-ac)] and heparan sulfate.	Heparin	155-163	plasminogen activator, urokinase	Mus musculus	86-89
9335347-0	1997	Inhibition of the plasma contact activation system of immobilized heparin: relation to surface density of functional antithrombin binding sites.	Heparin	66-73	serpin family C member 1	Homo sapiens	117-129
9335347-2	1997	The present investigation was undertaken to determine what density of immobilized heparin molecules expressing functionally intact antithrombin binding sites is required to achieve these blood compatible properties.	Heparin	82-89	serpin family C member 1	Homo sapiens	131-143
9335347-7	1997	Addition of heparin to the plasma phase reduced the capacity of the heparin surfaces to bind antithrombin, leading to a diminished ability of the surfaces to prevent contact activation.	Heparin	12-19	serpin family C member 1	Homo sapiens	93-105
9335347-7	1997	Addition of heparin to the plasma phase reduced the capacity of the heparin surfaces to bind antithrombin, leading to a diminished ability of the surfaces to prevent contact activation.	Heparin	68-75	serpin family C member 1	Homo sapiens	93-105
9335347-8	1997	This finding supports the hypothesis that antithrombin is the critical coagulation inhibitor for the suppression of contact activation on end-point immobilized heparin.	Heparin	160-167	serpin family C member 1	Homo sapiens	42-54
9348117-4	1997	Heparinised antithrombin was more resistant to polymerisation and peptide insertion, indicating that heparin induces a conformational change that closes the A-sheet and expels the reactive loop.	Heparin	101-108	serpin family C member 1	Homo sapiens	12-24
9351527-0	1997	Exogenous heparin reduces soluble plasma thrombomodulin levels.	Heparin	10-17	thrombomodulin	Homo sapiens	41-55
9332733-8	1997	Heparin, which inhibits the neurite growth-promoting effects of PGs in vitro, and heparitinase, which catalyzes the cleavage of heparan sulphate, also inhibited the glutamate-dependent induction of T alpha 1, MAP-2 and GAP-43 mRNA expression and neurite growth when added to culture medium following glutamate exposure.	Heparin	0-7	growth associated protein 43	Homo sapiens	219-225
9356883-7	1997	LPL activity was measured in plasma post-heparin administration.	Heparin	41-48	lipoprotein lipase	Homo sapiens	0-3
9323582-5	1997	A significant increase in monocyte adhesion was also observed when BAEC were incubated with LPL at 4 degrees C. Heparin or heparinase treatment of BAEC totally abolished the LPL stimulatory effect on monocyte adhesion.	Heparin	112-119	lipoprotein lipase	Homo sapiens	92-95
9323582-5	1997	A significant increase in monocyte adhesion was also observed when BAEC were incubated with LPL at 4 degrees C. Heparin or heparinase treatment of BAEC totally abolished the LPL stimulatory effect on monocyte adhesion.	Heparin	112-119	lipoprotein lipase	Homo sapiens	174-177
9288518-9	1997	The concentration of p-selectin was found to be significantly higher in the non-bonded circuits than in the heparin-bonded circuits at 30 (37 versus 29 ng/ml P &lt; 0.01), 60 (37 versus 28 ng/ml P &lt; 0.01).	Heparin	108-115	selectin P	Homo sapiens	21-31
9483172-4	1997	Heparin-cofactor-II-dependent antithrombin activity of DHG or UFH was neutralized by PF4 at a high concentration to the same extent; however, prolongation of the APTT by DHG was more resistant to neutralization by PF4 at a physiological plasma level than that by UFH.	Heparin	62-65	serpin family D member 1	Rattus norvegicus	0-19
9483172-4	1997	Heparin-cofactor-II-dependent antithrombin activity of DHG or UFH was neutralized by PF4 at a high concentration to the same extent; however, prolongation of the APTT by DHG was more resistant to neutralization by PF4 at a physiological plasma level than that by UFH.	Heparin	263-266	serpin family D member 1	Rattus norvegicus	0-19
9617183-5	1997	The clear influence of the studied lipid parameters on the bilirubin albumin binding, invites us to consider the systematic use of heparin for the mobilization of lipoprotein-lipase from the vascular endothelium and to promote a better management of lipids in term newborns, especially if there is an important hyperbilirubinemia.	Heparin	131-138	lipoprotein lipase	Homo sapiens	163-181
9198206-0	1997	Structural mobility of antithrombin and its modulation by heparin.	Heparin	58-65	serpin family C member 1	Homo sapiens	23-35
9177183-0	1997	Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells.	Heparin	0-7	peroxiredoxin 5	Homo sapiens	50-71
9177183-1	1997	Mammalian selenocysteine-containing thioredoxin reductase (TR) isolated from HeLa cells and from human lung adenocarcinoma cells was separated into two major enzyme species by heparin-agarose affinity chromatography.	Heparin	176-183	peroxiredoxin 5	Homo sapiens	36-57
9177183-1	1997	Mammalian selenocysteine-containing thioredoxin reductase (TR) isolated from HeLa cells and from human lung adenocarcinoma cells was separated into two major enzyme species by heparin-agarose affinity chromatography.	Heparin	176-183	peroxiredoxin 5	Homo sapiens	59-61
9177183-4	1997	The C-terminal amino acid sequences of 75Se-labeled tryptic peptides from lung adenocarcinoma low- and high heparin-affinity enzyme forms were identical to the predicted C-terminal sequence of human placental TR.	Heparin	108-115	peroxiredoxin 5	Homo sapiens	209-211
9184147-2	1997	Binding of thrombomodulin is affected drastically by the particular salt present in solution and is positively linked to Na+ binding to thrombin and the conversion of the enzyme from the slow to the fast form, but is opposed by Cl- binding to the fibrinogen recognition site and especially to the heparin binding site.	Heparin	297-304	thrombomodulin	Homo sapiens	11-25
9184147-3	1997	Binding of thrombomodulin has an unusually large salt dependence (gamma(salt) = -4.8) contributed mostly by the polyelectrolyte-like nature of the chondroitin sulfate moiety that binds to the heparin binding site and increases the affinity of the cofactor by almost 10-fold.	Heparin	192-199	thrombomodulin	Homo sapiens	11-25
9184147-7	1997	These results demonstrate that recognition of thrombomodulin by thrombin is steered electrostatically by the highly charged regions of the fibrinogen recognition site and the heparin binding site, to which the chondroitin sulfate moiety binds and enhances the affinity of the interaction.	Heparin	175-182	thrombomodulin	Homo sapiens	46-60
9184148-0	1997	The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change.	Heparin	108-115	serpin family C member 1	Homo sapiens	51-63
9184148-0	1997	The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change.	Heparin	159-166	serpin family C member 1	Homo sapiens	51-63
9184148-1	1997	The beta-form of antithrombin, lacking a carbohydrate side chain on Asn-135, is known to bind heparin more tightly than the fully glycosylated alpha-form.	Heparin	94-101	serpin family C member 1	Homo sapiens	17-29
9184148-2	1997	The molecular basis for this difference in affinity was elucidated by rapid-kinetic studies of the binding of heparin and the antithrombin-binding heparin pentasaccharide to plasma and recombinant forms of alpha- and beta-antithrombin.	Heparin	110-117	serpin family C member 1	Homo sapiens	222-234
9184148-3	1997	The dissociation equilibrium constant for the first step of the two-step mechanism of binding of both heparin and pentasaccharide to alpha-antithrombin was only slightly higher than that for the binding to the beta-form.	Heparin	102-109	serpin family C member 1	Homo sapiens	139-151
9184148-4	1997	The oligosaccharide at Asn-135 thus at most moderately interferes with the initial, weak binding of heparin to alpha-antithrombin.	Heparin	100-107	serpin family C member 1	Homo sapiens	117-129
9184148-5	1997	In contrast, the rate constant for the conformational change induced by heparin and pentasaccharide in the second binding step was substantially lower for alpha-antithrombin than for beta-antithrombin.	Heparin	72-79	serpin family C member 1	Homo sapiens	161-173
9184148-5	1997	In contrast, the rate constant for the conformational change induced by heparin and pentasaccharide in the second binding step was substantially lower for alpha-antithrombin than for beta-antithrombin.	Heparin	72-79	serpin family C member 1	Homo sapiens	188-200
9184148-7	1997	The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change.	Heparin	56-63	serpin family C member 1	Homo sapiens	82-94
9184148-7	1997	The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change.	Heparin	129-136	serpin family C member 1	Homo sapiens	82-94
9184148-8	1997	These and previous results suggest a model in which the Asn-135 oligosaccharide of alpha-antithrombin is oriented away from the heparin binding site and does not interfere with the first step of heparin binding.	Heparin	128-135	serpin family C member 1	Homo sapiens	89-101
9184148-11	1997	This effect results in a higher energy for inducing the activated conformation in alpha-antithrombin, leading to a decrease in heparin binding affinity.	Heparin	127-134	serpin family C member 1	Homo sapiens	88-100
9165012-0	1997	Heparin-binding, highly basic regions within the thyroglobulin type-1 repeat of insulin-like growth factor (IGF)-binding proteins (IGFBPs) -3, -5, and -6 inhibit IGFBP-4 degradation.	Heparin	0-7	insulin-like growth factor binding protein 3	Mus musculus	131-137
9165012-6	1997	The IGFBP-3, -5, and -6 peptides, each of which contains the heparin-binding consensus sequence XBBBXXBX, bind heparin, yet the IGFBP-3 and -5 peptides bind heparin with the highest affinities, whereas the IGFBP-6 peptide binds heparin with approximately 10-fold less affinity.	Heparin	61-68	insulin-like growth factor binding protein 3	Mus musculus	4-11
9165012-6	1997	The IGFBP-3, -5, and -6 peptides, each of which contains the heparin-binding consensus sequence XBBBXXBX, bind heparin, yet the IGFBP-3 and -5 peptides bind heparin with the highest affinities, whereas the IGFBP-6 peptide binds heparin with approximately 10-fold less affinity.	Heparin	111-118	insulin-like growth factor binding protein 3	Mus musculus	4-11
9165012-6	1997	The IGFBP-3, -5, and -6 peptides, each of which contains the heparin-binding consensus sequence XBBBXXBX, bind heparin, yet the IGFBP-3 and -5 peptides bind heparin with the highest affinities, whereas the IGFBP-6 peptide binds heparin with approximately 10-fold less affinity.	Heparin	111-118	insulin-like growth factor binding protein 3	Mus musculus	4-11
9165012-6	1997	The IGFBP-3, -5, and -6 peptides, each of which contains the heparin-binding consensus sequence XBBBXXBX, bind heparin, yet the IGFBP-3 and -5 peptides bind heparin with the highest affinities, whereas the IGFBP-6 peptide binds heparin with approximately 10-fold less affinity.	Heparin	111-118	insulin-like growth factor binding protein 3	Mus musculus	4-11
9165012-8	1997	Together, these data demonstrate that IGFBP-3, -5, and -6 can function as IGF-reversible inhibitors of IGFBP-4 proteolysis, likely through homologous, highly basic, heparin-binding domains contained within the conserved thyroglobulin type-1 motif present in the C-termini of these IGFBPs.	Heparin	165-172	insulin-like growth factor binding protein 3	Mus musculus	38-57
9165012-8	1997	Together, these data demonstrate that IGFBP-3, -5, and -6 can function as IGF-reversible inhibitors of IGFBP-4 proteolysis, likely through homologous, highly basic, heparin-binding domains contained within the conserved thyroglobulin type-1 motif present in the C-termini of these IGFBPs.	Heparin	165-172	insulin-like growth factor binding protein 3	Mus musculus	281-287
9169495-8	1997	These mechanisms include: first, heparin enhancement of antithrombin III-dependent inhibition of factor V activation by thrombin; second, the inactivation of membrane-bound FVa by APC; and third, the proteolytic inactivation of membrane-bound factor V by APC, which is enhanced by heparin.	Heparin	33-40	serpin family C member 1	Homo sapiens	56-72
9174558-11	1997	Heparin was associated with a significant excess of 9 (SD 1) transfused or fatal extracranial bleeds per 1000.	Heparin	0-7	CUP2Q35	Homo sapiens	55-59
15619827-4	1997	The results suggested that plasma heparin may be one of factors resulting in decreased BPC and defect platelet function in HFRS patients with 80% AT-III: alpha or above.	Heparin	34-41	serpin family C member 1	Homo sapiens	146-152
9184077-8	1997	Both proteins are found in the ECM, although Cyr61 associates with the ECM more strongly and binds heparin with higher affinity.	Heparin	99-106	cellular communication network factor 1	Homo sapiens	45-50
9153200-8	1997	The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded.	Heparin	62-69	serpin family C member 1	Homo sapiens	45-57
9153200-8	1997	The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded.	Heparin	62-69	serpin family C member 1	Homo sapiens	123-135
9164872-7	1997	In a concentration-dependent fashion, PAI-1, CaCl2, heparin and heparan sulphate, but not other glycosaminoglycans, interfered with the binding of vitronectin to osteonectin.	Heparin	52-59	serpin family E member 1	Homo sapiens	38-43
9115748-8	1997	The growth-promoting activity from U937 cells that bound to heparin-sepharose was inhibited by a neutralizing antibody to human HB-EGF.	Heparin	60-67	heparin binding EGF like growth factor	Homo sapiens	128-134
9135573-12	1997	Increasing concentrations of heparin had little or no effect on IGF-I binding, but strongly inhibited IGF-II binding.	Heparin	29-36	insulin like growth factor 2	Homo sapiens	102-108
9135573-14	1997	Possibly, the interaction of IGFBP-3 with heparin or heparin-like structures in vivo can lead to the selective release of IGF-II from this binding protein.	Heparin	42-49	insulin like growth factor binding protein 3	Homo sapiens	29-36
9135573-14	1997	Possibly, the interaction of IGFBP-3 with heparin or heparin-like structures in vivo can lead to the selective release of IGF-II from this binding protein.	Heparin	42-49	insulin like growth factor 2	Homo sapiens	122-128
9135573-14	1997	Possibly, the interaction of IGFBP-3 with heparin or heparin-like structures in vivo can lead to the selective release of IGF-II from this binding protein.	Heparin	53-60	insulin like growth factor binding protein 3	Homo sapiens	29-36
9135573-14	1997	Possibly, the interaction of IGFBP-3 with heparin or heparin-like structures in vivo can lead to the selective release of IGF-II from this binding protein.	Heparin	53-60	insulin like growth factor 2	Homo sapiens	122-128
9135573-15	1997	Our results with heparin also suggest that the binding sites on IGFBP-3 for IGF-I and IGF-II are not completely identical.	Heparin	17-24	insulin like growth factor binding protein 3	Homo sapiens	64-71
9084504-4	1997	Cyclophosphamide administration resulted in a profound decline in the heparin-releasable lipoprotein lipase activity, concordant with a higher recovery in the residual heart tissue.	Heparin	70-77	lipoprotein lipase	Oryctolagus cuniculus	89-107
9084504-6	1997	In agreement, the proportion of neosynthesized [35S]methionine-labelled lipoprotein lipase released by heparin was decreased by 50% following antimitotic treatment.	Heparin	103-110	lipoprotein lipase	Oryctolagus cuniculus	72-90
9050848-3	1997	Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity.	Heparin	35-42	serpin family C member 1	Homo sapiens	141-157
9050848-3	1997	Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity.	Heparin	35-42	serpin family C member 1	Homo sapiens	159-165
9050848-3	1997	Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity.	Heparin	192-199	serpin family C member 1	Homo sapiens	141-157
9050848-3	1997	Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity.	Heparin	192-199	serpin family C member 1	Homo sapiens	159-165
9050848-4	1997	The HIP peptide was shown to compete with AT-III for binding to heparin and to neutralize the anticoagulant activity of heparin in blood plasma assays.	Heparin	64-71	serpin family C member 1	Homo sapiens	42-48
9130607-2	1997	Our results confirmed the predictions: under very strict conditions of pH (6.3), CaCl2 concentration (2 mM), ionic strength (25 mM) and protein/heparin ratio (1/1), the first component of the complement recognizes the high antithrombin III affinity fraction of heparin, and allows a concentration of the biological activity of the original low molecular weight-heparin.	Heparin	261-268	serpin family C member 1	Homo sapiens	223-239
9130607-2	1997	Our results confirmed the predictions: under very strict conditions of pH (6.3), CaCl2 concentration (2 mM), ionic strength (25 mM) and protein/heparin ratio (1/1), the first component of the complement recognizes the high antithrombin III affinity fraction of heparin, and allows a concentration of the biological activity of the original low molecular weight-heparin.	Heparin	261-268	serpin family C member 1	Homo sapiens	223-239
9118690-11	1997	MEASUREMENTS AND RESULTS: CPB with a noncoated extracorporeal circuit induced a sharp increase in neutrophil-derived BPI, manifest directly after release of the aortic crossclamp, which was significantly attenuated using a heparin-coated system.	Heparin	223-230	bactericidal permeability increasing protein	Homo sapiens	117-120
9127746-7	1997	These findings suggest that heparin-induced lipoprotein lipase stimulation is the principal cause of the post-dialysis increase in pancreatic lipase, and that fluid removal during dialysis makes only a minor contribution to this increase.	Heparin	28-35	lipoprotein lipase	Homo sapiens	44-62
8999916-7	1997	Proteins containing a BPI N-terminal domain had greater heparin binding capacities in vitro and were cleared more rapidly from the plasma of whole animals.	Heparin	56-63	bactericidal permeability increasing protein	Homo sapiens	22-25
9040053-8	1997	Based on Northern blot analysis, we observed that both MMP-1 and MMP-2 were induced at the gene transcription level by heparin and that TIMP-1 was induced by cholesterol.	Heparin	119-126	matrix metallopeptidase 1	Homo sapiens	55-60
9200337-7	1997	Heparin (0.5 U/mL) inhibited both TF and PAI-2 production and gene expression.	Heparin	0-7	serpin family B member 2	Homo sapiens	41-46
8943254-1	1996	Two new oligosaccharides were prepared from heparin by its partial depolymerization using heparin lyase I (EC 4.2.2.7) in an attempt to prepare oligosaccharides having intact antithrombin III binding sites.	Heparin	44-51	serpin family C member 1	Homo sapiens	175-187
8943254-10	1996	Interestingly, while both decasaccharide and heparin bound to antithrombin with nanomolar affinity, very little heat of binding was observed.	Heparin	45-52	serpin family C member 1	Homo sapiens	62-74
8961947-1	1996	Human matrilysin devoid of its propeptide is expressed in Escherichia coli and purified to homogeneity by heparin chromatography after refolding of the guanidine hydrochloride solubilized protein.	Heparin	106-113	matrix metallopeptidase 7	Homo sapiens	6-16
8980646-7	1996	Apparent second-order rate constant (ki) for the inhibition of factor Xa by PAI-1 at 5 mM Ca2+ was 1.6 x 10(4) M-1 s-1, and was enhanced 3-fold by 2 u/ml of heparin (4.6 x 10(4) M-1 s-1) and 10-fold by 100 nM vitronectin (1.6 x 10(5) M-1 s-1), respectively.	Heparin	157-164	serpin family E member 1	Homo sapiens	76-81
9017514-1	1996	We previously reported a compound heterozygote [T(-39)C/T(-93)G] in the human lipoprotein lipase (LPL) gene promoter in one out of 19 patients with familial combined hyperlipidemia (FCHL) and reduced post-heparin plasma LPL levels.	Heparin	205-212	lipoprotein lipase	Homo sapiens	78-96
9017514-1	1996	We previously reported a compound heterozygote [T(-39)C/T(-93)G] in the human lipoprotein lipase (LPL) gene promoter in one out of 19 patients with familial combined hyperlipidemia (FCHL) and reduced post-heparin plasma LPL levels.	Heparin	205-212	lipoprotein lipase	Homo sapiens	98-101
8900394-0	1996	Structure-function relations of antithrombin III-heparin interactions as assessed by biophysical and biological assays and molecular modeling of peptide-pentasaccharide-docked complexes.	Heparin	49-56	serpin family C member 1	Homo sapiens	32-48
8900394-2	1996	ATIII attains its full biological activity only upon binding polysulfated glycosaminoglycans, such as heparin.	Heparin	102-109	serpin family C member 1	Homo sapiens	0-5
8900394-4	1996	3, 620-627, 1994) to encompass part (or all) of the purported high-affinity heparin binding region of ATIII.	Heparin	76-83	serpin family C member 1	Homo sapiens	102-107
8900394-10	1996	Furthermore, each of the Ala-replacement peptides was a less-effective inhibitor of ATIII-heparin complex formation than the reference peptide.	Heparin	90-97	serpin family C member 1	Homo sapiens	84-89
8900394-17	1996	The observations from molecular modeling allow us to suggest that ATIII Geneva displays decreased heparin binding affinity due to its inability to form a productive binding complex in which essential electrostatic contacts are made between suitably juxtaposed saccharide anionic functional groups and cationic amino acid side chains.	Heparin	98-105	serpin family C member 1	Homo sapiens	66-71
8958394-0	1996	Homozygous variant of antithrombin with lack of affinity for heparin: management of severe thrombotic complications associated with intrauterine fetal demise.	Heparin	61-68	serpin family C member 1	Homo sapiens	22-34
8958394-1	1996	Patients with homozygous heparin-binding-site (HBS) qualitative antithrombin deficiencies are at significant risk of venous and arterial thrombosis.	Heparin	25-32	serpin family C member 1	Homo sapiens	64-76
8941683-2	1996	This study was undertaken to determine whether heparin and/or protamine could enhance endothelium-derived relaxing factor (EDRF), as determined by nitric oxide (NO) production.	Heparin	47-54	alpha hemoglobin stabilizing protein	Homo sapiens	86-121
8941683-2	1996	This study was undertaken to determine whether heparin and/or protamine could enhance endothelium-derived relaxing factor (EDRF), as determined by nitric oxide (NO) production.	Heparin	47-54	alpha hemoglobin stabilizing protein	Homo sapiens	123-127
8902986-4	1996	The corresponding region of antithrombin III gene is affected by a cluster of frameshift mutations suggesting that heparin cofactor II and antithrombin III could share similar mutational patterns.	Heparin	115-122	serpin family C member 1	Homo sapiens	28-44
8902986-5	1996	The heparin cofactor II gene alteration was associated with, in one patient, the factor V Leiden mutation and, in the other, type I protein C deficiency.	Heparin	4-11	coagulation factor V	Homo sapiens	81-96
8843739-0	1996	IGFBP-3 proteolysis by plasmin, thrombin, serum: heparin binding, IGF binding, and structure of fragments.	Heparin	49-56	insulin like growth factor binding protein 3	Homo sapiens	0-7
8894654-9	1996	The findings suggest that the risk of bleeding complications might be reduced, without compromising efficacy, by administering heparin on a weight-adjusted basis in patients treated with c7E3 Fab.	Heparin	127-134	FA complementation group B	Homo sapiens	192-195
8702852-1	1996	Variant forms of human antithrombin III with glutamine or threonine substitutions at Lys114, Lys125, Lys133, Lys136, and Lys139 were expressed in insect cells to evaluate their roles in heparin binding and activation.	Heparin	186-193	serpin family C member 1	Homo sapiens	23-39
8702852-2	1996	Recombinant native ATIII and all of the variants had very similar second order rate constants for thrombin inhibition in the absence of heparin, ranging from 1.13 x 10(5) M-1min-1 to 1.66 x 10(5) M-1min-1.	Heparin	136-143	serpin family C member 1	Homo sapiens	19-24
8702852-3	1996	Direct binding studies using 125I-flouresceinamine-heparin yielded a Kd of 6 nM for the recombinant native ATIII and K136T, whereas K114Q and K139Q bound heparin so poorly that a Kd could not be determined.	Heparin	51-58	serpin family C member 1	Homo sapiens	107-112
8702852-8	1996	Based on these data, Lys114 and Lys139, which are outside of the putative pentasaccharide binding site, play pivotal roles in the high affinity binding of heparin to ATIII and the activation of thrombin inhibitory activity.	Heparin	155-162	serpin family C member 1	Homo sapiens	166-171
8819242-0	1996	Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin.	Heparin	120-127	serpin family C member 1	Homo sapiens	0-12
8819242-0	1996	Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin.	Heparin	120-127	serpin family C member 1	Homo sapiens	144-156
8819242-1	1996	We examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor VIIa bound to tissue factor.	Heparin	97-104	serpin family C member 1	Homo sapiens	128-140
8819242-4	1996	In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3).	Heparin	65-72	serpin family C member 1	Homo sapiens	122-127
8819242-4	1996	In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3).	Heparin	65-72	serpin family C member 1	Homo sapiens	157-162
8819242-4	1996	In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3).	Heparin	171-178	serpin family C member 1	Homo sapiens	122-127
8819242-4	1996	In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3).	Heparin	171-178	serpin family C member 1	Homo sapiens	157-162
8663298-1	1996	Matrix metalloproteinase 3 cleaves insulin-like growth factor-binding protein-3 (IGFBP-3) into six fragments, four of which bind heparin-Sepharose (Fowlkes, J. L., Enghild, J. J., Suzuki, K., and Nagase, H. (1994) J. Biol.	Heparin	129-136	insulin like growth factor binding protein 3	Homo sapiens	81-88
8663298-4	1996	Sequence analysis of IGFBP-3 heparin-binding fragments shows that all fragments contain at least one of two highly basic, putative heparin-binding consensus sequences present in IGFBP-3.	Heparin	29-36	insulin like growth factor binding protein 3	Homo sapiens	21-28
8663298-4	1996	Sequence analysis of IGFBP-3 heparin-binding fragments shows that all fragments contain at least one of two highly basic, putative heparin-binding consensus sequences present in IGFBP-3.	Heparin	131-138	insulin like growth factor binding protein 3	Homo sapiens	178-185
8663298-5	1996	Epitope-specific antibodies generated against synthetic peptides containing these domains recognized IGFBP-3, yet were significantly inhibited from binding in the presence of heparin, demonstrating that these regions of IGFBP-3 contain functional heparin-binding domains.	Heparin	175-182	insulin like growth factor binding protein 3	Homo sapiens	220-227
8663298-5	1996	Epitope-specific antibodies generated against synthetic peptides containing these domains recognized IGFBP-3, yet were significantly inhibited from binding in the presence of heparin, demonstrating that these regions of IGFBP-3 contain functional heparin-binding domains.	Heparin	247-254	insulin like growth factor binding protein 3	Homo sapiens	220-227
8663298-6	1996	IGFBP-3 peptides containing one of the two heparin-binding consensus sequences bound heparin in a solid phase binding assay in a dose-dependent and saturable manner.	Heparin	43-50	insulin like growth factor binding protein 3	Homo sapiens	0-7
8662798-6	1996	Analysis of baculovirus-expressed HGF/NK1 revealed that this isoform possesses the heparin binding properties of HGF/SF and modest mitogenic and scattering activity relative to HGF/SF.	Heparin	83-90	tachykinin receptor 1	Homo sapiens	38-41
8665956-7	1996	The bindings of Sg II to both iPr2P-PSA and PCI were influenced by pH, ionic strength, heparin, dextran sulfate, and divalent cations, particularly by Zn2+.	Heparin	87-94	semenogelin 2	Homo sapiens	16-21
8665956-7	1996	The bindings of Sg II to both iPr2P-PSA and PCI were influenced by pH, ionic strength, heparin, dextran sulfate, and divalent cations, particularly by Zn2+.	Heparin	87-94	kallikrein related peptidase 3	Homo sapiens	36-39
8928888-4	1996	In eight animals VEGF (2 microgram) with heparin (50 U) was administered extraluminally to the LCX myocardium with an osmotic pump for 4 wk and 11 other animals served as controls.	Heparin	41-48	vascular endothelial growth factor A	Sus scrofa	17-21
8718936-3	1996	In addition to their capacity to adsorb thrombin, such surfaces were shown to be able to catalyse its inhibition by antithrombin III (AT), i.e. they are endowed with heparin-like activity.	Heparin	166-173	serpin family C member 1	Homo sapiens	116-132
8718936-3	1996	In addition to their capacity to adsorb thrombin, such surfaces were shown to be able to catalyse its inhibition by antithrombin III (AT), i.e. they are endowed with heparin-like activity.	Heparin	166-173	serpin family C member 1	Homo sapiens	134-136
8613463-0	1996	Fibroblast growth factor and heparin protect endothelial cells from the effects of interleukin 1.	Heparin	29-36	interleukin 1 alpha	Homo sapiens	83-96
8613463-7	1996	This study indicates that aFGF/heparin in the culture medium of HUVEC abrogates the measured responses to IL-1.	Heparin	31-38	interleukin 1 alpha	Homo sapiens	106-110
8612679-5	1996	FGF6, added at 5 ng/ml and in the presence of heparin, increased the expression of a subset of muscle cell differentiation markers.	Heparin	46-53	fibroblast growth factor 6	Homo sapiens	0-4
8616093-0	1996	Pathogenicity of IgA and/or IgM antibodies to heparin-PF4 complexes in patients with heparin-induced thrombocytopenia.	Heparin	46-53	immunoglobulin heavy variable 4-38-2-like	Homo sapiens	17-20
8857192-9	1996	As the TAT complex dissociates from immobilized heparin, this "recovered" heparin is available for subsequent binding of more ATIII and thrombin.	Heparin	48-55	serpin family C member 1	Homo sapiens	126-131
8857192-9	1996	As the TAT complex dissociates from immobilized heparin, this "recovered" heparin is available for subsequent binding of more ATIII and thrombin.	Heparin	74-81	serpin family C member 1	Homo sapiens	126-131
9208634-3	1996	The LPL and HL in the post-heparin plasma could hydrolyse the triglyceride in intralipid into glycerine and free fatty acid (FFA).	Heparin	27-34	lipoprotein lipase	Homo sapiens	4-7
8815578-0	1996	Low molecular weight heparin is responsible for the anti-Xa activity of Desmin 370.	Heparin	21-28	desmin	Homo sapiens	72-78
8785033-7	1996	Following heparin administration, lipoprotein lipase activity improved (p &lt; 0.02), associated with a decrease apolipoprotein C3 (p &lt; 0.05).	Heparin	10-17	lipoprotein lipase	Homo sapiens	34-52
8785033-7	1996	Following heparin administration, lipoprotein lipase activity improved (p &lt; 0.02), associated with a decrease apolipoprotein C3 (p &lt; 0.05).	Heparin	10-17	apolipoprotein C3	Homo sapiens	113-130
8707164-2	1996	The anticoagulant activity of unfractionated heparin is mainly accounted for by its fractions with a sequence with binding affinity for antithrombin III.	Heparin	45-52	serpin family C member 1	Homo sapiens	136-152
8713577-10	1996	Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species.	Heparin	74-81	serpin family C member 1	Homo sapiens	36-52
8713577-10	1996	Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species.	Heparin	74-81	serpin family C member 1	Homo sapiens	168-184
8713577-10	1996	Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species.	Heparin	107-114	serpin family C member 1	Homo sapiens	36-52
8713577-10	1996	Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species.	Heparin	107-114	serpin family C member 1	Homo sapiens	168-184
8788110-8	1996	The extent of ATIII binding to heparin in each experiment was assayed using a chromogenic substrate for ATIII, S-2238.	Heparin	31-38	serpin family C member 1	Homo sapiens	14-19
8788110-8	1996	The extent of ATIII binding to heparin in each experiment was assayed using a chromogenic substrate for ATIII, S-2238.	Heparin	31-38	serpin family C member 1	Homo sapiens	104-109
8788110-9	1996	The results of this study demonstrate that the displacement of ATIII from immobilized heparin was proportional to the fibronectin concentration, and was reversible.	Heparin	86-93	serpin family C member 1	Homo sapiens	63-68
9225215-0	1996	Lipase activities in post-heparin plasma and tissues, and susceptibilities of lipoproteins in experimental diabetic rats.	Heparin	26-33	lipase G, endothelial type	Rattus norvegicus	0-6
9005073-3	1996	The judicious employment in a complex of therapeutic measures of aerosols of hydrocarbonate of sodium and heparin promotes neutralization of cationic proteins and large major protein of eosinophiles in the bronchial lumen whereby there occurs normalization of Ig A levels in the sputum along with lowering of its fibrinolytic activity.	Heparin	106-113	immunoglobulin heavy variable 4-38-2-like	Homo sapiens	260-264
8683171-6	1996	The decline of AT-III may be due to bonding of coated heparin to AT-III, leading to effective anticoagulation.	Heparin	54-61	serpin family C member 1	Homo sapiens	15-21
8683171-6	1996	The decline of AT-III may be due to bonding of coated heparin to AT-III, leading to effective anticoagulation.	Heparin	54-61	serpin family C member 1	Homo sapiens	65-71
9112630-6	1996	The heparin binding site of TFPI (HBS-1) locates in its C-terminal basic portion.	Heparin	4-11	HBS1 like translational GTPase	Homo sapiens	34-39
8726866-7	1996	IN CONCLUSION: (1) heparin caused acute elevations in plasma FS concentrations probably by binding to FS, thereby reducing its plasma clearance; (2) rapid blood sampling per se did not elevate plasma FS concentrations; (3) alpha-2 macroglobulin concentrations were not elevated at the same time as plasma FS concentrations 10-12 h after surgery; and (4) the small increase in alpha-2 macroglobulin concentrations before surgery was attributable to a stress-induced response as seen in other species.	Heparin	19-26	alpha-2-macroglobulin	Ovis aries	223-244
7494001-1	1995	Diphtheria toxin receptor (DTR), which is identical to the membrane-anchored form of heparin-binding EGF-like growth factor (proHB-EGF), has a high affinity for heparin.	Heparin	85-92	heparin binding EGF like growth factor	Homo sapiens	27-30
7494001-2	1995	We studied the effect of heparin-like molecules on the binding of diphtheria toxin (DT) to DTR/proHB-EGF.	Heparin	25-32	heparin binding EGF like growth factor	Homo sapiens	91-94
7494001-5	1995	Studies of binding of 125I-labeled DT to HS-deficient CHO cells transfected with human DTR/proHB-EGF cDNA indicated that the increased sensitivity to DT after addition of heparin is due to increased binding of DT to cells.	Heparin	171-178	heparin binding EGF like growth factor	Homo sapiens	87-90
7494001-7	1995	Enhancement of DT binding by the addition of heparin was also observed with CHO-K1 cells and L cells that had been transfected with human DTR/proHB-EGF cDNA, but the degree of enhancement was less than that observed with the HS-deficient CHO cells.	Heparin	45-52	heparin binding EGF like growth factor	Homo sapiens	138-141
7494001-10	1995	Scatchard plot analysis for the binding of DT to a recombinant HB-EGF in vitro and to L cells expressing human DTR/proHB-EGF revealed that heparin increases the affinity of DTR/proHB-EGF for DT but does not change the number of binding sites.	Heparin	139-146	heparin binding EGF like growth factor	Homo sapiens	63-69
7494001-10	1995	Scatchard plot analysis for the binding of DT to a recombinant HB-EGF in vitro and to L cells expressing human DTR/proHB-EGF revealed that heparin increases the affinity of DTR/proHB-EGF for DT but does not change the number of binding sites.	Heparin	139-146	heparin binding EGF like growth factor	Homo sapiens	111-114
7494001-10	1995	Scatchard plot analysis for the binding of DT to a recombinant HB-EGF in vitro and to L cells expressing human DTR/proHB-EGF revealed that heparin increases the affinity of DTR/proHB-EGF for DT but does not change the number of binding sites.	Heparin	139-146	heparin binding EGF like growth factor	Homo sapiens	173-176
7494002-3	1995	Heparan sulfate (HS)-conjugated gel also bound HGF, and the binding was competitively inhibited by heparin and bovine liver HS, but not by Engelbreth-Holm-Swarm sarcoma HS, pig aorta HS, or other glycosaminoglycans, suggesting the specific structural domain in HS for the binding of HGF.	Heparin	99-106	hepatocyte growth factor	Bos taurus	47-50
8746633-3	1995	Approximately 40 micrograms of partially purified rHCII was routinely recovered from 50 ml of media after sequential heparin and Q-Sepharose affinity adsorption.	Heparin	117-124	serpin family D member 1	Rattus norvegicus	50-55
7492555-1	1995	All mammalian pancreatic cholesterol esterases (CEase) bind to membrane-associated heparin at a single site on the intestinal brush border membrane with a dissociation constant of 100 nM.	Heparin	83-90	carboxyl ester lipase	Homo sapiens	48-53
7492555-3	1995	On the other hand, soluble heparin potently inhibits the human CEase-catalyzed hydrolysis of cholesterol oleate with an IC50 of 2 x 10(-4) mg/mL, a value that is about 10(4) times more potent than that found with the bovine enzyme.	Heparin	27-34	carboxyl ester lipase	Homo sapiens	63-68
7499272-1	1995	Isolation of a biologically active 160-kilodalton heparin-binding pro-EGF with a truncated carboxyl terminus.	Heparin	50-57	epidermal growth factor	Homo sapiens	70-73
7499272-2	1995	In this report, we describe the isolation from human urine of a predominant 160-kDa epidermal growth factor (EGF)-immunoreactive glycoprotein that exhibits affinity for heparin.	Heparin	169-176	epidermal growth factor	Homo sapiens	84-107
7499272-2	1995	In this report, we describe the isolation from human urine of a predominant 160-kDa epidermal growth factor (EGF)-immunoreactive glycoprotein that exhibits affinity for heparin.	Heparin	169-176	epidermal growth factor	Homo sapiens	109-112
7499272-9	1995	When immobilized onto culture dishes, the heparin-binding pro-EGF appeared to function both as an adhesion molecule and as a growth factor for serum-free mouse embryo cells.	Heparin	42-49	epidermal growth factor	Homo sapiens	62-65
7586247-0	1995	Prolonged antithrombin activity of low-molecular-weight heparins.	Heparin	56-64	serpin family C member 1	Homo sapiens	10-22
8595612-9	1995	The medians of down-regulation of L-selectin were 79 (32-192) for heparin vs. 18.4 (0-188) for EDTA and 36.2 (7.4-135) for citrate mixture, P &lt; 0.05.	Heparin	66-73	selectin L	Homo sapiens	34-44
8595612-12	1995	Heparin-protamine complex was less stimulant to expression of CD11b and L-selectin than heparin or protamine (P &lt; 0.05).	Heparin	0-7	selectin L	Homo sapiens	72-82
8529028-1	1995	The catalytic subunit of protein phosphatase 2A (PP2Ac) was purified from Neurospora crassa extract by (NH4)2SO4-ethanol precipitation followed by DEAE-Sephacel, heparin-Sepharose, and MonoQ chromatography steps about 900-fold to a specific activity of 1200 U/g with a 2% yield.	Heparin	162-169	protein phosphatase 2 catalytic subunit alpha	Homo sapiens	49-54
7593431-7	1995	Adipose LPL was measured in the heparin-released fraction as well as the cellular fraction extracted with nonionic detergent (EXT).	Heparin	32-39	lipoprotein lipase	Homo sapiens	8-11
8656074-13	1995	Moreover, sites involved in heparin and lipid binding between residues 390-421 are important for LpL-mediated lipoprotein uptake.	Heparin	28-35	lipoprotein lipase	Homo sapiens	97-100
8607111-12	1995	The antithrombotic effects of both heparins were correlated with their plasma activities as measured by the antifactor Xa or the antithrombin assays.	Heparin	35-43	serpin family C member 1	Homo sapiens	129-141
7583546-9	1995	The heparin-binding affinity of the mutant LPL was not impaired.	Heparin	4-11	lipoprotein lipase	Homo sapiens	43-46
7475162-12	1995	RESULTS: Additional heparin was given to 48% patients in the aprotinin group and to 44% of control patients.	Heparin	20-27	pancreatic trypsin inhibitor	Bos taurus	61-70
7475162-20	1995	CONCLUSION: We conclude that, at the dosages given, recombinant bovine aprotinin decreases surgical blood loss and transfusion requirements in patients undergoing coronary artery bypass grafting, but its use requires appropriate monitoring of heparin use during bypass.	Heparin	243-250	pancreatic trypsin inhibitor	Bos taurus	71-80
7677475-3	1995	METHODS: This initial study evaluated the impact of heparin-bonded CPB circuits on production of the cytokines interleukin-1 (IL-1), tumor necrosis factor-alpha (TNF-a), IL-6, and IL-8 in adults undergoing complex cardiac operations with prolonged CPB.	Heparin	52-59	interleukin 1 alpha	Homo sapiens	126-130
7559767-6	1995	Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.	Heparin	45-53	selectin E	Homo sapiens	109-119
7559767-6	1995	Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.	Heparin	45-52	selectin E	Homo sapiens	109-119
7642636-8	1995	Site-directed mutagenesis confirmed the prediction that the conversion of His residues 8,68, and 70 in the positively charged region into Glu prevents the binding of pro-mMCP-7 to heparin.	Heparin	180-187	tryptase alpha/beta 1	Mus musculus	170-176
7642636-11	1995	The heparin/mMCP-7 interaction, which depends on the tertiary structure of the tryptase, may be representative of a general control mechanism by which hematopoietic cells maximize storage of properly folded, enzymatically active proteins in their granules.	Heparin	4-11	tryptase alpha/beta 1	Mus musculus	12-18
7642636-11	1995	The heparin/mMCP-7 interaction, which depends on the tertiary structure of the tryptase, may be representative of a general control mechanism by which hematopoietic cells maximize storage of properly folded, enzymatically active proteins in their granules.	Heparin	4-11	tryptase alpha/beta 1	Mus musculus	79-87
7646463-0	1995	Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells.	Heparin	53-60	serpin family C member 1	Homo sapiens	91-107
7646463-1	1995	In order to promote homogeneity of recombinant antithrombin III interactions with heparin, an asparagine-135 to alanine substitution mutant was expressed in baculovirus-infected insect cells.	Heparin	82-89	serpin family C member 1	Homo sapiens	47-63
7646463-4	1995	Second-order rate constants for thrombin and factor Xa inhibition determined in the absence and presence of heparin are in good agreement with values established for plasma antithrombin and these enzymes.	Heparin	108-115	serpin family C member 1	Homo sapiens	173-185
7646463-7	1995	The Kds of bv.hat3.N135A for high-affinity heparin and pentasaccharide were determined and are in good agreement with those of the plasma beta-antithrombin isoform.	Heparin	43-50	serpin family C member 1	Homo sapiens	143-155
7627700-4	1995	Hence, heparin releases mainly active LPL.	Heparin	7-14	lipoprotein lipase	Homo sapiens	38-41
7627700-5	1995	The four LPL parameters (mass and activity in plasma and their increase after heparin administration) were not related to each other, except for postheparin plasma LPL mass and activity, and they showed different correlations with plasma lipoprotein lipid concentrations.	Heparin	78-85	lipoprotein lipase	Homo sapiens	9-12
7500917-3	1995	We have previously shown that a region of this protein shows structural similarities to the high-affinity heparin-binding site of the serum protease-inhibitor antithrombin III (ATII).	Heparin	106-113	serpin family C member 1	Homo sapiens	159-175
7500917-9	1995	Since amino acids 130-137 of the high affinity heparin-binding site of ATIII show structural similarities to amino acids 134-141 of PrV-gC, both sequences were synthesized as synthetic peptides.	Heparin	47-54	serpin family C member 1	Homo sapiens	71-76
7500917-10	1995	Although interaction of the peptide derived from ATIII with heparin was significantly stronger, both peptides interacted specifically with heparin in assays in vitro.	Heparin	60-67	serpin family C member 1	Homo sapiens	49-54
7576611-3	1995	A 40 kD COOH-terminal chymotryptic fragment of fibronectin containing both a heparin-binding region and an alternate (non-RGD) cell-binding site was inactive in supporting trophoblast adhesion.	Heparin	77-84	fibronectin 1	Mus musculus	47-58
7608185-4	1995	The avian Cdc37 binds hyaluronan, chondroitin sulfate and heparin in vitro, and both isoforms contain glycosaminoglycan-binding motifs previously described in several hyaluronan-binding proteins.	Heparin	58-65	cell division cycle 37	Gallus gallus	10-15
7614042-2	1995	AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation.	Heparin	21-28	serpin family C member 1	Homo sapiens	0-6
7614042-2	1995	AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation.	Heparin	76-83	serpin family C member 1	Homo sapiens	0-6
7614042-2	1995	AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation.	Heparin	76-83	serpin family C member 1	Homo sapiens	0-6
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	9-16	serpin family C member 1	Homo sapiens	144-160
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	serpin family C member 1	Homo sapiens	52-58
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	serpin family C member 1	Homo sapiens	144-160
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	serpin family C member 1	Homo sapiens	52-58
7614042-3	1995	Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin.	Heparin	73-80	serpin family C member 1	Homo sapiens	144-160
7630130-7	1995	The ability of the splenocytes to release IL-2 and IL-3 in response to mitogen was markedly improved in hemorrhaged animals which were treated with GM1892 or conventional heparin compared to saline-treated mice.	Heparin	171-178	interleukin 2	Mus musculus	42-46
7647222-7	1995	This proposed heparin recognition region in TFPI is similar to the recognition region in antithrombin III and other proteins.	Heparin	14-21	serpin family C member 1	Homo sapiens	89-105
7647222-9	1995	A comparison of a helical wheel diagram of antithrombin III and tissue factor pathway inhibitor support also the proposal of this form of a heparin recognition region in TFPI.	Heparin	140-147	serpin family C member 1	Homo sapiens	43-59
7647223-1	1995	It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs).	Heparin	163-170	serpin family C member 1	Homo sapiens	27-43
7647223-1	1995	It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs).	Heparin	163-170	serpin family C member 1	Homo sapiens	45-50
7647223-1	1995	It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs).	Heparin	172-175	serpin family C member 1	Homo sapiens	27-43
7647223-1	1995	It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs).	Heparin	172-175	serpin family C member 1	Homo sapiens	45-50
7647223-1	1995	It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs).	Heparin	202-210	serpin family C member 1	Homo sapiens	27-43
7554525-7	1995	Together with the enhanced hepatic clearance of lipoprotein lipase induced by low molecular weight heparins, this may decrease lipoprotein lipase activity with a subsequent increase in plasma triglycerides, total and LDL cholesterol.	Heparin	99-107	lipoprotein lipase	Homo sapiens	48-66
7554525-7	1995	Together with the enhanced hepatic clearance of lipoprotein lipase induced by low molecular weight heparins, this may decrease lipoprotein lipase activity with a subsequent increase in plasma triglycerides, total and LDL cholesterol.	Heparin	99-107	lipoprotein lipase	Homo sapiens	127-145
7571947-4	1995	On the other hand, heparin could lessen the function of EGF and progesterone, which implies that calcium participated the effect of EGF and progesterone.	Heparin	19-26	epidermal growth factor	Mus musculus	56-59
7571947-4	1995	On the other hand, heparin could lessen the function of EGF and progesterone, which implies that calcium participated the effect of EGF and progesterone.	Heparin	19-26	epidermal growth factor	Mus musculus	132-135
7660353-2	1995	While beta 2GPI could be the true antigen, beta 2GPI binding to solid phase heparin did not determine its recognition by CL-rA when using patient plasmas.	Heparin	76-83	apolipoprotein H	Homo sapiens	43-52
7660353-5	1995	Thus, after recognizing beta 2 GPI, CL-rA bind heparin.	Heparin	47-54	apolipoprotein H	Homo sapiens	24-34
7727433-2	1995	The inhibitory activity is enhanced by heparin, and the C-terminal basic part has been shown to be a heparin-binding site (HBS-1).	Heparin	101-108	HBS1 like translational GTPase	Homo sapiens	123-128
7622551-8	1995	After depletion of antithrombin, but not complement C1 esterase inhibitor, the recalcified plasma clotted in contact with the unfractionated heparin surface as well.	Heparin	141-148	serpin family C member 1	Homo sapiens	19-31
7622551-9	1995	We conclude that antithrombin and the antithrombin-binding sequence in the surface-immobilized heparin are essential for the prevention of surface activation of FXII and triggering of the intrinsic coagulation system.	Heparin	95-102	serpin family C member 1	Homo sapiens	17-29
7622551-9	1995	We conclude that antithrombin and the antithrombin-binding sequence in the surface-immobilized heparin are essential for the prevention of surface activation of FXII and triggering of the intrinsic coagulation system.	Heparin	95-102	serpin family C member 1	Homo sapiens	38-50
7706382-0	1995	Carboxyl-terminal truncation of leucine76 converts heparin-binding EGF-like growth factor from a heparin-enhancible to a heparin-suppressible growth factor.	Heparin	97-104	heparin-binding EGF-like growth factor	Mus musculus	51-89
7706382-1	1995	Previous studies have indicated that heparin differentially regulates heparin-binding EGF-like growth factor (HB-EGF) and amphiregulin (AR) mitogenic activity.	Heparin	37-44	heparin-binding EGF-like growth factor	Mus musculus	70-108
7706382-1	1995	Previous studies have indicated that heparin differentially regulates heparin-binding EGF-like growth factor (HB-EGF) and amphiregulin (AR) mitogenic activity.	Heparin	37-44	heparin-binding EGF-like growth factor	Mus musculus	110-116
7706382-7	1995	Analysis of recombinant forms of HB-EGF demonstrated that HB-EGF can be converted to a heparin-inhibited growth factor if the putative mature form of the protein is truncated by two residues (leucine76 and proline77) at the carboxyl terminus.	Heparin	87-94	heparin-binding EGF-like growth factor	Mus musculus	33-39
7706382-7	1995	Analysis of recombinant forms of HB-EGF demonstrated that HB-EGF can be converted to a heparin-inhibited growth factor if the putative mature form of the protein is truncated by two residues (leucine76 and proline77) at the carboxyl terminus.	Heparin	87-94	heparin-binding EGF-like growth factor	Mus musculus	58-64
7706382-8	1995	Further analysis demonstrated that only leucine76 appears to be required for heparin-dependent enhancement of HB-EGF-mediated mitogenic activity, indicating that this amino acid may play a pivotal role in controlling the response of HB-EGF to heparin or related glycosaminoglycan sulfates.	Heparin	77-84	heparin-binding EGF-like growth factor	Mus musculus	110-116
7706382-8	1995	Further analysis demonstrated that only leucine76 appears to be required for heparin-dependent enhancement of HB-EGF-mediated mitogenic activity, indicating that this amino acid may play a pivotal role in controlling the response of HB-EGF to heparin or related glycosaminoglycan sulfates.	Heparin	77-84	heparin-binding EGF-like growth factor	Mus musculus	233-239
7706382-8	1995	Further analysis demonstrated that only leucine76 appears to be required for heparin-dependent enhancement of HB-EGF-mediated mitogenic activity, indicating that this amino acid may play a pivotal role in controlling the response of HB-EGF to heparin or related glycosaminoglycan sulfates.	Heparin	243-250	heparin-binding EGF-like growth factor	Mus musculus	110-116
7706382-8	1995	Further analysis demonstrated that only leucine76 appears to be required for heparin-dependent enhancement of HB-EGF-mediated mitogenic activity, indicating that this amino acid may play a pivotal role in controlling the response of HB-EGF to heparin or related glycosaminoglycan sulfates.	Heparin	243-250	heparin-binding EGF-like growth factor	Mus musculus	233-239
7706383-0	1995	Differential effects of a heparin antagonist (hexadimethrine) or chlorate on amphiregulin, basic fibroblast growth factor, and heparin-binding EGF-like growth factor activity.	Heparin	26-33	heparin-binding EGF-like growth factor	Mus musculus	127-165
7721830-8	1995	The novel aspect of this molecule is the presence of a terminal alpha-Gal-NAc residue at a position that is normally occupied by beta-GalNAc in chondroitin/dermatan sulfate or by alpha-Glc-NAc in heparin or heparan sulfate chains.	Heparin	196-203	synuclein alpha	Homo sapiens	74-77
7721830-8	1995	The novel aspect of this molecule is the presence of a terminal alpha-Gal-NAc residue at a position that is normally occupied by beta-GalNAc in chondroitin/dermatan sulfate or by alpha-Glc-NAc in heparin or heparan sulfate chains.	Heparin	196-203	synuclein alpha	Homo sapiens	137-140
7727531-3	1995	It could be retained on albumin-coated tissue culture wells without loosing its capacity to stimulate thymidine incorporation into erythroid cells of fetal bovine liver and on fibronectin-heparin coated wells keeping its mitogenic activity towards L6 muscle cells.	Heparin	188-195	fibronectin 1	Bos taurus	176-187
7717977-0	1995	Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low-density-lipoprotein-receptor-related protein by heparin fragments.	Heparin	13-20	lipoprotein lipase	Homo sapiens	54-72
7717977-0	1995	Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low-density-lipoprotein-receptor-related protein by heparin fragments.	Heparin	13-20	lipoprotein lipase	Homo sapiens	91-109
7717977-0	1995	Structure of heparin fragments with high affinity for lipoprotein lipase and inhibition of lipoprotein lipase binding to alpha 2-macroglobulin-receptor/low-density-lipoprotein-receptor-related protein by heparin fragments.	Heparin	204-211	lipoprotein lipase	Homo sapiens	91-109
7717977-1	1995	Heparin-derived deca- and octa-saccharides were subjected to affinity chromatography on lipoprotein lipase-Sepharose and the fractions eluted at high salt concentration were analysed by strong-anion-exchange chromatography.	Heparin	0-7	lipoprotein lipase	Homo sapiens	88-106
7717977-4	1995	The affinities of 3H-labelled low-molecular-mass heparin and size-fractionated deca-, octa-, and hexa-saccharides for lipoprotein lipase immobilized on microtitre plates were determined from saturation curves.	Heparin	49-56	lipoprotein lipase	Homo sapiens	118-136
7717977-8	1995	Heparin inhibits binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein.	Heparin	0-7	lipoprotein lipase	Homo sapiens	28-46
7717977-10	1995	The ability of the heparin fragments to inhibit binding correlated with their affinity for lipoprotein lipase.	Heparin	19-26	lipoprotein lipase	Homo sapiens	91-109
7717977-11	1995	This indicates that the inhibition of the binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein by heparin is exclusively mediated by binding of heparin to lipoprotein lipase.	Heparin	158-165	lipoprotein lipase	Homo sapiens	53-71
7717977-11	1995	This indicates that the inhibition of the binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein by heparin is exclusively mediated by binding of heparin to lipoprotein lipase.	Heparin	158-165	lipoprotein lipase	Homo sapiens	215-233
7717977-11	1995	This indicates that the inhibition of the binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein by heparin is exclusively mediated by binding of heparin to lipoprotein lipase.	Heparin	204-211	lipoprotein lipase	Homo sapiens	53-71
7717977-11	1995	This indicates that the inhibition of the binding of lipoprotein lipase to alpha 2-macroglobulin-receptor/low-density-lipoprotein receptor-related protein by heparin is exclusively mediated by binding of heparin to lipoprotein lipase.	Heparin	204-211	lipoprotein lipase	Homo sapiens	215-233
7495073-0	1995	Inhibition of prothrombinase by antithrombin-heparin at a macroscopic surface.	Heparin	45-52	serpin family C member 1	Homo sapiens	32-44
7495073-6	1995	Inhibition was much faster when antithrombin was complexed with heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	32-44
7495073-9	1995	The heparin-independent inhibition of prothrombinase by antithrombin (4 microM) in the presence of prothrombin (0.2 microM) was virtually negligible.	Heparin	4-11	serpin family C member 1	Homo sapiens	56-68
7736468-0	1995	Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements.	Heparin	90-97	serpin family C member 1	Homo sapiens	102-118
7534133-6	1995	However, in the presence of heparin (1 or 50 U/mL), C1Inh appeared to be the major inhibitor of FXIa, followed by ATIII.	Heparin	28-35	serpin family C member 1	Homo sapiens	114-119
7538797-2	1995	One of these factors, which appeared to be a relatively minor HBGF, was eluted from heparin affinity columns by 1.0 M NaCl and was found to compete with 125I-epidermal growth factor (EGF) for binding to an endometrial carcinoma cell line.	Heparin	84-91	epidermal growth factor	Sus scrofa	183-186
7540495-3	1995	This inhibition can be reversed by antithrombin III (ATIII), an inhibitor of thrombin, in combination with heparin, a cofactor of ATIII and a glycosaminoglycan.	Heparin	107-114	serpin family C member 1	Homo sapiens	130-135
7860647-9	1995	M1Q-bFGF also induced an increase in cell-associated uPA activity only when added to the cell cultures in the presence of soluble heparin.	Heparin	130-137	plasminogen activator, urokinase	Bos taurus	53-56
7545318-2	1995	Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical uses of heparin.	Heparin	96-103	serpin family C member 1	Homo sapiens	0-16
7545318-2	1995	Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical uses of heparin.	Heparin	142-149	serpin family C member 1	Homo sapiens	0-16
7873519-2	1995	Heparin is best known as an anticoagulant, an activity that results largely from a specific pentasaccharide sequence in heparin that interacts with a unique site in antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	165-181
7873519-2	1995	Heparin is best known as an anticoagulant, an activity that results largely from a specific pentasaccharide sequence in heparin that interacts with a unique site in antithrombin III.	Heparin	120-127	serpin family C member 1	Homo sapiens	165-181
7873519-7	1995	Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides.	Heparin	34-41	serpin family C member 1	Homo sapiens	54-70
7873519-7	1995	Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides.	Heparin	34-41	serpin family C member 1	Homo sapiens	196-212
7832187-10	1995	Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin.	Heparin	141-148	serpin family C member 1	Homo sapiens	38-44
7832187-10	1995	Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin.	Heparin	141-148	serpin family C member 1	Homo sapiens	249-265
7832187-10	1995	Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin.	Heparin	270-277	serpin family C member 1	Homo sapiens	38-44
7832187-10	1995	Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin.	Heparin	270-277	serpin family C member 1	Homo sapiens	249-265
7735426-6	1995	Chemotherapy was discontinued and the patient was given intravenous amphotericin B (1.0 mg/kg/day) and heparin associated with G.CSF.	Heparin	103-110	colony stimulating factor 3	Homo sapiens	127-132
7833248-6	1995	Cell adhesion studies to dishes coated with the fibronectin 40 kD fragment, containing the heparin-binding domain, demonstrated that adhesiveness of IL-3-treated cells was higher than that of untreated cells.	Heparin	91-98	fibronectin 1	Mus musculus	48-59
7833248-7	1995	These results suggest that in multipotent haemopoietic cells IL-3 regulates the amount of membrane-associated proteoglycans, which in turn modify the adhesive interactions of cells with the heparin-binding domain of fibronectin.	Heparin	190-197	fibronectin 1	Mus musculus	216-227
7863710-5	1995	The AT III activity dropped significantly (p &lt; 0.0001) after a heparin loading dose of 15,000 IU during stenting.	Heparin	66-73	serpin family C member 1	Homo sapiens	4-10
7863710-6	1995	As the heparin dose was reduced on the following days, AT III levels increased significantly (p &lt; 0.0001) during the observation time.	Heparin	7-14	serpin family C member 1	Homo sapiens	55-61
7863710-7	1995	There was a highly significant (p &lt; 0.001) negative correlation between AT III and heparin levels.	Heparin	86-93	serpin family C member 1	Homo sapiens	75-81
7991602-0	1994	Heparin-dependent binding and autophosphorylation of epidermal growth factor (EGF) receptor by heparin-binding EGF-like growth factor but not by EGF.	Heparin	0-7	epidermal growth factor receptor	Cricetulus griseus	53-91
7634317-4	1994	Heparin is the principal antithrombin drug currently used in acute syndromes; it acts mainly by binding to antithrombin III and increasing its inhibitory effect on thrombin and other coagulation factors.	Heparin	0-7	serpin family C member 1	Homo sapiens	25-37
7634317-4	1994	Heparin is the principal antithrombin drug currently used in acute syndromes; it acts mainly by binding to antithrombin III and increasing its inhibitory effect on thrombin and other coagulation factors.	Heparin	0-7	serpin family C member 1	Homo sapiens	107-123
7634317-5	1994	The heparin-antithrombin III complex, however, does not inhibit thrombus-bound thrombin; moreover, iv heparin requires frequent laboratory monitoring and dose adjustments.	Heparin	4-11	serpin family C member 1	Homo sapiens	12-24
7634317-7	1994	heparin has been found to be effective in unstable angina and in myocardial infarction, especially when treated with accelerated rt-PA. New antithrombin drugs that selectively and directly inhibit thrombin are hirudin, its synthetic derivate hirulog, and argatroban.	Heparin	0-7	serpin family C member 1	Homo sapiens	140-152
7705307-5	1994	We found that rabbit ECSOD incubated with either trypsin or activated neutrophils loses affinity for heparin.	Heparin	101-108	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	21-26
7853703-5	1994	LPL is released into the circulation after intravenous injection of heparin, and LPL is recovered in postheparin plasma (PHP).	Heparin	68-75	lipoprotein lipase	Homo sapiens	0-3
7947925-8	1994	We propose that heparin might be a regulator to modulate the anticoagulant activity of SAP and a useful drug to prevent SAP deposition on amyloid deposits.	Heparin	16-23	amyloid P component, serum	Homo sapiens	87-90
7947925-8	1994	We propose that heparin might be a regulator to modulate the anticoagulant activity of SAP and a useful drug to prevent SAP deposition on amyloid deposits.	Heparin	16-23	amyloid P component, serum	Homo sapiens	120-123
7947934-0	1994	Heparin and heparan sulfate enhancement of the inhibitory activity of plasminogen activator inhibitor type 1 toward urokinase type plasminogen activator.	Heparin	0-7	serpin family E member 1	Homo sapiens	70-108
7947934-5	1994	The intrinsic fluorescence of rpPAI-1 was shown to be slightly increased following addition of heparin (1.49 +/- 0.22%, n = 6), suggesting that heparin may enhance the inhibitory activity of PAI-1 toward tcu-PA both by a template mechanism and by a modification of PAI-1 structure.	Heparin	95-102	serpin family E member 1	Homo sapiens	32-37
7947934-5	1994	The intrinsic fluorescence of rpPAI-1 was shown to be slightly increased following addition of heparin (1.49 +/- 0.22%, n = 6), suggesting that heparin may enhance the inhibitory activity of PAI-1 toward tcu-PA both by a template mechanism and by a modification of PAI-1 structure.	Heparin	95-102	serpin family E member 1	Homo sapiens	191-196
7947934-5	1994	The intrinsic fluorescence of rpPAI-1 was shown to be slightly increased following addition of heparin (1.49 +/- 0.22%, n = 6), suggesting that heparin may enhance the inhibitory activity of PAI-1 toward tcu-PA both by a template mechanism and by a modification of PAI-1 structure.	Heparin	144-151	serpin family E member 1	Homo sapiens	32-37
7947934-5	1994	The intrinsic fluorescence of rpPAI-1 was shown to be slightly increased following addition of heparin (1.49 +/- 0.22%, n = 6), suggesting that heparin may enhance the inhibitory activity of PAI-1 toward tcu-PA both by a template mechanism and by a modification of PAI-1 structure.	Heparin	144-151	serpin family E member 1	Homo sapiens	191-196
7959685-3	1994	The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin.	Heparin	159-166	serpin family C member 1	Homo sapiens	74-79
7959685-3	1994	The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin.	Heparin	159-166	serpin family C member 1	Homo sapiens	97-102
7959685-3	1994	The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin.	Heparin	159-166	serpin family C member 1	Homo sapiens	97-102
7896748-2	1994	As a step towards a better understanding of the heparin-binding mechanism of mammalian ATIIIs, the amino acid sequence of porcine ATIII was established by sequence analysis of the peptides derived from cyanogen bromide cleavage and enzymatic digestion with lysyl endopeptidase, V8 protease, and trypsin.	Heparin	48-55	serpin family C member 1	Homo sapiens	87-92
7896748-5	1994	Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds.	Heparin	102-109	serpin family C member 1	Homo sapiens	8-13
7896748-10	1994	Neuraminidase treatment of each ATIII enhanced the heparin-affinity to the same extent.	Heparin	51-58	serpin family C member 1	Homo sapiens	32-37
7533846-19	1994	We conjecture that the mechanism of GRASP function features: 1) exposure of a cryptic sequence--after a change in conformation induced upon binding to polylysine--with affinity for an OLG signal-transducing receptor; and 2) interaction of its heparin-binding domain with OLG surface heparin sulfate proteoglycans and/or the aforementioned receptor.	Heparin	243-250	trafficking regulator and scaffold protein tamalin	Homo sapiens	36-41
7925646-5	1994	Heparin increased the expression of alpha-SM actin protein and mRNA in SMC from young and old rats, while TGF-beta 1 exerted the opposite action.	Heparin	0-7	actin gamma 2, smooth muscle	Rattus norvegicus	42-50
7925646-7	1994	In SMC cultured from intimal thickening, heparin induced a reduction of cell proliferation without modifying their characteristic epithelioid shape; TGF-beta 1 increased the proliferative activity and induced an elongated cell shape as well as a "hills and valleys" growth pattern similar to that observed in control medial SMC; both heparin and TGF-beta 1 induced an increase of alpha-SM actin expression.	Heparin	41-48	actin gamma 2, smooth muscle	Rattus norvegicus	386-394
7803746-0	1994	Management of cardiopulmonary bypass in a patient with heparin-induced thrombocytopenia using prostaglandin E1 and aspirin.	Heparin	55-62	small nucleolar RNA, H/ACA box 73A	Homo sapiens	108-122
8089154-6	1994	PIPLC released 23% of the total heparin-releasable LPL.	Heparin	32-39	lipoprotein lipase	Homo sapiens	51-54
8049432-5	1994	In contrast, when low-affinity heparin was added at the beginning of the reaction, there was an initial increase in PAI-1-thrombin complex formation, but this was rapidly followed by substantial proteolytic cleavage of unreacted PAI-1 and of the thrombin-PAI-1 complex.	Heparin	31-38	serpin family E member 1	Homo sapiens	229-234
8049432-5	1994	In contrast, when low-affinity heparin was added at the beginning of the reaction, there was an initial increase in PAI-1-thrombin complex formation, but this was rapidly followed by substantial proteolytic cleavage of unreacted PAI-1 and of the thrombin-PAI-1 complex.	Heparin	31-38	serpin family E member 1	Homo sapiens	229-234
8049432-7	1994	Quantitative zymographic analysis of tissue plasminogen activator and PAI-1 activities and chromogenic substrate assay of thrombin activity showed that low-affinity heparin stimulated the inactivation of PAI-1 by an equimolar amount of thrombin, but caused only a minimal stimulation of thrombin inhibition.	Heparin	165-172	serpin family E member 1	Homo sapiens	70-75
8049432-7	1994	Quantitative zymographic analysis of tissue plasminogen activator and PAI-1 activities and chromogenic substrate assay of thrombin activity showed that low-affinity heparin stimulated the inactivation of PAI-1 by an equimolar amount of thrombin, but caused only a minimal stimulation of thrombin inhibition.	Heparin	165-172	serpin family E member 1	Homo sapiens	204-209
8049432-8	1994	It is concluded that low-affinity heparin stimulates thrombin inhibition when PAI-1 is in excess, but, unexpectedly, that low-affinity heparin enhances PAI-1 inactivation when thrombin is equimolar to PAI-1.	Heparin	135-142	serpin family E member 1	Homo sapiens	152-157
8049432-8	1994	It is concluded that low-affinity heparin stimulates thrombin inhibition when PAI-1 is in excess, but, unexpectedly, that low-affinity heparin enhances PAI-1 inactivation when thrombin is equimolar to PAI-1.	Heparin	135-142	serpin family E member 1	Homo sapiens	152-157
7971256-1	1994	A male patient of 24 years who had experienced thrombotic episodes since the age of 15 displayed an unusually low antithrombin III (AT III) activity measured as heparin cofactor (13% of the normal), while a similarly decreased value (16% of normal) was found in a 26 year old brother who had suffered from thrombotic events since the age of 12 years.	Heparin	161-168	serpin family C member 1	Homo sapiens	114-130
7971256-1	1994	A male patient of 24 years who had experienced thrombotic episodes since the age of 15 displayed an unusually low antithrombin III (AT III) activity measured as heparin cofactor (13% of the normal), while a similarly decreased value (16% of normal) was found in a 26 year old brother who had suffered from thrombotic events since the age of 12 years.	Heparin	161-168	serpin family C member 1	Homo sapiens	132-138
7971256-2	1994	AT III heparin cofactor activities were close to 50% of normal in the father, mother, another brother and a sister, none of whom had experienced thrombotic episodes.	Heparin	7-14	serpin family C member 1	Homo sapiens	0-6
7950376-3	1994	Latent recombinant PAI-1 was purified by two chromatographic steps, cation exchange chromatography on CM-Sepharose and affinity chromatography on heparin-Sepharose.	Heparin	146-153	serpin family E member 1	Homo sapiens	19-24
8037658-0	1994	Interaction of heparin with synthetic antithrombin III peptide analogues.	Heparin	15-22	serpin family C member 1	Homo sapiens	38-54
8037658-8	1994	Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin.	Heparin	233-240	serpin family C member 1	Homo sapiens	200-216
7948751-4	1994	Recombinant murine D-factor produced a dose- and time-dependent inhibition of heparin-releasable LPL activity in differentiated 3T3-L1 adipocytes.	Heparin	78-85	leukemia inhibitory factor	Mus musculus	19-27
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	60-67	serpin family C member 1	Homo sapiens	78-94
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	60-67	serpin family C member 1	Homo sapiens	96-102
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	133-140	serpin family C member 1	Homo sapiens	78-94
7952425-5	1994	This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream.	Heparin	133-140	serpin family C member 1	Homo sapiens	96-102
7520898-7	1994	ELAM-1-mediated enhancement of tumor cell adhesion to HSE monolayer was also inhibited in a concentration-dependent manner by CH-271 fusion polypeptide or the sulfated chitin derivative sulfated carboxymethyl-chitin, which can bind to the heparin-binding domain of CH-271.	Heparin	239-246	selectin E	Homo sapiens	0-6
7664058-0	1994	A mechanism for heparin-induced potentiation of antithrombin III.	Heparin	16-23	serpin family C member 1	Homo sapiens	48-64
8011637-0	1994	Localization of the heparin-binding site of glia-derived nexin/protease nexin-1 by site-directed mutagenesis.	Heparin	20-27	serpin family E member 2	Rattus norvegicus	44-62
8011637-0	1994	Localization of the heparin-binding site of glia-derived nexin/protease nexin-1 by site-directed mutagenesis.	Heparin	20-27	serpin family E member 2	Rattus norvegicus	63-79
8011637-5	1994	A putative heparin-binding site is found in glia-derived nexin between residues 71 and 86; heparin-binding sites are found in homologous regions of antithrombin III and heparin cofactor II.	Heparin	11-18	serpin family E member 2	Rattus norvegicus	44-62
8011637-5	1994	A putative heparin-binding site is found in glia-derived nexin between residues 71 and 86; heparin-binding sites are found in homologous regions of antithrombin III and heparin cofactor II.	Heparin	91-98	serpin family E member 2	Rattus norvegicus	44-62
8011637-5	1994	A putative heparin-binding site is found in glia-derived nexin between residues 71 and 86; heparin-binding sites are found in homologous regions of antithrombin III and heparin cofactor II.	Heparin	91-98	serpin family D member 1	Rattus norvegicus	169-188
8011637-9	1994	These results support the hypothesis that the heparin-binding sites of glia-derived nexin, antithrombin III, and heparin cofactor II are found in homologous regions of the molecules.	Heparin	46-53	serpin family E member 2	Rattus norvegicus	71-89
8011637-9	1994	These results support the hypothesis that the heparin-binding sites of glia-derived nexin, antithrombin III, and heparin cofactor II are found in homologous regions of the molecules.	Heparin	46-53	serpin family D member 1	Rattus norvegicus	113-132
7516153-1	1994	The interaction between bovine lipoprotein lipase (bLPL) and human alpha 2-macroglobulin (alpha 2M) was studied by use of non-denaturing PAGE and gel-permeation, Zn(2+)-Sepharose and heparin-Sepharose chromatography.	Heparin	183-190	alpha-2-macroglobulin	Homo sapiens	90-98
7516153-5	1994	Preincubation of bLPL with heparin prevented complex-formation with alpha 2M, suggesting that alpha 2M interacts with the heparin-binding domain of bLPL.	Heparin	27-34	alpha-2-macroglobulin	Homo sapiens	68-76
7516153-5	1994	Preincubation of bLPL with heparin prevented complex-formation with alpha 2M, suggesting that alpha 2M interacts with the heparin-binding domain of bLPL.	Heparin	27-34	alpha-2-macroglobulin	Homo sapiens	94-102
7516153-5	1994	Preincubation of bLPL with heparin prevented complex-formation with alpha 2M, suggesting that alpha 2M interacts with the heparin-binding domain of bLPL.	Heparin	122-129	alpha-2-macroglobulin	Homo sapiens	68-76
7516153-5	1994	Preincubation of bLPL with heparin prevented complex-formation with alpha 2M, suggesting that alpha 2M interacts with the heparin-binding domain of bLPL.	Heparin	122-129	alpha-2-macroglobulin	Homo sapiens	94-102
8205697-8	1994	Thus, VCL increases the length of time required for thrombus formation in coronary arteries, and, when given with TPA and heparin, delays coronary artery reocclusion more effectively than aspirin.	Heparin	122-129	vinculin	Canis lupus familiaris	6-9
8175739-1	1994	Lipoprotein lipase (LPL) increases the cellular uptake and degradation of LDL by fibroblasts and macrophages via a heparin-sensitive process.	Heparin	115-122	lipoprotein lipase	Homo sapiens	0-18
8175739-1	1994	Lipoprotein lipase (LPL) increases the cellular uptake and degradation of LDL by fibroblasts and macrophages via a heparin-sensitive process.	Heparin	115-122	lipoprotein lipase	Homo sapiens	20-23
8180167-1	1994	Heparin was found to be an allosteric modulator of the amidolytic activity of the protease acrosin.	Heparin	0-7	acrosin	Homo sapiens	91-98
8180167-9	1994	At the optimal heparin concentration, the value of kass for the acrosin-protein C inhibitor reaction was 230-fold higher ((5.6 +/- 0.1) x 10(7) M-1 s-1) than in the absence of heparin.	Heparin	15-22	acrosin	Homo sapiens	64-71
8180167-9	1994	At the optimal heparin concentration, the value of kass for the acrosin-protein C inhibitor reaction was 230-fold higher ((5.6 +/- 0.1) x 10(7) M-1 s-1) than in the absence of heparin.	Heparin	176-183	acrosin	Homo sapiens	64-71
8180167-10	1994	The results suggest that protein C inhibitor may be important in the physiological control of acrosin activity, particularly where the presence of heparin-like glycosaminoglycans would stimulate the acrosin-protein C inhibitor reaction.	Heparin	147-154	acrosin	Homo sapiens	94-101
8180167-10	1994	The results suggest that protein C inhibitor may be important in the physiological control of acrosin activity, particularly where the presence of heparin-like glycosaminoglycans would stimulate the acrosin-protein C inhibitor reaction.	Heparin	147-154	acrosin	Homo sapiens	199-206
8013675-6	1994	The alterations in PAI-1 showed no correlation with those of t-PA, whereas heparin had a sparing effect on PAI-1 consumption.	Heparin	75-82	serpin family E member 1	Homo sapiens	107-112
7512382-0	1994	Conformational change in antithrombin induced by heparin probed with a monoclonal antibody against the 1C/4B region.	Heparin	49-56	serpin family C member 1	Homo sapiens	25-37
7512382-1	1994	A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin.	Heparin	74-81	serpin family C member 1	Homo sapiens	61-73
7512382-1	1994	A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin.	Heparin	74-81	serpin family C member 1	Homo sapiens	160-172
7512382-1	1994	A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin.	Heparin	182-189	serpin family C member 1	Homo sapiens	61-73
7512382-1	1994	A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin.	Heparin	182-189	serpin family C member 1	Homo sapiens	160-172
8144612-1	1994	Human lipoprotein lipase (LPL) monomer consists of two domains, a larger NH2-terminal domain that contains catalytic residues and a smaller COOH-terminal domain that modulates substrate specificity and is a major determinant of heparin binding.	Heparin	228-235	lipoprotein lipase	Homo sapiens	6-24
8144612-1	1994	Human lipoprotein lipase (LPL) monomer consists of two domains, a larger NH2-terminal domain that contains catalytic residues and a smaller COOH-terminal domain that modulates substrate specificity and is a major determinant of heparin binding.	Heparin	228-235	lipoprotein lipase	Homo sapiens	26-29
8144612-9	1994	Also, the affinity of antibody-reacted LPL for heparin was not significantly different from that of LPL alone, suggesting that (i) the heparin-binding site is physically distinct from the COOH-terminal domain region required for lipolysis and (ii) binding of antibody did not cause dimer dissociation.	Heparin	47-54	lipoprotein lipase	Homo sapiens	39-42
8144612-9	1994	Also, the affinity of antibody-reacted LPL for heparin was not significantly different from that of LPL alone, suggesting that (i) the heparin-binding site is physically distinct from the COOH-terminal domain region required for lipolysis and (ii) binding of antibody did not cause dimer dissociation.	Heparin	135-142	lipoprotein lipase	Homo sapiens	39-42
8054465-0	1994	Prolonged oral contraceptive therapy in a woman with an antithrombin III abnormality involving heparin binding (type IIc) without thromboembolic complications.	Heparin	95-102	serpin family C member 1	Homo sapiens	56-72
8070483-1	1994	The purpose of this study was to evaluate the effect of low molecular weight heparin Fragmin on thrombolysis with tissue-type plasminogen activator (rt-PA) and to compare its effect to that of standard heparin.	Heparin	77-84	tissue-type plasminogen activator	Oryctolagus cuniculus	114-147
8144523-3	1994	Recently, using ligand blotting and affinity chromatography we identified a 116-kDa heparin-releasable LPL-binding protein (hrp-116) from endothelial cells which was not a HSPG (Sivaram, P., Klein, M. G., and Goldberg, I. J.	Heparin	84-91	lipoprotein lipase	Homo sapiens	103-106
8144523-8	1994	Using heparin-agarose affinity chromatography, a 116-kDa LPL-binding protein was purified from endothelial cell extracts.	Heparin	6-13	lipoprotein lipase	Homo sapiens	57-60
8144523-15	1994	The inhibitory effects of mAb3 and mAb19 were abolished following treatment of cells with heparin, which removes the 116-kDa LPL-binding protein.	Heparin	90-97	lipoprotein lipase	Homo sapiens	125-128
8028039-2	1994	One possible site of HSPG attachment is a heparin binding domain of fibronectin, which is present in the synthetic peptide FN-C/H II.	Heparin	42-49	fibronectin 1	Rattus norvegicus	68-79
8003980-2	1994	ATIII attains its full biological activity only upon binding polysulfated oligosaccharides, such as heparin.	Heparin	100-107	serpin family C member 1	Homo sapiens	0-5
8003980-3	1994	A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay.	Heparin	72-79	serpin family C member 1	Homo sapiens	99-104
8003980-3	1994	A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay.	Heparin	131-138	serpin family C member 1	Homo sapiens	99-104
8003980-3	1994	A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay.	Heparin	131-138	serpin family C member 1	Homo sapiens	265-270
8003980-3	1994	A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay.	Heparin	131-138	serpin family C member 1	Homo sapiens	99-104
8003980-3	1994	A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay.	Heparin	131-138	serpin family C member 1	Homo sapiens	265-270
8003980-4	1994	Peptide F123-G148, which encompasses both the purported high-affinity pentasaccharide binding region and an adjacent, C-terminally directed segment of ATIII, was found to bind heparin with good affinity, but amino-terminal truncations of this sequence, including L130-G148 and K136-G148 displayed attenuated heparin binding activities.	Heparin	176-183	serpin family C member 1	Homo sapiens	151-156
8003980-8	1994	K121-A134 also effectively competes with ATIII for binding heparin.	Heparin	59-66	serpin family C member 1	Homo sapiens	41-46
8003980-9	1994	Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions.	Heparin	84-91	serpin family C member 1	Homo sapiens	115-120
8003980-9	1994	Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions.	Heparin	84-91	serpin family C member 1	Homo sapiens	193-198
8003980-9	1994	Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions.	Heparin	185-192	serpin family C member 1	Homo sapiens	115-120
8003980-9	1994	Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions.	Heparin	185-192	serpin family C member 1	Homo sapiens	193-198
8135813-1	1994	A 15kDa-protein (HBp15) was purified from mouse submandibular gland and bovine brain by virtue of its heparin-binding property.	Heparin	102-109	ribosomal protein L22	Homo sapiens	17-22
8208096-6	1994	Based on experimental evidence, a scheme was proposed, which describes the impact of protein adsorption processes on the anticoagulative activity of surface-bound heparin, It is concluded that AT-III plays a particular role as the major component of the adsorption layer that is responsible for the nature of interactions of polymer materials with blood at the protein and cellular levels.	Heparin	163-170	serpin family C member 1	Homo sapiens	193-199
7517074-3	1994	At 0.5-1.0 units/mL antithrombin activity with heparin or hirudin, the ACT was lowered progressively by the addition of increasing concentrations of lysed platelets to as much as 20 seconds below the baseline clotting time obtained with unanticoagulated blood samples.	Heparin	47-54	serpin family C member 1	Homo sapiens	20-32
8172405-1	1994	Diamine oxidase (DAO), an enzyme of small intestinal origin, is released from mucosal storage sites by IV administration of heparin, to yield the plasma postheparin DAO (PHD) curve.	Heparin	124-131	D-amino acid oxidase	Equus caballus	0-15
8172405-1	1994	Diamine oxidase (DAO), an enzyme of small intestinal origin, is released from mucosal storage sites by IV administration of heparin, to yield the plasma postheparin DAO (PHD) curve.	Heparin	124-131	D-amino acid oxidase	Equus caballus	17-20
8172405-1	1994	Diamine oxidase (DAO), an enzyme of small intestinal origin, is released from mucosal storage sites by IV administration of heparin, to yield the plasma postheparin DAO (PHD) curve.	Heparin	124-131	D-amino acid oxidase	Equus caballus	165-168
8172405-9	1994	Peritoneal fluid DAO activity remained low throughout the study, but increased slightly in horses with VSO that received heparin, possibly because of DAO from extravasated blood in the peritoneal fluid.	Heparin	121-128	D-amino acid oxidase	Equus caballus	17-20
8172405-9	1994	Peritoneal fluid DAO activity remained low throughout the study, but increased slightly in horses with VSO that received heparin, possibly because of DAO from extravasated blood in the peritoneal fluid.	Heparin	121-128	D-amino acid oxidase	Equus caballus	150-153
8172405-10	1994	Results indicated that the plasma DAO response to IV administered heparin in horses is similar to that in other mammals, but, unlike other species, baseline and postheparin DAO activities did not change as expected after small intestinal vascular obstruction and mucosal injury.	Heparin	66-73	D-amino acid oxidase	Equus caballus	34-37
8180343-2	1994	Antithrombin is also the major plasma cofactor of heparin which exerts its therapeutic effect primarily through its ability to substantially increase the rate of inactivation by antithrombin of the procoagulant serine proteases.	Heparin	50-57	serpin family C member 1	Homo sapiens	0-12
8180343-2	1994	Antithrombin is also the major plasma cofactor of heparin which exerts its therapeutic effect primarily through its ability to substantially increase the rate of inactivation by antithrombin of the procoagulant serine proteases.	Heparin	50-57	serpin family C member 1	Homo sapiens	178-190
8180343-3	1994	Binding of heparin to antithrombin is thus believed to be a prerequisite for this rate enhancement effect.	Heparin	11-18	serpin family C member 1	Homo sapiens	22-34
8180343-4	1994	Heparin binding to antithrombin is mediated by a well-defined unique heparin pentasaccharide sequence.	Heparin	69-76	serpin family C member 1	Homo sapiens	19-31
8180343-6	1994	Heparin species with longer polysaccharide chains appear to be required in order to enhance the inhibition of thrombin by antithrombin.	Heparin	0-7	serpin family C member 1	Homo sapiens	122-134
8180343-7	1994	This may be because the enhancement of this reaction requires that heparin interacts simultaneously with both the antithrombin and the thrombin molecules.	Heparin	67-74	serpin family C member 1	Homo sapiens	114-126
8180343-8	1994	This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin.	Heparin	47-54	serpin family C member 1	Homo sapiens	59-71
8180343-8	1994	This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin.	Heparin	47-54	serpin family C member 1	Homo sapiens	89-101
8180343-8	1994	This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin.	Heparin	148-155	serpin family C member 1	Homo sapiens	59-71
8180343-8	1994	This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin.	Heparin	148-155	serpin family C member 1	Homo sapiens	89-101
8180343-9	1994	The role of the heparin-induced conformational change in enhancing serine protease inhibition by antithrombin is also explored.	Heparin	16-23	serpin family C member 1	Homo sapiens	97-109
8180343-10	1994	Then, based on available data, an hypothesis is proposed to explain the mechanisms by which heparin accelerates the rate of inactivation by antithrombin of the various serine proteases.	Heparin	92-99	serpin family C member 1	Homo sapiens	140-152
8294485-3	1994	We have cloned, by cross-hybridization with the cDNA from rat liver heparan sulfate N-deacetylase/N-sulfotransferase, a protein from a heparin synthesizing mastocytoma derived cell line called MST.	Heparin	135-142	N-deacetylase and N-sulfotransferase 1	Rattus norvegicus	68-116
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	36-43	serpin family C member 1	Homo sapiens	92-104
8186356-2	1994	Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus.	Heparin	36-43	serpin family C member 1	Homo sapiens	139-151
7735321-2	1994	One abundant ecto-PK component is believed to be a protein kinase CKII since it phosphorylates phosvitin and casein, is sensitive to heparin at low concentrations, and can use both ATP and GTP as cosubstrate.	Heparin	133-140	casein kinase 2 alpha 1	Homo sapiens	66-70
8186654-7	1994	Mean post-heparin LPL was significantly lower in patients than controls 10 min after heparin administration (2.98 +/- 1.04 and 3.86 +/- 0.93 mumol ml-1 h-1, respectively, P = 0.001), and 37% patients had values below the 10th percentile of controls.	Heparin	10-17	lipoprotein lipase	Homo sapiens	18-21
8152901-1	1994	Some commercially available chronometric assays are influenced by the residual antithrombin activity of low molecular weight heparins (LMWH) and they underestimate the ex vivo anti Xa activity.	Heparin	125-133	serpin family C member 1	Homo sapiens	79-91
8263926-7	1993	This latter form also had a low affinity for heparin and in these ways resembles latent antithrombin.	Heparin	45-52	serpin family C member 1	Homo sapiens	88-100
8274446-4	1993	The biological ability of AIGF to stimulate SC-3 cell growth is inhibited by heparin or suramin.	Heparin	77-84	fibroblast growth factor 8	Homo sapiens	26-30
8243674-0	1993	Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinities.	Heparin	67-74	serpin family C member 1	Homo sapiens	25-37
7692967-5	1993	Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present.	Heparin	375-382	serpin family C member 1	Homo sapiens	212-224
7692967-6	1993	Similarly, the presence of therapeutic levels of heparin (approximately 1 unit/mL) in normal, factor XII-deficient, and prekallikrein-deficient plasmas enhanced the rate of inactivation of added kallikrein by 2.3-fold and significantly altered the partitioning of radiolabeled kallikrein from predominantly C1-inhibitor and alpha 2-macroglobulin complexes (86-92%) to mostly antithrombin complexes (50-53%).	Heparin	49-56	serpin family C member 1	Homo sapiens	375-387
7692967-8	1993	The contribution of antithrombin to kallikrein inhibition in plasma remained significant (approximately 40-70%) at optimal concentrations of unfractionated or size- and antithrombin affinity-fractionated heparin, in the presence of plasma levels of calcium and zinc ions, at 37 degrees C, and with minimal plasma dilution.	Heparin	204-211	serpin family C member 1	Homo sapiens	20-32
7692967-9	1993	These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans.	Heparin	141-148	serpin family C member 1	Homo sapiens	27-39
7692967-9	1993	These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans.	Heparin	152-159	serpin family C member 1	Homo sapiens	27-39
8218292-3	1993	Both H-kininogen-stimulated and unstimulated heparin rate enhancements initially increased with increasing heparin concentration in a manner corresponding to the saturation of antithrombin with heparin (KD = 10-30 nM).	Heparin	45-52	serpin family C member 1	Homo sapiens	176-188
8218292-3	1993	Both H-kininogen-stimulated and unstimulated heparin rate enhancements initially increased with increasing heparin concentration in a manner corresponding to the saturation of antithrombin with heparin (KD = 10-30 nM).	Heparin	107-114	serpin family C member 1	Homo sapiens	176-188
8218292-3	1993	Both H-kininogen-stimulated and unstimulated heparin rate enhancements initially increased with increasing heparin concentration in a manner corresponding to the saturation of antithrombin with heparin (KD = 10-30 nM).	Heparin	107-114	serpin family C member 1	Homo sapiens	176-188
8218292-5	1993	These results implied that H-kininogen stimulation required the formation of a quaternary complex in which antithrombin and H-kininogen-kallikrein complex were bound to the same heparin chain.	Heparin	178-185	serpin family C member 1	Homo sapiens	107-119
8218292-7	1993	The importance of H-kininogen-kallikrein complex binding to heparin for kininogen stimulation was further indicated from the marked salt dependence of the second-order rate constant for the association of H-kininogen-kallikrein complex but not free kallikrein with antithrombin-heparin complex, under conditions where saturation of the two binary complexes was maintained.	Heparin	60-67	serpin family C member 1	Homo sapiens	265-277
8219221-6	1993	Induction of TF activity by PC-Al was antagonized by dextran sulfate, heparin, fucoidan, and concanavalin A but not by ovalbumin, polyglutamic acid, or polyvinyl sulfate.	Heparin	70-77	coagulation factor III, tissue factor	Homo sapiens	13-15
8288243-6	1993	The mutated LPL protein was secreted from the cells in a manner similar to that of wild-type LPL and bound to heparin-Sepharose with identical properties.	Heparin	110-117	lipoprotein lipase	Homo sapiens	12-15
8227328-3	1993	In muscle, detraining resulted in a decrease in LPL activity in both the heparin-releasable (HR) (-45%, P &lt; 0.05) and cellular (extractable [EXT]) (-75%, P &lt; 0.005) fractions, with no significant changes in LPL immunoreactive mass and mRNA levels.	Heparin	73-80	lipoprotein lipase	Homo sapiens	48-51
8226804-4	1993	Since both PDGF A-chain and HB-EGF have affinity for heparin, we also examined the effect of thrombin and DEX on the release of heparin binding mitogenic activity from SMCs.	Heparin	53-60	heparin binding EGF like growth factor	Homo sapiens	28-34
8374612-6	1993	Flight muscle LpL shows affinity for immobilized copper as well as for immobilized heparin.	Heparin	83-90	lipoprotein lipase	Homo sapiens	14-17
8360197-2	1993	High salt and heparin-containing buffers are capable of solubilizing asymmetric AChE molecules from skeletal muscle; however, detachment of AChE specifically from synaptic basal lamina using these procedures has not been demonstrated.	Heparin	14-21	acetylcholinesterase	Rattus norvegicus	80-84
8259547-6	1993	However, when heparin was added ATIII was the major anticoagulant, but profound prolongation of the clotting time was only seen when TFPI was also added.	Heparin	14-21	serpin family C member 1	Homo sapiens	32-37
8259547-7	1993	In an ATIII deficient plasma heparin did not augment the effect of TFPI, showing that the increased effect of TFPI in the presence of heparin is dependent on the anticoagulant activity of ATIII/heparin.	Heparin	134-141	serpin family C member 1	Homo sapiens	188-193
8357789-0	1993	Transmission of conformational change from the heparin binding site to the reactive center of antithrombin.	Heparin	47-54	serpin family C member 1	Homo sapiens	94-106
8357789-1	1993	Heparin greatly increases the rates at which antithrombin inhibits target proteinases.	Heparin	0-7	serpin family C member 1	Homo sapiens	45-57
8357789-2	1993	An important part of this rate acceleration is a heparin-induced conformational change in antithrombin.	Heparin	49-56	serpin family C member 1	Homo sapiens	90-102
8215954-3	1993	The other surface consisted of a fraction of heparin molecules with low affinity for antithrombin (LA heparin surface) and essentially devoid of antithrombin-binding as well as anticoagulant activity.	Heparin	45-52	serpin family C member 1	Homo sapiens	85-97
8343518-3	1993	The heparin binding affinities and proportions of normal and variant AT III in plasma from patients with mutations of AT III have been quantitated for the first time using the binding assay.	Heparin	4-11	serpin family C member 1	Homo sapiens	118-124
8362374-3	1993	One of these antibodies was studied in detail and was found to inhibit the heparin dependent activation of antithrombin III by up to 80%.	Heparin	75-82	serpin family C member 1	Homo sapiens	107-123
8392335-3	1993	The phosphorylation of dystrophin was activated by cyclic AMP, cyclic GMP, calcium and calmodulin, and was inhibited by cyclic AMP-dependent protein kinase peptide inhibitor, mastoparan and heparin.	Heparin	190-197	dystrophin	Homo sapiens	23-33
8236084-8	1993	The drug heparin and blood vessel wall heparan sulfates probably also inhibit SMC growth via suppression of c-myb.	Heparin	9-16	MYB proto-oncogene, transcription factor	Homo sapiens	108-113
7687250-5	1993	A high yield of p66/p51 RT was obtained when the time from application to elution of heparin-Sepharose in the second chromatographic step was prolonged.	Heparin	85-92	DNA polymerase delta 3, accessory subunit	Homo sapiens	16-19
7687250-5	1993	A high yield of p66/p51 RT was obtained when the time from application to elution of heparin-Sepharose in the second chromatographic step was prolonged.	Heparin	85-92	tumor protein p63	Homo sapiens	20-23
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	serpin family C member 1	Homo sapiens	125-141
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	serpin family C member 1	Homo sapiens	143-148
8408111-1	1993	Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE).	Heparin	20-27	serpin family C member 1	Homo sapiens	51-67
8408111-1	1993	Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE).	Heparin	20-27	serpin family C member 1	Homo sapiens	69-74
7681826-12	1993	Heparin and heparan sulfate, but not other glycosaminoglycans such as chondroitin sulfate, efficiently inhibited the binding of 125I-VEGF to alpha 2M.	Heparin	0-7	alpha-2-macroglobulin	Homo sapiens	141-149
8458417-1	1993	We have previously communicated that heparin co-solubilizes the asymmetric form of acetylcholinesterase (AChE) and a dermatan sulfate proteoglycan from the extracellular matrix (ECM) of rat skeletal muscles.	Heparin	37-44	acetylcholinesterase	Rattus norvegicus	105-109
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	145-152	thrombomodulin	Homo sapiens	34-48
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	145-152	serpin family C member 1	Homo sapiens	100-116
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	161-168	thrombomodulin	Homo sapiens	34-48
8388351-8	1993	The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin.	Heparin	161-168	serpin family C member 1	Homo sapiens	100-116
8388354-7	1993	In whole plasma in the absence of platelet release, antithrombin III was the most abundant protein bound to therapeutic doses of unfractionated heparin, and histidine-rich glycoprotein its only effective competitor, while both histidine-rich glycoprotein and vitronectin were potentially important modulators of LMW heparin activity.	Heparin	144-151	serpin family C member 1	Homo sapiens	52-68
8486606-1	1993	CK-II has been partially purified from a 1.5 M KCl extract of unfertilized sea urchin eggs by means of DEAE-cellulose column chromatography, gel filtration on Sephacryl S300, and heparin-agarose column chromatography, successively.	Heparin	179-186	casein kinase 2 alpha 1	Homo sapiens	0-5
8291376-3	1993	After discovery of acquired antithrombin III deficiency superimposed on the protein S deficiency, he was given antithrombin III concentrates with the intravenous heparin.	Heparin	162-169	serpin family C member 1	Homo sapiens	28-44
8362268-9	1993	These studies suggest that specific synthetic analogues of heparin such as the pentasaccharide and lactobionic acid can be used to study the relative contributions of AT III and HC II in the control of protease activation during thrombogenesis.	Heparin	59-66	serpin family C member 1	Homo sapiens	167-173
8097075-3	1993	Standard heparin (hep) and non-anticoagulant N-desulfated acetylated heparin (DSA-hep) significantly reduced the fibronectin content in the conditioned media of subconfluent, confluent, and supraconfluent rat glomerular mesangial cells (MCs) in culture, as assessed by a sandwich ELISA technique.	Heparin	9-16	fibronectin 1	Rattus norvegicus	113-124
8097075-3	1993	Standard heparin (hep) and non-anticoagulant N-desulfated acetylated heparin (DSA-hep) significantly reduced the fibronectin content in the conditioned media of subconfluent, confluent, and supraconfluent rat glomerular mesangial cells (MCs) in culture, as assessed by a sandwich ELISA technique.	Heparin	69-76	fibronectin 1	Rattus norvegicus	113-124
8097075-4	1993	Both heparins significantly increased the amount of cell-associated fibronectin in sparse and subconfluent MCs.	Heparin	5-13	fibronectin 1	Rattus norvegicus	68-79
1463450-7	1992	The heparin affinity, a fundamental and distinguishing property of EC-SOD, was found to be slightly increased.	Heparin	4-11	extracellular superoxide dismutase [Cu-Zn]	Oryctolagus cuniculus	67-73
1484387-0	1992	The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans.	Heparin	41-48	neural cell adhesion molecule 1	Homo sapiens	4-33
1484387-0	1992	The neural cell adhesion molecule (NCAM) heparin binding domain binds to cell surface heparan sulfate proteoglycans.	Heparin	41-48	neural cell adhesion molecule 1	Homo sapiens	35-39
1434535-7	1992	Adhesion was inhibited by antiserum against TSP, and by an anti-CD36 monoclonal antibody tested in the presence of heparin, but not by the peptide Gly-Arg-Gly-Asp-Ser.	Heparin	115-122	CD36 molecule	Homo sapiens	64-68
1415434-12	1992	Prophylactic heparin is suggested during pregnancy for protein C--deficient women with personal or family histories of thrombosis.	Heparin	13-20	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	55-64
1382959-6	1992	Heparin, which releases proteins attached to cell surface proteoglycans, increased medium concentrations of IGFBP-3 and decreased IGFBP-3 binding to fibroblasts.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	108-115
1382959-6	1992	Heparin, which releases proteins attached to cell surface proteoglycans, increased medium concentrations of IGFBP-3 and decreased IGFBP-3 binding to fibroblasts.	Heparin	0-7	insulin like growth factor binding protein 3	Homo sapiens	130-137
1644832-11	1992	After heparin treatment of endothelial cells, LPL binding to and internalization by the cells decreased greater than 70% compared to control cells.	Heparin	6-13	lipoprotein lipase	Homo sapiens	46-49
1644832-12	1992	These results suggest that endothelial cells synthesize a heparin-releasable, high affinity 116-kDa LPL binding protein.	Heparin	58-65	lipoprotein lipase	Homo sapiens	100-103
1412157-1	1992	The decay rate of thrombin in plasma is shown to be linearly proportional to the concentration of antithrombin III (AT III), not only in the absence but also in the presence of heparin.	Heparin	177-184	serpin family C member 1	Homo sapiens	98-114
1412157-1	1992	The decay rate of thrombin in plasma is shown to be linearly proportional to the concentration of antithrombin III (AT III), not only in the absence but also in the presence of heparin.	Heparin	177-184	serpin family C member 1	Homo sapiens	116-122
1412157-2	1992	This is a consequence of partitioning of heparin between AT III and other plasma proteins.	Heparin	41-48	serpin family C member 1	Homo sapiens	57-63
1412157-7	1992	From the results presented it is evident that characteristic parameters of heparin action have to be normalised to the AT III concentration.	Heparin	75-82	serpin family C member 1	Homo sapiens	119-125
1412157-8	1992	On this basis we define a Standard Independent Unit of the antithrombin activity of heparin.	Heparin	84-91	serpin family C member 1	Homo sapiens	59-71
10078276-4	1992	We found in the heparin-coated group a significantly reduced complement hemolytic activity (CH50), remaining higher leukocyte numbers, significantly decreased release of beta-glucuronidase, and most strikingly a complete prevention of tumor necrosis factor (TNF) formation.	Heparin	16-23	tumor necrosis factor	Oryctolagus cuniculus	235-256
10078276-4	1992	We found in the heparin-coated group a significantly reduced complement hemolytic activity (CH50), remaining higher leukocyte numbers, significantly decreased release of beta-glucuronidase, and most strikingly a complete prevention of tumor necrosis factor (TNF) formation.	Heparin	16-23	tumor necrosis factor	Oryctolagus cuniculus	258-261
1279089-0	1992	Human lipoprotein lipase: relationship of activity, heparin affinity, and conformation as studied with monoclonal antibodies.	Heparin	52-59	lipoprotein lipase	Homo sapiens	6-24
1279089-12	1992	The effect of conformation and dimeric structure on LPL-heparin interaction was studied by heparin-Sepharose chromatography.	Heparin	56-63	lipoprotein lipase	Homo sapiens	52-55
1279089-12	1992	The effect of conformation and dimeric structure on LPL-heparin interaction was studied by heparin-Sepharose chromatography.	Heparin	91-98	lipoprotein lipase	Homo sapiens	52-55
1634549-7	1992	Using low concentrations of heparin, more LPL was released from endothelial cells than BFC-1 beta, suggesting that the affinity of LPL binding to the adipocytes was greater than LPL affinity for endothelial cells.	Heparin	28-35	lipoprotein lipase	Homo sapiens	42-45
1351851-9	1992	One milligram per milliliter of heparin, a concentration that inhibited bFGF-induced neurite outgrowth, also inhibited bFGF-induced increases in S6 phosphorylation and ODC activity.	Heparin	32-39	ornithine decarboxylase 1	Rattus norvegicus	168-171
1618758-2	1992	The synthetic antithrombin-binding heparin pentasaccharide and a full-length heparin of approximately 26 saccharides containing this specific sequence have been compared with respect to their interactions with antithrombin and their ability to promote inhibition and substrate reactions of antithrombin with thrombin and factor Xa.	Heparin	35-42	serpin family C member 1	Homo sapiens	14-26
1618758-7	1992	In contrast, the full-length heparin produced large ionic strength-dependent enhancements in second order rate constants for both antithrombin reactions of 4,300-fold for thrombin and 580-fold for factor Xa at I 0.15.	Heparin	29-36	serpin family C member 1	Homo sapiens	130-142
1374298-0	1992	Heparin inhibits the expression of tissue-type plasminogen activator by smooth muscle cells in injured rat carotid artery.	Heparin	0-7	plasminogen activator, tissue type	Rattus norvegicus	35-68
1374298-2	1992	Since heparin inhibits SMC migration and intimal thickening, we have examined the possibility that heparin might also inhibit t-PA expression.	Heparin	99-106	plasminogen activator, tissue type	Rattus norvegicus	126-130
1374298-7	1992	Heparin treatment decreased t-PA, but not u-PA, activity.	Heparin	0-7	plasminogen activator, tissue type	Rattus norvegicus	28-32
1374298-8	1992	Total t-PA protein was decreased by treatment with heparin but not chondroitin sulfate, and the decrease in t-PA protein was associated with decreased t-PA mRNA in the media.	Heparin	51-58	plasminogen activator, tissue type	Rattus norvegicus	6-10
1315738-4	1992	This differs from the putative heparin-binding site in the related proteins antithrombin and heparin cofactor.	Heparin	31-38	serpin family C member 1	Homo sapiens	76-88
1315739-3	1992	Synthetic peptides corresponding to the putative heparin binding regions of antithrombin, heparin cofactor, and protein C inhibitor bound to heparin directly and interfered in heparin-enhanced proteinase inhibition assays.	Heparin	49-56	serpin family C member 1	Homo sapiens	76-88
1519763-8	1992	The generation of cleaved AT-III in human plasma by HNE in the presence of heparin could be monitored as well.	Heparin	75-82	serpin family C member 1	Homo sapiens	26-32
1569403-11	1992	DNA and heparin inhibited binding of CRP trimers to intact C1q, as well as to each peptide 14-26 and 76-92, suggesting involvement of these regions in C1q-CLR binding reactions generally.	Heparin	8-15	complement C1q A chain	Homo sapiens	59-62
1569403-11	1992	DNA and heparin inhibited binding of CRP trimers to intact C1q, as well as to each peptide 14-26 and 76-92, suggesting involvement of these regions in C1q-CLR binding reactions generally.	Heparin	8-15	complement C1q A chain	Homo sapiens	151-154
1554734-0	1992	Characterization of the heparin-binding site of glia-derived nexin/protease nexin-1.	Heparin	24-31	serpin family E member 2	Homo sapiens	48-66
1554734-1	1992	The interaction of heparin with glia-derived nexin (GDN) has been characterized and compared to that observed between heparin and antithrombin III (ATIII).	Heparin	19-26	serpin family E member 2	Homo sapiens	32-50
1554734-1	1992	The interaction of heparin with glia-derived nexin (GDN) has been characterized and compared to that observed between heparin and antithrombin III (ATIII).	Heparin	19-26	serpin family E member 2	Homo sapiens	52-55
1554734-2	1992	Heparin was fractionated according to its affinity for immobilized GDN, and the ability of various fractions to accelerate the inhibition rate of thrombin by either GDN or ATIII was examined.	Heparin	0-7	serpin family E member 2	Homo sapiens	67-70
1554734-4	1992	Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII.	Heparin	109-116	serpin family C member 1	Homo sapiens	93-98
1554734-4	1992	Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII.	Heparin	196-203	serpin family C member 1	Homo sapiens	93-98
1554734-4	1992	Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII.	Heparin	196-203	serpin family E member 2	Homo sapiens	229-232
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	76-83	serpin family E member 2	Homo sapiens	21-24
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	76-83	serpin family E member 2	Homo sapiens	130-133
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	76-83	serpin family E member 2	Homo sapiens	130-133
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	190-197	serpin family E member 2	Homo sapiens	21-24
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	190-197	serpin family E member 2	Homo sapiens	130-133
1554734-5	1992	The CNBr fragment of GDN between residues 63 and 144 was able to reduce the heparin-accelerated rate of inhibition of thrombin by GDN indicating that this region of GDN was able to bind the heparin molecules responsible for the acceleration.	Heparin	190-197	serpin family E member 2	Homo sapiens	130-133
1554734-7	1992	Fragment 63-144 was less effective in decreasing the heparin-accelerated rate of inhibition of thrombin by ATIII.	Heparin	53-60	serpin family C member 1	Homo sapiens	107-112
1554734-8	1992	The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII.	Heparin	42-49	serpin family E member 2	Homo sapiens	107-110
1554734-8	1992	The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII.	Heparin	42-49	serpin family C member 1	Homo sapiens	116-121
1554734-8	1992	The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII.	Heparin	149-156	serpin family E member 2	Homo sapiens	174-177
1554734-8	1992	The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII.	Heparin	149-156	serpin family C member 1	Homo sapiens	182-187
1555650-1	1992	An antithrombin variant with reduced heparin affinity resulting from the substitution L99F.	Heparin	37-44	serpin family C member 1	Homo sapiens	3-15
1551206-2	1992	Both heparin and hirudin enhanced total fibrinolysis in an ex vivo arteriovenous shunt preparation: 82 +/- 2% and 79 +/- 2%, respectively, compared with 51 +/- 8% for t-PA alone (P less than 0.05) and 50 +/- 4% for t-PA plus aspirin (p less than 0.05).	Heparin	5-12	tissue-type plasminogen activator	Oryctolagus cuniculus	215-219
1551206-3	1992	Heparin coadministered with t-PA significantly reduced the half-time for clot lysis compared with t-PA alone (p less than 0.05), whereas hirudin coadministered with t-PA significantly reduced the half-time for clot lysis compared with that for t-PA alone, t-PA plus aspirin, and t-PA plus heparin (5.5 +/- 0.6 versus 12.1 +/- 2.0 versus 12.6 +/- 2.2 versus 10.0 +/- 0.8 minutes, respectively; p less than 0.05).	Heparin	0-7	tissue-type plasminogen activator	Oryctolagus cuniculus	28-32
1551206-4	1992	Both heparin and hirudin prevented the increase in ADP-induced platelet aggregation normally seen with t-PA alone (p less than 0.01 by t test; p less than 0.05 by two-way analysis of variance).	Heparin	5-12	tissue-type plasminogen activator	Oryctolagus cuniculus	103-107
1554373-8	1992	Skin fibroblast alpha-L-iduronidase activity towards the heparin-derived oligosaccharides was influenced by the same substrate aglycone structural features as was observed for the human liver enzyme.	Heparin	57-64	alpha-L-iduronidase	Homo sapiens	16-35
1311309-5	1992	rsk kinase is inhibited by low concentrations of heparin as well as by beta-glycerophosphate and calcium.	Heparin	49-56	ribosomal protein S6 kinase A3 L homeolog	Xenopus laevis	0-3
1540583-0	1992	A peptide model for the heparin binding site of antithrombin III.	Heparin	24-31	serpin family C member 1	Homo sapiens	48-64
1540583-1	1992	A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding.	Heparin	24-31	serpin family C member 1	Homo sapiens	48-64
1540583-1	1992	A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding.	Heparin	24-31	serpin family C member 1	Homo sapiens	66-71
1540583-1	1992	A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding.	Heparin	133-140	serpin family C member 1	Homo sapiens	48-64
1540583-1	1992	A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding.	Heparin	133-140	serpin family C member 1	Homo sapiens	66-71
1540583-3	1992	In the presence of heparin, however, the peptide ATIII(123-139) assumed a stable conformation, whereas peptide ATIII random did not.	Heparin	19-26	serpin family C member 1	Homo sapiens	49-54
1540583-5	1992	The ATIII(123-139)-heparin complex contained beta-structure, rather than helical structure.	Heparin	19-26	serpin family C member 1	Homo sapiens	4-9
1540583-6	1992	This finding is incompatible with current models of heparin binding and suggests that heparin binding may induce nonnative structures at the binding site which could, in turn, lead to activation of ATIII.	Heparin	52-59	serpin family C member 1	Homo sapiens	198-203
1540583-6	1992	This finding is incompatible with current models of heparin binding and suggests that heparin binding may induce nonnative structures at the binding site which could, in turn, lead to activation of ATIII.	Heparin	86-93	serpin family C member 1	Homo sapiens	198-203
1540583-7	1992	The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site.	Heparin	71-78	serpin family C member 1	Homo sapiens	12-17
1540583-7	1992	The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site.	Heparin	71-78	serpin family C member 1	Homo sapiens	62-67
1540583-7	1992	The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site.	Heparin	148-155	serpin family C member 1	Homo sapiens	12-17
1540583-7	1992	The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site.	Heparin	148-155	serpin family C member 1	Homo sapiens	62-67
1546950-0	1992	The N-terminal domain of antithrombin-III is essential for heparin binding and complex-formation with, but not cleavage by, alpha-thrombin.	Heparin	59-66	serpin family C member 1	Homo sapiens	25-41
1546950-14	1992	A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide.	Heparin	87-94	serpin family C member 1	Homo sapiens	20-26
1546950-14	1992	A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide.	Heparin	87-94	serpin family C member 1	Homo sapiens	115-121
1546950-14	1992	A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide.	Heparin	87-94	serpin family C member 1	Homo sapiens	115-121
1546950-14	1992	A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide.	Heparin	146-153	serpin family C member 1	Homo sapiens	20-26
1546950-14	1992	A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide.	Heparin	146-153	serpin family C member 1	Homo sapiens	115-121
1546950-14	1992	A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide.	Heparin	146-153	serpin family C member 1	Homo sapiens	115-121
1546950-16	1992	We conclude therefore that the N-terminal domain of AT-III is essential for both heparin binding and complex-formation with alpha-thrombin, but not for the cleavage of AT-III at its reactive centre by alpha-thrombin.	Heparin	81-88	serpin family C member 1	Homo sapiens	52-58
1636497-6	1992	Type 2 enzyme had an affinity to heparin, and was completely inhibited by anti-rat platelet 14-kDa secretory phospholipase A2.	Heparin	33-40	phospholipase A2 group IB	Rattus norvegicus	109-125
1466276-1	1992	High molecular weight kininogen (HK) or its procoagulant light-chain but not the heavy chain potentiated the heparin enhancement of antithrombin III inactivation of plasma kallikrein and factor XIa from 10-50-fold to approximately 1000-fold at I 0.15, pH 7.4, 25 degrees C. This potentiation resulted in antithrombin becoming a predominant inhibitor of kallikrein and factor XIa in heparinized normal but not HK-deficient plasmas.	Heparin	109-116	serpin family C member 1	Homo sapiens	132-148
1466276-1	1992	High molecular weight kininogen (HK) or its procoagulant light-chain but not the heavy chain potentiated the heparin enhancement of antithrombin III inactivation of plasma kallikrein and factor XIa from 10-50-fold to approximately 1000-fold at I 0.15, pH 7.4, 25 degrees C. This potentiation resulted in antithrombin becoming a predominant inhibitor of kallikrein and factor XIa in heparinized normal but not HK-deficient plasmas.	Heparin	109-116	serpin family C member 1	Homo sapiens	132-144
1306684-0	1992	Interaction of heparin-binding EGF-like growth factor (HB-EGF) with the epidermal growth factor receptor: modulation by heparin, heparinase, or synthetic heparin-binding HB-EGF fragments.	Heparin	15-22	heparin binding EGF like growth factor	Homo sapiens	55-61
1306684-0	1992	Interaction of heparin-binding EGF-like growth factor (HB-EGF) with the epidermal growth factor receptor: modulation by heparin, heparinase, or synthetic heparin-binding HB-EGF fragments.	Heparin	15-22	heparin binding EGF like growth factor	Homo sapiens	170-176
1306684-2	1992	The inhibitory effect of HB-EGF on 125I-EGF binding was reversed either in the presence of heparin (but not by chondroitin sulfate) or by pre-treating the cells with heparinase.	Heparin	91-98	heparin binding EGF like growth factor	Homo sapiens	25-31
1306684-4	1992	To map potential regions in the HB-EGF molecule that mediate its heparin-dependent interaction with the EGF receptor, HB-EGF peptides were synthesized that were non-homologous to EGF.	Heparin	65-72	heparin binding EGF like growth factor	Homo sapiens	32-38
1306684-5	1992	Accordingly residues 20-25 and 36-41, but not residues 8-19, of HB-EGF were found to be (i) heparin-binding and (ii) modulators of HB-EGF (but not of EGF) binding to the EGF receptor.	Heparin	92-99	heparin binding EGF like growth factor	Homo sapiens	64-70
1729274-1	1992	Vascular endothelial growth factor (VEGF) is a secreted heparin-binding mitogen; its growth-promoting activity is limited to vascular endothelial cells in vitro and VEGF also stimulates angiogenesis in vivo.	Heparin	56-63	vascular endothelial growth factor A	Rattus norvegicus	0-34
1729274-1	1992	Vascular endothelial growth factor (VEGF) is a secreted heparin-binding mitogen; its growth-promoting activity is limited to vascular endothelial cells in vitro and VEGF also stimulates angiogenesis in vivo.	Heparin	56-63	vascular endothelial growth factor A	Rattus norvegicus	36-40
1309590-2	1992	So that this heparin requirement could be evaluated in the absence of other cell surface molecules, we designed a simple assay based on a genetically engineered soluble form of murine FGF receptor 1 (mFR1) tagged with placental alkaline phosphatase.	Heparin	13-20	aldo-keto reductase family 1, member B8	Mus musculus	200-204
1326098-3	1992	It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM).	Heparin	62-69	serpin family C member 1	Homo sapiens	103-119
1326098-3	1992	It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM).	Heparin	62-69	serpin family C member 1	Homo sapiens	103-115
1839474-4	1991	In rabbits treated with t-PA plus saline, heparin or r-hirudin, an accumulation of 125I-fibrinogen on the thrombi of 52.5 +/- 5.1 micrograms, 49.5 +/- 5.6 micrograms and 23.5 +/- 3.5 micrograms was observed, respectively, the difference between r-hirudin and both saline and heparin being statistically significant (p less than 0.01).	Heparin	275-282	tissue-type plasminogen activator	Oryctolagus cuniculus	24-28
1839474-7	1991	The same doses of t-PA infused with heparin, 0.75 mg/kg, produced 32 +/- 3%, 54 +/- 5% and 78 +/- 6% fibrinolysis, respectively and infused with r-hirudin, 1.25 mg/kg, 38 +/- 3%, 57 +/- 5% and 82 +/- 8%, respectively.	Heparin	36-43	tissue-type plasminogen activator	Oryctolagus cuniculus	18-22
1655283-2	1991	These activities appear to be mediated by a unique 60 kd protein exposed on the T. cruzi surface, which promotes selective adhesion of trypomastigotes to three ECM components: heparin, heparan sulfate, and collagen.	Heparin	176-183	multimerin 1	Homo sapiens	160-163
1918380-5	1991	The reduction was apparent during co-incubations as short as 2 h and as long as 24 h. Heparin, which blocks receptor-mediated binding of lipoproteins, abolished the effect of LpL on apo B output, without causing enzyme inhibition.	Heparin	86-93	lipoprotein lipase	Homo sapiens	175-178
1663665-2	1991	With the help of a combined assay method heparin characterization is made possible using the TAT/XAT quotient under consideration of the simultaneous inhibition of the two serine proteases thrombin and factor Xa by antithrombin III.	Heparin	41-48	serpin family C member 1	Homo sapiens	215-231
1911389-3	1991	Accordingly, the antithrombin was isolated by heparin-Sepharose chromatography: this produced a mixture of normal and variant antithrombin, as the patient was heterozygous for the abnormality.	Heparin	46-53	serpin family C member 1	Homo sapiens	17-29
1783073-1	1991	Heparin and its derivatives inhibit human leucocyte proteinases i.e. elastase and cathepsin G, but do not inhibit porcine pancreatic elastase and Pseudomonas aeruginosa elastase.	Heparin	0-7	cathepsin G	Homo sapiens	82-93
1783073-3	1991	Nevertheless, the inhibitory capacity of the heparin fragment still remains elevated with IC50 = 2.7 x 10(-7) M and still inhibits HLE in its free and adsorbed state to elastin.	Heparin	45-52	elastin	Mus musculus	169-176
1908552-6	1991	In addition, their interaction with petD RNA is highly sensitive to heparin.	Heparin	68-75	cytochrome b6/f complex subunit 4	Spinacia oleracea	36-40
1936107-2	1991	In this regard, heparin-releasable LPL activity was measured in abdominal and femoral adipose tissues of 29 pre-menopausal women.	Heparin	16-23	lipoprotein lipase	Homo sapiens	35-38
2071579-0	1991	Heparin influence on the complex of serum amyloid P component and complement C4b-binding protein.	Heparin	0-7	amyloid P component, serum	Homo sapiens	36-61
2071579-2	1991	this study demonstrated that heparin interacted with SAP in a calcium-dependent manner and prevented formation of the SAP.C4BP complex.	Heparin	29-36	amyloid P component, serum	Homo sapiens	53-56
2071579-2	1991	this study demonstrated that heparin interacted with SAP in a calcium-dependent manner and prevented formation of the SAP.C4BP complex.	Heparin	29-36	amyloid P component, serum	Homo sapiens	118-121
2071579-3	1991	Furthermore, the SAP-heparin interaction interfered with SAP binding to membranes.	Heparin	21-28	amyloid P component, serum	Homo sapiens	17-20
2071579-3	1991	Furthermore, the SAP-heparin interaction interfered with SAP binding to membranes.	Heparin	21-28	amyloid P component, serum	Homo sapiens	57-60
2071579-7	1991	Gel filtration and sucrose density gradient ultracentrifugation suggested that heparin and heparan sulfate produced a dimer of SAP.	Heparin	79-86	amyloid P component, serum	Homo sapiens	127-130
2071579-9	1991	While low molecular weight heparin interacted with SAP and inhibited SAP association with membranes, the SAP dimer was not detected in sucrose density gradient ultracentrifugation studies.	Heparin	27-34	amyloid P component, serum	Homo sapiens	51-54
2071579-9	1991	While low molecular weight heparin interacted with SAP and inhibited SAP association with membranes, the SAP dimer was not detected in sucrose density gradient ultracentrifugation studies.	Heparin	27-34	amyloid P component, serum	Homo sapiens	69-72
2071579-9	1991	While low molecular weight heparin interacted with SAP and inhibited SAP association with membranes, the SAP dimer was not detected in sucrose density gradient ultracentrifugation studies.	Heparin	27-34	amyloid P component, serum	Homo sapiens	69-72
2071579-10	1991	Polybrene prevented the interaction between SAP and heparin in both a purified system and in human serum that was enriched in SAP and heparin.	Heparin	52-59	amyloid P component, serum	Homo sapiens	126-129
2071579-10	1991	Polybrene prevented the interaction between SAP and heparin in both a purified system and in human serum that was enriched in SAP and heparin.	Heparin	134-141	amyloid P component, serum	Homo sapiens	44-47
2071579-13	1991	Dissociation of the SAP.C4BP complex by sulfated polysaccharides such as heparin may be a physiological response that could be important during tissue damage or complement activation.	Heparin	73-80	amyloid P component, serum	Homo sapiens	20-23
1782153-8	1991	Furthermore, Cyr61 appears to bind heparin with high affinity.	Heparin	35-42	cellular communication network factor 1	Homo sapiens	13-18
1646824-3	1991	However, heparin and protein-free dermatan sulfate were able to inhibit endocytosis of decorin in a concentration-dependent manner.	Heparin	9-16	decorin	Homo sapiens	87-94
2029579-1	1991	Antithrombin-III-Hamilton has been shown to be a structural variant of antithrombin-III (AT-III) with normal heparin affinity but impaired protease inhibitory activity.	Heparin	109-116	serpin family C member 1	Homo sapiens	0-16
2029579-1	1991	Antithrombin-III-Hamilton has been shown to be a structural variant of antithrombin-III (AT-III) with normal heparin affinity but impaired protease inhibitory activity.	Heparin	109-116	serpin family C member 1	Homo sapiens	71-87
2029579-1	1991	Antithrombin-III-Hamilton has been shown to be a structural variant of antithrombin-III (AT-III) with normal heparin affinity but impaired protease inhibitory activity.	Heparin	109-116	serpin family C member 1	Homo sapiens	89-95
2029579-4	1991	When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions.	Heparin	62-69	serpin family C member 1	Homo sapiens	5-11
2029579-5	1991	However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone.	Heparin	103-110	serpin family C member 1	Homo sapiens	13-19
2029579-5	1991	However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone.	Heparin	258-265	serpin family C member 1	Homo sapiens	13-19
2029579-6	1991	Under nonreducing conditions this AT-III-Hamilton species had decreased mobility compared with AT-III from the propositus (or normal AT-III) isolated only by heparin-Sepharose chromatography.	Heparin	158-165	serpin family C member 1	Homo sapiens	34-40
2022745-5	1991	The inhibitory potency of heparin was not dependent upon its affinity for antithrombin III, but was molecular weight dependent: homogeneous preparations of lower molecular weight were less inhibitory.	Heparin	26-33	serpin family C member 1	Homo sapiens	74-90
2016290-7	1991	Chromatography on antithrombin III-Sepharose gel indicated that the structural change involved in ST heparin resulted in an obvious increase in the ability to bind antithrombin III.	Heparin	101-108	serpin family C member 1	Homo sapiens	18-34
2016290-7	1991	Chromatography on antithrombin III-Sepharose gel indicated that the structural change involved in ST heparin resulted in an obvious increase in the ability to bind antithrombin III.	Heparin	101-108	serpin family C member 1	Homo sapiens	164-180
2007588-0	1991	Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction.	Heparin	70-77	serpin family C member 1	Homo sapiens	98-110
2007588-2	1991	Heparin has been shown to accelerate the inactivation of alpha-thrombin by antithrombin III (AT) by promoting the initial encounter of proteinase and inhibitor in a ternary thrombin-AT-heparin complex.	Heparin	0-7	serpin family C member 1	Homo sapiens	75-91
1930634-4	1991	The primary structures of bovine and human ATIII were compared: all the residues required for the integrity of the heparin-binding domain are strictly conserved.	Heparin	115-122	serpin family C member 1	Homo sapiens	43-48
1861674-5	1991	Of these, the intrinsic heparin-sensitive PK-N2 as compared with heparin-insensitive PK-N1 appeared to be the predominant protein kinase engaged in phosphorylation of NHPs in intact nuclei.	Heparin	24-31	protein kinase N2	Rattus norvegicus	42-47
1999418-7	1991	For example, interactions of the sulfate monoanion are important for the binding of heparin, a sulfated glycosaminoglycan, to antithrombin III.	Heparin	84-91	serpin family C member 1	Homo sapiens	126-142
1998643-3	1991	In the presence of 10% fetal calf serum (FCS), heparin-treated primary and passage 5 SMCs showed a decrease of proliferation and an increase of alpha-SM actin (measured by Western blots or two-dimensional gel electrophoresis) compared with untreated SMCs.	Heparin	47-54	actin gamma 2, smooth muscle	Rattus norvegicus	150-158
1998643-6	1991	SMCs cultured in the presence of 10% FCS plus heparin had the same level of proliferation as SMCs cultured in 5% FCS but had a higher content of alpha-SM actin.	Heparin	46-53	actin gamma 2, smooth muscle	Rattus norvegicus	151-159
1780907-1	1991	Affinity chromatography on heparin-Sepharose has been widely used for the purification of post-heparin plasma triglyceride lipases, but this procedure alone yields lipase fractions with a high content of antithrombin III (AT), which also binds to heparin and coelutes with the lipases.	Heparin	27-34	serpin family C member 1	Homo sapiens	204-220
2055603-4	1991	Addition of heparin accelerated the inactivation of purified C1-s by C1 inhibitor up to 25-fold but increased the inactivation of intact C1- only about 5-fold.	Heparin	12-19	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	61-64
2033902-5	1991	Hematological examinations concerning coagulation and fibrinolysis remained within a normal range except for the serum concentration of antithrombin III (AT III) and its functional property with regard to the heparin cofactor, which were 8.8 mg/dl and 48%, respectively.	Heparin	209-216	serpin family C member 1	Homo sapiens	136-152
1703436-9	1991	This is shown by (i) quenching of thrombin activity of PAI-1 in the presence of heparin and (ii) induction of the formation of SDS-stable complexes between thrombin and PAI-1 by heparin.	Heparin	178-185	serpin family E member 1	Homo sapiens	169-174
1704799-5	1991	Reaction of alpha 2M with thrombin or trypsin reduced the binding of 125I-TGF-beta 1 and 125I-TGF-beta 2; the resulting complexes were readily dissociated by heparin.	Heparin	158-165	alpha-2-macroglobulin	Homo sapiens	12-20
1704799-6	1991	Complexes between TGF-beta 2 and native or reacted forms of alpha 2M were less dissociable by heparin than the equivalent complexes with TGF-beta 1.	Heparin	94-101	alpha-2-macroglobulin	Homo sapiens	60-68
2007184-5	1991	Instead, S115 cells growth without testosterone showed epithelial morphology and binding to the heparin-binding domain of FN, suggesting an alteration of syndecan expression in hormone-treated S115 cells.	Heparin	96-103	fibronectin 1	Mus musculus	122-124
1685979-6	1991	After heparin affinity chromatography, two of these polypeptides strongly cross-reacted with an antibody that recognizes Alzheimer beta-amyloid precursor protein.	Heparin	6-13	amyloid beta (A4) precursor protein	Mus musculus	131-161
1665467-2	1991	We define a standard independent unit (SIU) of heparin as that amount that, in plasma containing 1 mumol of ATIII, raises the (pseudo-)first-order breakdown constant of factor Xa by 1 min-1.	Heparin	47-54	serpin family C member 1	Homo sapiens	108-113
1366314-4	1991	The index of biologic activity of Antithrombin III was significantly decreased after giving heparin to the patients with chronic renal failure on hemodialysis.	Heparin	92-99	serpin family C member 1	Homo sapiens	34-50
2268349-5	1990	CKII-DNA interaction was stimulated in the presence of a polyamine and inhibited by heparin.	Heparin	84-91	casein kinase 2 alpha 1	Homo sapiens	0-4
1701177-7	1990	Furthermore, EMR1a/212D recognized rabbit vitronectin purified by heparin-affinity chromatography.	Heparin	66-73	vitronectin	Oryctolagus cuniculus	42-53
2133241-4	1990	Two of the MAbs (11 and 16) inhibited heparin cofactor but not AT III progressive activity, and the binding of AT III to MAb 11, used for the IRMA, was blocked by heparin.	Heparin	163-170	serpin family C member 1	Homo sapiens	111-117
2133241-5	1990	These results indicate that MAb 11 is directed at or near to the heparin binding site, and could therefore be useful in the study of structural aspects of this site in normal and genetically abnormal AT III.	Heparin	65-72	serpin family C member 1	Homo sapiens	200-206
2122919-0	1990	Effects of therapeutic doses of heparin on thrombolysis with tissue-type plasminogen activator in rabbits.	Heparin	32-39	tissue-type plasminogen activator	Oryctolagus cuniculus	61-94
2122919-1	1990	The objective of the study was to evaluate the ability of heparin to enhance the thrombolytic effect of recombinant tissue type plasminogen activator (rt-PA) and to prevent thrombus growth during and after thrombolysis with rt-PA.	Heparin	58-65	tissue-type plasminogen activator	Oryctolagus cuniculus	116-149
2229057-8	1990	We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction.	Heparin	178-185	serpin family C member 1	Homo sapiens	212-217
1977621-1	1990	Antithrombin Dublin is an electrophoretically fast variant of antithrombin which has normal heparin affinity.	Heparin	92-99	serpin family C member 1	Homo sapiens	0-12
1977621-1	1990	Antithrombin Dublin is an electrophoretically fast variant of antithrombin which has normal heparin affinity.	Heparin	92-99	serpin family C member 1	Homo sapiens	62-74
2121673-2	1990	CS1 peptide which is present within type III homology connecting segment (IIICS) as well as C-274 (cell-binding domain) were able to inhibit experimental lung metastasis when co-injected intravenously (iv) with B16-BL6 melanoma cells, while H-271 (heparin-binding domain) could not.	Heparin	248-255	ITPR interacting domain containing 2	Mus musculus	0-3
2271570-2	1990	The interaction between ATIII and thrombin is enhanced several thousandfold by the glycosaminoglycan, heparin.	Heparin	102-109	serpin family C member 1	Homo sapiens	24-29
2271570-3	1990	We have previously proposed that the heparin binding site of ATIII resides within a region extending from amino acid residues 114-156 [Smith, J. W., &amp; Knauer, D. J.	Heparin	37-44	serpin family C member 1	Homo sapiens	61-66
2271570-9	1990	Affinity-purified IgG from these antisera, as well as monovalent Fab"s derived from them, specifically blocked the binding of heparin to ATIII.	Heparin	126-133	FA complementation group B	Homo sapiens	65-68
2271570-9	1990	Affinity-purified IgG from these antisera, as well as monovalent Fab"s derived from them, specifically blocked the binding of heparin to ATIII.	Heparin	126-133	serpin family C member 1	Homo sapiens	137-142
2271570-10	1990	Additionally, occupancy of the heparin binding site by these same monovalent and bivalent IgG"s at least partially substituted for heparin, accelerating linkage formation between ATIII and thrombin.	Heparin	31-38	serpin family C member 1	Homo sapiens	179-184
2271570-10	1990	Additionally, occupancy of the heparin binding site by these same monovalent and bivalent IgG"s at least partially substituted for heparin, accelerating linkage formation between ATIII and thrombin.	Heparin	131-138	serpin family C member 1	Homo sapiens	179-184
2271570-11	1990	These results provide the first immunological evidence that region 124-145 is directly involved in the binding of heparin to ATIII and that an antibody-induced conformational change within this region can mediate ATIII activation.	Heparin	114-121	serpin family C member 1	Homo sapiens	125-130
2271570-11	1990	These results provide the first immunological evidence that region 124-145 is directly involved in the binding of heparin to ATIII and that an antibody-induced conformational change within this region can mediate ATIII activation.	Heparin	114-121	serpin family C member 1	Homo sapiens	213-218
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	13-20	serpin family C member 1	Homo sapiens	112-117
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	13-20	serpin family C member 1	Homo sapiens	187-192
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	148-155	serpin family C member 1	Homo sapiens	112-117
2264021-5	1990	By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII.	Heparin	148-155	serpin family C member 1	Homo sapiens	187-192
2228409-6	1990	The activity of adipose tissue lipoprotein lipase (LPL) released with heparin was also measured.	Heparin	70-77	lipoprotein lipase	Homo sapiens	31-49
2228409-6	1990	The activity of adipose tissue lipoprotein lipase (LPL) released with heparin was also measured.	Heparin	70-77	lipoprotein lipase	Homo sapiens	51-54
2390061-2	1990	We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities.	Heparin	178-185	serpin family C member 1	Homo sapiens	57-63
2126464-4	1990	The biological activity of antithrombin III is mediated by a polysaccharide, heparin.	Heparin	77-84	serpin family C member 1	Homo sapiens	27-43
2384594-10	1990	These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin.	Heparin	95-102	serpin family C member 1	Homo sapiens	272-288
2237824-3	1990	This paper reports on the effect of a series of high-affinity heparin fractions with decreasing affinity for ATIII.	Heparin	62-69	serpin family C member 1	Homo sapiens	109-114
2237824-4	1990	As affinity decreased, the ability of the heparin fractions to increase the rate of the ATIII-thrombin reactions decreased, and these fractions slightly more effectively increased the rate of thrombin inhibition by the higher-affinity ATIII isoform.	Heparin	42-49	serpin family C member 1	Homo sapiens	88-93
2237824-4	1990	As affinity decreased, the ability of the heparin fractions to increase the rate of the ATIII-thrombin reactions decreased, and these fractions slightly more effectively increased the rate of thrombin inhibition by the higher-affinity ATIII isoform.	Heparin	42-49	serpin family C member 1	Homo sapiens	235-240
2237824-5	1990	The effect of the heparin fractions on the ATIII-factor Xa reactions was also investigated.	Heparin	18-25	serpin family C member 1	Homo sapiens	43-48
2237824-7	1990	Studies on the competition of isoforms for immobilized heparin showed that the isoform with higher affinity for ATIII effectively competes with its congener for binding to heparin.	Heparin	55-62	serpin family C member 1	Homo sapiens	112-117
2237824-7	1990	Studies on the competition of isoforms for immobilized heparin showed that the isoform with higher affinity for ATIII effectively competes with its congener for binding to heparin.	Heparin	172-179	serpin family C member 1	Homo sapiens	112-117
2237824-8	1990	The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions.	Heparin	57-64	serpin family C member 1	Homo sapiens	106-111
2237824-8	1990	The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions.	Heparin	57-64	serpin family C member 1	Homo sapiens	191-196
2237824-8	1990	The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions.	Heparin	169-176	serpin family C member 1	Homo sapiens	106-111
2237824-8	1990	The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions.	Heparin	169-176	serpin family C member 1	Homo sapiens	191-196
2237824-9	1990	In spite of about equal activation of the ATIII isoforms by high-affinity heparin, the importance of the higher-affinity isoform is indicated by its ability to compete effectively for these heparin species.	Heparin	74-81	serpin family C member 1	Homo sapiens	42-47
2373692-2	1990	Following proteolytic digestion with thermolysin, an intact fragment of the laminin A chain carboxyl-terminal domain exhibiting sulfatide-binding activity was isolated using gel filtration and heparin affinity chromatography.	Heparin	193-200	laminin subunit alpha 1	Homo sapiens	76-91
2078567-8	1990	Mutant NCAM polypeptides purified from transfected cell lines have substantially reduced binding to heparin and fail to promote chick retinal cell attachment.	Heparin	100-107	neural cell adhesion molecule 1	Gallus gallus	7-11
2365065-2	1990	A variant antithrombin with reduced heparin affinity was shown by mass spectrometry sequencing and DNA amplification to have a substitution of a cysteine for an arginine at residue 24.	Heparin	36-43	serpin family C member 1	Homo sapiens	10-22
2372510-3	1990	The abnormal AT III was purified from the propositus" plasma, taking advantage of the difference in NaCl concentrations required to elute variant and normal AT III from heparin-Sepharose.	Heparin	169-176	serpin family C member 1	Homo sapiens	13-19
2372510-7	1990	The quantification of heparin AT III interaction with both normal and variant purified proteins in a double reciprocal plot yielded similar dissociation constants but a 9-fold decrease in the maximal pseudo-first order constant.	Heparin	22-29	serpin family C member 1	Homo sapiens	30-36
2164263-3	1990	Using this assay we have estimated the relative potency of the following glycosaminoglycans: heparin; a fraction of heparin with high affinity for antithrombin III (high affinity heparin); the low molecular weight heparin Fragmin; the low molecular weight heparinoid Org 10172; a fraction of Org 10172 with high affinity for antithrombin III (high affinity Org 10172) and the O-methyl derivative of the pentasaccharide, representing the minimal structure required for binding to antithrombin III.	Heparin	116-123	serpin family C member 1	Homo sapiens	147-163
2383300-1	1990	Heparin sodium was assayed by turbidimetric measurement of the clotting time of bovine citrate plasma with thromboplastin, between the moment of recalcification and the moment of maximal speed of polymerization of the fibrinogen monomer, as marked by the turning-point of the trace of the turbidimetric record.	Heparin	0-14	coagulation factor III, tissue factor	Bos taurus	107-121
2324746-1	1990	Chicken muscle and retina, and rat muscle asymmetric acetylcholinesterase (AChE) species were bound to immobilized heparin at 0.4 M NaCl.	Heparin	115-122	acetylcholinesterase	Rattus norvegicus	75-79
1699396-3	1990	Vitronectin was purified from rabbit serum by heparin-Sepharose affinity chromatography and autoclaved at 121 degrees C for 20 min after adjusting the concentration to 0.2 mg/ml with saline.	Heparin	46-53	vitronectin	Oryctolagus cuniculus	0-11
2354155-6	1990	Like cholesterol esterase, the enzyme binds to immobilized heparin, and this property was critical for its purification to homogeneity.	Heparin	59-66	carboxyl ester lipase	Homo sapiens	5-25
2179409-5	1990	Dextran sulfate, like heparin, stabilizes the catalytic activity and quaternary structure of tryptase and also maintains the native secondary structure of the enzyme at and beyond a temperature of 40 degrees C. Dextran sulfate-stabilized tryptase therefore was used as an immunogen to which were produced three murine mAb (B2, C11, and G4) recognizing the catalytically active form of the enzyme.	Heparin	22-29	tryptase alpha/beta 1	Mus musculus	93-101
2179409-9	1990	A pragmatic result of these newly generated antibodies is the affinity purification to homogeneity of active tryptase by sequential chromatography with B2 coupled to CH-Sepharose and heparin-agarose.	Heparin	183-190	tryptase alpha/beta 1	Mus musculus	109-117
2354485-6	1990	Lipoprotein lipase activity in heparin-treated plasma was significantly higher after pindolol administration.	Heparin	31-38	lipoprotein lipase	Homo sapiens	0-18
2156335-4	1990	The in vivo release of LPL activity was greater with heparin in both species.	Heparin	53-60	lipoprotein lipase	Homo sapiens	23-26
2156335-6	1990	In the in vitro studies the LMWH fragment consistently released more LPL activity from the tissues investigated, i.e. fat, skeletal muscle and heart muscle.	Heparin	28-32	lipoprotein lipase	Homo sapiens	69-72
2302223-4	1990	The affinities of human recombinant IGF I and II were compared with those of apolipoprotein H (a plasma heparin-binding protein) and bovine insulin in a heparin-affinity column.	Heparin	104-111	apolipoprotein H	Homo sapiens	77-93
1963017-2	1990	In the intrinsic system, unfractionated heparin does have an indirect antiprothrombinase action because its antithrombin activity inhibits the feedback activation of Factor VIII.	Heparin	40-47	serpin family C member 1	Homo sapiens	108-120
1963018-1	1990	When measured in terms of biological activities (using only markers of molecules with affinity for antithrombin III), the pharmacokinetics of low molecular weight heparins are clearly different from those of unfractionated heparin after intravenous and subcutaneous injections.	Heparin	163-171	serpin family C member 1	Homo sapiens	99-115
1963018-1	1990	When measured in terms of biological activities (using only markers of molecules with affinity for antithrombin III), the pharmacokinetics of low molecular weight heparins are clearly different from those of unfractionated heparin after intravenous and subcutaneous injections.	Heparin	163-170	serpin family C member 1	Homo sapiens	99-115
1688695-7	1990	Third, based on the knowledge that tryptase stability is regulated by its interaction with heparin, antithrombin III was used as a model heparin-binding protein to demonstrate that a protein competitor for heparin-binding sites, presumably by displacement of tryptase, destabilizes this enzyme.	Heparin	91-98	serpin family C member 1	Homo sapiens	100-116
1688695-7	1990	Third, based on the knowledge that tryptase stability is regulated by its interaction with heparin, antithrombin III was used as a model heparin-binding protein to demonstrate that a protein competitor for heparin-binding sites, presumably by displacement of tryptase, destabilizes this enzyme.	Heparin	137-144	serpin family C member 1	Homo sapiens	100-116
1688695-8	1990	Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III.	Heparin	76-83	serpin family C member 1	Homo sapiens	56-72
1688695-8	1990	Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III.	Heparin	76-83	serpin family C member 1	Homo sapiens	152-168
1688695-8	1990	Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III.	Heparin	109-116	serpin family C member 1	Homo sapiens	56-72
1688695-8	1990	Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III.	Heparin	109-116	serpin family C member 1	Homo sapiens	152-168
2322419-4	1990	Thus, the slow reactions in the case of bovine and pig HA-heparins were probably due to preferential binding of the two HA-heparins to thrombin rather than to ATIII, thus causing the HA-heparins to be inhibitory for the reaction by reducing the turnover rates of the polysaccharides as catalysts.	Heparin	58-66	serpin family C member 1	Homo sapiens	159-164
2322419-6	1990	Since the strength of the interactions of these HA-heparins with thrombin was in the order, pig greater than or equal to bovine greater than whale, the faster reactions were probably due to higher associations of the enzyme with the essential HA-heparin-ATIII complex.	Heparin	51-59	serpin family C member 1	Homo sapiens	254-259
1697824-9	1990	The present results indicate that low-dose heparin treatment modulates the plasmatic fluctuation of TAT complex as well as factor X, AT III and protein C levels in patients with acute myocardial infarction.	Heparin	43-50	serpin family C member 1	Homo sapiens	133-139
2298818-10	1990	The plasma thrombin inhibitor, antithrombin III, stimulated neurite outgrowth but only when its thrombin inhibitory activity was accelerated by heparin.	Heparin	144-151	serpin family C member 1	Homo sapiens	31-47
1724191-5	1990	With UFH 5 patients (5%) demonstrated a positive uptake (3 patients with HES).	Heparin	5-8	ribosome binding protein 1	Homo sapiens	73-76
1983502-1	1990	Heparin exerts its anticoagulant function by accelerating the inhibitory effect of antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	83-99
2154059-4	1990	The intensity of ATIII activity in the presence of heparin (0.01U/ml) was also diminished by the human TM.	Heparin	51-58	serpin family C member 1	Homo sapiens	17-22
2154059-4	1990	The intensity of ATIII activity in the presence of heparin (0.01U/ml) was also diminished by the human TM.	Heparin	51-58	thrombomodulin	Homo sapiens	103-105
2154059-5	1990	However, this ATIII- heparin cofactor activity recovered with the addition of a 10-fold amount of heparin (0.1U/ml).	Heparin	21-28	serpin family C member 1	Homo sapiens	14-19
33806140-3	2021	We evaluated the diagnostic performance of a functional flow cytometric assay (FCA) based on the detection of heparin-dependent platelet activation with an anti-p-selectin.	Heparin	110-117	selectin P	Homo sapiens	161-171
34610468-0	2022	Heparin binding triggers human VLDL remodeling by circulating lipoprotein lipase: Relevance to VLDL functionality in health and disease.	Heparin	0-7	lipoprotein lipase	Homo sapiens	62-80
34937572-13	2021	Genetic analyses showed the same mutation causing ATD in both son and mother: heterozygote missense mutation c.248 T > C, p.(Leu83Pro), within the heparin binding domain of antithrombin.	Heparin	147-154	serpin family C member 1	Homo sapiens	173-185
34743814-4	2021	Herein, we found that the S protein can competitively inhibit the bindings of antithrombin and heparin cofactor II to heparin/HS, causing abnormal increase in thrombin activity.	Heparin	118-125	serpin family C member 1	Homo sapiens	78-90
34887403-7	2021	Heparin can bind to both HHIP-N and HHIP-C, thereby inducing clustering at the cell surface and generating a high-avidity platform for SHH sequestration and inhibition.	Heparin	0-7	sonic hedgehog signaling molecule	Homo sapiens	135-138
34261860-0	2021	P-selectin expression assay in a repeatedly serotonin-release assay-negative patient with heparin-induced thrombocytopenia.	Heparin	90-97	selectin P	Homo sapiens	0-10
34494046-0	2021	Heparin remodels the microtubule-binding repeat R3 of Tau protein towards fibril-prone conformations.	Heparin	0-7	microtubule associated protein tau	Homo sapiens	54-57
34553121-0	2021	Low ADAMTS-13 predicts adverse outcomes in hospitalized patients with suspected heparin-induced thrombocytopenia.	Heparin	80-87	ADAM metallopeptidase with thrombospondin type 1 motif 13	Homo sapiens	4-13
34368018-5	2021	Methods: For the experiments LDN-193189 and oversulfated heparins were used, which interact with the BMP6-SMAD pathway thereby inhibiting hepcidin expression.	Heparin	57-65	bone morphogenetic protein 6	Mus musculus	101-105
34193922-4	2021	Here we describe a chromatographic method to isolate recombinant soluble tau seeds derived from heparin treatment.	Heparin	96-103	microtubule associated protein tau	Homo sapiens	73-76
34112123-1	2021	BACKGROUND: Glypican 3 (GPC3) is a heparin sulphate proteoglycan whose expression is associated with several malignancies.	Heparin	35-42	glypican 3	Homo sapiens	12-22
34112123-1	2021	BACKGROUND: Glypican 3 (GPC3) is a heparin sulphate proteoglycan whose expression is associated with several malignancies.	Heparin	35-42	glypican 3	Homo sapiens	24-28
34061194-7	2021	CONCLUSIONS: Risk factors for heparin resistance include antithrombin deficiency, elevation of factor VIII or fibrinogen level, elevation in heparin-binding proteins, increased heparin clearance, sepsis, trauma, and burns.	Heparin	30-37	serpin family C member 1	Homo sapiens	57-69
34381596-7	2021	Unique spectral markers were identified for tau fibrils generated using heparin or RNA cofactors, as well as for phosphorylated tau.	Heparin	72-79	microtubule associated protein tau	Homo sapiens	44-47
34513063-6	2021	Results: The greatest sensitivity was revealed when using heparin-binding growth factor, annexin A2, osteopontin.	Heparin	58-65	secreted phosphoprotein 1	Homo sapiens	101-112
35609633-6	2022	At the molecular level, nord encodes a secreted heparin-binding protein, and we show that its overexpression is sufficient to antagonize Dpp/BMP signaling.	Heparin	48-55	decapentaplegic	Drosophila melanogaster	137-140
35609633-6	2022	At the molecular level, nord encodes a secreted heparin-binding protein, and we show that its overexpression is sufficient to antagonize Dpp/BMP signaling.	Heparin	48-55	decapentaplegic	Drosophila melanogaster	141-144
35124550-5	2022	The two other methods, direct grafting on aldehyde preactivated monoliths and immobilization of biotinylated antithrombin III to streptavidin-functionalized columns, require the presence of fondaparinux to protect the heparin binding site during the grafting process.	Heparin	218-225	serpin family C member 1	Homo sapiens	109-125
35016968-5	2022	Ubiquitin conjugation at specific sites weakened multivalent tau/RNA interactions and disfavored tau/heparin condensation.	Heparin	101-108	microtubule associated protein tau	Homo sapiens	97-100
35281253-4	2022	Using 2D-NMR analysis and molecular modelling, the binding motif of heparin oligoaccharides to Abeta was determined to be HexA-GlcNS-IdoA2S-GlcNS6S.	Heparin	68-75	hexosaminidase subunit alpha	Homo sapiens	122-126
35102343-4	2022	This occurs independent of interleukin-22 (IL-22), and we identify that ILC3s are a dominant source of heparin-binding epidermal growth factor-like growth factor (HB-EGF).	Heparin	103-110	heparin binding EGF like growth factor	Homo sapiens	163-169
2572276-10	1989	Furthermore, plasmin(ogen) bound to heparin was protected from alpha 2-antiplasmin inhibition.	Heparin	36-43	serpin family F member 2	Homo sapiens	63-82
2611046-10	1989	By using heparin treated, uncoated AC, elevation of C3a levels and transient neutropenia were suppressed.	Heparin	9-16	complement C3	Homo sapiens	52-55
2613105-2	1989	Both FR-860 and UF-heparin dose-dependently prolonged the recalcification time, activated partial thromboplastin time, prothrombin time, factor Xa (F.Xa) clotting time and thrombin time.	Heparin	19-26	coagulation factor X	Homo sapiens	137-146
2806479-6	1989	These combined results suggest the participation of GP IIb/IIIa but not GP Ib in heparin-induced platelet aggregation.	Heparin	81-88	integrin subunit alpha 2b	Homo sapiens	52-58
2545782-0	1989	Dextran sulfate and heparin interact with CD4 molecules to inhibit the binding of coat protein (gp120) of HIV.	Heparin	20-27	CD4 antigen	Mus musculus	42-45
2545782-1	1989	Dextran sulfate, heparin, and certain other sulfated polysaccharides potently inhibit the adsorption of HIV to CD4+ cells.	Heparin	17-24	CD4 antigen	Mus musculus	111-114
2753911-7	1989	This was shown in cells treated with heparin and cycloheximide to be equal to 1 for LPL antigen but significantly greater than 1 for LPL activity assayed under standard conditions.	Heparin	37-44	lipoprotein lipase	Mus musculus	84-87
2753911-7	1989	This was shown in cells treated with heparin and cycloheximide to be equal to 1 for LPL antigen but significantly greater than 1 for LPL activity assayed under standard conditions.	Heparin	37-44	lipoprotein lipase	Mus musculus	133-136
2753911-11	1989	The existence of an inhibitor of LPL activity has been excluded as well as that of an increase in the catalytic activity of LPL during its secretion, before or after exposure to heparin.	Heparin	178-185	lipoprotein lipase	Mus musculus	124-127
2753912-9	1989	Under heparin stimulation, quantitative secretion of the mature form of LPL takes place whereas the intracellular degradation is arrested.	Heparin	6-13	lipoprotein lipase	Mus musculus	72-75
2753912-10	1989	Heparin is able to mobilize intracellular LPL without changing the rate of LPL export from the endoplasmic reticulum to the cell surface.	Heparin	0-7	lipoprotein lipase	Mus musculus	42-45
2722856-1	1989	Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation.	Heparin	0-7	coagulation factor X	Homo sapiens	180-189
2920417-1	1989	The Heptest kit (Haemachem, Inc., St. Louis, MO) for quantifying heparin in plasma is based on heparin-mediated inhibition of factor Xa, resulting in prolongation of clotting time.	Heparin	65-72	coagulation factor X	Homo sapiens	126-135
2920417-1	1989	The Heptest kit (Haemachem, Inc., St. Louis, MO) for quantifying heparin in plasma is based on heparin-mediated inhibition of factor Xa, resulting in prolongation of clotting time.	Heparin	95-102	coagulation factor X	Homo sapiens	126-135
2914894-1	1989	Platelet factor 4 (PF4), which is released by platelets during coagulation, binds very tightly to negatively charged oligosaccharides such as heparin.	Heparin	142-149	platelet factor 4	Bos taurus	0-17
2914894-1	1989	Platelet factor 4 (PF4), which is released by platelets during coagulation, binds very tightly to negatively charged oligosaccharides such as heparin.	Heparin	142-149	platelet factor 4	Bos taurus	19-22
2465300-4	1989	Under conditions where heparin potentiated aFGF-induced neurite outgrowth, we observed that heparin increased the biological half-life of aFGF from 7 to 39 hr.	Heparin	92-99	fibroblast growth factor 1	Rattus norvegicus	138-142
2465300-6	1989	If aFGF activity was maintained for greater than 25 hr by periodic readdition of factor, heparin no longer potentiated aFGF-induced neurite outgrowth.	Heparin	89-96	fibroblast growth factor 1	Rattus norvegicus	3-7
2465300-7	1989	These observations strongly suggest that heparin potentiates the activity of aFGF by prolonging its biological half-life.	Heparin	41-48	fibroblast growth factor 1	Rattus norvegicus	77-81
2465300-10	1989	These observations suggest that heparin regulates the activity of aFGF by regulating its proteolytic degradation, thereby regulating its biological half-life.	Heparin	32-39	fibroblast growth factor 1	Rattus norvegicus	66-70
2465906-9	1989	These results support recent findings in which the function of S-protein as complement inhibitor was dependent on conformational changes of the protein molecule with concomitant exposure of the heparin-binding domain.	Heparin	194-201	vitronectin	Homo sapiens	63-72
2483705-6	1989	The assay is based on the inactivation of factor Xa by antithrombin III which is catalysed by heparin or smaller fragments of it.	Heparin	94-101	coagulation factor X	Homo sapiens	42-51
2973992-4	1988	From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present.	Heparin	332-339	coagulation factor X	Homo sapiens	186-195
2973992-4	1988	From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present.	Heparin	332-339	coagulation factor X	Homo sapiens	199-213
2849981-7	1988	Analysis of the results indicate that plasma fibrinopeptide A (FPA) levels correlate with anti-factor Xa (r = -0.45) and anti-thrombin (substrate) (r = -0.63) levels of UFH, but only with the anti-factor Xa levels (r = -0.41) of CY222.	Heparin	169-172	coagulation factor X	Homo sapiens	197-206
2849981-8	1988	These results suggest that the anti-factor Xa assay is currently the most suitable assay for monitoring low MW heparins such as CY222 in humans.	Heparin	111-119	coagulation factor X	Homo sapiens	36-45
3272188-3	1988	Heparin strongly potentiates aFGF-dependent neuritic outgrowth but not aFGF-dependent proliferation.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	29-33
2847825-2	1988	Low molecular weight heparin had less affinity to antithrombin III than unfractionated heparin and had less anticoagulant and anti-IIa activities.	Heparin	21-28	serpin family C member 1	Rattus norvegicus	50-66
2847825-5	1988	In the modified model of the arteriovenous shunt thrombosis in normal and nephrotic syndrome rats it was shown that the low molecular weight heparin was the most efficient antithrombotic remedy in normal and decreased level of antithrombin III in the organism.	Heparin	141-148	serpin family C member 1	Rattus norvegicus	227-243
3196315-1	1988	Plasma extracellular superoxide dismutase (EC-SOD) from the pig, cat, rabbit, guinea pig and mouse was found to be heterogeneous with regard to heparin affinity and could be separated into three fractions: A without affinity, B with weak affinity and C with relatively high affinity.	Heparin	144-151	superoxide dismutase 3	Sus scrofa	7-41
3196315-4	1988	Intravenous injection of heparin resulted in the pig, dog, cat, rabbit, guinea pig and mouse in a prompt increase in the plasma SOD activity.	Heparin	25-32	superoxide dismutase 3	Rattus norvegicus	128-131
3196315-7	1988	The relative heparin-induced increase in plasma EC-SOD C varied between 2 and 11 in the different species and was distinctly correlated with the heparin affinity of EC-SOD C in the particular species.	Heparin	13-20	superoxide dismutase 3	Rattus norvegicus	48-54
3196315-7	1988	The relative heparin-induced increase in plasma EC-SOD C varied between 2 and 11 in the different species and was distinctly correlated with the heparin affinity of EC-SOD C in the particular species.	Heparin	13-20	superoxide dismutase 3	Rattus norvegicus	165-171
3196315-7	1988	The relative heparin-induced increase in plasma EC-SOD C varied between 2 and 11 in the different species and was distinctly correlated with the heparin affinity of EC-SOD C in the particular species.	Heparin	145-152	superoxide dismutase 3	Rattus norvegicus	48-54
3196315-7	1988	The relative heparin-induced increase in plasma EC-SOD C varied between 2 and 11 in the different species and was distinctly correlated with the heparin affinity of EC-SOD C in the particular species.	Heparin	145-152	superoxide dismutase 3	Rattus norvegicus	165-171
3260474-11	1988	Addition of heparin to 20 U/mL decreased ng/mL C3a generated from 10,872 to 913 and C5a from 200 to 8.	Heparin	12-19	complement C3	Homo sapiens	47-50
2836066-4	1988	The 0.5 M KCI eluates from a heparin-Sepharose column were applied to a DNA affinity column of synthetic oligonucleotides of the octamer sequence and the sequence TATTTTAGGAAGCAAA in the HpaII-BgIII region of the HIG1 gene enhancer.	Heparin	29-36	HIG1 hypoxia inducible domain family member 1A pseudogene 1	Homo sapiens	213-217
3396757-4	1988	MGSA was eluted from the heparin-Sepharose resin with 0.1-0.3 M NaCl.	Heparin	25-32	C-X-C motif chemokine ligand 1	Homo sapiens	0-4
3396757-8	1988	This bioactivity was progressively inactivated during storage at -80 degrees C. These results indicate that the combination of heparin-Sepharose chromatography and reverse phase-HPLC provides a more efficient means of purification of MGSA.	Heparin	127-134	C-X-C motif chemokine ligand 1	Homo sapiens	234-238
3382640-4	1988	The cleavage of aFGF by thrombin is inhibited by heparin (50 micrograms/mL) and is completely blocked by the irreversible thrombin inhibitors D-Phe-Pro-Arg chloromethyl ketone and hirudin.	Heparin	49-56	coagulation factor II, thrombin	Bos taurus	24-32
3181034-6	1988	The chick MIF seemed somewhat heterogeneous by chromatofocusing and a portion of its activity bound to heparin sepharose.	Heparin	103-110	macrophage migration inhibitory factor (glycosylation-inhibiting factor)	Gallus gallus	10-13
2449171-0	1987	The autoactivation of factor XII (Hageman factor) induced by low-Mr heparin and dextran sulphate.	Heparin	68-75	coagulation factor XII	Homo sapiens	34-48
2449172-12	1987	The mast cell proteoglycans heparin and chondroitin sulphate E, by virtue of containing the naturally occurring glycosaminoglycans of highest negative charge density, may play a major role in the regulation of mast cell tryptase activity in vivo.	Heparin	28-35	tryptase delta 1	Homo sapiens	210-228
2445746-11	1987	Furthermore, the results suggest that S protein/vitronectin may be a physiologically important modulator of the anticoagulant activity of heparin-like material on or near the vascular endothelium.	Heparin	138-145	vitronectin	Homo sapiens	38-47
2445746-11	1987	Furthermore, the results suggest that S protein/vitronectin may be a physiologically important modulator of the anticoagulant activity of heparin-like material on or near the vascular endothelium.	Heparin	138-145	vitronectin	Homo sapiens	48-59
2442161-0	1987	Neutralization and binding of heparin by S protein/vitronectin in the inhibition of factor Xa by antithrombin III.	Heparin	30-37	vitronectin	Homo sapiens	41-50
2442161-0	1987	Neutralization and binding of heparin by S protein/vitronectin in the inhibition of factor Xa by antithrombin III.	Heparin	30-37	vitronectin	Homo sapiens	51-62
2442161-0	1987	Neutralization and binding of heparin by S protein/vitronectin in the inhibition of factor Xa by antithrombin III.	Heparin	30-37	coagulation factor X	Homo sapiens	84-93
2442161-2	1987	The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system.	Heparin	24-31	vitronectin	Homo sapiens	62-71
2442161-2	1987	The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system.	Heparin	24-31	vitronectin	Homo sapiens	73-84
2442161-2	1987	The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system.	Heparin	105-112	vitronectin	Homo sapiens	62-71
2442161-2	1987	The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system.	Heparin	105-112	vitronectin	Homo sapiens	73-84
2442161-2	1987	The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system.	Heparin	105-112	coagulation factor X	Homo sapiens	149-158
2442161-4	1987	Using purified components in the presence of heparin, S protein induced a concentration-dependent reduction of the inhibition rate of factor Xa by antithrombin III.	Heparin	45-52	vitronectin	Homo sapiens	54-63
2442161-4	1987	Using purified components in the presence of heparin, S protein induced a concentration-dependent reduction of the inhibition rate of factor Xa by antithrombin III.	Heparin	45-52	coagulation factor X	Homo sapiens	134-143
2442161-6	1987	S protein not only counteracted the anticoagulant activity of commercial heparin but also of low molecular weight forms of heparin (mean Mr of 4,500).	Heparin	73-80	vitronectin	Homo sapiens	0-9
2442161-7	1987	The heparin-neutralizing activity of S protein was found to be mainly expressed in the range 0.2-10 micrograms/ml of high Mr as well as low Mr heparin.	Heparin	4-11	vitronectin	Homo sapiens	37-46
2442161-7	1987	The heparin-neutralizing activity of S protein was found to be mainly expressed in the range 0.2-10 micrograms/ml of high Mr as well as low Mr heparin.	Heparin	143-150	vitronectin	Homo sapiens	37-46
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	70-77	vitronectin	Homo sapiens	83-92
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	70-77	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	70-77	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	70-77	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	145-152	vitronectin	Homo sapiens	83-92
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	83-92
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	83-92
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	198-207
2442161-9	1987	As deduced from dot-blot analysis, direct interaction of radiolabeled heparin with S protein revealed a dissociation constant KD = 4 X 10(-8) M. Heparin binding as well as heparin neutralization by S protein increased significantly when reduced/carboxymethylated or guanidine-treated S protein was employed indicating the existence of a partly buried heparin-binding domain in native S protein.	Heparin	172-179	vitronectin	Homo sapiens	198-207
2442161-12	1987	These data provide evidence that the heparin-binding domain of S protein appears to be unique in binding to heparin and thereby neutralizing its anticoagulant activity in the inhibition of coagulation factors by antithrombin III.	Heparin	37-44	vitronectin	Homo sapiens	63-72
2442161-13	1987	The induction of heparin binding and neutralization may be considered a possible physiological mechanism initiated by conformational alteration of the S protein molecule.	Heparin	17-24	vitronectin	Homo sapiens	151-160
2440809-6	1987	Likewise, unlabeled human fibronectin and heparin inhibited the binding of labeled S protein to group G streptococci, S. aureus, and E. coli, but did not influence the binding to group A and C streptococci.	Heparin	42-49	vitronectin	Homo sapiens	83-92
3311146-4	1987	CKI-1 and CKI-2 correspond to mammalian type I casein kinase, because they bind to CM-Sephadex, they are monomeric enzymes of molecular weights below 50,000, they accept ATP exclusively (CKI-1) or predominantly (CKI-2) as phosphate donor, and they are either completely or relatively heparin insensitive.	Heparin	284-291	serine/threonine protein kinase YCK1	Saccharomyces cerevisiae S288C	10-15
3116701-4	1987	Increasing concentrations of heparin (greater than 0.066 micrograms/mL or 0.01 USP units/mL) and dermatan sulfate (greater than 0.1 micrograms/mL) could be readily demonstrated in undiluted plasma by enhanced formation of complexes of thrombin with antithrombin III and heparin cofactor II respectively.	Heparin	29-36	prothrombin	Oryctolagus cuniculus	235-243
3116701-4	1987	Increasing concentrations of heparin (greater than 0.066 micrograms/mL or 0.01 USP units/mL) and dermatan sulfate (greater than 0.1 micrograms/mL) could be readily demonstrated in undiluted plasma by enhanced formation of complexes of thrombin with antithrombin III and heparin cofactor II respectively.	Heparin	29-36	heparin cofactor 2	Oryctolagus cuniculus	270-289
3617870-3	1987	The dose of the low molecular weight heparin ranged individually from 2,500 to 12,000 units once a day subcutaneously and was adjusted on the basis of the general bleeding tendency of the patient and the specific anticoagulant effect on factor Xa.	Heparin	37-44	coagulation factor X	Homo sapiens	237-246
2443128-1	1987	Heparin catalyses the inhibition of two key enzymes of blood coagulation, namely Factor Xa and thrombin, by enhancing the antiproteinase activities of plasma antithrombin III and heparin cofactor II.	Heparin	0-7	coagulation factor X	Homo sapiens	81-90
3606581-0	1987	The effect of Ca2+, phospholipid and factor V on the anti-(factor Xa) activity of heparin and its high-affinity oligosaccharides.	Heparin	82-89	coagulation factor X	Homo sapiens	59-68
3606581-6	1987	These results indicate that in the presence of Ca2+/phospholipid/Factor V optimum inhibition of Factor Xa requires a saccharide sequence of heparin additional to that involved in binding to antithrombin III.	Heparin	140-147	coagulation factor X	Homo sapiens	96-105
3606581-7	1987	The use of free enzyme for the assessment of anti-(Factor Xa) activity of low-Mr heparin fractions could give misleading results.	Heparin	81-88	coagulation factor X	Homo sapiens	51-60
3590093-1	1987	The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III).	Heparin	22-29	coagulation factor X	Homo sapiens	169-178
3590093-4	1987	However, after isolation of the reaction products, both thrombin and prothrombin fragment 1.2 exhibited heparin neutralizing properties in the factor Xa inactivation reaction.	Heparin	104-111	coagulation factor X	Homo sapiens	143-152
3590093-6	1987	Prothrombin fragment 1, when present at 125 nM, caused a 50% reduction of the heparin-dependent rate of inactivation of factor Xa and prothrombin fragment 2 had no effect at all.	Heparin	78-85	coagulation factor X	Homo sapiens	120-129
3590084-3	1987	Rapid inactivation of cell-bound thrombin by antithrombin III (ATIII) accelerated by heparin-like structures represents another anticoagulant mechanism.	Heparin	85-92	coagulation factor II, thrombin	Bos taurus	33-41
3590084-9	1987	However, heparin added to the reaction mixture substantially increased the inactivation of cell-bound thrombin.	Heparin	9-16	coagulation factor II, thrombin	Bos taurus	102-110
3428717-4	1987	At high thrombin doses, tolerated only during additional administration of thrombin inhibitors, heparin leads to increased consumption of antithrombin III, whereas hirudin and the synthetic inhibitor do not.	Heparin	96-103	serpin family C member 1	Rattus norvegicus	138-154
2431720-6	1986	Incubation of the macrophages with heparin caused a marked increase in the secretion of lipoprotein lipase.	Heparin	35-42	lipoprotein lipase	Mus musculus	88-106
2431720-7	1986	Short incubations with heparin (5 min) caused a release of the enzyme into the media, while longer incubations caused a 2-8-fold increase in net lipoprotein lipase secretion which was maximal after 2-16 h depending on cell type, and persisted for 24 h. The effect of heparin was dose-dependent and specific (it was not duplicated by other glycosaminoglycans).	Heparin	267-274	lipoprotein lipase	Mus musculus	145-163
2431720-10	1986	The heparin-induced increase in lipoprotein lipase secretion was dependent on protein synthesis.	Heparin	4-11	lipoprotein lipase	Mus musculus	32-50
2431720-11	1986	The secretion of lipoprotein lipase by macrophages in response to low levels of heparin may be a significant factor in the formation of atherosclerotic lesions.	Heparin	80-87	lipoprotein lipase	Mus musculus	17-35
3798412-6	1986	This suggests that Factor Xa and antithrombin III have similar affinities for this immobilized heparin, unlike the situation for thrombin (Thromb-Res., 20, 543-554, 1980).	Heparin	95-102	coagulation factor X	Homo sapiens	19-28
3828107-5	1986	The activity of lipoprotein lipase accumulated in the heparin-releasable fraction during differentiation was increased 2- to 3-fold and the intracellular enzyme was enhanced 15- to 20-fold by the addition of phenobarbital.	Heparin	54-61	lipoprotein lipase	Mus musculus	16-34
2434472-8	1986	About 12-20% of the vitronectin molecules in plasma were found to bind to heparin-Sepharose under physiological conditions.	Heparin	74-81	vitronectin	Homo sapiens	20-31
2434472-9	1986	Vitronectin in plasma bound 30-fold more efficiently to heparin immobilized by amino groups than by carboxyl groups.	Heparin	56-63	vitronectin	Homo sapiens	0-11
3020033-3	1986	Both the nonoccupied and in vitro occupied forms of the receptors interacted with heparin-Sepharose but with varying strength, as determined by ligand binding assays or an enzyme-linked immunosorbent assay based on a monoclonal antibody against the steroid- and DNA-binding Mr approximately 94,000 glucocorticoid receptor protein.	Heparin	82-89	nuclear receptor subfamily 3, group C, member 1	Rattus norvegicus	298-321
3766461-6	1986	The authors have also studied the effect of the divalent cations (Ca+2, Mg+2, Zn+2, and Sr+2) on the anti-Factor Xa activity of heparin to determine whether the calcium-dependent increase in the aPTT was due to an increase in the anti-Factor Xa activity.	Heparin	128-135	coagulation factor X	Homo sapiens	106-115
3766461-7	1986	The anti-Factor Xa activity of heparin was measured using chromogenic substrate S-2251, purified Factor Xa, and excess antithrombin III.	Heparin	31-38	coagulation factor X	Homo sapiens	9-18
3766461-7	1986	The anti-Factor Xa activity of heparin was measured using chromogenic substrate S-2251, purified Factor Xa, and excess antithrombin III.	Heparin	31-38	coagulation factor X	Homo sapiens	97-106
3766461-12	1986	Furthermore, divalent cations play an important role in regulating the anti-Factor Xa activity of heparin in vitro.	Heparin	98-105	coagulation factor X	Homo sapiens	76-85
2430628-0	1986	[Release of Ca2+ ions from the sarcoplasmic reticulum of skeletal muscle induced by heparin.	Heparin	84-91	carbonic anhydrase 2	Homo sapiens	12-15
3823117-0	1986	[The effect of heparin on the relative myosin content of cultured smooth muscle cells of the pig aorta].	Heparin	15-22	myosin X	Sus scrofa	39-45
3823117-1	1986	Heparin inhibits the proliferation of aortic smooth muscle cells cultured in serum containing culture medium and leads to an increase of their relative myosin content.	Heparin	0-7	myosin X	Sus scrofa	152-158
3823117-3	1986	Thrombin is able to inhibit the increase of myosin content caused by heparin.	Heparin	69-76	myosin X	Sus scrofa	44-50
3754869-4	1986	Functionally, S-protein in the presence of low concentrations of heparin, protects thrombin from inactivation by ATIII.	Heparin	65-72	vitronectin	Homo sapiens	14-23
3754869-9	1986	The protective effect of S-protein on inactivation of thrombin by ATIII was demonstrated in functional assays with purified proteins and in plasma only in the presence of low concentrations of heparin.	Heparin	193-200	vitronectin	Homo sapiens	25-34
3753469-1	1986	Mouse brain ornithine decarboxylase (ODC) was purified to near-homogeneity by using (NH4)2SO4 precipitation and chromatography on heparin-Sepharose, pyridoxamine phosphate-agarose and DEAE-cellulose.	Heparin	130-137	ornithine decarboxylase, structural 1	Mus musculus	37-40
3087006-1	1986	Aggregation of platelets in heparin- and citrate-anticoagulated platelet-rich-plasma (PRP) from rats anesthetized with methoxyflurane (M), diethyl ether (E), acepromazine/ketamine (A/K), or sodium pentobarbital (P) is described, as are platelet counts.	Heparin	28-35	proline rich protein 2-like 1	Rattus norvegicus	64-84
3082185-3	1986	In the heparin group, there was less of a drop in the platelet count and the level of AT-III than in the control group, but the FDP levels were the same as in the control group.	Heparin	7-14	serpin family C member 1	Canis lupus familiaris	86-92
3955233-9	1986	125I-antithrombin III, when bound to the deendothelialized vessel surface, was actively displaced by either heparin, thrombin, or by unlabeled antithrombin III.	Heparin	108-115	prothrombin	Oryctolagus cuniculus	9-17
3947172-4	1986	In vitro, only the combination of protamine sulfate and heparin, and neither alone, resulted in increased C3a and C4a.	Heparin	56-63	complement C3	Homo sapiens	106-109
3000827-0	1986	The heparin-binding site(s) of histidine-rich glycoprotein as suggested by sequence homology with antithrombin III.	Heparin	4-11	histidine rich glycoprotein	Homo sapiens	31-58
3000827-1	1986	A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located.	Heparin	174-181	histidine rich glycoprotein	Homo sapiens	83-110
3000827-1	1986	A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located.	Heparin	174-181	histidine rich glycoprotein	Homo sapiens	112-115
3000827-2	1986	The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG.	Heparin	99-106	histidine rich glycoprotein	Homo sapiens	180-183
3000827-3	1986	These observations strongly suggest that the heparin-binding sites of HRG and AT III are evolutionarily related.	Heparin	45-52	histidine rich glycoprotein	Homo sapiens	70-73
4082111-6	1985	injection of a large amount of thrombin (5,000-15,000 units/day) with heparin significantly affected AT III metabolism except for a transient decrease in AT III concentration in the latter case, although decrease in plasma fibrinogen concentration and platelet count was observed in both cases.	Heparin	70-77	serpin family C member 1	Canis lupus familiaris	101-107
4062902-11	1985	The acceleration of this inhibition reaction by heparin was counteracted by S-protein, indicating the ability of S-protein to neutralize heparin activity.	Heparin	48-55	vitronectin	Homo sapiens	113-122
4062902-11	1985	The acceleration of this inhibition reaction by heparin was counteracted by S-protein, indicating the ability of S-protein to neutralize heparin activity.	Heparin	137-144	vitronectin	Homo sapiens	76-85
4062902-11	1985	The acceleration of this inhibition reaction by heparin was counteracted by S-protein, indicating the ability of S-protein to neutralize heparin activity.	Heparin	137-144	vitronectin	Homo sapiens	113-122
4071064-1	1985	HRG demonstrated a high affinity for heparin and could thus participate in the inhibition of the clotting mechanism.	Heparin	37-44	histidine rich glycoprotein	Homo sapiens	0-3
4082106-6	1985	S.c. administration showed that the AUC of LMW heparin on the factor Xa inhibition was 10 times larger compared to normal heparin.	Heparin	47-54	coagulation factor X	Homo sapiens	62-71
4008652-8	1985	The TSP-HRGP-Plg complex bound a similar amount of heparin as the TSP-HRGP complex, demonstrating that the HRGP within the trimolecular complex maintained functional capability.	Heparin	51-58	histidine rich glycoprotein	Homo sapiens	8-12
3968434-8	1985	At 42 micrograms, cathepsin D-derived, non-gelatin-binding, low affinity heparin fragments that contained both BD4 and CE9 determinants or only the BD4 determinant inhibited monocyte ingestion by 53 and 74%, respectively, when concurrently incubated with 180K-opFnf and target Er, but were without effect when used to pretreat Er before the addition of 180K-opFnf.	Heparin	73-80	defensin beta 104A	Homo sapiens	111-114
6509363-0	1984	Effects of heparin fractions of different affinities to antithrombin III and thrombin on the inactivation of thrombin and factor Xa by antithrombin III.	Heparin	11-18	coagulation factor X	Homo sapiens	122-131
6509363-2	1984	There was a good correlation between heparin affinity for antithrombin III and its ability to enhance the inactivation of thrombin and factor Xa.	Heparin	37-44	coagulation factor X	Homo sapiens	135-144
6690635-3	1984	Blood samples in heparin, but not in citrate, developed aggregates at shear rates below 500 sec-1.	Heparin	17-24	secretory blood group 1, pseudogene	Homo sapiens	92-97
6198531-8	1984	The therapeutic effects of heparin were assessed by prolonged APTT (45-250 sec) and elevated Anti-FXa activity (0.2-1.2 u/ml of plasma heparin concentration) as an indicator for the evaluation of anticoagulation activity and by normalized FPA, Fbg, FDP, Plg and AT III as an indicator for evaluation of antithrombolic activity.	Heparin	27-34	coagulation factor X	Homo sapiens	98-101
6651824-0	1983	Structure-activity relationship in heparin: a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity.	Heparin	35-42	coagulation factor X	Homo sapiens	136-145
6356454-4	1983	125I-labelled thrombin became associated with the endothelium and also with de-endothelialized vessels, and some of it could be displaced by high concentrations of heparin.	Heparin	164-171	prothrombin	Oryctolagus cuniculus	14-22
6356454-5	1983	Exposure of vessels to heparin after thrombin treatment eliminated the enhanced platelet accumulation caused by the thrombin treatment, probably because heparin displaced thrombin from the aortae, as demonstrated in experiments with 125I-thrombin.	Heparin	23-30	prothrombin	Oryctolagus cuniculus	116-124
6356454-5	1983	Exposure of vessels to heparin after thrombin treatment eliminated the enhanced platelet accumulation caused by the thrombin treatment, probably because heparin displaced thrombin from the aortae, as demonstrated in experiments with 125I-thrombin.	Heparin	23-30	prothrombin	Oryctolagus cuniculus	116-124
6356454-5	1983	Exposure of vessels to heparin after thrombin treatment eliminated the enhanced platelet accumulation caused by the thrombin treatment, probably because heparin displaced thrombin from the aortae, as demonstrated in experiments with 125I-thrombin.	Heparin	23-30	prothrombin	Oryctolagus cuniculus	116-124
6356454-5	1983	Exposure of vessels to heparin after thrombin treatment eliminated the enhanced platelet accumulation caused by the thrombin treatment, probably because heparin displaced thrombin from the aortae, as demonstrated in experiments with 125I-thrombin.	Heparin	153-160	prothrombin	Oryctolagus cuniculus	116-124
6356454-5	1983	Exposure of vessels to heparin after thrombin treatment eliminated the enhanced platelet accumulation caused by the thrombin treatment, probably because heparin displaced thrombin from the aortae, as demonstrated in experiments with 125I-thrombin.	Heparin	153-160	prothrombin	Oryctolagus cuniculus	116-124
6356454-5	1983	Exposure of vessels to heparin after thrombin treatment eliminated the enhanced platelet accumulation caused by the thrombin treatment, probably because heparin displaced thrombin from the aortae, as demonstrated in experiments with 125I-thrombin.	Heparin	153-160	prothrombin	Oryctolagus cuniculus	116-124
6581148-5	1983	On the contrary, the minor cytosolic casein kinase CTS, is inhibited by both 2,3-DPG and heparin under all conditions tested in the assay.	Heparin	89-96	transthyretin	Homo sapiens	51-54
6847629-1	1983	Heparin fractions of differing Mr (7800-18 800) prepared from commercial heparin by gel filtration and affinity chromatography on immobilized anti-thrombin III had specific activities when determined by anti-Factor Xa and anti-thrombin assays that ranged from 228 to 448 units/mg.	Heparin	0-7	coagulation factor X	Homo sapiens	208-217
6822493-5	1983	Differences between thrombin and Factor Xa at low (nanomolar) concentrations of heparin were evident in this rate constant and the relative affinities for the heparin-antithrombin complex (Km for Factor Xa = 100 nM; Km for thrombin less than or equal to 2 nM).	Heparin	80-87	coagulation factor X	Homo sapiens	33-42
7165705-11	1982	Purification of lipoprotein lipase from adipose tissue of glucose-fed rats was also carried out using affinity chromatography on Sepharose 4B linked to heparin with low affinity for antithrombin-III.	Heparin	152-159	serpin family C member 1	Rattus norvegicus	182-198
6817749-4	1982	In the absence of heparin, the inactivation of trypsin by antithrombin was 20 times faster than the inactivation of thrombin; the second-order rate constant was 1.5 x 10(5)m(-1).s(-1) at 25 degrees C and pH 7.4.	Heparin	18-25	coagulation factor II, thrombin	Bos taurus	62-70
6817749-5	1982	However, the inhibition of thrombin was accelerated about 30 times more efficiently by small amounts of heparin than was trypsin inhibition.	Heparin	104-111	coagulation factor II, thrombin	Bos taurus	27-35
6817945-4	1982	The use of heparin as an anticoagulant interfered with the assay resulting in apparent HCAI concentrations as low as 60% of those obtained using EDTA.	Heparin	11-18	cytochrome P450 family 24 subfamily A member 1	Homo sapiens	87-91
7157229-6	1982	The inactivation of thrombin or factor Xa by antithrombin is catalysed by the presence in the mixture of these insoluble materials as it is with soluble heparin.	Heparin	153-160	coagulation factor X	Homo sapiens	32-41
7082850-3	1982	The Ca2+ leakiness developed gradually after day 2 and reached a maximum by day 7 of cold storage in ACD, CPD, CPD-adenine, or heparin anticoagulants.	Heparin	127-134	carbonic anhydrase 2	Homo sapiens	4-7
6977539-4	1982	As in the latter reaction, the formation of the modified antithrombin by Factor Xa was increased in the presence of heparin, while only small amounts were produced by Factor IXa both in the absence and presence of the polysaccharide.	Heparin	116-123	coagulation factor X	Homo sapiens	73-82
7099168-2	1982	We provide evidence here that heparin"s most effective inhibition is mediated through interaction with and potentiation of C1-INH.	Heparin	30-37	serpin family G member 1	Homo sapiens	123-129
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Heparin	54-61	coagulation factor X	Homo sapiens	112-121
7191289-1	1980	2nd communication: Chemical analysis of the carbohydrate content and determination of the biological activity of a new potent heparin preparation in vitro, using protamine neutralization and amidolytic methods for factor Xa and thrombin.	Heparin	126-133	coagulation factor X	Homo sapiens	214-223
7191289-2	1980	A new potent heparin preparation was further characterized for carbohydrate content and for biological activities in vitro using the protamine neutralization test and amidolytic methods for factor Xa and thrombin.	Heparin	13-20	coagulation factor X	Homo sapiens	190-199
7191289-5	1980	The amidolytic method using chromogenic substrates S-2222 for factor Xa and S-2238 for thrombin demonstrated that the new heparin was also at least two times more effective than commercial heparin in increasing the rate of inactivation of these serin proteases through antithrombin III.	Heparin	122-129	coagulation factor X	Homo sapiens	62-71
515019-0	1979	Quantitative aspects of lipoprotein lipase release by heparin in mice.	Heparin	54-61	lipoprotein lipase	Mus musculus	24-42
501288-0	1979	Surface-associated heparin inhibits zymosan-induced activation of the human alternative complement pathway by augmenting the regulatory action of the control proteins on particle-bound C3b.	Heparin	19-26	complement C3	Homo sapiens	185-188
501288-6	1979	The increased numbers of C3b sites susceptible to inactivation by C3bINA in the presence of beta 1H were significantly correlated to the number of molecules of heparin/particle.	Heparin	160-167	complement C3	Homo sapiens	25-28
501288-6	1979	The increased numbers of C3b sites susceptible to inactivation by C3bINA in the presence of beta 1H were significantly correlated to the number of molecules of heparin/particle.	Heparin	160-167	complement factor I	Homo sapiens	66-72
501288-6	1979	The increased numbers of C3b sites susceptible to inactivation by C3bINA in the presence of beta 1H were significantly correlated to the number of molecules of heparin/particle.	Heparin	160-167	complement factor H	Homo sapiens	92-99
501288-7	1979	By linear regression analysis of the correlation (r = 0.99) the number of heparin molecules/particle required to promote total inactivation of bound C3b by purified control proteins was 13.8 X 10(6).	Heparin	74-81	complement C3	Homo sapiens	149-152
501288-8	1979	This molecular analysis suggests that the action of heparin coupled to an activating particle of the alternative pathway is to promote the interaction between particle-bound C3b and the regulatory proteins, thereby preventing particle-associated amplified C3 cleavage.	Heparin	52-59	complement C3	Homo sapiens	174-177
476156-0	1979	Evidence for a plasma inhibitor of the heparin accelerated inhibition of factor Xa by antithrombin III.	Heparin	39-46	coagulation factor X	Homo sapiens	73-82
486539-0	1979	Interactions between heparin and factor Xa.	Heparin	21-28	coagulation factor X	Homo sapiens	33-42
486539-3	1979	Heparin was found to inhibit the rate of prothrombin activation by Factor Xa, calcium and phospholipid.	Heparin	0-7	coagulation factor X	Homo sapiens	67-76
486539-7	1979	In accord with this, binding studies demonstrated that heparin could displace Factor Xa, and in separate experiments, prothrombin, from phospholipid vesicles.	Heparin	55-62	coagulation factor X	Homo sapiens	78-87
720957-2	1978	When factor Xa was added to a system containing antithrombin III in excess and heparin in low concentration, the amount of factor Xa immediately inactivated was found to be a function of the concentration of heparin.	Heparin	79-86	coagulation factor X	Homo sapiens	123-132
720957-2	1978	When factor Xa was added to a system containing antithrombin III in excess and heparin in low concentration, the amount of factor Xa immediately inactivated was found to be a function of the concentration of heparin.	Heparin	208-215	coagulation factor X	Homo sapiens	5-14
720957-2	1978	When factor Xa was added to a system containing antithrombin III in excess and heparin in low concentration, the amount of factor Xa immediately inactivated was found to be a function of the concentration of heparin.	Heparin	208-215	coagulation factor X	Homo sapiens	123-132
888033-7	1977	The factor Xa inhibition assay measured heparin levels most precisely and mirrored the A-PTT results in all but one instance.	Heparin	40-47	coagulation factor X	Homo sapiens	4-13
969504-4	1976	Second, low-dose heparin probably works by augmenting the effect of the naturally occurring inhibitor to Factor Xa.	Heparin	17-24	coagulation factor X	Homo sapiens	105-114
790496-8	1976	The inhibitory effect of heparin on the basal insulin secretion and the glucose stimulated insulin secretion was observed in Langerhans islets in vitro model, too.	Heparin	25-32	insulin	Canis lupus familiaris	46-53
790496-9	1976	This suggests that heparin, at least partly, inhibits insulin secretion directly through its influence on the beta cells.	Heparin	19-26	insulin	Canis lupus familiaris	54-61
1256330-1	1976	The activity of monoglyceride lipase was studied in plasma from 74 patients with liver disease in whom blood was drawn 10 min after the injection of heparin (10 U/kg body weight).	Heparin	149-156	monoglyceride lipase	Homo sapiens	16-36
1202536-2	1975	Heparin is a true anticoagulant, and directly opposes fibrin formation (antithrombotic action) and potentiates the inactivation of prothrombinase ; this global action, immediately effective, makes heparin undoubtedly superior to the antivitamins K. Nevertheless, its action on thrombogenesis is incomplete : it reacts only slightly or not at all on platelet aggregation and fibrinolysis.	Heparin	0-7	coagulation factor X	Homo sapiens	131-145
1202536-2	1975	Heparin is a true anticoagulant, and directly opposes fibrin formation (antithrombotic action) and potentiates the inactivation of prothrombinase ; this global action, immediately effective, makes heparin undoubtedly superior to the antivitamins K. Nevertheless, its action on thrombogenesis is incomplete : it reacts only slightly or not at all on platelet aggregation and fibrinolysis.	Heparin	197-204	coagulation factor X	Homo sapiens	131-145
4853677-1	1974	Assay based on factor-Xa inactivation by heparin and antifactor Xa.	Heparin	41-48	coagulation factor X	Homo sapiens	15-24
33758009-9	2021	Solid-phase competition assays showed that the PCSK9 interaction with heparin-albumin (HS-proteoglycan analogue) was critically dependent on polysaccharide chain length.	Heparin	70-77	proprotein convertase subtilisin/kexin type 9	Rattus norvegicus	47-52
34003115-4	2021	Both functions of Ihog (trans-homophilic binding for cytoneme stabilization and Hh binding for ligand sensing) involve a heparin-binding site on the first fibronectin repeat of the extracellular domain.	Heparin	121-128	interference hedgehog	Drosophila melanogaster	18-22
33987731-5	2021	She was administered intravenous and oral antibiotics with injection heparin/remdesivir, during her 7 day stay at the hospital.	Heparin	69-76	Src homology 2 domain containing E	Homo sapiens	0-3
33610598-0	2021	Low anticoagulant heparin-iron complex targeting inhibition of hepcidin ameliorates anemia of chronic disease in rodents.	Heparin	18-25	hepcidin antimicrobial peptide	Mus musculus	63-71
33610598-1	2021	Hepcidin is the only known hormone negatively regulates systemic iron availability, its excess contributes to anemia of chronic disease (ACD).Heparin has been shown to be an efficient hepcidin inhibitor both in vitro and in vivo, but its powerful anticoagulant activity limits this therapeutic application.	Heparin	142-149	hepcidin antimicrobial peptide	Mus musculus	0-8
33610598-1	2021	Hepcidin is the only known hormone negatively regulates systemic iron availability, its excess contributes to anemia of chronic disease (ACD).Heparin has been shown to be an efficient hepcidin inhibitor both in vitro and in vivo, but its powerful anticoagulant activity limits this therapeutic application.	Heparin	142-149	hepcidin antimicrobial peptide	Mus musculus	184-192
33128209-5	2021	The adult and adapted models were used to predict the time courses of anti-factor Xa activity (aXa) and activated partial thromboplastin time (aPTT) in patients receiving UFH infusion.	Heparin	171-174	coagulation factor X	Homo sapiens	75-84
33216354-1	2021	BACKGROUND: Some cancer patients who are diagnosed with thromboembolism may require dual treatment with vascular endothelial growth factor receptor (VEGFR) tyrosine kinase inhibitors (TKIs) and factor Xa inhibitors (low-molecular-weight heparin [LMWH] or direct oral anticoagulants [DOACs]).	Heparin	237-244	kinase insert domain receptor	Homo sapiens	104-147
33216354-1	2021	BACKGROUND: Some cancer patients who are diagnosed with thromboembolism may require dual treatment with vascular endothelial growth factor receptor (VEGFR) tyrosine kinase inhibitors (TKIs) and factor Xa inhibitors (low-molecular-weight heparin [LMWH] or direct oral anticoagulants [DOACs]).	Heparin	237-244	kinase insert domain receptor	Homo sapiens	149-154
33216354-1	2021	BACKGROUND: Some cancer patients who are diagnosed with thromboembolism may require dual treatment with vascular endothelial growth factor receptor (VEGFR) tyrosine kinase inhibitors (TKIs) and factor Xa inhibitors (low-molecular-weight heparin [LMWH] or direct oral anticoagulants [DOACs]).	Heparin	237-244	coagulation factor X	Homo sapiens	194-203
33571828-4	2021	Here, a tetragonal and a monoclinic co-crystal structure of CK2alpha, the catalytic subunit of CK2, with a decameric heparin fragment are described.	Heparin	117-124	casein kinase 2 alpha 2	Homo sapiens	60-68
33571828-5	2021	In the tetragonal structure, the heparin molecule binds to the polybasic stretch at the beginning of CK2alpha"s helix alphaC, whereas in the monoclinic structure it occupies the central substrate-recognition region around the P+1 loop.	Heparin	33-40	casein kinase 2 alpha 2	Homo sapiens	101-109
33571828-7	2021	The monoclinic CK2alpha/heparin structure, in which the heparin fragment is particularly well defined, is the first CK2 structure with an anionic inhibitor of considerable size at the central part of the substrate-recognition site.	Heparin	24-31	casein kinase 2 alpha 2	Homo sapiens	15-23
33571828-7	2021	The monoclinic CK2alpha/heparin structure, in which the heparin fragment is particularly well defined, is the first CK2 structure with an anionic inhibitor of considerable size at the central part of the substrate-recognition site.	Heparin	56-63	casein kinase 2 alpha 2	Homo sapiens	15-23
33683394-0	2021	Protein A of Staphylococcus aureus strain NCTC8325 interacted with heparin.	Heparin	67-74	SAOUHSC_00069	Staphylococcus aureus subsp. aureus NCTC 8325	0-9
33683394-4	2021	Here, we found that protein A (SpA) of S. aureus was a heparin-binding protein, contributing to the interaction between S. aureus and heparin.	Heparin	55-62	SAOUHSC_00069	Staphylococcus aureus subsp. aureus NCTC 8325	20-29
32833716-3	2021	METHODS: In the derivation cohort then in the validation cohort, via receiver operatingcharacteristics (ROC) curve analysis, we evaluated the ability of heparin anti-Xaassay to detect levels of factor-Xa inhibitors above or below the abovementioned safety thresholds recommended for an invasive procedure (screening test).	Heparin	153-160	coagulation factor X	Homo sapiens	194-203
32833716-5	2021	In a validation cohort, the estimated level of each factor-Xa inhibitor was thus inferred from heparin anti-Xa activity.	Heparin	95-102	coagulation factor X	Homo sapiens	52-61
32833716-7	2021	RESULTS: Among 989 (355 patients) and 756 blood samples (420 patients) in the derivation and validation cohort, there was a strong linear relationship between heparin anti-Xa activities and factor-Xa inhibitors measured level (r = 0.99 [95% confidence interval {CI}, 0.99-0.99]).	Heparin	159-166	coagulation factor X	Homo sapiens	190-199
33176060-1	2021	BACKGROUND: Heparin enhances the ability of the plasma protease inhibitor, antithrombin, to neutralize coagulation factor Xa and thrombin.	Heparin	12-19	coagulation factor X	Homo sapiens	115-124
33176060-4	2021	METHODS: Inhibition of factor Xa and thrombin by antithrombin in the presence of different heparins and skeletal muscle myosin or cardiac myosin was studied by measuring inhibition of each enzyme"s chromogenic substrate hydrolysis.	Heparin	91-99	coagulation factor X	Homo sapiens	23-32
33176060-5	2021	RESULTS AND CONCLUSIONS: Skeletal muscle myosin and cardiac myosin neutralized unfractionated heparin"s enhancement of antithrombin"s inhibition of purified factor Xa and thrombin.	Heparin	94-101	coagulation factor X	Homo sapiens	157-166
33302210-0	2021	Discordance in activated partial thromboplastin time and anti-factor Xa levels in COVID-19 patients on heparin therapy.	Heparin	103-110	coagulation factor X	Homo sapiens	62-71
32888192-2	2021	INTRODUCTION: Standard subcutaneous low-molecular-weight heparin (LMWH) thromboprophylaxis yields low anti-factor Xa activity in patients in the intensive care unit (ICU).	Heparin	57-64	coagulation factor X	Homo sapiens	107-116
32928959-8	2020	The interaction of N-MADD-4B with NLG-1 is also disrupted by heparin, used as a surrogate for the extracellular matrix component, heparan sulphate, and whose high-affinity binding to the Ig-like domain may proceed from surface charge complementarity, as suggested by homology 3D modelling.	Heparin	61-68	COesterase domain-containing protein;Neuroligin-1	Caenorhabditis elegans	34-39
33149192-2	2020	Heparin has antifibrotic activity, mediated by cellular secretion of hepatocyte growth factor (HGF).	Heparin	0-7	hepatocyte growth factor	Mus musculus	69-93
33149192-2	2020	Heparin has antifibrotic activity, mediated by cellular secretion of hepatocyte growth factor (HGF).	Heparin	0-7	hepatocyte growth factor	Mus musculus	95-98
32898824-5	2020	Presence of heparin in the medium reinforced the ZP hardening effect of ezrin and HSP-701A up to one more min, but not HSP-90alpha nor PDI4.	Heparin	12-19	LOC100153898	Sus scrofa	72-77
33128275-7	2021	Compared to plain BCP, expression of endothelial-related genes Flt1 and Vcam1 was higher in BCP-HA and BCP-Hep group at day 30.	Heparin	107-110	FMS-like tyrosine kinase 1	Mus musculus	63-67
33128275-8	2021	Expression of osteogenesis-related genes Sp7 and Bglap after 30 days was the highest in BCP group, followed by BCP-Hep, while the lowest expression was in BCP-HA group which correlates with collagen amount.	Heparin	115-118	Sp7 transcription factor 7	Mus musculus	41-44
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	CD4 antigen	Mus musculus	28-31
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	interleukin 2 receptor, alpha chain	Mus musculus	33-37
32562271-8	2020	Heparin promoted functional CD4+ CD25+ forkhead box protein 3 (FoxP3)+ Treg generation from naive CD4+ T cells, increased interleukin (IL)-2 production and enhanced the activation of pre-existing Tregs with IL-2.	Heparin	0-7	CD4 antigen	Mus musculus	98-101
32385825-13	2020	Physicians ordered intravenous antemortem heparin for 94.8% of DCD donors.	Heparin	42-49	dermcidin	Homo sapiens	63-66
32526007-0	2020	Design and Implementation of an Anti-Factor Xa Heparin Monitoring Protocol.	Heparin	47-54	coagulation factor X	Homo sapiens	37-46
32526007-1	2020	BACKGROUND: The VA Northeast Ohio Healthcare System introduced a new nurse-driven anti-factor Xa (anti-Xa) protocol for monitoring unfractionated heparin to replace the previous activated partial thromboplastin time protocol.	Heparin	146-153	coagulation factor X	Homo sapiens	87-96
32526007-3	2020	METHODS: An interdisciplinary team of providers collaborated to develop and implement a nurse-driven, facility-wide anti-factor Xa protocol for monitoring unfractionated heparin therapy.	Heparin	170-177	coagulation factor X	Homo sapiens	121-130
31471680-6	2020	SELENOP was interacted with apolipoprotein E (ApoE) through heparin-binding sites of SELENOP, and the interaction regulated the secretion of exosomal SELENOP.	Heparin	60-67	selenoprotein P	Mus musculus	0-7
31471680-6	2020	SELENOP was interacted with apolipoprotein E (ApoE) through heparin-binding sites of SELENOP, and the interaction regulated the secretion of exosomal SELENOP.	Heparin	60-67	selenoprotein P	Mus musculus	85-92
31471680-6	2020	SELENOP was interacted with apolipoprotein E (ApoE) through heparin-binding sites of SELENOP, and the interaction regulated the secretion of exosomal SELENOP.	Heparin	60-67	selenoprotein P	Mus musculus	85-92
32481593-0	2020	Heparin Blocks the Inhibition of Tissue Kallikrein 1 by Kallistatin through Electrostatic Repulsion.	Heparin	0-7	serpin family A member 4	Homo sapiens	56-67
32481593-1	2020	Kallistatin, also known as SERPINA4, has been implicated in the regulation of blood pressure and angiogenesis, due to its specific inhibition of tissue kallikrein 1 (KLK1) and/or by its heparin binding ability.	Heparin	186-193	serpin family A member 4	Homo sapiens	0-11
32481593-1	2020	Kallistatin, also known as SERPINA4, has been implicated in the regulation of blood pressure and angiogenesis, due to its specific inhibition of tissue kallikrein 1 (KLK1) and/or by its heparin binding ability.	Heparin	186-193	serpin family A member 4	Homo sapiens	27-35
32481593-2	2020	The binding of heparin on kallistatin has been shown to block the inhibition of KLK1 by kallistatin but the detailed molecular mechanism underlying this blockade is unclear.	Heparin	15-22	serpin family A member 4	Homo sapiens	26-37
32481593-2	2020	The binding of heparin on kallistatin has been shown to block the inhibition of KLK1 by kallistatin but the detailed molecular mechanism underlying this blockade is unclear.	Heparin	15-22	serpin family A member 4	Homo sapiens	88-99
32481593-3	2020	Here we solved the crystal structures of human kallistatin and its complex with heparin at 1.9 and 1.8 A resolution, respectively.	Heparin	80-87	serpin family A member 4	Homo sapiens	47-58
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	58-65	serpin family A member 4	Homo sapiens	82-93
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	58-65	serpin family A member 4	Homo sapiens	302-313
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	58-65	serpin family A member 4	Homo sapiens	302-313
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	236-243	serpin family A member 4	Homo sapiens	82-93
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	236-243	serpin family A member 4	Homo sapiens	302-313
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	236-243	serpin family A member 4	Homo sapiens	302-313
32481593-5	2020	Structural analysis and mutagenesis studies show that the heparin binding site of kallistatin is located on a surface with positive electrostatic potential near a unique protruded 310 helix between helix H and strand 2 of beta-sheet C. Heparin binding on this site would prevent KLK1 from docking onto kallistatin due to the electrostatic repulsion between heparin and the negatively charged surface of KLK1, thus blocking the inhibition of KLK1 by kallistatin.	Heparin	357-364	serpin family A member 4	Homo sapiens	82-93
32481593-7	2020	Taken together, these data indicate that heparin controls the specificity of kallistatin, such that kinin generation by KLK1 within the microcirculation will be locally protected by the binding of kallistatin to the heparin-like glycosaminoglycans of the endothelium.	Heparin	41-48	serpin family A member 4	Homo sapiens	77-88
32481593-7	2020	Taken together, these data indicate that heparin controls the specificity of kallistatin, such that kinin generation by KLK1 within the microcirculation will be locally protected by the binding of kallistatin to the heparin-like glycosaminoglycans of the endothelium.	Heparin	41-48	serpin family A member 4	Homo sapiens	197-208
32481593-7	2020	Taken together, these data indicate that heparin controls the specificity of kallistatin, such that kinin generation by KLK1 within the microcirculation will be locally protected by the binding of kallistatin to the heparin-like glycosaminoglycans of the endothelium.	Heparin	216-223	serpin family A member 4	Homo sapiens	77-88
32481593-7	2020	Taken together, these data indicate that heparin controls the specificity of kallistatin, such that kinin generation by KLK1 within the microcirculation will be locally protected by the binding of kallistatin to the heparin-like glycosaminoglycans of the endothelium.	Heparin	216-223	serpin family A member 4	Homo sapiens	197-208
32187531-5	2020	Our binding analyses further revealed that glycosaminoglycans, heparin and heparan sulfate, are ligands for OTK and thus may play a role in the Sema1a-PlexA axon guidance system.	Heparin	63-70	Semaphorin 1a	Drosophila melanogaster	144-150
32187531-5	2020	Our binding analyses further revealed that glycosaminoglycans, heparin and heparan sulfate, are ligands for OTK and thus may play a role in the Sema1a-PlexA axon guidance system.	Heparin	63-70	Plexin A	Drosophila melanogaster	151-156
32036969-7	2020	The gene ontology terms of DEG were highly enriched in heparin binding (9 genes including COMP, CTGF, and IMPG2), glycosaminoglycan binding (10 genes including PCOLCE, POSTN, and RSPO3), and response to estradiol and ion transport (AREG, RAMP3, SFRP1, and SSTR1).	Heparin	55-62	interphotoreceptor matrix proteoglycan 2	Gallus gallus	106-111
31408890-1	2020	BACKGROUND:  Unfractionated heparin has anticoagulant properties by catalyzing antithrombin III, which inactivates coagulation enzymes.	Heparin	28-35	serpin family C member 1	Rattus norvegicus	79-95
32009036-8	2020	The heparin-binding domain corresponding to the pre-S1(30-42) region has a strong affinity to heparin as compared to that of known heparin-binding peptides, such as vitronectin and gp120 in human immunodeficiency virus-1.	Heparin	4-11	vitronectin	Homo sapiens	165-176
32009036-9	2020	This heparin-binding domain binds to heparan sulfate proteoglycan (HSPG) at the cell surface of human hepatic cells.	Heparin	5-12	CD44 molecule (Indian blood group)	Homo sapiens	37-65
32009036-9	2020	This heparin-binding domain binds to heparan sulfate proteoglycan (HSPG) at the cell surface of human hepatic cells.	Heparin	5-12	CD44 molecule (Indian blood group)	Homo sapiens	67-71
31893201-12	2019	Therefore, these types of anomalies should be actively looked for, particularly in young patients with DVT.Treatment with low molecular weight heparin or oral anticoagulation medication is the mainstay of therapy, directed towards preventing thrombosis or its recurrence.A direct factor Xa inhibitor could be a possible alternative to vitamin K antagonists in these patients, despite the lack of clinical evidence supporting its use at the moment.	Heparin	143-150	coagulation factor X	Homo sapiens	280-289
31162876-10	2019	On the contrary, heparin prevented adsorption and cleavage of several heparin-binding proteins; especially complement factor H-related protein 3, insulin-like growth factor binding proteins (2, 4, and 5), and chemerin.	Heparin	17-24	complement factor H related 3	Homo sapiens	107-202
31162876-10	2019	On the contrary, heparin prevented adsorption and cleavage of several heparin-binding proteins; especially complement factor H-related protein 3, insulin-like growth factor binding proteins (2, 4, and 5), and chemerin.	Heparin	17-24	retinoic acid receptor responder 2	Homo sapiens	209-217
31649362-2	2019	HRG has been shown to modulate sepsis-related biological reactions by binding to several substances and cells, including heparin, factor XII, fibrinogen, thrombospondin, plasminogen, C1q, IgG, heme, LPS, dead cells, bacteria, and fungi.	Heparin	121-128	histidine rich glycoprotein	Homo sapiens	0-3
31289905-9	2019	Thus, our research shows that exogenous FGF13 can act as secreted FGF to participate in cell signal transmission and heparin is still required as an ancillary cofactor for the mitogenic effects of FGF13, which may help people to discover more potential functions of FGF13 in cell life activities.	Heparin	117-124	fibroblast growth factor 13	Homo sapiens	197-202
31289905-9	2019	Thus, our research shows that exogenous FGF13 can act as secreted FGF to participate in cell signal transmission and heparin is still required as an ancillary cofactor for the mitogenic effects of FGF13, which may help people to discover more potential functions of FGF13 in cell life activities.	Heparin	117-124	fibroblast growth factor 13	Homo sapiens	197-202
31454337-11	2019	In vitro, UFH significantly reduced the histone-induced cytotoxicity of HIMECs, reduced the release of vWF from the cytoplasm into the culture medium, and inhibited calcium influx into HIMECs.	Heparin	10-13	von Willebrand factor	Rattus norvegicus	103-106
31307055-3	2019	Objective: To compare outcomes between continuous administration of anticoagulants (CA) with CSP (CA+CSP) and periprocedural heparin bridging (HB) with HSP (HB+HSP) for subcentimeter colorectal polyps.	Heparin	125-132	heat shock protein 90 beta family member 2, pseudogene	Homo sapiens	157-163
30994901-6	2019	Second, we find that the V1727F mutation significantly impairs binding of y+z+ agrin to both heparin and the low-density lipoprotein receptor-related protein 4 (LRP4) coreceptor.	Heparin	93-100	agrin	Homo sapiens	79-84
30994901-7	2019	Third, molecular modeling of the LG2 domain suggests that the V1727F mutation primarily disrupts the y splice insert, and consistent with this we find that it partially occludes the contribution of the y splice insert to agrin binding to heparin and LRP4.	Heparin	238-245	agrin	Homo sapiens	221-226
30813751-1	2019	Background: Lab tests such as activated partial thromboplastin time (aPTT) or anti-factor Xa (anti-Xa) levels are typically used to monitor intravenous unfractionated heparin (IV heparin), with recent evidence suggesting that anti-Xa levels may provide a more accurate measure of anticoagulation.	Heparin	179-186	coagulation factor X	Homo sapiens	83-92
31175919-9	2019	The endopolyphosphatase activity of Ppn1 was inhibited by 0.01 mg mL-1 of heparin, while endopolphosphatase activity of Ppn2 was weakly sensitive to 0.25 mg mL-1 of heparin.	Heparin	74-81	endopolyphosphatase	Saccharomyces cerevisiae S288C	36-40
31175919-9	2019	The endopolyphosphatase activity of Ppn1 was inhibited by 0.01 mg mL-1 of heparin, while endopolphosphatase activity of Ppn2 was weakly sensitive to 0.25 mg mL-1 of heparin.	Heparin	165-172	endopolyphosphatase	Saccharomyces cerevisiae S288C	36-40
31472056-7	2019	In addition to above  mechanisms, possibly  the infused protamine binds heparin and causes the coagulation cascade to activate heparin-AT complex on thrombin beside activating FXIa, FXa and FIXa and causing the re-use of Ca2+.	Heparin	127-134	coagulation factor X	Homo sapiens	182-185
30639395-3	2019	Our aim is to achieve this goal by covalently incorporating heparin into acellular nerve scaffolds and by physically immobilizing VEGF to heparin.	Heparin	138-145	vascular endothelial growth factor A	Mus musculus	130-134
30961988-0	2019	Anti-Factor Xa-Based Monitoring of Unfractionated Heparin: Clinical Outcomes in a Pediatric Cohort.	Heparin	50-57	coagulation factor X	Homo sapiens	5-14
30961988-5	2019	The median unfractionated heparin dose required to reach therapeutic Anti-FXa goal was significantly greater in infants compared with older children (P <.0001).	Heparin	26-33	coagulation factor X	Homo sapiens	74-77
30961988-10	2019	CONCLUSIONS: Using an anti-FXa-based nomogram to monitor unfractionated heparin in children is feasible.	Heparin	72-79	coagulation factor X	Homo sapiens	27-30
31261534-4	2019	When assayed within 2 hours, each time point of ProGRP in heparin plasma had no significant difference and the difference of PrpGRP in serum separating gel existed at 1.5 hours.Heparin plasma is the best option for clinical test of ProGRP.	Heparin	58-65	gastrin releasing peptide	Homo sapiens	48-54
31261534-4	2019	When assayed within 2 hours, each time point of ProGRP in heparin plasma had no significant difference and the difference of PrpGRP in serum separating gel existed at 1.5 hours.Heparin plasma is the best option for clinical test of ProGRP.	Heparin	177-184	gastrin releasing peptide	Homo sapiens	232-238
30689028-8	2019	The expression of the adherens junction protein beta-catenin was slightly elevated in heparin treated animals, on day 2 the increase was statistically significant.	Heparin	86-93	catenin (cadherin associated protein), beta 1	Mus musculus	48-60
30378437-9	2019	Heparin requirements were reduced from 15.1 +- 4.1 to 12.8 +- 4.2 U/kg/h for patients who achieved a therapeutic aPTT both prior to and during tPA infusion.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	143-146
30894640-5	2019	SH and HE influenced MMP2 and TIMP3 protein levels and MMP2 activity.	Heparin	7-9	TIMP metallopeptidase inhibitor 3	Homo sapiens	30-35
30849987-5	2019	Module-trait analysis identified that a module involved in microtubule bundle formation, drug metabolism-cytochrome P450, and IL-17 signaling pathway was negatively correlated with osteosarcoma and positively correlated with metastasis; a module involved in DNA replication was positively correlated with osteosarcoma; a module involved in cell junction was positively correlated with metastasis; and a module involved in heparin binding negatively correlated with osteosarcoma.	Heparin	422-429	interleukin 17A	Homo sapiens	126-131
30638770-9	2019	The binding of rLIC13259 to C8 and vitronectin was slight and pronounced inhibited in the presence of increasing heparin concentration, respectively, suggesting that the interaction with vitronectin occurs via heparin domain.	Heparin	113-120	vitronectin	Homo sapiens	35-46
30638770-9	2019	The binding of rLIC13259 to C8 and vitronectin was slight and pronounced inhibited in the presence of increasing heparin concentration, respectively, suggesting that the interaction with vitronectin occurs via heparin domain.	Heparin	113-120	vitronectin	Homo sapiens	187-198
30582952-0	2019	Anti-tumour activity of low molecular weight heparin doxorubicin nanoparticles for histone H1 high-expressive prostate cancer PC-3M cells.	Heparin	45-52	H1.0 linker histone	Homo sapiens	83-93
30680875-2	2019	Recently, we described multilayer nanoparticles (nanotraps) with heparin surface and cationic peptides comprising the N-terminal tail (Nt) and the second extracellular loop (ECL2) of CCR5 receptor, which could bind with high affinity some inflammatory chemokines, in particular, Rantes.	Heparin	65-72	C-C motif chemokine receptor 5	Homo sapiens	183-187
30680875-6	2019	Heparin-covered nanoparticles bearing CCR5 peptides effectively bound V3 as well.	Heparin	0-7	C-C motif chemokine receptor 5	Homo sapiens	38-42
30523825-8	2019	Overall, HE staining and vWF immunohistochemistry all confirmed that heparin-coated DSM has a satisfactory anticoagulant effect.	Heparin	69-76	von Willebrand factor	Rattus norvegicus	25-28
31030744-7	2019	Thus, heparin is responsible for the simultaneous inhibition of both thrombin generation and thrombin activity in the blood circulation.	Heparin	6-13	coagulation factor II, thrombin	Bos taurus	93-101
30798810-0	2019	The role of heparin, heparanase and heparan sulfates in hepcidin regulation.	Heparin	12-19	hepcidin antimicrobial peptide	Mus musculus	56-64
30798810-3	2019	Heparin was found to inhibit hepcidin expression and BMP6 activity in hepatic cell lines and in mice, suggesting that endogenous heparan sulfates are involved in the pathway of hepcidin expression.	Heparin	0-7	hepcidin antimicrobial peptide	Mus musculus	29-37
30798810-3	2019	Heparin was found to inhibit hepcidin expression and BMP6 activity in hepatic cell lines and in mice, suggesting that endogenous heparan sulfates are involved in the pathway of hepcidin expression.	Heparin	0-7	hepcidin antimicrobial peptide	Mus musculus	177-185
30474653-6	2018	The evolutionarily conserved amino acid residues Asp-31, Trp-32, and Asp-33 are indispensable for the heparin-binding activity.	Heparin	102-109	thioredoxin like 1	Homo sapiens	57-63
30403126-0	2018	Rosuvastatin- and Heparin-Loaded Poly(l-lactide- co-caprolactone) Nanofiber Aneurysm Stent Promotes Endothelialization via Vascular Endothelial Growth Factor Type A Modulation.	Heparin	18-25	vascular endothelial growth factor A	Oryctolagus cuniculus	123-157
29730503-12	2018	Addition of heparin reduced binding between aCPP and wild-type cells to levels of Fbln7-/- cells.	Heparin	12-19	fibulin 7	Mus musculus	82-87
29730503-13	2018	Taken together, our study suggests that Fbln7 is a local mediator of calcium deposition and that releasing Fbln7 from the cell surface by heparin/heparin derivatives or Fbln7 inhibitory antibodies may provide a novel strategy to prevent ectopic calcification in vivo.	Heparin	138-145	fibulin 7	Mus musculus	107-112
29730503-13	2018	Taken together, our study suggests that Fbln7 is a local mediator of calcium deposition and that releasing Fbln7 from the cell surface by heparin/heparin derivatives or Fbln7 inhibitory antibodies may provide a novel strategy to prevent ectopic calcification in vivo.	Heparin	138-145	fibulin 7	Mus musculus	107-112
29730503-13	2018	Taken together, our study suggests that Fbln7 is a local mediator of calcium deposition and that releasing Fbln7 from the cell surface by heparin/heparin derivatives or Fbln7 inhibitory antibodies may provide a novel strategy to prevent ectopic calcification in vivo.	Heparin	146-153	fibulin 7	Mus musculus	107-112
29730503-13	2018	Taken together, our study suggests that Fbln7 is a local mediator of calcium deposition and that releasing Fbln7 from the cell surface by heparin/heparin derivatives or Fbln7 inhibitory antibodies may provide a novel strategy to prevent ectopic calcification in vivo.	Heparin	146-153	fibulin 7	Mus musculus	107-112
30389911-7	2018	Furthermore, mice injected with syndecan ectodomains, heparan sulfate, and N-desulfated heparin derivatives into periosteal regions of calvaria showed reduction in the formation of tartrate-resistant acid phosphatase (TRAP)-positive mature osteoclasts on the calvarial bone surface, thereby exhibiting decreased bone resorption.	Heparin	88-95	acid phosphatase 5, tartrate resistant	Mus musculus	181-216
30389911-7	2018	Furthermore, mice injected with syndecan ectodomains, heparan sulfate, and N-desulfated heparin derivatives into periosteal regions of calvaria showed reduction in the formation of tartrate-resistant acid phosphatase (TRAP)-positive mature osteoclasts on the calvarial bone surface, thereby exhibiting decreased bone resorption.	Heparin	88-95	acid phosphatase 5, tartrate resistant	Mus musculus	218-222
29303375-4	2018	In this new TCPP, a specific alpha helix structure was inserted into a repeated amino acid (AA) sequence formed by tandem multiple selected key AA residues of vaccinia growth factor (VGF), and this sequence was then fused to a tailored heparin binding domain sequence (C6H) derived from heparin-binding epidermal growth factor-like growth factor to intensify its targeting delivery ability.	Heparin	236-243	VGF nerve growth factor inducible	Homo sapiens	159-181
29303375-4	2018	In this new TCPP, a specific alpha helix structure was inserted into a repeated amino acid (AA) sequence formed by tandem multiple selected key AA residues of vaccinia growth factor (VGF), and this sequence was then fused to a tailored heparin binding domain sequence (C6H) derived from heparin-binding epidermal growth factor-like growth factor to intensify its targeting delivery ability.	Heparin	236-243	VGF nerve growth factor inducible	Homo sapiens	183-186
30425728-5	2018	FGF10 is a typical paracrine FGF and chiefly mediates biological responses by activating FGFR2b with heparin/heparan sulfate (HS) as cofactor.	Heparin	101-108	fibroblast growth factor 10	Mus musculus	0-5
30425728-5	2018	FGF10 is a typical paracrine FGF and chiefly mediates biological responses by activating FGFR2b with heparin/heparan sulfate (HS) as cofactor.	Heparin	101-108	fibroblast growth factor 10	Mus musculus	0-3
29753267-0	2018	The localisation of the heparin binding sites of human and murine interleukin-12 within the carboxyterminal domain of the P40 subunit.	Heparin	24-31	interleukin 12b	Mus musculus	122-125
29753267-4	2018	Heparin markedly protects the human and murine p40 subunits, but not the p35 subunits, from cleavage by the bacterial endoprotease LysC, further implicating the larger subunit as the location of the heparin binding site.	Heparin	0-7	interleukin 12b	Mus musculus	47-50
30248108-7	2018	We found differential affinities of CXCL1, CXCL2 and CCL2 for HS in isolated mGEnC-1 glycocalyx, heparan sulfate from bovine kidney or low molecular weight heparin in competition ELISAs using mGEnC-1 as a substrate, indicating that chemokine binding is affected by the domain structure of the different HS preparations.	Heparin	156-163	growth-regulated protein homolog alpha	Bos taurus	36-41
30248108-7	2018	We found differential affinities of CXCL1, CXCL2 and CCL2 for HS in isolated mGEnC-1 glycocalyx, heparan sulfate from bovine kidney or low molecular weight heparin in competition ELISAs using mGEnC-1 as a substrate, indicating that chemokine binding is affected by the domain structure of the different HS preparations.	Heparin	156-163	C-C motif chemokine 2	Bos taurus	53-57
30533518-5	2018	The results indicate that inhibition of HSPG binding to Abeta42 using either heparinase III or heparin reduces Abeta42 expression and increases the population of beta-tubulin III+ neurons, whereas the inhibition of MMP2/9 induces more neurotoxicity.	Heparin	77-84	syndecan 2	Homo sapiens	40-44
29420785-8	2018	Heparin showed higher affinity to RPTPsigma than the CS library.	Heparin	0-7	protein tyrosine phosphatase receptor type S	Homo sapiens	34-43
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	interleukin 18	Homo sapiens	76-81
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	13-16	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	206-211
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	114-117	interleukin 18	Homo sapiens	76-81
30016181-13	2018	As expected, UFH decreased LPS-induced IL-1beta, TNF-alpha, IL-6, IL-8, and IL-18 protein levels, suggesting that UFH has an anti-inflammatory effect on THP-1 cells by interrupting the MAPK, NF-kappaB, and c-Jun signaling pathways.	Heparin	114-117	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	206-211
29550439-7	2018	Heparin functionalization increased the amount of TGF-beta2 and GDF5 remaining attached to the scaffold matrix and resulted in biological effects at low growth factor doses.	Heparin	0-7	transforming growth factor beta 2	Homo sapiens	50-59
29461035-8	2018	Heparin immobilization on the positively charged nanofiber yarns was visualized using fluorescein-conjugated heparin (F-Hep), and the amount of immobilized F-Hep was higher on both PLGA/PEO/PgP3.7 and PLGA/PEO/PgP1 than yarns without PgP (PLGA/PEO).	Heparin	0-7	CD44 molecule (Indian blood group)	Homo sapiens	210-214
29461035-10	2018	Finally, we observed that heparin-eluting nanofiber yarns with both PgP1 and PgP3.7 showed significantly longer clotting times than nanofiber yarns without PgP.	Heparin	26-33	CD44 molecule (Indian blood group)	Homo sapiens	68-72
29315961-13	2018	An optimized protocol of heparin before TP, double TP, and intravenous aspirin in non-ARP resulted in a significantly lowered CE incidence and severity.	Heparin	25-32	arginine-glutamic acid dipeptide repeats	Homo sapiens	86-89
29378054-11	2018	Conclusions: Confounders in plasma miR analysis include the use of heparin tubes, erythrocyte hemolysis, and storage of thawed plasma at room temperature.	Heparin	67-74	membrane associated ring-CH-type finger 8	Homo sapiens	35-38
29312404-9	2017	Sequence analysis, structural studies, and in silico modeling revealed that bleogen pB1 has a cation-polar-cation motif, a signature heparin-binding motif that was confirmed by heparin affinity chromatography.	Heparin	133-140	polybromo 1	Homo sapiens	84-87
29312404-9	2017	Sequence analysis, structural studies, and in silico modeling revealed that bleogen pB1 has a cation-polar-cation motif, a signature heparin-binding motif that was confirmed by heparin affinity chromatography.	Heparin	177-184	polybromo 1	Homo sapiens	84-87
28939773-7	2017	While binding to PTN, Mac-1 on Mac-1-expressing HEK293 cells appears to cooperate with cell-surface proteoglycans because both anti-Mac-1 function-blocking mAb and heparin were required to block adhesion.	Heparin	164-171	integrin subunit alpha M	Homo sapiens	22-27
28939773-7	2017	While binding to PTN, Mac-1 on Mac-1-expressing HEK293 cells appears to cooperate with cell-surface proteoglycans because both anti-Mac-1 function-blocking mAb and heparin were required to block adhesion.	Heparin	164-171	integrin subunit alpha M	Homo sapiens	31-36
28939773-7	2017	While binding to PTN, Mac-1 on Mac-1-expressing HEK293 cells appears to cooperate with cell-surface proteoglycans because both anti-Mac-1 function-blocking mAb and heparin were required to block adhesion.	Heparin	164-171	integrin subunit alpha M	Homo sapiens	31-36
29149067-2	2017	Moreover, we investigated, in physiological placental tissue, the ability of Low Molecular Weight Heparin (LMWH) to modify HMGB1 structural conformation thus inhibiting RAGE binding and HMGB1/RAGE axis inflammatory activity.	Heparin	98-105	long intergenic non-protein coding RNA 914	Homo sapiens	169-173
29149067-2	2017	Moreover, we investigated, in physiological placental tissue, the ability of Low Molecular Weight Heparin (LMWH) to modify HMGB1 structural conformation thus inhibiting RAGE binding and HMGB1/RAGE axis inflammatory activity.	Heparin	98-105	long intergenic non-protein coding RNA 914	Homo sapiens	192-196
29096838-7	2017	We found that heparin precipitation and direct absorption apheresis procedures led to a significant decrease of plasma n-3 and n-6 PUFA by 40-50%.	Heparin	14-21	pumilio RNA binding family member 3	Homo sapiens	131-135
29044377-8	2017	HEP is a natural precursor to heparin biosynthesis in mammals.	Heparin	30-37	DNL-type zinc finger	Homo sapiens	0-3
29093712-10	2017	Of all FHR dimers, FHR-5/5 homodimers demonstrated strong binding affinity toward heparin.	Heparin	82-89	complement factor H related 5	Homo sapiens	19-24
28118750-1	2017	Heparin-induced thrombocytopenia (HIT) is associated with antibodies to complexes between heparin and platelet factor 4 (PF4), a basic protein usually found in platelet alpha granules.	Heparin	0-7	platelet factor 4	Bos taurus	121-124
28118750-2	2017	Heparin-induced thrombocytopenia antibodies preferentially recognize macromolecular complexes formed between positively charged PF4 and polyanionic heparins over a narrow range of molar ratios.	Heparin	0-7	platelet factor 4	Bos taurus	128-131
28118750-4	2017	The resulting data of the PF4 complexes with unfractionated heparins (UFHs), LMWHs and their fractions, and oligosaccharide components suggest that the size of aggregates is not only a simple function of average molecular weight but also of the molecular weight distribution of the sample.	Heparin	60-68	platelet factor 4	Bos taurus	26-29
28118750-4	2017	The resulting data of the PF4 complexes with unfractionated heparins (UFHs), LMWHs and their fractions, and oligosaccharide components suggest that the size of aggregates is not only a simple function of average molecular weight but also of the molecular weight distribution of the sample.	Heparin	70-74	platelet factor 4	Bos taurus	26-29
28118750-5	2017	Moreover, it was found that lower concentrations of the tested ovine-derived mucosal heparin are required to form the large PF4/heparin complexes as compared to mucosal porcine and bovine heparin.	Heparin	85-92	platelet factor 4	Bos taurus	124-127
28846877-2	2017	INTRODUCTION: In intensive care unit (ICU) patients, subcutaneous low-molecular weight heparin thromboprophylaxis results in lower plasma anti-factor Xa (anti-FXa) levels compared to general ward patients.	Heparin	87-94	coagulation factor X	Homo sapiens	159-162
28509406-0	2017	High heparin content surface-modified polyurethane discs promote rapid and stable angiogenesis in full thickness skin defects through VEGF immobilization.	Heparin	5-12	vascular endothelial growth factor A	Mus musculus	134-138
28509406-7	2017	We therefore attribute the superior performance of HCV due to its ability to hold more VEGF165, based on its increased heparin surface coverage, as also demonstrated in VEGF elution dynamics.	Heparin	119-126	vascular endothelial growth factor A	Mus musculus	87-91
28319494-0	2017	Heparin-Binding Protein (HBP): A Causative Marker and Potential Target for Heparin Treatment of Human Sepsis-Induced Acute Kidney Injury.	Heparin	0-7	azurocidin 1	Homo sapiens	25-28
28319494-11	2017	Different heparin derivatives abrogated the HBP-induced increased inflammatory response in vitro and in vivo.	Heparin	10-17	azurocidin 1	Homo sapiens	44-47
28817384-8	2017	Heparin coating also increased cell infiltration into the electrospun grafts, thus increasing the production of collagen and elastin within the graft wall.	Heparin	0-7	elastin	Rattus norvegicus	125-132
28486148-4	2017	Furthermore, FXa-cleavable gels enabled a faster release of heparin, which was attributed to the lower affinity of the factor for heparin.	Heparin	60-67	coagulation factor X	Homo sapiens	13-16
28486148-4	2017	Furthermore, FXa-cleavable gels enabled a faster release of heparin, which was attributed to the lower affinity of the factor for heparin.	Heparin	130-137	coagulation factor X	Homo sapiens	13-16
28486148-5	2017	Combining early and fast responses, FXa-cleavable gels were shown to provide anticoagulant protection of biomaterial surfaces at low levels of released heparin in human whole-blood incubation experiments.	Heparin	152-159	coagulation factor X	Homo sapiens	36-39
28442532-7	2017	Our data showed that compared with saline and heparin controls, monotherapy of simvastatin and the adjunctive therapy with simvastatin and heparin significantly improved the thrombus resolution and reduced inflammatory cells migration into the venous wall, the release of the inflammatory cell adhesion molecule (P-selectin), inflammatory chemokine (MCP-1) and pleiotropic proinflammatory cytokines (IL-6) into the blood, and the local expression of P-selectin and MCP-1 in the venous wall.	Heparin	139-146	C-C motif chemokine 2	Oryctolagus cuniculus	350-355
28442532-7	2017	Our data showed that compared with saline and heparin controls, monotherapy of simvastatin and the adjunctive therapy with simvastatin and heparin significantly improved the thrombus resolution and reduced inflammatory cells migration into the venous wall, the release of the inflammatory cell adhesion molecule (P-selectin), inflammatory chemokine (MCP-1) and pleiotropic proinflammatory cytokines (IL-6) into the blood, and the local expression of P-selectin and MCP-1 in the venous wall.	Heparin	139-146	C-C motif chemokine 2	Oryctolagus cuniculus	465-470
28557441-0	2017	Tyrosinase-Mediated Surface Coimmobilization of Heparin and Silver Nanoparticles for Antithrombotic and Antimicrobial Activities.	Heparin	48-55	tyrosinase	Homo sapiens	0-10
28557441-4	2017	This consists of tyrosinase-oxidized phenolic groups of a heparin derivative (heparin-grafted tyramine, HT) to catechol groups, followed by immobilizing heparin and inducing the in situ Ag NP formation onto poly(urethane) (PU) substrates.	Heparin	58-65	tyrosinase	Homo sapiens	17-27
28557441-4	2017	This consists of tyrosinase-oxidized phenolic groups of a heparin derivative (heparin-grafted tyramine, HT) to catechol groups, followed by immobilizing heparin and inducing the in situ Ag NP formation onto poly(urethane) (PU) substrates.	Heparin	78-85	tyrosinase	Homo sapiens	17-27
28557441-4	2017	This consists of tyrosinase-oxidized phenolic groups of a heparin derivative (heparin-grafted tyramine, HT) to catechol groups, followed by immobilizing heparin and inducing the in situ Ag NP formation onto poly(urethane) (PU) substrates.	Heparin	78-85	tyrosinase	Homo sapiens	17-27
28397746-7	2017	This review summarizes recent findings on the anti-hepcidin activity of heparins and their possible use for the treatment of anemia caused by hepcidin excess, including the anemia of chronic diseases.	Heparin	72-80	hepcidin antimicrobial peptide	Mus musculus	142-150
27807702-5	2017	Despite the widely accepted dogma of transcriptional/translational quiescence, incubation of sperm with either ouabain (specific ligand for ATP1A4) or heparin increased ATP1A4 content in raft and non-raft sperm membrane fractions, total sperm protein extracts (immunoblotting) and fixed sperm (flow cytometry), with a concurrent increase in Na/K-ATPase enzyme activity.	Heparin	151-158	ATPase Na+/K+ transporting subunit alpha 4	Bos taurus	169-175
28043992-11	2017	Conclusions: Direct thrombin and FXa inhibitors exhibit distinct effects on assay results when used concomitantly with heparins.	Heparin	119-127	coagulation factor X	Homo sapiens	33-36
27878865-2	2017	The members of this subfamily, FGF19, FGF21 and FGF23, are characterized by their reduced binding affinity for heparin that enables them to be transported in the circulation and function in an endocrine manner.	Heparin	111-118	fibroblast growth factor 23	Homo sapiens	48-53
27936565-5	2017	The aromatic residue Trp4 acted as an irreplaceable moiety for membrane insertion, as the replacement of Trp4 with Arg4 abolished cell penetration, although it significantly improved the heparin-binding ability.	Heparin	187-194	transient receptor potential cation channel subfamily C member 4	Homo sapiens	21-25
28035852-0	2017	Lysyl Oxidase Inhibition by Heparin in Idiopathic Pulmonary Fibrosis: Is There Still Hope?	Heparin	28-35	lysyl oxidase	Homo sapiens	0-13
27779234-8	2016	Recombinant C-termini of ADAMTS10 and ADAMTS6, both of which induce focal adhesions, bind heparin and syndecan-4.	Heparin	90-97	ADAM metallopeptidase with thrombospondin type 1 motif 6	Homo sapiens	38-45
27602496-0	2016	Heparins that block VEGF-A-mediated von Willebrand factor fiber generation are potent inhibitors of hematogenous but not lymphatic metastasis.	Heparin	0-8	vascular endothelial growth factor A	Mus musculus	20-26
27602496-5	2016	Unlike the anticoagulant Fondaparinux, an inhibitor of thrombin generation, the low-molecular-weight heparin (LMWH) Tinzaparin inhibited VWF fiber formation and vessel occlusion in tumor vessels by blocking thrombin-induced EC activation and vascular endothelial growth factor-A (VEGF-A)-mediated VWF release.	Heparin	101-108	vascular endothelial growth factor A	Mus musculus	242-278
27602496-5	2016	Unlike the anticoagulant Fondaparinux, an inhibitor of thrombin generation, the low-molecular-weight heparin (LMWH) Tinzaparin inhibited VWF fiber formation and vessel occlusion in tumor vessels by blocking thrombin-induced EC activation and vascular endothelial growth factor-A (VEGF-A)-mediated VWF release.	Heparin	101-108	vascular endothelial growth factor A	Mus musculus	280-286
27711215-4	2016	Among them are exogenous heparins, which are strong hepcidin repressors with a mechanism of action not fully understood but that may involve the competition with the structurally similar endogenous Heparan Sulfates (HS).	Heparin	25-33	hepcidin antimicrobial peptide	Mus musculus	52-60
27542222-4	2016	We found that the acidic domain of MZF-1 and the heparin-binding domain of Elk-1 facilitate the heterodimeric interaction between the two genes before the complex formation binds to the PKCalpha promoter.	Heparin	49-56	ETS transcription factor ELK1	Homo sapiens	75-80
27538028-5	2016	In vitro lysis of a heparin blood sample resulted in a 1.7-fold increase of ALP activity, supporting the origin of the hyperphosphatasemia at least in part from the leukemic cell population.	Heparin	20-27	ATHS	Homo sapiens	76-79
27412396-2	2016	These inactive ATs were previously proven to effectively neutralise anticoagulant activity associated with heparin derivatives in vitro and in vivo, as assessed by direct measurement of anti-FXa activity.	Heparin	107-114	coagulation factor X	Homo sapiens	191-194
27311558-6	2016	The ternary nanoassemblies could efficiently protect the condensed pDNA from enzymatic degradation by DNase I, and HA could significantly improve the stability of nanoassemblies in the sodium heparin solution or serum in vitro.	Heparin	185-199	deoxyribonuclease I	Mus musculus	102-109
26991001-7	2016	Zn(2+) binding to neuropilin-2 destabilizes the protein structure but this effect was counteracted by heparin, suggesting that modifications by glycans and zinc in the extracellular matrix may affect functional neuropilin-2 ligand binding and signalling activity.	Heparin	102-109	neuropilin 2	Homo sapiens	211-223
27252904-12	2016	CONCLUSIONS: Low-dose heparin infusion compared to subcutaneous heparin can decrease the plasma PAI-1 and urinary NGAL levels more rapidly.	Heparin	22-29	lipocalin 2	Homo sapiens	114-118
27252904-12	2016	CONCLUSIONS: Low-dose heparin infusion compared to subcutaneous heparin can decrease the plasma PAI-1 and urinary NGAL levels more rapidly.	Heparin	64-71	lipocalin 2	Homo sapiens	114-118
27067972-3	2016	The therapeutic range of anti-factor Xa activity during therapy with low-molecular weight heparins and danaparoid are less well and of direct oral anticoagulants (DOAC) poorly defined.	Heparin	90-98	coagulation factor X	Homo sapiens	30-39
26607136-12	2016	Direct FXa inhibition by TFPI is modulated by physiological concentrations prothrombin, FV, FVa, protein S, phospholipids and heparin indicating the importance of these modulators for the in vivo anticoagulant activity of TFPI.	Heparin	126-133	coagulation factor X	Homo sapiens	7-10
26793973-7	2016	To address these problems, we added to the medium an inhibitor of hyaluronan synthesis and heparin to compete with the binding of TSG-6 to hyaluronan.	Heparin	91-98	TNF alpha induced protein 6	Homo sapiens	130-135
26790955-5	2016	Moreover, kallistatin via its heparin-binding site antagonized Wnt3a-induced cancer cell proliferation and increased PPARgamma expression.	Heparin	30-37	serpin family A member 4	Homo sapiens	10-21
26278168-4	2015	The %GalN test was sensitive to the presence of NS-OSCS in heparin.	Heparin	59-66	galanin and GMAP prepropeptide	Homo sapiens	5-9
26272754-0	2015	Heparin/heparan sulfates bind to and modulate neuronal L-type (Cav1.2) voltage-dependent Ca(2+) channels.	Heparin	0-7	calcium voltage-gated channel subunit alpha1 C	Homo sapiens	63-69
26577032-3	2015	Furthermore, T4 PNKP inhibition by the inhibitor heparin is shown, demonstrating the potential to screen suitable inhibitor drugs for T4 PNKP.	Heparin	49-56	polynucleotide kinase 3'-phosphatase	Homo sapiens	16-20
26577032-3	2015	Furthermore, T4 PNKP inhibition by the inhibitor heparin is shown, demonstrating the potential to screen suitable inhibitor drugs for T4 PNKP.	Heparin	49-56	polynucleotide kinase 3'-phosphatase	Homo sapiens	137-141
26478127-7	2015	H2 O2 -induced increases in Fura signals were mimicked by Ba(2+) and reduced by heparin, Gd(3+) ions and by Pyr6, a selective inhibitor of the Orai1-mediated Ca(2+) entry,.	Heparin	80-87	ORAI calcium release-activated calcium modulator 1	Rattus norvegicus	143-148
26519056-6	2015	Heparin use, however, was associated with an increase in in- and outlet plasma TWEAK.	Heparin	0-7	TNF superfamily member 12	Homo sapiens	79-84
32262646-0	2015	Delivery of AIB1 siRNA by Ca2+/PEI/heparin composite nanoparticles effectively inhibits the growth of human breast cancer.	Heparin	35-42	ANIB1	Homo sapiens	12-16
32262646-1	2015	Here, a novel carrier fabricated by the interaction of negatively charged heparin and positively charged PEI and Ca2+ was investigated to deliver AIB1 siRNA into breast cancer cells both in vitro and in vivo.	Heparin	74-81	ANIB1	Homo sapiens	146-150
26459242-10	2015	The glycosaminoglycan biosynthesis-heparin sulphate/heparin pathway is significantly enriched in the TOP2B gene ontology analysis, suggesting changes in this pathway in the absence of TOP2B may cause the axon guidance faults.	Heparin	35-42	DNA topoisomerase II beta	Homo sapiens	101-106
26459242-10	2015	The glycosaminoglycan biosynthesis-heparin sulphate/heparin pathway is significantly enriched in the TOP2B gene ontology analysis, suggesting changes in this pathway in the absence of TOP2B may cause the axon guidance faults.	Heparin	35-42	DNA topoisomerase II beta	Homo sapiens	184-189
26022967-6	2015	This layer is loaded with resorbable nanoparticles of bemiparin (a fractionated low molecular weight heparin), which promotes the activation of growth factors, FGF and VEGF, and provides a good biomechanical stability and controlled permeability of the bilayered dressing.	Heparin	101-108	vascular endothelial growth factor A	Mus musculus	168-172
26323298-1	2015	Kallistatin is a serine protease inhibitor (serpin) which specifically inhibits human tissue kallikrein; however, its inhibitory activity is inhibited by heparin.	Heparin	154-161	serpin family A member 4	Homo sapiens	0-11
25744159-6	2015	(3) The MCp had fewer transcripts of mast cell-specific proteases and the enzyme responsible for sulfation of heparin than mature mast cells.	Heparin	110-117	complement component (3b/4b) receptor 1-like	Mus musculus	8-11
25957844-4	2015	In an effort to explore the binding interactions that heparin-like VLPs make with cationic targets, described herein are bio-layer interferometry studies utilizing the BLItz platform that evaluate the interaction of sulf-VLP with the cationic peptide CDK5 (50% Lys).	Heparin	54-61	cyclin dependent kinase 5	Bos taurus	251-255
25855705-4	2015	OBJECTIVE: To determine whether FDA-approved commercial kits for measuring heparin anti-factor Xa activity can be used to assess rivaroxaban concentrations when calibrated for unfractionated heparin or low-molecular-weight heparins.	Heparin	75-82	coagulation factor X	Homo sapiens	88-97
25736604-3	2015	Besides, recently, well-documented association of SAA with high-density lipoprotein or glycosaminoglycans, in particular heparin/heparin sulfate (HS), and specific interaction between SAA and human cystatin C (hCC), the ubiquitous inhibitor of cysteine proteases, was proved.	Heparin	121-128	serum amyloid A1 cluster	Homo sapiens	50-53
25256819-4	2015	In this study, novel VEGF-loaded heparin/poly-L-lysine (Hep/PLL) particles were developed and immobilized on a dopamine coated titanium surface.	Heparin	33-40	DNL-type zinc finger	Homo sapiens	56-59
26157187-0	2015	Erratum: Measuring Anti-Factor Xa Activity to Monitor Low-Molecular-Weight Heparin in Obesity: A Critical Review - Correction.	Heparin	75-82	coagulation factor X	Homo sapiens	24-33
25813285-9	2015	Unfractionated heparin and LMWHs attenuated the TNF-alpha-mediated induction of CXCL8 and enhanced CXCL5, CCL2, and CCL5.	Heparin	15-22	C-C motif chemokine ligand 5	Homo sapiens	116-120
25752613-3	2015	Previous studies have shown that closely related heparin octasaccharides bind to Drosophila Robo directly, and surface plasmon resonance analysis revealed that Robo1 binds more tightly to full-length unfractionated heparin.	Heparin	49-56	roundabout 1	Drosophila melanogaster	92-96
25752613-3	2015	Previous studies have shown that closely related heparin octasaccharides bind to Drosophila Robo directly, and surface plasmon resonance analysis revealed that Robo1 binds more tightly to full-length unfractionated heparin.	Heparin	49-56	roundabout 1	Drosophila melanogaster	160-165
25752613-4	2015	For the first time, we utilized electron transfer dissociation-based high spatial resolution hydroxyl radical protein footprinting to identify two separate binding sites for heparin interaction with Robo1: one binding site at the previously identified site for heparin dp8 and a second binding site at the N terminus of Robo1 that is disordered in the x-ray crystal structure.	Heparin	174-181	roundabout 1	Drosophila melanogaster	199-204
25752613-4	2015	For the first time, we utilized electron transfer dissociation-based high spatial resolution hydroxyl radical protein footprinting to identify two separate binding sites for heparin interaction with Robo1: one binding site at the previously identified site for heparin dp8 and a second binding site at the N terminus of Robo1 that is disordered in the x-ray crystal structure.	Heparin	174-181	roundabout 1	Drosophila melanogaster	320-325
25752613-7	2015	These results indicate a second low affinity binding site in the Robo-Slit complex as well as suggesting the role of the Ig2 domain of Robo1 in heparin-mediated signal transduction.	Heparin	144-151	roundabout 1	Drosophila melanogaster	65-69
25752613-7	2015	These results indicate a second low affinity binding site in the Robo-Slit complex as well as suggesting the role of the Ig2 domain of Robo1 in heparin-mediated signal transduction.	Heparin	144-151	roundabout 1	Drosophila melanogaster	135-140
25760599-5	2015	The (APLP1 E2)2-(heparin)2 complex structure revealed two distinct binding modes, with APLP1 E2 explicitly recognizing the heparin terminus but also interacting with a continuous heparin chain.	Heparin	17-24	amyloid beta precursor like protein 1	Homo sapiens	5-10
25760599-5	2015	The (APLP1 E2)2-(heparin)2 complex structure revealed two distinct binding modes, with APLP1 E2 explicitly recognizing the heparin terminus but also interacting with a continuous heparin chain.	Heparin	17-24	amyloid beta precursor like protein 1	Homo sapiens	87-92
25760599-7	2015	Terminal binding of APLP1 E2 to heparin specifically involves a structure of the nonreducing end that is very similar to heparanase-processed HS chains.	Heparin	32-39	amyloid beta precursor like protein 1	Homo sapiens	20-25
25541060-6	2015	However, when HepG2 cells overexpressing Mfn2 were treated with both heparin and RU360, there was no induction of apoptosis, decline in DeltaPsim or ER Ca(2+), or increase in intracellular ROS or mitochondrial Ca(2+).	Heparin	69-76	mitofusin 2	Homo sapiens	41-45
25534939-6	2015	Coincubation with heparin blocked LcpA-vitronectin interaction in a dose-dependent manner, strongly suggesting that binding may occur through the heparin binding domains of vitronectin.	Heparin	18-25	vitronectin	Homo sapiens	39-50
25534939-6	2015	Coincubation with heparin blocked LcpA-vitronectin interaction in a dose-dependent manner, strongly suggesting that binding may occur through the heparin binding domains of vitronectin.	Heparin	18-25	vitronectin	Homo sapiens	173-184
25534939-6	2015	Coincubation with heparin blocked LcpA-vitronectin interaction in a dose-dependent manner, strongly suggesting that binding may occur through the heparin binding domains of vitronectin.	Heparin	146-153	vitronectin	Homo sapiens	39-50
25534939-6	2015	Coincubation with heparin blocked LcpA-vitronectin interaction in a dose-dependent manner, strongly suggesting that binding may occur through the heparin binding domains of vitronectin.	Heparin	146-153	vitronectin	Homo sapiens	173-184
25463496-8	2015	The efficacy of heparin linkage was demonstrated with factor Xa anti-thrombogenic assay and platelet adhesion studies.	Heparin	16-23	coagulation factor X	Homo sapiens	54-63
25605971-3	2015	In this issue of Science Signaling, Murray and colleagues identify heparin as an ALK ligand.	Heparin	67-74	ALK receptor tyrosine kinase	Homo sapiens	81-84
25605972-0	2015	Heparin is an activating ligand of the orphan receptor tyrosine kinase ALK.	Heparin	0-7	ALK receptor tyrosine kinase	Homo sapiens	71-74
25605972-6	2015	We found that heparin is a ligand that binds specifically to the ALK extracellular domain.	Heparin	14-21	ALK receptor tyrosine kinase	Homo sapiens	65-68
25605972-7	2015	Whereas heparins with short chain lengths bound to ALK in a monovalent manner and did not activate the receptor, longer heparin chains induced ALK dimerization and activation in cultured neuroblastoma cells.	Heparin	8-16	ALK receptor tyrosine kinase	Homo sapiens	51-54
25605972-7	2015	Whereas heparins with short chain lengths bound to ALK in a monovalent manner and did not activate the receptor, longer heparin chains induced ALK dimerization and activation in cultured neuroblastoma cells.	Heparin	8-15	ALK receptor tyrosine kinase	Homo sapiens	51-54
25605972-9	2015	Moreover, antibodies that bound to the extracellular domain of ALK interfered with heparin binding and prevented heparin-mediated activation of ALK.	Heparin	83-90	ALK receptor tyrosine kinase	Homo sapiens	63-66
25605972-9	2015	Moreover, antibodies that bound to the extracellular domain of ALK interfered with heparin binding and prevented heparin-mediated activation of ALK.	Heparin	113-120	ALK receptor tyrosine kinase	Homo sapiens	63-66
25605972-9	2015	Moreover, antibodies that bound to the extracellular domain of ALK interfered with heparin binding and prevented heparin-mediated activation of ALK.	Heparin	113-120	ALK receptor tyrosine kinase	Homo sapiens	144-147
25605972-10	2015	Thus, heparin and perhaps related glycosaminoglycans function as ligands for ALK, revealing a potential mechanism for the regulation of ALK activity in vivo and suggesting an approach for developing ALK-targeted therapies for cancer.	Heparin	6-13	ALK receptor tyrosine kinase	Homo sapiens	77-80
25605972-10	2015	Thus, heparin and perhaps related glycosaminoglycans function as ligands for ALK, revealing a potential mechanism for the regulation of ALK activity in vivo and suggesting an approach for developing ALK-targeted therapies for cancer.	Heparin	6-13	ALK receptor tyrosine kinase	Homo sapiens	136-139
25605972-10	2015	Thus, heparin and perhaps related glycosaminoglycans function as ligands for ALK, revealing a potential mechanism for the regulation of ALK activity in vivo and suggesting an approach for developing ALK-targeted therapies for cancer.	Heparin	6-13	ALK receptor tyrosine kinase	Homo sapiens	136-139
26307704-1	2015	Here we report ion mobility mass spectrometry (IMMS) separation and tandem mass spectrometry (MS(2)) sequencing methods used to analyze and differentiate six synthetically produced heparin/heparan sulfate (HS)-like octasaccharide (dp8) isomeric structures.	Heparin	181-188	dipeptidyl peptidase 8	Homo sapiens	231-234
25034634-8	2015	The substrate specificity, cation requirement, and inhibition by heparin were found to be similar to native PPN1.	Heparin	65-72	endopolyphosphatase	Saccharomyces cerevisiae S288C	108-112
25181963-7	2015	Binding of pneumococcal Hic was localised to the C-terminal heparin-binding domain (HBD3) of vitronectin.	Heparin	60-67	vitronectin	Homo sapiens	93-104
25521480-9	2014	These studies aid in the design and development of heparin derivatives or analogues that can inhibit steps in virus infection and are informative regarding the HSPG/SU interaction.	Heparin	51-58	syndecan 2	Homo sapiens	160-164
25219815-0	2014	The dual binding site of angiogenin and its inhibition mechanism: the crystal structure of the rat angiogenin-heparin complex.	Heparin	110-117	angiogenin	Rattus norvegicus	25-35
25219815-0	2014	The dual binding site of angiogenin and its inhibition mechanism: the crystal structure of the rat angiogenin-heparin complex.	Heparin	110-117	angiogenin	Rattus norvegicus	99-109
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	4-11	angiogenin	Rattus norvegicus	27-37
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	4-11	angiogenin	Rattus norvegicus	151-161
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	4-11	angiogenin	Rattus norvegicus	151-161
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	54-61	angiogenin	Rattus norvegicus	27-37
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	54-61	angiogenin	Rattus norvegicus	151-161
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	54-61	angiogenin	Rattus norvegicus	151-161
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	54-61	angiogenin	Rattus norvegicus	27-37
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	54-61	angiogenin	Rattus norvegicus	151-161
25219815-1	2014	The heparin complex of rat angiogenin revealed that a heparin strand is fitted into a positively charged groove formed by the dual binding site of rat angiogenin, suggesting that cell adhesion to angiogenin is facilitated by its interaction with substrates on the cell surface and can be inhibited by heparin.	Heparin	54-61	angiogenin	Rattus norvegicus	151-161
24832962-6	2014	It is postulated that heparin binding to the CD11b receptor facilitates the internalisation of the QDs into the nucleus of THP-1 cells.	Heparin	22-29	integrin subunit alpha M	Homo sapiens	45-50
24832962-9	2014	The authors postulate that heparin binding to the CD11b receptor facilitates QD internalization to the nucleus, and the heparin layer may reduce the in vivo thrombogenic properties of quantum dots.	Heparin	27-34	integrin subunit alpha M	Homo sapiens	50-55
25242245-0	2014	Sulfated low molecular weight lignins, allosteric inhibitors of coagulation proteinases via the heparin binding site, significantly alter the active site of thrombin and factor xa compared to heparin.	Heparin	96-103	coagulation factor X	Homo sapiens	170-179
25248688-5	2014	In contrast, aPTT was significantly shorter and anti-FXa activity was significantly lower in partial-draw than in full-draw tubes collected from 46 patients receiving unfractionated heparin (UFH).	Heparin	191-194	coagulation factor X	Homo sapiens	53-56
25043635-4	2014	Heat exposed (40 C) FGF-1 exhibited binding to GroEL-biosensors, which was significantly diminished in the presence of heparin.	Heparin	119-126	heat shock protein family D (Hsp60) member 1	Homo sapiens	47-52
24842928-1	2014	Decorin-binding protein A (DbpA) of Borrelia burgdorferi mediates bacterial adhesion to heparin and dermatan sulfate associated with decorin.	Heparin	88-95	Y box protein 3	Mus musculus	27-31
24583690-10	2014	This study validates the practicality of using the A20-corlayne complex to determine the concentration of heparin in plasma.	Heparin	106-113	immunoglobulin kappa variable 1-27	Homo sapiens	51-54
24467264-9	2014	In cultured endothelial cells, human kallistatin via its heparin-binding site inhibited HMGB1-induced nuclear factor-kappaB activation and inflammatory gene expression.	Heparin	57-64	serpin family A member 4	Homo sapiens	37-48
25200044-0	2014	[The effect of low molecular heparin and urokinase on MCP-1 of acute experimental pulmonary embolism in rabbits].	Heparin	29-36	C-C motif chemokine 2	Oryctolagus cuniculus	54-59
24561026-1	2014	Heparin and low-molecular-weight heparins (LMWHs) are anticoagulant drugs that mainly inhibit the coagulation cascade by indirectly interacting with factor Xa and factor IIa (thrombin).	Heparin	0-7	coagulation factor X	Homo sapiens	149-173
24561026-1	2014	Heparin and low-molecular-weight heparins (LMWHs) are anticoagulant drugs that mainly inhibit the coagulation cascade by indirectly interacting with factor Xa and factor IIa (thrombin).	Heparin	33-41	coagulation factor X	Homo sapiens	149-173
24748467-6	2014	In this report, we use surface plasmon resonance (SPR) spectroscopy to study the impact of the GFP tagging on the binding interaction between heparin and a heparin-binding protein, the Roundabout homolog 1 (Robo1).	Heparin	142-149	azurocidin 1	Homo sapiens	156-179
24706838-5	2014	Structure-based mutational studies revealed two positive-charge clusters, near the center and apex of the hexamer, that are involved in SAA association with heparin.	Heparin	157-164	serum amyloid A1 cluster	Homo sapiens	136-139
24706838-6	2014	The binding of high-density lipoprotein involves only the apex region of SAA and can be inhibited by heparin.	Heparin	101-108	serum amyloid A1 cluster	Homo sapiens	73-76
25237354-5	2014	SERUM CONCENTRATIONS OF SAA (P: 0.02), CRP (P: 0.02) and ferritin (P: 0.01) significantly reduced in heparin group during measurements compared to baseline, circulating levels of IL-6 (P: 0.002), SAA (P: 0.009), CRP (P: 0.01) were significantly decreased in enoxaparin group.	Heparin	101-108	serum amyloid A1 cluster	Homo sapiens	24-27
25237354-5	2014	SERUM CONCENTRATIONS OF SAA (P: 0.02), CRP (P: 0.02) and ferritin (P: 0.01) significantly reduced in heparin group during measurements compared to baseline, circulating levels of IL-6 (P: 0.002), SAA (P: 0.009), CRP (P: 0.01) were significantly decreased in enoxaparin group.	Heparin	101-108	serum amyloid A1 cluster	Homo sapiens	196-199
24501198-4	2014	In this study, we have shown that TSG-6 inhibits chemokine-stimulated transendothelial migration of neutrophils via a direct interaction (KD, ~ 25 nM) between TSG-6 and the glycosaminoglycan binding site of CXCL8, which antagonizes the association of CXCL8 with heparin.	Heparin	262-269	TNF alpha induced protein 6	Homo sapiens	34-39
24501198-4	2014	In this study, we have shown that TSG-6 inhibits chemokine-stimulated transendothelial migration of neutrophils via a direct interaction (KD, ~ 25 nM) between TSG-6 and the glycosaminoglycan binding site of CXCL8, which antagonizes the association of CXCL8 with heparin.	Heparin	262-269	TNF alpha induced protein 6	Homo sapiens	159-164
24647152-3	2014	Therefore, low molecular weight heparins (LMWHs) and ultra low molecular weight heparins (ULMWHs), with lower molecular weights, higher anti-FXa activity, longer half-life times and lower incidence of adverse events than unfractionated heparin (UFH), were researched and developed.	Heparin	32-40	coagulation factor X	Homo sapiens	141-144
24048373-4	2014	Heparin releases sFlt-1 by displacing the sFlt-1 heparin-binding site from heparin sulfate proteoglycans.	Heparin	0-7	FMS-like tyrosine kinase 1	Mus musculus	17-23
24048373-4	2014	Heparin releases sFlt-1 by displacing the sFlt-1 heparin-binding site from heparin sulfate proteoglycans.	Heparin	0-7	FMS-like tyrosine kinase 1	Mus musculus	42-48
24048373-4	2014	Heparin releases sFlt-1 by displacing the sFlt-1 heparin-binding site from heparin sulfate proteoglycans.	Heparin	49-56	FMS-like tyrosine kinase 1	Mus musculus	17-23
24048373-4	2014	Heparin releases sFlt-1 by displacing the sFlt-1 heparin-binding site from heparin sulfate proteoglycans.	Heparin	49-56	FMS-like tyrosine kinase 1	Mus musculus	42-48
24048373-7	2014	More importantly, sFlt-1 levels were inversely related to atherosclerosis in CKD patients, and this correlation was more robust after heparin injection, as verified by subsequent cardiovascular events.	Heparin	134-141	FMS-like tyrosine kinase 1	Mus musculus	18-24
24048373-9	2014	Thus, the relationship between atherosclerosis and PlGF signaling, as regulated by sFlt-1, underscores the underappreciated role of heparin in sFlt-1 release.	Heparin	132-139	FMS-like tyrosine kinase 1	Mus musculus	143-149
24335992-0	2014	Anti-factor Xa assay is a superior correlate of heparin dose than activated partial thromboplastin time or activated clotting time in pediatric extracorporeal membrane oxygenation*.	Heparin	48-55	coagulation factor X	Homo sapiens	5-14
24335992-12	2014	CONCLUSIONS: The anti-Factor Xa assay correlated better with heparin dosing than activated clotting time or activated partial thromboplastin time.	Heparin	61-68	coagulation factor X	Homo sapiens	22-31
24335992-14	2014	In pediatric extracorporeal membrane oxygenation, anti-Factor Xa assay may be a more valuable monitor of heparin administration.	Heparin	105-112	coagulation factor X	Homo sapiens	55-64
24985584-9	2014	Heparin reduced the burn-induced apoptosis in the spleens (heparin treated: 8.6%+- 3.4%, P &lt; 0.005), which could be blocked by IL-1Ra.	Heparin	0-7	interleukin 1 receptor antagonist	Mus musculus	130-136
24985584-9	2014	Heparin reduced the burn-induced apoptosis in the spleens (heparin treated: 8.6%+- 3.4%, P &lt; 0.005), which could be blocked by IL-1Ra.	Heparin	59-66	interleukin 1 receptor antagonist	Mus musculus	130-136
24357866-0	2013	Effectiveness of Unfractionated Heparin in Normal Saline versus Dextrose for Achieving and Maintaining Therapeutic Anti-Factor Xa Levels in Patients with Non-ST-Elevation Acute Coronary Syndrome.	Heparin	32-39	coagulation factor X	Homo sapiens	120-129
24357866-4	2013	OBJECTIVE: To compare the effectiveness of UFH-NS and UFH-D5W for achieving and maintaining therapeutic anti-factor Xa levels in patients with non-ST-elevation acute coronary syndrome.	Heparin	43-46	coagulation factor X	Homo sapiens	109-118
24205388-5	2013	Heparin-binding domains within Fg (residues 15-66 of the beta chain, Fg beta15-66) and FN (FNI1-5, but not FNIII12-14) were involved in binding to CXCL10 and CXCL11 but not CXCL9.	Heparin	0-7	C-X-C motif chemokine ligand 10	Homo sapiens	147-153
24205388-5	2013	Heparin-binding domains within Fg (residues 15-66 of the beta chain, Fg beta15-66) and FN (FNI1-5, but not FNIII12-14) were involved in binding to CXCL10 and CXCL11 but not CXCL9.	Heparin	0-7	C-X-C motif chemokine ligand 11	Homo sapiens	158-164
23990470-9	2013	As a consequence, heparin-catalyzed inhibition of factor Xa by antithrombin is compromised by fibrinogen to a greater extent when Zn(2+) is present.	Heparin	18-25	coagulation factor X	Homo sapiens	50-59
24510786-1	2013	This unit describes the purification of extracellular vitronectin from plasma or serum by using heparin-affinity chromatography.	Heparin	96-103	vitronectin	Homo sapiens	54-65
24510786-2	2013	First, the plasma is depleted of fibronectin plus other heparin- and Sepharose-binding proteins and treated with urea to activate the heparin-binding activity of vitronectin, which is subsequently bound to a heparin affinity column and eluted.	Heparin	56-63	vitronectin	Homo sapiens	162-173
24510786-2	2013	First, the plasma is depleted of fibronectin plus other heparin- and Sepharose-binding proteins and treated with urea to activate the heparin-binding activity of vitronectin, which is subsequently bound to a heparin affinity column and eluted.	Heparin	134-141	vitronectin	Homo sapiens	162-173
23643605-6	2013	The selective binding and proliferation of human mesenchymal stem cells on heparin-based hydrogel over other hydrogels were largely mediated by integrin beta1 and selectin, and these superior characteristics were observed regardless of the presence of serum proteins in the culture medium.	Heparin	75-82	integrin subunit beta 1	Homo sapiens	144-158
23844141-9	2013	Likewise, the HSPG-binding peptide prevented apoE from binding to heparin in a dose-dependent manner, as determined by an in vitro heparin pull-down assay.	Heparin	66-73	syndecan 2	Homo sapiens	14-18
23867845-3	2013	To stimulate this process, heparin, a glycosaminoglycan involved in growth factor binding, was covalently bound to porous collagenous scaffolds (14%), with or without vascular endothelial growth factor (VEGF; 0.4 microg/mg scaffold), hepatocyte growth factor (HGF; 0.5 microg/mg scaffold) or a combination of VEGF + HGF (0.2 + 0.5 microg/mg scaffold).	Heparin	27-34	hepatocyte growth factor	Rattus norvegicus	234-258
23867845-3	2013	To stimulate this process, heparin, a glycosaminoglycan involved in growth factor binding, was covalently bound to porous collagenous scaffolds (14%), with or without vascular endothelial growth factor (VEGF; 0.4 microg/mg scaffold), hepatocyte growth factor (HGF; 0.5 microg/mg scaffold) or a combination of VEGF + HGF (0.2 + 0.5 microg/mg scaffold).	Heparin	27-34	hepatocyte growth factor	Rattus norvegicus	260-263
23867845-3	2013	To stimulate this process, heparin, a glycosaminoglycan involved in growth factor binding, was covalently bound to porous collagenous scaffolds (14%), with or without vascular endothelial growth factor (VEGF; 0.4 microg/mg scaffold), hepatocyte growth factor (HGF; 0.5 microg/mg scaffold) or a combination of VEGF + HGF (0.2 + 0.5 microg/mg scaffold).	Heparin	27-34	hepatocyte growth factor	Rattus norvegicus	316-319
24164039-0	2013	[An assay for anti-factor Xa activity of low molecular weight heparins by high performance liquid size exclusion chromatography].	Heparin	62-70	coagulation factor X	Homo sapiens	19-28
23888776-0	2013	[A novel human bone morphogenetic protein-7 variant with an enriched heparin-binding site].	Heparin	69-76	bone morphogenetic protein 7	Homo sapiens	15-43
23888776-7	2013	Substitution of the Bone morphogenetic protein-7 N-terminus by the heparin-binding site of Bone morphogenetic protein-2 was carried out to increase the heparin binding capacity of the novel protein.	Heparin	67-74	bone morphogenetic protein 7	Homo sapiens	20-48
23888776-7	2013	Substitution of the Bone morphogenetic protein-7 N-terminus by the heparin-binding site of Bone morphogenetic protein-2 was carried out to increase the heparin binding capacity of the novel protein.	Heparin	152-159	bone morphogenetic protein 7	Homo sapiens	20-48
23888776-9	2013	The novel protein as the first variant of hBMP-7 with the enriched heparin-binding site may offer more advantages in clinical use as compared to the existing commercial form.	Heparin	67-74	bone morphogenetic protein 7	Homo sapiens	42-48
23404505-5	2013	We report for the first time that VEGF-D binds heparin, and that the C-terminal propeptide significantly enhances this interaction (removal of this propeptide from full-length VEGF-D completely prevents heparin binding).	Heparin	47-54	vascular endothelial growth factor D	Mus musculus	34-40
23365078-5	2013	Our data show that the CCP6-8 region of CFH binds more strongly to heparin (a highly sulfated form of HS) than CCP19-20, and that their sulfate specificities are different.	Heparin	67-74	AGBL carboxypeptidase 4	Homo sapiens	23-29
23365078-5	2013	Our data show that the CCP6-8 region of CFH binds more strongly to heparin (a highly sulfated form of HS) than CCP19-20, and that their sulfate specificities are different.	Heparin	67-74	complement factor H	Homo sapiens	40-43
23223449-10	2013	It is thus likely that 6-O-sulfation of heparin plays important roles in regulating MCP functions.	Heparin	40-47	complement component (3b/4b) receptor 1-like	Mus musculus	84-87
23025322-8	2013	The participation of the catalytic triad (His15, Lys38, His128) in recognizing the heparin mimetic reveals, at atomic resolution, the mechanism of heparin"s inhibition of ECP"s ribonucleolytic activity.	Heparin	83-90	ribonuclease A family member 3	Homo sapiens	171-174
23025322-8	2013	The participation of the catalytic triad (His15, Lys38, His128) in recognizing the heparin mimetic reveals, at atomic resolution, the mechanism of heparin"s inhibition of ECP"s ribonucleolytic activity.	Heparin	147-154	ribonuclease A family member 3	Homo sapiens	171-174
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-81	C-X-C motif chemokine receptor 1	Homo sapiens	251-256
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	73-80	C-X-C motif chemokine receptor 1	Homo sapiens	251-256
23166320-9	2013	Evaluation of the p17 antagonist activity of a panel of biotechnological heparins derived by chemical sulfation of the Escherichia coli K5 polysaccharide revealed that the highly N,O-sulfated derivative prevents the binding of p17 to both heparin and CXCR1, thus inhibiting p17-driven chemotactic migration of human monocytes with an efficiency that is higher than those of heparin and HS.	Heparin	239-246	C-X-C motif chemokine receptor 1	Homo sapiens	251-256
23844507-2	2013	The impurities of aromatic aminoacids Phe, Tyr and elastin protein was revealed in drug of heparin.	Heparin	91-98	elastin	Homo sapiens	51-58
24151519-6	2013	Heparin treatment of B/W mice reduced the in vivo expression of CCR2, IL1 beta , and TLR7 compared to untreated B/W mice.	Heparin	0-7	toll-like receptor 7	Mus musculus	85-89
23469189-2	2013	Herein, we describe cell-binding, internalization, and targeting characteristics of a newly identified 10-residue CPP, denoted ECP(32-41), derived from the core heparin-binding motif of human eosinophil cationic protein (ECP).	Heparin	161-168	ribonuclease A family member 3	Homo sapiens	192-219
23105116-8	2012	To further evaluate the functional role of Trx-1, we used a heparin-binding EGF shedding cell model and observed that the overexpression of Trx-1 in HEK293 cells could decrease the activity of ADAM17, activated by either phorbol 12-myristate 13-acetate or EGF.	Heparin	60-67	ADAM metallopeptidase domain 17	Homo sapiens	193-199
22782595-3	2012	We found that heparin effectively rescued lethality, improved lung pathological changes, inhibited myeloperoxidase (MPO) activity, and reduced malondialdehyde (MDA) level, lung wet/dry weight ratio and Evans blue values in LPS-induced septic mice.	Heparin	14-21	myeloperoxidase	Mus musculus	99-114
22782595-3	2012	We found that heparin effectively rescued lethality, improved lung pathological changes, inhibited myeloperoxidase (MPO) activity, and reduced malondialdehyde (MDA) level, lung wet/dry weight ratio and Evans blue values in LPS-induced septic mice.	Heparin	14-21	myeloperoxidase	Mus musculus	116-119
23019343-5	2012	For interaction with heparin, the FGFs exhibit K(D) values varying between 38 nM (FGF-18) and 620 nM (FGF-9) and association rate constants spanning over 20-fold (FGF-1, 2,900,000 M(-1) s(-1) and FGF-9, 130,000 M(-1) s(-1)).	Heparin	21-28	fibroblast growth factor 18	Homo sapiens	82-88
23019343-5	2012	For interaction with heparin, the FGFs exhibit K(D) values varying between 38 nM (FGF-18) and 620 nM (FGF-9) and association rate constants spanning over 20-fold (FGF-1, 2,900,000 M(-1) s(-1) and FGF-9, 130,000 M(-1) s(-1)).	Heparin	21-28	fibroblast growth factor 9	Homo sapiens	102-107
23019343-5	2012	For interaction with heparin, the FGFs exhibit K(D) values varying between 38 nM (FGF-18) and 620 nM (FGF-9) and association rate constants spanning over 20-fold (FGF-1, 2,900,000 M(-1) s(-1) and FGF-9, 130,000 M(-1) s(-1)).	Heparin	21-28	fibroblast growth factor 9	Homo sapiens	196-201
22592843-0	2012	Livedoid vasculopathy in a patient with lupus anticoagulant and MTHFR mutation: treatment with low-molecular-weight heparin.	Heparin	116-123	methylenetetrahydrofolate reductase	Homo sapiens	64-69
22759380-6	2012	Exogenous growth differentiation factor (GDF)-9 reversed these heparin effects; furthermore, GDF9 strongly bound to heparin sepharose.	Heparin	116-123	growth differentiation factor 9	Homo sapiens	93-97
22759380-7	2012	These observations indicate that heparin binds endogenous GDF9 and disrupts interaction with heparan sulphate proteoglycan coreceptor(s), important for GDF9 signaling.	Heparin	33-40	growth differentiation factor 9	Homo sapiens	58-62
22759380-7	2012	These observations indicate that heparin binds endogenous GDF9 and disrupts interaction with heparan sulphate proteoglycan coreceptor(s), important for GDF9 signaling.	Heparin	33-40	growth differentiation factor 9	Homo sapiens	152-156
22326478-0	2012	Multiple roles of heparin in the aggregation of p25alpha.	Heparin	18-25	tubulin polymerization promoting protein	Homo sapiens	48-56
22326478-4	2012	Heparin, polyglutamate, arachidonic acid micelles, and RNA all induce p25alpha aggregation.	Heparin	0-7	tubulin polymerization promoting protein	Homo sapiens	70-78
22326478-6	2012	Bona fide fibrils are only formed at intermediate heparin concentrations, possibly because an excess of heparin binding sites blocks the inter-p25alpha contacts required for amyloid formation.	Heparin	104-111	tubulin polymerization promoting protein	Homo sapiens	143-151
22326478-10	2012	We are able to reproduce these observations in a model involving two levels of binding of p25alpha to heparin.	Heparin	102-109	tubulin polymerization promoting protein	Homo sapiens	90-98
22641378-8	2012	The heparin inhibition step identified "reactive" samples that were associated with clinical scores and SRA release indistinguishable from the "negative" result groups, confirming that this step further improves specificity of the test.	Heparin	4-11	steroid receptor RNA activator 1	Homo sapiens	104-107
22518847-1	2012	Factor-Xa assembly into the prothrombinase complex decreases its availability for inhibition by antithrombin + unfractionated heparin (AT + UFH).	Heparin	126-133	coagulation factor X	Homo sapiens	0-9
22518847-1	2012	Factor-Xa assembly into the prothrombinase complex decreases its availability for inhibition by antithrombin + unfractionated heparin (AT + UFH).	Heparin	126-133	coagulation factor X	Homo sapiens	28-42
22518847-11	2012	Overall, the results suggest that covalent linkage between AT-heparin assists access and neutralization of complexed Xa, with concomitant inhibition of prothrombinase function compared with conventional non-conjugated heparin.	Heparin	62-69	coagulation factor X	Homo sapiens	152-166
22453684-4	2012	The conformational activation of antithrombin by heparin is a critical step in the inhibition of factor Xa by antithrombin.	Heparin	49-56	coagulation factor X	Homo sapiens	97-106
22453684-5	2012	Despite heparin being the most potent physiological activator which enhances the otherwise very lethargic antithrombin inhibition of factor Xa by approximately 1,000-fold, the conventional heparin therapy poses serious complications because of heparin"s polyanionic nature and its cross-reactivity.	Heparin	8-15	coagulation factor X	Homo sapiens	133-142
22453684-6	2012	A number of attempts have been carried out in designing alternative non-heparin based conformational activators of antithrombin for factor Xa inhibition.	Heparin	72-79	coagulation factor X	Homo sapiens	132-141
22330023-11	2012	JNK and p38 MAPK were activated under heparin in TA and SOL of WT (P &lt; 0.05) but not in muscles of tlr2 and tlr4 mice.	Heparin	38-45	mitogen-activated protein kinase 8	Mus musculus	0-3
22684947-5	2012	In our study, a recombinant plasmid expressing IP-10 (pVITRO-IP-10)             was constructed, and biodegradable cationic heparin-polyethyleneimine (HPEI) nanogels             were prepared to deliver pVITRO-IP-10 into SKOV3 human ovarian cancer cells.	Heparin	124-131	C-X-C motif chemokine ligand 10	Homo sapiens	47-52
22684947-5	2012	In our study, a recombinant plasmid expressing IP-10 (pVITRO-IP-10)             was constructed, and biodegradable cationic heparin-polyethyleneimine (HPEI) nanogels             were prepared to deliver pVITRO-IP-10 into SKOV3 human ovarian cancer cells.	Heparin	124-131	C-X-C motif chemokine ligand 10	Homo sapiens	54-66
22871410-0	2012	[Therapeutic effects of unfractionated heparin on lipopolysaccharide-activated matrix metalloproteinase-9 and tissue inhibitors of metalloproteinase-1 in endothelial cells].	Heparin	39-46	matrix metallopeptidase 9	Homo sapiens	79-105
22871410-7	2012	While as UFH pretreatment could significantly down-regulated the mRNA expressions of MMP-9 and TIMP-1 (UFH 0.1 U/ml group MMP-9 mRNA: 2.74+-0.30, TIMP-1 mRNA: 2.96+-0.13; UFH 1 U/ml group MMP-9 mRNA: 3.08+-0.48, TIMP-1 mRNA: 2.93+-0.27, all P&lt;0.05).	Heparin	9-12	matrix metallopeptidase 9	Homo sapiens	85-90
22871410-7	2012	While as UFH pretreatment could significantly down-regulated the mRNA expressions of MMP-9 and TIMP-1 (UFH 0.1 U/ml group MMP-9 mRNA: 2.74+-0.30, TIMP-1 mRNA: 2.96+-0.13; UFH 1 U/ml group MMP-9 mRNA: 3.08+-0.48, TIMP-1 mRNA: 2.93+-0.27, all P&lt;0.05).	Heparin	9-12	matrix metallopeptidase 9	Homo sapiens	122-127
22871410-7	2012	While as UFH pretreatment could significantly down-regulated the mRNA expressions of MMP-9 and TIMP-1 (UFH 0.1 U/ml group MMP-9 mRNA: 2.74+-0.30, TIMP-1 mRNA: 2.96+-0.13; UFH 1 U/ml group MMP-9 mRNA: 3.08+-0.48, TIMP-1 mRNA: 2.93+-0.27, all P&lt;0.05).	Heparin	9-12	matrix metallopeptidase 9	Homo sapiens	122-127
22471560-5	2012	Unchanged FH structures that are bivalently cross-linked at SCR-7 and SCR-20 with heparin explained the sedimentation coefficients of the FH-heparin oligomers.	Heparin	141-148	complement factor H	Homo sapiens	10-12
22471560-5	2012	Unchanged FH structures that are bivalently cross-linked at SCR-7 and SCR-20 with heparin explained the sedimentation coefficients of the FH-heparin oligomers.	Heparin	141-148	complement factor H	Homo sapiens	138-140
22471560-6	2012	The X-ray radius of gyration, R(G), of FH in the presence of heparin fragments 18-36 monosaccharide units long increased significantly from 10.4 to 11.7 nm, and the maximum lengths of FH increased from 35 to 40 nm, confirming that large compact oligomers had formed.	Heparin	61-68	complement factor H	Homo sapiens	39-41
22471560-7	2012	Surface plasmon resonance of immobilized heparin with full-length FH gave K(d) values of 1-3 muM, and similar but weaker K(d) values of 4-20 muM for the SCR-6/8 and SCR-16/20 fragments, confirming co-operativity between the two binding sites.	Heparin	41-48	complement factor H	Homo sapiens	66-68
22547069-4	2012	Here, we identify the modifications and length of the heparin polymer that are required for binding and endocytosis by both human Stabilin receptors: Stabilin-2 and its homolog Stabilin-1 (also found in liver endothelium).	Heparin	54-61	stabilin 1	Homo sapiens	177-187
21080209-0	2012	Modulating the interaction of CXCR4 and CXCL12 by low-molecular-weight heparin inhibits hepatic metastasis of colon cancer.	Heparin	71-78	C-X-C motif chemokine receptor 4	Homo sapiens	30-35
22239992-0	2012	Interleukin-10 promoter microsatellite polymorphisms influence the immune response to heparin and the risk of heparin-induced thrombocytopenia.	Heparin	86-93	interleukin 10	Homo sapiens	0-14
22239992-0	2012	Interleukin-10 promoter microsatellite polymorphisms influence the immune response to heparin and the risk of heparin-induced thrombocytopenia.	Heparin	110-117	interleukin 10	Homo sapiens	0-14
21749932-5	2012	The apoA-I binding to ABCA1 and the cross-linking between them were inhibited by the highly charged molecules heparin and poly-L-lysine.	Heparin	110-117	ATP binding cassette subfamily A member 1	Homo sapiens	22-27
21930168-1	2012	A targetable, heparin-triggered release system for tissue plasminogen activator (tPA) was designed to prevent the excessive "lytic" state associated with the current tPA therapy for acute thrombotic conditions, such as myocardial infarction (MI).	Heparin	14-21	chromosome 20 open reading frame 181	Homo sapiens	51-79
21930168-1	2012	A targetable, heparin-triggered release system for tissue plasminogen activator (tPA) was designed to prevent the excessive "lytic" state associated with the current tPA therapy for acute thrombotic conditions, such as myocardial infarction (MI).	Heparin	14-21	chromosome 20 open reading frame 181	Homo sapiens	81-84
21930168-1	2012	A targetable, heparin-triggered release system for tissue plasminogen activator (tPA) was designed to prevent the excessive "lytic" state associated with the current tPA therapy for acute thrombotic conditions, such as myocardial infarction (MI).	Heparin	14-21	chromosome 20 open reading frame 181	Homo sapiens	166-169
21930168-2	2012	The strategy is, upon target accumulation, to trigger tPA release from a prodrug construct by a usual heparin dose.	Heparin	102-109	chromosome 20 open reading frame 181	Homo sapiens	54-57
21930168-3	2012	A relatively inactive form of tPA was constructed by conjugating tPA with low-molecular weight heparin followed by complexation with albumin-protamine conjugate, termed "camouflage".	Heparin	95-102	chromosome 20 open reading frame 181	Homo sapiens	30-33
21930168-3	2012	A relatively inactive form of tPA was constructed by conjugating tPA with low-molecular weight heparin followed by complexation with albumin-protamine conjugate, termed "camouflage".	Heparin	95-102	chromosome 20 open reading frame 181	Homo sapiens	65-68
21930168-5	2012	The prodrug construct of tPA significantly masked the enzymatic activity, which was fully recovered upon heparin addition.	Heparin	105-112	chromosome 20 open reading frame 181	Homo sapiens	25-28
21930168-6	2012	The camouflaged tPA was stable in human blood for at least 30min and was able to trigger enzyme activation in vitro at heparin level of 0.4U/mL.	Heparin	119-126	chromosome 20 open reading frame 181	Homo sapiens	16-19
21930168-8	2012	This proof-of-principle study suggests that the activity of the tPA prodrug construct can be triggered at the thrombus site at therapeutic heparin concentration conjunctively used for MI with reduced bleeding risk.	Heparin	139-146	chromosome 20 open reading frame 181	Homo sapiens	64-67
22056285-6	2012	More heparin reacted to chitosan nanofiber in gradient CS/PCL than in uniform CS/PCL nanofibrous scaffolds.	Heparin	5-12	fms related receptor tyrosine kinase 4	Homo sapiens	58-61
22056285-6	2012	More heparin reacted to chitosan nanofiber in gradient CS/PCL than in uniform CS/PCL nanofibrous scaffolds.	Heparin	5-12	fms related receptor tyrosine kinase 4	Homo sapiens	81-84
22089943-0	2012	Effects of four commercially available factor Xa proteins on the fluorogenic anti-factor Xa assay when monitoring unfractionated heparin.	Heparin	129-136	coagulation factor X	Homo sapiens	82-91
22916091-3	2012	Among them, compound 8 (2-butyl-5-chloro-3-(4-nitro-benzyl)-3H-imidazole-4-carbaldehyde) was identified as a significant binding molecule for the heparin-binding domain of VEGF, determined by high-throughput-surface plasmon resonance assay.	Heparin	146-153	vascular endothelial growth factor A	Mus musculus	172-176
22916091-6	2012	Molecular docking studies predicted that compound 8 binds at the heparin binding domain of VEGF through strong hydrogen bonding with Lys-30 and Gln-20 amino acid residues, and consistent with the prediction, compound 8 inhibited binding of VEGF to immobilized heparin.	Heparin	65-72	vascular endothelial growth factor A	Mus musculus	91-95
22916091-6	2012	Molecular docking studies predicted that compound 8 binds at the heparin binding domain of VEGF through strong hydrogen bonding with Lys-30 and Gln-20 amino acid residues, and consistent with the prediction, compound 8 inhibited binding of VEGF to immobilized heparin.	Heparin	65-72	vascular endothelial growth factor A	Mus musculus	240-244
22916091-6	2012	Molecular docking studies predicted that compound 8 binds at the heparin binding domain of VEGF through strong hydrogen bonding with Lys-30 and Gln-20 amino acid residues, and consistent with the prediction, compound 8 inhibited binding of VEGF to immobilized heparin.	Heparin	260-267	vascular endothelial growth factor A	Mus musculus	91-95
22916091-6	2012	Molecular docking studies predicted that compound 8 binds at the heparin binding domain of VEGF through strong hydrogen bonding with Lys-30 and Gln-20 amino acid residues, and consistent with the prediction, compound 8 inhibited binding of VEGF to immobilized heparin.	Heparin	260-267	vascular endothelial growth factor A	Mus musculus	240-244
21852056-0	2011	Quantification of unfractionated heparin in human plasma and whole blood by means of novel fluorogenic anti-FXa assays.	Heparin	33-40	coagulation factor X	Homo sapiens	108-111
21852056-1	2011	Novel and sensitive plate-based fluorogenic anti-factor Xa (FXa) assays were investigated to quantify unfractionated heparin (UFH) in human plasma and whole blood within the therapeutic ranges of 0-1.6 U/mL and 0-0.8 U/mL, respectively.	Heparin	117-124	coagulation factor X	Homo sapiens	60-63
21852056-2	2011	Two fluorogenic anti-FXa assay methods were defined for low (0-0.6 U/mL) and high (0.6-1.2 U/mL) pharmacologically relevant UFH concentration ranges in pooled human plasma.	Heparin	124-127	coagulation factor X	Homo sapiens	21-24
21882808-1	2011	A water-soluble pyrene-based butterfly shaped conjugated oligoelectrolyte (TFP) is synthesized and integrated with graphene oxide (GO) to form a label-free assay for heparin detection.	Heparin	166-173	inhibitor of carbonic anhydrase pseudogene	Homo sapiens	75-78
21882808-3	2011	Addition of heparin into TFP solution significantly minimizes the fluorescence quenching of GO toward TFP, which is less effective for the heparin analogues, such as hyaluronic acid and chondroitin 4-sulfate.	Heparin	12-19	inhibitor of carbonic anhydrase pseudogene	Homo sapiens	25-28
21882808-3	2011	Addition of heparin into TFP solution significantly minimizes the fluorescence quenching of GO toward TFP, which is less effective for the heparin analogues, such as hyaluronic acid and chondroitin 4-sulfate.	Heparin	12-19	inhibitor of carbonic anhydrase pseudogene	Homo sapiens	102-105
21882808-3	2011	Addition of heparin into TFP solution significantly minimizes the fluorescence quenching of GO toward TFP, which is less effective for the heparin analogues, such as hyaluronic acid and chondroitin 4-sulfate.	Heparin	139-146	inhibitor of carbonic anhydrase pseudogene	Homo sapiens	25-28
21882808-5	2011	Moreover, the linear light-up response of the TFP/GO integrated assay enables heparin quantification in the range of 0-1.76 U/mL with a limit of detection of 0.046 U/mL, which is practical for heparin monitoring during postoperative and long-term care.	Heparin	78-85	inhibitor of carbonic anhydrase pseudogene	Homo sapiens	46-49
21882808-5	2011	Moreover, the linear light-up response of the TFP/GO integrated assay enables heparin quantification in the range of 0-1.76 U/mL with a limit of detection of 0.046 U/mL, which is practical for heparin monitoring during postoperative and long-term care.	Heparin	193-200	inhibitor of carbonic anhydrase pseudogene	Homo sapiens	46-49
21767328-11	2011	Only 28% of the 32 cases treated with low molecular weight heparin titrated dosing to a goal anti-FXa level 0.5-1.	Heparin	59-66	coagulation factor X	Homo sapiens	98-101
21593136-5	2011	The data indicate that at low concentrations, soluble heparin modulates CXCR4/CXCL12 interaction and at high concentrations, abrogates binding.	Heparin	54-61	C-X-C motif chemokine receptor 4	Homo sapiens	72-77
21447033-5	2011	Recently, we have shown that ephrin-B3 binds to a sulphated cell surface receptor on HEK293T cells and that this binding can be blocked with heparin.	Heparin	141-148	ephrin B3	Homo sapiens	29-38
21447033-6	2011	Ephrin-B3 binding to B lymphocytes is partially affected by heparin, and a basic amino acid in the extracellular juxtamembrane region, Arg-188, is here shown to be involved in this binding.	Heparin	60-67	ephrin B3	Homo sapiens	0-9
21642433-0	2011	Heparin impairs angiogenesis through inhibition of microRNA-10b.	Heparin	0-7	microRNA 10b	Homo sapiens	51-63
21642433-3	2011	Here, we show that microRNA-10b (miR-10b) is down-regulated by heparin and up-regulated by thrombin in human microvascular endothelial cells (HMEC-1).	Heparin	63-70	microRNA 10b	Homo sapiens	19-31
21642433-3	2011	Here, we show that microRNA-10b (miR-10b) is down-regulated by heparin and up-regulated by thrombin in human microvascular endothelial cells (HMEC-1).	Heparin	63-70	microRNA 10b	Homo sapiens	33-40
21642433-7	2011	Using quartz crystal microbalance analysis, we show that heparin binds to thrombin, thereby inhibiting thrombin-induced expression of Twist and miR-10b.	Heparin	57-64	microRNA 10b	Homo sapiens	144-151
21642433-9	2011	Interestingly, we find that heparin attenuates miR-10b expression and induces HoxD10 expression in vivo to inhibit angiogenesis and impair the growth of MDA-MB-231 tumor xenografts.	Heparin	28-35	microRNA 10b	Homo sapiens	47-54
21566135-0	2011	TSG-6 protein, a negative regulator of inflammatory arthritis, forms a ternary complex with murine mast cell tryptases and heparin.	Heparin	123-130	tumor necrosis factor alpha induced protein 6	Mus musculus	0-5
21566135-6	2011	Whereas TSG-6 was broadly detectable in arthritic synovial tissue, the highest level of TSG-6 was co-localized with tryptases in the heparin-containing secretory granules of mast cells.	Heparin	133-140	tumor necrosis factor alpha induced protein 6	Mus musculus	88-93
21566135-7	2011	In vitro, TSG-6 formed complexes with the tryptases murine mast cell protease-6 and -7 via either heparin or HA.	Heparin	98-105	tumor necrosis factor alpha induced protein 6	Mus musculus	10-15
21672195-9	2011	HD5 and HD6 blocked anti-HIV activities of soluble glycosaminoglycans including heparin, chondroitin sulfate, and dextran sulfate.	Heparin	80-87	defensin alpha 6	Homo sapiens	8-11
21276692-0	2011	Low molecular weight (LMW) heparin inhibits injury-induced femoral artery remodeling in mouse via upregulating CD44 expression.	Heparin	27-34	CD44 antigen	Mus musculus	111-115
21276692-13	2011	In vitro, LMW heparin decreased mouse VSMC growth capacity and upregulated its CD44 expression simultaneously in a dose-dependent and time-dependent manner, which could be partially blocked by CD44 inhibitor.	Heparin	14-21	CD44 antigen	Mus musculus	79-83
21276692-13	2011	In vitro, LMW heparin decreased mouse VSMC growth capacity and upregulated its CD44 expression simultaneously in a dose-dependent and time-dependent manner, which could be partially blocked by CD44 inhibitor.	Heparin	14-21	CD44 antigen	Mus musculus	193-197
21422279-10	2011	The effect of heparin on TTR fibril formation was further demonstrated in a Drosophila model that overexpresses TTR.	Heparin	14-21	transthyretin	Homo sapiens	25-28
21422279-10	2011	The effect of heparin on TTR fibril formation was further demonstrated in a Drosophila model that overexpresses TTR.	Heparin	14-21	transthyretin	Homo sapiens	112-115
21422279-11	2011	Heparin was colocalized with TTR deposits in the head of the flies reared on heparin-supplemented medium, whereas no heparin was detected in the nontreated flies.	Heparin	0-7	transthyretin	Homo sapiens	29-32
21422279-11	2011	Heparin was colocalized with TTR deposits in the head of the flies reared on heparin-supplemented medium, whereas no heparin was detected in the nontreated flies.	Heparin	77-84	transthyretin	Homo sapiens	29-32
20558775-5	2011	We found that: (1) hypoxia increased ROCK expression in mice and PASMCs; (2) overexpression of RhoA diminished the inhibitory effect of heparin on PASMC proliferation and down-regulated p27 expression; and (3) overexpression of GEF-H1 negated heparin inhibition of PASMC proliferation, which was accompanied by increased GTP-RhoA and decreased p27.	Heparin	136-143	cyclin-dependent kinase inhibitor 1B	Mus musculus	186-189
20558775-5	2011	We found that: (1) hypoxia increased ROCK expression in mice and PASMCs; (2) overexpression of RhoA diminished the inhibitory effect of heparin on PASMC proliferation and down-regulated p27 expression; and (3) overexpression of GEF-H1 negated heparin inhibition of PASMC proliferation, which was accompanied by increased GTP-RhoA and decreased p27.	Heparin	136-143	cyclin-dependent kinase inhibitor 1B	Mus musculus	344-347
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	cyclin-dependent kinase inhibitor 1B	Mus musculus	200-203
20558775-6	2011	This study demonstrates that the RhoA/ROCK pathway plays an important role in heparin inhibition on PASMC proliferation, and reveals that heparin inhibits PASMC proliferation through GEF-H1/RhoA/ROCK/p27 signaling pathway, by down-regulating GEF-H1, RhoA, and ROCK, and then up-regulating p27.	Heparin	138-145	cyclin-dependent kinase inhibitor 1B	Mus musculus	289-292
21487375-8	2011	Combined thrombolytic therapy with urokinase and tissue plasminogen activator, in association with low-dose heparin, allows the use of lower drug doses, less therapy"s duration and a rapid resolution of thrombus.	Heparin	108-115	chromosome 20 open reading frame 181	Homo sapiens	49-77
21193389-8	2011	Examination of chondroitin/dermatan sulfate catabolic enzymes showed that heparan sulfate and heparin can inhibit iduronate 2-sulfatase.	Heparin	94-101	iduronate 2-sulfatase	Homo sapiens	114-135
21147501-0	2011	The enhancement of VEGF-mediated angiogenesis by polycaprolactone scaffolds with surface cross-linked heparin.	Heparin	102-109	vascular endothelial growth factor A	Mus musculus	19-23
21227626-7	2011	The results showed that low-molecular-weight heparin oral colon-specific delivery capsule significantly decreased the serum levels of TNF-alpha, IL-6 as well as FXa, while increased the expression of Musashi-1 in colon compared with acetic acid-induced ulcerative colitis model group.	Heparin	45-52	musashi RNA-binding protein 1	Mus musculus	200-209
21386996-0	2011	PKCalpha and PKCdelta regulate ADAM17-mediated ectodomain shedding of heparin binding-EGF through separate pathways.	Heparin	70-77	ADAM metallopeptidase domain 17	Homo sapiens	31-37
21556121-8	2011	The internalisation of HRG was inhibited by the addition of heparin.	Heparin	60-67	histidine rich glycoprotein	Homo sapiens	23-26
20971949-2	2011	HRG has a multidomain structure that allows the molecule to interact with many ligands, including heparin, phospholipids, plasminogen, fibrinogen, immunoglobulin G, C1q, heme, and Zn2(+).	Heparin	98-105	histidine rich glycoprotein	Homo sapiens	0-3
21262445-8	2011	In subsequent studies we found that sFlt1 is a strong heparin binder: this capability enables it to stay attached to blood vessels and to the placenta.	Heparin	54-61	FMS-like tyrosine kinase 1	Mus musculus	36-41
21262445-9	2011	Ex vivo, sFlt1 can be heparin displaced to medium from aortic segments and placental villi.	Heparin	22-29	FMS-like tyrosine kinase 1	Mus musculus	9-14
21262445-10	2011	In vivo, pregnant women treated with the low molecular weight heparin (LMWH) have elevated sFlt1 levels in their circulations.	Heparin	62-69	FMS-like tyrosine kinase 1	Mus musculus	91-96
21076043-3	2011	Treatment of mice with pharmacologic doses of heparin inhibited liver hepcidin mRNA expression and SMAD phosphorylation, reduced spleen iron concentration, and increased serum iron.	Heparin	46-53	hepcidin antimicrobial peptide	Mus musculus	70-78
20980681-2	2011	We found that CXCL4L1 has lower affinity for heparin and chondroitin sulfate-E than platelet factor-4 (CXCL4) and showed that CXCL10 and CXCL4L1 could displace each other on microvascular endothelial cells.	Heparin	45-52	C-X-C motif chemokine ligand 10	Homo sapiens	126-132
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	C-C motif chemokine ligand 5	Homo sapiens	292-298
20827464-1	2011	The preparation and characterization of heparin-immobilized microspheres which were used to bind acidic fibroblast growth factor (aFGF), vascular endothelial growth factor (VEGF), monocyte chemoattractant protein 1 (MCP-1/CCL2), and regulation upon activation normal T cell express sequence (RANTES/CCL5) is described.	Heparin	40-47	C-C motif chemokine ligand 5	Homo sapiens	299-303
20827464-6	2011	These heparin-immobilized microspheres exhibited broad dynamic ranges for binding to the four cytokines (aFGF, 1.0-1,000 ng/mL; VEGF, 0.5-1,000 ng/mL; CCL2, 1.95-1,000 ng/mL; CCL5, 1.95-500 ng/mL).	Heparin	6-13	C-C motif chemokine ligand 5	Homo sapiens	175-179
20953779-0	2011	Combination of a two-step fluorescence assay and a two-step anti-Factor Xa assay for detection of heparin falsifications and protein in heparins.	Heparin	98-105	coagulation factor X	Homo sapiens	65-74
20953779-0	2011	Combination of a two-step fluorescence assay and a two-step anti-Factor Xa assay for detection of heparin falsifications and protein in heparins.	Heparin	136-144	coagulation factor X	Homo sapiens	65-74
20925654-2	2011	In the present paper, we provide data showing that ephrin-B3 binds a sulfated cell-surface protein on HEK-293T (human embryonic kidney-293 cells expressing the large T-antigen of simian virus 40) and HeLa cells, a binding that is nearly completely blocked by treatment of these cell lines with chlorate or heparinase, or by addition of the heavily sulfated glycosaminoglycan heparin.	Heparin	306-313	ephrin B3	Homo sapiens	51-60
20925654-5	2011	Site-directed mutagenesis analysis revealed that Arg178 and Lys179 are important for heparin binding of ephrin-B3 and also for ephrin-B3 binding to cells.	Heparin	85-92	ephrin B3	Homo sapiens	104-113
21467630-1	2011	Plasma hyaluronan-binding protein (PHBP), a serine protease that can activate coagulation factor VII and prourokinase, circulates in a single-chain form (pro-PHBP) and autoproteolytically converts to an active two-chain form with the aid of an effector such as spermidine and heparin.	Heparin	276-283	hyaluronan binding protein 2	Homo sapiens	0-33
21467630-1	2011	Plasma hyaluronan-binding protein (PHBP), a serine protease that can activate coagulation factor VII and prourokinase, circulates in a single-chain form (pro-PHBP) and autoproteolytically converts to an active two-chain form with the aid of an effector such as spermidine and heparin.	Heparin	276-283	hyaluronan binding protein 2	Homo sapiens	35-39
21720505-0	2011	Controlled release of chitosan/heparin nanoparticle-delivered VEGF enhances regeneration of decellularized tissue-engineered scaffolds.	Heparin	31-38	vascular endothelial growth factor A	Mus musculus	62-66
21720505-5	2011	The scaffolds immobilized with heparin/chitosan nanoparticles exhibited highly effective localization and sustained release of VEGF for several weeks in vitro.	Heparin	31-38	vascular endothelial growth factor A	Mus musculus	127-131
21720505-7	2011	Importantly, utilization of heparin/chitosan nanoparticles to localize VEGF significantly increased fibroblast infiltration, extracellular matrix production, and accelerated vascularization in mouse subcutaneous implantation model in vivo.	Heparin	28-35	vascular endothelial growth factor A	Mus musculus	71-75
20213669-0	2011	Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site.	Heparin	43-50	ribonuclease A family member 3	Homo sapiens	0-27
20213669-0	2011	Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site.	Heparin	43-50	ribonuclease A family member 3	Homo sapiens	29-32
20213669-4	2011	ECP presents a high affinity for heparin and this property might be crucial for its immunomodulating properties, antipathogen action, and its toxicity against eukaryotic cells.	Heparin	33-40	ribonuclease A family member 3	Homo sapiens	0-3
20213669-6	2011	We have now proven that ECP heparin binding affinity depends on its RNase catalytic site, as the enzymatic activity is blocked by heparin.	Heparin	28-35	ribonuclease A family member 3	Homo sapiens	24-27
20213669-6	2011	We have now proven that ECP heparin binding affinity depends on its RNase catalytic site, as the enzymatic activity is blocked by heparin.	Heparin	130-137	ribonuclease A family member 3	Homo sapiens	24-27
20213669-7	2011	We have applied molecular modeling to analyze ECP binding to heparin representative probes, and identified protein residues at the catalytic and substrate binding sites that could contribute to the interaction.	Heparin	61-68	ribonuclease A family member 3	Homo sapiens	46-49
20213669-8	2011	ECP affinity for heparin and other negatively charged glycosaminoglycans (GAGs) can explain not only its binding to the eukaryote cells glycocalix but also the reported high affinity for the specific carbohydrates at bacteria cell wall, promoting its antimicrobial action.	Heparin	17-24	ribonuclease A family member 3	Homo sapiens	0-3
21150227-0	2011	Effects of nadroparin, enoxaparin, and unfractionated heparin on endogenous formation of factor Xa and IIa and on thrombelastometry profiles in cord versus adult blood.	Heparin	54-61	coagulation factor X	Homo sapiens	89-98
21150227-4	2011	METHODS: The effects of nadroparin, enoxaparin, or UH on endogenous formation of FXa or FIIa was investigated in tissue factor-activated PPP using a subsampling technique and chromogenic substrates.	Heparin	51-53	coagulation factor X	Homo sapiens	81-84
22180365-2	2011	We have previously reported that heparin competitively inhibits the binding activity of bone morphogenic protein-2 (BMP-2) to BMP and the BMP receptor (BMPR) and suppresses BMP-2 osteogenic activity.	Heparin	33-40	bone morphogenetic protein receptor, type 1A	Mus musculus	152-156
22180365-7	2011	In addition, 72 h of treatment with heparin enhanced the mRNA expression of runx2 and osterix in BMP-2-stimulated MC3T3-E1 cells.	Heparin	36-43	Sp7 transcription factor 7	Mus musculus	86-93
21205210-0	2010	WITHDRAWN: Interaction of Human Seminal Plasma beta-Microseminoprotein with Heparin: Binding Mechanism and Thermodynamic Parameters.	Heparin	76-83	microseminoprotein beta	Homo sapiens	47-70
21210971-0	2010	How does heparin prevent the pH inactivation of cathepsin B?	Heparin	9-16	cathepsin B	Homo sapiens	48-59
21210971-5	2010	However, the molecular mechanism of stabilization is not well understood, indicating the need for more detailed structural and dynamic studies in order to clarify the influence of pH and heparin binding on catB stability.	Heparin	187-194	cathepsin B	Homo sapiens	206-210
21210971-12	2010	Essential dynamics analysis revealed that heparin binding modulates large amplitude motions promoting rearrangement of contacts between catB domains, thus favoring the maintenance of helical content as well as active site stability.	Heparin	42-49	cathepsin B	Homo sapiens	136-140
21210971-14	2010	Moreover, we propose an allosteric role for heparin in the regulation of catB stability in such a manner that the restriction of enzyme flexibility would allow the establishment of stronger contacts and thus the maintenance of overall structure.	Heparin	44-51	cathepsin B	Homo sapiens	73-77
20960494-0	2010	Spin-labeled heparins as polarizing agents for dynamic nuclear polarization.	Heparin	13-21	spindlin 1	Homo sapiens	0-4
20960494-1	2010	A potentially biocompatible class of spin-labeled macromolecules, spin-labeled (SL) heparins, and their use as nuclear magnetic resonance (NMR) signal enhancers are introduced.	Heparin	84-92	spindlin 1	Homo sapiens	66-70
20960494-5	2010	A striking result is that for spin-labeled heparins, the off-resonant electron paramagnetic resonance (EPR) hyperfine lines contribute a non-negligible part to the total saturation, even in the absence of Heisenberg spin exchange (HSE) and electron spin-nuclear spin relaxation (T(1ne)).	Heparin	43-51	spindlin 1	Homo sapiens	30-34
20960494-5	2010	A striking result is that for spin-labeled heparins, the off-resonant electron paramagnetic resonance (EPR) hyperfine lines contribute a non-negligible part to the total saturation, even in the absence of Heisenberg spin exchange (HSE) and electron spin-nuclear spin relaxation (T(1ne)).	Heparin	43-51	spindlin 1	Homo sapiens	216-220
20960494-5	2010	A striking result is that for spin-labeled heparins, the off-resonant electron paramagnetic resonance (EPR) hyperfine lines contribute a non-negligible part to the total saturation, even in the absence of Heisenberg spin exchange (HSE) and electron spin-nuclear spin relaxation (T(1ne)).	Heparin	43-51	spindlin 1	Homo sapiens	216-220
20960494-5	2010	A striking result is that for spin-labeled heparins, the off-resonant electron paramagnetic resonance (EPR) hyperfine lines contribute a non-negligible part to the total saturation, even in the absence of Heisenberg spin exchange (HSE) and electron spin-nuclear spin relaxation (T(1ne)).	Heparin	43-51	spindlin 1	Homo sapiens	216-220
20388016-6	2010	Our data suggest that TIMP-3 interacts with heparan sulfate and heparan sulfate proteoglycans and to a lesser extent with heparin and chondroitin sulfate.	Heparin	122-129	TIMP metallopeptidase inhibitor 3	Homo sapiens	22-28
20847691-4	2010	RECENT FINDINGS: Oral administration, predictable anticoagulant responses, low potential for drug-drug interactions render direct thrombin and factor Xa inhibitors good candidates to replace UFH, LMWH and fondaparinux for VTE prophylaxis.	Heparin	191-194	coagulation factor X	Homo sapiens	143-152
20685328-7	2010	Binding of a specific heparin or heparan sulfate pentasaccharide to antithrombin induces allosteric activating changes that mitigate the unfavorable interactions and promote template bridging of the serpin and proteinase.	Heparin	22-29	endogenous retrovirus group K member 10	Homo sapiens	210-220
20975989-8	2010	The binding of VEGF-A and HUVECs was reduced under a high concentration of heparin or ocular fluid compared to lower concentrations of heparin.	Heparin	75-82	vascular endothelial growth factor A	Mus musculus	15-21
20975989-8	2010	The binding of VEGF-A and HUVECs was reduced under a high concentration of heparin or ocular fluid compared to lower concentrations of heparin.	Heparin	135-142	vascular endothelial growth factor A	Mus musculus	15-21
20975989-9	2010	In vitro assays demonstrated that the ocular fluid or soluble heparan sulfate or heparin inhibited the binding of VEGF-A and immobilized heparin or VEGF receptor 2 but not VEGF receptor 1.	Heparin	81-88	vascular endothelial growth factor A	Mus musculus	114-120
20975989-9	2010	In vitro assays demonstrated that the ocular fluid or soluble heparan sulfate or heparin inhibited the binding of VEGF-A and immobilized heparin or VEGF receptor 2 but not VEGF receptor 1.	Heparin	81-88	vascular endothelial growth factor A	Mus musculus	114-118
20805441-7	2010	Furthermore, unfractionated heparin induced activation of focal adhesion protein kinase, Src, and paxillin.	Heparin	28-35	SRC proto-oncogene, non-receptor tyrosine kinase	Rattus norvegicus	89-92
20524207-6	2010	Exogenous heparin was also found to play a cross-bridging role between VEGF-A(165) and putative heparin-binding sites within its cognate receptor, VEGFR2 when they were examined in isolation.	Heparin	10-17	kinase insert domain receptor	Homo sapiens	147-153
20524207-6	2010	Exogenous heparin was also found to play a cross-bridging role between VEGF-A(165) and putative heparin-binding sites within its cognate receptor, VEGFR2 when they were examined in isolation.	Heparin	96-103	kinase insert domain receptor	Homo sapiens	147-153
20457258-4	2010	Identification of approximately 15 nm structures as the cytoplasmic domain of InsP(3)R was indirectly supported by a marked increase in their frequency after transient transfections with cDNAs for rat types 1 and 3 InsP(3)R, and directly confirmed by gold labeling either with heparin or a specific anti-InsP(3)R antibody.	Heparin	277-284	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	78-86
24323522-0	2010	A Pilot Trial of Low-Dose Intravenous Abciximab and Unfractionated Heparin for Acute Ischemic Stroke: Translating GP IIb/IIIa Receptor Inhibition to Clinical Practice.	Heparin	67-74	integrin subunit alpha 2b	Homo sapiens	114-120
20375277-0	2010	Low anticoagulant heparin targets multiple sites of inflammation, suppresses heparin-induced thrombocytopenia, and inhibits interaction of RAGE with its ligands.	Heparin	18-25	advanced glycosylation end-product specific receptor	Homo sapiens	139-143
20524194-2	2010	End-thiolated heparin retained anticoagulant activity as shown by the activated partial thromboplastin time (aPTT) and anti-Factor Xa (anti-FXa) assays.	Heparin	14-21	coagulation factor X	Homo sapiens	124-133
20524194-2	2010	End-thiolated heparin retained anticoagulant activity as shown by the activated partial thromboplastin time (aPTT) and anti-Factor Xa (anti-FXa) assays.	Heparin	14-21	coagulation factor X	Homo sapiens	140-143
20524194-6	2010	However, immobilized heparin retained substantial anti-FXa activity, with significantly greater activity exhibited by the end-thiolated HepNH(2) than the internally (randomly) thiolated UFH.	Heparin	21-28	coagulation factor X	Homo sapiens	55-58
20513355-4	2010	Both heparin and a homologue of C3b, substrates binding to the C-terminus of Factor H, were inhibitory of the interaction, as was EDTA.	Heparin	5-12	complement factor H	Homo sapiens	77-85
20513415-0	2010	NMR structural determinants of eosinophil cationic protein binding to membrane and heparin mimetics.	Heparin	83-90	ribonuclease A family member 3	Homo sapiens	31-58
20513415-2	2010	We have used NMR spectroscopy to characterize the binding of ECP to membrane and heparin mimetics at a residue level.	Heparin	81-88	ribonuclease A family member 3	Homo sapiens	61-64
20513415-4	2010	Importantly, we have provided evidence that the interaction surface of ECP with heparin mimetics is extended with respect to that previously described (fragment 34-38).	Heparin	80-87	ribonuclease A family member 3	Homo sapiens	71-74
20513415-6	2010	We have also shown that a biologically active ECP N-terminal fragment comprising the first 45 residues (ECP1-45) retains the capacity to bind membrane and heparin mimetics, thus neither the ECP tertiary structure nor its high conformational stability are required for cytotoxicity.	Heparin	155-162	ribonuclease A family member 3	Homo sapiens	46-49
20513415-6	2010	We have also shown that a biologically active ECP N-terminal fragment comprising the first 45 residues (ECP1-45) retains the capacity to bind membrane and heparin mimetics, thus neither the ECP tertiary structure nor its high conformational stability are required for cytotoxicity.	Heparin	155-162	ribonuclease A family member 3	Homo sapiens	104-107
20382221-10	2010	LTBP-2 was found to interact strongly in a heparin-inhibitable manner with cell surface HSPG syndecan-4, but showed no interaction with recombinant syndecan-2.	Heparin	43-50	syndecan 2	Homo sapiens	88-92
20368520-2	2010	M118 is a novel low-molecular-weight heparin that has been rationally designed to capture the desired attributes of unfractionated heparin (UFH) and low-molecular-weight heparin: Potent activity against factor Xa and IIa, predictable pharmacokinetics after both intravenous and subcutaneous administration, ability to be monitored by use of point-of-care coagulation assays, and reversibility with protamine sulfate.	Heparin	37-44	coagulation factor X	Homo sapiens	203-212
20010091-1	2010	Whereas heparin functions as an antithrombotic agent by promoting antithrombin III-based inhibition of thrombin and factor Xa, there is less appreciation for the combination behavior with small-molecule, direct inhibitors of these proteases.	Heparin	8-15	serpin family C member 1	Rattus norvegicus	66-82
22993547-5	2010	Quantitative PCR showed that PDL cells expressed mRNA for the EC-specific markers, VE-cadherin and VEGFR2, when cultured in the presence of heparin alone or with FGF-2.	Heparin	140-147	kinase insert domain receptor	Homo sapiens	99-105
19722264-7	2010	In studies of glycosaminoglycan binding, P2-RANTES was found to be significantly less able to bind heparin than wild type RANTES.	Heparin	99-106	C-C motif chemokine ligand 5	Homo sapiens	44-50
20024502-1	2010	Heparin promotes the antithrombin (AT) inactivation of factors IXa (fIXa) and Xa (fXa) through a conformational activation of the serpin and also by a template mechanism in the presence of physiological levels of Ca2+.	Heparin	0-7	coagulation factor X	Homo sapiens	82-85
20024502-2	2010	Recently, it was reported that heparin induces conformational changes in the active-sites of fIXa and fXa, raising the possibility that heparin also modulates the reactivity of these proteases with AT by this mechanism.	Heparin	31-38	coagulation factor X	Homo sapiens	102-105
20024502-2	2010	Recently, it was reported that heparin induces conformational changes in the active-sites of fIXa and fXa, raising the possibility that heparin also modulates the reactivity of these proteases with AT by this mechanism.	Heparin	136-143	coagulation factor X	Homo sapiens	102-105
20024502-6	2010	Full-length heparin-concentration dependence of the AT inhibition of fIXa and fXa revealed that in contrast to a greater than 4-5 orders of magnitude accelerating effect for heparin on the AT inhibition of fIXa and fXa, heparin exhibits a negligible cofactor effect (&lt;2-fold) on the mutant AT inhibition of these proteases.	Heparin	12-19	coagulation factor X	Homo sapiens	78-81
20711705-9	2010	(4) Heparin is an analogue of the polyanionic host cell surface, and FH forms higher oligomers with larger heparin fragments, suggesting a mechanism for more effective FH regulation.	Heparin	107-114	complement factor H	Homo sapiens	69-71
19940766-0	2010	Heparin inhibits the production of matrix metalloproteinase-2 and improves atherosclerosis in LDL receptor-deficient mice.	Heparin	0-7	matrix metallopeptidase 2	Mus musculus	35-61
19940766-0	2010	Heparin inhibits the production of matrix metalloproteinase-2 and improves atherosclerosis in LDL receptor-deficient mice.	Heparin	0-7	low density lipoprotein receptor	Mus musculus	94-106
19940766-1	2010	OBJECTIVE: This study aimed to find the effects of heparin on atherosclerosis and the production of matrix metalloproteinase (MMP)-2 in low-density lipoprotein receptor-deficient (LDLr(-/-)) mice.	Heparin	51-58	low density lipoprotein receptor	Mus musculus	180-184
19619365-6	2009	Total and heparin-releasable LPL activities were determined in subcutaneous adipose tissue by fluorimetry and FAS activity by spectrophotometry.	Heparin	10-17	lipoprotein lipase	Mesocricetus auratus	29-32
19909382-1	2009	This study was conducted to establish age-related reference ranges for two heparin-binding proteins--vitronectin and platelet factor 4 (PF4)--and to determine if the quantitative values of these proteins may contribute to the reported age-dependent effect of unfractionated heparin (UFH).	Heparin	75-82	vitronectin	Homo sapiens	101-112
19915053-6	2009	The expression of N-deacetylase/N-sulfotransferase (NDST)-2, a key enzyme in heparin synthesis, also correlated strongly with MC maturation, whereas the expression of the NDST-1 isoform was approximately equal at all stages of maturation.	Heparin	77-84	N-deacetylase and N-sulfotransferase 2	Homo sapiens	18-59
20101991-1	2009	To investigate the affinity constants of heparin with high mobility group protein 1(HMGB1) and HMGB1 with the receptor of advanced glycation end products (RAGE) and to analyze the impact of heparin on the affinity of HMGB1 and RAGE, the standard BIAcore amine coupling chemistry protocol using EDC and NHS was employed for immobilizing.	Heparin	41-48	long intergenic non-protein coding RNA 914	Homo sapiens	155-159
20101991-1	2009	To investigate the affinity constants of heparin with high mobility group protein 1(HMGB1) and HMGB1 with the receptor of advanced glycation end products (RAGE) and to analyze the impact of heparin on the affinity of HMGB1 and RAGE, the standard BIAcore amine coupling chemistry protocol using EDC and NHS was employed for immobilizing.	Heparin	41-48	long intergenic non-protein coding RNA 914	Homo sapiens	227-231
20101991-3	2009	Binding analysis was used to investigate the impact of heparin on the affinity of HMGB1 and RAGE.	Heparin	55-62	long intergenic non-protein coding RNA 914	Homo sapiens	92-96
20101991-8	2009	After 50 mg x L(-1) of HMGB1 was mixed with heparin of 50, 100, 1 000, 10 000 u x L(-1), the combining amount of HMGB1 and RAGE declined from 100 to 50 RU.	Heparin	44-51	long intergenic non-protein coding RNA 914	Homo sapiens	123-127
20101991-10	2009	It was concluded that heparin can combine with HMGB1 and affect the affinity of HMGB1/RAGE.	Heparin	22-29	long intergenic non-protein coding RNA 914	Homo sapiens	86-90
19712047-10	2009	However, both intact and plasmin-cleaved HRG enhanced the binding of plasminogen to heparin-coated surfaces to a similar extent.	Heparin	84-91	histidine rich glycoprotein	Homo sapiens	41-44
19712047-11	2009	Furthermore, the presence of heparin, Zn2+ or acidic pH was found to protect HRG from plasmin cleavage.	Heparin	29-36	histidine rich glycoprotein	Homo sapiens	77-80
19700767-4	2009	Two other family members, PRELP and chondroadherin, have distinctly different clusters of basic amino acids in their N and C termini, respectively, and PRELP is known to bind to heparin via this domain.	Heparin	178-185	proline and arginine rich end leucine rich repeat protein	Homo sapiens	26-31
19664058-9	2009	For FSAP-mediated inhibition of PDGF-BB-induced vascular smooth muscle cell proliferation, heparin as well as a polyphosphate served as efficient co-factors.	Heparin	91-98	hyaluronan binding protein 2	Homo sapiens	4-8
19564416-5	2009	Interestingly, the monomeric ligands exhibit reduced heparin binding, resulting in their increased radii of heparan sulfate-dependent diffusion and biologic action, as evidenced by the wider dilation area of ex vivo lung cultures in response to implanted mutant FGF9-loaded beads.	Heparin	53-60	fibroblast growth factor 9	Homo sapiens	262-266
19446554-0	2009	Structure-function analysis of factor VII activating protease (FSAP): sequence determinants for heparin binding and cellular functions.	Heparin	96-103	hyaluronan binding protein 2	Homo sapiens	31-61
19446554-0	2009	Structure-function analysis of factor VII activating protease (FSAP): sequence determinants for heparin binding and cellular functions.	Heparin	96-103	hyaluronan binding protein 2	Homo sapiens	63-67
19369870-4	2009	The pattern of lipoprotein lipase (LPL) release into the plasma after an intravenous injection of heparin is abnormal in Gpihbp1-deficient mice, suggesting that GPIHBP1 plays a direct role in binding LPL within the tissues of mice.	Heparin	98-105	lipoprotein lipase	Mus musculus	15-33
19369870-4	2009	The pattern of lipoprotein lipase (LPL) release into the plasma after an intravenous injection of heparin is abnormal in Gpihbp1-deficient mice, suggesting that GPIHBP1 plays a direct role in binding LPL within the tissues of mice.	Heparin	98-105	lipoprotein lipase	Mus musculus	35-38
19454698-6	2009	Although we found four aHUS-linked fH mutations that decreased binding to C3b and/or to heparin (a model compound for cell surface polyanionic carbohydrates), we identified five aHUS-associated mutants with increased affinity for either or both ligands.	Heparin	88-95	complement factor H	Homo sapiens	35-37
19309011-6	2009	The distribution of several spots around pI 5.0-5.6 and apparent molecular mass 1.2-1.5x10(2) kDa was also found to be different; the fragments of complement C3 and C4 were detected in heparin-plasma but not in EDTA-plasma.	Heparin	185-192	complement C3	Homo sapiens	147-160
19150337-6	2009	These findings suggest that PF4 in the presence of heparin is an allosteric effector of the prothrombinase complex.	Heparin	51-58	coagulation factor X	Homo sapiens	92-106
19154352-0	2009	Murine serum nucleases--contrasting effects of plasmin and heparin on the activities of DNase1 and DNase1-like 3 (DNase1l3).	Heparin	59-66	deoxyribonuclease I	Mus musculus	88-94
19118218-3	2009	Specific interaction of S. pneumoniae with the heparin-binding sites of purified multimeric vitronectin was demonstrated by flow cytometry analysis.	Heparin	47-54	vitronectin	Homo sapiens	92-103
19027296-6	2009	The ternary heparin conjugate is characterized by (13)C NMR, FT-IR and GPC, respectively.	Heparin	12-19	glycophorin C (Gerbich blood group)	Homo sapiens	61-74
18845532-4	2008	Heparin is known to release LPL from its in vivo binding sites, allowing it to enter the plasma.	Heparin	0-7	lipoprotein lipase	Mus musculus	28-31
18845532-5	2008	After an injection of heparin, we reasoned that LPL bound to GPIHBP1 in capillaries would be released very quickly, and we hypothesized that the kinetics of LPL entry into the plasma would differ in Gpihbp1(-/-) and control mice.	Heparin	22-29	lipoprotein lipase	Mus musculus	48-51
18546203-1	2008	In vitro, heparin and antithrombotic drugs specifically stimulate the synthesis of an antithrombotic heparan sulfate proteoglycan (HSPG) produced by endothelial cells.	Heparin	10-17	CD44 molecule (Indian blood group)	Homo sapiens	101-129
18546203-1	2008	In vitro, heparin and antithrombotic drugs specifically stimulate the synthesis of an antithrombotic heparan sulfate proteoglycan (HSPG) produced by endothelial cells.	Heparin	10-17	CD44 molecule (Indian blood group)	Homo sapiens	131-135
18794898-6	2008	Drosophila Ihog and its vertebrate homologues CDO and BOC contain multiple immunoglobulin and fibronectin type III (FNIII) repeats, and the first FNIII repeat of Ihog binds Drosophila HhN in a heparin-dependent manner.	Heparin	193-200	interference hedgehog	Drosophila melanogaster	11-15
18794898-6	2008	Drosophila Ihog and its vertebrate homologues CDO and BOC contain multiple immunoglobulin and fibronectin type III (FNIII) repeats, and the first FNIII repeat of Ihog binds Drosophila HhN in a heparin-dependent manner.	Heparin	193-200	interference hedgehog	Drosophila melanogaster	162-166
18615592-0	2008	Modulation of integrin antagonist signaling by ligand binding of the heparin-binding domain of vitronectin to the alphaVbeta3 integrin.	Heparin	69-76	vitronectin	Homo sapiens	95-106
18615592-4	2008	We determined that amino acids within the heparin-binding domain of vitronectin bind to a cysteine loop (C-loop) region of beta3 and that this interaction is required for the positive effects of alphaVbeta3 ligand occupancy on IGF-I signaling in smooth muscle cells.	Heparin	42-49	vitronectin	Homo sapiens	68-79
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	intercellular adhesion molecule 1	Homo sapiens	298-331
19967061-4	2008	In the present study, we examined the anti-inflammatory mechanism of heparin in cultured cerebral endothelial cells (CECs), and found that heparin inhibited the tumor necrosis factor alpha(TNFalpha)-induced and nuclear factor kappa B (NF-kappaB)-dependent expression of adhesion molecules, such as intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1), which are crucial for inflammatory responses.	Heparin	139-146	intercellular adhesion molecule 1	Homo sapiens	333-339
17942351-0	2008	Effects of unfractionated and fractionated heparins on myeloperoxidase activity and interactions with endothelial cells: possible effects on the pathophysiology of equine laminitis.	Heparin	43-51	myeloperoxidase	Equus caballus	55-70
17942351-2	2008	The effects of the heparins on purified equine MPO activity were tested by immunocapture followed by enzymatic detection.	Heparin	19-27	myeloperoxidase	Equus caballus	47-50
17942351-4	2008	A dose-dependent MPO inhibition by UFH and LMWH was seen, with the greatest reduction in MPO activity noted with the highest concentration of LMWH.	Heparin	43-47	myeloperoxidase	Equus caballus	17-20
17942351-4	2008	A dose-dependent MPO inhibition by UFH and LMWH was seen, with the greatest reduction in MPO activity noted with the highest concentration of LMWH.	Heparin	43-47	myeloperoxidase	Equus caballus	89-92
17942351-4	2008	A dose-dependent MPO inhibition by UFH and LMWH was seen, with the greatest reduction in MPO activity noted with the highest concentration of LMWH.	Heparin	142-146	myeloperoxidase	Equus caballus	17-20
17942351-4	2008	A dose-dependent MPO inhibition by UFH and LMWH was seen, with the greatest reduction in MPO activity noted with the highest concentration of LMWH.	Heparin	142-146	myeloperoxidase	Equus caballus	89-92
17942351-5	2008	The MPO capture was greater in arterial cells, but heparins better inhibited MPO capture in venous cells.	Heparin	51-59	myeloperoxidase	Equus caballus	77-80
17942351-6	2008	The activity of cell-bound MPO was almost completely suppressed by the heparins, and no differences were observed between UFH and LMWH.	Heparin	71-79	myeloperoxidase	Equus caballus	27-30
18579401-0	2008	Heparin-induced thrombocytopenia and cardiopulmonary bypass: anticoagulation with unfractionated heparin and the GPIIb/IIIa inhibitor tirofiban and successful use of rFVIIa for post-protamine bleeding due to persistent platelet blockade.	Heparin	0-7	integrin subunit alpha 2b	Homo sapiens	113-118
18566753-15	2008	Immunoblotting with this antibody showed that heparin and 4,5,6,7-tetrabromobenzotriazole (TBB), known CK2 inhibitors, inhibited in vitro phosphorylation of Cdc37 on Ser13 by CK2 holoenzyme or CK2alpha, confirming the specificity of the antibody to detect CK2 activity.	Heparin	46-53	casein kinase 2 alpha 2	Homo sapiens	193-201
18585707-3	2008	LTBP-4 was found to possess heparin binding activity, especially in its N-terminal region.	Heparin	28-35	latent transforming growth factor beta binding protein 4	Homo sapiens	0-6
18585707-4	2008	The C-terminal domain of LTBP-4 supported fibroblast adhesion, a property reduced by soluble heparin.	Heparin	93-100	latent transforming growth factor beta binding protein 4	Homo sapiens	25-31
18474426-4	2008	Intravenous unfractionated heparin was given 24 h after treatment with tPA.	Heparin	27-34	chromosome 20 open reading frame 181	Homo sapiens	71-74
18547105-3	2008	We found a significant effect, particularly of heparin, on the minimum or critical concentration of tropoelastin, which was required for microassembly, lowering critical concentration to a point that it was no longer detectable.	Heparin	47-54	elastin	Homo sapiens	100-112
18547105-5	2008	The spherules readily coalesced in the presence of heparin and higher concentrations of tropoelastin, resulting in an almost continuous layer of coacervated tropoelastin.	Heparin	51-58	elastin	Homo sapiens	157-169
18574264-2	2008	UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors.	Heparin	0-3	coagulation factor X	Homo sapiens	159-168
18178677-6	2008	In addition, the sensitizing effect of MBP was completely abolished when its cationic charge was neutralized by mixing with a polyanion, such as low-molecular-weight heparin or poly-L-glutamic or poly-L-aspartic acid, before its delivery to the neurons.	Heparin	166-173	myelin basic protein	Rattus norvegicus	39-42
18396724-7	2008	There was a significant difference in the amount of binding bFGF between two different scaffolds throughout all bFGF concentrations (P &lt; 0.05), and up to 100 ng/mL, the local and sustained release of bFGF from the heparin treated scaffolds were assayed up to 20 days.	Heparin	217-224	fibroblast growth factor 2	Canis lupus familiaris	60-64
18347539-5	2008	RESULTS: Reverse transcription-polymerase chain reaction analysis of the resultant cartilage tissue revealed that a thermo-reversible hydrogels with a heparin-bound TGF-beta3 was optimal for cartilage tissue formation as measured by production of collagen Type II, aggrecan, and SOX9, and cartilage oligomeric matrix protein gene expression.	Heparin	151-158	LOW QUALITY PROTEIN: transcription factor SOX-9	Oryctolagus cuniculus	279-283
17964826-0	2008	Low molecular weight heparin treatment decreases MMP-9 plasma activity in patients with abdominal aortic aneurysm.	Heparin	21-28	matrix metallopeptidase 9	Homo sapiens	49-54
18006516-1	2008	We have studied the effect of heparin, a glycosaminoglycan widely used in releasing tags from fusion proteins, on isoform 8 of Arabidopsis thaliana PM Ca(2+)-ATPase (ACA8) expressed in Saccharomyces cerevisiae strain K616.	Heparin	30-37	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	166-170
18006516-2	2008	Heparin stimulates hydrolytic activity of ACA8 with an estimated K(0.5) value for the complex of 15 +/- 1 microg ml(-1), which is unaffected by free [Ca(2+)].	Heparin	0-7	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	42-46
18006516-5	2008	Altogether, these results indicate that heparin activation is due to partial suppression of the auto-inhibitory function of ACA8 N-terminus.	Heparin	40-47	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	124-128
18006516-6	2008	Pull-down assays using heparin-agarose gel show that heparin directly interacts with ACA8.	Heparin	23-30	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	85-89
18006516-6	2008	Pull-down assays using heparin-agarose gel show that heparin directly interacts with ACA8.	Heparin	53-60	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	85-89
18006516-7	2008	Binding to the heparin-agarose gel occurs also with a peptide reproducing ACA8 sequence (1)M-I(116).	Heparin	15-22	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	74-78
18006516-8	2008	Several single-point mutations within ACA8 sequence A56-T63 significantly alter the enzyme response to heparin, suggesting that heparin interaction with this site may be involved in ACA8 activation.	Heparin	103-110	autoinhibited Ca2+ -ATPase	Arabidopsis thaliana	38-42
17607711-2	2008	PTN contains a thrombospondin repeat-I (TSR-I) motif in its two beta-sheet domains that are involved in its binding to heparin and its neurite outgrowth activity.	Heparin	119-126	activin A receptor type 1	Homo sapiens	15-38
17607711-2	2008	PTN contains a thrombospondin repeat-I (TSR-I) motif in its two beta-sheet domains that are involved in its binding to heparin and its neurite outgrowth activity.	Heparin	119-126	activin A receptor type 1	Homo sapiens	40-45
18042685-2	2008	In contrast to human TFPI, Ixolaris specifically binds to factor Xa (FXa) heparin-binding exosite (HBE).	Heparin	74-81	coagulation factor X	Homo sapiens	58-67
18042685-2	2008	In contrast to human TFPI, Ixolaris specifically binds to factor Xa (FXa) heparin-binding exosite (HBE).	Heparin	74-81	coagulation factor X	Homo sapiens	69-72
17996279-4	2008	Low-molecular-weight heparins are fragments of unfractionated heparin produced by controlled enzymatic or chemical depolymerization processes with the main difference being in their relative inhibitory activity against factor Xa and thrombin.	Heparin	21-29	coagulation factor X	Homo sapiens	219-228
17996279-4	2008	Low-molecular-weight heparins are fragments of unfractionated heparin produced by controlled enzymatic or chemical depolymerization processes with the main difference being in their relative inhibitory activity against factor Xa and thrombin.	Heparin	21-28	coagulation factor X	Homo sapiens	219-228
17979153-1	2007	Vascular endothelial growth factor A (VEGF-A) belongs to a family of heparin binding growth factors that include VEGF-B, VEGF-C, VEGF-D, and placental-like growth factor (PLGF).	Heparin	69-76	vascular endothelial growth factor B	Homo sapiens	113-119
17879163-8	2007	These findings provide evidence that mutations in the high-affinity heparin-binding domain in association with the V region of fibronectin, or altered fibronectin matrices, induce anoikis in human SCC cells by modulating integrin alpha v-mediated phosphorylation of FAK and ERK.	Heparin	68-75	integrin subunit alpha V	Homo sapiens	221-237
18060241-4	2007	The low molecular weight heparins (LMWH) show favourable pharmacokinetics over UFH and have a more pronounced activity against factor Xa as opposed to thrombin which may partially account for the benefits observed with LMWH in clinical trials.	Heparin	25-33	coagulation factor X	Homo sapiens	127-136
17981869-5	2007	Because LPL is naturally bound to the endothelium, we have used heparin to release the enzyme in the circulation and to characterize reserve capacity for lipoprotein catabolism.	Heparin	64-71	lipoprotein lipase	Oncorhynchus mykiss	8-11
17981869-8	2007	In resting fish, heparin administration caused a 27-fold increase in plasma LPL activity that reached a maximum of 1.32+/- 0.67 micromol fatty acids min(-1) ml(-1) plasma.	Heparin	17-24	lipoprotein lipase	Oncorhynchus mykiss	76-79
17981869-9	2007	This heparin-induced response of plasma LPL was not different between resting controls and exercised fish.	Heparin	5-12	lipoprotein lipase	Oncorhynchus mykiss	40-43
17675559-8	2007	Heparin, a known CD11b ligand, which is administered during cardiac surgery, markedly reduced neutrophil expression of conformationally active CD11b in vivo and in vitro, identifying a potential mechanism for its anti-inflammatory properties.	Heparin	0-7	integrin subunit alpha M	Homo sapiens	17-22
17675559-8	2007	Heparin, a known CD11b ligand, which is administered during cardiac surgery, markedly reduced neutrophil expression of conformationally active CD11b in vivo and in vitro, identifying a potential mechanism for its anti-inflammatory properties.	Heparin	0-7	integrin subunit alpha M	Homo sapiens	143-148
17699513-10	2007	Heparin, EDTA, and anti-integrin beta1 antibody inhibited TM14 binding to dental mesenchyme cells, suggesting that both a heparan sulfate-containing cell surface receptor and an integrin are involved in TM14 cell binding.	Heparin	0-7	fibulin 7	Mus musculus	58-62
17699513-10	2007	Heparin, EDTA, and anti-integrin beta1 antibody inhibited TM14 binding to dental mesenchyme cells, suggesting that both a heparan sulfate-containing cell surface receptor and an integrin are involved in TM14 cell binding.	Heparin	0-7	fibulin 7	Mus musculus	203-207
17711860-5	2007	In addition, heparin further enhanced the effects of both alphaKlotho and betaKlotho in FGF19 signaling and interaction experiments.	Heparin	13-20	klotho beta	Homo sapiens	74-84
17649979-11	2007	NMR translational diffusion experiments show that agrin-G3 binds heparin with a 2:1 stoichiometry.	Heparin	65-72	agrin	Homo sapiens	50-55
17560185-0	2007	Heparin enhances osteoclastic bone resorption by inhibiting osteoprotegerin activity.	Heparin	0-7	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	60-75
17560185-8	2007	Instead, heparin specifically binds to OPG and prevents OPG-mediated inhibition of osteoclastic bone resorption in the coculture.	Heparin	9-16	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	39-42
17560185-8	2007	Instead, heparin specifically binds to OPG and prevents OPG-mediated inhibition of osteoclastic bone resorption in the coculture.	Heparin	9-16	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	56-59
17560185-10	2007	A (125)I-OPG binding assay showed that OPG binds to osteoblasts and that this binding is inhibited by the addition of heparin, suggesting that OPG binds to RANKL on the osteoblast membrane and that heparin blocks this interaction.	Heparin	118-125	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	9-12
17560185-10	2007	A (125)I-OPG binding assay showed that OPG binds to osteoblasts and that this binding is inhibited by the addition of heparin, suggesting that OPG binds to RANKL on the osteoblast membrane and that heparin blocks this interaction.	Heparin	118-125	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	39-42
17560185-10	2007	A (125)I-OPG binding assay showed that OPG binds to osteoblasts and that this binding is inhibited by the addition of heparin, suggesting that OPG binds to RANKL on the osteoblast membrane and that heparin blocks this interaction.	Heparin	118-125	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	39-42
17560185-10	2007	A (125)I-OPG binding assay showed that OPG binds to osteoblasts and that this binding is inhibited by the addition of heparin, suggesting that OPG binds to RANKL on the osteoblast membrane and that heparin blocks this interaction.	Heparin	198-205	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	39-42
17560185-10	2007	A (125)I-OPG binding assay showed that OPG binds to osteoblasts and that this binding is inhibited by the addition of heparin, suggesting that OPG binds to RANKL on the osteoblast membrane and that heparin blocks this interaction.	Heparin	198-205	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	39-42
17560185-11	2007	These results demonstrate that heparin enhances osteoclastic bone resorption by inhibiting OPG activity.	Heparin	31-38	tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin)	Mus musculus	91-94
17706514-2	2007	The child was affected by a right hemiparesis because of a hypoxic-ischemic disorder that occurred in the first hours of life and was heterozygous for the methylenetetrahydrofolate reductase gene mutation 677C-T. Intravenous heparin and aspirin were initiated on postoperative day 7.	Heparin	225-232	methylenetetrahydrofolate reductase	Homo sapiens	155-190
17339423-1	2007	The heparan sulfate (HS) proteoglycan, syndecan-1, plays a major role in multiple myeloma (MM) by concentrating heparin-binding growth factors on the surface of MM cells (MMCs).	Heparin	112-119	CD44 molecule (Indian blood group)	Homo sapiens	4-37
17672188-0	2007	Heparin monitoring during cardiopulmonary bypass surgery using the one-step point-of-care whole blood anti-factor-Xa clotting assay heptest-POC-Hi.	Heparin	0-7	coagulation factor X	Homo sapiens	107-116
17300216-2	2007	The auto-activation of FSAP is facilitated by negatively charged polyanions such as heparin, dextransulfate or extracellular ribonucleic acids.	Heparin	84-91	hyaluronan binding protein 2	Homo sapiens	23-27
17485493-4	2007	The secreted extracellular domain of gliomedin binds to Schwann cells and is incorporated into the extracellular matrix (ECM) in a heparin-dependent manner, suggesting the involvement of heparan sulfate proteoglycans (HSPGs).	Heparin	131-138	gliomedin	Homo sapiens	37-46
17069767-8	2007	Heparin, an inhibitor for HB-EGF, suppressed PAR1-mediated PGE(2) formation and persistent ERK phosphorylation.	Heparin	0-7	coagulation factor II (thrombin) receptor	Rattus norvegicus	45-49
17150202-9	2007	CONCLUSIONS: These results suggest that the circulating levels of MMP-9 should be assessed in citrate or heparin plasma samples, but not in serum samples because of artificially higher MMP-9 levels in serum, independently of TBDC, and because they do not correlate with the MMP-9 levels in plasma samples.	Heparin	105-112	matrix metallopeptidase 9	Homo sapiens	66-71
17335986-0	2007	Anti-metastatic activity of heparin is probably associated with modulation of SDF-1-CXCR4 axis.	Heparin	28-35	C-X-C motif chemokine receptor 4	Homo sapiens	84-89
16816960-1	2007	INTRODUCTION: We report a simplified method of performing antibiotic lock therapy (ALT) based on a disposable central venous catheter (CVC) hub device, CLC 2000, enabling an open-ended CVC to be flushed with normal saline solution without heparin.	Heparin	239-246	Charcot-Leyden crystal galectin	Homo sapiens	152-155
17176096-2	2006	The two analogue peptides were found to be equally effective for neutralization of the anticoagulant activity of heparin, as measured by restoration of the activity of serine protease factor Xa by the Coatest heparin method.	Heparin	113-120	coagulation factor X	Homo sapiens	184-193
16940049-6	2006	Rates of heparin-independent Y131L and Y131A factor Xa inhibition were 25 and 29 times faster than for the control and Y131F, suggesting that Tyr(131) ring interactions with neighboring helix D and strand 2A residues shift the uncatalyzed native-to-activated conformational equilibrium toward the RCL-inserted state.	Heparin	9-16	coagulation factor X	Homo sapiens	45-54
17004727-0	2006	Heparin derivatives as inhibitors of BACE-1, the Alzheimer"s beta-secretase, with reduced activity against factor Xa and other proteases.	Heparin	0-7	coagulation factor X	Homo sapiens	107-116
16965447-0	2006	Methylenetetrahydrofolate reductase polymorphism associated with moderate hyperhomocysteinaemia in a patient with livedo vasculopathy: treatment with vitamin supplementation and low molecular weight heparin.	Heparin	199-206	methylenetetrahydrofolate reductase	Homo sapiens	0-35
16771712-5	2006	In contrast, TIMP-3 is demonstrated to inhibit ADAMTS-2 in vitro with apparent Ki values of 160 and 602 nM, in the presence of heparin or without respectively; and TIMP-3 is shown to inhibit procollagen processing by cells.	Heparin	127-134	TIMP metallopeptidase inhibitor 3	Homo sapiens	13-19
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	44-51	TNF superfamily member 11	Homo sapiens	207-212
16828054-4	2006	Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL.	Heparin	127-134	TNF superfamily member 11	Homo sapiens	207-212
16828054-7	2006	The results demonstrated that sulfation is essential in the OPG-blocking function of GAGs since a totally desulfated heparin loses its capacity to bind and to block OPG binding to RANKL.	Heparin	117-124	TNF superfamily member 11	Homo sapiens	180-185
16399871-7	2006	Heparin, which is hypothesized to displace XOR from a heparin-binding domain in the Gcx, reduced the effects of I/R.	Heparin	0-7	xanthine dehydrogenase	Mus musculus	43-46
16709187-8	2006	More recently, we and others have been investigating the heparin/heparan sulphate-binding properties of BMP-7, which is a representative of a distinct BMP subgroup from that of BMPs -2 and -4.	Heparin	57-64	bone morphogenetic protein 7	Homo sapiens	104-109
16768833-4	2006	Total and heparin-releasable LPL and lipogenic enzyme activities (acetyl-CoA carboxylase (ACC); fatty acid synthase (FAS); glucose-6-phosphate dehydrogenase (G6PDH); and malic enzyme (ME)) were assessed.	Heparin	10-17	fatty acid synthase	Homo sapiens	96-115
16768833-4	2006	Total and heparin-releasable LPL and lipogenic enzyme activities (acetyl-CoA carboxylase (ACC); fatty acid synthase (FAS); glucose-6-phosphate dehydrogenase (G6PDH); and malic enzyme (ME)) were assessed.	Heparin	10-17	fatty acid synthase	Homo sapiens	117-120
16768833-4	2006	Total and heparin-releasable LPL and lipogenic enzyme activities (acetyl-CoA carboxylase (ACC); fatty acid synthase (FAS); glucose-6-phosphate dehydrogenase (G6PDH); and malic enzyme (ME)) were assessed.	Heparin	10-17	glucose-6-phosphate dehydrogenase	Homo sapiens	123-156
16768833-4	2006	Total and heparin-releasable LPL and lipogenic enzyme activities (acetyl-CoA carboxylase (ACC); fatty acid synthase (FAS); glucose-6-phosphate dehydrogenase (G6PDH); and malic enzyme (ME)) were assessed.	Heparin	10-17	glucose-6-phosphate dehydrogenase	Homo sapiens	158-163
16517611-1	2006	We previously showed that conformational activation of the anticoagulant serpin, antithrombin, by heparin generates new exosites in strand 3 of beta-sheet C, which promote the reaction of the inhibitor with the target proteases, factor Xa and factor IXa.	Heparin	98-105	coagulation factor X	Homo sapiens	229-253
16619025-5	2006	Here we present the crystallographic structure of the recognition (Michaelis) complex between heparin-activated AT and S195A fXa, revealing the extensive exosite contacts that confer specificity.	Heparin	94-101	coagulation factor X	Homo sapiens	125-128
16619025-6	2006	The heparin-induced conformational change in AT is required to allow simultaneous contacts within the active site and two distinct exosites of fXa (36-loop and the autolysis loop).	Heparin	4-11	coagulation factor X	Homo sapiens	143-146
16634809-1	2006	The complement inhibitor Factor H has three distinct binding sites for C3b and for heparin, but in solution uses specifically the most C-terminal domain, i.e. short consensus repeats (SCR) 20 for ligand interaction.	Heparin	83-90	complement factor H	Homo sapiens	25-33
16856476-6	2006	CONCLUSION: Na-MCS represented a potent anticoagulation activity in vitro, which matched the efficacy of heparin in a certain range of concentrations.	Heparin	105-112	Miles-Carpenter X-linked mental retardation syndrome	Homo sapiens	15-18
16413680-1	2006	A novel phospholipase A2 (PLA2) with Asn at its site 49 was purified from the snake venom of Protobothrops mucrosquamatus by using SP-Sephadex C25, Superdex 75, Heparin-Sepharose (FF) and HPLC reverse-phage C18 chromatography and designated as TM-N49.	Heparin	161-168	phospholipase A2, group IB, pancreas	Mus musculus	8-24
16413680-1	2006	A novel phospholipase A2 (PLA2) with Asn at its site 49 was purified from the snake venom of Protobothrops mucrosquamatus by using SP-Sephadex C25, Superdex 75, Heparin-Sepharose (FF) and HPLC reverse-phage C18 chromatography and designated as TM-N49.	Heparin	161-168	phospholipase A2, group IB, pancreas	Mus musculus	26-30
16436680-1	2006	Plasmin-catalyzed cleavage of the vascular endothelial growth factor (VEGF)-A isoform VEGF165 results in loss of its carboxyl-terminal heparin-binding domain and significant loss in its bioactivity.	Heparin	135-142	vascular endothelial growth factor A	Mus musculus	34-68
16436680-1	2006	Plasmin-catalyzed cleavage of the vascular endothelial growth factor (VEGF)-A isoform VEGF165 results in loss of its carboxyl-terminal heparin-binding domain and significant loss in its bioactivity.	Heparin	135-142	vascular endothelial growth factor A	Mus musculus	70-74
16337042-9	2006	The activities of lysosomal enzymes (N-acetyl glucosaminidase, beta-glucuronidase, beta-galactosaminidase and cathepsin-D) showed a marked increase in the CCT-diet fed rats, while LMWH treated rats showed normal activities (p &lt; 0.001).	Heparin	180-184	FLVCR heme transporter 2	Rattus norvegicus	155-158
16146728-2	2006	Various types of low molecular weight (LMW) heparin, which function as semi-selective and indirect FXa inhibitors, are replacing unfractionated heparin (UFH) as agents for the prevention and treatment of venous thromboembolism (VTE), as well as in initial treatment for coronary events.	Heparin	44-51	coagulation factor X	Homo sapiens	99-102
16409124-8	2006	When tested in vivo, either in CD4 knockout mice or in a hemophilic mouse model, the heparin-purified hybrid vector showed &gt;10-fold higher activity than similarly purified AAV2.	Heparin	85-92	CD4 antigen	Mus musculus	31-34
16324873-2	2006	Since heparin-binding FGFs are tightly bound to heparansulfate proteoglycans, and therefore, trapped in the extracellular matrix, their release through the action of an FGF-binding protein (FGF-BP) is one of the critical steps in FGF bioactivation.	Heparin	6-13	fibroblast growth factor binding protein 1	Mus musculus	169-188
16324873-2	2006	Since heparin-binding FGFs are tightly bound to heparansulfate proteoglycans, and therefore, trapped in the extracellular matrix, their release through the action of an FGF-binding protein (FGF-BP) is one of the critical steps in FGF bioactivation.	Heparin	6-13	fibroblast growth factor binding protein 1	Mus musculus	190-196
16411608-8	2006	The heparin gel with loaded VEGF was implanted sub-cutaneously in the dorsal region of mice.	Heparin	4-11	vascular endothelial growth factor A	Mus musculus	28-32
16284070-4	2006	The EGFR ligands EGF (100 ng ml(-1)), transforming growth factor alpha (0.4 ng ml(-1)) and heparin-binding EGF (100 ng ml(-1)) all caused a 20% increase in maxi-K(Ca) channel current that was blocked by AG-1478 or by knock-down of EGFR expression using cisterna magna infusion of antisense oligodeoxynucleotide (AS-ODN).	Heparin	91-98	epidermal growth factor receptor	Rattus norvegicus	231-235
16125850-5	2005	Complement proteins C1, C2, C3, C4, C5, C6, C7, C8, C9, C1INH, factor I, factor H, factor B and factor P all bind heparin but exhibit different binding kinetics and dissociation constants (Kd) ranging from 2 to 320 nM.	Heparin	114-121	serpin family G member 1	Homo sapiens	56-104
16386592-3	2005	We sought to determine the impact of heparin on m-hepatocyte growth factor (HGF) plasma concentrations.	Heparin	37-44	hepatocyte growth factor	Rattus norvegicus	76-79
16386592-15	2005	Peak values were obtained at 120 and 240 minutes (225.21 pg/mL and 221.78 pg/mL) among groups C and D. CONCLUSION: Heparin has a positive effect to increase serum HGF concentrations among rats.	Heparin	115-122	hepatocyte growth factor	Rattus norvegicus	163-166
16195480-0	2005	Cyclin-dependent kinase inhibitor p27Kip1, but not p21WAF1/Cip1, is required for inhibition of hypoxia-induced pulmonary hypertension and remodeling by heparin in mice.	Heparin	152-159	cyclin-dependent kinase inhibitor 1B	Mus musculus	34-41
16195480-3	2005	In this study, we investigated the role of cyclin-dependent kinase inhibitors, p21(WAF1/cip1) (p21) and p27Kip1 (p27), in the inhibitory effect of heparin on PASMC proliferation in vitro and on hypoxia-induced pulmonary hypertension in vivo using p21 and p27-null mice.	Heparin	147-154	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	79-92
16195480-3	2005	In this study, we investigated the role of cyclin-dependent kinase inhibitors, p21(WAF1/cip1) (p21) and p27Kip1 (p27), in the inhibitory effect of heparin on PASMC proliferation in vitro and on hypoxia-induced pulmonary hypertension in vivo using p21 and p27-null mice.	Heparin	147-154	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	79-82
16195480-3	2005	In this study, we investigated the role of cyclin-dependent kinase inhibitors, p21(WAF1/cip1) (p21) and p27Kip1 (p27), in the inhibitory effect of heparin on PASMC proliferation in vitro and on hypoxia-induced pulmonary hypertension in vivo using p21 and p27-null mice.	Heparin	147-154	cyclin-dependent kinase inhibitor 1B	Mus musculus	104-107
16195480-3	2005	In this study, we investigated the role of cyclin-dependent kinase inhibitors, p21(WAF1/cip1) (p21) and p27Kip1 (p27), in the inhibitory effect of heparin on PASMC proliferation in vitro and on hypoxia-induced pulmonary hypertension in vivo using p21 and p27-null mice.	Heparin	147-154	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	95-98
16195480-3	2005	In this study, we investigated the role of cyclin-dependent kinase inhibitors, p21(WAF1/cip1) (p21) and p27Kip1 (p27), in the inhibitory effect of heparin on PASMC proliferation in vitro and on hypoxia-induced pulmonary hypertension in vivo using p21 and p27-null mice.	Heparin	147-154	cyclin-dependent kinase inhibitor 1B	Mus musculus	113-116
16195480-4	2005	In vitro, loss of the p27 gene negated the inhibitory effect of heparin on PASMC proliferation, but p21 was not critical for this inhibition.	Heparin	64-71	cyclin-dependent kinase inhibitor 1B	Mus musculus	22-25
16195480-5	2005	In vivo, heparin significantly inhibited the development of hypoxia-induced pulmonary hypertension and remodeling, as evidenced by decreased right ventricular systolic pressure, ratio of right ventricular weight to left ventricle plus septum weight, and percent wall thickness of pulmonary artery, in p21(+/+), p21(-/-), p27(+/+), and p27(+/-), but not in p27(-/-) mice.	Heparin	9-16	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	301-304
16195480-5	2005	In vivo, heparin significantly inhibited the development of hypoxia-induced pulmonary hypertension and remodeling, as evidenced by decreased right ventricular systolic pressure, ratio of right ventricular weight to left ventricle plus septum weight, and percent wall thickness of pulmonary artery, in p21(+/+), p21(-/-), p27(+/+), and p27(+/-), but not in p27(-/-) mice.	Heparin	9-16	cyclin-dependent kinase inhibitor 1A (P21)	Mus musculus	311-314
16195480-5	2005	In vivo, heparin significantly inhibited the development of hypoxia-induced pulmonary hypertension and remodeling, as evidenced by decreased right ventricular systolic pressure, ratio of right ventricular weight to left ventricle plus septum weight, and percent wall thickness of pulmonary artery, in p21(+/+), p21(-/-), p27(+/+), and p27(+/-), but not in p27(-/-) mice.	Heparin	9-16	cyclin-dependent kinase inhibitor 1B	Mus musculus	321-324
16195480-5	2005	In vivo, heparin significantly inhibited the development of hypoxia-induced pulmonary hypertension and remodeling, as evidenced by decreased right ventricular systolic pressure, ratio of right ventricular weight to left ventricle plus septum weight, and percent wall thickness of pulmonary artery, in p21(+/+), p21(-/-), p27(+/+), and p27(+/-), but not in p27(-/-) mice.	Heparin	9-16	cyclin-dependent kinase inhibitor 1B	Mus musculus	335-338
16195480-5	2005	In vivo, heparin significantly inhibited the development of hypoxia-induced pulmonary hypertension and remodeling, as evidenced by decreased right ventricular systolic pressure, ratio of right ventricular weight to left ventricle plus septum weight, and percent wall thickness of pulmonary artery, in p21(+/+), p21(-/-), p27(+/+), and p27(+/-), but not in p27(-/-) mice.	Heparin	9-16	cyclin-dependent kinase inhibitor 1B	Mus musculus	335-338
16195480-6	2005	We also observed that hypoxia decreased p27 expression significantly in mouse lung, which was restored by heparin.	Heparin	106-113	cyclin-dependent kinase inhibitor 1B	Mus musculus	40-43
16195480-7	2005	Heparin inhibited Ki67 proliferative index in terminal bronchial vessel walls in p27(+/+) and p27(+/-), but not in p27(-/-) mice exposed to hypoxia.	Heparin	0-7	antigen identified by monoclonal antibody Ki 67	Mus musculus	18-22
16195480-7	2005	Heparin inhibited Ki67 proliferative index in terminal bronchial vessel walls in p27(+/+) and p27(+/-), but not in p27(-/-) mice exposed to hypoxia.	Heparin	0-7	cyclin-dependent kinase inhibitor 1B	Mus musculus	81-84
16195480-7	2005	Heparin inhibited Ki67 proliferative index in terminal bronchial vessel walls in p27(+/+) and p27(+/-), but not in p27(-/-) mice exposed to hypoxia.	Heparin	0-7	cyclin-dependent kinase inhibitor 1B	Mus musculus	94-97
16195480-7	2005	Heparin inhibited Ki67 proliferative index in terminal bronchial vessel walls in p27(+/+) and p27(+/-), but not in p27(-/-) mice exposed to hypoxia.	Heparin	0-7	cyclin-dependent kinase inhibitor 1B	Mus musculus	94-97
16195480-8	2005	Therefore, we conclude that the cyclin-dependent kinase inhibitor p27, but not p21, is required for the inhibition of hypoxic pulmonary vascular remodeling by heparin.	Heparin	159-166	cyclin-dependent kinase inhibitor 1B	Mus musculus	66-69
16192651-3	2005	Domain 20 of FH contains binding sites for heparin, C3b, and the cleavage product C3d.	Heparin	43-50	complement factor H	Homo sapiens	13-15
16192651-6	2005	Similarly, an aHUS-derived mutant FH protein (E1172Stop, lacking domain 20) failed to bind endothelial cells and showed impaired binding to heparin.	Heparin	140-147	complement factor H	Homo sapiens	34-36
16192651-7	2005	Binding of FH to endothelial cells was inhibited by heparin and a specific monoclonal antibody that inhibited heparin but not C3d binding, demonstrating that the heparin site on domains 19 to 20 mediates interaction of FH to endothelial cells.	Heparin	52-59	complement factor H	Homo sapiens	11-13
16192651-7	2005	Binding of FH to endothelial cells was inhibited by heparin and a specific monoclonal antibody that inhibited heparin but not C3d binding, demonstrating that the heparin site on domains 19 to 20 mediates interaction of FH to endothelial cells.	Heparin	110-117	complement factor H	Homo sapiens	11-13
16192651-7	2005	Binding of FH to endothelial cells was inhibited by heparin and a specific monoclonal antibody that inhibited heparin but not C3d binding, demonstrating that the heparin site on domains 19 to 20 mediates interaction of FH to endothelial cells.	Heparin	110-117	complement factor H	Homo sapiens	11-13
16211534-10	2005	Increase of CD11b expression on circulating leukocytes and of plasma C3a was ameliorated in the heparin- and PMEA-coated circuits (P&lt;0.05).	Heparin	96-103	integrin subunit alpha M	Homo sapiens	12-17
16211534-10	2005	Increase of CD11b expression on circulating leukocytes and of plasma C3a was ameliorated in the heparin- and PMEA-coated circuits (P&lt;0.05).	Heparin	96-103	complement C3	Homo sapiens	69-72
15962217-0	2005	Effector functions of heparin-binding hemagglutinin-specific CD8+ T lymphocytes in latent human tuberculosis.	Heparin	22-29	CD8a molecule	Homo sapiens	61-64
16568610-4	2005	At the same time, some inhibition of blood serum LCAT activity two hours after food reception (evidently, as a result of endogenic heparin action) and to a considerable extent inhibition of cholesterol etherification under the action of exogenic heparin in vivo were ascertain.	Heparin	131-138	lecithin-cholesterol acyltransferase	Homo sapiens	49-53
15701679-9	2005	Addition of either heparin or LpL inhibitor P407 to Intralipid-containing perfusate restored [14C]palmitate uptake and confirmed that Intralipid inhibition requires local LpL.	Heparin	19-26	lipoprotein lipase	Mus musculus	171-174
15617517-3	2005	Here we provide evidence that Ixolaris binds specifically to the FXa HBE (heparin-binding exosite), since (i) it markedly decreases the inhibition of FXa by the antithrombin-heparin but not the antithrombin-pentasaccharide complex, (ii) it impairs FXa binding to Sepharose-immobilized heparin, and (iii) it allosterically modulates the catalytic activity of FXa for small chromogenic substrates (S-2765).	Heparin	74-81	coagulation factor X	Homo sapiens	65-68
15617517-3	2005	Here we provide evidence that Ixolaris binds specifically to the FXa HBE (heparin-binding exosite), since (i) it markedly decreases the inhibition of FXa by the antithrombin-heparin but not the antithrombin-pentasaccharide complex, (ii) it impairs FXa binding to Sepharose-immobilized heparin, and (iii) it allosterically modulates the catalytic activity of FXa for small chromogenic substrates (S-2765).	Heparin	74-81	coagulation factor X	Homo sapiens	150-153
15617517-3	2005	Here we provide evidence that Ixolaris binds specifically to the FXa HBE (heparin-binding exosite), since (i) it markedly decreases the inhibition of FXa by the antithrombin-heparin but not the antithrombin-pentasaccharide complex, (ii) it impairs FXa binding to Sepharose-immobilized heparin, and (iii) it allosterically modulates the catalytic activity of FXa for small chromogenic substrates (S-2765).	Heparin	74-81	coagulation factor X	Homo sapiens	150-153
15617517-3	2005	Here we provide evidence that Ixolaris binds specifically to the FXa HBE (heparin-binding exosite), since (i) it markedly decreases the inhibition of FXa by the antithrombin-heparin but not the antithrombin-pentasaccharide complex, (ii) it impairs FXa binding to Sepharose-immobilized heparin, and (iii) it allosterically modulates the catalytic activity of FXa for small chromogenic substrates (S-2765).	Heparin	74-81	coagulation factor X	Homo sapiens	150-153
15617517-3	2005	Here we provide evidence that Ixolaris binds specifically to the FXa HBE (heparin-binding exosite), since (i) it markedly decreases the inhibition of FXa by the antithrombin-heparin but not the antithrombin-pentasaccharide complex, (ii) it impairs FXa binding to Sepharose-immobilized heparin, and (iii) it allosterically modulates the catalytic activity of FXa for small chromogenic substrates (S-2765).	Heparin	174-181	coagulation factor X	Homo sapiens	65-68
15617517-3	2005	Here we provide evidence that Ixolaris binds specifically to the FXa HBE (heparin-binding exosite), since (i) it markedly decreases the inhibition of FXa by the antithrombin-heparin but not the antithrombin-pentasaccharide complex, (ii) it impairs FXa binding to Sepharose-immobilized heparin, and (iii) it allosterically modulates the catalytic activity of FXa for small chromogenic substrates (S-2765).	Heparin	174-181	coagulation factor X	Homo sapiens	65-68
15785094-3	2005	To clarify the mechanism of this inhibition, we investigated the effect of heparin on transcriptional regulation of the ET-1 gene in bovine aortic endothelial cells (BAEC) cultured in fetal calf serum.	Heparin	75-82	endothelin 1	Bos taurus	120-124
15668233-6	2005	A significant part of PrP(Sc) binding to both lines could be inhibited by heparin.	Heparin	74-81	major prion protein	Cricetulus griseus	22-25
15795534-10	2005	The anti-FXa assay appears to be a better method for monitoring heparin subjects than the aPTT due to the lack of effect of pre-analytical variables.	Heparin	64-71	coagulation factor X	Homo sapiens	9-12
15748207-2	2005	HRG ligands include Zn(2+) and haem, tropomyosin, heparin and heparan sulphate, plasminogen, plasmin, fibrinogen, thrombospondin, IgG, FcgammaR and complement.	Heparin	50-57	histidine rich glycoprotein	Homo sapiens	0-3
15383398-4	2005	Heparin (1 microg/ml), but not chondroitin or dermatan sulfate, significantly attenuated both serum- or ionomycin-induced CaMK-II activity, and attendant c-fos mRNA expression, but did not affect upstream Ca(2+)/calmodulin.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	154-159
15960391-6	2005	The synthetic peptide (A3G756)-induced cell migration and MMP-9 upregulation were inhibited by each application of a heparin and an IL-1 receptor antagonist (IL-1RA), suggesting the involvement of syndecans and IL-1beta autocrine.	Heparin	117-124	matrix metallopeptidase 9	Homo sapiens	58-63
15633734-4	2004	The newest, third generation heparin, the pentasaccharide inhibits specifically FXa.	Heparin	29-36	coagulation factor X	Homo sapiens	80-83
15530372-2	2004	We have determined the structure of the chemokine RANTES (regulated on activation normal T cell expressed) in the presence of heparin-derived disaccharide analogs by X-ray crystallography.	Heparin	126-133	C-C motif chemokine ligand 5	Homo sapiens	50-56
15726889-8	2004	The results of this study showed that in presence of the buffer containing 0.1 M NaCl, heparin was interacting with t-PA while the two fucoidans were interacting with both t-PA and Glu-Plg.	Heparin	87-94	chromosome 20 open reading frame 181	Homo sapiens	116-120
15226301-4	2004	These sites, like LRP-1, are sensitive to receptor-associated protein and calcium depletion but, unlike LRP-1, are also sensitive to chondroitin sulfate and heparin and capable of directly binding ligands, which do not bind to LRP-1.	Heparin	157-164	LDL receptor related protein 1	Bos taurus	18-23
15226301-4	2004	These sites, like LRP-1, are sensitive to receptor-associated protein and calcium depletion but, unlike LRP-1, are also sensitive to chondroitin sulfate and heparin and capable of directly binding ligands, which do not bind to LRP-1.	Heparin	157-164	LDL receptor related protein 1	Bos taurus	104-109
15226301-4	2004	These sites, like LRP-1, are sensitive to receptor-associated protein and calcium depletion but, unlike LRP-1, are also sensitive to chondroitin sulfate and heparin and capable of directly binding ligands, which do not bind to LRP-1.	Heparin	157-164	LDL receptor related protein 1	Bos taurus	104-109
15313154-5	2004	RESULTS: TRACP 5b specificity was achieved at pH 6.3 with 2.5 mmol/l substrate and 25 U/ml heparin.	Heparin	91-98	acid phosphatase 5, tartrate resistant	Homo sapiens	9-17
15262419-2	2004	A heparin-based delivery system (HBDS) was used to immobilize NT-3 within fibrin gels via non-covalent interactions to slow diffusion-based release of NT-3, thus allowing cell-activated degradation of fibrin to mediate release.	Heparin	2-9	neurotrophin 3	Homo sapiens	62-66
15262419-2	2004	A heparin-based delivery system (HBDS) was used to immobilize NT-3 within fibrin gels via non-covalent interactions to slow diffusion-based release of NT-3, thus allowing cell-activated degradation of fibrin to mediate release.	Heparin	2-9	neurotrophin 3	Homo sapiens	151-155
15262419-5	2004	This immobilized linker peptide sequesters heparin within fibrin gels, and sequestered heparin binds NT-3, preventing its diffusion.	Heparin	87-94	neurotrophin 3	Homo sapiens	101-105
15262419-6	2004	Mathematical modeling was performed to examine the effect of heparin concentration on the fraction of NT-3 initially bound to fibrin.	Heparin	61-68	neurotrophin 3	Homo sapiens	102-106
15262419-7	2004	In vitro release studies confirmed that heparin concentration modulates diffusion-based release of NT-3.	Heparin	40-47	neurotrophin 3	Homo sapiens	99-103
15138272-7	2004	Furthermore, blocking studies with various GAG species indicated that only heparin was a potent inhibitor of HRG binding.	Heparin	75-82	histidine rich glycoprotein	Homo sapiens	109-112
15138272-9	2004	Using recombinant forms of full-length HRG and the N-terminal N1N2 domain, it was shown that the N1N2 domain bound specifically to immobilized heparin and cell-surface heparan sulfate.	Heparin	143-150	histidine rich glycoprotein	Homo sapiens	39-42
15209861-1	2004	The objective of this study was to determine the effect of basic fibroblast growth factor (bFGF) coating on endothelial cell seeding and proliferation on a decellularized heparin coated vascular graft and to determine the retention of seeded cells on the graft under flow conditions.	Heparin	171-178	fibroblast growth factor 2	Canis lupus familiaris	59-89
15209861-1	2004	The objective of this study was to determine the effect of basic fibroblast growth factor (bFGF) coating on endothelial cell seeding and proliferation on a decellularized heparin coated vascular graft and to determine the retention of seeded cells on the graft under flow conditions.	Heparin	171-178	fibroblast growth factor 2	Canis lupus familiaris	91-95
15209861-8	2004	These data demonstrate that bFGF coating on the heparin bound decellularized grafts significantly increases both HMEC and dog EPC proliferation and that seeded cells are stable under perfusion conditions.	Heparin	48-55	fibroblast growth factor 2	Canis lupus familiaris	28-32
15201252-6	2004	Coadministration of heparin with Gp IIb/IIIa blockers provides improved protection against persistent platelet activation, thereby improving outcome after percutaneous coronary intervention.	Heparin	20-27	integrin subunit alpha 2b	Homo sapiens	33-39
15219196-2	2004	The serpin antithrombin (AT) is an important physiological regulator of FXa activity in an inhibition reaction that is enhanced by heparin.	Heparin	131-138	coagulation factor X	Homo sapiens	72-75
15219196-3	2004	Recently, Rezaie showed that calcium further enhanced the heparin-catalyzed AT inhibition of FXa by promoting "ternary complex" formation, and these results showed a role for the gamma-carboxyl-glutamate (Gla)-domain of FXa.	Heparin	58-65	coagulation factor X	Homo sapiens	93-96
15219196-3	2004	Recently, Rezaie showed that calcium further enhanced the heparin-catalyzed AT inhibition of FXa by promoting "ternary complex" formation, and these results showed a role for the gamma-carboxyl-glutamate (Gla)-domain of FXa.	Heparin	58-65	coagulation factor X	Homo sapiens	220-223
15219196-7	2004	Interestingly, three different effects were found with the recombinant FXa Gla-mutants for AT-heparin inhibition: (i) Gla--&gt;Asp 14 and 29 were enhanced without calcium; (ii) Gla--&gt;Asp 16 and 26 were not enhanced by calcium; and (iii) Gla--&gt;Asp 19 was essentially the same as wild-type recombinant FXa.	Heparin	94-101	coagulation factor X	Homo sapiens	71-74
15219196-7	2004	Interestingly, three different effects were found with the recombinant FXa Gla-mutants for AT-heparin inhibition: (i) Gla--&gt;Asp 14 and 29 were enhanced without calcium; (ii) Gla--&gt;Asp 16 and 26 were not enhanced by calcium; and (iii) Gla--&gt;Asp 19 was essentially the same as wild-type recombinant FXa.	Heparin	94-101	coagulation factor X	Homo sapiens	306-309
15223860-4	2004	FGF-2 is a member of a family of heparin binding growth factors that bind to heparan sulphate proteoglycans (HSPG), an important determinant of FGF-2 activity.	Heparin	33-40	syndecan 2	Homo sapiens	109-113
15199558-3	2004	In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade.	Heparin	82-89	coagulation factor X	Homo sapiens	187-196
15085072-6	2004	P-407 directly inhibits the heparin-releasable fraction of LPL and HL and indirectly increases the biologic activity of CETP and LCAT.	Heparin	28-35	lipoprotein lipase	Mus musculus	59-62
14707146-2	2004	Lymphotactin, the unique member of the "C" chemokine subclass, is a highly basic protein that binds heparin, a glycosaminoglycan, with high affinity (approximately 10 nm).	Heparin	100-107	X-C motif chemokine ligand 1	Homo sapiens	0-12
15005634-8	2004	Surface plasmon resonance studies of the interaction between heparin and BPTI indicated an unstable interaction with very low affinity (K(d) = 172 microM).	Heparin	61-68	spleen trypsin inhibitor I	Bos taurus	73-77
15005634-9	2004	In contrast, kinetic studies revealed a high-affinity interaction between heparin and fIXa (K(d) = 128 +/- 26 nM) and showed that the enhancement of BPTI inhibition of fIXa by heparin was well described by a competitive inhibition model where heparin acts as an affecter of fIXa reactivity with inhibitor.	Heparin	74-81	spleen trypsin inhibitor I	Bos taurus	149-153
15005634-9	2004	In contrast, kinetic studies revealed a high-affinity interaction between heparin and fIXa (K(d) = 128 +/- 26 nM) and showed that the enhancement of BPTI inhibition of fIXa by heparin was well described by a competitive inhibition model where heparin acts as an affecter of fIXa reactivity with inhibitor.	Heparin	176-183	spleen trypsin inhibitor I	Bos taurus	149-153
15005634-9	2004	In contrast, kinetic studies revealed a high-affinity interaction between heparin and fIXa (K(d) = 128 +/- 26 nM) and showed that the enhancement of BPTI inhibition of fIXa by heparin was well described by a competitive inhibition model where heparin acts as an affecter of fIXa reactivity with inhibitor.	Heparin	176-183	spleen trypsin inhibitor I	Bos taurus	149-153
14643896-11	2004	Heparin-releasable LPL activity in heart was 1.8-fold higher in mice fasted for 6h compared to fed controls.	Heparin	0-7	lipoprotein lipase	Mus musculus	19-22
14725788-14	2004	Anti-thrombin III alone was not inhibitory, but in the presence of heparin inhibited both MASP-1 and MASP-2.	Heparin	67-74	MBL associated serine protease 2	Homo sapiens	101-107
15035435-1	2004	Recently we identified a plasma serine protease with a high affinity to glycosaminoglycans like heparin or hyaluronic acid, termed hyaluronan-binding protease (HABP).	Heparin	96-103	hyaluronan binding protein 2	Homo sapiens	160-164
15035435-8	2004	Heparin and heparan sulfate fully protected bFGF from complexation and cleavage by HABP, although these glycosaminoglycans are known to enhance the proteolytic activity of HABP.	Heparin	0-7	hyaluronan binding protein 2	Homo sapiens	83-87
13679071-2	2003	AT inhibits clotting factors such as thrombin and factor Xa, a reaction catalyzed by heparin.	Heparin	85-92	coagulation factor X	Homo sapiens	50-59
12832413-7	2003	Heparin binding to f.Xa was previously shown to be promoted in the presence of Ca2+.	Heparin	0-7	coagulation factor X	Homo sapiens	19-23
12832413-9	2003	Thus, Ca2+ promotes heparin-catalyzed inhibition of f.IXa and f.Xa by antithrombin by augmenting the template mechanism.	Heparin	20-27	coagulation factor X	Homo sapiens	62-66
12886459-5	2003	On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times).	Heparin	19-26	kallikrein related peptidase 4	Homo sapiens	110-120
12695507-1	2003	Covalent antithrombin-heparin (ATH) complexes, formed spontaneously between antithrombin (AT) and unfractionated standard heparin (H), have a potent ability to catalyze the inhibition of factor Xa (or thrombin) by added AT.	Heparin	22-29	coagulation factor X	Homo sapiens	187-196
12695507-10	2003	Thus, exogenous AT can compete with the AT moiety of ATH for binding to the covalently linked heparin chain, leading to catalytic inhibition of factor Xa or thrombin.	Heparin	94-101	coagulation factor X	Homo sapiens	144-153
12796128-4	2003	METHODS AND RESULTS: We examined the relationship between the APTT and recurrent cardiovascular events and bleeding among 5058 patients with an acute coronary syndrome without ST elevation who received intravenous heparin in the OASIS-2 trial.	Heparin	214-221	cAMP responsive element binding protein 3 like 1	Homo sapiens	229-234
12734113-4	2003	Kallistatin mutants at the hinge region (A377T) and a major heparin-binding domain (K312A/K313A) were created by site-directed mutagenesis.	Heparin	60-67	serpin family A member 4	Homo sapiens	0-11
12734113-8	2003	To elucidate the role of the heparin-binding domain in modulating angiogenesis, we showed that wild-type kallistatin interrupted the binding of (125)I-labeled VEGF to endothelial cells, whereas kallistatin mutant K312A/K313A did not interfere with VEGF binding.	Heparin	29-36	serpin family A member 4	Homo sapiens	105-116
12770900-7	2003	The lifetime of the BPTI decamer is 101 +/- 4 min at 27 degrees C. We propose that the BPTI decamer, with a heparin chain threading the decamer channel, plays a functional role in the mast cell.	Heparin	108-115	spleen trypsin inhibitor I	Bos taurus	20-24
12770900-7	2003	The lifetime of the BPTI decamer is 101 +/- 4 min at 27 degrees C. We propose that the BPTI decamer, with a heparin chain threading the decamer channel, plays a functional role in the mast cell.	Heparin	108-115	spleen trypsin inhibitor I	Bos taurus	87-91
12773489-8	2003	Treatment of CD95-stimulated T cells with hIIA PLA2 resulted in the release of arachidonic acid but not oleic acid from cells and this release was blocked by heparin and heparinase III.	Heparin	158-165	phospholipase A2 group IIA	Homo sapiens	47-51
12948833-3	2003	Therefore, attention has focused on the development of low molecular weight heparins (LMW-heparins) that inhibit factor Xa but not thrombin.	Heparin	76-84	coagulation factor X	Homo sapiens	113-122
12948833-3	2003	Therefore, attention has focused on the development of low molecular weight heparins (LMW-heparins) that inhibit factor Xa but not thrombin.	Heparin	90-98	coagulation factor X	Homo sapiens	113-122
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	coagulation factor X	Homo sapiens	180-189
12948833-5	2003	Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin.	Heparin	125-132	coagulation factor X	Homo sapiens	180-189
12606556-11	2003	Furthermore, cleavage at Lys(36) appears to be selectively modulated by the C-terminal acidic region of A1, a region that may interact with factor Xa via its heparin-binding exosite.	Heparin	158-165	coagulation factor X	Homo sapiens	140-149
12704698-4	2003	VEGF was delivered by implanting VEGF-soaked heparin chromatography beads at three rostral-caudal locations in embryos with six somite pairs, which allowed us to study the effect of VEGF on different cellular activities.	Heparin	45-52	vascular endothelial growth factor A	Mus musculus	0-4
12704698-4	2003	VEGF was delivered by implanting VEGF-soaked heparin chromatography beads at three rostral-caudal locations in embryos with six somite pairs, which allowed us to study the effect of VEGF on different cellular activities.	Heparin	45-52	vascular endothelial growth factor A	Mus musculus	33-37
12704698-4	2003	VEGF was delivered by implanting VEGF-soaked heparin chromatography beads at three rostral-caudal locations in embryos with six somite pairs, which allowed us to study the effect of VEGF on different cellular activities.	Heparin	45-52	vascular endothelial growth factor A	Mus musculus	33-37
12731055-5	2003	Heparin inhibited intracellular calcium flux, respiratory burst and chemotactic responses of eosinophils to CCL11, but not to the chemoattractant C5a, and inhibited binding of CCL11 to CCR3.	Heparin	0-7	C-C motif chemokine receptor 3	Homo sapiens	185-189
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	0-7	C-C motif chemokine ligand 7	Homo sapiens	63-67
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	0-7	C-C motif chemokine ligand 5	Homo sapiens	79-83
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	166-173	C-C motif chemokine ligand 7	Homo sapiens	63-67
12731055-6	2003	Heparin also inhibited eosinophil stimulation by CCL11, CCL24, CCL7, CCL13 and CCL5 to differing degrees, which broadly correlated with their relative affinities for heparin.	Heparin	166-173	C-C motif chemokine ligand 5	Homo sapiens	79-83
12759624-12	2003	Prophylactic unfractionated or low-molecular-weight heparin was infused concomitant with TPA in 42% of the children and did not increase the risk of bleeding.	Heparin	52-59	chromosome 20 open reading frame 181	Homo sapiens	89-92
12505440-1	2003	We have found that incubation of heparin plasma with Ni(2+) or Co(2+) at concentrations below 100 microM can stimulate the conversion of complement factor C3 to C3b faster than magnesium, which is the natural cofactor in the alternative complement activation.	Heparin	33-40	complement C3	Homo sapiens	161-164
12600899-0	2003	Gene transfer of extracellular superoxide dismutase reduces arterial pressure in spontaneously hypertensive rats: role of heparin-binding domain.	Heparin	122-129	superoxide dismutase 3	Rattus norvegicus	17-51
12388125-5	2003	Inhibition of lipoprotein lipase (LPL) with tetrahydrolipstatin or dissociation of LPL from the heart with heparin reduced cardiac uptake of TG by 82 and 64%, respectively (P &lt; 0.01).	Heparin	107-114	lipoprotein lipase	Mus musculus	83-86
12668866-0	2003	Prolactin regulation by heparin-binding growth factors expressed in mouse pituitary cell lines.	Heparin	24-31	prolactin	Mus musculus	0-9
12749745-12	2003	CONCLUSION: The GP IIb/IIIa receptor antagonist abciximab, when used with aspirin and heparin, has demonstrated efficacy in reducing the short- and long-term risk of ischaemic complications in patients with ischaemic heart disease undergoing percutaneous coronary intervention, when used with aspirin and heparin.	Heparin	86-93	integrin subunit alpha 2b	Homo sapiens	16-22
12749745-12	2003	CONCLUSION: The GP IIb/IIIa receptor antagonist abciximab, when used with aspirin and heparin, has demonstrated efficacy in reducing the short- and long-term risk of ischaemic complications in patients with ischaemic heart disease undergoing percutaneous coronary intervention, when used with aspirin and heparin.	Heparin	305-312	integrin subunit alpha 2b	Homo sapiens	16-22
12557236-10	2003	Competition assay results suggested that the RNA aptamers might bind to the electropositive domain of bovine thrombin, that is, heparin-binding site, instead of fibrinogen-recognition exosite.	Heparin	128-135	coagulation factor II, thrombin	Bos taurus	109-117
12627496-3	2003	Herein, we show that the ORF47 kinase was resistant to heparin, while CKII activity is profoundly inhibited by the acidic molecule in vitro.	Heparin	55-62	tegument serine/threonine protein kinase	Human alphaherpesvirus 3	25-30
12471127-5	2002	To identify amino acids of FH involved in binding to C3d and heparin, we compared the sequences of FH and FHRs and constructed a homology-based molecular model of SCR19-20 of FH.	Heparin	61-68	complement factor H	Homo sapiens	27-29
12423774-4	2002	Adhesion could be blocked by heparin, which is also known to block vitronectin binding to Staphylococcus aureus.	Heparin	29-36	vitronectin	Homo sapiens	67-78
12381667-2	2002	We found that VEGF(120/120) mouse embryos, engineered to express solely an isoform of VEGF-A that lacks heparin-binding, and therefore extracellular matrix interaction domains, exhibited a specific decrease in capillary branch formation.	Heparin	104-111	vascular endothelial growth factor A	Mus musculus	86-92
12239166-2	2002	In the present study, we investigated this phenomenon by examining the ability of heparin to synergistically enhance interleukin-11 (IL-11)-induced osteoclast formation.	Heparin	82-89	interleukin 11	Mus musculus	117-131
12239166-2	2002	In the present study, we investigated this phenomenon by examining the ability of heparin to synergistically enhance interleukin-11 (IL-11)-induced osteoclast formation.	Heparin	82-89	interleukin 11	Mus musculus	133-138
12239166-5	2002	However, when cocultures were treated with both IL-11 and heparin, IL-11"s ability to induce TRAP(+) MNC formation was enhanced 6-fold.	Heparin	58-65	interleukin 11	Mus musculus	67-72
12239166-6	2002	In an attempt to resolve the mechanism responsible for this effect, we examined the ability of heparin to influence IL-11 signaling using murine calvaria cells.	Heparin	95-102	interleukin 11	Mus musculus	116-121
12239166-7	2002	Heparin was found to enhance both IL-11-induced STAT3-DNA complex formation and transactivation without altering either STAT3 (signal transducer and activator of transcription-3) tyrosine or serine phosphorylation.	Heparin	0-7	interleukin 11	Mus musculus	34-39
12190995-14	2002	The LPL activity was increased in post-heparin plasma and epididymal fat of treated db/db mice.	Heparin	39-46	lipoprotein lipase	Mus musculus	4-7
11994286-0	2002	Basic residues in azurocidin/HBP contribute to both heparin binding and antimicrobial activity.	Heparin	52-59	azurocidin 1	Homo sapiens	29-32
12071840-0	2002	New insights into heparin binding to vitronectin: studies with monoclonal antibodies.	Heparin	18-25	vitronectin	Homo sapiens	37-48
12270764-1	2002	OBJECTIVES: Heparin is thought to play a crucial role in the clinical monitoring of patients with acute coronary syndrome as well as after coronary bypass surgery in that it interferes with different commercial immunoassay test systems for cardiac troponin T (cTnT) and troponin I (cTnI).	Heparin	12-19	troponin I3, cardiac type	Homo sapiens	282-286
12270764-2	2002	The mechanism, however, by which heparin apparently affects the cTnT and cTnI levels in plasma is not yet resolved.	Heparin	33-40	troponin I3, cardiac type	Homo sapiens	73-77
12270764-6	2002	RESULTS: The data obtained indicate that heparin produces an apparent decrease in cTnT as well as of cTnI levels, analyzed either by the Elecsys, the Opus or the ACS:Centaur immunoassay systems.	Heparin	41-48	troponin I3, cardiac type	Homo sapiens	101-105
12270764-8	2002	Pretreatment of the heparin plasma samples either with heparinase or protamine cannot completely reverse the heparin-induced decrease in cTnT and cTnI levels and therefore addition of these reagents to the commercial test systems could not significantly improve the performance of the assay.	Heparin	20-27	troponin I3, cardiac type	Homo sapiens	146-150
12270764-10	2002	Affinity chromatography with heparin Sepharose demonstrates that cTnT and cTnI interact differentially with the negatively charged ligand.	Heparin	29-36	troponin I3, cardiac type	Homo sapiens	74-78
12270764-13	2002	In contrast, the effect of heparin on the cTnI immunoassay systems, is primarily indirect, most possibly induced by changes within the sample matrix itself.	Heparin	27-34	troponin I3, cardiac type	Homo sapiens	42-46
12076866-0	2002	Heparin accelerates liver regeneration following portal branch ligation in normal and cirrhotic rats with increased plasma hepatocyte growth factor levels.	Heparin	0-7	hepatocyte growth factor	Rattus norvegicus	123-147
12076866-1	2002	BACKGROUND/AIMS: Heparin is widely used as a general anticoagulant, and has been recently reported to elevate plasma hepatocyte growth factor (HGF) levels by releasing HGF sequestrated in the extracellular matrix.	Heparin	17-24	hepatocyte growth factor	Rattus norvegicus	117-141
12076866-1	2002	BACKGROUND/AIMS: Heparin is widely used as a general anticoagulant, and has been recently reported to elevate plasma hepatocyte growth factor (HGF) levels by releasing HGF sequestrated in the extracellular matrix.	Heparin	17-24	hepatocyte growth factor	Rattus norvegicus	143-146
12076866-1	2002	BACKGROUND/AIMS: Heparin is widely used as a general anticoagulant, and has been recently reported to elevate plasma hepatocyte growth factor (HGF) levels by releasing HGF sequestrated in the extracellular matrix.	Heparin	17-24	hepatocyte growth factor	Rattus norvegicus	168-171
12076866-5	2002	The plasma HGF concentrations were elevated by heparin treatment in both groups.	Heparin	47-54	hepatocyte growth factor	Rattus norvegicus	11-14
12076866-7	2002	CONCLUSIONS: Heparin treatment significantly accelerated liver regeneration following the PBL, with an increase in the plasma HGF levels in both normal and cirrhotic rats.	Heparin	13-20	hepatocyte growth factor	Rattus norvegicus	126-129
11896050-8	2002	rMCP-4 bound to heparin, and the enzymatic activity toward MeO-Suc-Arg-Ala-Tyr-pNA was strongly enhanced in the presence of heparin.	Heparin	16-23	mast cell protease 4	Rattus norvegicus	0-6
11896050-8	2002	rMCP-4 bound to heparin, and the enzymatic activity toward MeO-Suc-Arg-Ala-Tyr-pNA was strongly enhanced in the presence of heparin.	Heparin	124-131	mast cell protease 4	Rattus norvegicus	0-6
22896898-1	2002	Limited proteolysis of buffalo plasma fibronectin (FN) by thermolysin yielded four gelatin-binding fragments of which, the major 59 kDa fragment, GBF1, was isolated by gelatin-Sepharose and heparin-Sepharose affinity columns.	Heparin	190-197	golgi brefeldin A resistant guanine nucleotide exchange factor 1	Homo sapiens	146-150
11773078-3	2002	Heparin and plasminogen bound to VN fragments containing the heparin-binding domain, indicating that this domain was functionally active in the recombinant peptides.	Heparin	61-68	vitronectin	Homo sapiens	33-35
11751872-12	2002	Together, these results suggest that Schwann cells bind to collagen type V via syndecan-3-dependent binding to a novel high affinity heparin binding site in the alpha4(V)-NTD.	Heparin	133-140	syndecan 3	Rattus norvegicus	79-89
11851332-0	2002	Molecular modelling of the C-terminal domains of factor H of human complement: a correlation between haemolytic uraemic syndrome and a predicted heparin binding site.	Heparin	145-152	complement factor H	Homo sapiens	49-57
11723110-5	2002	The cell surface binding of MRP-14 was blocked by heparin, heparan sulfate, and chondroitin sulfate B, and the binding sites were sensitive to heparinase I and trypsin treatment but not to chondroitinase ABC.	Heparin	50-57	S100 calcium binding protein A9	Homo sapiens	28-34
11723110-7	2002	MRP-14 has a high affinity for heparin (K(d) = 6.1 +/- 3.4 nm), and this interaction mimicked that with the endothelial cells.	Heparin	31-38	S100 calcium binding protein A9	Homo sapiens	0-6
11854876-1	2002	OBJECTIVE: To determine the incidence of cerebral dysfunction in cardiac surgical patients exposed to heparin-bonded cardiopulmonary bypass (HB-CPB) versus nonheparin-bonded cardiopulmonary bypass (NH-CPB) circuits through neuropsychometric testing and to correlate these findings with markers of the systemic inflammatory response to CPB.	Heparin	102-109	carboxypeptidase B1	Homo sapiens	144-147
11801647-9	2002	Functionally, heparin-treated DCs respond to LPS or LPS plus IFN-gamma with higher IL-10 and less IL-12 production than heparin-untreated DCs.	Heparin	14-21	interleukin 10	Homo sapiens	83-88
11963730-12	2002	CONCLUSIONS: Of the patients in MITRA and MIR 92% received heparin during AMI.	Heparin	59-66	membrane associated ring-CH-type finger 8	Homo sapiens	42-45
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	79-86	low density lipoprotein receptor-related protein 1	Mus musculus	58-61
11705989-5	2002	Further analysis showed that association of rC4BPalpha to LRP was inhibited by heparin or by anti-C4BP antibody RU-3B9, which recognizes the heparin-binding region of the C4BP alpha-chains.	Heparin	141-148	low density lipoprotein receptor-related protein 1	Mus musculus	58-61
11795878-4	2002	The PKA phosphorylation of Vn is enhanced in the presence of either PAI-1, or heparin, or both.	Heparin	78-85	vitronectin	Homo sapiens	27-29
12613545-5	2002	Additional VEGF family members such as the heparin binding form of placenta growth factor (PlGF-2) and VEGF-B bind to NRP1, and it was also shown that both PlGF-2 and VEGF-C bind to NRP2.	Heparin	43-50	neuropilin 2	Homo sapiens	182-186
12124713-3	2002	These studies characterize a serum albumin (SA) solder containing heparin, designed to reduce microvascular thrombosis rates.	Heparin	66-73	albumin	Rattus norvegicus	29-42
11776314-4	2001	Four mutations, at positions C509, V551, R552 and R611 lead to significantly decreased binding to heparin in both plasma and rVWF.	Heparin	98-105	von Willebrand factor	Rattus norvegicus	125-129
11683636-2	2001	Recent studies have shown that the thrombin domain referred to as heparin binding site (HBS) is involved in the interaction with the platelet Gp(Ib)alpha.	Heparin	66-73	glycoprotein Ib platelet subunit alpha	Homo sapiens	142-153
11546811-6	2001	We have also identified a kinase activity associated with CDC34 in proliferating cells, and we show that this kinase is sensitive to heparin and can utilize GTP, strongly suggesting it is CK2.	Heparin	133-140	cell division cycle 34, ubiqiutin conjugating enzyme	Homo sapiens	58-63
11687304-6	2001	A similar 10(4)-10(5)-fold enhancement in the reactivity of factor Xa with prethrombin-2 and the HAT mutants was observed in the presence of the cofactors Va and heparin, respectively.	Heparin	162-169	coagulation factor X	Homo sapiens	60-69
11668418-0	2001	Cellular effects of factor Xa on vascular smooth muscle cells--inhibition by heparins?	Heparin	77-85	coagulation factor X	Homo sapiens	20-29
11668418-3	2001	Unfractionated heparin (UFH) as well as low molecular weight heparin (LMWH) (enoxaparin) inhibited the mitogenic effects of FXa, thrombin and fetal calf serum (FCS), but did not reduce mitogenesis induced by PDGF.	Heparin	15-22	coagulation factor X	Homo sapiens	124-127
11668418-3	2001	Unfractionated heparin (UFH) as well as low molecular weight heparin (LMWH) (enoxaparin) inhibited the mitogenic effects of FXa, thrombin and fetal calf serum (FCS), but did not reduce mitogenesis induced by PDGF.	Heparin	24-27	coagulation factor X	Homo sapiens	124-127
11668418-3	2001	Unfractionated heparin (UFH) as well as low molecular weight heparin (LMWH) (enoxaparin) inhibited the mitogenic effects of FXa, thrombin and fetal calf serum (FCS), but did not reduce mitogenesis induced by PDGF.	Heparin	61-68	coagulation factor X	Homo sapiens	124-127
11668418-4	2001	Similarly, both UFH and LMWH inhibited the activation of extracellular signal-regulated kinase (ERK-1/2) by FXa, thrombin and FCS, but not by PDGF.	Heparin	16-19	coagulation factor X	Homo sapiens	108-111
11557039-3	2001	Heparin competed with Grp94-CT for binding to CK2 alpha.	Heparin	0-7	casein kinase 2 alpha 2	Homo sapiens	46-55
11531671-0	2001	Maternal anti-factor Xa activity following subcutaneous unfractionated heparin after Caesarean section.	Heparin	71-78	coagulation factor X	Homo sapiens	14-23
11560562-1	2001	AIMS: The objective of our study was to define the interaction between either unfractionated heparin (UFH) or a low molecular weight heparin, reviparin (REV), and the pharmacodynamic profile of the GPIIb/IIIa-antagonists abciximab (ABC) or tirofiban (T).	Heparin	93-100	integrin subunit alpha 2b	Homo sapiens	198-203
11560562-1	2001	AIMS: The objective of our study was to define the interaction between either unfractionated heparin (UFH) or a low molecular weight heparin, reviparin (REV), and the pharmacodynamic profile of the GPIIb/IIIa-antagonists abciximab (ABC) or tirofiban (T).	Heparin	102-105	integrin subunit alpha 2b	Homo sapiens	198-203
11560562-1	2001	AIMS: The objective of our study was to define the interaction between either unfractionated heparin (UFH) or a low molecular weight heparin, reviparin (REV), and the pharmacodynamic profile of the GPIIb/IIIa-antagonists abciximab (ABC) or tirofiban (T).	Heparin	133-140	integrin subunit alpha 2b	Homo sapiens	198-203
11440913-3	2001	This heparin-releasable LPL pool remained constant over a variety of experimental conditions, including workload and fatty acid concentrations, making the mouse heart a suitable model to study chylomicron catabolism.	Heparin	5-12	lipoprotein lipase	Mus musculus	24-27
11432747-5	2001	This autoactivation was significantly enhanced in the presence of heparin, whereas Ca2+ ions stabilized single-chain FSAP (the proenzyme) resulting in slower autoactivation kinetics.	Heparin	66-73	hyaluronan binding protein 2	Homo sapiens	117-121
11460008-4	2001	The kinetic studies of inhibition of thrombin by C1-INH showed an average second-order rate constant of 19/s per mol/l, which was significantly increased in the presence of heparin.	Heparin	173-180	serpin family G member 1	Homo sapiens	49-55
11460009-3	2001	Accordingly, in this study, we measured maximal t-PA release in patients with ACS before, during, and after heparin treatment.	Heparin	108-115	chromosome 20 open reading frame 181	Homo sapiens	48-52
11460009-9	2001	Heparin treatment was associated with a significant increase of plasma t-PA, while it did not affect maximal t-PA release.	Heparin	0-7	chromosome 20 open reading frame 181	Homo sapiens	71-75
11434701-1	2001	Heparin-induced thrombocytopenia (HIT) is a hypercoagulable syndrome strongly associated with thrombosis that is usually treated with drugs that inhibit factor Xa (danaparoid) or thrombin (lepirudin).	Heparin	0-7	coagulation factor X	Homo sapiens	153-162
11278930-0	2001	Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence.	Heparin	0-7	coagulation factor X	Homo sapiens	66-75
11278930-2	2001	Heparin activates the primary serpin inhibitor of blood clotting proteinases, antithrombin, both by an allosteric conformational change mechanism that specifically enhances factor Xa inactivation and by a ternary complex bridging mechanism that promotes the inactivation of thrombin and other target proteinases.	Heparin	0-7	coagulation factor X	Homo sapiens	173-182
18228300-2	2001	First plasma is depleted of fibronectin and other heparin-binding proteins; the sample is then treated with urea to activate the heparin-binding activity of vitronectin.	Heparin	50-57	vitronectin	Homo sapiens	157-168
11358513-7	2001	Heparin, but not other glycosaminoglycans, enhanced dramatically the ability of hK3 but not hK2 to degrade IGFBP-3 and IGFBP-4.	Heparin	0-7	RBPJ pseudogene 3	Homo sapiens	92-95
11358513-7	2001	Heparin, but not other glycosaminoglycans, enhanced dramatically the ability of hK3 but not hK2 to degrade IGFBP-3 and IGFBP-4.	Heparin	0-7	insulin like growth factor binding protein 4	Homo sapiens	119-126
11342582-3	2001	Three basic amino acids in the carboxyl terminal region of LpL were mutated, yielding an active enzyme with reduced heparin binding.	Heparin	116-123	lipoprotein lipase	Mus musculus	59-62
11342582-8	2001	Thus, heparin association is required for LpL stability and normal physiologic functions.	Heparin	6-13	lipoprotein lipase	Mus musculus	42-45
11312365-2	2001	Pretreatment of cells with heparinase 1 or heparin blocks the binding of radiolabeled virus to the cell surface, and heparin prevents infection of rhabdomyosarcoma cells by certain EV, including several low-passage clinical isolates of EV 6 and some EV that do not bind DAF.	Heparin	27-34	CD55 molecule (Cromer blood group)	Homo sapiens	270-273
11340354-8	2001	The mRNA levels for heparin-binding EGF and TGF-alpha, two EGF receptor ligands, increased within 1 h of injury.	Heparin	20-27	epidermal growth factor receptor	Rattus norvegicus	59-71
11287128-1	2001	Fluorescence and stopped flow methods were used to compare clinically used heparins with regard to their ability to bind to antithrombin and to accelerate the inactivation of factor Xa.	Heparin	75-83	coagulation factor X	Homo sapiens	175-184
11287128-4	2001	The rate of factor Xa inhibition by antithrombin increased with the concentration of the examined heparins to the same limiting value, but the concentration required for maximal acceleration depended on the preparation.	Heparin	98-106	coagulation factor X	Homo sapiens	12-21
11287128-6	2001	In contrast, in the presence of Ca UFH accelerated the inhibition of factor Xa by antithrombin 10-fold more efficiently than comparable concentrations of the high affinity fractions of enoxaparin and fragmin.	Heparin	35-38	coagulation factor X	Homo sapiens	69-78
11287128-8	2001	In conclusion, under physiologic conditions the anti-factor Xa activity of heparin results from a composite effect of chain length and the content of material with high affinity to antithrombin.	Heparin	75-82	coagulation factor X	Homo sapiens	53-62
11341511-6	2001	At 28 days, bound thrombin activity and platelet adhesion 1 h after a repeated balloon injury decreased in animals receiving NAC, HEP and NAC+HEP bv 54%, 63% and 64% for thrombin activity (p &lt;0.05 vs CONTROLS), and by 56%, 66% and 75% respectively for 111Indium-platelet deposition (p &lt;0.05 vs CONTROLS).	Heparin	130-133	prothrombin	Oryctolagus cuniculus	170-178
11106649-2	2001	In human embryonic kidney 293 cells, the heparin-binding enzymes sPLA(2)-IIA, -IID, and -V promote stimulus-dependent arachidonic acid release and prostaglandin E(2) production in a manner dependent on the heparan sulfate proteoglycan glypican.	Heparin	41-48	glypican 1	Homo sapiens	235-243
11106649-4	2001	Heparin nonbinding sPLA(2)-X liberates arachidonic acid most likely from the phosphatidylcholine-rich outer plasma membrane in a glypican-independent manner.	Heparin	0-7	glypican 1	Homo sapiens	129-137
11024046-10	2001	Finally, we demonstrated that low molecular weight heparin (which binds to thrombin exosite II) but not hirugen (residues 54-65 of hirudin, which binds to exosite I of thrombin) inhibited thrombin binding to GPIb alpha.	Heparin	51-58	glycoprotein Ib platelet subunit alpha	Homo sapiens	208-218
11367528-2	2001	Factor H (fH) plays a vital role in restricting complement activation on host cells through interactions with polyanions such as heparin, while allowing activation to proceed on foreign surfaces.	Heparin	129-136	complement factor H	Homo sapiens	0-8
11367528-2	2001	Factor H (fH) plays a vital role in restricting complement activation on host cells through interactions with polyanions such as heparin, while allowing activation to proceed on foreign surfaces.	Heparin	129-136	complement factor H	Homo sapiens	10-12
11367528-8	2001	By alanine replacement mutagenesis, we demonstrated that these residues are involved in heparin, CRP and M protein binding, which indicates that there is a common site within fH SCR 7 responsible for multiple ligand recognition.	Heparin	88-95	complement factor H	Homo sapiens	175-177
11392963-5	2001	Purified E and NS1 proteins did not react with viral RNA, while incubation with recombinant nonstructural TBE virus NS3 protein led to a shift in the mobility of TBE virus RNA in gel in the absence of cross-linking under conditions of UV exposure after addition of heparin.	Heparin	265-272	KRAS proto-oncogene, GTPase	Homo sapiens	116-119
11157673-9	2001	In cells microinjected with a low dose of heparin, VP-induced CCE was more susceptible than IICR to mild inhibition of both IP(3)R(1) and IP(3)R(3).	Heparin	42-49	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	124-133
11157673-10	2001	A high dose of heparin had a similar effect to complete inhibition of IP(3)R(1) expression: it blocked VP-evoked IICR entirely and CCE by 90%.	Heparin	15-22	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	70-78
11179981-7	2001	Heparin, a known in vitro activator of PKR, enhanced eIF2alpha phosphorylation by PKR mutants lacking their entire N-terminal sequences, including the dsRBDs.	Heparin	0-7	eukaryotic translation initiation factor 2A	Homo sapiens	53-62
11207370-2	2001	The paper presents a structural model derived from two crystal forms of the protein (PDB: 1G40 and 1G44) that defines an interaction surface implicated in inhibition of complement C3 proteins and visualizes heparin binding sites.	Heparin	207-214	complement C3	Homo sapiens	169-182
11770031-10	2001	Using heparin-coated circuits in group 3 led to IL-10 upregulation (P &lt; 0.05) and IL-6 suppression (P &lt; 0.05).	Heparin	6-13	interleukin 10	Homo sapiens	48-53
11480172-11	2001	There was a heparin-binding site in positions 175-181 (L-R-R-D-S-H-K) among prolactin amino acid sequences of broiler and Taihe Silkies.	Heparin	12-19	prolactin	Gallus gallus	76-85
11007795-0	2000	The amino-terminal part of PRELP binds to heparin and heparan sulfate.	Heparin	42-49	proline and arginine rich end leucine rich repeat protein	Homo sapiens	27-32
11007795-5	2000	We show here that PRELP indeed binds heparin and heparan sulfate.	Heparin	37-44	proline and arginine rich end leucine rich repeat protein	Homo sapiens	18-23
11007795-7	2000	The dissociation constant for the interaction of PRELP with heparin was determined by an in solution binding assay and by surface plasmon resonance analysis to be in the range of 10-30 nm.	Heparin	60-67	proline and arginine rich end leucine rich repeat protein	Homo sapiens	49-54
11007795-11	2000	Fibroblasts bind PRELP, and this interaction is inhibited with heparin, suggesting a function for PRELP as a linker between the matrix and cell surface proteoglycans.	Heparin	63-70	proline and arginine rich end leucine rich repeat protein	Homo sapiens	17-22
11007795-11	2000	Fibroblasts bind PRELP, and this interaction is inhibited with heparin, suggesting a function for PRELP as a linker between the matrix and cell surface proteoglycans.	Heparin	63-70	proline and arginine rich end leucine rich repeat protein	Homo sapiens	98-103
11100007-2	2000	Current and evolving technologies to monitor the extent of inhibition of platelet aggregation and activity of factor Xa caused by IIb/IIIa antagonists and low-molecular-weight heparin, respectively, will be covered in this overview.	Heparin	176-183	coagulation factor X	Homo sapiens	110-119
11211922-9	2000	Heparin also impaired the drop in the pleural leukocyte numbers evoked by PAF and bradykinin.	Heparin	0-7	PCNA clamp associated factor	Rattus norvegicus	74-77
11053056-3	2000	The expression was suppressed by heparin and quercetin, the drugs with anti-AP-1 activities.	Heparin	33-40	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	76-80
10944521-8	2000	This second processing step removes two thrombospondin repeats from the carboxyl-terminal end of p87-METH-1 and alters the affinity of the protein to heparin and endothelial cultures.	Heparin	150-157	inner membrane mitochondrial protein	Homo sapiens	97-100
11041873-0	2000	Mechanism for activation of mouse mast cell tryptase: dependence on heparin and acidic pH for formation of active tetramers of mouse mast cell protease 6.	Heparin	68-75	tryptase beta 2	Mus musculus	133-153
11041873-7	2000	However, when heparin was present, 6xHis-EK-mMCP-6 yielded active enzyme when enterokinase cleavage was performed at pH 5.5-6.0 but not at neutral pH.	Heparin	14-21	tryptase beta 2	Mus musculus	44-50
11041873-8	2000	Affinity chromatography analysis showed that mMCP-6 bound strongly to heparin-Sepharose at pH 6.0 but not at neutral pH.	Heparin	70-77	tryptase beta 2	Mus musculus	45-51
11009624-0	2000	Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex.	Heparin	17-24	coagulation factor X	Homo sapiens	140-149
11009624-2	2000	Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa.	Heparin	0-7	coagulation factor X	Homo sapiens	36-45
11009624-2	2000	Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa.	Heparin	0-7	coagulation factor X	Homo sapiens	349-358
11009624-2	2000	Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa.	Heparin	146-153	coagulation factor X	Homo sapiens	36-45
11009624-3	2000	To provide direct evidence for this bridging mechanism, we studied the heparin-catalyzed reaction of antithrombin with factor Xa, Gla-domainless factor Xa (GDFXa), and a heparin binding exosite mutant of GDFXa in the absence and presence of calcium using rapid kinetic methods.	Heparin	71-78	coagulation factor X	Homo sapiens	119-128
11009624-3	2000	To provide direct evidence for this bridging mechanism, we studied the heparin-catalyzed reaction of antithrombin with factor Xa, Gla-domainless factor Xa (GDFXa), and a heparin binding exosite mutant of GDFXa in the absence and presence of calcium using rapid kinetic methods.	Heparin	71-78	coagulation factor X	Homo sapiens	145-154
11009624-4	2000	The pseudo-first-order rate constant for factor Xa inhibition by antithrombin complexed with a long-chain approximately 70-saccharide heparin showed a saturable dependence on inhibitor concentration in the presence but not in the absence of 2.5 mM Ca(2+), indicating the formation of an intermediate heparin-serpin-proteinase encounter complex with a dissociation constant of approximately 90 nM prior to formation of the stable serpin-proteinase complex with a rate constant of approximately 20 s(-1).	Heparin	134-141	coagulation factor X	Homo sapiens	41-50
11009624-7	2000	These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism.	Heparin	51-58	coagulation factor X	Homo sapiens	83-92
11009624-7	2000	These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism.	Heparin	51-58	coagulation factor X	Homo sapiens	245-254
11009624-7	2000	These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism.	Heparin	224-231	coagulation factor X	Homo sapiens	83-92
11009624-7	2000	These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism.	Heparin	224-231	coagulation factor X	Homo sapiens	245-254
11050697-12	2000	Both CTC-111 (100,000 U/kg) and heparin (800 IU/kg) decreased the increase in GOT and GPT levels significantly, whereas neither affected the increase in Cre or BUN.	Heparin	32-39	glutamic--pyruvic transaminase	Rattus norvegicus	86-89
10961890-0	2000	Heparin and heparan sulfate bind interleukin-10 and modulate its activity.	Heparin	0-7	interleukin 10	Homo sapiens	33-47
10961890-3	2000	It was demonstrated by affinity chromatography that hIL-10 binds strongly to heparin-agarose at physiological pH.	Heparin	77-84	interleukin 10	Homo sapiens	52-58
10961890-6	2000	Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner.	Heparin	8-15	interleukin 10	Homo sapiens	102-108
10961890-6	2000	Soluble heparin, heparan sulfate, chondroitin sulfate, and dermatan sulfate were shown to inhibit the hIL-10-induced expression of CD16 and CD64 in a concentration-dependent manner.	Heparin	8-15	Fc gamma receptor IIIa	Homo sapiens	131-135
10961890-9	2000	The antagonistic effect of heparin on hIL-10 activity was shown to be dependent on N-sulfation, inasmuch as de-N-sulfated heparin had little or no inhibitory effect on the IL-10- induced expression of CD16, whereas the effect of de-O-sulfated heparin was comparable to that of unmodified heparin.	Heparin	27-34	interleukin 10	Homo sapiens	38-44
10961890-9	2000	The antagonistic effect of heparin on hIL-10 activity was shown to be dependent on N-sulfation, inasmuch as de-N-sulfated heparin had little or no inhibitory effect on the IL-10- induced expression of CD16, whereas the effect of de-O-sulfated heparin was comparable to that of unmodified heparin.	Heparin	27-34	interleukin 10	Homo sapiens	39-44
10961890-9	2000	The antagonistic effect of heparin on hIL-10 activity was shown to be dependent on N-sulfation, inasmuch as de-N-sulfated heparin had little or no inhibitory effect on the IL-10- induced expression of CD16, whereas the effect of de-O-sulfated heparin was comparable to that of unmodified heparin.	Heparin	27-34	Fc gamma receptor IIIa	Homo sapiens	201-205
10961890-9	2000	The antagonistic effect of heparin on hIL-10 activity was shown to be dependent on N-sulfation, inasmuch as de-N-sulfated heparin had little or no inhibitory effect on the IL-10- induced expression of CD16, whereas the effect of de-O-sulfated heparin was comparable to that of unmodified heparin.	Heparin	122-129	interleukin 10	Homo sapiens	38-44
10961890-9	2000	The antagonistic effect of heparin on hIL-10 activity was shown to be dependent on N-sulfation, inasmuch as de-N-sulfated heparin had little or no inhibitory effect on the IL-10- induced expression of CD16, whereas the effect of de-O-sulfated heparin was comparable to that of unmodified heparin.	Heparin	122-129	interleukin 10	Homo sapiens	38-44
10974231-3	2000	RESULTS: A significantly higher IC50s was shown with heparin (free ionized calcium=1.1 mM) as compared to that with citrate (free ionized calcium=0.12 mM) with class II GPIIb/IIIa antagonists (P&lt;0.01) such as Orbofiban, and Integrilin.	Heparin	53-60	integrin subunit alpha 2b	Homo sapiens	169-174
10973863-5	2000	RESULTS: Mean results (+/- 95% confidence interval) in heparin-plasma compared with serum were 101% +/- 2% (AxSYM cTnI), 94% +/- 3% (ACS:Centaur cTnI), and 99% +/- 3% (Elecsys cTnT).	Heparin	55-62	troponin I3, cardiac type	Homo sapiens	114-118
11019977-7	2000	At high pharmacologic concentrations, unfractionated heparin and enoxaparin, but not hirudin, further reduced factor V/Va binding to the surface of activated platelets in the presence of GPIIb-IIa antagonists.	Heparin	53-60	integrin subunit alpha 2b	Homo sapiens	187-192
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	syndecan 2	Homo sapiens	219-223
10873433-2	2000	Fibroblast growth factor-2 (FGF-2) is one of the best characterized of the heparin-binding growth factors and it has been shown experimentally that heparin regulation of FGF-2 activity is dependent on the level of cell HSPG and the concentration of heparin.	Heparin	148-155	syndecan 2	Homo sapiens	219-223
10949727-6	2000	Mean finger blood flow recovery time improved, and serum levels of circulating ICAM-1, VCAM-1 and E-selectin were lower at completion of heparin therapy, but changes did not reach statistical significance.	Heparin	137-144	intercellular adhesion molecule 1	Homo sapiens	79-85
10769077-7	2000	Finally, our analysis of NS3 processive unwinding under single cycle conditions by addition of heparin in both helicase and RNA-stimulated ATPase assays led to two conclusions: (i) NS3-associated helicase acts processively; (ii) most of the NS3 RNA-stimulated ATPase activity may not be directly coupled to translocation of the enzyme along the substrate RNA molecule.	Heparin	95-102	KRAS proto-oncogene, GTPase	Homo sapiens	181-184
10769077-7	2000	Finally, our analysis of NS3 processive unwinding under single cycle conditions by addition of heparin in both helicase and RNA-stimulated ATPase assays led to two conclusions: (i) NS3-associated helicase acts processively; (ii) most of the NS3 RNA-stimulated ATPase activity may not be directly coupled to translocation of the enzyme along the substrate RNA molecule.	Heparin	95-102	KRAS proto-oncogene, GTPase	Homo sapiens	181-184
10775589-9	2000	Finally, analysis of the biochemical properties of recombinant gp65 revealed a specific interaction with heparin and heparan sulfate proteoglycans and not with closely related molecules such as N-acetylheparin and de-N-sulfated heparin.	Heparin	105-112	neuroplastin	Homo sapiens	63-67
10850654-3	2000	Correlation between the transfection efficiency and the stability of the carrier/DNA complex was investigated by measuring the carrier size changes and by observing the degree of DNA protection against DNase I digestion in the presence of heparin.	Heparin	239-246	deoxyribonuclease I	Mus musculus	202-209
10725457-5	2000	We report here that hsp40, hsp60, hsc70, hsp70, hsp84, hsp86, and gp96 (grp94) but not BiP (grp78) and calreticulin can be separated from a single tumor sample in one step using heparin-agarose chromatography.	Heparin	178-185	heat shock protein family A (Hsp70) member 8	Homo sapiens	34-39
10725457-5	2000	We report here that hsp40, hsp60, hsc70, hsp70, hsp84, hsp86, and gp96 (grp94) but not BiP (grp78) and calreticulin can be separated from a single tumor sample in one step using heparin-agarose chromatography.	Heparin	178-185	heat shock protein family A (Hsp70) member 4	Homo sapiens	41-46
10725457-5	2000	We report here that hsp40, hsp60, hsc70, hsp70, hsp84, hsp86, and gp96 (grp94) but not BiP (grp78) and calreticulin can be separated from a single tumor sample in one step using heparin-agarose chromatography.	Heparin	178-185	heat shock protein 90 beta family member 1	Homo sapiens	66-70
10725457-5	2000	We report here that hsp40, hsp60, hsc70, hsp70, hsp84, hsp86, and gp96 (grp94) but not BiP (grp78) and calreticulin can be separated from a single tumor sample in one step using heparin-agarose chromatography.	Heparin	178-185	heat shock protein 90 beta family member 1	Homo sapiens	72-77
10735780-4	2000	Unfractionated heparin increased adenosine diphosphate-induced expression of P-selectin and GP IIb-IIIa in a dose-dependent manner.	Heparin	15-22	integrin subunit alpha 2b	Homo sapiens	92-98
10735780-8	2000	In contrast, protamine antagonized the effect of heparin on GP IIb-IIIa expression but potentiated the effect of heparin on P-selectin expression.	Heparin	49-56	integrin subunit alpha 2b	Homo sapiens	60-66
10760814-9	2000	We show that FHL-1 presents a higher binding affinity for S. pyogenes than factor H because it carries a hydrophobic, high-affinity, GAS binding site in addition to the heparin binding site in SCR7.	Heparin	169-176	complement factor H	Homo sapiens	75-83
10731722-0	2000	Peroxiredoxin IV is a secretable protein with heparin-binding properties under reduced conditions.	Heparin	46-53	peroxiredoxin 4	Homo sapiens	0-16
10660541-0	2000	The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III.	Heparin	81-88	glycoprotein Ib platelet subunit alpha	Homo sapiens	41-61
10660541-0	2000	The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III.	Heparin	153-160	glycoprotein Ib platelet subunit alpha	Homo sapiens	41-61
10660541-6	2000	To identify the thrombin-binding domain on GpIbalpha, we examined the effect of GpIbalpha(1-282), a GpIbalpha fragment released by the cobra venom mocarhagin on the heparin-catalyzed rate of thrombin inhibition by antithrombin III (AT).	Heparin	165-172	glycoprotein Ib platelet subunit alpha	Homo sapiens	80-89
10660541-6	2000	To identify the thrombin-binding domain on GpIbalpha, we examined the effect of GpIbalpha(1-282), a GpIbalpha fragment released by the cobra venom mocarhagin on the heparin-catalyzed rate of thrombin inhibition by antithrombin III (AT).	Heparin	165-172	glycoprotein Ib platelet subunit alpha	Homo sapiens	80-89
10660541-9	2000	Measurements of the apparent equilibrium constant of the GpIbalpha(1-282) binding to thrombin as a function of different salts (NaCl and tetramethyl-ammonium chloride) concentration (0.1-0.2 M) indicated a large salt dependence (Gamma(+/-) = -4.5), similar to that pertaining to the heparin binding to thrombin.	Heparin	283-290	glycoprotein Ib platelet subunit alpha	Homo sapiens	57-66
10660541-13	2000	Neither alpha- nor gamma(T)-thrombin bound to GpIbalpha(1-271), suggesting that the Asp(272)-Glu(282) region of GpIbalpha may act as a "heparin-like" ligand for the thrombin HBS, thereby inhibiting heparin binding to thrombin.	Heparin	136-143	glycoprotein Ib platelet subunit alpha	Homo sapiens	112-121
10660541-13	2000	Neither alpha- nor gamma(T)-thrombin bound to GpIbalpha(1-271), suggesting that the Asp(272)-Glu(282) region of GpIbalpha may act as a "heparin-like" ligand for the thrombin HBS, thereby inhibiting heparin binding to thrombin.	Heparin	198-205	glycoprotein Ib platelet subunit alpha	Homo sapiens	112-121
10958381-11	2000	Only heparin inhibited both MMP-1 and MMP-2/MMP-9 activity.	Heparin	5-12	matrix metallopeptidase 9	Homo sapiens	44-49
10653134-4	2000	Agrin actions were blocked by heparin and the formation of functional neuromuscular contacts was quantitated.	Heparin	30-37	agrin	Homo sapiens	0-5
28176065-4	2000	Agrin actions were blocked by heparin and the formation of functional neuromuscular contacts was quantitated.	Heparin	30-37	agrin	Homo sapiens	0-5
10607857-10	1999	HepArrest binds low molecular weight heparins and causes reversal of anticoagulation by low molecular weight heparins, as determined by activated partial thromboplastin time, thrombin time, or factor Xa neutralization assays.	Heparin	109-117	coagulation factor X	Homo sapiens	193-202
10607916-1	1999	Pleiotrophin (PTN) is a secreted heparin-binding, developmentally regulated protein that is found in abundance in fetal, but not mature, cartilage.	Heparin	33-40	pleiotrophin	Bos taurus	0-12
10607916-1	1999	Pleiotrophin (PTN) is a secreted heparin-binding, developmentally regulated protein that is found in abundance in fetal, but not mature, cartilage.	Heparin	33-40	pleiotrophin	Bos taurus	14-17
10562536-1	1999	Recombinant mouse endostatin produced by mammalian cells was shown to bind to heparin with a K(d) of 0.3 microM, suggesting that this interaction may play a role in its anti-angiogenic activity.	Heparin	78-85	collagen, type XVIII, alpha 1	Mus musculus	18-28
10619025-1	1999	Laminin G-like (LG) modules in the extracellular matrix glycoproteins laminin, perlecan, and agrin mediate the binding to heparin and the cell surface receptor alpha-dystroglycan (alpha-DG).	Heparin	122-129	agrin	Homo sapiens	93-98
10510057-0	1999	Heparin inhibits ligand binding to the leukocyte integrin Mac-1 (CD11b/CD18).	Heparin	0-7	integrin subunit alpha M	Homo sapiens	58-63
10510057-0	1999	Heparin inhibits ligand binding to the leukocyte integrin Mac-1 (CD11b/CD18).	Heparin	0-7	integrin subunit alpha M	Homo sapiens	65-70
10510057-2	1999	Recently, it has been described that leukocytes adhere on immobilized heparin mediated by the integrin Mac-1 (CD11b/CD18, alphaMbeta2, or CR3).	Heparin	70-77	integrin subunit alpha M	Homo sapiens	103-108
10510057-2	1999	Recently, it has been described that leukocytes adhere on immobilized heparin mediated by the integrin Mac-1 (CD11b/CD18, alphaMbeta2, or CR3).	Heparin	70-77	integrin subunit alpha M	Homo sapiens	110-115
10510057-4	1999	METHODS AND RESULTS: Binding of unfractionated heparin to Mac-1 on PMA-stimulated monocytes and granulocytes was directly demonstrated in flow cytometry, whereas no binding of heparin was detected on unstimulated leukocytes.	Heparin	47-54	integrin subunit alpha M	Homo sapiens	58-63
10510057-5	1999	Unfractionated heparin inhibited binding of the soluble ligands fibrinogen, factor X, and iC3b to Mac-1.	Heparin	15-22	integrin subunit alpha M	Homo sapiens	98-103
10510057-6	1999	Adhesion of the monocytic cell line THP-1 and of peripheral monocytes and granulocytes to immobilized ICAM-1 was impaired by unfractionated heparin, to the same extent as with inhibition of Mac-1 by monoclonal antibodies such as c7E3.	Heparin	140-147	intercellular adhesion molecule 1	Homo sapiens	102-108
10510057-7	1999	Low-molecular-weight heparin also inhibits binding of fibrinogen to Mac-1.	Heparin	21-28	integrin subunit alpha M	Homo sapiens	68-73
10510057-8	1999	Additionally, flow cytometry of whole blood preparations of patients treated with unfractionated heparin revealed an inhibitory effect of heparin on the binding of fibrinogen to Mac-1 that correlates (n= 48, r=0.63, P&lt;0.001) to the extent of prolongation of the activated partial thromboplastin time.	Heparin	97-104	integrin subunit alpha M	Homo sapiens	178-183
10510057-8	1999	Additionally, flow cytometry of whole blood preparations of patients treated with unfractionated heparin revealed an inhibitory effect of heparin on the binding of fibrinogen to Mac-1 that correlates (n= 48, r=0.63, P&lt;0.001) to the extent of prolongation of the activated partial thromboplastin time.	Heparin	138-145	integrin subunit alpha M	Homo sapiens	178-183
10510057-10	1999	The binding of heparin to Mac-1 and the resulting inhibition in binding of Mac-1 ligands may directly modulate coagulation, inflammation, and cell proliferation.	Heparin	15-22	integrin subunit alpha M	Homo sapiens	26-31
10510057-10	1999	The binding of heparin to Mac-1 and the resulting inhibition in binding of Mac-1 ligands may directly modulate coagulation, inflammation, and cell proliferation.	Heparin	15-22	integrin subunit alpha M	Homo sapiens	75-80
10497166-1	1999	A sequence-specific heparin pentasaccharide activates the serpin, antithrombin, to inhibit factor Xa through an allosteric mechanism, whereas full-length heparin chains containing this sequence further activate the serpin to inhibit thrombin by an alternative bridging mechanism.	Heparin	20-27	coagulation factor X	Homo sapiens	91-100
10505759-8	1999	These data suggest that glypican-1 plays an important role in the responses of pancreatic cancer cells to heparin-binding growth factors, and documents for the first time that its expression may enhance tumorigenic potential in vivo.	Heparin	106-113	glypican 1	Homo sapiens	24-34
10480945-8	1999	The interaction of cells with the heparin-binding domain of vitronectin resulted in changes in actin microfilament organization and the subcellular distribution of the actin-associated proteins alpha-actinin and talin.	Heparin	34-41	vitronectin	Homo sapiens	60-71
10480945-9	1999	These data suggest a mechanism whereby the heparin-binding domain of vitronectin regulates the deposition of fibronectin into the extracellular matrix through alterations in the organization of the actin cytoskeleton.	Heparin	43-50	vitronectin	Homo sapiens	69-80
11721408-1	1999	OBJECTIVE: To verify whether heparin could enhance the stimulating effect of Tpo on megakaryocytopoiesis.	Heparin	29-36	thyroid peroxidase	Homo sapiens	77-80
11721408-4	1999	RESULTS: Heparin could enhance the stimulating effect of Tpo on stimulating the proliferation of M-07e, the growth of CFU-MK from human cord blood CD34+ cells and in vivo megakaryocytopoiesis in mice.	Heparin	9-16	thyroid peroxidase	Homo sapiens	57-60
10446158-2	1999	Surface plasmon resonance kinetic analysis shows that the CXC chemokine stromal cell-derived factor-1alpha (SDF-1alpha), which binds the CXCR4 receptor, associates with heparin with an affinity constant of 38.4 nM (k(on) = 2.16 x 10(6) M(-1) s(-1) and k(off) = 0.083 x s(-1)).	Heparin	169-176	C-X-C motif chemokine receptor 4	Homo sapiens	137-142
10409677-5	1999	The binding of VEGF-B(167) was mediated by the heparin binding domain, whereas the binding of VEGF-B(186) to NRP1 was regulated by exposure of a short COOH-terminal proline-rich peptide upon its proteolytic processing.	Heparin	47-54	vascular endothelial growth factor B	Homo sapiens	15-21
10402474-4	1999	We report here that IP-10 inhibited EGF- and heparin-binding EGF-like growth factor-induced Hs68 human dermal fibroblast motility in a dose-dependent manner (to 52% and 44%, respectively, at 50 ng/ml IP-10), whereas IP-10 had no effect on either basal or EGFR-mediated mitogenesis (96 +/- 15% at 50 ng/ml).	Heparin	45-52	C-X-C motif chemokine ligand 10	Homo sapiens	20-25
10402474-4	1999	We report here that IP-10 inhibited EGF- and heparin-binding EGF-like growth factor-induced Hs68 human dermal fibroblast motility in a dose-dependent manner (to 52% and 44%, respectively, at 50 ng/ml IP-10), whereas IP-10 had no effect on either basal or EGFR-mediated mitogenesis (96 +/- 15% at 50 ng/ml).	Heparin	45-52	C-X-C motif chemokine ligand 10	Homo sapiens	200-205
10402474-4	1999	We report here that IP-10 inhibited EGF- and heparin-binding EGF-like growth factor-induced Hs68 human dermal fibroblast motility in a dose-dependent manner (to 52% and 44%, respectively, at 50 ng/ml IP-10), whereas IP-10 had no effect on either basal or EGFR-mediated mitogenesis (96 +/- 15% at 50 ng/ml).	Heparin	45-52	C-X-C motif chemokine ligand 10	Homo sapiens	200-205
10414365-13	1999	Binding of vitronectin and lactoferrin was efficiently inhibited by preincubating of staphylococcal cells with sulphated carbohydrate compounds as heparin, dextran sulphate and fucoidan, but not by other non-sulphated highly charged glycoconjugates such as hyaluronic acid.	Heparin	147-154	vitronectin	Homo sapiens	11-22
10435777-8	1999	The use of nonspecific intracellular PLA2 inhibitors (quinacrine, heparin, gangliosides, vitamin E) in animal model studies of neurological disorders in vivo has provided some useful information on tolerance, toxicity, and effectiveness of these compounds.	Heparin	66-73	phospholipase A2 group IIA	Homo sapiens	37-41
10350466-0	1999	Structural analysis of the heparin-binding site of the NC1 domain of collagen XIV by CD and NMR.	Heparin	27-34	collagen type XIV alpha 1 chain	Gallus gallus	69-81
10350466-2	1999	To further characterize such interactions in the NC1 domain of chicken collagen XIV, we identified amino acids essential for heparin binding by affinity chromatography analysis after proteolytic digestion of the synthetic peptide NC1(84-116).	Heparin	125-132	collagen type XIV alpha 1 chain	Gallus gallus	71-83
10408366-12	1999	Three proteins (FHR-1, FHR-2 and FHR-4) are constituents of lipoproteins, while FHR-3 interacts with heparin.	Heparin	101-108	complement factor H related 3	Homo sapiens	80-85
10212279-2	1999	Megalin-bound Tg was releasable by heparin.	Heparin	35-42	LDL receptor related protein 2	Rattus norvegicus	0-7
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	LDL receptor related protein 2	Rattus norvegicus	148-155
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	LDL receptor related protein associated protein 1	Rattus norvegicus	169-196
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	LDL receptor related protein associated protein 1	Rattus norvegicus	198-201
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	LDL receptor related protein 2	Rattus norvegicus	240-247
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	29-36	LDL receptor related protein 2	Rattus norvegicus	240-247
10212279-8	1999	The amount of Tg released by heparin from FRTL-5 and IRPT cells, measured by enzyme-linked immunosorbent assay (ELISA), was markedly reduced by two megalin competitors, receptor-associated protein (RAP) and 1H2 (monoclonal antibody against megalin), indicating that much of the Tg released by heparin had been bound to megalin ( approximately 60-80%).	Heparin	293-300	LDL receptor related protein 2	Rattus norvegicus	148-155
10320244-3	1999	We compared these methods with respect to their ability to reflect the actual heparin concentration in plasma determined by an anti-FXa method.	Heparin	78-85	coagulation factor X	Homo sapiens	132-135
10208268-3	1999	In order to develop new therapeutic strategies to reduce wound-healing intensity, we investigated the effect of heparin on the proliferation of cultured human corneal stromal fibroblasts (HCF) alone and in the presence of growth factors.	Heparin	112-119	host cell factor C1	Homo sapiens	188-191
10208268-7	1999	Modulation of HCF proliferation by heparin (50 microg/ml and 2000 microg/ml) was also investigated under serum-free conditions and in the presence of bFGF, EGF and PDGF-BB.	Heparin	35-42	host cell factor C1	Homo sapiens	14-17
10208268-12	1999	CONCLUSION: Our observations indicate that heparin can inhibit proliferation of HCF effectively.	Heparin	43-50	host cell factor C1	Homo sapiens	80-83
10037735-0	1999	Orientation of heparin-binding sites in native vitronectin.	Heparin	15-22	vitronectin	Homo sapiens	47-58
10037735-2	1999	A primary heparin-binding site in vitronectin has been localized to a cluster of cationic residues near the C terminus of the protein.	Heparin	10-17	vitronectin	Homo sapiens	34-45
10037735-4	1999	In order to investigate whether the binding site originally identified on vitronectin functions as an exclusive and independent heparin-binding domain, solution binding methods have been used in combination with NMR and recombinant approaches to evaluate ligand binding to the primary site.	Heparin	128-135	vitronectin	Homo sapiens	74-85
10037735-5	1999	Evaluation of the ionic strength dependence of heparin binding to vitronectin according to classical linkage theory indicates that a single ionic bond is prominent.	Heparin	47-54	vitronectin	Homo sapiens	66-77
10037735-10	1999	The label has now been localized to arginine residues within the cyanogen bromide fragment-(341-380) that contains the primary heparin-binding site on vitronectin.	Heparin	127-134	vitronectin	Homo sapiens	151-162
10037735-12	1999	A recombinant polypeptide corresponding to the C-terminal 129 amino acids of vitronectin exhibits heparin-binding affinity that is comparable to that of full-length vitronectin and is equally effective at neutralizing heparin anticoagulant activity.	Heparin	98-105	vitronectin	Homo sapiens	77-88
10037735-12	1999	A recombinant polypeptide corresponding to the C-terminal 129 amino acids of vitronectin exhibits heparin-binding affinity that is comparable to that of full-length vitronectin and is equally effective at neutralizing heparin anticoagulant activity.	Heparin	218-225	vitronectin	Homo sapiens	77-88
10037735-13	1999	Results from this broad experimental approach argue that the behavior of the primary site is sufficient to account for the heparin binding activity of vitronectin and support an exposed orientation for the site in the structure of the native protein.	Heparin	123-130	vitronectin	Homo sapiens	151-162
10037743-2	1999	Recent studies have shown that CD44 isoforms containing the alternatively spliced exon v3 carry heparan sulfate side chains and are able to bind heparin-binding growth factors.	Heparin	145-152	CD44 molecule (Indian blood group)	Homo sapiens	31-35
10064614-7	1999	Antibodies directed against vitronectin, a plasma protein and extracellular matrix component, exhibit intense and consistent reactivity with drusen; antibodies to the conformationally distinct, heparin binding form of human vitronectin are similarly immunoreactive.	Heparin	194-201	vitronectin	Homo sapiens	224-235
9882449-12	1999	Hence, although surface plasmon resonance shows that heparin binds to C1INH, heparin augmentation of C1INH activity appears to require a terniary complex in which cell bound C1 interacts with both heparin and C1INH.	Heparin	53-60	serpin family G member 1	Homo sapiens	70-75
9882449-12	1999	Hence, although surface plasmon resonance shows that heparin binds to C1INH, heparin augmentation of C1INH activity appears to require a terniary complex in which cell bound C1 interacts with both heparin and C1INH.	Heparin	77-84	serpin family G member 1	Homo sapiens	101-106
9882449-12	1999	Hence, although surface plasmon resonance shows that heparin binds to C1INH, heparin augmentation of C1INH activity appears to require a terniary complex in which cell bound C1 interacts with both heparin and C1INH.	Heparin	77-84	serpin family G member 1	Homo sapiens	101-106
9882449-12	1999	Hence, although surface plasmon resonance shows that heparin binds to C1INH, heparin augmentation of C1INH activity appears to require a terniary complex in which cell bound C1 interacts with both heparin and C1INH.	Heparin	77-84	serpin family G member 1	Homo sapiens	101-106
9882449-12	1999	Hence, although surface plasmon resonance shows that heparin binds to C1INH, heparin augmentation of C1INH activity appears to require a terniary complex in which cell bound C1 interacts with both heparin and C1INH.	Heparin	77-84	serpin family G member 1	Homo sapiens	101-106
9935214-5	1999	Most of the chemotactic activity was retained by a heparin affinity column, indicating that the motility factor(s) is a heparin-binding protein.	Heparin	51-58	azurocidin 1	Homo sapiens	120-143
9878651-5	1999	Group 2 (Hep) was anticoagulated with heparin to raise the activated partial thromboplastin time to 1.5-2.0 times control.	Heparin	38-45	DNL-type zinc finger	Homo sapiens	9-12
10562441-5	1999	On the contrary, at low concentration, i.e. 1-10 microg/ml, heparins stimulated the secretion of both 72-kDa gelatinase (1.4-1.6-fold) and particularly TIMP-2 (&gt;4-fold).	Heparin	60-68	TIMP metallopeptidase inhibitor 2	Homo sapiens	152-158
12623570-6	1999	A number of unresolved efficacy and safety issues remain, including the duration of treatment before and after intervention; whether a reduction in the heparin dose would further decrease the risk of hemorrhage without affecting the periprocedural thrombotic rate in patients undergoing PTCA with adjunctive GPIIb/IIIa inhibitors; and the cost-effectiveness of this therapy.	Heparin	152-159	integrin subunit alpha 2b	Homo sapiens	308-313
10094387-3	1999	Some of these residues, notably K49 in the "Gly rich loop", K74, K75, K76, K77, K79, R80, K83 in the "Lys rich segment" and R191, R195, K198 in the "p+1 loop", have been shown by mutational studies to be implicated to various extents and with distinct roles in substrate recognition, inhibition by heparin and by pseudosubstrate and instrasteric regulation.	Heparin	298-305	keratin 83	Homo sapiens	90-93
9920492-7	1999	These results indicate that wedelolactone, para-bromophenacyl bromide and heparin are antagonists of these two phospholipase A2 myotoxins, and that antagonism by the first two compounds may be due to a more specific interaction with these proteins than that by the latter.	Heparin	74-81	phospholipase A2, group IB, pancreas	Mus musculus	111-127
9837939-2	1998	Heparin cofactor II is a naturally occurring anticoagulant that acts by specifically inhibiting thrombin and is facilitated by the binding of glycosaminoglycans such as heparin and dermatan sulfate.	Heparin	169-176	heparin cofactor 2	Oryctolagus cuniculus	0-19
9837939-5	1998	Covalent heparin cofactor II-heparin and heparin cofactor II-dermatan sulfate complexes had catalytic antithrombin activities similar to those of the corresponding starting heparin and dermatan sulfate (86% and 110% of standard heparin and dermatan sulfate activity, respectively).	Heparin	29-36	heparin cofactor 2	Oryctolagus cuniculus	9-28
9759631-7	1998	Also, heparin was found to suppress increases in ICAM-1 mRNA at a concentration as low as 5 microg/ml.	Heparin	6-13	intercellular adhesion molecule 1	Homo sapiens	49-55
9759631-8	1998	These findings indicate that heparin deficiency induces endothelial activation characterized by increased ICAM-1, and that such induction is not dependent on cytokines or endotoxin.	Heparin	29-36	intercellular adhesion molecule 1	Homo sapiens	106-112
9759631-9	1998	The modulation of ICAM-1 expression by heparin appears to occur at the transcriptional level.	Heparin	39-46	intercellular adhesion molecule 1	Homo sapiens	18-24
9759631-10	1998	Thus, heparin may have a role in regulating endothelial function by affecting the expression of ICAM-1, thereby impacting upon the trans-endothelial trafficking of leukocytes.	Heparin	6-13	intercellular adhesion molecule 1	Homo sapiens	96-102
9650567-13	1998	In KM12SM cells, amphiregulin was induced by heparin in cells on fibronectin and collagen IV.	Heparin	45-52	amphiregulin	Homo sapiens	17-29
9634701-3	1998	The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate.	Heparin	103-110	kinase insert domain receptor	Homo sapiens	48-51
9634701-3	1998	The binding of VEGF to its two known receptors, KDR and Flt-1, is modulated by cell-surface-associated heparin-like glycosaminoglycans and exogenous heparin or heparan sulfate.	Heparin	149-156	kinase insert domain receptor	Homo sapiens	48-51
9603425-1	1998	We have investigated postgastrulation functions of FGFs in Xenopus development by the implantation of heparin beads soaked in FGF2 to various positions at various stages.	Heparin	102-109	fibroblast growth factor 2 L homeolog	Xenopus laevis	126-130
9535876-9	1998	F2 and sF2-(63-116) bind to exosite II on thrombin because both reduce the heparin-catalyzed rate of thrombin inhibition by antithrombin approximately 4-fold.	Heparin	75-82	serine and arginine rich splicing factor 1	Homo sapiens	7-10
9516434-9	1998	The binding of the HS to bFGF or FS-288 was markedly inhibited by heparin (HP) and various HS preparations, but not by chondroitin sulfate, supporting the binding specificity of HS.	Heparin	66-73	fibroblast growth factor 2 L homeolog	Xenopus laevis	25-29
9516434-9	1998	The binding of the HS to bFGF or FS-288 was markedly inhibited by heparin (HP) and various HS preparations, but not by chondroitin sulfate, supporting the binding specificity of HS.	Heparin	75-77	fibroblast growth factor 2 L homeolog	Xenopus laevis	25-29
9524273-2	1998	wt kininogen, factor XII and the heparin-binding, multimeric form of vitronectin.	Heparin	33-40	vitronectin	Mus musculus	69-80
9524273-8	1998	The amino acid sequence responsible for binding to the heparin-binding, multimeric form of vitronectin is located in exon 2.	Heparin	55-62	vitronectin	Mus musculus	91-102
9488672-2	1998	The middle domain of plasma histidine-proline-rich glycoprotein (HPRG) contains unusual tandem pentapeptide repeats (consensus G(H/P)(H/P)PH) and binds heparin and transition metals.	Heparin	152-159	histidine rich glycoprotein	Homo sapiens	65-69
9488672-3	1998	Unlike other proteins that interact with heparin via lysine or arginine residues, HPRG relies exclusively on histidine residues for this interaction.	Heparin	41-48	histidine rich glycoprotein	Homo sapiens	82-86
9488672-5	1998	HPRG binding to immobilized heparin was strikingly pH-sensitive, producing a titration curve with a midpoint at pH 6.8.	Heparin	28-35	histidine rich glycoprotein	Homo sapiens	0-4
9488672-6	1998	There was little binding of HPRG to heparin at physiological pH in the absence of metals, but the interaction was promoted by nanomolar concentrations of free zinc and copper, and its pH dependence was shifted toward alkaline pH by zinc.	Heparin	36-43	histidine rich glycoprotein	Homo sapiens	28-32
9488672-7	1998	The affinity of HPRG for various GAGs measured in a competition assay decreased in the following order: heparin &gt; dermatan sulfate &gt; heparan sulfate &gt; chondroitin sulfate A.	Heparin	104-111	histidine rich glycoprotein	Homo sapiens	16-20
9521646-1	1998	Regulation of the inhibitory activity of antithrombin, the principal inhibitor of the blood-clotting proteinases factor Xa and thrombin, is accomplished by binding to heparin.	Heparin	167-174	coagulation factor X	Homo sapiens	113-122
9521646-3	1998	By derivatization of this cysteine with a bulky group, fluorescein, the antithrombin became permanently and fully activated toward reaction with factor Xa in a manner analogous to heparin activation, albeit as a substrate.	Heparin	180-187	coagulation factor X	Homo sapiens	145-154
9521646-4	1998	These findings establish a structural basis for the mechanism of heparin activation of antithrombin against factor Xa in agreement with that proposed from an X-ray structure of antithrombin.	Heparin	65-72	coagulation factor X	Homo sapiens	108-117
9538935-9	1998	Delivery of FGF-2 into the infarct border area, also increased the number of arterioles when FGF-2 was given with heparin (736 +/- 154%, P &lt; 0.001) or heparin beads (700 +/- 109%, P &lt; 0.001), as compared to control.	Heparin	114-121	fibroblast growth factor 2	Sus scrofa	12-17
9538935-9	1998	Delivery of FGF-2 into the infarct border area, also increased the number of arterioles when FGF-2 was given with heparin (736 +/- 154%, P &lt; 0.001) or heparin beads (700 +/- 109%, P &lt; 0.001), as compared to control.	Heparin	114-121	fibroblast growth factor 2	Sus scrofa	93-98
9538935-9	1998	Delivery of FGF-2 into the infarct border area, also increased the number of arterioles when FGF-2 was given with heparin (736 +/- 154%, P &lt; 0.001) or heparin beads (700 +/- 109%, P &lt; 0.001), as compared to control.	Heparin	154-161	fibroblast growth factor 2	Sus scrofa	12-17
9538935-10	1998	FGF-2 administered with heparin was the most effective method of enhancing angiogenesis as compared to FGF-2 alone, FGF-2 plus heparan sulfate, or FGF-2 coated heparin agarose beads.	Heparin	24-31	fibroblast growth factor 2	Sus scrofa	0-5
9519732-6	1998	In contrast, elevation of circulating free fatty acid levels in fed animals by Intralipid plus heparin infusion caused significant increases in the UCP3/actin mRNA ratio compared with saline-infused fed controls in both extensor digitorum longus (2.01 +/- 0.34 vs. 0.68 +/- 0.11, P = 0.002) and soleus muscles (0.31 +/- 0.07 vs. 0.09 +/- 0.02, P = 0.014).	Heparin	95-102	uncoupling protein 3	Homo sapiens	148-152
9666310-7	1998	H3 was further purified, and the single peak of heparin-binding activity, designated H3b, represented a 681-fold purification of endothelial mitogenic activity from endometrial ECM.	Heparin	48-55	histocompatibility 3b, Th stimulating	Mus musculus	85-88
9666310-8	1998	H3 and H3b were heat labile and trypsin sensitive, and their biological activity was heparin enhanced.	Heparin	85-92	histocompatibility 3b, Th stimulating	Mus musculus	7-10
9681155-7	1998	The plasma motilin concentration decreased significantly when heparin was given, and that of substance P increased, both these peptides being vasodilators.	Heparin	62-69	motilin	Homo sapiens	11-18
9681155-10	1998	To sum up, administration of heparin but not of saline affected the plasma concentrations of motilin and substance P.	Heparin	29-36	motilin	Homo sapiens	93-100
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	interleukin 11	Mus musculus	115-120
9505144-3	1998	The suppression of heparin-releasable LPL activity produced by combinations of IL-1 and IL-11, IL-1 and TNF-alpha, IL-11 and TNF-alpha, and, IL-11 and INF-gamma was substantially lower than that expected from the additive action of the corresponding two cytokines.	Heparin	19-26	interleukin 11	Mus musculus	115-120
9438869-9	1997	CONCLUSIONS: The F2 kringle domain in mzTBN-F1 is bound to the electropositive heparin-binding site on thrombin in an orientation that is systematically shifted and has significantly more interdomain contacts compared to a noncovalent complex of free F2 and free thrombin.	Heparin	79-86	coagulation factor II, thrombin	Bos taurus	103-111
9341129-0	1997	Deleted in colorectal carcinoma (DCC) binds heparin via its fifth fibronectin type III domain.	Heparin	44-51	DCC netrin 1 receptor	Homo sapiens	0-31
9341129-0	1997	Deleted in colorectal carcinoma (DCC) binds heparin via its fifth fibronectin type III domain.	Heparin	44-51	DCC netrin 1 receptor	Homo sapiens	33-36
9341129-9	1997	The interaction between DCC-Ig and heparan sulfate/heparin, both on the surface of cells and immobilized on plastic, was blocked by the same anti-DCC antibody that blocks netrin-1-dependent commissural axon outgrowth.	Heparin	51-58	DCC netrin 1 receptor	Homo sapiens	24-27
9341129-9	1997	The interaction between DCC-Ig and heparan sulfate/heparin, both on the surface of cells and immobilized on plastic, was blocked by the same anti-DCC antibody that blocks netrin-1-dependent commissural axon outgrowth.	Heparin	51-58	DCC netrin 1 receptor	Homo sapiens	146-149
9341129-9	1997	The interaction between DCC-Ig and heparan sulfate/heparin, both on the surface of cells and immobilized on plastic, was blocked by the same anti-DCC antibody that blocks netrin-1-dependent commissural axon outgrowth.	Heparin	51-58	netrin 1	Homo sapiens	171-179
9341129-10	1997	Taken together, these findings suggest that the DCC-Ig/heparin interaction may contribute to the biological activity of DCC.	Heparin	55-62	DCC netrin 1 receptor	Homo sapiens	48-51
9341129-10	1997	Taken together, these findings suggest that the DCC-Ig/heparin interaction may contribute to the biological activity of DCC.	Heparin	55-62	DCC netrin 1 receptor	Homo sapiens	120-123
9342064-8	1997	The HSPG-bound Tat can be retrieved into a soluble form by heparin, heparinase or trypsin.	Heparin	59-66	syndecan 2	Homo sapiens	4-8
9342064-9	1997	Binding to heparin is competed out by heparin-binding factors such as basic fibroblast growth factor (bFGF), and it is mediated by the Tat basic region which forms a specific complex with heparin which blocks HIV-1 rescue by exogenous Tat and allows purification of a highly biologically active protein.	Heparin	11-18	Tat	Human immunodeficiency virus 1	135-138
9342064-9	1997	Binding to heparin is competed out by heparin-binding factors such as basic fibroblast growth factor (bFGF), and it is mediated by the Tat basic region which forms a specific complex with heparin which blocks HIV-1 rescue by exogenous Tat and allows purification of a highly biologically active protein.	Heparin	11-18	Tat	Human immunodeficiency virus 1	235-238
9323025-3	1997	Selective uptake of HDL3-CEs into a releasable pool (presumably located in the cellular plasma membrane) was temperature insensitive while prominent internalization into a non-releasable and subsequent hydrolysis in a non-chloroquine sensitive compartment occurred at 37 degrees C. Release of membrane bound endogenous LPL by heparin resulted in decreased HDL3 holoparticle, total CE and selective CE uptake.	Heparin	326-333	high density lipoprotein (HDL) level 3	Mus musculus	20-24
9332733-8	1997	Heparin, which inhibits the neurite growth-promoting effects of PGs in vitro, and heparitinase, which catalyzes the cleavage of heparan sulphate, also inhibited the glutamate-dependent induction of T alpha 1, MAP-2 and GAP-43 mRNA expression and neurite growth when added to culture medium following glutamate exposure.	Heparin	0-7	microtubule associated protein 2	Homo sapiens	209-214
9284164-8	1997	Binding of VN was inhibited by heparin in a concentration-dependent manner, indicating that the heparin binding sites present in VN or Opa50 may play an essential role in this interaction.	Heparin	31-38	vitronectin	Homo sapiens	11-13
9284164-8	1997	Binding of VN was inhibited by heparin in a concentration-dependent manner, indicating that the heparin binding sites present in VN or Opa50 may play an essential role in this interaction.	Heparin	31-38	vitronectin	Homo sapiens	129-131
9284164-8	1997	Binding of VN was inhibited by heparin in a concentration-dependent manner, indicating that the heparin binding sites present in VN or Opa50 may play an essential role in this interaction.	Heparin	96-103	vitronectin	Homo sapiens	11-13
9284164-8	1997	Binding of VN was inhibited by heparin in a concentration-dependent manner, indicating that the heparin binding sites present in VN or Opa50 may play an essential role in this interaction.	Heparin	96-103	vitronectin	Homo sapiens	129-131
9309585-2	1997	Peptides from the type I repeats of TSP1 mimic the adhesive and growth inhibitory activities of the intact protein and specifically interact with heparin and transforming growth factor-beta (TGF beta).	Heparin	146-153	thrombospondin 1	Mus musculus	36-40
9309585-7	1997	Their antiproliferative activities were independent of latent TGF beta activation, because substitution of an Ala residue for the essential Phe residue in the TSP1 type-1 repeat peptide increased their potency for inhibiting TSP1 binding to heparin and for inhibiting endothelial cell proliferation.	Heparin	241-248	thrombospondin 1	Mus musculus	159-163
9309585-7	1997	Their antiproliferative activities were independent of latent TGF beta activation, because substitution of an Ala residue for the essential Phe residue in the TSP1 type-1 repeat peptide increased their potency for inhibiting TSP1 binding to heparin and for inhibiting endothelial cell proliferation.	Heparin	241-248	thrombospondin 1	Mus musculus	225-229
9309585-9	1997	Thus, these TSP-derived peptide analogs antagonize endothelial growth through their heparin-binding activity rather than through activation of latent TGF beta or increasing cell adhesion.	Heparin	84-91	CTR9 homolog, Paf1/RNA polymerase II complex component	Mus musculus	12-15
9387191-0	1997	Plasma collagen-binding vitronectin activated by heparin and dextran sulfate in chronic liver disease.	Heparin	49-56	vitronectin	Homo sapiens	24-35
9387191-5	1997	After treatment with heparin, the percent collagen-binding vitronectin to total vitronectin was 20.6 +/- 2.0% in the controls, 24.7 +/- 4.1% in chronic persistent hepatitis, 28.6 +/- 2.5% in chronic active hepatitis, 42.6 +/- 4.5% in liver cirrhosis, and 31.8 +/- 2.3% in hepatocellular carcinoma.	Heparin	21-28	vitronectin	Homo sapiens	59-70
9387191-5	1997	After treatment with heparin, the percent collagen-binding vitronectin to total vitronectin was 20.6 +/- 2.0% in the controls, 24.7 +/- 4.1% in chronic persistent hepatitis, 28.6 +/- 2.5% in chronic active hepatitis, 42.6 +/- 4.5% in liver cirrhosis, and 31.8 +/- 2.3% in hepatocellular carcinoma.	Heparin	21-28	vitronectin	Homo sapiens	80-91
9252396-8	1997	Moreover, in contrast to other PKC isoenzymes PKCmu is activated by heparin and dextran sulfate.	Heparin	68-75	protein kinase D1	Homo sapiens	46-51
9224287-2	1997	METHODS: Vitronectin was removed from fetal bovine serum by heparin-agarose affinity chromatography.	Heparin	60-67	vitronectin	Homo sapiens	9-20
29512538-1	1997	Myelin basic protein (MBP) from one month old rat brain was purified by CM-52 cellulose chromatography and heparin sepharose chromatography.	Heparin	107-114	myelin basic protein	Rattus norvegicus	0-20
29512538-1	1997	Myelin basic protein (MBP) from one month old rat brain was purified by CM-52 cellulose chromatography and heparin sepharose chromatography.	Heparin	107-114	myelin basic protein	Rattus norvegicus	22-25
9165012-0	1997	Heparin-binding, highly basic regions within the thyroglobulin type-1 repeat of insulin-like growth factor (IGF)-binding proteins (IGFBPs) -3, -5, and -6 inhibit IGFBP-4 degradation.	Heparin	0-7	insulin-like growth factor binding protein 4	Mus musculus	162-169
9165012-7	1997	Consistent with these regions being involved in proteinase inhibition, heparin completely reverses their inhibitory effects on 125I-IGFBP-4 proteolysis.	Heparin	71-78	insulin-like growth factor binding protein 4	Mus musculus	132-139
9165012-8	1997	Together, these data demonstrate that IGFBP-3, -5, and -6 can function as IGF-reversible inhibitors of IGFBP-4 proteolysis, likely through homologous, highly basic, heparin-binding domains contained within the conserved thyroglobulin type-1 motif present in the C-termini of these IGFBPs.	Heparin	165-172	insulin-like growth factor binding protein 4	Mus musculus	103-110
9153200-8	1997	The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded.	Heparin	62-69	histidine rich glycoprotein	Homo sapiens	4-7
9164872-4	1997	In vitro, the heparin-binding multimeric isoform of vitronectin bound to immobilized osteonectin in a saturable manner with half-maximal binding at 30-40 nM.	Heparin	14-21	vitronectin	Homo sapiens	52-63
9164872-7	1997	In a concentration-dependent fashion, PAI-1, CaCl2, heparin and heparan sulphate, but not other glycosaminoglycans, interfered with the binding of vitronectin to osteonectin.	Heparin	52-59	vitronectin	Homo sapiens	147-158
9139688-8	1997	Addition of purified soluble glypican effectively replaced heparin in supporting basic FGF-induced cellular proliferation of heparan sulfate-negative cells expressing recombinant FGF receptor-1.	Heparin	59-66	fibroblast growth factor 7	Rattus norvegicus	87-90
9166899-4	1997	Horse seminal plasma proteins HSP-1 and HSP-2, and boar protein pB1, belong to the same family as the bull heparin- and phosphorylcholine-binding proteins BSP-A1/2, BSP-A3, and BSP-30K.	Heparin	107-114	polybromo 1	Bos taurus	64-67
9166899-4	1997	Horse seminal plasma proteins HSP-1 and HSP-2, and boar protein pB1, belong to the same family as the bull heparin- and phosphorylcholine-binding proteins BSP-A1/2, BSP-A3, and BSP-30K.	Heparin	107-114	binder of sperm 2	Equus caballus	155-163
9079718-4	1997	Unmodified ATAC is a cationic protein with a pI of 11.35 and is capable of binding to heparin.	Heparin	86-93	X-C motif chemokine ligand 1	Homo sapiens	11-15
9054371-0	1997	Native and multimeric vitronectin exhibit similar affinity for heparin.	Heparin	63-70	vitronectin	Homo sapiens	22-33
9054371-2	1997	For many years, the concept that the heparin-binding sequence is sequestered within vitronectin and exposed upon denaturation of the protein has guided experimental design and interpretation of related structure-function studies on the protein.	Heparin	37-44	vitronectin	Homo sapiens	84-95
9054371-3	1997	To evaluate binding of heparin to both native and denatured/renatured vitronectin, methods for monitoring binding in solution have been developed.	Heparin	23-30	vitronectin	Homo sapiens	70-81
9054371-4	1997	A fluorescence method based on changes in an extrinsic probe attached to heparin has been used to evaluate heparin binding to native and denatured/renatured vitronectin.	Heparin	73-80	vitronectin	Homo sapiens	157-168
9054371-4	1997	A fluorescence method based on changes in an extrinsic probe attached to heparin has been used to evaluate heparin binding to native and denatured/renatured vitronectin.	Heparin	107-114	vitronectin	Homo sapiens	157-168
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	149-156	vitronectin	Homo sapiens	130-141
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	223-230	vitronectin	Homo sapiens	130-141
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	223-230	vitronectin	Homo sapiens	248-259
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	223-230	vitronectin	Homo sapiens	248-259
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	223-230	vitronectin	Homo sapiens	130-141
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	223-230	vitronectin	Homo sapiens	248-259
9054371-10	1997	On the basis of the binding data from solution studies and interaction of the native monomer and the denatured multimeric form of vitronectin with a heparin column, along with evaluation of the ionic strength dependence of heparin binding to these vitronectin forms in solution, an alternative model is favored to account for the altered heparin binding properties of vitronectin associated with denaturation of the protein.	Heparin	223-230	vitronectin	Homo sapiens	248-259
9054371-11	1997	This model proposes that multivalent interactions between heparin and multimeric vitronectin are responsible for differences in heparin affinity chromatography and ionic strength dependence compared with the native protein.	Heparin	58-65	vitronectin	Homo sapiens	81-92
9054371-11	1997	This model proposes that multivalent interactions between heparin and multimeric vitronectin are responsible for differences in heparin affinity chromatography and ionic strength dependence compared with the native protein.	Heparin	128-135	vitronectin	Homo sapiens	81-92
9118690-12	1997	Also, CPB induced a gradual increase of the acute-phase reactant LBP, which was identical in the noncoated and heparin-coated groups.	Heparin	111-118	lipopolysaccharide binding protein	Homo sapiens	65-68
9127746-1	1997	Our aim was to determine whether the increase in serum pancreatic lipase values, reported in patients with chronic renal failure maintained on haemodialysis, is the result of haemoconcentration by fluid removal during dialysis, or whether it is due to lipase stimulation by endothelial lipoprotein lipase, induced by the heparin used as an anticoagulant.	Heparin	321-328	pancreatic lipase	Homo sapiens	55-72
9127746-7	1997	These findings suggest that heparin-induced lipoprotein lipase stimulation is the principal cause of the post-dialysis increase in pancreatic lipase, and that fluid removal during dialysis makes only a minor contribution to this increase.	Heparin	28-35	pancreatic lipase	Homo sapiens	131-148
9075122-7	1997	Interestingly, a shift in the balance of alpha 1(IV)COLL, MMP-2 and TIMP-2 was observed in high glucose, which was partially reversed by heparin supplementation.	Heparin	137-144	TIMP metallopeptidase inhibitor 2	Homo sapiens	68-74
9030577-6	1997	These results were complemented by labeling vitronectin with an arginine-specific coumarin probe which compromises heparin binding but does not interfere with PAI-1 binding to the protein.	Heparin	115-122	vitronectin	Homo sapiens	44-55
9030584-9	1997	Although CFR binds heparin with high affinity, an analysis of the heparin-CFR interaction failed to identify a linear sequence containing a heparin binding site.	Heparin	19-26	golgi glycoprotein 1	Gallus gallus	9-12
9225113-8	1997	Uterine GCP-2 exhibited high affinity to heparin agarose, a characteristic shared by all alpha chemokines.	Heparin	41-48	C-X-C motif chemokine 6	Bos taurus	8-13
21153117-8	1997	Uterine GCP-2 exhibited high affinity to heparin agarose, a characteristic shared by all alpha chemokines.	Heparin	41-48	C-X-C motif chemokine 6	Bos taurus	8-13
9058215-10	1997	Protamine titration (Hepcon) correlated with the factor Xa inhibitory assay for heparin (r2 = 0.76).	Heparin	80-87	coagulation factor X	Homo sapiens	49-58
9016860-7	1997	Interestingly, this inhibitory effect of TSP on megakaryocyte colony growth could be counteracted by Fraxiparin, a low-molecular-weight heparin.	Heparin	136-143	CTR9 homolog, Paf1/RNA polymerase II complex component	Mus musculus	41-44
9016860-8	1997	These results demonstrate that TSP is a negative modulator of megakaryocytopoiesis and suggest that its inhibitory effect is at least partially mediated by N-terminal heparin-binding domain.	Heparin	167-174	CTR9 homolog, Paf1/RNA polymerase II complex component	Mus musculus	31-34
9272378-4	1997	MCP/JE expression was also demonstrated in ECGF/heparin-treated murine cEC.	Heparin	48-55	complement component (3b/4b) receptor 1-like	Mus musculus	0-3
9386990-5	1997	In this manuscript we provide results which are consistent with the hypothesis that an interaction between heparin and a site on the KDR receptor subtype is essential for VEGF165 binding.	Heparin	107-114	vascular endothelial growth factor receptor 2	Cricetulus griseus	133-136
9386990-7	1997	Secondly, we show that a ten amino acid synthetic peptide, corresponding to a sequence from the extracellular domain of the KDR, both inhibits VEGF165 binding to the receptor and also binds heparin with high avidity.	Heparin	190-197	vascular endothelial growth factor receptor 2	Cricetulus griseus	124-127
9386990-8	1997	Third, affinity purification of heparin molecules on a KDR-derived peptide affinity column, together with capillary electrophoresis and polyacrylamide electrophoresis analysis, was used to show that the KDR-derived peptide interacts with a specific subset of polysaccharide chains contained in the unfractionated heparin.	Heparin	32-39	vascular endothelial growth factor receptor 2	Cricetulus griseus	55-58
9386990-8	1997	Third, affinity purification of heparin molecules on a KDR-derived peptide affinity column, together with capillary electrophoresis and polyacrylamide electrophoresis analysis, was used to show that the KDR-derived peptide interacts with a specific subset of polysaccharide chains contained in the unfractionated heparin.	Heparin	32-39	vascular endothelial growth factor receptor 2	Cricetulus griseus	203-206
9386990-8	1997	Third, affinity purification of heparin molecules on a KDR-derived peptide affinity column, together with capillary electrophoresis and polyacrylamide electrophoresis analysis, was used to show that the KDR-derived peptide interacts with a specific subset of polysaccharide chains contained in the unfractionated heparin.	Heparin	313-320	vascular endothelial growth factor receptor 2	Cricetulus griseus	55-58
9386990-8	1997	Third, affinity purification of heparin molecules on a KDR-derived peptide affinity column, together with capillary electrophoresis and polyacrylamide electrophoresis analysis, was used to show that the KDR-derived peptide interacts with a specific subset of polysaccharide chains contained in the unfractionated heparin.	Heparin	313-320	vascular endothelial growth factor receptor 2	Cricetulus griseus	203-206
9144032-6	1997	Low molecular weight heparin, administered to 7 patients on dietary treatment, caused a marked drop in the F1 + 2 plasma level, providing evidence that the elevation in F1 + 2 indicates an accelerated in vivo thrombin generation rather than impaired renal catabolism.	Heparin	21-28	coagulation factor XII	Homo sapiens	107-113
9144032-6	1997	Low molecular weight heparin, administered to 7 patients on dietary treatment, caused a marked drop in the F1 + 2 plasma level, providing evidence that the elevation in F1 + 2 indicates an accelerated in vivo thrombin generation rather than impaired renal catabolism.	Heparin	21-28	coagulation factor XII	Homo sapiens	169-175
8986950-7	1997	Spin columns could be used with serum or plasma containing acid-citrate-dextrose or heparin anticoagulant, but heparinized samples required treatment with heparinase prior to amplification.	Heparin	84-91	spindlin 1	Homo sapiens	0-4
8980140-9	1996	The mosaic structure of BSP-30K suggests that this glycoprotein might be a factor contributing to the different sperm-capacitating effects exerted by heparin in different mammalian species.	Heparin	150-157	seminal plasma protein BSP-30 kDa	Bos taurus	24-31
8980646-7	1996	Apparent second-order rate constant (ki) for the inhibition of factor Xa by PAI-1 at 5 mM Ca2+ was 1.6 x 10(4) M-1 s-1, and was enhanced 3-fold by 2 u/ml of heparin (4.6 x 10(4) M-1 s-1) and 10-fold by 100 nM vitronectin (1.6 x 10(5) M-1 s-1), respectively.	Heparin	157-164	coagulation factor X	Homo sapiens	63-72
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	15-22	chromosome 20 open reading frame 181	Homo sapiens	80-83
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	15-22	kallikrein related peptidase 4	Homo sapiens	178-188
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	165-172	kallikrein related peptidase 4	Homo sapiens	178-188
8972021-4	1996	Differences in heparin stimulation were more pronounced for thrombin, APC, uPA, tPA and XIa, whereas inactivation of Xa by PCI was less dependent on the presence of heparin, and kallikrein showed higher potentiation with LMWH than with UF heparin.	Heparin	165-172	kallikrein related peptidase 4	Homo sapiens	178-188
8824227-4	1996	Heparin acted through a selective inhibition of the PKC-alpha since preincubation of the cells with a 20-mer phosphorothioate PKC-alpha antisense oligodeoxynucleotide (ODN) eliminated the heparin effect.	Heparin	188-195	protein kinase C, alpha	Rattus norvegicus	52-61
8824227-4	1996	Heparin acted through a selective inhibition of the PKC-alpha since preincubation of the cells with a 20-mer phosphorothioate PKC-alpha antisense oligodeoxynucleotide (ODN) eliminated the heparin effect.	Heparin	188-195	protein kinase C, alpha	Rattus norvegicus	126-135
8824227-6	1996	Heparin, administered at the time of injury or shortly thereafter, inhibited the activity of the particulate PKC and suppressed the in situ phosphorylation of an 80-kDa myristoylated alanine-rich protein kinase C substrate (MARCKS), a substrate of PKC.	Heparin	0-7	protein kinase C, alpha	Rattus norvegicus	109-112
8824227-6	1996	Heparin, administered at the time of injury or shortly thereafter, inhibited the activity of the particulate PKC and suppressed the in situ phosphorylation of an 80-kDa myristoylated alanine-rich protein kinase C substrate (MARCKS), a substrate of PKC.	Heparin	0-7	myristoylated alanine rich protein kinase C substrate	Rattus norvegicus	224-230
8824227-6	1996	Heparin, administered at the time of injury or shortly thereafter, inhibited the activity of the particulate PKC and suppressed the in situ phosphorylation of an 80-kDa myristoylated alanine-rich protein kinase C substrate (MARCKS), a substrate of PKC.	Heparin	0-7	protein kinase C, alpha	Rattus norvegicus	248-251
8824227-9	1996	These results therefore suggest that heparin might block SMC proliferation by interfering with the PKC pathway through a selective direct inhibition of the PKC-alpha isoenzyme.	Heparin	37-44	protein kinase C, alpha	Rattus norvegicus	99-102
8824227-9	1996	These results therefore suggest that heparin might block SMC proliferation by interfering with the PKC pathway through a selective direct inhibition of the PKC-alpha isoenzyme.	Heparin	37-44	protein kinase C, alpha	Rattus norvegicus	156-165
8824228-8	1996	PGHS-2-dependent delayed-phase PGD2 generation elicited by IgE-dependent activation of BALB/cJ BMMC primed with KL + IL-10 was also accompanied by the induction of type IIA PLA2 transcripts and was suppressed by heparin, with concomitant release of PLA2 into the supernatant.	Heparin	212-219	prostaglandin D2 synthase (brain)	Mus musculus	31-35
8824228-8	1996	PGHS-2-dependent delayed-phase PGD2 generation elicited by IgE-dependent activation of BALB/cJ BMMC primed with KL + IL-10 was also accompanied by the induction of type IIA PLA2 transcripts and was suppressed by heparin, with concomitant release of PLA2 into the supernatant.	Heparin	212-219	phospholipase A2, group IIA (platelets, synovial fluid)	Mus musculus	173-177
8878536-0	1996	Heparin functions as a hepatotrophic factor by inducing production of hepatocyte growth factor.	Heparin	0-7	hepatocyte growth factor	Rattus norvegicus	70-94
8878536-3	1996	Administration of heparin to rats increased blood HGF levels to a 2.5-5-fold higher level than that in control rats given saline alone, and consequently induced a remarkable enhancement of liver regeneration in vivo after a 30% partial hepatectomy.	Heparin	18-25	hepatocyte growth factor	Rattus norvegicus	50-53
8878536-5	1996	These results indicate that heparin has hepatotrophic function, an action possibly mediated through the stimulation of production of HGF.	Heparin	28-35	hepatocyte growth factor	Rattus norvegicus	133-136
8980877-1	1996	The effect of anticoagulant (heparin vs EDTA) on chemokine induced CD11b upregulation on neutrophils, eosinophils, and monocytes in human whole blood was determined.	Heparin	29-36	integrin subunit alpha M	Homo sapiens	67-72
8980877-6	1996	RANTES-induced CD11b expression on monocytes and eosinophils in these samples were the same in either heparin or EDTA.	Heparin	102-109	C-C motif chemokine ligand 5	Homo sapiens	0-6
8980877-6	1996	RANTES-induced CD11b expression on monocytes and eosinophils in these samples were the same in either heparin or EDTA.	Heparin	102-109	integrin subunit alpha M	Homo sapiens	15-20
8810913-1	1996	We have shown previously that the platelet-derived growth factor (PDGF) and a synthetic oligopeptide, corresponding to the basic carboxyl-terminal amino acid extension of the long PDGF-A isoform, bind to heparin.	Heparin	204-211	platelet derived growth factor subunit A	Homo sapiens	180-186
8701996-8	1996	Although the membrane-anchored form of heparin-binding epidermal-growth-factor-like growth factor (proHB-EGF), which is identical to the diphtheria toxin receptor, forms a complex with CD9 in some human and monkey cell lines, proHB-EGF was not detected in myelin immunocytochemically.	Heparin	39-46	CD9 molecule	Homo sapiens	185-188
8766721-0	1996	Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin.	Heparin	97-104	tenascin C	Homo sapiens	72-80
8764216-4	1996	AT III given alone, but not heparin plus AT III or Trp49-modified AT III, which lacks affinity for heparin, significantly increased the plasma concentration of 6-keto-prostaglandin F1alpha, suggesting that the interaction of AT III with heparin-like substances at the endothelial cell surface promotes the release of prostacyclin from endothelial cells in vivo.	Heparin	99-106	serpin family C member 1	Rattus norvegicus	0-6
8764216-4	1996	AT III given alone, but not heparin plus AT III or Trp49-modified AT III, which lacks affinity for heparin, significantly increased the plasma concentration of 6-keto-prostaglandin F1alpha, suggesting that the interaction of AT III with heparin-like substances at the endothelial cell surface promotes the release of prostacyclin from endothelial cells in vivo.	Heparin	99-106	serpin family C member 1	Rattus norvegicus	0-6
8643556-2	1996	While EC-SOD from most mammals is tetrameric and has a high affinity for heparin and heparan sulfate, rat EC-SOD has a low affinity for heparin, does not bind to heparan sulfate in vivo, and is apparently dimeric.	Heparin	73-80	superoxide dismutase 3	Rattus norvegicus	6-12
8643556-2	1996	While EC-SOD from most mammals is tetrameric and has a high affinity for heparin and heparan sulfate, rat EC-SOD has a low affinity for heparin, does not bind to heparan sulfate in vivo, and is apparently dimeric.	Heparin	136-143	superoxide dismutase 3	Rattus norvegicus	106-112
8643556-7	1996	Rat EC-SOD carrying an Asp --&gt; Val mutation is tetrameric and has a high heparin affinity, while mouse EC-SOD with a Val --&gt; Asp mutation is dimeric and has lost its high heparin affinity.	Heparin	76-83	superoxide dismutase 3	Rattus norvegicus	4-10
8697103-4	1996	Heparin-Sepharose chromatography, nondenaturing electrophoresis and sucrose gradient centrifugation were used to study heparin interaction with the G2 form BChE.	Heparin	119-126	butyrylcholinesterase	Rattus norvegicus	156-160
8697103-11	1996	In summary, these studies demonstrate that the ionic properties of the G2 form BChE are involved in the binding with heparin.	Heparin	117-124	butyrylcholinesterase	Rattus norvegicus	79-83
8698881-2	1996	We have shown that the heparin-binding growth factor FGF-1 is expressed by olfactory nerve ensheathing cells which surround fascicles of primary olfactory axons en route to the olfactory bulb.	Heparin	23-30	fibroblast growth factor 1	Rattus norvegicus	53-58
8641011-8	1996	The inhibitory effect of heparin on Ang II-induced cardiomyocyte hypertrophy also was confirmed by Northern blot analysis: heparin dose-dependently inhibited skeletal alpha-actin and atrial natriuretic peptide gene expression, genetic markers for cardiomyocyte hypertrophy.	Heparin	25-32	natriuretic peptide A	Rattus norvegicus	183-209
8641011-8	1996	The inhibitory effect of heparin on Ang II-induced cardiomyocyte hypertrophy also was confirmed by Northern blot analysis: heparin dose-dependently inhibited skeletal alpha-actin and atrial natriuretic peptide gene expression, genetic markers for cardiomyocyte hypertrophy.	Heparin	123-130	natriuretic peptide A	Rattus norvegicus	183-209
8785492-9	1996	These findings suggest that the heparin -binding C-tail of the mucin may be removed at an early stage of biosynthesis.	Heparin	32-39	solute carrier family 13 member 2	Rattus norvegicus	63-68
8821828-0	1996	Inhibition of mitogenesis and c-fos induction in mesangial cells by heparin and heparan sulfates.	Heparin	68-75	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	30-35
8821828-3	1996	Added at the time of serum stimulation, heparin (1 microgram/ml or less) causes a decrease in the subsequent expression of c-fos mRNA in RMC, and a similar effect is observed with heparan sulfate chains isolated from RMC-cultures themselves.	Heparin	40-47	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	123-128
8821828-6	1996	The effect of heparin on c-fos induction may be independent of interaction with cytokines or cytokine receptors; its magnitude is not diminished when heparin-binding substances are removed from serum by heparin-Sepharose.	Heparin	14-21	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	25-30
8821828-6	1996	The effect of heparin on c-fos induction may be independent of interaction with cytokines or cytokine receptors; its magnitude is not diminished when heparin-binding substances are removed from serum by heparin-Sepharose.	Heparin	150-157	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	25-30
8821828-6	1996	The effect of heparin on c-fos induction may be independent of interaction with cytokines or cytokine receptors; its magnitude is not diminished when heparin-binding substances are removed from serum by heparin-Sepharose.	Heparin	150-157	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	25-30
8821828-11	1996	We conclude that low concentrations of heparin and heparan sulfate suppress the mitogenic response of mesangial cells to serum and inhibit c-fos mRNA induction through an effect of cell surface-bound glycosaminoglycan on a signalling pathway downstream of PKC.	Heparin	39-46	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	139-144
8807714-4	1996	Due to a conformational switch in the vitronectin molecule, ternary complexes are endowed with heparin-binding properties and become specifically bound to cell surface sites on endothelial and other cells.	Heparin	95-102	vitronectin	Homo sapiens	38-49
8643109-8	1995	Both heparin and sulfated dextrans also inhibit agglutination, suggesting that charged residues on rCD4 played an important role in agglutination mediated by rCD4 or CD4 peptide.	Heparin	5-12	Cd4 molecule	Rattus norvegicus	99-103
8643109-8	1995	Both heparin and sulfated dextrans also inhibit agglutination, suggesting that charged residues on rCD4 played an important role in agglutination mediated by rCD4 or CD4 peptide.	Heparin	5-12	Cd4 molecule	Rattus norvegicus	158-162
8595612-8	1995	RESULTS: The medians of up-regulation of CD11b were 540.2 (range 235.2-653.3) for heparin vs. 186.5 (55.7-207.1) for EDTA and 192.5 (69.2-263.8) for citrate mixture, P &lt; 0.01.	Heparin	82-89	integrin subunit alpha M	Homo sapiens	41-46
8595612-10	1995	Up-regulation of CD11b, down-regulation of L-s and release of IL8 were inversely related to heparin concentration (r = 0.87, P &lt; 0.05).	Heparin	92-99	integrin subunit alpha M	Homo sapiens	17-22
8595612-12	1995	Heparin-protamine complex was less stimulant to expression of CD11b and L-selectin than heparin or protamine (P &lt; 0.05).	Heparin	0-7	integrin subunit alpha M	Homo sapiens	62-67
7556445-8	1995	Whereas addition of suramin to COS cell cultures significantly increases the levels of all six Wnts in the medium, the addition of heparin only influences the levels of Wnt-1, Wnt-6, and Wnt-7b.	Heparin	131-138	wingless-type MMTV integration site family, member 6	Mus musculus	176-181
8608187-3	1995	Brief exposure (60 min) of cells to the phospholipase A2 inhibitors, mepacrine (500 mumol/l) and heparin (1 g/l), reduced the number of colonies formed in the control group and completely abolished the increase in the number of colonies formed after treatment of the cells with phorbol ester.	Heparin	97-104	phospholipase A2, group IB, pancreas	Mus musculus	40-56
7559767-5	1995	Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1.	Heparin	126-133	integrin subunit alpha M	Homo sapiens	116-121
7559767-5	1995	Inhibition studies with mAbs and chemically modified forms of heparin suggest the I domain as a recognition site on Mac-1 for heparin, and suggest that either N- or O-sulfation is sufficient for heparin to bind efficiently to Mac-1.	Heparin	126-133	integrin subunit alpha M	Homo sapiens	116-121
7559767-6	1995	Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.	Heparin	45-53	integrin subunit alpha M	Homo sapiens	154-159
7559767-6	1995	Under conditions of continuous flow in which heparins and E-selectin are cosubstrates, neutrophils tether to E-selectin and form firm adhesions through a Mac-1-heparin interaction.	Heparin	45-52	integrin subunit alpha M	Homo sapiens	154-159
7646440-3	1995	PMA increased particulate phospholipase A2 (PLA2) activity, lysophosphatidylcholine formation and arachidonic acid release from bone marrow cells; these effects were abolished when cells were pretreated with the putative PLA2 inhibitors heparin and mepacrine.	Heparin	237-244	phospholipase A2, group IB, pancreas	Mus musculus	221-225
7543105-12	1995	PMA was also able to reverse the inhibition of vitronectin degradation seen when cells were pretreated with heparinase or incubated with exogenous heparin.	Heparin	108-115	vitronectin	Homo sapiens	47-58
7638745-8	1995	EC proliferation on FG containing FGF-1 was significantly increased by addition of 5, 50, or 500 units/ml heparin (+68%, +99%, and +106%, respectively; p (0.0001 for all), reflecting the synergism of FGF-1 by heparin.	Heparin	106-113	fibroblast growth factor 1	Canis lupus familiaris	34-39
7638745-8	1995	EC proliferation on FG containing FGF-1 was significantly increased by addition of 5, 50, or 500 units/ml heparin (+68%, +99%, and +106%, respectively; p (0.0001 for all), reflecting the synergism of FGF-1 by heparin.	Heparin	106-113	fibroblast growth factor 1	Canis lupus familiaris	200-205
7638745-8	1995	EC proliferation on FG containing FGF-1 was significantly increased by addition of 5, 50, or 500 units/ml heparin (+68%, +99%, and +106%, respectively; p (0.0001 for all), reflecting the synergism of FGF-1 by heparin.	Heparin	209-216	fibroblast growth factor 1	Canis lupus familiaris	34-39
8566122-7	1995	At the same time, the rat trachea contraction induced by PAF-loaded liposomes could be linked to the PtdIns(1,4,5)P3-dependent Ca2+ channels from the endoplasmic reticulum and/or to the interaction with G proteins, as shown by the blocking effects of heparin-containing liposomes.	Heparin	251-258	PCNA clamp associated factor	Rattus norvegicus	57-60
7542204-0	1995	Evidence that conformational changes upon the transition of the native to the modified form of vitronectin are not limited to the heparin binding domain.	Heparin	130-137	vitronectin	Homo sapiens	95-106
7790818-5	1995	This conclusion is based on the findings that IP-10 binding to cells is: (a) inhibited by heparin and heparan sulfate; (b) sensitive to a 1 M NaCl wash; (c) eliminated by treatment with heparinase and trypsin; and (d) absent on mutant CHO cells that do not express cell surface HSPG.	Heparin	90-97	C-X-C motif chemokine ligand 10	Homo sapiens	46-51
7727433-0	1995	Effect of heparin on the inhibition of factor Xa by tissue factor pathway inhibitor: a segment, Gly212-Phe243, of the third Kunitz domain is a heparin-binding site.	Heparin	10-17	coagulation factor X	Homo sapiens	39-48
7727433-0	1995	Effect of heparin on the inhibition of factor Xa by tissue factor pathway inhibitor: a segment, Gly212-Phe243, of the third Kunitz domain is a heparin-binding site.	Heparin	143-150	coagulation factor X	Homo sapiens	39-48
7537960-7	1995	N-terminal sequence analysis indicated that this binding fragment of vitronectin originates with Thr-122 and comprises the hemopexin domain, including the heparin-binding region of the vitronectin molecule.	Heparin	155-162	vitronectin	Homo sapiens	69-80
7537960-7	1995	N-terminal sequence analysis indicated that this binding fragment of vitronectin originates with Thr-122 and comprises the hemopexin domain, including the heparin-binding region of the vitronectin molecule.	Heparin	155-162	vitronectin	Homo sapiens	185-196
7730327-0	1995	Alternately spliced NH2-terminal immunoglobulin-like Loop I in the ectodomain of the fibroblast growth factor (FGF) receptor 1 lowers affinity for both heparin and FGF-1.	Heparin	152-159	Fibroblast growth factor receptor 1	Rattus norvegicus	85-126
7730327-3	1995	Here we show that a lower affinity of FGFR1 alpha for heparin parallels the lower affinity for FGF-1.	Heparin	54-61	Fibroblast growth factor receptor 1	Rattus norvegicus	38-43
7727531-0	1995	Increased heparin binding by site directed mutagenesis of a recombinant chimera of bombyxin and insulin-like growth factor II.	Heparin	10-17	insulin like growth factor 2	Bos taurus	96-125
7495073-0	1995	Inhibition of prothrombinase by antithrombin-heparin at a macroscopic surface.	Heparin	45-52	coagulation factor X	Homo sapiens	14-28
7495073-9	1995	The heparin-independent inhibition of prothrombinase by antithrombin (4 microM) in the presence of prothrombin (0.2 microM) was virtually negligible.	Heparin	4-11	coagulation factor X	Homo sapiens	38-52
7534133-6	1995	However, in the presence of heparin (1 or 50 U/mL), C1Inh appeared to be the major inhibitor of FXIa, followed by ATIII.	Heparin	28-35	serpin family G member 1	Homo sapiens	52-57
7533163-0	1995	Tenascin-C binds heparin by its fibronectin type III domain five.	Heparin	17-24	tenascin C	Homo sapiens	0-10
7534055-7	1995	The heparin-coated surface causes less activation of eosinophils; also released eosinophil cationic protein is bound to the heparinized surface.	Heparin	4-11	ribonuclease A family member 3	Homo sapiens	80-107
7899079-2	1995	Although CRP binding to the lac DNA is stabilized in the ternary open complex, a high concentration of heparin dissociates CRP from the open complex without affecting the interaction between RNA polymerase and promoter, resulting in a binary complex.	Heparin	103-110	catabolite gene activator protein	Escherichia coli	123-126
7531786-5	1995	RESULTS: Animals in both VEGF-treated groups had a significantly higher (p &lt; 0.01) increase in calf blood pressure ratio at day 10 (control, 0.44 +/- 0.02; heparin, 0.47 +/- 0.02; VEGF, 0.60 +/- 0.01; heparin+VEGF, 0.61 +/- 0.02) and day 30 (control, 0.49 +/- 0.05; heparin, 0.48 +/- 0.02; VEGF, 0.70 +/- 0.03; heparin+VEGF, 0.73 +/- 0.03).	Heparin	159-166	vascular endothelial growth factor A	Bos taurus	25-29
7531786-5	1995	RESULTS: Animals in both VEGF-treated groups had a significantly higher (p &lt; 0.01) increase in calf blood pressure ratio at day 10 (control, 0.44 +/- 0.02; heparin, 0.47 +/- 0.02; VEGF, 0.60 +/- 0.01; heparin+VEGF, 0.61 +/- 0.02) and day 30 (control, 0.49 +/- 0.05; heparin, 0.48 +/- 0.02; VEGF, 0.70 +/- 0.03; heparin+VEGF, 0.73 +/- 0.03).	Heparin	204-211	vascular endothelial growth factor A	Bos taurus	25-29
7531786-5	1995	RESULTS: Animals in both VEGF-treated groups had a significantly higher (p &lt; 0.01) increase in calf blood pressure ratio at day 10 (control, 0.44 +/- 0.02; heparin, 0.47 +/- 0.02; VEGF, 0.60 +/- 0.01; heparin+VEGF, 0.61 +/- 0.02) and day 30 (control, 0.49 +/- 0.05; heparin, 0.48 +/- 0.02; VEGF, 0.70 +/- 0.03; heparin+VEGF, 0.73 +/- 0.03).	Heparin	204-211	vascular endothelial growth factor A	Bos taurus	25-29
7531786-5	1995	RESULTS: Animals in both VEGF-treated groups had a significantly higher (p &lt; 0.01) increase in calf blood pressure ratio at day 10 (control, 0.44 +/- 0.02; heparin, 0.47 +/- 0.02; VEGF, 0.60 +/- 0.01; heparin+VEGF, 0.61 +/- 0.02) and day 30 (control, 0.49 +/- 0.05; heparin, 0.48 +/- 0.02; VEGF, 0.70 +/- 0.03; heparin+VEGF, 0.73 +/- 0.03).	Heparin	204-211	vascular endothelial growth factor A	Bos taurus	25-29
7531786-6	1995	Both VEGF-treated groups had a significantly higher (p &lt; 0.05) angiographic score at day 30 (control, 0.28 +/- 0.01; heparin, 0.28 +/- 0.01; VEGF, 0.37 +/- 0.01; heparin+VEGF, 0.38 +/- 0.02).	Heparin	120-127	vascular endothelial growth factor A	Oryctolagus cuniculus	5-9
7531786-6	1995	Both VEGF-treated groups had a significantly higher (p &lt; 0.05) angiographic score at day 30 (control, 0.28 +/- 0.01; heparin, 0.28 +/- 0.01; VEGF, 0.37 +/- 0.01; heparin+VEGF, 0.38 +/- 0.02).	Heparin	165-172	vascular endothelial growth factor A	Oryctolagus cuniculus	5-9
7531786-7	1995	Maximum flow reserve at day 30 in the ischemic limb was higher (p &lt; 0.05) in VEGF-treated rabbits (control, 1.87 +/- 0.07; heparin, 1.92 +/- 0.08; VEGF, 2.42 +/- 0.16; heparin+VEGF, 2.33 +/- 0.12).	Heparin	126-133	vascular endothelial growth factor A	Oryctolagus cuniculus	80-84
7531786-7	1995	Maximum flow reserve at day 30 in the ischemic limb was higher (p &lt; 0.05) in VEGF-treated rabbits (control, 1.87 +/- 0.07; heparin, 1.92 +/- 0.08; VEGF, 2.42 +/- 0.16; heparin+VEGF, 2.33 +/- 0.12).	Heparin	171-178	vascular endothelial growth factor A	Oryctolagus cuniculus	80-84
7531786-8	1995	Capillary density was higher (p &lt; 0.01) in the ischemic muscles of VEGF-treated rabbits (control, 156 +/- 10/mm2; heparin, 178 +/- 8/mm2; VEGF, 230 +/- 10/mm2; heparin+VEGF, 233 +/- 8/mm2).	Heparin	117-124	vascular endothelial growth factor A	Oryctolagus cuniculus	70-74
7814368-5	1995	The resulting thrombin was also purified by heparin affinity chromatography.	Heparin	44-51	coagulation factor II, thrombin	Bos taurus	14-22
7530915-10	1995	Heparin in the patch pipette reduced the increase in outward currents induced by bradykinin, an agonist known to raise IP3 and to release Ca2+, but did not prevent CPA-induced increases in outward current.	Heparin	0-7	kininogen 1	Bos taurus	81-91
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	50-57	kinase insert domain receptor	Homo sapiens	4-8
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	50-57	kinase insert domain receptor	Homo sapiens	95-100
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	50-57	kinase insert domain receptor	Homo sapiens	158-163
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	184-191	kinase insert domain receptor	Homo sapiens	4-8
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	184-191	kinase insert domain receptor	Homo sapiens	95-100
8527158-9	1995	The Flk1-AP fusion protein was also found to bind heparin, implying that ligand binding by the Flk-1 receptor may involve a three way interaction between the Flk-1 receptor, VEGF, and heparin-like cell surface proteoglycans.	Heparin	184-191	kinase insert domain receptor	Homo sapiens	158-163
7991602-0	1994	Heparin-dependent binding and autophosphorylation of epidermal growth factor (EGF) receptor by heparin-binding EGF-like growth factor but not by EGF.	Heparin	0-7	proheparin-binding EGF-like growth factor	Cricetulus griseus	95-133
7991602-5	1994	Moreover, binding of radiolabeled EGF to HSPG-deficient EGF receptor-expressing cells is efficiently displaced by nonlabeled HB-EGF only in the presence of heparin.	Heparin	156-163	proheparin-binding EGF-like growth factor	Cricetulus griseus	125-131
7991602-6	1994	Signal transduction by the EGF receptor tyrosine kinase as evidenced by receptor autophosphorylation is induced by HB-EGF only in the presence of heparin, in contrast to EGF-induced receptor autophosphorylation, which is independent of heparin.	Heparin	146-153	proheparin-binding EGF-like growth factor	Cricetulus griseus	115-121
7740455-7	1994	At concentrations which doubled the clotting time of contact-activated normal plasma, heparin and three low Mr heparins also abrogated prothrombin activation initiated with 0.5 nM factor Xa, but not with 5 nM factor Xa.	Heparin	111-119	coagulation factor X	Homo sapiens	180-189
7740455-10	1994	When 5 or 10 pM relipidated r-human tissue factor and CaCl2 were added to normal plasma, heparin and the three low Mr heparins delayed the onset of prothrombin activation until the concentration of factor Xa generated exceeded 1 nM, and they subsequently inhibited prothrombin activation to the same extent.	Heparin	89-96	coagulation factor X	Homo sapiens	198-207
7859927-3	1994	N-Terminal and tryptic peptide fragment analysis of these polypeptides revealed that they are identical to midkine (MK) and pleiotrophin (PTN), respectively, which form a new family of heparin-binding growth/differentiation factors.	Heparin	185-192	pleiotrophin	Bos taurus	124-136
7859927-3	1994	N-Terminal and tryptic peptide fragment analysis of these polypeptides revealed that they are identical to midkine (MK) and pleiotrophin (PTN), respectively, which form a new family of heparin-binding growth/differentiation factors.	Heparin	185-192	pleiotrophin	Bos taurus	138-141
7820850-4	1994	Nuclear IP3R is sensitive to heparin and is phosphorylated by nuclear PKC, enhancing the efficiency of IP3 in nuclear calcium release.	Heparin	29-36	inositol 1,4,5-trisphosphate receptor, type 1	Rattus norvegicus	8-12
7522235-7	1994	Reactivity of the antibody which inhibited heparin binding greatly increased upon denaturation of vitronectin, implying that this region is normally inaccessible in the native form of the molecule.	Heparin	43-50	vitronectin	Homo sapiens	98-109
8067842-2	1994	Here we assessed the effect of immobilized heparin on the generation of C3a and terminal complement complexes during CPB.	Heparin	43-50	complement C3	Homo sapiens	72-75
8067842-8	1994	Although there was no difference in C3a levels between the two groups at the end of CPB, C3a levels were significantly lower in the heparin-coated group 30 minutes after CPB (194 +/- 18 ng/mL and 307 +/- 18 ng/mL in heparin-coated and control groups, respectively; p &lt; 0.001).	Heparin	132-139	complement C3	Homo sapiens	89-92
8045504-1	1994	Because hepatocyte growth factor is known to have affinity for heparin, we studied the binding isotherm and found that hepatocyte growth factor has a high-affinity binding site for 35S-heparin with an equilibrium dissociation constant of approximately 0.6 nmol/L.	Heparin	63-70	hepatocyte growth factor	Rattus norvegicus	8-32
8045504-1	1994	Because hepatocyte growth factor is known to have affinity for heparin, we studied the binding isotherm and found that hepatocyte growth factor has a high-affinity binding site for 35S-heparin with an equilibrium dissociation constant of approximately 0.6 nmol/L.	Heparin	63-70	hepatocyte growth factor	Rattus norvegicus	119-143
8045504-1	1994	Because hepatocyte growth factor is known to have affinity for heparin, we studied the binding isotherm and found that hepatocyte growth factor has a high-affinity binding site for 35S-heparin with an equilibrium dissociation constant of approximately 0.6 nmol/L.	Heparin	185-192	hepatocyte growth factor	Rattus norvegicus	8-32
8045504-1	1994	Because hepatocyte growth factor is known to have affinity for heparin, we studied the binding isotherm and found that hepatocyte growth factor has a high-affinity binding site for 35S-heparin with an equilibrium dissociation constant of approximately 0.6 nmol/L.	Heparin	185-192	hepatocyte growth factor	Rattus norvegicus	119-143
8045504-6	1994	Furthermore, the steady state hepatic extraction ratio of 125I-hepatocyte growth factor in perfused rat liver decreased depending on the heparin concentration.	Heparin	137-144	hepatocyte growth factor	Rattus norvegicus	63-87
8045504-8	1994	Although the half-effective concentration of hepatocyte growth factor increased slightly--namely, two to three times in the presence of heparin compared with that in its absence--the maximal activity was not changed.	Heparin	136-143	hepatocyte growth factor	Rattus norvegicus	45-69
7948751-4	1994	Recombinant murine D-factor produced a dose- and time-dependent inhibition of heparin-releasable LPL activity in differentiated 3T3-L1 adipocytes.	Heparin	78-85	lipoprotein lipase	Mus musculus	97-100
8011637-5	1994	A putative heparin-binding site is found in glia-derived nexin between residues 71 and 86; heparin-binding sites are found in homologous regions of antithrombin III and heparin cofactor II.	Heparin	91-98	serpin family C member 1	Rattus norvegicus	148-164
8011637-9	1994	These results support the hypothesis that the heparin-binding sites of glia-derived nexin, antithrombin III, and heparin cofactor II are found in homologous regions of the molecules.	Heparin	46-53	serpin family C member 1	Rattus norvegicus	91-107
7922353-5	1994	RESULTS: Using affinity co-electrophoresis we found that interleukin-8 preferentially bound a subfraction of heparin that also showed increased affinity for melanoma growth stimulating activity (also known as MGSA, GRO or GRO alpha).	Heparin	109-116	C-X-C motif chemokine ligand 1	Homo sapiens	209-213
7922353-5	1994	RESULTS: Using affinity co-electrophoresis we found that interleukin-8 preferentially bound a subfraction of heparin that also showed increased affinity for melanoma growth stimulating activity (also known as MGSA, GRO or GRO alpha).	Heparin	109-116	C-X-C motif chemokine ligand 1	Homo sapiens	222-231
8196366-1	1994	BACKGROUND: The secretory glycoprotein, extracellular-superoxide dismutase (EC-SOD) is in the body, primarily located to the tissue interstitial space, and in tissue is almost completely composed of homotetrameric high-heparin-affinity C-type.	Heparin	219-226	superoxide dismutase 3	Rattus norvegicus	40-74
8196366-1	1994	BACKGROUND: The secretory glycoprotein, extracellular-superoxide dismutase (EC-SOD) is in the body, primarily located to the tissue interstitial space, and in tissue is almost completely composed of homotetrameric high-heparin-affinity C-type.	Heparin	219-226	superoxide dismutase 3	Rattus norvegicus	76-82
8196366-5	1994	RESULTS: EC-SOD C displayed a tissue half-life of about 85 hours, whereas the EC-SOD variants with reduced and absent heparin-affinities displayed half-lives of about 20 and 7 hours, respectively.	Heparin	118-125	superoxide dismutase 3	Rattus norvegicus	78-84
8196366-7	1994	CONCLUSIONS: The findings established that EC-SOD C in the tissue interstitium exists almost completely anchored to heparan sulfate proteoglycan via the carboxyterminal heparin-binding domains, and that this binding is the determinant of the long tissue retention of the enzyme.	Heparin	169-176	superoxide dismutase 3	Rattus norvegicus	43-49
8196366-8	1994	The findings further suggest that reductions in heparin-affinity, e.g., by proteolytic truncation of the highly susceptible heparin-binding domain, may be an important mechanism of elimination of EC-SOD from tissues, both physiologically and as enhanced under pathologic conditions.	Heparin	48-55	superoxide dismutase 3	Rattus norvegicus	196-202
8196366-8	1994	The findings further suggest that reductions in heparin-affinity, e.g., by proteolytic truncation of the highly susceptible heparin-binding domain, may be an important mechanism of elimination of EC-SOD from tissues, both physiologically and as enhanced under pathologic conditions.	Heparin	124-131	superoxide dismutase 3	Rattus norvegicus	196-202
8175651-0	1994	Heparin modulates the interaction of VEGF165 with soluble and cell associated flk-1 receptors.	Heparin	0-7	kinase insert domain receptor	Homo sapiens	78-83
8175651-8	1994	The effect of heparin on the binding of 125I-VEGF165 to flk-1/SEAP could not be mimicked by desulfated heparin or by chondroitin sulfate.	Heparin	14-21	kinase insert domain receptor	Homo sapiens	56-61
8054461-6	1994	It was concluded that at least twice the dose of Fragmin (anti-FXa), compared with heparin, was required, suggesting that thrombin inhibition is crucial for the antithrombotic efficacy of heparin in CPB circuits.	Heparin	188-195	coagulation factor X	Homo sapiens	63-66
8135737-2	1994	Heparin-releasable and cell-associated LPL activity rose immediately after birth, followed 1-2 days later by an increase in LPL mRNA.	Heparin	0-7	lipoprotein lipase	Mus musculus	124-127
8135737-4	1994	During lactation, both milk and heparin-releasable LPL were substantially decreased by an overnight fast, whereas cell-associated LPL was less affected and LPL mRNA did not change.	Heparin	32-39	lipoprotein lipase	Mus musculus	51-54
8135737-5	1994	These studies indicate that the extracellular, heparin-releasable, fraction of mammary LPL activity responds most rapidly to alterations in physiological state, usually accompanied by smaller changes in cellular enzyme activity.	Heparin	47-54	lipoprotein lipase	Mus musculus	87-90
8114701-10	1994	We propose that the heparin-binding domain of mature AR necessitates the presence of a specific structural motif in an N-terminal pro-region to permit proper folding, and thus secretion, of a bioactive molecule.	Heparin	20-27	amphiregulin	Homo sapiens	53-55
8028773-0	1994	Heparin treatment increases 9-kb MAP2 mRNA levels in neuronal cell cultures.	Heparin	0-7	microtubule associated protein 2	Homo sapiens	33-37
8028773-2	1994	24 h after treatment, Northern blots analysis revealed an increase in the expression of the 9-kb MAP2 mRNA in the heparin-treated neuronal cultures.	Heparin	114-121	microtubule associated protein 2	Homo sapiens	97-101
7819340-6	1994	A strong heparin-binding site within a region conserved in rodent and human APP, APLP1 and APLP2, was identified.	Heparin	9-16	amyloid beta precursor like protein 1	Homo sapiens	81-86
7819340-10	1994	Since all APP and L-APP isoforms so far described include these exons, the strong heparin binding site is a ubiquitous feature of all APP and L-APP isoforms strongly suggesting that the brain-specific and neuronal, as well as the non-neuronal and peripheral APPs and L-APPs do have CAM- and SAM-like activities.	Heparin	82-89	cathepsin B	Homo sapiens	258-262
7819340-10	1994	Since all APP and L-APP isoforms so far described include these exons, the strong heparin binding site is a ubiquitous feature of all APP and L-APP isoforms strongly suggesting that the brain-specific and neuronal, as well as the non-neuronal and peripheral APPs and L-APPs do have CAM- and SAM-like activities.	Heparin	82-89	cathepsin B	Homo sapiens	269-273
7734144-6	1994	The concentration of heparin required for half maximal stimulation of VEGF binding to KDR-expressing cells (500 ng/ml) was 25 times greater than that required for half maximal inhibition of binding to FLT1-expressing cells (20 ng/ml).	Heparin	21-28	kinase insert domain receptor	Homo sapiens	86-89
8078383-1	1994	Experimentally, heparin inhibits mechanisms that promote fibrosis, neointimal cellular proliferation, and thrombin bound to fibrin at the surface of intraluminal thrombus, but only in relatively high concentrations.	Heparin	16-23	prothrombin	Oryctolagus cuniculus	106-114
7693706-9	1993	Oligomeric urea-treated vitronectin reacted more strongly with the 8E6 antibody, bound biotinylated heparin more strongly, and neutralized the anticoagulant activity of heparin better than monomeric altered vitronectin or native vitronectin.	Heparin	100-107	vitronectin	Homo sapiens	24-35
7693706-9	1993	Oligomeric urea-treated vitronectin reacted more strongly with the 8E6 antibody, bound biotinylated heparin more strongly, and neutralized the anticoagulant activity of heparin better than monomeric altered vitronectin or native vitronectin.	Heparin	169-176	vitronectin	Homo sapiens	24-35
7693706-10	1993	After incubation with urea at 25 degrees C, native vitronectin, treated during purification with dithionitrobenzoic acid to force free sulfhydryls to intramolecular disulfides, exhibited increased reactivity with antibody 8E6, increased binding to heparin, and oligomerization.	Heparin	248-255	vitronectin	Homo sapiens	51-62
7693706-13	1993	Thus, an irreversible conformational alteration occurs upon treatment of vitronectin with urea, resulting in oligomers that bind avidly to heparin.	Heparin	139-146	vitronectin	Homo sapiens	73-84
7692967-5	1993	Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present.	Heparin	375-382	kallikrein related peptidase 4	Homo sapiens	75-85
7692967-5	1993	Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present.	Heparin	375-382	kallikrein related peptidase 4	Homo sapiens	135-145
7692967-5	1993	Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present.	Heparin	375-382	kallikrein related peptidase 4	Homo sapiens	135-145
7692967-5	1993	Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present.	Heparin	375-382	kallikrein related peptidase 4	Homo sapiens	135-145
7692967-6	1993	Similarly, the presence of therapeutic levels of heparin (approximately 1 unit/mL) in normal, factor XII-deficient, and prekallikrein-deficient plasmas enhanced the rate of inactivation of added kallikrein by 2.3-fold and significantly altered the partitioning of radiolabeled kallikrein from predominantly C1-inhibitor and alpha 2-macroglobulin complexes (86-92%) to mostly antithrombin complexes (50-53%).	Heparin	49-56	kallikrein related peptidase 4	Homo sapiens	123-133
7692967-6	1993	Similarly, the presence of therapeutic levels of heparin (approximately 1 unit/mL) in normal, factor XII-deficient, and prekallikrein-deficient plasmas enhanced the rate of inactivation of added kallikrein by 2.3-fold and significantly altered the partitioning of radiolabeled kallikrein from predominantly C1-inhibitor and alpha 2-macroglobulin complexes (86-92%) to mostly antithrombin complexes (50-53%).	Heparin	49-56	kallikrein related peptidase 4	Homo sapiens	195-205
7692967-9	1993	These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans.	Heparin	141-148	kallikrein related peptidase 4	Homo sapiens	102-112
7692967-9	1993	These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans.	Heparin	152-159	kallikrein related peptidase 4	Homo sapiens	102-112
8222396-10	1993	These results demonstrate that the conjugation of RGDS peptide with SCM-chitin led to augmentation of therapeutic potential to cancer metastasis, thus implying an importance of the conjugation of cell-adhesive RGDS peptide with structurally heparin-like SCM-chitin, which possess binding ability to the heparin-binding domain of fibronectin or laminin and extremely low anticoagulant properties.	Heparin	241-248	ral guanine nucleotide dissociation stimulator	Mus musculus	50-54
8222396-10	1993	These results demonstrate that the conjugation of RGDS peptide with SCM-chitin led to augmentation of therapeutic potential to cancer metastasis, thus implying an importance of the conjugation of cell-adhesive RGDS peptide with structurally heparin-like SCM-chitin, which possess binding ability to the heparin-binding domain of fibronectin or laminin and extremely low anticoagulant properties.	Heparin	241-248	ral guanine nucleotide dissociation stimulator	Mus musculus	210-214
8222396-10	1993	These results demonstrate that the conjugation of RGDS peptide with SCM-chitin led to augmentation of therapeutic potential to cancer metastasis, thus implying an importance of the conjugation of cell-adhesive RGDS peptide with structurally heparin-like SCM-chitin, which possess binding ability to the heparin-binding domain of fibronectin or laminin and extremely low anticoagulant properties.	Heparin	303-310	ral guanine nucleotide dissociation stimulator	Mus musculus	50-54
8222396-10	1993	These results demonstrate that the conjugation of RGDS peptide with SCM-chitin led to augmentation of therapeutic potential to cancer metastasis, thus implying an importance of the conjugation of cell-adhesive RGDS peptide with structurally heparin-like SCM-chitin, which possess binding ability to the heparin-binding domain of fibronectin or laminin and extremely low anticoagulant properties.	Heparin	303-310	ral guanine nucleotide dissociation stimulator	Mus musculus	210-214
7693680-9	1993	During plasmin proteolysis of VN, fragments were generated that lacked the heparin binding region and that lost the ability to multimerize following urea or detergent treatment, implicating that the highly basic region is essential for multimer formation.	Heparin	75-82	vitronectin	Homo sapiens	30-32
7693680-10	1993	These data suggest that non-plasma forms of VN, which are abundant in platelets and subendothelium, represent the prototype conformer of the reactive heparin binding form of VN.	Heparin	150-157	vitronectin	Homo sapiens	44-46
7693680-10	1993	These data suggest that non-plasma forms of VN, which are abundant in platelets and subendothelium, represent the prototype conformer of the reactive heparin binding form of VN.	Heparin	150-157	vitronectin	Homo sapiens	174-176
8360182-0	1993	Modulation of tissue plasminogen activator-catalyzed plasminogen activation by synthetic peptides derived from the amino-terminal heparin binding domain of fibronectin.	Heparin	130-137	chromosome 20 open reading frame 181	Homo sapiens	14-42
8390244-1	1993	Two molecular species of glioma-derived motility factor (GMF), GMF-I and GMF-II, have been purified to homogeneity from the serum-free conditioned medium of a highly invasive human glioma cell line, T98G, by gelatin affinity chromatography and heparin affinity-, DEAE-, hydroxyapatite-, gel permeation- and sulfopropyl high performance liquid chromatography.	Heparin	244-251	glia maturation factor beta	Homo sapiens	25-55
8390244-1	1993	Two molecular species of glioma-derived motility factor (GMF), GMF-I and GMF-II, have been purified to homogeneity from the serum-free conditioned medium of a highly invasive human glioma cell line, T98G, by gelatin affinity chromatography and heparin affinity-, DEAE-, hydroxyapatite-, gel permeation- and sulfopropyl high performance liquid chromatography.	Heparin	244-251	glia maturation factor beta	Homo sapiens	57-60
8408111-3	1993	High affinity heparin oligosaccharides (HA-heparin, anti-factor Xa activity of 592 +/- 120 IU/mg) prepared by partial deaminative cleavage of commercial crude heparin and fractionated by agarose-ATIII affinity chromatography, were immobilized to surface-modified PE by reductive amination.	Heparin	14-21	coagulation factor X	Homo sapiens	57-66
8390882-10	1993	The reconstituted recombinant casein kinase II exhibited characteristics of the native holoenzyme in subunit composition, inhibition by heparin, stimulation by basic compounds, and the KCl concentration required for optimal activity.	Heparin	136-143	casein kinase IIalpha	Drosophila melanogaster	30-46
8496151-3	1993	PC cell-derived growth factor (PCDGF) was purified to homogeneity from PC cell-conditioned medium as an apparent 88-kDa protein by chromatography on heparin-Sepharose, Sephacryl S-200, and phenyl-Sepharose.	Heparin	149-156	granulin	Mus musculus	0-29
8496151-3	1993	PC cell-derived growth factor (PCDGF) was purified to homogeneity from PC cell-conditioned medium as an apparent 88-kDa protein by chromatography on heparin-Sepharose, Sephacryl S-200, and phenyl-Sepharose.	Heparin	149-156	granulin	Mus musculus	31-36
8320164-0	1993	Carboxyl-terminal heparin-binding fragments of platelet factor 4 retain the blocking effect on the receptor binding of basic fibroblast growth factor.	Heparin	18-25	platelet factor 4	Bos taurus	47-64
8320164-2	1993	In the present study, we constructed carboxyl-terminal fragments, which represent the heparin-binding region of the PF-4 molecule, and examined whether these synthetic peptides retain the blocking effects on the receptor binding of bFGF.	Heparin	86-93	platelet factor 4	Bos taurus	116-120
8386194-6	1993	MBP also inhibits APC generation by purified soluble rabbit TM with an IC50 of 100 nM without altering its apparent Kd for thrombin or Km for protein C. This inhibition is reversed by polyanions such as chondroitin sulfate E and heparin.	Heparin	229-236	myelin basic protein	Oryctolagus cuniculus	0-3
8458417-0	1993	Decorin is specifically solubilized by heparin from the extracellular matrix of rat skeletal muscles.	Heparin	39-46	decorin	Rattus norvegicus	0-7
8458417-2	1993	In this report we unequivocally demonstrate by biochemical and immunological analyses that the proteoglycan that is solubilized by heparin from rat skeletal muscle ECM corresponds to decorin.	Heparin	131-138	decorin	Rattus norvegicus	183-190
8388354-8	1993	Sequestration of vitronectin and complement factor H by immobilised heparins could promote an effective defence against complement-mediated prothrombotic activity and cell damage under physiological conditions.	Heparin	68-76	vitronectin	Homo sapiens	17-28
7678252-7	1993	Furthermore, TAT in patient plasmas (disseminated intravascular coagulation and sepsis) was found to bind to heparin-Sepharose, indicating that this endogenously formed TAT was also associated with VN.	Heparin	109-116	vitronectin	Homo sapiens	198-200
8446937-5	1993	Pretreating the microvasculature with large amounts of heparin resulted in recovery of antithrombin III in the recirculated heparin solution.	Heparin	55-62	serpin family C member 1	Rattus norvegicus	87-103
8446937-5	1993	Pretreating the microvasculature with large amounts of heparin resulted in recovery of antithrombin III in the recirculated heparin solution.	Heparin	124-131	serpin family C member 1	Rattus norvegicus	87-103
8446937-7	1993	It is concluded that disappearance of thrombin enzymatic activity from a solution when recirculated through the microcirculation can be considerably increased if recirculated together with heparin, which probably reacts with endogenous antithrombin III on the vessel wall.	Heparin	189-196	serpin family C member 1	Rattus norvegicus	236-252
8439679-7	1993	Thrombin time changed from 18 +/- 0 sec before to 19 +/- 1 sec after 6 hours for heparin, as compared with 16 +/- 1 sec to 18 +/- 1 sec for phospholipid (NS).	Heparin	81-88	coagulation factor II, thrombin	Bos taurus	0-8
7509997-0	1993	Heparin inhibits endothelin-1 and proto-oncogene c-fos gene expression in cultured bovine endothelial cells.	Heparin	0-7	endothelin 1	Bos taurus	17-54
7509997-2	1993	Northern blot analysis using cDNA for bovine prepro-ET-1 as a probe showed that heparin lowered not only the basal but also the stimulated expression of prepro-ET-1 mRNA by thrombin.	Heparin	80-87	endothelin 1	Bos taurus	45-56
7509997-2	1993	Northern blot analysis using cDNA for bovine prepro-ET-1 as a probe showed that heparin lowered not only the basal but also the stimulated expression of prepro-ET-1 mRNA by thrombin.	Heparin	80-87	endothelin 1	Bos taurus	153-164
7509997-2	1993	Northern blot analysis using cDNA for bovine prepro-ET-1 as a probe showed that heparin lowered not only the basal but also the stimulated expression of prepro-ET-1 mRNA by thrombin.	Heparin	80-87	coagulation factor II, thrombin	Bos taurus	173-181
7509997-4	1993	Heparin similarly inhibited thrombin-induced c-fos proto-oncogene mRNA expression in ECs.	Heparin	0-7	coagulation factor II, thrombin	Bos taurus	28-36
7509997-5	1993	These data suggest that heparin, in addition to its antithrombin effect, has an inhibitory effect on prepro-ET-1 mRNA expression, possibly via a PKC-dependent pathway.	Heparin	24-31	endothelin 1	Bos taurus	101-112
7678767-8	1993	This activity was inhibited by heparin, indicating that the expressed protein has activity similar to those reported for animal and yeast CKII.	Heparin	31-38	casein kinase II, alpha chain 2	Arabidopsis thaliana	138-142
8362270-1	1993	Anti-factor Xa methods have been generally accepted for the monitoring of heparin treatment mainly due to their sensitivity to LMWH and excellent performance on automated equipment.	Heparin	74-81	coagulation factor X	Homo sapiens	5-14
8395736-0	1993	Anti-factor Xa determination in blood: a new method for controlling heparin therapy.	Heparin	68-75	coagulation factor X	Homo sapiens	5-14
1459996-9	1992	Thus, the heparin affinity of TSP can be modulated by the expression of TSP as homo- or heterotrimers.	Heparin	10-17	CTR9 homolog, Paf1/RNA polymerase II complex component	Mus musculus	30-33
1459996-9	1992	Thus, the heparin affinity of TSP can be modulated by the expression of TSP as homo- or heterotrimers.	Heparin	10-17	CTR9 homolog, Paf1/RNA polymerase II complex component	Mus musculus	72-75
1280270-2	1992	This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity.	Heparin	201-208	vitronectin	Gallus gallus	37-48
1280270-2	1992	This is the first report on a unique vitronectin molecule, yolk vitronectin, which is similar to its blood homologue in cell spreading activity but different in molecular size, bound carbohydrate, and heparin and collagen binding activity.	Heparin	201-208	vitronectin	Gallus gallus	64-75
1492975-2	1992	This homologue, which we have named HBP due to its strong affinity to heparin, is a chemoattractant for monocytes and has been shown to induce reversible detachment and contraction when added to monolayers of endothelial cells or fibroblasts.	Heparin	70-77	azurocidin 1	Homo sapiens	36-39
1283096-4	1992	A single heparin-Sepharose chromatography of the ultrafiltrates yielded essentially homogenous, biologically active, recombinant rat aFGF or bFGF.	Heparin	9-16	fibroblast growth factor 1	Rattus norvegicus	133-137
1279676-10	1992	The interaction between extracellular matrix proteins and 4-1BB was completely blocked by the anionic carbohydrate polymer fucoidan and was partially blocked by the anionic carbohydrate polymer dextran sulfate and the glycosaminoglycan heparin sulfate but was unaffected by desulfated heparin.	Heparin	236-243	TNF receptor superfamily member 9	Homo sapiens	58-63
1471071-0	1992	Interaction of heparin with myosin ATPase: possible involvement with the hemorrhagic activity and a correlation with antithrombin III high affinity-heparin molecules.	Heparin	15-22	serpin family C member 1	Rattus norvegicus	117-133
1471071-0	1992	Interaction of heparin with myosin ATPase: possible involvement with the hemorrhagic activity and a correlation with antithrombin III high affinity-heparin molecules.	Heparin	148-155	serpin family C member 1	Rattus norvegicus	117-133
1471071-4	1992	Heparin with high affinity for antithrombin III, prepared by antithrombin-affinity chromatography, dislodges up to 90% of the bound [35S]-heparin.	Heparin	0-7	serpin family C member 1	Rattus norvegicus	31-47
1471071-4	1992	Heparin with high affinity for antithrombin III, prepared by antithrombin-affinity chromatography, dislodges up to 90% of the bound [35S]-heparin.	Heparin	138-145	serpin family C member 1	Rattus norvegicus	31-47
1471071-5	1992	Furthermore, antithrombin III-high affinity heparin shows a high affinity for myosin ATPase when compared to antithrombin III-low affinity heparin which shows a low affinity for the enzyme.	Heparin	44-51	serpin family C member 1	Rattus norvegicus	13-29
1471071-5	1992	Furthermore, antithrombin III-high affinity heparin shows a high affinity for myosin ATPase when compared to antithrombin III-low affinity heparin which shows a low affinity for the enzyme.	Heparin	139-146	serpin family C member 1	Rattus norvegicus	109-125
1382088-5	1992	Binding of 125I-labeled 40 KD protein to electroblotted gp330 and to coated apical membrane regions in sections of renal proximal tubules was abolished by excess unlabeled 40 KD protein, heparin, and EDTA.	Heparin	187-194	LDL receptor related protein 2	Rattus norvegicus	56-61
1279864-7	1992	Other activities suggested for SGP-2 are lipid transport and cell-cell interactions, which are consistent with sequence data that predict binding of dinucleotides, heparin and lipids.	Heparin	164-171	clusterin	Rattus norvegicus	31-36
1326560-2	1992	The cytochrome b558 was solubilized from membranes with the detergent n-heptyl-beta-thioglucoside and purified by DEAE-Sepharose and heparin-Sepharose chromatographies.	Heparin	133-140	cytochrome b	Sus scrofa	4-16
1412157-6	1992	The (absence of) inhibition of prothrombin conversion by prothrombinase in the presence of heparins found with the previous method is also found using the new algorithm.	Heparin	91-99	coagulation factor X	Homo sapiens	57-71
1638523-4	1992	Both human and murine IL-6 reduced heparin-releasable LPL activity in 3T3-L1 adipocytes in a dose-dependent manner; half-maximal inhibition of LPL activity was achieved with 5000 hybridoma growth factor units/ml.	Heparin	35-42	lipoprotein lipase	Mus musculus	54-57
1638523-4	1992	Both human and murine IL-6 reduced heparin-releasable LPL activity in 3T3-L1 adipocytes in a dose-dependent manner; half-maximal inhibition of LPL activity was achieved with 5000 hybridoma growth factor units/ml.	Heparin	35-42	lipoprotein lipase	Mus musculus	143-146
1351851-8	1992	Heparin, at a concentration that potentiated aFGF-induced neurite outgrowth 100-fold (100 micrograms/ml), did not alter the ability of aFGF to increase S6 phosphorylation or ODC activity.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	45-49
1380514-14	1992	This exogenously applied bFGF could be largely removed by treatment of cultures with heparin, suggesting its association with HSPG at the cell surface.	Heparin	85-92	fibroblast growth factor 2 L homeolog	Xenopus laevis	25-29
1618758-7	1992	In contrast, the full-length heparin produced large ionic strength-dependent enhancements in second order rate constants for both antithrombin reactions of 4,300-fold for thrombin and 580-fold for factor Xa at I 0.15.	Heparin	29-36	coagulation factor X	Homo sapiens	197-206
1376317-4	1992	Utilizing synthetic peptides encompassing overlapping sequences of the heparin-binding domain of VN, adjacent heparin and PAI-1-binding sites were localized within the sequence 348-370 of VN.	Heparin	71-78	vitronectin	Homo sapiens	97-99
1376317-0	1992	Mapping of binding sites for heparin, plasminogen activator inhibitor-1, and plasminogen to vitronectin"s heparin-binding region reveals a novel vitronectin-dependent feedback mechanism for the control of plasmin formation.	Heparin	29-36	vitronectin	Homo sapiens	92-103
1329249-0	1992	Heparin potentiation of collagen-induced platelet aggregation is related to the GPIIb/GPIIIa receptor and not to the GPIb receptor, as tested by whole blood aggregometry.	Heparin	0-7	integrin subunit alpha 2b	Homo sapiens	80-85
1329249-8	1992	In conclusion, the potentiation of collagen-induced platelet aggregation by heparin was not inhibited by MAb 7E3, RGDS, aurin or MAb 6D1, but was abolished by MAb 10E5, implying that the heparin effect is related to activation of the platelet GP IIb/IIIa receptor complex.	Heparin	76-83	integrin subunit alpha 2b	Homo sapiens	243-249
1517347-3	1992	Their application is then illustrated by consideration of results from recycling partition equilibrium studies of the heparin-facilitated desorption of thrombin from heparin-Sepharose, and of the competition between methyl-alpha-D-mannoside and p-nitrophenyl-alpha-D- mannoside for concanavalin A immobilized on CPG-170.	Heparin	118-125	prothrombin	Oryctolagus cuniculus	152-160
1517347-3	1992	Their application is then illustrated by consideration of results from recycling partition equilibrium studies of the heparin-facilitated desorption of thrombin from heparin-Sepharose, and of the competition between methyl-alpha-D-mannoside and p-nitrophenyl-alpha-D- mannoside for concanavalin A immobilized on CPG-170.	Heparin	166-173	prothrombin	Oryctolagus cuniculus	152-160
1314393-7	1992	Heparin inhibited GH3 cell labeling by (-)-STBodipy-DHP with an IC50 value of 9.7 micrograms/ml and blocked L-type Ca(2+)-channel-mediated 45Ca2+ uptake with an IC50 value of 32 micrograms/ml.	Heparin	0-7	dihydropyrimidinase	Rattus norvegicus	52-55
1582992-2	1992	The platelet-derived growth factor A-chain contains a sequence that specifically binds heparin.	Heparin	87-94	platelet derived growth factor subunit A	Homo sapiens	4-42
1582992-5	1992	Oligo-108-124 (corresponding to amino acid residues 108-124 of the long PDGF A-chain isoform) had no effect on DNA synthesis in itself but competed at 10(-10) M concentration effectively with PDGF for binding to heparin and released the block on thymidine incorporation induced by heparin.	Heparin	212-219	platelet derived growth factor subunit A	Homo sapiens	72-84
1582992-5	1992	Oligo-108-124 (corresponding to amino acid residues 108-124 of the long PDGF A-chain isoform) had no effect on DNA synthesis in itself but competed at 10(-10) M concentration effectively with PDGF for binding to heparin and released the block on thymidine incorporation induced by heparin.	Heparin	281-288	platelet derived growth factor subunit A	Homo sapiens	72-84
1377956-5	1992	Furthermore, we have shown that the main inhibitor of the contact phase, C1-esterase-inhibitor, loses some of its activity against beta-FXIIa in the presence of heparin.	Heparin	161-168	serpin family G member 1	Homo sapiens	73-94
1306682-0	1992	The alternative-splice isoforms of the PDGF A-chain differ in their ability to associate with the extracellular matrix and to bind heparin in vitro.	Heparin	131-138	platelet derived growth factor subunit A	Homo sapiens	39-45
1326098-3	1992	It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM).	Heparin	62-69	coagulation factor X	Homo sapiens	251-260
1326098-3	1992	It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM).	Heparin	62-69	coagulation factor X	Homo sapiens	348-357
1381819-4	1992	This vitronectin had been purified by heparin-affinity chromatography.	Heparin	38-45	vitronectin	Homo sapiens	5-16
1719529-1	1991	Mouse vitronectin (Vn) was isolated from serum by heparin affinity chromatography.	Heparin	50-57	vitronectin	Mus musculus	6-17
1811339-5	1991	The specific activities of different pools of heparin were evaluated using a colorimetric microwell kinetics assay using antithrombin and thrombin.	Heparin	46-53	coagulation factor II, thrombin	Bos taurus	125-133
1768492-13	1991	Although the heparin coating limits the reduction in antithrombin III and blood elements, it does not eliminate the risk of thromboembolus formation.	Heparin	13-20	serpin family C member 1	Canis lupus familiaris	53-69
1663665-2	1991	With the help of a combined assay method heparin characterization is made possible using the TAT/XAT quotient under consideration of the simultaneous inhibition of the two serine proteases thrombin and factor Xa by antithrombin III.	Heparin	41-48	coagulation factor X	Homo sapiens	202-211
1665594-0	1991	Low molecular weight heparin-catalyzed inactivation of factor Xa and thrombin by antithrombin III--effect of platelet factor 4.	Heparin	21-28	coagulation factor X	Homo sapiens	55-64
1772437-6	1991	Furthermore, binding of gp 80 to immobilized fibrinogen (or heparin) was inhibited in the presence of free fibrinogen (or heparin) added in the assay mixture.	Heparin	60-67	clusterin	Canis lupus familiaris	24-29
1715701-1	1991	We previously observed that Ser378 in the heparin-binding domain of vitronectin becomes phosphorylated by a protein kinase in plasma upon addition of ATP and divalent cations.	Heparin	42-49	vitronectin	Homo sapiens	68-79
1777434-0	1991	A lipophilic heparin derivative protects elastin against degradation by leucocyte elastase.	Heparin	13-20	elastin	Homo sapiens	41-48
1777434-4	1991	When insoluble elastin is pretreated with I its degradation by leucocyte elastase is inhibited by almost 90% while pretreatment of elastin with heparin exhibited only a moderate effect on elastolysis (10% inhibition).	Heparin	144-151	elastin	Homo sapiens	131-138
1875911-8	1991	Furthermore, the Ca2+ signals elicited by both bradykinin and epidermal growth factor were blocked in cells microinjected with the inositol 1,4,5-trisphosphate receptor antagonist heparin, whereas the intracellular Ca(2+)-ATPase inhibitor thapsigargin still mobilized Ca2+.	Heparin	180-187	carbonic anhydrase 2	Homo sapiens	17-20
1712728-10	1991	Native tenascin and all fragments containing the distal part of its arms bind to heparin-agarose, whereas the proximal fragments do not.	Heparin	81-88	avian tenascin X	Gallus gallus	7-15
1906461-4	1991	HSPG binding was inhibited by heparin and dextran sulfate, but not by dermatan or chondroitin sulfate.	Heparin	30-37	CD44 molecule (Indian blood group)	Homo sapiens	0-4
1711938-3	1991	METHODS AND RESULTS: Western-blot analysis of heparin-bound material from neonatal heart extracts identified a single band with a molecular weight of approximately 18 kD for both bFGF and aFGF.	Heparin	46-53	fibroblast growth factor 1	Rattus norvegicus	188-192
1646716-2	1991	The relationship between thrombomodulin-associated O-linked glycosammoglycans (GAGs) and the exogenous GAGs heparin or dermatan sulfate was studied in the inhibition of thrombin by antithrombin III (AT III) or heparin cofactor II (HC II).	Heparin	108-115	prothrombin	Oryctolagus cuniculus	169-177
1646716-7	1991	When thrombin inhibition by AT III in the presence of heparin was studied, both high-Mr rec-TM and rabbit TM again invoked a similar reduction of inactivation rates, whereas in the absence of exogenous heparin, both high-Mr forms accelerated thrombin inhibition by AT III.	Heparin	54-61	prothrombin	Oryctolagus cuniculus	5-13
2017164-1	1991	A novel human keratinocyte-derived autocrine factor (KAF) was purified from conditioned medium by using heparin affinity chromatography as the first step.	Heparin	104-111	complement factor I	Homo sapiens	14-51
2017164-1	1991	A novel human keratinocyte-derived autocrine factor (KAF) was purified from conditioned medium by using heparin affinity chromatography as the first step.	Heparin	104-111	complement factor I	Homo sapiens	53-56
1806764-3	1991	The major findings in clinical evaluation for acute myocardial infarction to date include (1) substantial mortality reduction and improvement in cardiac function; (2) an excess of serious bleeding complications at high doses (150 mg) of t-PA; (3) rapid infarct vessel recanalization with an accelerated "front-loaded" regimen; (4) the importance of conjunctive intravenous heparin; and (5) the potential for new, combined plasminogen activator therapies.	Heparin	373-380	chromosome 20 open reading frame 181	Homo sapiens	237-241
1704799-6	1991	Complexes between TGF-beta 2 and native or reacted forms of alpha 2M were less dissociable by heparin than the equivalent complexes with TGF-beta 1.	Heparin	94-101	transforming growth factor beta 2	Homo sapiens	18-28
1658965-1	1991	In determining heparin one has the choice to test a specific activity, such as the decay constant of thrombin or factor Xa on a global test such as the aPTT.	Heparin	15-22	coagulation factor X	Homo sapiens	113-122
2123154-4	1990	We conclude that heparin-induced thromboses in the pulmonary arteries are amenable to thrombolytic therapy, including tPA, whereas this regimen appears to have little effect on saphenous vein grafts.	Heparin	17-24	chromosome 20 open reading frame 181	Homo sapiens	118-121
2127808-4	1990	At the time of demonstrating decreased HRGP values, expression of HRGP fragment was studied using heparin-Sepharose beads.	Heparin	98-105	histidine rich glycoprotein	Homo sapiens	66-70
2127808-7	1990	As HRGP is a potent heparin antagonist, HRGP levels in plasma during hemodialysis with heparin were studied.	Heparin	20-27	histidine rich glycoprotein	Homo sapiens	3-7
2229039-1	1990	A neurite-promoting factor (p18) was isolated from bovine brain using ammonium sulfate fractionation, sulfated Sephadex G-50 chromatography, heparin-Sepharose gel chromatography, and reverse phase high performance liquid chromatography.	Heparin	141-148	pleiotrophin	Bos taurus	28-31
2403299-7	1990	Since lipoprotein lipase has a similar size as hepatic triacylglycerol lipase, the disproportionate amount of lipoprotein lipase in lymph as compared to hepatic triacylglycerol lipase could be due to heparin crossing the capillary endothelium and displacing lipoprotein lipase from peripheral cells.	Heparin	200-207	lipoprotein lipase	Canis lupus familiaris	110-128
2253091-1	1990	Human mast cell tryptase was purified from lung tissue by high salt extraction, ammonium sulphate precipitation, octyl Sepharose and heparin-agarose chromatography.	Heparin	133-140	tryptase delta 1	Homo sapiens	6-24
2386199-3	1990	In the present study, the effect of heparin on the content and regional distribution of elastin, collagen, and proteoglycans (PGs) in blood vessels following experimental injury was determined.	Heparin	36-43	elastin	Rattus norvegicus	88-95
2386199-6	1990	Heparin treatment inhibited intimal thickening and decreased the elastin content in the ECM domain in the upper and lower arterial intima.	Heparin	0-7	elastin	Rattus norvegicus	65-72
1693270-3	1990	Heparin only moderately interfered with the vitronectin-plasminogen interaction, whereas high concentrations of 6-amino-hexanoic acid inhibited binding.	Heparin	0-7	vitronectin	Homo sapiens	44-55
1693270-4	1990	Utilizing a ligand-blotting procedure in which plasminogen was reacted with proteolytic fragments of vitronectin, transblotted onto nitrocellulose, the plasminogen-binding site of vitronectin was localized to the heparin-binding domain of the adhesive protein.	Heparin	213-220	vitronectin	Homo sapiens	101-112
1693270-4	1990	Utilizing a ligand-blotting procedure in which plasminogen was reacted with proteolytic fragments of vitronectin, transblotted onto nitrocellulose, the plasminogen-binding site of vitronectin was localized to the heparin-binding domain of the adhesive protein.	Heparin	213-220	vitronectin	Homo sapiens	180-191
2157492-13	1990	Using heparin as well as excess unlabeled LDL, it was shown that HDL3 uptake is independent of LDL (apo B,E) receptors.	Heparin	6-13	high density lipoprotein (HDL) level 3	Mus musculus	65-69
2331791-8	1990	Heparin-affinity high performance liquid chromatography (HPLC) showed a proportionately greater increase in levels of aFGF than bFGF between the tenth and fortieth postnatal days.	Heparin	0-7	fibroblast growth factor 1	Rattus norvegicus	118-122
1715199-8	1990	Since heparin protected FGF from kallikrein inactivation, it is suggested that inactivation was caused by proteolytic degradation of part of the FGF molecule by kallikrein.	Heparin	6-13	kallikrein related peptidase 4	Homo sapiens	33-43
2139477-9	1990	alpha 2-PI-PM levels were improved in 5 out of 7 cases with the heparin treatment.	Heparin	64-71	serpin family F member 2	Homo sapiens	0-10
2139477-10	1990	On the other hand only one in 6 cases who did not receive heparin therapy showed the improvement of alpha 2-PI-PM level.	Heparin	58-65	serpin family F member 2	Homo sapiens	100-110
2139477-11	1990	In some cases without heparin treatment, the alpha 2-PI-PM level increased in the course of treatment.	Heparin	22-29	serpin family F member 2	Homo sapiens	45-55
2302223-3	1990	The potential heparin-binding site of IGF II is probably situated in the arginine-rich C-peptide region.	Heparin	14-21	insulin like growth factor 2	Bos taurus	38-44
1963017-1	1990	Unfractionated heparin in the extrinsic system has an action on prothrombinase that is insignificant compared to its antithrombin action.	Heparin	15-22	coagulation factor X	Homo sapiens	64-78
1963018-2	1990	The plasmatic anti-Factor Xa activity half-life, whatever the injected dose of the different low molecular weight heparins, is about two to four times longer than for unfractionated heparin while anti-Factor IIa plasmatic half-life is only slightly longer for enoxaparin than for unfractionated heparin.	Heparin	114-122	coagulation factor X	Homo sapiens	19-28
1963018-2	1990	The plasmatic anti-Factor Xa activity half-life, whatever the injected dose of the different low molecular weight heparins, is about two to four times longer than for unfractionated heparin while anti-Factor IIa plasmatic half-life is only slightly longer for enoxaparin than for unfractionated heparin.	Heparin	114-121	coagulation factor X	Homo sapiens	19-28
2174783-6	1990	The peak heparin concentration on Day 2 ranged from 0.40 to 0.75 anti-FXa U/ml and adjustment was only required in 3 patients.	Heparin	9-16	coagulation factor X	Homo sapiens	70-73
2083864-3	1990	Heparin subcutaneously (200 U/kg) injected for 2 weeks resulted in an enhanced inactivation of thrombin and factor Xa by the endothelium.	Heparin	0-7	coagulation factor X	Homo sapiens	108-117
2132533-0	1990	Heparin inhibits transcriptional activation by Fos and Jun oncoproteins.	Heparin	0-7	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	47-50
33771558-0	2021	VEGF and VEGFR2 bind to similar pH-sensitive sites on fibronectin, exposed by heparin-mediated conformational changes.	Heparin	78-85	kinase insert domain receptor	Homo sapiens	9-15
11825873-0	2002	CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling.	Heparin	51-58	CD44 antigen	Mus musculus	0-4
11825873-0	2002	CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling.	Heparin	51-58	matrix metallopeptidase 7	Mus musculus	29-39
11825873-0	2002	CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling.	Heparin	51-58	matrix metallopeptidase 7	Mus musculus	40-45
34694067-4	2022	Heparin lithium hydrogel (Li-hep-gel) is synthesized to act as a lithium and MiR@TDNs delivery agent.	Heparin	0-7	membrane associated ring-CH-type finger 8	Homo sapiens	77-80
34987706-10	2021	Heparin downregulated the expression of hepcidin and DMT1, increased FPN1, and exerted protective effects that were equivalent to those of ebselen on ferroptosis and EBI.	Heparin	0-7	RoBo-1	Rattus norvegicus	53-57
34816442-2	2022	This study aimed to: (i) develop a PK/PD model for UFH, quantified by anti-factor Xa assay and the UFH effect measured by activated partial thromboplastin time (aPTT) (ii) evaluate pediatric UFH infusions in achieving anti-factor Xa (0.3 - 0.7 IU/mL) therapeutic target by simulations.	Heparin	191-194	coagulation factor X	Homo sapiens	75-84
34816442-2	2022	This study aimed to: (i) develop a PK/PD model for UFH, quantified by anti-factor Xa assay and the UFH effect measured by activated partial thromboplastin time (aPTT) (ii) evaluate pediatric UFH infusions in achieving anti-factor Xa (0.3 - 0.7 IU/mL) therapeutic target by simulations.	Heparin	191-194	coagulation factor X	Homo sapiens	223-232
34816442-10	2022	In conclusion, the UFH anti-factor Xa target is not achieved initially especially in young pediatrics, suggesting the need to optimize UFH dosing to achieve higher therapeutic success.	Heparin	19-22	coagulation factor X	Homo sapiens	28-37
34794445-3	2021	Rosetting is influenced by the host"s ABO blood group (Bg) and rosettes formed in BgA have previously been shown to be more resilient to disruption by heparin and shield the parasite derived surface antigens from antibodies.	Heparin	151-158	ABO, alpha 1-3-N-acetylgalactosaminyltransferase and alpha 1-3-galactosyltransferase	Homo sapiens	38-53
34428806-3	2021	Anti-factor Xa (aFXa) level is a measure of unfractionated heparin efficacy and safety.	Heparin	59-66	coagulation factor X	Homo sapiens	5-14
34368018-5	2021	Methods: For the experiments LDN-193189 and oversulfated heparins were used, which interact with the BMP6-SMAD pathway thereby inhibiting hepcidin expression.	Heparin	57-65	hepcidin antimicrobial peptide	Mus musculus	138-146
34205548-9	2021	In this study, we illustrate the performances of different anti-FXa assays used for testing heparin on UFH or LMWH treated patients" plasmas and obtained using citrate or CTAD anticoagulants.	Heparin	92-99	coagulation factor X	Homo sapiens	64-67
35331832-1	2022	A novel drug eluting retrievable vena cava filter (RVCF) with a heparin-modified poly(epsilon-caprolactone) (hPCL) coating containing rapamycin was prepared by electrospraying.	Heparin	64-71	PHD finger protein 1	Homo sapiens	109-113
35551912-2	2022	ZPI is also activated by heparin to inhibit free FXa at a physiologically significant rate.	Heparin	25-32	coagulation factor X	Homo sapiens	49-52
35551912-8	2022	Together, these findings suggest that heparin binding to a site on ZPI extending from helix C to helix H promotes ZPI inhibition of FXa and allosterically antagonizes PZ binding to ZPI through long-range conformational changes.	Heparin	38-45	coagulation factor X	Homo sapiens	132-135
35551912-9	2022	Heparin antagonism of PZ binding to ZPI may serve to spare limiting PZ and allow PZ and heparin cofactors to target FXa at different sites of action.	Heparin	0-7	coagulation factor X	Homo sapiens	116-119
35551912-9	2022	Heparin antagonism of PZ binding to ZPI may serve to spare limiting PZ and allow PZ and heparin cofactors to target FXa at different sites of action.	Heparin	88-95	coagulation factor X	Homo sapiens	116-119
35510711-6	2022	Most ROS1 and ALK patients on anticoagulation received low-molecular-weight heparin (75% and 64.1%, respectively).	Heparin	76-83	ROS proto-oncogene 1, receptor tyrosine kinase	Homo sapiens	5-9
35510711-6	2022	Most ROS1 and ALK patients on anticoagulation received low-molecular-weight heparin (75% and 64.1%, respectively).	Heparin	76-83	ALK receptor tyrosine kinase	Homo sapiens	14-17
35513125-9	2022	Thus, soluble klotho and heparin act as independent FGF23 co-receptors with opposite effects on the pathologic actions of FGF23, with soluble klotho reducing and heparin increasing FGF23-induced cardiac hypertrophy.	Heparin	25-32	fibroblast growth factor 23	Mus musculus	122-127
35513125-9	2022	Thus, soluble klotho and heparin act as independent FGF23 co-receptors with opposite effects on the pathologic actions of FGF23, with soluble klotho reducing and heparin increasing FGF23-induced cardiac hypertrophy.	Heparin	25-32	klotho	Mus musculus	142-148
35513125-9	2022	Thus, soluble klotho and heparin act as independent FGF23 co-receptors with opposite effects on the pathologic actions of FGF23, with soluble klotho reducing and heparin increasing FGF23-induced cardiac hypertrophy.	Heparin	25-32	fibroblast growth factor 23	Mus musculus	181-186
35513125-9	2022	Thus, soluble klotho and heparin act as independent FGF23 co-receptors with opposite effects on the pathologic actions of FGF23, with soluble klotho reducing and heparin increasing FGF23-induced cardiac hypertrophy.	Heparin	162-169	fibroblast growth factor 23	Mus musculus	122-127
35513125-9	2022	Thus, soluble klotho and heparin act as independent FGF23 co-receptors with opposite effects on the pathologic actions of FGF23, with soluble klotho reducing and heparin increasing FGF23-induced cardiac hypertrophy.	Heparin	162-169	fibroblast growth factor 23	Mus musculus	181-186
35513125-10	2022	Hence, whether heparin injections during hemodialysis in patients with extremely high serum FGF23 levels contribute to their high rates of cardiovascular events and mortality remains to be studied.	Heparin	15-22	fibroblast growth factor 23	Homo sapiens	92-97
35485302-3	2022	The hE/N-cadherin-functionalized PLGA/chitosan-heparin-TGFbeta1 (Duo hE/N-cad@P/C-h-TGFbeta1) microparticles spatiotemporally upregulates the endogenous E/N-cadherin expression of hMSC aggregates which further amplifies the chondrogenic differentiation and modulate paracrine and anti-inflammatory functions of hMSCs toward constructing a favorable microenvironment for chondrogenesis.	Heparin	47-54	cadherin 2	Homo sapiens	7-17
35485302-3	2022	The hE/N-cadherin-functionalized PLGA/chitosan-heparin-TGFbeta1 (Duo hE/N-cad@P/C-h-TGFbeta1) microparticles spatiotemporally upregulates the endogenous E/N-cadherin expression of hMSC aggregates which further amplifies the chondrogenic differentiation and modulate paracrine and anti-inflammatory functions of hMSCs toward constructing a favorable microenvironment for chondrogenesis.	Heparin	47-54	cadherin 2	Homo sapiens	155-165
35438981-4	2022	To this end, we produced heparin-doped polypyrrole (PPy/Hep) electrodes of different surface roughness, with Ra values from 5.5 to 17.6 nm, by varying the charge densities during electrochemical synthesis.	Heparin	25-32	DNL-type zinc finger	Homo sapiens	56-59
35456329-6	2022	Both agents allowed for accurate measurement of anti-factor Xa activity in the plasma containing rivaroxaban and heparins in the concentration range reached in patients" blood.	Heparin	113-120	coagulation factor X	Homo sapiens	53-62
35366771-2	2022	Methods- In this research, we developed the amphiphilic Heparin-Poloxamer P403 (HSP) nanogel that can load curcumin (CUR) and Paclitaxel (PTX) through the hydrophobic core of Poloxamer P403.	Heparin	56-63	heat shock protein 90 beta family member 2, pseudogene	Homo sapiens	80-83
35381662-0	2022	(Heparin-binding hemagglutinin as a composition antigen of tuberculosis vaccine exerts protective immune effects by inducing IL-17).	Heparin	1-8	interleukin 17A	Mus musculus	125-130
35200221-4	2022	Using a routine hybrid heparin anti-Factor Xa assay, 1 patient demonstrated a strong linear correlation up to a serum rivaroxaban concentration of 940 ng/mL.	Heparin	23-30	coagulation factor X	Homo sapiens	36-45
35102343-4	2022	This occurs independent of interleukin-22 (IL-22), and we identify that ILC3s are a dominant source of heparin-binding epidermal growth factor-like growth factor (HB-EGF).	Heparin	103-110	interleukin 22	Homo sapiens	43-48
35052866-1	2022	Syndecan-2 (SDC2), a cell-surface heparin sulfate proteoglycan of the glycocalyx, is mainly expressed in endothelial cells.	Heparin	34-41	syndecan 2	Homo sapiens	0-10
35052866-1	2022	Syndecan-2 (SDC2), a cell-surface heparin sulfate proteoglycan of the glycocalyx, is mainly expressed in endothelial cells.	Heparin	34-41	syndecan 2	Homo sapiens	12-16
34995358-7	2022	RESULTS: Low-molecular-weight heparin (LMWH, an indirect inhibitor of thrombin) restrained both papain- and fungus-induced type 2 immune responses in mice by inhibiting IL-33 cleavage.	Heparin	30-37	interleukin 33	Mus musculus	169-174